data_4BGX # _entry.id 4BGX # _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 4BGX PDBE EBI-56327 WWPDB D_1290056327 # 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 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 4BH0 unspecified ;H5 (TYTY) INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'-SLN ; 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 4BGX _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.' 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.' 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 4BGX _cell.length_a 101.338 _cell.length_b 101.338 _cell.length_c 451.102 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 18 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4BGX _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat HEMAGGLUTININ 36950.766 1 ? ? 'HA1 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 17-340' ? 2 polymer nat HEMAGGLUTININ 19097.990 1 ? ? 'HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 347-512' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 3 ? ? ? ? 4 non-polymer man 'O-SIALIC ACID' 309.270 1 ? ? ? ? 5 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 6 non-polymer syn '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' 238.305 1 ? ? ? ? 7 water nat water 18.015 211 ? ? ? ? # 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 ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; ;DQICIGYHANNSTEQVDTIMEKNVTVTHAQDILEKTHNGKLCDLDGVKPLILRDCSVAGWLLGNPMCDEFINVPEWSYIV EKANPVNDLCYPGDFNDYEELKHLLSRINHFEKIQIIPKSSWSSHEASLGVSSACPYQGKSSFFRNVVWLIKKNSTYPTI KRSYNNTNQEDLLVLWGIHHPNDAAEQTKLYQNPTTYISVGTSTLNQRLVPRIATRSKVNGQSGRMEFFWTILKPNDAIN FESNGNFIAPEYAYKIVKKGDSTIMKSELEYGNCNTKCQTPMGAINSSMPFHNIHPLTIGECPKYVKSNRLVLATGLRNS PQRETR ; A ? 2 'polypeptide(L)' no no ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNEQGSGYAADKESTQKAIDGVTNKVNSIIDKMNTQFEAVGREFNNLERRIENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRLQLRDNAKELGNGCFEFYHKCDNECMESVRNGTYDYP QYSEEA ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 GLN n 1 3 ILE n 1 4 CYS n 1 5 ILE n 1 6 GLY n 1 7 TYR n 1 8 HIS n 1 9 ALA n 1 10 ASN n 1 11 ASN n 1 12 SER n 1 13 THR n 1 14 GLU n 1 15 GLN n 1 16 VAL n 1 17 ASP n 1 18 THR n 1 19 ILE n 1 20 MET n 1 21 GLU n 1 22 LYS n 1 23 ASN n 1 24 VAL n 1 25 THR n 1 26 VAL n 1 27 THR n 1 28 HIS n 1 29 ALA n 1 30 GLN n 1 31 ASP n 1 32 ILE n 1 33 LEU n 1 34 GLU n 1 35 LYS n 1 36 THR n 1 37 HIS n 1 38 ASN n 1 39 GLY n 1 40 LYS n 1 41 LEU n 1 42 CYS n 1 43 ASP n 1 44 LEU n 1 45 ASP n 1 46 GLY n 1 47 VAL n 1 48 LYS n 1 49 PRO n 1 50 LEU n 1 51 ILE n 1 52 LEU n 1 53 ARG n 1 54 ASP n 1 55 CYS n 1 56 SER n 1 57 VAL n 1 58 ALA n 1 59 GLY n 1 60 TRP n 1 61 LEU n 1 62 LEU n 1 63 GLY n 1 64 ASN n 1 65 PRO n 1 66 MET n 1 67 CYS n 1 68 ASP n 1 69 GLU n 1 70 PHE n 1 71 ILE n 1 72 ASN n 1 73 VAL n 1 74 PRO n 1 75 GLU n 1 76 TRP n 1 77 SER n 1 78 TYR n 1 79 ILE n 1 80 VAL n 1 81 GLU n 1 82 LYS n 1 83 ALA n 1 84 ASN n 1 85 PRO n 1 86 VAL n 1 87 ASN n 1 88 ASP n 1 89 LEU n 1 90 CYS n 1 91 TYR n 1 92 PRO n 1 93 GLY n 1 94 ASP n 1 95 PHE n 1 96 ASN n 1 97 ASP n 1 98 TYR n 1 99 GLU n 1 100 GLU n 1 101 LEU n 1 102 LYS n 1 103 HIS n 1 104 LEU n 1 105 LEU n 1 106 SER n 1 107 ARG n 1 108 ILE n 1 109 ASN n 1 110 HIS n 1 111 PHE n 1 112 GLU n 1 113 LYS n 1 114 ILE n 1 115 GLN n 1 116 ILE n 1 117 ILE n 1 118 PRO n 1 119 LYS n 1 120 SER n 1 121 SER n 1 122 TRP n 1 123 SER n 1 124 SER n 1 125 HIS n 1 126 GLU n 1 127 ALA n 1 128 SER n 1 129 LEU n 1 130 GLY n 1 131 VAL n 1 132 SER n 1 133 SER n 1 134 ALA n 1 135 CYS n 1 136 PRO n 1 137 TYR n 1 138 GLN n 1 139 GLY n 1 140 LYS n 1 141 SER n 1 142 SER n 1 143 PHE n 1 144 PHE n 1 145 ARG n 1 146 ASN n 1 147 VAL n 1 148 VAL n 1 149 TRP n 1 150 LEU n 1 151 ILE n 1 152 LYS n 1 153 LYS n 1 154 ASN n 1 155 SER n 1 156 THR n 1 157 TYR n 1 158 PRO n 1 159 THR n 1 160 ILE n 1 161 LYS n 1 162 ARG n 1 163 SER n 1 164 TYR n 1 165 ASN n 1 166 ASN n 1 167 THR n 1 168 ASN n 1 169 GLN n 1 170 GLU n 1 171 ASP n 1 172 LEU n 1 173 LEU n 1 174 VAL n 1 175 LEU n 1 176 TRP n 1 177 GLY n 1 178 ILE n 1 179 HIS n 1 180 HIS n 1 181 PRO n 1 182 ASN n 1 183 ASP n 1 184 ALA n 1 185 ALA n 1 186 GLU n 1 187 GLN n 1 188 THR n 1 189 LYS n 1 190 LEU n 1 191 TYR n 1 192 GLN n 1 193 ASN n 1 194 PRO n 1 195 THR n 1 196 THR n 1 197 TYR n 1 198 ILE n 1 199 SER n 1 200 VAL n 1 201 GLY n 1 202 THR n 1 203 SER n 1 204 THR n 1 205 LEU n 1 206 ASN n 1 207 GLN n 1 208 ARG n 1 209 LEU n 1 210 VAL n 1 211 PRO n 1 212 ARG n 1 213 ILE n 1 214 ALA n 1 215 THR n 1 216 ARG n 1 217 SER n 1 218 LYS n 1 219 VAL n 1 220 ASN n 1 221 GLY n 1 222 GLN n 1 223 SER n 1 224 GLY n 1 225 ARG n 1 226 MET n 1 227 GLU n 1 228 PHE n 1 229 PHE n 1 230 TRP n 1 231 THR n 1 232 ILE n 1 233 LEU n 1 234 LYS n 1 235 PRO n 1 236 ASN n 1 237 ASP n 1 238 ALA n 1 239 ILE n 1 240 ASN n 1 241 PHE n 1 242 GLU n 1 243 SER n 1 244 ASN n 1 245 GLY n 1 246 ASN n 1 247 PHE n 1 248 ILE n 1 249 ALA n 1 250 PRO n 1 251 GLU n 1 252 TYR n 1 253 ALA n 1 254 TYR n 1 255 LYS n 1 256 ILE n 1 257 VAL n 1 258 LYS n 1 259 LYS n 1 260 GLY n 1 261 ASP n 1 262 SER n 1 263 THR n 1 264 ILE n 1 265 MET n 1 266 LYS n 1 267 SER n 1 268 GLU n 1 269 LEU n 1 270 GLU n 1 271 TYR n 1 272 GLY n 1 273 ASN n 1 274 CYS n 1 275 ASN n 1 276 THR n 1 277 LYS n 1 278 CYS n 1 279 GLN n 1 280 THR n 1 281 PRO n 1 282 MET n 1 283 GLY n 1 284 ALA n 1 285 ILE n 1 286 ASN n 1 287 SER n 1 288 SER n 1 289 MET n 1 290 PRO n 1 291 PHE n 1 292 HIS n 1 293 ASN n 1 294 ILE n 1 295 HIS n 1 296 PRO n 1 297 LEU n 1 298 THR n 1 299 ILE n 1 300 GLY n 1 301 GLU n 1 302 CYS n 1 303 PRO n 1 304 LYS n 1 305 TYR n 1 306 VAL n 1 307 LYS n 1 308 SER n 1 309 ASN n 1 310 ARG n 1 311 LEU n 1 312 VAL n 1 313 LEU n 1 314 ALA n 1 315 THR n 1 316 GLY n 1 317 LEU n 1 318 ARG n 1 319 ASN n 1 320 SER n 1 321 PRO n 1 322 GLN n 1 323 ARG n 1 324 GLU n 1 325 THR n 1 326 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 LYS 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_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _entity_src_nat.genus _entity_src_nat.species _entity_src_nat.strain _entity_src_nat.tissue _entity_src_nat.tissue_fraction _entity_src_nat.pdbx_secretion _entity_src_nat.pdbx_fragment _entity_src_nat.pdbx_variant _entity_src_nat.pdbx_cell_line _entity_src_nat.pdbx_atcc _entity_src_nat.pdbx_cellular_location _entity_src_nat.pdbx_organ _entity_src_nat.pdbx_organelle _entity_src_nat.pdbx_cell _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 1 1 sample ? ? ? 'INFLUENZA VIRUS' 644788 ? ? 'A/VIETNAM/1194/2004(H5N1)' ? ? ? ? 'A/VN/1194/04/NIBRG14 VACCINE STRAIN' ? ? ? ? ? ? ? ? 'THE NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL (NIBSC)' 2 1 sample ? ? ? 'INFLUENZA VIRUS' 644788 ? ? 'A/VIETNAM/1194/2004(H5N1)' ? ? ? ? 'A/VN/1194/04/NIBRG14 VACCINE STRAIN' ? ? ? ? ? ? ? ? 'THE NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS AND CONTROL (NIBSC)' # 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 Q6DQ34_9INFA 1 ? ? Q6DQ34 ? 2 UNP Q6DQ34_9INFA 2 ? ? Q6DQ34 ? # 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 4BGX A 1 ? 326 ? Q6DQ34 17 ? 342 ? 1 326 2 2 4BGX B 1 ? 166 ? Q6DQ34 347 ? 512 ? 1 166 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 4BGX _struct_ref_seq_dif.mon_id THR _struct_ref_seq_dif.pdbx_pdb_strand_id A _struct_ref_seq_dif.seq_num 325 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code Q6DQ34 _struct_ref_seq_dif.db_mon_id ARG _struct_ref_seq_dif.pdbx_seq_db_seq_num 341 _struct_ref_seq_dif.details conflict _struct_ref_seq_dif.pdbx_auth_seq_num 325 _struct_ref_seq_dif.pdbx_ordinal 1 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EPE non-polymer . '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' HEPES 'C8 H18 N2 O4 S' 238.305 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 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 4BGX _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.98 _exptl_crystal.density_percent_sol 69.07 _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 '0.1 M HEPES PH 7.0, 0.05 M MGCL2, 28-30% PEG 550' # _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 2M' _diffrn_detector.pdbx_collection_date 2012-04-23 _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 0.9173 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04-1' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04-1 _diffrn_source.pdbx_wavelength 0.9173 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4BGX _reflns.observed_criterion_sigma_I 3.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 37.15 _reflns.d_resolution_high 2.48 _reflns.number_obs 32249 _reflns.number_all ? _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs 0.07 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 17.20 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 9.2 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.48 _reflns_shell.d_res_low 2.61 _reflns_shell.percent_possible_all 99.8 _reflns_shell.Rmerge_I_obs 0.63 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.00 _reflns_shell.pdbx_redundancy 7.9 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4BGX _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 30613 _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 37.18 _refine.ls_d_res_high 2.48 _refine.ls_percent_reflns_obs 99.82 _refine.ls_R_factor_obs 0.19480 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.19361 _refine.ls_R_factor_R_free 0.21776 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 1634 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.956 _refine.correlation_coeff_Fo_to_Fc_free 0.948 _refine.B_iso_mean 76.792 _refine.aniso_B[1][1] 2.17 _refine.aniso_B[2][2] 2.17 _refine.aniso_B[3][3] -7.05 _refine.aniso_B[1][2] 2.17 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.U VALUES WITH TLS ADDED' _refine.pdbx_starting_model 'PDB ENTRY 2IBX' _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 0.267 _refine.pdbx_overall_ESU_R_Free 0.203 _refine.overall_SU_ML 0.159 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 13.959 _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 3859 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 89 _refine_hist.number_atoms_solvent 211 _refine_hist.number_atoms_total 4159 _refine_hist.d_res_high 2.48 _refine_hist.d_res_low 37.18 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.008 0.019 ? 4051 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3725 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.245 1.962 ? 5498 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.711 3.003 ? 8569 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.190 5.000 ? 483 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.265 25.174 ? 201 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 15.720 15.000 ? 678 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.902 15.000 ? 17 'X-RAY DIFFRACTION' ? r_chiral_restr 0.065 0.200 ? 593 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.004 0.020 ? 4603 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 943 '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 1.388 3.375 ? 1932 'X-RAY DIFFRACTION' ? r_mcbond_other 1.386 3.374 ? 1931 'X-RAY DIFFRACTION' ? r_mcangle_it 2.250 5.060 ? 2412 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.257 3.795 ? 2119 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.480 _refine_ls_shell.d_res_low 2.544 _refine_ls_shell.number_reflns_R_work 2229 _refine_ls_shell.R_factor_R_work 0.306 _refine_ls_shell.percent_reflns_obs 99.91 _refine_ls_shell.R_factor_R_free 0.331 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 108 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4BGX _struct.title ;H5 (VN1194) 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 4BGX _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 3 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 3 ? H N N 6 ? I N N 7 ? J 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 56 ? GLY A 63 ? SER A 56 GLY A 63 1 ? 8 HELX_P HELX_P2 2 ASN A 64 ? ILE A 71 ? ASN A 64 ILE A 71 5 ? 8 HELX_P HELX_P3 3 ASP A 97 ? SER A 106 ? ASP A 97 SER A 106 1 ? 10 HELX_P HELX_P4 4 ASP A 183 ? GLN A 192 ? ASP A 183 GLN A 192 1 ? 10 HELX_P HELX_P5 5 ASP B 37 ? MET B 59 ? ASP B 37 MET B 59 1 ? 23 HELX_P HELX_P6 6 GLU B 74 ? ARG B 127 ? GLU B 74 ARG B 127 1 ? 54 HELX_P HELX_P7 7 ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 # _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 4 SG ? ? ? 1_555 B CYS 137 SG ? ? A CYS 4 B CYS 137 1_555 ? ? ? ? ? ? ? 2.132 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.050 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.046 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 135 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.073 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.077 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.049 ? covale1 covale ? ? A ASN 23 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 23 A NAG 1023 1_555 ? ? ? ? ? ? ? 1.449 ? covale2 covale ? ? A ASN 165 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 165 A NAG 1165 1_555 ? ? ? ? ? ? ? 1.437 ? covale3 covale ? ? E SIA . C2 ? ? ? 1_555 F GAL . O6 ? ? A SIA 1322 A GAL 1323 1_555 ? ? ? ? ? ? ? 1.424 ? covale4 covale ? ? B ASN 154 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 154 B NAG 1154 1_555 ? ? ? ? ? ? ? 1.436 ? # 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 ? # 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 # 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 GLY B 31 ? ALA B 36 ? GLY B 31 ALA B 36 BA 2 TYR B 22 ? ASN B 28 ? TYR B 22 ASN B 28 BA 3 GLN A 2 ? TYR A 7 ? 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 15 ? VAL A 16 ? GLN A 15 VAL A 16 AA 2 VAL A 24 ? THR A 25 ? VAL A 24 THR A 25 AB 1 ALA A 29 ? ASP A 31 ? ALA A 29 ASP A 31 AB 2 VAL A 312 ? ALA A 314 ? VAL A 312 ALA A 314 AC 1 LEU A 33 ? GLU A 34 ? LEU A 33 GLU A 34 AC 2 PHE A 291 ? HIS A 292 ? PHE A 291 HIS A 292 AC 3 LYS A 304 ? TYR A 305 ? LYS A 304 TYR A 305 AD 1 LEU A 41 ? LEU A 44 ? LEU A 41 LEU A 44 AD 2 TYR A 271 ? THR A 276 ? TYR A 271 THR A 276 AE 1 LEU A 50 ? ILE A 51 ? LEU A 50 ILE A 51 AE 2 ILE A 79 ? GLU A 81 ? ILE A 79 GLU A 81 AE 3 ILE A 264 ? LYS A 266 ? ILE A 264 LYS A 266 AF 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AF 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AF 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AF 4 PHE A 247 ? PRO A 250 ? PHE A 247 PRO A 250 AF 5 VAL A 147 ? TRP A 149 ? VAL A 147 TRP A 149 AG 1 GLY A 93 ? PHE A 95 ? GLY A 93 PHE A 95 AG 2 ARG A 225 ? LEU A 233 ? ARG A 225 LEU A 233 AG 3 LEU A 172 ? HIS A 180 ? LEU A 172 HIS A 180 AG 4 TYR A 252 ? LYS A 259 ? TYR A 252 LYS A 259 AG 5 ILE A 108 ? GLN A 115 ? ILE A 108 GLN A 115 AH 1 SER A 132 ? TYR A 137 ? SER A 132 TYR A 137 AH 2 LYS A 140 ? SER A 142 ? LYS A 140 SER A 142 AI 1 ILE A 160 ? ASN A 165 ? ILE A 160 ASN A 165 AI 2 ALA A 238 ? SER A 243 ? ALA A 238 SER A 243 AI 3 ILE A 198 ? GLY A 201 ? ILE A 198 GLY A 201 AI 4 ASN A 206 ? LEU A 209 ? ASN A 206 LEU A 209 AJ 1 GLY A 283 ? ALA A 284 ? GLY A 283 ALA A 284 AJ 2 CYS A 278 ? THR A 280 ? CYS A 278 THR A 280 AJ 3 ILE A 299 ? GLY A 300 ? ILE A 299 GLY A 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 2 ? O GLN A 2 BA 3 4 N ILE A 3 ? 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 16 ? N VAL A 16 O VAL A 24 ? O VAL A 24 AB 1 2 N GLN A 30 ? N GLN A 30 O LEU A 313 ? O LEU A 313 AC 1 2 N GLU A 34 ? N GLU A 34 O PHE A 291 ? O PHE A 291 AC 2 3 N HIS A 292 ? N HIS A 292 O LYS A 304 ? O LYS A 304 AD 1 2 O LEU A 41 ? O LEU A 41 N GLY A 272 ? N GLY A 272 AE 1 2 O LEU A 50 ? O LEU A 50 N VAL A 80 ? N VAL A 80 AE 2 3 N GLU A 81 ? N GLU A 81 O MET A 265 ? O MET A 265 AF 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AF 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AF 3 4 N GLY A 177 ? N GLY A 177 O ILE A 248 ? O ILE A 248 AF 4 5 N ALA A 249 ? N ALA A 249 O VAL A 148 ? O VAL A 148 AG 1 2 N ASP A 94 ? N ASP A 94 O MET A 226 ? O MET A 226 AG 2 3 N LEU A 233 ? N LEU A 233 O LEU A 172 ? O LEU A 172 AG 3 4 N LEU A 173 ? N LEU A 173 O TYR A 254 ? O TYR A 254 AG 4 5 O LYS A 258 ? O LYS A 258 N ASN A 109 ? N ASN A 109 AH 1 2 N TYR A 137 ? N TYR A 137 O LYS A 140 ? O LYS A 140 AI 1 2 N TYR A 164 ? N TYR A 164 O ILE A 239 ? O ILE A 239 AI 2 3 N GLU A 242 ? N GLU A 242 O SER A 199 ? O SER A 199 AI 3 4 N VAL A 200 ? N VAL A 200 O GLN A 207 ? O GLN A 207 AJ 1 2 N GLY A 283 ? N GLY A 283 O THR A 280 ? O THR A 280 AJ 2 3 N GLN A 279 ? N GLN A 279 O ILE A 299 ? O ILE A 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE EPE B 1163' AC2 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1023 bound to ASN A 23' AC3 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A1165 bound to ASN A 165' AC4 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG B1154 bound to ASN B 154' AC5 Software ? ? ? ? 13 'Binding site for Poly-Saccharide residues SIA A1322 through GAL A1323' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 5 TRP B 14 ? TRP B 14 . ? 1_555 ? 2 AC1 5 HIS B 25 ? HIS B 25 . ? 1_555 ? 3 AC1 5 TYR B 34 ? TYR B 34 . ? 1_555 ? 4 AC1 5 ASN B 135 ? ASN B 135 . ? 1_555 ? 5 AC1 5 CYS B 137 ? CYS B 137 . ? 1_555 ? 6 AC2 1 ASN A 23 ? ASN A 23 . ? 1_555 ? 7 AC3 3 ASN A 165 ? ASN A 165 . ? 1_555 ? 8 AC3 3 ASN A 236 ? ASN A 236 . ? 1_555 ? 9 AC3 3 HOH I . ? HOH A 2121 . ? 1_555 ? 10 AC4 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 11 AC4 3 GLU B 150 ? GLU B 150 . ? 1_555 ? 12 AC4 3 ASN B 154 ? ASN B 154 . ? 1_555 ? 13 AC5 13 TYR A 91 ? TYR A 91 . ? 1_555 ? 14 AC5 13 LEU A 129 ? LEU A 129 . ? 1_555 ? 15 AC5 13 VAL A 131 ? VAL A 131 . ? 1_555 ? 16 AC5 13 SER A 132 ? SER A 132 . ? 1_555 ? 17 AC5 13 SER A 133 ? SER A 133 . ? 1_555 ? 18 AC5 13 HIS A 179 ? HIS A 179 . ? 1_555 ? 19 AC5 13 ASN A 182 ? ASN A 182 . ? 1_555 ? 20 AC5 13 GLU A 186 ? GLU A 186 . ? 1_555 ? 21 AC5 13 LEU A 190 ? LEU A 190 . ? 1_555 ? 22 AC5 13 GLY A 221 ? GLY A 221 . ? 1_555 ? 23 AC5 13 GLN A 222 ? GLN A 222 . ? 1_555 ? 24 AC5 13 HOH I . ? HOH A 2065 . ? 1_555 ? 25 AC5 13 HOH I . ? HOH A 2122 . ? 1_555 ? # _database_PDB_matrix.entry_id 4BGX _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 4BGX _atom_sites.fract_transf_matrix[1][1] 0.009868 _atom_sites.fract_transf_matrix[1][2] 0.005697 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.011395 _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] 0.002217 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 1 ? 36.904 -15.613 -83.472 1.00 59.76 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 36.073 -16.202 -82.391 1.00 60.47 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 36.966 -16.910 -81.381 1.00 58.94 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 37.919 -17.567 -81.770 1.00 55.40 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 35.053 -17.195 -82.964 1.00 60.96 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 34.065 -16.541 -83.881 1.00 63.27 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 34.307 -15.385 -84.286 1.00 63.43 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 33.035 -17.180 -84.195 1.00 68.81 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? 36.639 -16.766 -80.094 1.00 59.35 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? 37.425 -17.349 -79.024 1.00 56.12 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? 36.631 -17.690 -77.781 1.00 55.14 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? 35.560 -17.131 -77.528 1.00 54.38 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? 38.592 -16.440 -78.652 1.00 57.24 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? 38.262 -15.118 -78.028 1.00 61.13 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? 39.504 -14.406 -77.503 1.00 63.31 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? 39.467 -13.786 -76.434 1.00 68.67 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? 40.596 -14.473 -78.252 1.00 61.39 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? 37.168 -18.643 -77.022 1.00 52.29 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 36.650 -18.963 -75.708 1.00 51.63 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 37.807 -18.925 -74.738 1.00 50.32 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 38.905 -19.394 -75.057 1.00 50.40 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 35.894 -20.313 -75.687 1.00 53.30 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 35.220 -20.537 -74.331 1.00 54.60 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 36.792 -21.492 -76.005 1.00 51.03 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 34.026 -21.459 -74.449 1.00 56.50 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 37.574 -18.345 -73.565 1.00 50.58 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 38.632 -18.161 -72.562 1.00 49.86 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 38.243 -18.812 -71.269 1.00 48.10 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 37.062 -18.868 -70.951 1.00 47.65 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 38.843 -16.681 -72.283 1.00 52.29 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 39.159 -15.736 -73.769 1.00 55.99 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? 39.231 -19.290 -70.519 1.00 45.66 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? 38.988 -19.785 -69.185 1.00 45.28 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? 39.479 -18.748 -68.189 1.00 46.35 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? 40.566 -18.174 -68.346 1.00 44.97 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? 39.723 -21.097 -68.946 1.00 45.29 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? 39.297 -22.115 -69.986 1.00 47.23 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? 39.477 -21.608 -67.541 1.00 44.46 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? 37.811 -22.264 -70.063 1.00 51.28 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? 38.683 -18.512 -67.151 1.00 46.54 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 39.023 -17.478 -66.190 1.00 46.98 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 38.378 -17.667 -64.854 1.00 46.70 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 37.681 -18.643 -64.621 1.00 49.83 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? 38.597 -16.703 -63.981 1.00 46.48 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? 38.158 -16.827 -62.620 1.00 46.80 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? 37.562 -15.535 -62.107 1.00 47.91 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? 37.748 -14.481 -62.687 1.00 47.53 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? 39.312 -17.289 -61.741 1.00 46.28 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? 40.575 -16.467 -61.835 1.00 46.02 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? 41.492 -16.673 -62.847 1.00 45.42 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? 40.868 -15.505 -60.875 1.00 47.61 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? 42.647 -15.896 -62.924 1.00 47.63 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? 42.024 -14.743 -60.939 1.00 47.06 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? 42.904 -14.935 -61.956 1.00 47.14 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? 44.032 -14.152 -61.998 1.00 48.58 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? 36.839 -15.660 -61.006 1.00 48.99 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? 36.098 -14.575 -60.376 1.00 51.66 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? 36.997 -13.509 -59.780 1.00 51.68 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? 38.072 -13.792 -59.255 1.00 50.73 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? 35.245 -15.188 -59.265 1.00 53.15 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? 34.380 -14.222 -58.529 1.00 55.50 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? 33.285 -13.606 -59.104 1.00 58.33 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? 34.402 -13.820 -57.237 1.00 55.26 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? 32.696 -12.834 -58.207 1.00 58.14 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? 33.353 -12.947 -57.066 1.00 55.97 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? 36.543 -12.267 -59.862 1.00 53.75 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? 37.141 -11.174 -59.109 1.00 53.75 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? 36.010 -10.322 -58.558 1.00 56.15 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? 34.870 -10.444 -58.997 1.00 60.26 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? 38.070 -10.366 -59.988 1.00 53.13 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? 36.299 -9.492 -57.571 1.00 55.55 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? 35.272 -8.649 -57.003 1.00 58.13 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? 35.894 -7.468 -56.279 1.00 59.79 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? 37.083 -7.248 -56.398 1.00 59.31 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? 34.354 -9.463 -56.097 1.00 58.23 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? 35.044 -9.939 -54.840 1.00 57.54 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? 36.119 -9.477 -54.495 1.00 56.69 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? 34.420 -10.875 -54.153 1.00 58.13 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? 35.087 -6.708 -55.551 1.00 63.98 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? 35.555 -5.480 -54.921 1.00 67.78 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? 36.090 -5.704 -53.493 1.00 66.27 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? 36.330 -4.735 -52.763 1.00 68.37 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? 34.447 -4.396 -54.976 1.00 71.74 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? 33.236 -4.727 -54.094 1.00 77.12 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? 33.270 -5.687 -53.316 1.00 79.28 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? 32.149 -3.936 -54.219 1.00 81.97 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? 36.307 -6.968 -53.115 1.00 61.89 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? 36.723 -7.326 -51.763 1.00 59.75 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? 38.124 -6.817 -51.442 1.00 60.44 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? 39.017 -6.834 -52.295 1.00 57.33 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? 36.688 -8.849 -51.572 1.00 58.52 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? 37.004 -9.244 -50.245 1.00 55.98 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? 38.287 -6.353 -50.202 1.00 62.59 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? 39.578 -5.977 -49.648 1.00 62.90 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? 39.912 -6.822 -48.428 1.00 62.41 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? 40.828 -6.472 -47.701 1.00 63.28 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? 39.585 -4.512 -49.174 1.00 65.71 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? 38.563 -4.336 -48.183 1.00 67.71 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? 39.356 -3.550 -50.337 1.00 67.19 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? 39.167 -7.900 -48.177 1.00 61.48 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? 39.533 -8.848 -47.132 1.00 63.08 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? 40.900 -9.459 -47.453 1.00 60.36 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? 41.200 -9.743 -48.611 1.00 59.87 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? 38.511 -9.980 -47.043 1.00 67.17 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? 37.100 -9.557 -46.676 1.00 72.78 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? 37.001 -9.059 -45.248 1.00 80.95 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? 37.491 -9.788 -44.350 1.00 82.14 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? 36.449 -7.938 -45.027 1.00 88.28 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? 41.716 -9.668 -46.425 1.00 58.63 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? 43.073 -10.188 -46.585 1.00 55.06 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? 43.302 -11.384 -45.681 1.00 52.50 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? 42.741 -11.450 -44.606 1.00 51.05 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? 44.082 -9.116 -46.199 1.00 56.61 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? 43.994 -7.827 -46.986 1.00 59.36 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? 45.117 -6.867 -46.653 1.00 62.00 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? 45.626 -6.170 -47.524 1.00 64.77 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? 45.507 -6.824 -45.385 1.00 63.64 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? 44.155 -12.311 -46.102 1.00 50.66 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? 44.520 -13.456 -45.278 1.00 48.57 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? 46.015 -13.611 -45.298 1.00 49.20 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? 46.662 -13.124 -46.222 1.00 49.96 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? 43.876 -14.769 -45.778 1.00 47.23 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? 42.377 -14.627 -45.819 1.00 47.99 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? 44.385 -15.167 -47.156 1.00 46.88 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? 46.561 -14.295 -44.289 1.00 49.15 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? 47.990 -14.618 -44.258 1.00 48.01 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? 48.223 -16.071 -44.628 1.00 46.20 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? 47.400 -16.935 -44.344 1.00 44.13 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? 48.569 -14.390 -42.872 1.00 49.74 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? 48.608 -12.926 -42.478 1.00 52.71 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? 48.667 -12.048 -43.380 1.00 53.76 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? 48.600 -12.659 -41.240 1.00 54.64 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? 49.353 -16.319 -45.281 1.00 47.01 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? 49.876 -17.674 -45.542 1.00 46.11 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? 51.316 -17.720 -45.019 1.00 46.48 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? 51.848 -16.699 -44.581 1.00 47.74 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? 49.900 -17.984 -47.052 1.00 45.21 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? 50.736 -17.037 -47.728 1.00 49.25 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? 48.563 -17.870 -47.632 1.00 43.96 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? 51.954 -18.882 -45.067 1.00 47.36 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? 53.351 -19.028 -44.605 1.00 47.23 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? 54.329 -18.148 -45.410 1.00 47.66 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? 55.248 -17.530 -44.866 1.00 47.06 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? 53.799 -20.493 -44.787 1.00 49.86 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? 53.011 -21.440 -43.874 1.00 52.68 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? 55.278 -20.665 -44.524 1.00 51.61 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? 53.391 -21.383 -42.411 1.00 52.55 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? 54.125 -18.125 -46.721 1.00 48.85 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? 55.040 -17.479 -47.662 1.00 50.89 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? 54.688 -16.034 -48.013 1.00 51.38 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? 55.496 -15.344 -48.645 1.00 51.15 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? 55.073 -18.262 -48.969 1.00 49.59 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? 56.040 -19.426 -48.981 1.00 50.76 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? 56.122 -20.124 -50.621 1.00 54.36 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? 57.608 -21.045 -50.436 1.00 57.34 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? 53.486 -15.603 -47.641 1.00 50.16 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? 52.972 -14.306 -48.034 1.00 52.26 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? 51.912 -13.822 -47.042 1.00 52.69 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? 50.999 -14.567 -46.673 1.00 52.81 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? 52.389 -14.344 -49.456 1.00 52.03 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? 52.213 -12.948 -50.042 1.00 55.73 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? 51.767 -12.916 -51.507 1.00 59.16 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? 51.643 -14.006 -52.130 1.00 54.01 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? 51.555 -11.768 -52.022 1.00 60.39 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? 52.043 -12.570 -46.625 1.00 54.32 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? 51.110 -11.952 -45.705 1.00 56.50 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? 50.241 -10.942 -46.445 1.00 54.99 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? 50.628 -10.424 -47.502 1.00 55.11 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? 51.892 -11.334 -44.546 1.00 62.14 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? 52.615 -12.417 -43.739 1.00 66.30 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? 53.665 -11.868 -42.788 1.00 73.74 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? 53.043 -11.334 -41.497 1.00 78.01 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? 54.013 -11.213 -40.371 1.00 77.14 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? 49.046 -10.703 -45.920 1.00 52.80 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? 48.145 -9.696 -46.478 1.00 55.07 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? 47.743 -9.917 -47.934 1.00 53.26 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? 47.735 -8.984 -48.724 1.00 53.69 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? 48.753 -8.295 -46.297 1.00 59.08 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? 48.869 -7.908 -44.850 1.00 64.86 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? 48.364 -8.622 -43.981 1.00 66.08 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? 49.516 -6.778 -44.570 1.00 75.21 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? 47.377 -11.152 -48.266 1.00 51.60 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? 46.894 -11.511 -49.598 1.00 49.15 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? 45.407 -11.167 -49.716 1.00 49.00 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? 44.598 -11.666 -48.947 1.00 47.56 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? 47.078 -13.018 -49.832 1.00 47.69 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? 46.555 -13.426 -51.207 1.00 48.05 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? 48.546 -13.396 -49.674 1.00 47.10 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? 45.042 -10.301 -50.656 1.00 49.15 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? 43.635 -9.940 -50.826 1.00 49.63 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? 42.878 -11.084 -51.478 1.00 48.76 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? 43.341 -11.657 -52.471 1.00 49.43 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? 43.464 -8.705 -51.705 1.00 51.19 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? 44.301 -7.662 -51.214 1.00 53.77 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? 42.044 -8.215 -51.651 1.00 53.76 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? 41.719 -11.418 -50.926 1.00 47.78 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? 40.947 -12.540 -51.410 1.00 46.16 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? 39.517 -12.109 -51.634 1.00 49.43 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? 39.071 -11.114 -51.075 1.00 53.53 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? 41.017 -13.739 -50.460 1.00 44.30 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? 42.434 -14.276 -50.405 1.00 42.91 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? 40.549 -13.379 -49.064 1.00 45.61 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? 38.814 -12.857 -52.479 1.00 49.39 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? 37.474 -12.522 -52.898 1.00 49.34 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? 36.485 -12.813 -51.806 1.00 50.59 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? 35.466 -12.140 -51.699 1.00 55.11 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? 37.063 -13.307 -54.161 1.00 49.99 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? 37.069 -14.723 -53.911 1.00 48.40 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? 38.014 -13.005 -55.291 1.00 50.11 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? 36.777 -13.823 -51.006 1.00 50.10 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? 35.941 -14.210 -49.880 1.00 51.18 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? 36.774 -14.790 -48.759 1.00 51.05 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? 37.766 -15.491 -48.997 1.00 50.58 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? 34.935 -15.259 -50.312 1.00 52.61 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? 34.120 -14.853 -51.489 1.00 54.21 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? 34.585 -14.957 -52.781 1.00 53.96 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? 32.882 -14.315 -51.572 1.00 55.40 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? 33.662 -14.509 -53.610 1.00 54.47 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? 32.620 -14.114 -52.902 1.00 54.99 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? 36.334 -14.535 -47.535 1.00 52.03 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? 37.045 -14.973 -46.344 1.00 52.24 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? 36.063 -15.137 -45.210 1.00 54.30 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? 34.918 -14.688 -45.300 1.00 59.73 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? 38.120 -13.975 -45.964 1.00 51.98 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? 36.510 -15.779 -44.146 1.00 53.88 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? 35.658 -16.041 -43.001 1.00 56.34 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? 36.442 -15.839 -41.713 1.00 54.74 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? 37.330 -16.627 -41.377 1.00 49.51 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? 35.086 -17.464 -43.052 1.00 58.51 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? 34.173 -17.778 -41.869 1.00 62.31 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? 33.464 -19.110 -41.988 1.00 63.89 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? 33.120 -19.551 -43.073 1.00 66.68 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? 33.234 -19.750 -40.863 1.00 66.86 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? 36.106 -14.770 -41.003 1.00 56.64 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? 36.625 -14.535 -39.662 1.00 58.24 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? 36.100 -15.653 -38.728 1.00 58.49 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? 34.916 -16.006 -38.786 1.00 59.77 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? 36.162 -13.169 -39.182 1.00 60.04 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? 36.920 -12.680 -37.977 1.00 61.21 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? 37.584 -13.494 -37.306 1.00 57.73 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? 36.845 -11.463 -37.701 1.00 63.91 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? 36.984 -16.213 -37.899 1.00 54.98 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? 36.602 -17.258 -36.942 1.00 53.33 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? 36.934 -16.918 -35.481 1.00 52.20 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? 36.783 -17.768 -34.612 1.00 49.63 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? 37.256 -18.607 -37.302 1.00 52.59 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? 38.776 -18.480 -37.384 1.00 50.82 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? 36.716 -19.111 -38.624 1.00 54.21 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? 39.466 -19.826 -37.441 1.00 50.42 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? 37.376 -15.685 -35.230 1.00 52.19 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? 37.750 -15.221 -33.906 1.00 54.07 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? 36.817 -14.120 -33.427 1.00 58.04 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? 36.725 -13.055 -34.048 1.00 60.75 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? 39.170 -14.661 -33.929 1.00 53.89 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? 39.749 -14.210 -32.587 1.00 54.54 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? 39.954 -15.411 -31.661 1.00 54.18 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? 41.070 -13.478 -32.795 1.00 55.77 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? 36.146 -14.367 -32.306 1.00 60.53 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? 35.315 -13.358 -31.681 1.00 61.26 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? 36.181 -12.428 -30.856 1.00 60.86 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? 36.879 -12.881 -29.963 1.00 61.04 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? 34.267 -14.016 -30.786 1.00 63.49 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? 33.332 -13.019 -30.122 1.00 65.11 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? 32.765 -12.042 -31.119 1.00 67.18 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? 32.036 -12.485 -32.034 1.00 70.80 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? 33.079 -10.841 -31.010 1.00 68.60 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? 36.124 -11.131 -31.146 1.00 63.07 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? 36.938 -10.131 -30.436 1.00 63.31 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? 36.144 -9.231 -29.485 1.00 63.35 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? 36.747 -8.536 -28.662 1.00 62.07 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? 37.703 -9.247 -31.426 1.00 63.43 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? 38.692 -9.996 -32.301 1.00 62.98 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? 39.196 -9.117 -33.440 1.00 65.05 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? 39.128 -9.822 -34.788 1.00 65.73 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? 37.784 -10.405 -35.144 1.00 65.68 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? 34.817 -9.253 -29.574 1.00 63.74 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? 33.992 -8.343 -28.775 1.00 68.18 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? 33.233 -9.040 -27.657 1.00 68.75 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? 32.864 -10.211 -27.775 1.00 66.18 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? 32.956 -7.595 -29.640 1.00 70.56 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? 32.060 -8.539 -30.232 1.00 73.10 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? 33.637 -6.798 -30.743 1.00 70.78 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? 33.004 -8.282 -26.584 1.00 69.83 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? 32.146 -8.683 -25.462 1.00 71.28 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? 31.287 -7.460 -25.071 1.00 75.20 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? 31.545 -6.352 -25.536 1.00 76.27 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? 32.989 -9.151 -24.270 1.00 68.57 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? 33.947 -8.117 -23.768 1.00 69.54 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? 33.607 -7.203 -22.794 1.00 72.40 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? 35.224 -7.832 -24.117 1.00 69.19 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? 34.634 -6.409 -22.550 1.00 72.21 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? 35.631 -6.771 -23.339 1.00 71.32 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? 30.275 -7.654 -24.227 1.00 77.48 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? 29.369 -6.552 -23.855 1.00 80.54 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? 29.814 -5.764 -22.611 1.00 82.19 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? 29.164 -4.797 -22.225 1.00 87.55 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? 27.921 -7.054 -23.677 1.00 80.63 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? 27.716 -7.836 -22.398 1.00 78.97 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? 28.649 -8.058 -21.638 1.00 78.14 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? 26.489 -8.272 -22.164 1.00 79.63 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? 30.880 -6.209 -21.958 1.00 80.07 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? 31.501 -5.451 -20.865 1.00 79.73 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? 30.777 -5.563 -19.532 1.00 79.87 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? 31.026 -4.766 -18.633 1.00 76.79 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? 29.902 -6.567 -19.412 1.00 80.66 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? 28.995 -6.707 -18.284 1.00 82.37 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? 28.992 -8.101 -17.684 1.00 81.59 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? 29.290 -9.083 -18.361 1.00 81.01 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? 27.576 -6.384 -18.741 1.00 86.03 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? 27.356 -4.915 -19.055 1.00 89.67 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? 26.087 -4.668 -19.846 1.00 92.30 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? 25.930 -3.180 -20.116 1.00 97.07 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? 24.886 -2.891 -21.136 1.00 101.03 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? 28.635 -8.180 -16.407 1.00 83.84 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? 28.329 -9.456 -15.764 1.00 84.61 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? 26.828 -9.729 -15.890 1.00 84.33 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? 26.006 -8.848 -15.602 1.00 86.18 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? 28.759 -9.424 -14.297 1.00 86.51 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? 30.256 -9.176 -14.084 1.00 87.39 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? 30.557 -9.030 -12.606 1.00 88.69 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? 31.106 -10.287 -14.687 1.00 85.88 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? 26.473 -10.936 -16.325 1.00 81.60 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? 25.089 -11.232 -16.705 1.00 84.32 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? 24.599 -12.538 -16.160 1.00 82.12 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? 25.385 -13.375 -15.738 1.00 80.25 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? 24.937 -11.304 -18.238 1.00 85.78 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? 25.719 -9.968 -19.162 1.00 85.69 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? 23.285 -12.723 -16.219 1.00 84.21 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? 22.692 -14.011 -15.891 1.00 84.73 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? 23.229 -15.015 -16.892 1.00 82.84 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? 23.405 -14.690 -18.060 1.00 82.29 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? 21.160 -13.986 -15.984 1.00 88.72 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? 20.504 -13.007 -15.013 1.00 90.81 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? 21.153 -12.533 -14.064 1.00 89.97 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? 19.309 -12.707 -15.212 1.00 93.97 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? 23.511 -16.222 -16.422 1.00 84.58 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? 23.929 -17.323 -17.273 1.00 85.00 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? 22.700 -18.190 -17.501 1.00 91.85 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? 22.218 -18.836 -16.577 1.00 94.35 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? 25.042 -18.129 -16.593 1.00 82.13 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? 25.634 -19.351 -17.316 1.00 81.37 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? 26.325 -18.969 -18.620 1.00 80.85 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? 26.607 -20.097 -16.424 1.00 79.30 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? 22.175 -18.182 -18.725 1.00 99.14 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? 20.959 -18.926 -19.054 1.00 102.91 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? 19.853 -18.625 -18.076 1.00 102.19 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? 19.241 -19.540 -17.535 1.00 101.62 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? 21.226 -20.437 -19.091 1.00 108.90 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? 20.954 -21.036 -20.451 1.00 115.53 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? 21.885 -21.046 -21.296 1.00 114.28 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? 19.800 -21.487 -20.669 1.00 121.13 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? 19.633 -17.332 -17.838 1.00 102.59 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? 18.547 -16.850 -16.989 1.00 102.18 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? 18.802 -16.929 -15.491 1.00 101.32 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? 18.081 -16.298 -14.720 1.00 103.27 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? 19.819 -17.696 -15.080 1.00 97.73 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? 20.137 -17.915 -13.661 1.00 94.25 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? 21.222 -16.939 -13.208 1.00 91.62 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? 22.373 -17.041 -13.619 1.00 89.00 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? 20.619 -19.358 -13.404 1.00 92.47 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? 20.880 -19.576 -11.922 1.00 93.72 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? 19.597 -20.366 -13.906 1.00 93.31 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? 20.845 -16.013 -12.338 1.00 92.86 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? 21.724 -14.930 -11.874 1.00 91.97 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? 22.944 -15.433 -11.102 1.00 87.70 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? 22.874 -16.461 -10.418 1.00 86.33 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? 20.895 -13.991 -10.988 1.00 97.57 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? 21.522 -12.670 -10.559 1.00 100.03 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? 20.596 -11.960 -9.558 1.00 105.18 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? 21.264 -10.794 -8.836 1.00 106.46 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? 21.701 -9.727 -9.785 1.00 107.40 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? 24.080 -14.716 -11.222 1.00 84.96 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? 25.237 -15.043 -10.390 1.00 81.17 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? 25.107 -14.450 -9.010 1.00 79.47 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? 24.365 -13.493 -8.833 1.00 80.57 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? 26.392 -14.355 -11.108 1.00 79.04 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? 25.770 -13.168 -11.751 1.00 81.25 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? 24.391 -13.624 -12.170 1.00 84.02 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? 25.835 -15.020 -8.054 1.00 76.62 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? 25.991 -14.430 -6.735 1.00 76.20 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? 27.072 -13.371 -6.812 1.00 76.24 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? 28.251 -13.702 -6.929 1.00 76.80 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? 26.376 -15.503 -5.714 1.00 75.06 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? 26.637 -15.085 -4.262 1.00 75.41 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? 25.367 -14.554 -3.637 1.00 77.52 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? 27.177 -16.246 -3.441 1.00 74.44 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? 26.682 -12.102 -6.780 1.00 78.99 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? 27.659 -11.016 -6.798 1.00 79.54 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? 27.895 -10.565 -5.365 1.00 79.85 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? 27.082 -9.840 -4.791 1.00 81.58 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? 27.215 -9.854 -7.712 1.00 82.13 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? 27.050 -10.375 -9.143 1.00 83.39 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? 28.234 -8.717 -7.691 1.00 82.36 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? 26.997 -9.304 -10.221 1.00 85.93 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? 29.022 -10.996 -4.798 1.00 77.29 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? 29.354 -10.717 -3.401 1.00 77.15 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? 29.696 -9.253 -3.118 1.00 79.46 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? 29.868 -8.873 -1.957 1.00 81.12 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? 30.501 -11.625 -2.939 1.00 74.22 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? 30.202 -13.128 -2.933 1.00 72.75 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? 31.440 -13.948 -2.608 1.00 70.42 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? 29.094 -13.453 -1.945 1.00 75.26 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? 29.805 -8.444 -4.168 1.00 80.87 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? 29.978 -7.005 -4.040 1.00 85.60 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? 31.260 -6.666 -3.256 1.00 86.27 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? 32.362 -6.899 -3.765 1.00 86.69 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? 28.717 -6.392 -3.431 1.00 92.14 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? 28.537 -4.901 -3.686 1.00 97.58 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? 27.347 -4.352 -2.902 1.00 103.02 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? 26.371 -3.697 -3.776 1.00 107.06 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? 25.475 -4.330 -4.537 1.00 107.31 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? 25.403 -5.660 -4.565 1.00 104.95 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? 24.642 -3.622 -5.288 1.00 109.47 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? 31.146 -6.128 -2.041 1.00 87.39 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? 32.329 -5.848 -1.224 1.00 86.88 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? 32.631 -6.933 -0.183 1.00 84.78 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? 33.510 -6.738 0.654 1.00 85.02 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? 32.171 -4.505 -0.509 1.00 90.48 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? 32.184 -3.320 -1.463 1.00 92.34 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? 32.974 -3.336 -2.432 1.00 88.80 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? 31.417 -2.357 -1.213 1.00 95.85 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? 31.911 -8.057 -0.222 1.00 82.69 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? 32.154 -9.166 0.709 1.00 81.13 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? 32.999 -10.265 0.069 1.00 77.15 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? 32.998 -10.435 -1.138 1.00 76.10 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? 30.833 -9.769 1.220 1.00 82.23 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? 29.810 -8.612 2.159 1.00 87.21 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? 33.714 -11.007 0.908 1.00 75.07 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? 34.458 -12.187 0.496 1.00 72.08 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? 33.642 -13.439 0.784 1.00 71.01 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? 32.627 -13.397 1.462 1.00 72.32 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? 35.760 -12.276 1.293 1.00 72.18 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? 35.506 -12.748 2.613 1.00 72.17 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? 34.114 -14.574 0.304 1.00 69.93 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? 33.444 -15.840 0.590 1.00 70.05 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? 33.425 -16.100 2.110 1.00 71.47 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? 32.445 -16.642 2.650 1.00 72.80 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? 34.097 -16.996 -0.201 1.00 68.63 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? 33.596 -18.350 0.271 1.00 69.27 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? 33.814 -16.822 -1.692 1.00 68.42 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? 34.492 -15.689 2.793 1.00 70.18 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? 34.574 -15.833 4.231 1.00 71.23 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? 33.540 -14.932 4.933 1.00 73.17 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? 32.743 -15.413 5.744 1.00 73.16 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? 35.976 -15.521 4.703 1.00 70.72 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? 33.545 -13.641 4.598 1.00 74.00 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? 32.548 -12.698 5.096 1.00 74.96 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? 31.143 -13.243 4.899 1.00 76.97 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? 30.348 -13.303 5.839 1.00 78.68 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? 30.841 -13.668 3.676 1.00 76.08 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? 29.545 -14.234 3.372 1.00 76.79 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? 29.237 -15.399 4.303 1.00 78.51 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? 28.248 -15.368 5.043 1.00 82.58 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? 29.486 -14.676 1.910 1.00 76.24 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? 28.343 -15.583 1.556 1.00 76.54 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? 27.078 -15.538 2.047 1.00 80.16 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? 28.365 -16.649 0.603 1.00 75.73 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? 26.306 -16.519 1.465 1.00 80.79 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? 27.081 -17.218 0.580 1.00 78.27 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? 29.349 -17.179 -0.236 1.00 74.40 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? 26.758 -18.295 -0.245 1.00 78.63 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? 29.027 -18.249 -1.046 1.00 73.66 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? 27.743 -18.792 -1.050 1.00 74.87 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? 30.096 -16.409 4.287 1.00 77.35 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? 29.781 -17.686 4.938 1.00 77.35 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? 29.754 -17.629 6.466 1.00 78.30 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? 28.887 -18.235 7.100 1.00 78.81 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? 30.759 -18.762 4.473 1.00 75.26 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? 30.574 -19.197 3.019 1.00 74.50 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? 31.742 -20.075 2.602 1.00 74.23 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? 29.261 -19.933 2.807 1.00 75.07 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? 30.717 -16.914 7.042 1.00 78.52 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? 30.745 -16.657 8.486 1.00 78.85 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? 29.667 -15.669 8.921 1.00 80.91 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? 29.324 -15.612 10.094 1.00 82.60 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? 32.112 -16.129 8.907 1.00 77.26 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? 33.216 -17.177 8.852 1.00 75.46 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? 34.581 -16.512 8.921 1.00 74.38 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? 33.044 -18.186 9.977 1.00 76.56 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? 29.136 -14.896 7.979 1.00 81.47 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? 28.083 -13.942 8.281 1.00 83.48 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? 28.631 -12.670 8.896 1.00 83.71 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? 28.138 -12.210 9.916 1.00 84.71 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? 29.663 -12.111 8.277 1.00 82.70 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? 30.126 -10.777 8.611 1.00 84.02 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? 28.930 -9.829 8.560 1.00 86.70 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? 28.244 -9.783 7.546 1.00 85.92 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? 31.192 -10.348 7.599 1.00 82.93 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? 31.756 -8.965 7.880 1.00 83.98 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? 31.014 -8.013 8.094 1.00 85.89 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? 33.075 -8.849 7.860 1.00 83.05 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? 28.673 -9.066 9.647 1.00 90.49 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? 27.426 -8.273 9.760 1.00 93.48 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? 27.240 -7.170 8.700 1.00 95.16 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? 26.135 -6.649 8.551 1.00 97.85 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? 27.514 -7.672 11.166 1.00 94.85 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? 28.963 -7.662 11.498 1.00 93.34 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? 29.560 -8.854 10.805 1.00 91.28 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? 28.308 -6.834 7.977 1.00 94.27 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? 28.236 -5.956 6.802 1.00 94.72 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? 27.803 -6.709 5.533 1.00 92.35 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? 27.726 -6.120 4.452 1.00 91.04 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? 29.607 -5.326 6.548 1.00 95.05 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? 30.131 -4.459 7.681 1.00 98.33 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? 29.691 -2.725 7.477 1.00 104.97 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? 30.655 -1.977 8.789 1.00 105.89 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? 27.537 -8.007 5.660 1.00 90.73 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? 27.220 -8.867 4.513 1.00 89.29 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? 25.840 -9.486 4.677 1.00 91.16 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? 25.601 -10.639 4.284 1.00 89.31 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? 28.285 -9.956 4.373 1.00 85.72 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? 29.920 -9.239 4.103 1.00 84.21 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? 24.942 -8.699 5.265 1.00 93.60 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? 23.570 -9.118 5.497 1.00 95.65 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? 22.813 -9.296 4.189 1.00 96.70 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? 21.895 -10.107 4.128 1.00 98.40 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? 22.850 -8.112 6.403 1.00 98.24 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? 23.360 -8.147 7.829 1.00 97.95 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? 24.257 -8.967 8.113 1.00 96.95 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? 22.875 -7.360 8.672 1.00 98.77 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? 23.206 -8.563 3.143 1.00 96.75 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? 22.644 -8.771 1.797 1.00 97.21 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? 22.605 -10.262 1.428 1.00 95.63 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? 21.652 -10.737 0.800 1.00 95.76 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? 23.431 -7.984 0.732 1.00 96.62 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? 22.825 -8.049 -0.675 1.00 97.58 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? 23.629 -7.293 -1.727 1.00 96.88 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? 24.633 -6.641 -1.369 1.00 96.57 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? 23.255 -7.346 -2.921 1.00 97.41 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? 23.634 -10.993 1.853 1.00 93.80 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? 23.795 -12.400 1.501 1.00 92.17 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? 23.395 -13.352 2.637 1.00 93.32 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? 23.875 -14.487 2.714 1.00 90.80 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? 25.244 -12.630 1.055 1.00 88.80 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? 25.768 -11.542 0.161 1.00 87.29 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? 25.302 -11.422 -1.139 1.00 86.26 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? 26.687 -10.611 0.632 1.00 86.49 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? 25.766 -10.421 -1.965 1.00 85.76 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? 27.150 -9.599 -0.190 1.00 86.54 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? 26.688 -9.505 -1.493 1.00 85.91 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? 22.486 -12.899 3.494 1.00 97.22 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? 22.073 -13.691 4.647 1.00 100.05 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? 21.295 -14.936 4.234 1.00 101.44 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? 21.350 -15.944 4.929 1.00 100.36 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? 21.253 -12.854 5.667 1.00 103.79 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? 21.254 -13.535 7.036 1.00 103.72 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? 19.824 -12.590 5.181 1.00 104.99 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? 21.217 -12.551 8.180 1.00 105.25 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? 20.565 -14.861 3.121 1.00 103.92 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? 19.986 -16.054 2.494 1.00 105.94 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? 19.923 -15.929 0.979 1.00 105.06 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? 18.990 -15.357 0.422 1.00 106.91 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? 18.610 -16.378 3.081 1.00 111.03 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? 18.701 -17.298 4.284 1.00 113.70 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? 19.559 -18.183 4.334 1.00 113.38 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? 17.828 -17.095 5.260 1.00 116.81 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? 20.936 -16.477 0.318 1.00 103.73 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? 21.079 -16.322 -1.120 1.00 101.14 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? 20.404 -17.448 -1.875 1.00 100.13 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? 20.547 -18.620 -1.506 1.00 98.76 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? 22.554 -16.280 -1.541 1.00 99.35 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? 23.261 -15.153 -0.818 1.00 98.77 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? 23.254 -17.617 -1.296 1.00 99.02 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? 19.685 -17.103 -2.953 1.00 100.27 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? 19.096 -18.149 -3.774 1.00 101.14 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? 20.148 -18.840 -4.636 1.00 95.79 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? 21.317 -18.451 -4.638 1.00 92.04 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? 18.086 -17.390 -4.647 1.00 102.90 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? 18.665 -16.024 -4.773 1.00 102.67 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? 19.429 -15.757 -3.499 1.00 101.60 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? 19.708 -19.867 -5.349 1.00 95.61 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? 20.543 -20.581 -6.287 1.00 93.62 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? 21.302 -19.608 -7.205 1.00 89.79 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? 20.734 -18.627 -7.688 1.00 88.71 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? 19.671 -21.522 -7.116 1.00 96.48 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? 20.454 -22.365 -8.112 1.00 96.21 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? 19.571 -23.303 -8.912 1.00 98.06 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? 18.397 -23.531 -8.524 1.00 101.57 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? 20.063 -23.801 -9.942 1.00 96.69 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? 22.587 -19.880 -7.424 1.00 86.60 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? 23.417 -19.052 -8.306 1.00 84.39 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? 23.964 -19.878 -9.468 1.00 84.05 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? 23.938 -21.110 -9.436 1.00 85.52 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? 24.563 -18.388 -7.528 1.00 81.10 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? 25.538 -19.360 -6.920 1.00 78.97 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? 26.634 -19.909 -7.523 1.00 76.45 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? 25.513 -19.889 -5.588 1.00 78.65 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? 27.282 -20.755 -6.654 1.00 74.86 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? 26.618 -20.758 -5.460 1.00 76.40 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? 24.661 -19.715 -4.490 1.00 80.98 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? 26.891 -21.451 -4.285 1.00 77.19 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? 24.934 -20.408 -3.317 1.00 80.17 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? 26.032 -21.266 -3.226 1.00 78.50 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? 24.449 -19.181 -10.491 1.00 83.72 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? 25.021 -19.803 -11.690 1.00 81.04 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? 26.531 -19.803 -11.608 1.00 77.73 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? 27.181 -20.772 -11.975 1.00 76.56 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? 24.597 -19.013 -12.920 1.00 81.70 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? 24.833 -17.626 -12.726 1.00 82.67 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? 27.074 -18.680 -11.152 1.00 75.61 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? 28.484 -18.557 -10.799 1.00 70.56 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? 28.600 -17.503 -9.702 1.00 69.63 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? 27.620 -16.847 -9.367 1.00 70.52 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? 29.331 -18.182 -12.031 1.00 68.18 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? 28.926 -16.901 -12.742 1.00 67.69 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? 27.879 -16.881 -13.665 1.00 67.78 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? 29.600 -15.717 -12.500 1.00 67.34 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? 27.514 -15.710 -14.309 1.00 67.88 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? 29.240 -14.542 -13.137 1.00 67.69 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? 28.200 -14.541 -14.043 1.00 67.98 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? 27.860 -13.351 -14.663 1.00 68.50 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? 29.791 -17.338 -9.144 1.00 67.87 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? 30.003 -16.378 -8.062 1.00 68.97 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? 30.991 -15.310 -8.502 1.00 68.73 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? 31.954 -15.604 -9.220 1.00 67.92 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? 30.552 -17.095 -6.820 1.00 69.10 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? 29.491 -18.037 -6.252 1.00 70.61 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? 30.995 -16.101 -5.759 1.00 70.28 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? 30.018 -18.984 -5.201 1.00 70.86 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? 30.775 -14.071 -8.076 1.00 70.20 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? 31.720 -13.002 -8.412 1.00 70.36 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? 32.283 -12.346 -7.160 1.00 71.09 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? 31.538 -11.822 -6.348 1.00 72.35 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? 31.090 -11.924 -9.314 1.00 71.38 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? 32.130 -10.883 -9.703 1.00 71.63 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? 30.490 -12.560 -10.554 1.00 71.37 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? 33.609 -12.360 -7.046 1.00 70.92 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? 34.318 -11.809 -5.905 1.00 72.09 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? 35.361 -10.830 -6.405 1.00 72.62 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? 36.073 -11.105 -7.352 1.00 73.23 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? 35.004 -12.939 -5.142 1.00 72.11 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? 35.669 -12.524 -3.843 1.00 73.12 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? 36.347 -13.680 -3.137 1.00 73.02 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? 37.110 -14.410 -3.822 1.00 70.78 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? 36.112 -13.854 -1.907 1.00 73.06 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? 35.465 -9.681 -5.766 1.00 76.33 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? 36.516 -8.737 -6.111 1.00 78.47 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? 37.897 -9.289 -5.737 1.00 77.67 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? 38.020 -10.280 -5.005 1.00 74.58 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? 36.259 -7.384 -5.439 1.00 81.04 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? 35.021 -6.676 -5.970 1.00 83.12 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? 34.848 -5.291 -5.361 1.00 86.44 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? 33.912 -4.425 -6.190 1.00 89.77 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? 32.523 -4.966 -6.254 1.00 91.92 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? 38.933 -8.650 -6.273 1.00 80.04 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? 40.318 -9.037 -5.994 1.00 80.70 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? 40.674 -8.868 -4.508 1.00 82.34 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? 41.287 -9.757 -3.916 1.00 84.17 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? 41.279 -8.250 -6.879 1.00 79.96 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? 40.279 -7.744 -3.911 1.00 83.66 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? 40.480 -7.526 -2.478 1.00 86.06 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? 39.228 -6.981 -1.782 1.00 84.91 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? 39.150 -5.790 -1.490 1.00 85.12 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? 41.678 -6.595 -2.246 1.00 90.04 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? 42.992 -7.207 -2.722 1.00 92.25 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? 43.535 -8.127 -2.094 1.00 93.10 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? 43.507 -6.704 -3.843 1.00 92.97 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? 38.245 -7.858 -1.504 1.00 82.79 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? 37.023 -7.382 -0.857 1.00 85.17 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? 37.322 -6.773 0.504 1.00 85.82 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? 38.126 -7.331 1.240 1.00 86.84 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? 36.178 -8.657 -0.700 1.00 84.13 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? 36.763 -9.645 -1.647 1.00 80.91 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? 38.221 -9.316 -1.702 1.00 80.48 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? 36.687 -5.649 0.831 1.00 86.69 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? 36.935 -4.978 2.114 1.00 87.62 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? 36.286 -5.684 3.313 1.00 86.31 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? 36.816 -5.625 4.429 1.00 85.64 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? 36.481 -3.496 2.103 1.00 90.90 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? 37.112 -2.749 0.932 1.00 90.67 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? 34.958 -3.383 2.077 1.00 92.96 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? 35.139 -6.326 3.088 1.00 83.91 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? 34.419 -7.004 4.157 1.00 83.83 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? 34.746 -8.476 4.174 1.00 82.50 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? 33.974 -9.316 3.702 1.00 83.31 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? 32.917 -6.798 4.030 1.00 84.91 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? 32.507 -5.374 4.314 1.00 87.68 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? 32.955 -4.766 5.284 1.00 90.15 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? 31.641 -4.833 3.473 1.00 89.79 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? 35.907 -8.778 4.735 1.00 82.18 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? 36.375 -10.143 4.878 1.00 80.78 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? 36.197 -10.524 6.358 1.00 82.26 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? 35.087 -10.429 6.895 1.00 81.55 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? 37.833 -10.235 4.378 1.00 79.50 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? 38.292 -11.666 4.130 1.00 78.42 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? 37.450 -12.577 4.052 1.00 80.70 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? 39.509 -11.892 4.018 1.00 78.51 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? 37.277 -10.943 7.010 1.00 82.29 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? 37.260 -11.231 8.430 1.00 82.93 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? 37.350 -9.917 9.213 1.00 84.38 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? 38.439 -9.356 9.388 1.00 85.63 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? 38.422 -12.166 8.790 1.00 81.70 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? 38.444 -13.522 8.066 1.00 79.63 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? 39.720 -14.279 8.417 1.00 79.54 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? 37.206 -14.359 8.381 1.00 78.70 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? 36.198 -9.446 9.691 1.00 84.50 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? 36.107 -8.171 10.394 1.00 85.15 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? 36.892 -8.188 11.703 1.00 83.29 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? 37.601 -7.240 12.007 1.00 84.44 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? 34.643 -7.792 10.628 1.00 88.93 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? 33.640 -9.055 11.447 1.00 91.46 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? 36.749 -9.263 12.469 1.00 81.10 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? 37.671 -9.578 13.548 1.00 80.76 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? 38.840 -10.316 12.916 1.00 79.21 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? 38.638 -11.331 12.251 1.00 78.79 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? 36.999 -10.468 14.596 1.00 81.70 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? 37.709 -10.457 15.932 1.00 83.54 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? 38.871 -11.197 16.132 1.00 83.40 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? 37.239 -9.677 16.990 1.00 84.65 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? 39.528 -11.177 17.354 1.00 84.26 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? 37.892 -9.651 18.209 1.00 85.17 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? 39.034 -10.398 18.389 1.00 84.75 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? 39.681 -10.364 19.605 1.00 85.39 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? 40.070 -9.828 13.111 1.00 79.10 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? 41.180 -10.417 12.366 1.00 77.43 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? 41.450 -11.876 12.707 1.00 77.48 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? 41.066 -12.358 13.775 1.00 77.82 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? 42.375 -9.556 12.778 1.00 78.54 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? 42.020 -9.055 14.136 1.00 80.51 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? 40.535 -8.836 14.096 1.00 80.94 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? 42.109 -12.570 11.789 1.00 78.88 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? 42.496 -13.957 12.003 1.00 79.79 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? 42.828 -14.715 10.732 1.00 80.20 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? 43.415 -14.164 9.798 1.00 79.28 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? 42.482 -16.001 10.725 1.00 80.40 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? 42.629 -16.849 9.554 1.00 79.44 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? 41.394 -17.697 9.394 1.00 77.45 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? 40.587 -17.837 10.315 1.00 77.79 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? 43.837 -17.775 9.682 1.00 81.32 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? 45.140 -17.015 9.874 1.00 84.60 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? 45.632 -16.407 8.890 1.00 85.19 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? 45.669 -17.031 11.011 1.00 87.73 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? 41.270 -18.263 8.202 1.00 75.32 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? 40.230 -19.209 7.877 1.00 72.01 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? 40.977 -20.442 7.397 1.00 70.84 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? 41.641 -20.423 6.366 1.00 69.99 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? 39.352 -18.617 6.794 1.00 71.23 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? 38.037 -19.300 6.627 1.00 71.22 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? 37.969 -20.612 6.210 1.00 71.77 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? 36.865 -18.615 6.846 1.00 72.03 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? 36.745 -21.232 6.024 1.00 73.48 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? 35.639 -19.228 6.667 1.00 73.11 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? 35.576 -20.541 6.266 1.00 73.07 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? 40.904 -21.508 8.173 1.00 70.68 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? 41.667 -22.704 7.878 1.00 70.55 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? 41.152 -23.436 6.628 1.00 69.01 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? 39.936 -23.581 6.436 1.00 66.96 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? 41.626 -23.625 9.095 1.00 72.86 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? 42.658 -24.712 9.022 1.00 74.23 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? 43.859 -24.442 9.083 1.00 74.74 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? 42.201 -25.952 8.869 1.00 75.41 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? 42.092 -23.899 5.800 1.00 69.35 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? 41.809 -24.586 4.520 1.00 68.71 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? 40.812 -23.802 3.667 1.00 65.79 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? 39.866 -24.370 3.100 1.00 63.57 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? 41.306 -26.022 4.758 1.00 72.29 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? 42.424 -26.990 5.114 1.00 75.00 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? 43.554 -26.812 4.617 1.00 77.30 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? 42.162 -27.947 5.876 1.00 78.61 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? 41.038 -22.492 3.597 1.00 64.10 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? 40.113 -21.570 2.944 1.00 64.03 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? 40.016 -21.877 1.453 1.00 63.12 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? 38.918 -21.975 0.905 1.00 63.49 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? 40.563 -20.121 3.184 1.00 63.99 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? 39.615 -19.028 2.703 1.00 65.11 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? 38.243 -19.102 2.952 1.00 66.52 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? 40.097 -17.897 2.023 1.00 64.40 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? 37.376 -18.098 2.534 1.00 66.64 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? 39.239 -16.891 1.600 1.00 64.76 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? 37.880 -17.000 1.860 1.00 66.66 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? 37.010 -16.020 1.462 1.00 68.99 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? 41.164 -22.081 0.817 1.00 61.56 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? 41.200 -22.295 -0.618 1.00 61.42 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? 40.549 -23.625 -0.984 1.00 61.48 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? 39.804 -23.709 -1.970 1.00 60.76 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? 42.634 -22.236 -1.157 1.00 61.45 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? 43.294 -20.860 -1.071 1.00 61.40 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? 43.664 -20.464 0.347 1.00 64.09 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? 43.774 -21.351 1.226 1.00 65.21 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? 43.828 -19.259 0.591 1.00 65.73 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? 40.811 -24.655 -0.180 1.00 61.62 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? 40.173 -25.943 -0.382 1.00 61.63 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? 38.652 -25.823 -0.258 1.00 63.32 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? 37.922 -26.552 -0.929 1.00 64.87 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? 40.709 -26.982 0.590 1.00 61.82 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? 42.043 -27.573 0.172 1.00 62.46 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? 41.960 -28.452 -1.062 1.00 62.73 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? 41.067 -29.330 -1.128 1.00 64.19 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? 42.791 -28.267 -1.973 1.00 61.80 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? 38.168 -24.909 0.576 1.00 63.44 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? 36.729 -24.710 0.685 1.00 64.77 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? 36.203 -23.984 -0.535 1.00 63.97 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? 35.176 -24.371 -1.091 1.00 62.92 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? 36.361 -23.928 1.941 1.00 65.70 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? 34.870 -23.676 2.161 1.00 66.67 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? 34.062 -24.966 2.228 1.00 67.19 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? 34.719 -22.875 3.438 1.00 68.79 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? 36.899 -22.931 -0.946 1.00 63.78 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? 36.511 -22.218 -2.152 1.00 64.45 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? 36.438 -23.166 -3.351 1.00 63.70 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? 35.563 -23.038 -4.198 1.00 63.36 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? 37.465 -21.071 -2.430 1.00 65.53 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? 37.334 -19.939 -1.428 1.00 69.49 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? 38.452 -18.907 -1.566 1.00 71.74 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? 38.054 -17.718 -2.434 1.00 73.56 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? 39.071 -16.637 -2.330 1.00 74.84 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? 37.354 -24.123 -3.416 1.00 63.37 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? 37.328 -25.097 -4.488 1.00 62.57 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? 36.057 -25.950 -4.433 1.00 64.47 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? 35.509 -26.337 -5.454 1.00 64.81 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? 38.548 -26.011 -4.429 1.00 61.36 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? 38.541 -27.054 -5.496 1.00 59.82 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? 39.006 -26.807 -6.769 1.00 58.67 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? 38.065 -28.318 -5.504 1.00 59.67 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? 38.844 -27.884 -7.510 1.00 58.07 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? 38.270 -28.813 -6.768 1.00 59.86 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? 35.625 -26.255 -3.224 1.00 66.78 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? 34.410 -27.020 -2.980 1.00 70.50 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? 33.163 -26.292 -3.507 1.00 71.67 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? 32.231 -26.918 -4.005 1.00 72.48 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? 34.271 -27.236 -1.468 1.00 73.01 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? 33.842 -28.597 -0.959 1.00 74.92 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? 34.803 -29.672 -1.435 1.00 75.29 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? 33.797 -28.546 0.553 1.00 76.37 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? 33.175 -24.967 -3.371 1.00 72.25 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? 32.107 -24.078 -3.833 1.00 72.64 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? 31.948 -24.035 -5.329 1.00 72.61 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? 30.887 -23.665 -5.828 1.00 77.64 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? 32.398 -22.641 -3.417 1.00 72.34 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? 31.840 -22.102 -2.131 1.00 73.76 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? 32.196 -20.627 -2.042 1.00 74.14 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? 30.334 -22.299 -2.113 1.00 77.29 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? 33.009 -24.351 -6.051 1.00 80.90 ? 106 SER A N 1 ATOM 834 C CA A SER A 1 106 ? 32.981 -24.356 -7.510 0.50 82.52 ? 106 SER A CA 1 ATOM 835 C CA B SER A 1 106 ? 32.948 -24.322 -7.497 0.50 82.47 ? 106 SER A CA 1 ATOM 836 C C . SER A 1 106 ? 32.105 -25.487 -8.027 1.00 84.53 ? 106 SER A C 1 ATOM 837 O O . SER A 1 106 ? 31.781 -25.536 -9.208 1.00 86.82 ? 106 SER A O 1 ATOM 838 C CB A SER A 1 106 ? 34.402 -24.488 -8.094 0.50 81.86 ? 106 SER A CB 1 ATOM 839 C CB B SER A 1 106 ? 34.367 -24.327 -8.066 0.50 81.75 ? 106 SER A CB 1 ATOM 840 O OG A SER A 1 106 ? 34.898 -25.822 -8.025 0.50 80.95 ? 106 SER A OG 1 ATOM 841 O OG B SER A 1 106 ? 35.127 -23.289 -7.458 0.50 78.98 ? 106 SER A OG 1 ATOM 842 N N . ARG A 1 107 ? 31.752 -26.413 -7.141 1.00 87.43 ? 107 ARG A N 1 ATOM 843 C CA . ARG A 1 107 ? 30.860 -27.521 -7.472 1.00 93.47 ? 107 ARG A CA 1 ATOM 844 C C . ARG A 1 107 ? 29.508 -27.372 -6.758 1.00 90.91 ? 107 ARG A C 1 ATOM 845 O O . ARG A 1 107 ? 28.755 -28.339 -6.659 1.00 92.01 ? 107 ARG A O 1 ATOM 846 C CB . ARG A 1 107 ? 31.486 -28.860 -7.063 1.00 99.28 ? 107 ARG A CB 1 ATOM 847 C CG . ARG A 1 107 ? 32.828 -29.194 -7.695 1.00 104.84 ? 107 ARG A CG 1 ATOM 848 C CD . ARG A 1 107 ? 33.629 -30.070 -6.732 1.00 111.12 ? 107 ARG A CD 1 ATOM 849 N NE . ARG A 1 107 ? 34.866 -30.626 -7.306 1.00 117.61 ? 107 ARG A NE 1 ATOM 850 C CZ . ARG A 1 107 ? 35.842 -31.209 -6.596 1.00 117.80 ? 107 ARG A CZ 1 ATOM 851 N NH1 . ARG A 1 107 ? 35.752 -31.317 -5.264 1.00 115.39 ? 107 ARG A NH1 1 ATOM 852 N NH2 . ARG A 1 107 ? 36.922 -31.683 -7.219 1.00 113.83 ? 107 ARG A NH2 1 ATOM 853 N N . ILE A 1 108 ? 29.209 -26.167 -6.267 1.00 86.88 ? 108 ILE A N 1 ATOM 854 C CA . ILE A 1 108 ? 27.975 -25.895 -5.528 1.00 84.65 ? 108 ILE A CA 1 ATOM 855 C C . ILE A 1 108 ? 27.220 -24.699 -6.122 1.00 84.67 ? 108 ILE A C 1 ATOM 856 O O . ILE A 1 108 ? 27.799 -23.637 -6.324 1.00 83.78 ? 108 ILE A O 1 ATOM 857 C CB . ILE A 1 108 ? 28.276 -25.630 -4.030 1.00 82.01 ? 108 ILE A CB 1 ATOM 858 C CG1 . ILE A 1 108 ? 28.841 -26.892 -3.370 1.00 80.82 ? 108 ILE A CG1 1 ATOM 859 C CG2 . ILE A 1 108 ? 27.025 -25.176 -3.293 1.00 81.48 ? 108 ILE A CG2 1 ATOM 860 C CD1 . ILE A 1 108 ? 29.372 -26.680 -1.970 1.00 79.09 ? 108 ILE A CD1 1 ATOM 861 N N . ASN A 1 109 ? 25.924 -24.878 -6.379 1.00 86.06 ? 109 ASN A N 1 ATOM 862 C CA . ASN A 1 109 ? 25.061 -23.806 -6.883 1.00 87.06 ? 109 ASN A CA 1 ATOM 863 C C . ASN A 1 109 ? 24.086 -23.254 -5.849 1.00 87.46 ? 109 ASN A C 1 ATOM 864 O O . ASN A 1 109 ? 23.509 -22.183 -6.067 1.00 86.49 ? 109 ASN A O 1 ATOM 865 C CB . ASN A 1 109 ? 24.248 -24.297 -8.078 1.00 90.21 ? 109 ASN A CB 1 ATOM 866 C CG . ASN A 1 109 ? 25.112 -24.623 -9.271 1.00 91.12 ? 109 ASN A CG 1 ATOM 867 O OD1 . ASN A 1 109 ? 25.733 -23.737 -9.866 1.00 89.74 ? 109 ASN A OD1 1 ATOM 868 N ND2 . ASN A 1 109 ? 25.158 -25.896 -9.633 1.00 93.15 ? 109 ASN A ND2 1 ATOM 869 N N . HIS A 1 110 ? 23.871 -23.975 -4.747 1.00 87.32 ? 110 HIS A N 1 ATOM 870 C CA . HIS A 1 110 ? 22.890 -23.528 -3.765 1.00 88.73 ? 110 HIS A CA 1 ATOM 871 C C . HIS A 1 110 ? 23.142 -24.029 -2.352 1.00 87.83 ? 110 HIS A C 1 ATOM 872 O O . HIS A 1 110 ? 23.365 -25.219 -2.113 1.00 85.96 ? 110 HIS A O 1 ATOM 873 C CB . HIS A 1 110 ? 21.476 -23.915 -4.217 1.00 93.20 ? 110 HIS A CB 1 ATOM 874 C CG . HIS A 1 110 ? 20.383 -23.188 -3.491 1.00 95.01 ? 110 HIS A CG 1 ATOM 875 N ND1 . HIS A 1 110 ? 19.111 -23.702 -3.354 1.00 97.22 ? 110 HIS A ND1 1 ATOM 876 C CD2 . HIS A 1 110 ? 20.374 -21.987 -2.862 1.00 94.54 ? 110 HIS A CD2 1 ATOM 877 C CE1 . HIS A 1 110 ? 18.365 -22.847 -2.678 1.00 98.18 ? 110 HIS A CE1 1 ATOM 878 N NE2 . HIS A 1 110 ? 19.109 -21.801 -2.364 1.00 96.15 ? 110 HIS A NE2 1 ATOM 879 N N . PHE A 1 111 ? 23.101 -23.082 -1.421 1.00 88.24 ? 111 PHE A N 1 ATOM 880 C CA . PHE A 1 111 ? 23.173 -23.370 -0.001 1.00 88.94 ? 111 PHE A CA 1 ATOM 881 C C . PHE A 1 111 ? 21.821 -23.043 0.587 1.00 91.60 ? 111 PHE A C 1 ATOM 882 O O . PHE A 1 111 ? 21.149 -22.132 0.114 1.00 93.37 ? 111 PHE A O 1 ATOM 883 C CB . PHE A 1 111 ? 24.221 -22.493 0.701 1.00 86.35 ? 111 PHE A CB 1 ATOM 884 C CG . PHE A 1 111 ? 25.641 -23.013 0.625 1.00 83.90 ? 111 PHE A CG 1 ATOM 885 C CD1 . PHE A 1 111 ? 25.937 -24.354 0.840 1.00 83.26 ? 111 PHE A CD1 1 ATOM 886 C CD2 . PHE A 1 111 ? 26.697 -22.131 0.402 1.00 81.12 ? 111 PHE A CD2 1 ATOM 887 C CE1 . PHE A 1 111 ? 27.244 -24.803 0.791 1.00 80.90 ? 111 PHE A CE1 1 ATOM 888 C CE2 . PHE A 1 111 ? 27.998 -22.579 0.358 1.00 78.78 ? 111 PHE A CE2 1 ATOM 889 C CZ . PHE A 1 111 ? 28.273 -23.916 0.553 1.00 79.16 ? 111 PHE A CZ 1 ATOM 890 N N . GLU A 1 112 ? 21.435 -23.783 1.620 1.00 93.46 ? 112 GLU A N 1 ATOM 891 C CA . GLU A 1 112 ? 20.216 -23.499 2.379 1.00 96.75 ? 112 GLU A CA 1 ATOM 892 C C . GLU A 1 112 ? 20.611 -23.444 3.857 1.00 93.17 ? 112 GLU A C 1 ATOM 893 O O . GLU A 1 112 ? 20.990 -24.457 4.444 1.00 90.35 ? 112 GLU A O 1 ATOM 894 C CB . GLU A 1 112 ? 19.162 -24.579 2.098 1.00 101.40 ? 112 GLU A CB 1 ATOM 895 C CG . GLU A 1 112 ? 17.719 -24.093 2.056 1.00 106.75 ? 112 GLU A CG 1 ATOM 896 C CD . GLU A 1 112 ? 16.942 -24.470 3.303 1.00 112.79 ? 112 GLU A CD 1 ATOM 897 O OE1 . GLU A 1 112 ? 17.286 -23.981 4.413 1.00 116.79 ? 112 GLU A OE1 1 ATOM 898 O OE2 . GLU A 1 112 ? 15.991 -25.273 3.174 1.00 116.65 ? 112 GLU A OE2 1 ATOM 899 N N . LYS A 1 113 ? 20.570 -22.250 4.438 1.00 91.51 ? 113 LYS A N 1 ATOM 900 C CA . LYS A 1 113 ? 21.023 -22.050 5.821 1.00 91.09 ? 113 LYS A CA 1 ATOM 901 C C . LYS A 1 113 ? 20.059 -22.689 6.808 1.00 91.84 ? 113 LYS A C 1 ATOM 902 O O . LYS A 1 113 ? 18.852 -22.515 6.678 1.00 92.88 ? 113 LYS A O 1 ATOM 903 C CB . LYS A 1 113 ? 21.155 -20.558 6.118 1.00 90.96 ? 113 LYS A CB 1 ATOM 904 C CG . LYS A 1 113 ? 21.642 -20.229 7.516 1.00 91.16 ? 113 LYS A CG 1 ATOM 905 C CD . LYS A 1 113 ? 22.794 -19.231 7.493 1.00 90.17 ? 113 LYS A CD 1 ATOM 906 C CE . LYS A 1 113 ? 22.396 -17.869 6.957 1.00 90.76 ? 113 LYS A CE 1 ATOM 907 N NZ . LYS A 1 113 ? 23.594 -17.087 6.532 1.00 89.99 ? 113 LYS A NZ 1 ATOM 908 N N . ILE A 1 114 ? 20.584 -23.455 7.766 1.00 90.87 ? 114 ILE A N 1 ATOM 909 C CA . ILE A 1 114 ? 19.756 -23.948 8.867 1.00 94.18 ? 114 ILE A CA 1 ATOM 910 C C . ILE A 1 114 ? 20.436 -23.855 10.225 1.00 94.60 ? 114 ILE A C 1 ATOM 911 O O . ILE A 1 114 ? 21.667 -23.961 10.332 1.00 95.32 ? 114 ILE A O 1 ATOM 912 C CB . ILE A 1 114 ? 19.263 -25.398 8.669 1.00 95.64 ? 114 ILE A CB 1 ATOM 913 C CG1 . ILE A 1 114 ? 20.434 -26.387 8.617 1.00 94.94 ? 114 ILE A CG1 1 ATOM 914 C CG2 . ILE A 1 114 ? 18.378 -25.494 7.431 1.00 96.31 ? 114 ILE A CG2 1 ATOM 915 C CD1 . ILE A 1 114 ? 20.040 -27.771 9.085 1.00 97.17 ? 114 ILE A CD1 1 ATOM 916 N N . GLN A 1 115 ? 19.606 -23.671 11.254 1.00 94.93 ? 115 GLN A N 1 ATOM 917 C CA . GLN A 1 115 ? 20.065 -23.534 12.630 1.00 93.46 ? 115 GLN A CA 1 ATOM 918 C C . GLN A 1 115 ? 20.313 -24.912 13.221 1.00 91.96 ? 115 GLN A C 1 ATOM 919 O O . GLN A 1 115 ? 19.419 -25.751 13.205 1.00 92.24 ? 115 GLN A O 1 ATOM 920 C CB . GLN A 1 115 ? 19.009 -22.806 13.466 1.00 94.97 ? 115 GLN A CB 1 ATOM 921 C CG . GLN A 1 115 ? 19.501 -22.415 14.851 1.00 95.33 ? 115 GLN A CG 1 ATOM 922 C CD . GLN A 1 115 ? 18.409 -21.836 15.724 1.00 97.13 ? 115 GLN A CD 1 ATOM 923 O OE1 . GLN A 1 115 ? 18.462 -20.668 16.096 1.00 96.91 ? 115 GLN A OE1 1 ATOM 924 N NE2 . GLN A 1 115 ? 17.415 -22.650 16.055 1.00 98.68 ? 115 GLN A NE2 1 ATOM 925 N N . ILE A 1 116 ? 21.510 -25.140 13.752 1.00 89.71 ? 116 ILE A N 1 ATOM 926 C CA . ILE A 1 116 ? 21.841 -26.440 14.350 1.00 90.59 ? 116 ILE A CA 1 ATOM 927 C C . ILE A 1 116 ? 22.010 -26.363 15.872 1.00 93.32 ? 116 ILE A C 1 ATOM 928 O O . ILE A 1 116 ? 21.602 -27.285 16.583 1.00 96.33 ? 116 ILE A O 1 ATOM 929 C CB . ILE A 1 116 ? 23.082 -27.109 13.690 1.00 87.41 ? 116 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 116 ? 24.243 -26.129 13.568 1.00 84.61 ? 116 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 116 ? 22.730 -27.656 12.316 1.00 86.44 ? 116 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 116 ? 25.577 -26.807 13.396 1.00 83.25 ? 116 ILE A CD1 1 ATOM 933 N N . ILE A 1 117 ? 22.591 -25.272 16.373 1.00 94.32 ? 117 ILE A N 1 ATOM 934 C CA . ILE A 1 117 ? 22.671 -25.031 17.820 1.00 96.44 ? 117 ILE A CA 1 ATOM 935 C C . ILE A 1 117 ? 22.121 -23.642 18.160 1.00 97.29 ? 117 ILE A C 1 ATOM 936 O O . ILE A 1 117 ? 22.856 -22.652 18.067 1.00 94.54 ? 117 ILE A O 1 ATOM 937 C CB . ILE A 1 117 ? 24.115 -25.164 18.347 1.00 95.74 ? 117 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 117 ? 24.723 -26.490 17.879 1.00 94.33 ? 117 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 117 ? 24.131 -25.073 19.873 1.00 98.43 ? 117 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 117 ? 26.096 -26.772 18.452 1.00 93.80 ? 117 ILE A CD1 1 ATOM 941 N N . PRO A 1 118 ? 20.833 -23.572 18.578 1.00 101.07 ? 118 PRO A N 1 ATOM 942 C CA . PRO A 1 118 ? 20.183 -22.286 18.868 1.00 102.53 ? 118 PRO A CA 1 ATOM 943 C C . PRO A 1 118 ? 20.963 -21.440 19.867 1.00 103.28 ? 118 PRO A C 1 ATOM 944 O O . PRO A 1 118 ? 21.571 -21.969 20.798 1.00 103.51 ? 118 PRO A O 1 ATOM 945 C CB . PRO A 1 118 ? 18.822 -22.685 19.462 1.00 105.35 ? 118 PRO A CB 1 ATOM 946 C CG . PRO A 1 118 ? 18.585 -24.090 19.038 1.00 104.95 ? 118 PRO A CG 1 ATOM 947 C CD . PRO A 1 118 ? 19.941 -24.713 18.872 1.00 103.43 ? 118 PRO A CD 1 ATOM 948 N N . LYS A 1 119 ? 20.942 -20.132 19.656 1.00 104.23 ? 119 LYS A N 1 ATOM 949 C CA . LYS A 1 119 ? 21.666 -19.202 20.503 1.00 106.17 ? 119 LYS A CA 1 ATOM 950 C C . LYS A 1 119 ? 21.089 -19.244 21.922 1.00 110.33 ? 119 LYS A C 1 ATOM 951 O O . LYS A 1 119 ? 21.831 -19.273 22.909 1.00 111.07 ? 119 LYS A O 1 ATOM 952 C CB . LYS A 1 119 ? 21.565 -17.797 19.915 1.00 106.79 ? 119 LYS A CB 1 ATOM 953 C CG . LYS A 1 119 ? 22.637 -16.836 20.378 1.00 107.65 ? 119 LYS A CG 1 ATOM 954 C CD . LYS A 1 119 ? 22.582 -15.567 19.547 1.00 109.24 ? 119 LYS A CD 1 ATOM 955 C CE . LYS A 1 119 ? 23.408 -14.454 20.168 1.00 111.15 ? 119 LYS A CE 1 ATOM 956 N NZ . LYS A 1 119 ? 23.406 -13.224 19.328 1.00 112.01 ? 119 LYS A NZ 1 ATOM 957 N N . SER A 1 120 ? 19.760 -19.276 22.007 1.00 112.74 ? 120 SER A N 1 ATOM 958 C CA . SER A 1 120 ? 19.057 -19.337 23.287 1.00 116.06 ? 120 SER A CA 1 ATOM 959 C C . SER A 1 120 ? 19.468 -20.532 24.149 1.00 116.40 ? 120 SER A C 1 ATOM 960 O O . SER A 1 120 ? 19.471 -20.433 25.368 1.00 120.55 ? 120 SER A O 1 ATOM 961 C CB . SER A 1 120 ? 17.539 -19.379 23.065 1.00 117.73 ? 120 SER A CB 1 ATOM 962 O OG . SER A 1 120 ? 17.137 -20.605 22.473 1.00 116.86 ? 120 SER A OG 1 ATOM 963 N N . SER A 1 121 ? 19.826 -21.650 23.522 1.00 114.10 ? 121 SER A N 1 ATOM 964 C CA . SER A 1 121 ? 20.056 -22.902 24.257 1.00 113.79 ? 121 SER A CA 1 ATOM 965 C C . SER A 1 121 ? 21.348 -22.961 25.108 1.00 112.72 ? 121 SER A C 1 ATOM 966 O O . SER A 1 121 ? 21.594 -23.975 25.765 1.00 111.12 ? 121 SER A O 1 ATOM 967 C CB . SER A 1 121 ? 20.019 -24.088 23.287 1.00 111.42 ? 121 SER A CB 1 ATOM 968 O OG . SER A 1 121 ? 21.126 -24.043 22.406 1.00 107.83 ? 121 SER A OG 1 ATOM 969 N N . TRP A 1 122 ? 22.159 -21.899 25.102 1.00 111.63 ? 122 TRP A N 1 ATOM 970 C CA . TRP A 1 122 ? 23.364 -21.837 25.945 1.00 111.22 ? 122 TRP A CA 1 ATOM 971 C C . TRP A 1 122 ? 23.056 -21.238 27.322 1.00 115.13 ? 122 TRP A C 1 ATOM 972 O O . TRP A 1 122 ? 23.400 -20.087 27.595 1.00 116.18 ? 122 TRP A O 1 ATOM 973 C CB . TRP A 1 122 ? 24.448 -21.004 25.268 1.00 108.19 ? 122 TRP A CB 1 ATOM 974 C CG . TRP A 1 122 ? 25.004 -21.594 24.005 1.00 105.71 ? 122 TRP A CG 1 ATOM 975 C CD1 . TRP A 1 122 ? 24.818 -21.132 22.733 1.00 103.06 ? 122 TRP A CD1 1 ATOM 976 C CD2 . TRP A 1 122 ? 25.869 -22.730 23.895 1.00 103.86 ? 122 TRP A CD2 1 ATOM 977 N NE1 . TRP A 1 122 ? 25.508 -21.911 21.841 1.00 101.25 ? 122 TRP A NE1 1 ATOM 978 C CE2 . TRP A 1 122 ? 26.160 -22.902 22.524 1.00 101.04 ? 122 TRP A CE2 1 ATOM 979 C CE3 . TRP A 1 122 ? 26.421 -23.622 24.821 1.00 104.37 ? 122 TRP A CE3 1 ATOM 980 C CZ2 . TRP A 1 122 ? 26.980 -23.932 22.052 1.00 99.23 ? 122 TRP A CZ2 1 ATOM 981 C CZ3 . TRP A 1 122 ? 27.235 -24.643 24.358 1.00 102.97 ? 122 TRP A CZ3 1 ATOM 982 C CH2 . TRP A 1 122 ? 27.512 -24.788 22.980 1.00 100.36 ? 122 TRP A CH2 1 ATOM 983 N N . SER A 1 123 ? 22.425 -22.029 28.188 1.00 117.46 ? 123 SER A N 1 ATOM 984 C CA . SER A 1 123 ? 21.940 -21.544 29.488 1.00 121.78 ? 123 SER A CA 1 ATOM 985 C C . SER A 1 123 ? 23.029 -21.461 30.574 1.00 123.47 ? 123 SER A C 1 ATOM 986 O O . SER A 1 123 ? 22.926 -20.651 31.501 1.00 126.14 ? 123 SER A O 1 ATOM 987 C CB . SER A 1 123 ? 20.775 -22.416 29.978 1.00 123.96 ? 123 SER A CB 1 ATOM 988 O OG . SER A 1 123 ? 21.111 -23.791 29.943 1.00 122.02 ? 123 SER A OG 1 ATOM 989 N N . SER A 1 124 ? 24.060 -22.296 30.459 1.00 120.96 ? 124 SER A N 1 ATOM 990 C CA . SER A 1 124 ? 25.175 -22.309 31.414 1.00 121.14 ? 124 SER A CA 1 ATOM 991 C C . SER A 1 124 ? 26.306 -21.325 31.060 1.00 119.15 ? 124 SER A C 1 ATOM 992 O O . SER A 1 124 ? 27.291 -21.222 31.792 1.00 119.73 ? 124 SER A O 1 ATOM 993 C CB . SER A 1 124 ? 25.750 -23.723 31.507 1.00 120.06 ? 124 SER A CB 1 ATOM 994 O OG . SER A 1 124 ? 24.711 -24.682 31.586 1.00 120.72 ? 124 SER A OG 1 ATOM 995 N N . HIS A 1 125 ? 26.174 -20.622 29.938 1.00 117.23 ? 125 HIS A N 1 ATOM 996 C CA . HIS A 1 125 ? 27.194 -19.671 29.485 1.00 115.73 ? 125 HIS A CA 1 ATOM 997 C C . HIS A 1 125 ? 26.540 -18.406 28.982 1.00 117.31 ? 125 HIS A C 1 ATOM 998 O O . HIS A 1 125 ? 25.349 -18.397 28.661 1.00 119.33 ? 125 HIS A O 1 ATOM 999 C CB . HIS A 1 125 ? 28.027 -20.255 28.342 1.00 110.41 ? 125 HIS A CB 1 ATOM 1000 C CG . HIS A 1 125 ? 28.732 -21.523 28.691 1.00 109.04 ? 125 HIS A CG 1 ATOM 1001 N ND1 . HIS A 1 125 ? 28.119 -22.754 28.620 1.00 108.99 ? 125 HIS A ND1 1 ATOM 1002 C CD2 . HIS A 1 125 ? 29.999 -21.754 29.109 1.00 108.60 ? 125 HIS A CD2 1 ATOM 1003 C CE1 . HIS A 1 125 ? 28.974 -23.689 28.992 1.00 109.42 ? 125 HIS A CE1 1 ATOM 1004 N NE2 . HIS A 1 125 ? 30.123 -23.109 29.293 1.00 109.07 ? 125 HIS A NE2 1 ATOM 1005 N N . GLU A 1 126 ? 27.332 -17.343 28.891 1.00 117.31 ? 126 GLU A N 1 ATOM 1006 C CA . GLU A 1 126 ? 26.863 -16.098 28.313 1.00 117.02 ? 126 GLU A CA 1 ATOM 1007 C C . GLU A 1 126 ? 27.067 -16.184 26.811 1.00 113.66 ? 126 GLU A C 1 ATOM 1008 O O . GLU A 1 126 ? 28.182 -16.433 26.339 1.00 112.26 ? 126 GLU A O 1 ATOM 1009 C CB . GLU A 1 126 ? 27.619 -14.912 28.905 1.00 119.27 ? 126 GLU A CB 1 ATOM 1010 C CG . GLU A 1 126 ? 27.144 -13.550 28.417 1.00 120.30 ? 126 GLU A CG 1 ATOM 1011 C CD . GLU A 1 126 ? 25.653 -13.316 28.620 1.00 123.00 ? 126 GLU A CD 1 ATOM 1012 O OE1 . GLU A 1 126 ? 25.196 -13.319 29.796 1.00 122.99 ? 126 GLU A OE1 1 ATOM 1013 O OE2 . GLU A 1 126 ? 24.952 -13.120 27.589 1.00 121.92 ? 126 GLU A OE2 1 ATOM 1014 N N . ALA A 1 127 ? 25.982 -15.993 26.065 1.00 112.65 ? 127 ALA A N 1 ATOM 1015 C CA . ALA A 1 127 ? 25.982 -16.191 24.617 1.00 107.79 ? 127 ALA A CA 1 ATOM 1016 C C . ALA A 1 127 ? 25.555 -14.948 23.839 1.00 107.60 ? 127 ALA A C 1 ATOM 1017 O O . ALA A 1 127 ? 25.385 -15.019 22.625 1.00 106.39 ? 127 ALA A O 1 ATOM 1018 C CB . ALA A 1 127 ? 25.078 -17.364 24.263 1.00 106.75 ? 127 ALA A CB 1 ATOM 1019 N N . SER A 1 128 ? 25.410 -13.816 24.529 1.00 110.14 ? 128 SER A N 1 ATOM 1020 C CA . SER A 1 128 ? 24.899 -12.579 23.924 1.00 109.89 ? 128 SER A CA 1 ATOM 1021 C C . SER A 1 128 ? 25.809 -11.366 24.138 1.00 108.57 ? 128 SER A C 1 ATOM 1022 O O . SER A 1 128 ? 25.416 -10.232 23.866 1.00 108.16 ? 128 SER A O 1 ATOM 1023 C CB . SER A 1 128 ? 23.508 -12.291 24.480 1.00 114.07 ? 128 SER A CB 1 ATOM 1024 O OG . SER A 1 128 ? 22.626 -13.339 24.127 1.00 114.55 ? 128 SER A OG 1 ATOM 1025 N N . LEU A 1 129 ? 27.026 -11.610 24.613 1.00 106.86 ? 129 LEU A N 1 ATOM 1026 C CA . LEU A 1 129 ? 28.008 -10.557 24.783 1.00 106.88 ? 129 LEU A CA 1 ATOM 1027 C C . LEU A 1 129 ? 29.273 -10.919 24.025 1.00 103.88 ? 129 LEU A C 1 ATOM 1028 O O . LEU A 1 129 ? 30.360 -10.512 24.411 1.00 105.43 ? 129 LEU A O 1 ATOM 1029 C CB . LEU A 1 129 ? 28.325 -10.369 26.262 1.00 110.62 ? 129 LEU A CB 1 ATOM 1030 C CG . LEU A 1 129 ? 27.145 -10.194 27.229 1.00 114.21 ? 129 LEU A CG 1 ATOM 1031 C CD1 . LEU A 1 129 ? 27.665 -9.994 28.646 1.00 116.25 ? 129 LEU A CD1 1 ATOM 1032 C CD2 . LEU A 1 129 ? 26.242 -9.038 26.820 1.00 115.82 ? 129 LEU A CD2 1 ATOM 1033 N N . GLY A 1 130 ? 29.118 -11.682 22.944 1.00 100.91 ? 130 GLY A N 1 ATOM 1034 C CA . GLY A 1 130 ? 30.228 -12.107 22.102 1.00 97.31 ? 130 GLY A CA 1 ATOM 1035 C C . GLY A 1 130 ? 30.407 -11.201 20.896 1.00 95.55 ? 130 GLY A C 1 ATOM 1036 O O . GLY A 1 130 ? 30.309 -11.645 19.743 1.00 91.29 ? 130 GLY A O 1 ATOM 1037 N N . VAL A 1 131 ? 30.706 -9.936 21.181 1.00 96.51 ? 131 VAL A N 1 ATOM 1038 C CA . VAL A 1 131 ? 30.786 -8.891 20.171 1.00 95.13 ? 131 VAL A CA 1 ATOM 1039 C C . VAL A 1 131 ? 32.102 -8.122 20.260 1.00 95.15 ? 131 VAL A C 1 ATOM 1040 O O . VAL A 1 131 ? 32.853 -8.269 21.219 1.00 97.06 ? 131 VAL A O 1 ATOM 1041 C CB . VAL A 1 131 ? 29.615 -7.895 20.322 1.00 97.49 ? 131 VAL A CB 1 ATOM 1042 C CG1 . VAL A 1 131 ? 28.281 -8.632 20.269 1.00 97.64 ? 131 VAL A CG1 1 ATOM 1043 C CG2 . VAL A 1 131 ? 29.739 -7.080 21.608 1.00 100.03 ? 131 VAL A CG2 1 ATOM 1044 N N . SER A 1 132 ? 32.351 -7.283 19.258 1.00 94.47 ? 132 SER A N 1 ATOM 1045 C CA . SER A 1 132 ? 33.576 -6.487 19.173 1.00 94.06 ? 132 SER A CA 1 ATOM 1046 C C . SER A 1 132 ? 33.399 -5.245 18.299 1.00 95.04 ? 132 SER A C 1 ATOM 1047 O O . SER A 1 132 ? 32.562 -5.222 17.391 1.00 95.15 ? 132 SER A O 1 ATOM 1048 C CB . SER A 1 132 ? 34.709 -7.332 18.599 1.00 90.44 ? 132 SER A CB 1 ATOM 1049 O OG . SER A 1 132 ? 35.778 -6.515 18.157 1.00 89.11 ? 132 SER A OG 1 ATOM 1050 N N . SER A 1 133 ? 34.221 -4.232 18.561 1.00 96.63 ? 133 SER A N 1 ATOM 1051 C CA . SER A 1 133 ? 34.220 -2.996 17.779 1.00 97.92 ? 133 SER A CA 1 ATOM 1052 C C . SER A 1 133 ? 34.785 -3.192 16.362 1.00 96.37 ? 133 SER A C 1 ATOM 1053 O O . SER A 1 133 ? 34.575 -2.355 15.487 1.00 96.32 ? 133 SER A O 1 ATOM 1054 C CB . SER A 1 133 ? 35.007 -1.909 18.511 1.00 100.17 ? 133 SER A CB 1 ATOM 1055 O OG . SER A 1 133 ? 36.279 -2.396 18.908 1.00 99.96 ? 133 SER A OG 1 ATOM 1056 N N . ALA A 1 134 ? 35.497 -4.292 16.136 1.00 95.87 ? 134 ALA A N 1 ATOM 1057 C CA . ALA A 1 134 ? 36.001 -4.625 14.799 1.00 94.84 ? 134 ALA A CA 1 ATOM 1058 C C . ALA A 1 134 ? 34.891 -5.078 13.823 1.00 93.78 ? 134 ALA A C 1 ATOM 1059 O O . ALA A 1 134 ? 35.032 -4.927 12.607 1.00 91.29 ? 134 ALA A O 1 ATOM 1060 C CB . ALA A 1 134 ? 37.085 -5.686 14.900 1.00 93.78 ? 134 ALA A CB 1 ATOM 1061 N N . CYS A 1 135 ? 33.795 -5.616 14.359 1.00 94.87 ? 135 CYS A N 1 ATOM 1062 C CA . CYS A 1 135 ? 32.646 -6.038 13.550 1.00 94.20 ? 135 CYS A CA 1 ATOM 1063 C C . CYS A 1 135 ? 31.384 -5.222 13.864 1.00 93.68 ? 135 CYS A C 1 ATOM 1064 O O . CYS A 1 135 ? 30.439 -5.745 14.457 1.00 93.35 ? 135 CYS A O 1 ATOM 1065 C CB . CYS A 1 135 ? 32.370 -7.518 13.792 1.00 95.17 ? 135 CYS A CB 1 ATOM 1066 S SG . CYS A 1 135 ? 33.795 -8.570 13.457 1.00 96.81 ? 135 CYS A SG 1 ATOM 1067 N N . PRO A 1 136 ? 31.360 -3.939 13.453 1.00 92.17 ? 136 PRO A N 1 ATOM 1068 C CA . PRO A 1 136 ? 30.245 -3.056 13.800 1.00 93.77 ? 136 PRO A CA 1 ATOM 1069 C C . PRO A 1 136 ? 28.989 -3.282 12.960 1.00 92.86 ? 136 PRO A C 1 ATOM 1070 O O . PRO A 1 136 ? 29.084 -3.680 11.811 1.00 89.79 ? 136 PRO A O 1 ATOM 1071 C CB . PRO A 1 136 ? 30.813 -1.664 13.516 1.00 94.79 ? 136 PRO A CB 1 ATOM 1072 C CG . PRO A 1 136 ? 31.790 -1.889 12.416 1.00 92.37 ? 136 PRO A CG 1 ATOM 1073 C CD . PRO A 1 136 ? 32.415 -3.218 12.716 1.00 90.73 ? 136 PRO A CD 1 ATOM 1074 N N . TYR A 1 137 ? 27.826 -3.018 13.548 1.00 95.21 ? 137 TYR A N 1 ATOM 1075 C CA . TYR A 1 137 ? 26.557 -3.049 12.825 1.00 96.09 ? 137 TYR A CA 1 ATOM 1076 C C . TYR A 1 137 ? 25.672 -1.899 13.278 1.00 98.71 ? 137 TYR A C 1 ATOM 1077 O O . TYR A 1 137 ? 25.270 -1.842 14.446 1.00 102.12 ? 137 TYR A O 1 ATOM 1078 C CB . TYR A 1 137 ? 25.829 -4.374 13.053 1.00 96.24 ? 137 TYR A CB 1 ATOM 1079 C CG . TYR A 1 137 ? 24.502 -4.459 12.330 1.00 97.35 ? 137 TYR A CG 1 ATOM 1080 C CD1 . TYR A 1 137 ? 24.449 -4.505 10.936 1.00 96.45 ? 137 TYR A CD1 1 ATOM 1081 C CD2 . TYR A 1 137 ? 23.297 -4.487 13.036 1.00 99.37 ? 137 TYR A CD2 1 ATOM 1082 C CE1 . TYR A 1 137 ? 23.237 -4.578 10.267 1.00 97.42 ? 137 TYR A CE1 1 ATOM 1083 C CE2 . TYR A 1 137 ? 22.084 -4.561 12.374 1.00 100.31 ? 137 TYR A CE2 1 ATOM 1084 C CZ . TYR A 1 137 ? 22.061 -4.606 10.993 1.00 98.95 ? 137 TYR A CZ 1 ATOM 1085 O OH . TYR A 1 137 ? 20.863 -4.683 10.334 1.00 100.17 ? 137 TYR A OH 1 ATOM 1086 N N . GLN A 1 138 ? 25.372 -0.989 12.353 1.00 98.47 ? 138 GLN A N 1 ATOM 1087 C CA . GLN A 1 138 ? 24.526 0.166 12.642 1.00 101.46 ? 138 GLN A CA 1 ATOM 1088 C C . GLN A 1 138 ? 25.019 0.888 13.893 1.00 103.55 ? 138 GLN A C 1 ATOM 1089 O O . GLN A 1 138 ? 24.251 1.155 14.816 1.00 106.54 ? 138 GLN A O 1 ATOM 1090 C CB . GLN A 1 138 ? 23.057 -0.260 12.792 1.00 102.66 ? 138 GLN A CB 1 ATOM 1091 C CG . GLN A 1 138 ? 22.545 -1.073 11.608 1.00 101.12 ? 138 GLN A CG 1 ATOM 1092 C CD . GLN A 1 138 ? 21.035 -1.262 11.587 1.00 102.73 ? 138 GLN A CD 1 ATOM 1093 O OE1 . GLN A 1 138 ? 20.336 -0.939 12.544 1.00 103.49 ? 138 GLN A OE1 1 ATOM 1094 N NE2 . GLN A 1 138 ? 20.530 -1.797 10.481 1.00 102.03 ? 138 GLN A NE2 1 ATOM 1095 N N . GLY A 1 139 ? 26.321 1.171 13.923 1.00 102.47 ? 139 GLY A N 1 ATOM 1096 C CA . GLY A 1 139 ? 26.929 1.973 14.989 1.00 103.51 ? 139 GLY A CA 1 ATOM 1097 C C . GLY A 1 139 ? 27.343 1.213 16.232 1.00 102.43 ? 139 GLY A C 1 ATOM 1098 O O . GLY A 1 139 ? 28.086 1.747 17.059 1.00 102.29 ? 139 GLY A O 1 ATOM 1099 N N . LYS A 1 140 ? 26.875 -0.029 16.350 1.00 101.02 ? 140 LYS A N 1 ATOM 1100 C CA . LYS A 1 140 ? 27.027 -0.822 17.566 1.00 102.24 ? 140 LYS A CA 1 ATOM 1101 C C . LYS A 1 140 ? 27.903 -2.032 17.294 1.00 98.63 ? 140 LYS A C 1 ATOM 1102 O O . LYS A 1 140 ? 27.939 -2.532 16.174 1.00 96.48 ? 140 LYS A O 1 ATOM 1103 C CB . LYS A 1 140 ? 25.653 -1.290 18.068 1.00 104.49 ? 140 LYS A CB 1 ATOM 1104 C CG . LYS A 1 140 ? 24.684 -0.156 18.388 1.00 108.68 ? 140 LYS A CG 1 ATOM 1105 C CD . LYS A 1 140 ? 23.229 -0.597 18.290 1.00 110.36 ? 140 LYS A CD 1 ATOM 1106 C CE . LYS A 1 140 ? 22.268 0.589 18.251 1.00 113.51 ? 140 LYS A CE 1 ATOM 1107 N NZ . LYS A 1 140 ? 22.287 1.418 19.491 1.00 116.61 ? 140 LYS A NZ 1 ATOM 1108 N N . SER A 1 141 ? 28.591 -2.506 18.332 1.00 98.62 ? 141 SER A N 1 ATOM 1109 C CA . SER A 1 141 ? 29.458 -3.683 18.234 1.00 95.13 ? 141 SER A CA 1 ATOM 1110 C C . SER A 1 141 ? 28.644 -4.956 17.974 1.00 93.78 ? 141 SER A C 1 ATOM 1111 O O . SER A 1 141 ? 27.646 -5.224 18.642 1.00 95.04 ? 141 SER A O 1 ATOM 1112 C CB . SER A 1 141 ? 30.290 -3.841 19.511 1.00 96.14 ? 141 SER A CB 1 ATOM 1113 O OG . SER A 1 141 ? 31.129 -2.714 19.723 1.00 96.56 ? 141 SER A OG 1 ATOM 1114 N N . SER A 1 142 ? 29.078 -5.732 16.989 1.00 91.47 ? 142 SER A N 1 ATOM 1115 C CA . SER A 1 142 ? 28.377 -6.941 16.590 1.00 90.49 ? 142 SER A CA 1 ATOM 1116 C C . SER A 1 142 ? 29.408 -8.041 16.346 1.00 88.94 ? 142 SER A C 1 ATOM 1117 O O . SER A 1 142 ? 30.539 -7.942 16.830 1.00 88.42 ? 142 SER A O 1 ATOM 1118 C CB . SER A 1 142 ? 27.543 -6.658 15.337 1.00 90.22 ? 142 SER A CB 1 ATOM 1119 O OG . SER A 1 142 ? 26.602 -7.686 15.102 1.00 90.19 ? 142 SER A OG 1 ATOM 1120 N N . PHE A 1 143 ? 29.021 -9.086 15.609 1.00 88.04 ? 143 PHE A N 1 ATOM 1121 C CA . PHE A 1 143 ? 29.916 -10.212 15.325 1.00 86.61 ? 143 PHE A CA 1 ATOM 1122 C C . PHE A 1 143 ? 29.396 -11.088 14.189 1.00 85.54 ? 143 PHE A C 1 ATOM 1123 O O . PHE A 1 143 ? 28.214 -11.037 13.846 1.00 86.19 ? 143 PHE A O 1 ATOM 1124 C CB . PHE A 1 143 ? 30.083 -11.075 16.577 1.00 87.52 ? 143 PHE A CB 1 ATOM 1125 C CG . PHE A 1 143 ? 31.304 -11.964 16.557 1.00 85.74 ? 143 PHE A CG 1 ATOM 1126 C CD1 . PHE A 1 143 ? 32.583 -11.417 16.607 1.00 84.90 ? 143 PHE A CD1 1 ATOM 1127 C CD2 . PHE A 1 143 ? 31.173 -13.346 16.524 1.00 84.44 ? 143 PHE A CD2 1 ATOM 1128 C CE1 . PHE A 1 143 ? 33.703 -12.232 16.611 1.00 83.63 ? 143 PHE A CE1 1 ATOM 1129 C CE2 . PHE A 1 143 ? 32.292 -14.164 16.532 1.00 83.11 ? 143 PHE A CE2 1 ATOM 1130 C CZ . PHE A 1 143 ? 33.558 -13.608 16.574 1.00 82.51 ? 143 PHE A CZ 1 ATOM 1131 N N . PHE A 1 144 ? 30.291 -11.887 13.612 1.00 82.64 ? 144 PHE A N 1 ATOM 1132 C CA . PHE A 1 144 ? 29.908 -12.915 12.655 1.00 81.13 ? 144 PHE A CA 1 ATOM 1133 C C . PHE A 1 144 ? 28.596 -13.575 13.091 1.00 82.52 ? 144 PHE A C 1 ATOM 1134 O O . PHE A 1 144 ? 28.539 -14.220 14.125 1.00 84.81 ? 144 PHE A O 1 ATOM 1135 C CB . PHE A 1 144 ? 30.999 -13.988 12.552 1.00 79.30 ? 144 PHE A CB 1 ATOM 1136 C CG . PHE A 1 144 ? 32.328 -13.476 12.054 1.00 78.11 ? 144 PHE A CG 1 ATOM 1137 C CD1 . PHE A 1 144 ? 32.479 -13.049 10.745 1.00 76.51 ? 144 PHE A CD1 1 ATOM 1138 C CD2 . PHE A 1 144 ? 33.437 -13.433 12.903 1.00 78.09 ? 144 PHE A CD2 1 ATOM 1139 C CE1 . PHE A 1 144 ? 33.704 -12.588 10.289 1.00 75.42 ? 144 PHE A CE1 1 ATOM 1140 C CE2 . PHE A 1 144 ? 34.663 -12.973 12.447 1.00 76.55 ? 144 PHE A CE2 1 ATOM 1141 C CZ . PHE A 1 144 ? 34.795 -12.550 11.139 1.00 75.13 ? 144 PHE A CZ 1 ATOM 1142 N N . ARG A 1 145 ? 27.552 -13.421 12.289 1.00 83.22 ? 145 ARG A N 1 ATOM 1143 C CA . ARG A 1 145 ? 26.205 -13.808 12.681 1.00 84.53 ? 145 ARG A CA 1 ATOM 1144 C C . ARG A 1 145 ? 25.946 -15.306 12.747 1.00 86.35 ? 145 ARG A C 1 ATOM 1145 O O . ARG A 1 145 ? 24.924 -15.724 13.294 1.00 90.40 ? 145 ARG A O 1 ATOM 1146 C CB . ARG A 1 145 ? 25.187 -13.216 11.713 1.00 84.03 ? 145 ARG A CB 1 ATOM 1147 C CG . ARG A 1 145 ? 25.211 -11.706 11.610 1.00 84.21 ? 145 ARG A CG 1 ATOM 1148 C CD . ARG A 1 145 ? 23.865 -11.246 11.114 1.00 86.02 ? 145 ARG A CD 1 ATOM 1149 N NE . ARG A 1 145 ? 23.820 -9.821 10.836 1.00 87.58 ? 145 ARG A NE 1 ATOM 1150 C CZ . ARG A 1 145 ? 23.678 -8.875 11.757 1.00 90.47 ? 145 ARG A CZ 1 ATOM 1151 N NH1 . ARG A 1 145 ? 23.606 -9.176 13.054 1.00 92.12 ? 145 ARG A NH1 1 ATOM 1152 N NH2 . ARG A 1 145 ? 23.629 -7.606 11.376 1.00 92.35 ? 145 ARG A NH2 1 ATOM 1153 N N . ASN A 1 146 ? 26.831 -16.116 12.175 1.00 85.99 ? 146 ASN A N 1 ATOM 1154 C CA . ASN A 1 146 ? 26.556 -17.551 12.036 1.00 85.74 ? 146 ASN A CA 1 ATOM 1155 C C . ASN A 1 146 ? 27.184 -18.403 13.136 1.00 85.06 ? 146 ASN A C 1 ATOM 1156 O O . ASN A 1 146 ? 26.755 -19.538 13.374 1.00 84.00 ? 146 ASN A O 1 ATOM 1157 C CB . ASN A 1 146 ? 26.983 -18.035 10.643 1.00 84.67 ? 146 ASN A CB 1 ATOM 1158 C CG . ASN A 1 146 ? 26.094 -17.488 9.543 1.00 85.30 ? 146 ASN A CG 1 ATOM 1159 O OD1 . ASN A 1 146 ? 24.887 -17.303 9.743 1.00 87.51 ? 146 ASN A OD1 1 ATOM 1160 N ND2 . ASN A 1 146 ? 26.681 -17.220 8.378 1.00 83.89 ? 146 ASN A ND2 1 ATOM 1161 N N . VAL A 1 147 ? 28.184 -17.844 13.812 1.00 84.51 ? 147 VAL A N 1 ATOM 1162 C CA . VAL A 1 147 ? 28.815 -18.509 14.942 1.00 85.24 ? 147 VAL A CA 1 ATOM 1163 C C . VAL A 1 147 ? 28.675 -17.658 16.207 1.00 86.49 ? 147 VAL A C 1 ATOM 1164 O O . VAL A 1 147 ? 28.622 -16.435 16.135 1.00 88.44 ? 147 VAL A O 1 ATOM 1165 C CB . VAL A 1 147 ? 30.287 -18.828 14.637 1.00 83.96 ? 147 VAL A CB 1 ATOM 1166 C CG1 . VAL A 1 147 ? 30.366 -19.849 13.518 1.00 82.96 ? 147 VAL A CG1 1 ATOM 1167 C CG2 . VAL A 1 147 ? 31.061 -17.574 14.251 1.00 83.48 ? 147 VAL A CG2 1 ATOM 1168 N N . VAL A 1 148 ? 28.610 -18.314 17.360 1.00 87.15 ? 148 VAL A N 1 ATOM 1169 C CA . VAL A 1 148 ? 28.310 -17.655 18.635 1.00 88.61 ? 148 VAL A CA 1 ATOM 1170 C C . VAL A 1 148 ? 29.561 -17.641 19.505 1.00 88.28 ? 148 VAL A C 1 ATOM 1171 O O . VAL A 1 148 ? 30.082 -18.698 19.853 1.00 88.08 ? 148 VAL A O 1 ATOM 1172 C CB . VAL A 1 148 ? 27.187 -18.408 19.387 1.00 90.73 ? 148 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 148 ? 26.872 -17.735 20.714 1.00 94.45 ? 148 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 148 ? 25.928 -18.520 18.527 1.00 90.93 ? 148 VAL A CG2 1 ATOM 1175 N N . TRP A 1 149 ? 30.040 -16.447 19.846 1.00 89.06 ? 149 TRP A N 1 ATOM 1176 C CA . TRP A 1 149 ? 31.220 -16.288 20.704 1.00 90.30 ? 149 TRP A CA 1 ATOM 1177 C C . TRP A 1 149 ? 30.794 -16.345 22.186 1.00 94.18 ? 149 TRP A C 1 ATOM 1178 O O . TRP A 1 149 ? 30.323 -15.360 22.757 1.00 96.28 ? 149 TRP A O 1 ATOM 1179 C CB . TRP A 1 149 ? 31.952 -14.985 20.347 1.00 89.68 ? 149 TRP A CB 1 ATOM 1180 C CG . TRP A 1 149 ? 33.212 -14.673 21.125 1.00 90.51 ? 149 TRP A CG 1 ATOM 1181 C CD1 . TRP A 1 149 ? 33.859 -15.476 22.020 1.00 91.40 ? 149 TRP A CD1 1 ATOM 1182 C CD2 . TRP A 1 149 ? 33.992 -13.469 21.037 1.00 90.08 ? 149 TRP A CD2 1 ATOM 1183 N NE1 . TRP A 1 149 ? 34.979 -14.838 22.507 1.00 91.95 ? 149 TRP A NE1 1 ATOM 1184 C CE2 . TRP A 1 149 ? 35.085 -13.609 21.913 1.00 90.91 ? 149 TRP A CE2 1 ATOM 1185 C CE3 . TRP A 1 149 ? 33.868 -12.287 20.302 1.00 89.87 ? 149 TRP A CE3 1 ATOM 1186 C CZ2 . TRP A 1 149 ? 36.046 -12.610 22.079 1.00 91.45 ? 149 TRP A CZ2 1 ATOM 1187 C CZ3 . TRP A 1 149 ? 34.829 -11.295 20.466 1.00 90.51 ? 149 TRP A CZ3 1 ATOM 1188 C CH2 . TRP A 1 149 ? 35.902 -11.465 21.346 1.00 91.12 ? 149 TRP A CH2 1 ATOM 1189 N N . LEU A 1 150 ? 30.960 -17.520 22.790 1.00 94.87 ? 150 LEU A N 1 ATOM 1190 C CA . LEU A 1 150 ? 30.504 -17.780 24.144 1.00 97.68 ? 150 LEU A CA 1 ATOM 1191 C C . LEU A 1 150 ? 31.543 -17.309 25.149 1.00 99.61 ? 150 LEU A C 1 ATOM 1192 O O . LEU A 1 150 ? 32.739 -17.555 24.953 1.00 98.64 ? 150 LEU A O 1 ATOM 1193 C CB . LEU A 1 150 ? 30.263 -19.277 24.337 1.00 98.05 ? 150 LEU A CB 1 ATOM 1194 C CG . LEU A 1 150 ? 29.224 -19.942 23.427 1.00 97.09 ? 150 LEU A CG 1 ATOM 1195 C CD1 . LEU A 1 150 ? 29.291 -21.459 23.545 1.00 97.10 ? 150 LEU A CD1 1 ATOM 1196 C CD2 . LEU A 1 150 ? 27.818 -19.449 23.743 1.00 99.00 ? 150 LEU A CD2 1 ATOM 1197 N N . ILE A 1 151 ? 31.079 -16.635 26.207 1.00 101.73 ? 151 ILE A N 1 ATOM 1198 C CA . ILE A 1 151 ? 31.932 -16.227 27.337 1.00 103.59 ? 151 ILE A CA 1 ATOM 1199 C C . ILE A 1 151 ? 31.347 -16.699 28.679 1.00 106.03 ? 151 ILE A C 1 ATOM 1200 O O . ILE A 1 151 ? 30.191 -17.131 28.759 1.00 105.42 ? 151 ILE A O 1 ATOM 1201 C CB . ILE A 1 151 ? 32.181 -14.694 27.369 1.00 104.37 ? 151 ILE A CB 1 ATOM 1202 C CG1 . ILE A 1 151 ? 30.924 -13.925 27.793 1.00 107.32 ? 151 ILE A CG1 1 ATOM 1203 C CG2 . ILE A 1 151 ? 32.665 -14.200 26.015 1.00 101.17 ? 151 ILE A CG2 1 ATOM 1204 C CD1 . ILE A 1 151 ? 31.106 -12.420 27.858 1.00 108.69 ? 151 ILE A CD1 1 ATOM 1205 N N . LYS A 1 152 ? 32.162 -16.606 29.725 1.00 108.85 ? 152 LYS A N 1 ATOM 1206 C CA . LYS A 1 152 ? 31.793 -17.080 31.072 1.00 112.91 ? 152 LYS A CA 1 ATOM 1207 C C . LYS A 1 152 ? 30.537 -16.413 31.653 1.00 117.65 ? 152 LYS A C 1 ATOM 1208 O O . LYS A 1 152 ? 30.245 -15.250 31.364 1.00 117.65 ? 152 LYS A O 1 ATOM 1209 C CB . LYS A 1 152 ? 32.963 -16.876 32.037 1.00 113.60 ? 152 LYS A CB 1 ATOM 1210 C CG . LYS A 1 152 ? 33.225 -15.422 32.394 1.00 115.61 ? 152 LYS A CG 1 ATOM 1211 C CD . LYS A 1 152 ? 34.415 -15.279 33.329 1.00 117.57 ? 152 LYS A CD 1 ATOM 1212 C CE . LYS A 1 152 ? 34.457 -13.905 33.972 1.00 119.84 ? 152 LYS A CE 1 ATOM 1213 N NZ . LYS A 1 152 ? 35.609 -13.809 34.904 1.00 122.59 ? 152 LYS A NZ 1 ATOM 1214 N N . LYS A 1 153 ? 29.810 -17.156 32.489 1.00 122.88 ? 153 LYS A N 1 ATOM 1215 C CA . LYS A 1 153 ? 28.594 -16.650 33.136 1.00 127.81 ? 153 LYS A CA 1 ATOM 1216 C C . LYS A 1 153 ? 28.705 -16.772 34.653 1.00 131.42 ? 153 LYS A C 1 ATOM 1217 O O . LYS A 1 153 ? 29.003 -17.852 35.174 1.00 132.10 ? 153 LYS A O 1 ATOM 1218 C CB . LYS A 1 153 ? 27.362 -17.404 32.626 1.00 128.85 ? 153 LYS A CB 1 ATOM 1219 C CG . LYS A 1 153 ? 26.078 -16.590 32.697 1.00 132.14 ? 153 LYS A CG 1 ATOM 1220 C CD . LYS A 1 153 ? 24.846 -17.436 32.404 1.00 133.27 ? 153 LYS A CD 1 ATOM 1221 C CE . LYS A 1 153 ? 24.443 -18.268 33.614 1.00 136.67 ? 153 LYS A CE 1 ATOM 1222 N NZ . LYS A 1 153 ? 23.095 -18.878 33.471 1.00 137.95 ? 153 LYS A NZ 1 ATOM 1223 N N . ASN A 1 154 ? 28.453 -15.655 35.343 1.00 135.28 ? 154 ASN A N 1 ATOM 1224 C CA . ASN A 1 154 ? 28.670 -15.512 36.797 1.00 139.23 ? 154 ASN A CA 1 ATOM 1225 C C . ASN A 1 154 ? 30.056 -16.033 37.220 1.00 138.06 ? 154 ASN A C 1 ATOM 1226 O O . ASN A 1 154 ? 30.198 -16.731 38.222 1.00 140.40 ? 154 ASN A O 1 ATOM 1227 C CB . ASN A 1 154 ? 27.534 -16.182 37.599 1.00 142.61 ? 154 ASN A CB 1 ATOM 1228 C CG . ASN A 1 154 ? 27.399 -15.630 39.022 1.00 148.97 ? 154 ASN A CG 1 ATOM 1229 O OD1 . ASN A 1 154 ? 27.836 -14.517 39.318 1.00 152.02 ? 154 ASN A OD1 1 ATOM 1230 N ND2 . ASN A 1 154 ? 26.778 -16.409 39.907 1.00 152.11 ? 154 ASN A ND2 1 ATOM 1231 N N . SER A 1 155 ? 31.069 -15.673 36.434 1.00 134.51 ? 155 SER A N 1 ATOM 1232 C CA . SER A 1 155 ? 32.451 -16.113 36.647 1.00 132.88 ? 155 SER A CA 1 ATOM 1233 C C . SER A 1 155 ? 32.599 -17.639 36.628 1.00 131.03 ? 155 SER A C 1 ATOM 1234 O O . SER A 1 155 ? 33.222 -18.215 37.510 1.00 133.19 ? 155 SER A O 1 ATOM 1235 C CB . SER A 1 155 ? 33.015 -15.533 37.952 1.00 136.44 ? 155 SER A CB 1 ATOM 1236 O OG . SER A 1 155 ? 32.937 -14.121 37.950 1.00 137.55 ? 155 SER A OG 1 ATOM 1237 N N . THR A 1 156 ? 32.031 -18.288 35.616 1.00 127.28 ? 156 THR A N 1 ATOM 1238 C CA . THR A 1 156 ? 32.123 -19.742 35.487 1.00 125.49 ? 156 THR A CA 1 ATOM 1239 C C . THR A 1 156 ? 31.935 -20.139 34.036 1.00 122.72 ? 156 THR A C 1 ATOM 1240 O O . THR A 1 156 ? 30.878 -19.876 33.465 1.00 126.30 ? 156 THR A O 1 ATOM 1241 C CB . THR A 1 156 ? 31.035 -20.463 36.309 1.00 127.05 ? 156 THR A CB 1 ATOM 1242 O OG1 . THR A 1 156 ? 31.038 -19.981 37.654 1.00 130.84 ? 156 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 156 ? 31.275 -21.963 36.322 1.00 125.93 ? 156 THR A CG2 1 ATOM 1244 N N . TYR A 1 157 ? 32.956 -20.752 33.434 1.00 119.79 ? 157 TYR A N 1 ATOM 1245 C CA . TYR A 1 157 ? 32.824 -21.357 32.104 1.00 114.35 ? 157 TYR A CA 1 ATOM 1246 C C . TYR A 1 157 ? 32.888 -22.863 32.300 1.00 113.58 ? 157 TYR A C 1 ATOM 1247 O O . TYR A 1 157 ? 33.973 -23.452 32.312 1.00 111.66 ? 157 TYR A O 1 ATOM 1248 C CB . TYR A 1 157 ? 33.923 -20.884 31.148 1.00 111.96 ? 157 TYR A CB 1 ATOM 1249 C CG . TYR A 1 157 ? 33.625 -21.130 29.670 1.00 108.49 ? 157 TYR A CG 1 ATOM 1250 C CD1 . TYR A 1 157 ? 33.665 -22.411 29.127 1.00 106.86 ? 157 TYR A CD1 1 ATOM 1251 C CD2 . TYR A 1 157 ? 33.308 -20.075 28.820 1.00 107.13 ? 157 TYR A CD2 1 ATOM 1252 C CE1 . TYR A 1 157 ? 33.401 -22.631 27.781 1.00 104.79 ? 157 TYR A CE1 1 ATOM 1253 C CE2 . TYR A 1 157 ? 33.042 -20.285 27.475 1.00 104.38 ? 157 TYR A CE2 1 ATOM 1254 C CZ . TYR A 1 157 ? 33.088 -21.567 26.954 1.00 103.09 ? 157 TYR A CZ 1 ATOM 1255 O OH . TYR A 1 157 ? 32.825 -21.779 25.612 1.00 98.83 ? 157 TYR A OH 1 ATOM 1256 N N . PRO A 1 158 ? 31.721 -23.492 32.498 1.00 114.63 ? 158 PRO A N 1 ATOM 1257 C CA . PRO A 1 158 ? 31.715 -24.937 32.661 1.00 114.36 ? 158 PRO A CA 1 ATOM 1258 C C . PRO A 1 158 ? 31.942 -25.627 31.327 1.00 109.80 ? 158 PRO A C 1 ATOM 1259 O O . PRO A 1 158 ? 31.764 -25.012 30.270 1.00 107.40 ? 158 PRO A O 1 ATOM 1260 C CB . PRO A 1 158 ? 30.311 -25.222 33.209 1.00 117.08 ? 158 PRO A CB 1 ATOM 1261 C CG . PRO A 1 158 ? 29.468 -24.117 32.679 1.00 116.77 ? 158 PRO A CG 1 ATOM 1262 C CD . PRO A 1 158 ? 30.367 -22.914 32.618 1.00 116.37 ? 158 PRO A CD 1 ATOM 1263 N N . THR A 1 159 ? 32.345 -26.891 31.379 1.00 108.94 ? 159 THR A N 1 ATOM 1264 C CA . THR A 1 159 ? 32.647 -27.645 30.168 1.00 105.36 ? 159 THR A CA 1 ATOM 1265 C C . THR A 1 159 ? 31.399 -27.733 29.297 1.00 104.83 ? 159 THR A C 1 ATOM 1266 O O . THR A 1 159 ? 30.304 -28.005 29.797 1.00 106.34 ? 159 THR A O 1 ATOM 1267 C CB . THR A 1 159 ? 33.154 -29.071 30.486 1.00 105.24 ? 159 THR A CB 1 ATOM 1268 O OG1 . THR A 1 159 ? 34.287 -29.003 31.360 1.00 105.90 ? 159 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 159 ? 33.557 -29.809 29.220 1.00 101.91 ? 159 THR A CG2 1 ATOM 1270 N N . ILE A 1 160 ? 31.585 -27.470 28.004 1.00 103.07 ? 160 ILE A N 1 ATOM 1271 C CA . ILE A 1 160 ? 30.542 -27.613 26.982 1.00 101.99 ? 160 ILE A CA 1 ATOM 1272 C C . ILE A 1 160 ? 30.629 -29.008 26.366 1.00 101.80 ? 160 ILE A C 1 ATOM 1273 O O . ILE A 1 160 ? 31.717 -29.468 26.028 1.00 100.13 ? 160 ILE A O 1 ATOM 1274 C CB . ILE A 1 160 ? 30.722 -26.563 25.860 1.00 98.84 ? 160 ILE A CB 1 ATOM 1275 C CG1 . ILE A 1 160 ? 30.467 -25.158 26.413 1.00 99.83 ? 160 ILE A CG1 1 ATOM 1276 C CG2 . ILE A 1 160 ? 29.797 -26.861 24.686 1.00 97.33 ? 160 ILE A CG2 1 ATOM 1277 C CD1 . ILE A 1 160 ? 30.748 -24.024 25.451 1.00 97.90 ? 160 ILE A CD1 1 ATOM 1278 N N . LYS A 1 161 ? 29.492 -29.679 26.221 1.00 103.66 ? 161 LYS A N 1 ATOM 1279 C CA . LYS A 1 161 ? 29.440 -30.966 25.526 1.00 103.56 ? 161 LYS A CA 1 ATOM 1280 C C . LYS A 1 161 ? 28.217 -30.995 24.623 1.00 103.15 ? 161 LYS A C 1 ATOM 1281 O O . LYS A 1 161 ? 27.123 -31.321 25.074 1.00 105.94 ? 161 LYS A O 1 ATOM 1282 C CB . LYS A 1 161 ? 29.366 -32.127 26.520 1.00 107.33 ? 161 LYS A CB 1 ATOM 1283 C CG . LYS A 1 161 ? 30.685 -32.574 27.139 1.00 109.06 ? 161 LYS A CG 1 ATOM 1284 C CD . LYS A 1 161 ? 30.487 -33.905 27.868 1.00 112.49 ? 161 LYS A CD 1 ATOM 1285 C CE . LYS A 1 161 ? 31.786 -34.631 28.203 1.00 113.55 ? 161 LYS A CE 1 ATOM 1286 N NZ . LYS A 1 161 ? 32.217 -34.442 29.616 1.00 116.38 ? 161 LYS A NZ 1 ATOM 1287 N N . ARG A 1 162 ? 28.396 -30.650 23.353 1.00 100.98 ? 162 ARG A N 1 ATOM 1288 C CA . ARG A 1 162 ? 27.278 -30.607 22.423 1.00 101.48 ? 162 ARG A CA 1 ATOM 1289 C C . ARG A 1 162 ? 27.490 -31.532 21.245 1.00 100.77 ? 162 ARG A C 1 ATOM 1290 O O . ARG A 1 162 ? 28.618 -31.790 20.831 1.00 99.64 ? 162 ARG A O 1 ATOM 1291 C CB . ARG A 1 162 ? 27.061 -29.191 21.906 1.00 100.73 ? 162 ARG A CB 1 ATOM 1292 C CG . ARG A 1 162 ? 26.681 -28.196 22.979 1.00 103.59 ? 162 ARG A CG 1 ATOM 1293 C CD . ARG A 1 162 ? 25.461 -28.630 23.770 1.00 106.94 ? 162 ARG A CD 1 ATOM 1294 N NE . ARG A 1 162 ? 24.713 -27.473 24.258 1.00 109.47 ? 162 ARG A NE 1 ATOM 1295 C CZ . ARG A 1 162 ? 23.754 -26.847 23.579 1.00 109.50 ? 162 ARG A CZ 1 ATOM 1296 N NH1 . ARG A 1 162 ? 23.394 -27.265 22.371 1.00 107.85 ? 162 ARG A NH1 1 ATOM 1297 N NH2 . ARG A 1 162 ? 23.141 -25.795 24.117 1.00 111.59 ? 162 ARG A NH2 1 ATOM 1298 N N . SER A 1 163 ? 26.380 -32.005 20.696 1.00 100.45 ? 163 SER A N 1 ATOM 1299 C CA . SER A 1 163 ? 26.402 -32.942 19.604 1.00 98.21 ? 163 SER A CA 1 ATOM 1300 C C . SER A 1 163 ? 25.266 -32.613 18.638 1.00 97.94 ? 163 SER A C 1 ATOM 1301 O O . SER A 1 163 ? 24.146 -32.364 19.070 1.00 98.48 ? 163 SER A O 1 ATOM 1302 C CB . SER A 1 163 ? 26.257 -34.358 20.153 1.00 99.53 ? 163 SER A CB 1 ATOM 1303 O OG . SER A 1 163 ? 26.359 -35.319 19.118 1.00 101.13 ? 163 SER A OG 1 ATOM 1304 N N . TYR A 1 164 ? 25.558 -32.573 17.338 1.00 96.17 ? 164 TYR A N 1 ATOM 1305 C CA . TYR A 1 164 ? 24.504 -32.430 16.340 1.00 95.80 ? 164 TYR A CA 1 ATOM 1306 C C . TYR A 1 164 ? 24.540 -33.567 15.323 1.00 97.03 ? 164 TYR A C 1 ATOM 1307 O O . TYR A 1 164 ? 25.578 -33.836 14.712 1.00 95.58 ? 164 TYR A O 1 ATOM 1308 C CB . TYR A 1 164 ? 24.577 -31.082 15.634 1.00 93.43 ? 164 TYR A CB 1 ATOM 1309 C CG . TYR A 1 164 ? 23.585 -31.001 14.505 1.00 94.52 ? 164 TYR A CG 1 ATOM 1310 C CD1 . TYR A 1 164 ? 22.241 -30.727 14.743 1.00 97.05 ? 164 TYR A CD1 1 ATOM 1311 C CD2 . TYR A 1 164 ? 23.983 -31.236 13.191 1.00 94.69 ? 164 TYR A CD2 1 ATOM 1312 C CE1 . TYR A 1 164 ? 21.326 -30.670 13.700 1.00 98.18 ? 164 TYR A CE1 1 ATOM 1313 C CE2 . TYR A 1 164 ? 23.080 -31.181 12.139 1.00 95.40 ? 164 TYR A CE2 1 ATOM 1314 C CZ . TYR A 1 164 ? 21.755 -30.904 12.395 1.00 97.13 ? 164 TYR A CZ 1 ATOM 1315 O OH . TYR A 1 164 ? 20.882 -30.856 11.338 1.00 98.02 ? 164 TYR A OH 1 ATOM 1316 N N . ASN A 1 165 ? 23.389 -34.216 15.153 1.00 101.02 ? 165 ASN A N 1 ATOM 1317 C CA . ASN A 1 165 ? 23.208 -35.331 14.223 1.00 104.35 ? 165 ASN A CA 1 ATOM 1318 C C . ASN A 1 165 ? 22.649 -34.810 12.902 1.00 103.61 ? 165 ASN A C 1 ATOM 1319 O O . ASN A 1 165 ? 21.586 -34.189 12.873 1.00 104.40 ? 165 ASN A O 1 ATOM 1320 C CB . ASN A 1 165 ? 22.248 -36.355 14.844 1.00 109.83 ? 165 ASN A CB 1 ATOM 1321 C CG . ASN A 1 165 ? 22.135 -37.648 14.050 1.00 114.74 ? 165 ASN A CG 1 ATOM 1322 O OD1 . ASN A 1 165 ? 22.166 -37.658 12.837 1.00 112.67 ? 165 ASN A OD1 1 ATOM 1323 N ND2 . ASN A 1 165 ? 21.993 -38.748 14.750 1.00 125.83 ? 165 ASN A ND2 1 ATOM 1324 N N . ASN A 1 166 ? 23.370 -35.058 11.811 1.00 102.24 ? 166 ASN A N 1 ATOM 1325 C CA . ASN A 1 166 ? 22.894 -34.673 10.484 1.00 101.87 ? 166 ASN A CA 1 ATOM 1326 C C . ASN A 1 166 ? 21.817 -35.624 9.992 1.00 103.40 ? 166 ASN A C 1 ATOM 1327 O O . ASN A 1 166 ? 22.108 -36.610 9.303 1.00 102.06 ? 166 ASN A O 1 ATOM 1328 C CB . ASN A 1 166 ? 24.035 -34.634 9.474 1.00 99.83 ? 166 ASN A CB 1 ATOM 1329 C CG . ASN A 1 166 ? 23.625 -33.975 8.175 1.00 100.54 ? 166 ASN A CG 1 ATOM 1330 O OD1 . ASN A 1 166 ? 22.641 -33.234 8.134 1.00 100.32 ? 166 ASN A OD1 1 ATOM 1331 N ND2 . ASN A 1 166 ? 24.376 -34.236 7.106 1.00 100.48 ? 166 ASN A ND2 1 ATOM 1332 N N . THR A 1 167 ? 20.577 -35.326 10.361 1.00 105.16 ? 167 THR A N 1 ATOM 1333 C CA . THR A 1 167 ? 19.443 -36.173 9.998 1.00 108.36 ? 167 THR A CA 1 ATOM 1334 C C . THR A 1 167 ? 18.815 -35.771 8.653 1.00 110.59 ? 167 THR A C 1 ATOM 1335 O O . THR A 1 167 ? 18.102 -36.573 8.035 1.00 113.79 ? 167 THR A O 1 ATOM 1336 C CB . THR A 1 167 ? 18.371 -36.196 11.109 1.00 108.98 ? 167 THR A CB 1 ATOM 1337 O OG1 . THR A 1 167 ? 17.958 -34.859 11.420 1.00 106.40 ? 167 THR A OG1 1 ATOM 1338 C CG2 . THR A 1 167 ? 18.933 -36.873 12.355 1.00 108.71 ? 167 THR A CG2 1 ATOM 1339 N N . ASN A 1 168 ? 19.071 -34.541 8.198 1.00 108.24 ? 168 ASN A N 1 ATOM 1340 C CA . ASN A 1 168 ? 18.691 -34.145 6.824 1.00 106.34 ? 168 ASN A CA 1 ATOM 1341 C C . ASN A 1 168 ? 19.503 -34.907 5.776 1.00 101.93 ? 168 ASN A C 1 ATOM 1342 O O . ASN A 1 168 ? 20.514 -35.503 6.102 1.00 100.65 ? 168 ASN A O 1 ATOM 1343 C CB . ASN A 1 168 ? 18.729 -32.622 6.576 1.00 105.35 ? 168 ASN A CB 1 ATOM 1344 C CG . ASN A 1 168 ? 19.538 -31.859 7.601 1.00 103.97 ? 168 ASN A CG 1 ATOM 1345 O OD1 . ASN A 1 168 ? 19.089 -30.823 8.086 1.00 104.84 ? 168 ASN A OD1 1 ATOM 1346 N ND2 . ASN A 1 168 ? 20.734 -32.346 7.922 1.00 102.35 ? 168 ASN A ND2 1 ATOM 1347 N N . GLN A 1 169 ? 19.031 -34.902 4.531 1.00 101.46 ? 169 GLN A N 1 ATOM 1348 C CA . GLN A 1 169 ? 19.627 -35.712 3.453 1.00 102.56 ? 169 GLN A CA 1 ATOM 1349 C C . GLN A 1 169 ? 20.899 -35.148 2.841 1.00 98.40 ? 169 GLN A C 1 ATOM 1350 O O . GLN A 1 169 ? 21.741 -35.905 2.367 1.00 96.77 ? 169 GLN A O 1 ATOM 1351 C CB . GLN A 1 169 ? 18.625 -35.927 2.306 1.00 106.82 ? 169 GLN A CB 1 ATOM 1352 C CG . GLN A 1 169 ? 17.976 -37.290 2.314 1.00 110.74 ? 169 GLN A CG 1 ATOM 1353 C CD . GLN A 1 169 ? 17.347 -37.570 3.651 1.00 114.52 ? 169 GLN A CD 1 ATOM 1354 O OE1 . GLN A 1 169 ? 17.992 -38.117 4.547 1.00 114.42 ? 169 GLN A OE1 1 ATOM 1355 N NE2 . GLN A 1 169 ? 16.095 -37.147 3.818 1.00 118.81 ? 169 GLN A NE2 1 ATOM 1356 N N . GLU A 1 170 ? 21.014 -33.825 2.854 1.00 95.18 ? 170 GLU A N 1 ATOM 1357 C CA . GLU A 1 170 ? 22.050 -33.099 2.146 1.00 91.47 ? 170 GLU A CA 1 ATOM 1358 C C . GLU A 1 170 ? 23.271 -32.862 3.016 1.00 89.32 ? 170 GLU A C 1 ATOM 1359 O O . GLU A 1 170 ? 23.130 -32.428 4.156 1.00 90.43 ? 170 GLU A O 1 ATOM 1360 C CB . GLU A 1 170 ? 21.505 -31.743 1.731 1.00 90.68 ? 170 GLU A CB 1 ATOM 1361 C CG . GLU A 1 170 ? 20.211 -31.810 0.947 1.00 93.28 ? 170 GLU A CG 1 ATOM 1362 C CD . GLU A 1 170 ? 18.982 -31.788 1.818 1.00 94.49 ? 170 GLU A CD 1 ATOM 1363 O OE1 . GLU A 1 170 ? 19.077 -32.186 3.000 1.00 96.37 ? 170 GLU A OE1 1 ATOM 1364 O OE2 . GLU A 1 170 ? 17.923 -31.370 1.320 1.00 94.61 ? 170 GLU A OE2 1 ATOM 1365 N N . ASP A 1 171 ? 24.460 -33.150 2.481 1.00 88.45 ? 171 ASP A N 1 ATOM 1366 C CA . ASP A 1 171 ? 25.728 -32.818 3.137 1.00 85.85 ? 171 ASP A CA 1 ATOM 1367 C C . ASP A 1 171 ? 25.610 -31.458 3.804 1.00 84.21 ? 171 ASP A C 1 ATOM 1368 O O . ASP A 1 171 ? 24.996 -30.539 3.262 1.00 83.22 ? 171 ASP A O 1 ATOM 1369 C CB . ASP A 1 171 ? 26.897 -32.746 2.122 1.00 86.42 ? 171 ASP A CB 1 ATOM 1370 C CG . ASP A 1 171 ? 27.361 -34.117 1.613 1.00 88.94 ? 171 ASP A CG 1 ATOM 1371 O OD1 . ASP A 1 171 ? 26.970 -35.159 2.175 1.00 91.66 ? 171 ASP A OD1 1 ATOM 1372 O OD2 . ASP A 1 171 ? 28.136 -34.145 0.627 1.00 90.36 ? 171 ASP A OD2 1 ATOM 1373 N N . LEU A 1 172 ? 26.224 -31.322 4.969 1.00 84.09 ? 172 LEU A N 1 ATOM 1374 C CA . LEU A 1 172 ? 26.141 -30.093 5.728 1.00 84.98 ? 172 LEU A CA 1 ATOM 1375 C C . LEU A 1 172 ? 27.526 -29.480 5.951 1.00 81.96 ? 172 LEU A C 1 ATOM 1376 O O . LEU A 1 172 ? 28.432 -30.143 6.461 1.00 80.63 ? 172 LEU A O 1 ATOM 1377 C CB . LEU A 1 172 ? 25.454 -30.376 7.068 1.00 88.13 ? 172 LEU A CB 1 ATOM 1378 C CG . LEU A 1 172 ? 25.061 -29.147 7.904 1.00 90.10 ? 172 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 172 ? 23.916 -28.371 7.269 1.00 91.76 ? 172 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 172 ? 24.678 -29.553 9.320 1.00 92.37 ? 172 LEU A CD2 1 ATOM 1381 N N . LEU A 1 173 ? 27.678 -28.218 5.555 1.00 80.42 ? 173 LEU A N 1 ATOM 1382 C CA . LEU A 1 173 ? 28.873 -27.436 5.858 1.00 78.88 ? 173 LEU A CA 1 ATOM 1383 C C . LEU A 1 173 ? 28.753 -26.810 7.235 1.00 79.88 ? 173 LEU A C 1 ATOM 1384 O O . LEU A 1 173 ? 27.937 -25.907 7.447 1.00 81.56 ? 173 LEU A O 1 ATOM 1385 C CB . LEU A 1 173 ? 29.066 -26.318 4.840 1.00 78.60 ? 173 LEU A CB 1 ATOM 1386 C CG . LEU A 1 173 ? 30.216 -25.339 5.119 1.00 77.56 ? 173 LEU A CG 1 ATOM 1387 C CD1 . LEU A 1 173 ? 31.545 -26.072 5.176 1.00 76.83 ? 173 LEU A CD1 1 ATOM 1388 C CD2 . LEU A 1 173 ? 30.282 -24.261 4.048 1.00 77.52 ? 173 LEU A CD2 1 ATOM 1389 N N . VAL A 1 174 ? 29.573 -27.282 8.166 1.00 79.12 ? 174 VAL A N 1 ATOM 1390 C CA . VAL A 1 174 ? 29.576 -26.766 9.529 1.00 77.99 ? 174 VAL A CA 1 ATOM 1391 C C . VAL A 1 174 ? 30.830 -25.917 9.716 1.00 76.23 ? 174 VAL A C 1 ATOM 1392 O O . VAL A 1 174 ? 31.933 -26.361 9.401 1.00 74.51 ? 174 VAL A O 1 ATOM 1393 C CB . VAL A 1 174 ? 29.580 -27.903 10.569 1.00 78.72 ? 174 VAL A CB 1 ATOM 1394 C CG1 . VAL A 1 174 ? 29.390 -27.340 11.969 1.00 80.55 ? 174 VAL A CG1 1 ATOM 1395 C CG2 . VAL A 1 174 ? 28.503 -28.927 10.252 1.00 79.41 ? 174 VAL A CG2 1 ATOM 1396 N N . LEU A 1 175 ? 30.642 -24.700 10.223 1.00 76.04 ? 175 LEU A N 1 ATOM 1397 C CA . LEU A 1 175 ? 31.733 -23.784 10.549 1.00 74.56 ? 175 LEU A CA 1 ATOM 1398 C C . LEU A 1 175 ? 31.791 -23.564 12.051 1.00 76.23 ? 175 LEU A C 1 ATOM 1399 O O . LEU A 1 175 ? 30.752 -23.472 12.708 1.00 77.57 ? 175 LEU A O 1 ATOM 1400 C CB . LEU A 1 175 ? 31.507 -22.430 9.885 1.00 74.13 ? 175 LEU A CB 1 ATOM 1401 C CG . LEU A 1 175 ? 31.471 -22.386 8.355 1.00 73.66 ? 175 LEU A CG 1 ATOM 1402 C CD1 . LEU A 1 175 ? 30.535 -21.281 7.889 1.00 74.99 ? 175 LEU A CD1 1 ATOM 1403 C CD2 . LEU A 1 175 ? 32.863 -22.190 7.787 1.00 72.08 ? 175 LEU A CD2 1 ATOM 1404 N N . TRP A 1 176 ? 33.006 -23.485 12.587 1.00 76.17 ? 176 TRP A N 1 ATOM 1405 C CA . TRP A 1 176 ? 33.225 -23.095 13.974 1.00 77.30 ? 176 TRP A CA 1 ATOM 1406 C C . TRP A 1 176 ? 34.571 -22.399 14.104 1.00 77.24 ? 176 TRP A C 1 ATOM 1407 O O . TRP A 1 176 ? 35.303 -22.276 13.130 1.00 75.64 ? 176 TRP A O 1 ATOM 1408 C CB . TRP A 1 176 ? 33.164 -24.313 14.895 1.00 79.03 ? 176 TRP A CB 1 ATOM 1409 C CG . TRP A 1 176 ? 34.297 -25.276 14.732 1.00 78.51 ? 176 TRP A CG 1 ATOM 1410 C CD1 . TRP A 1 176 ? 35.439 -25.331 15.473 1.00 78.61 ? 176 TRP A CD1 1 ATOM 1411 C CD2 . TRP A 1 176 ? 34.386 -26.337 13.779 1.00 77.72 ? 176 TRP A CD2 1 ATOM 1412 N NE1 . TRP A 1 176 ? 36.242 -26.357 15.036 1.00 77.75 ? 176 TRP A NE1 1 ATOM 1413 C CE2 . TRP A 1 176 ? 35.614 -26.994 14.000 1.00 77.94 ? 176 TRP A CE2 1 ATOM 1414 C CE3 . TRP A 1 176 ? 33.541 -26.802 12.764 1.00 76.92 ? 176 TRP A CE3 1 ATOM 1415 C CZ2 . TRP A 1 176 ? 36.025 -28.086 13.232 1.00 78.25 ? 176 TRP A CZ2 1 ATOM 1416 C CZ3 . TRP A 1 176 ? 33.945 -27.886 12.005 1.00 77.15 ? 176 TRP A CZ3 1 ATOM 1417 C CH2 . TRP A 1 176 ? 35.175 -28.515 12.238 1.00 77.80 ? 176 TRP A CH2 1 ATOM 1418 N N . GLY A 1 177 ? 34.905 -21.949 15.310 1.00 79.83 ? 177 GLY A N 1 ATOM 1419 C CA . GLY A 1 177 ? 36.163 -21.227 15.511 1.00 80.19 ? 177 GLY A CA 1 ATOM 1420 C C . GLY A 1 177 ? 36.739 -21.256 16.908 1.00 80.64 ? 177 GLY A C 1 ATOM 1421 O O . GLY A 1 177 ? 36.101 -21.720 17.849 1.00 82.74 ? 177 GLY A O 1 ATOM 1422 N N . ILE A 1 178 ? 37.959 -20.740 17.016 1.00 80.56 ? 178 ILE A N 1 ATOM 1423 C CA . ILE A 1 178 ? 38.693 -20.637 18.277 1.00 81.88 ? 178 ILE A CA 1 ATOM 1424 C C . ILE A 1 178 ? 39.133 -19.180 18.432 1.00 82.42 ? 178 ILE A C 1 ATOM 1425 O O . ILE A 1 178 ? 39.483 -18.530 17.451 1.00 80.13 ? 178 ILE A O 1 ATOM 1426 C CB . ILE A 1 178 ? 39.927 -21.576 18.286 1.00 81.99 ? 178 ILE A CB 1 ATOM 1427 C CG1 . ILE A 1 178 ? 40.634 -21.600 19.644 1.00 84.12 ? 178 ILE A CG1 1 ATOM 1428 C CG2 . ILE A 1 178 ? 40.946 -21.166 17.237 1.00 80.99 ? 178 ILE A CG2 1 ATOM 1429 C CD1 . ILE A 1 178 ? 40.310 -22.788 20.517 1.00 85.89 ? 178 ILE A CD1 1 ATOM 1430 N N . HIS A 1 179 ? 39.106 -18.673 19.661 1.00 85.15 ? 179 HIS A N 1 ATOM 1431 C CA . HIS A 1 179 ? 39.610 -17.333 19.951 1.00 87.11 ? 179 HIS A CA 1 ATOM 1432 C C . HIS A 1 179 ? 40.983 -17.369 20.628 1.00 87.71 ? 179 HIS A C 1 ATOM 1433 O O . HIS A 1 179 ? 41.153 -17.981 21.679 1.00 89.90 ? 179 HIS A O 1 ATOM 1434 C CB . HIS A 1 179 ? 38.619 -16.563 20.822 1.00 89.41 ? 179 HIS A CB 1 ATOM 1435 C CG . HIS A 1 179 ? 39.132 -15.238 21.285 1.00 91.66 ? 179 HIS A CG 1 ATOM 1436 N ND1 . HIS A 1 179 ? 39.354 -14.950 22.614 1.00 95.43 ? 179 HIS A ND1 1 ATOM 1437 C CD2 . HIS A 1 179 ? 39.488 -14.130 20.595 1.00 91.82 ? 179 HIS A CD2 1 ATOM 1438 C CE1 . HIS A 1 179 ? 39.809 -13.715 22.726 1.00 96.78 ? 179 HIS A CE1 1 ATOM 1439 N NE2 . HIS A 1 179 ? 39.900 -13.197 21.515 1.00 95.46 ? 179 HIS A NE2 1 ATOM 1440 N N . HIS A 1 180 ? 41.948 -16.695 20.014 1.00 87.04 ? 180 HIS A N 1 ATOM 1441 C CA . HIS A 1 180 ? 43.296 -16.584 20.544 1.00 88.68 ? 180 HIS A CA 1 ATOM 1442 C C . HIS A 1 180 ? 43.420 -15.226 21.215 1.00 91.49 ? 180 HIS A C 1 ATOM 1443 O O . HIS A 1 180 ? 43.387 -14.204 20.535 1.00 91.72 ? 180 HIS A O 1 ATOM 1444 C CB . HIS A 1 180 ? 44.322 -16.680 19.414 1.00 86.96 ? 180 HIS A CB 1 ATOM 1445 C CG . HIS A 1 180 ? 44.275 -17.970 18.661 1.00 85.14 ? 180 HIS A CG 1 ATOM 1446 N ND1 . HIS A 1 180 ? 44.559 -19.181 19.247 1.00 86.13 ? 180 HIS A ND1 1 ATOM 1447 C CD2 . HIS A 1 180 ? 43.982 -18.241 17.368 1.00 83.50 ? 180 HIS A CD2 1 ATOM 1448 C CE1 . HIS A 1 180 ? 44.439 -20.145 18.355 1.00 83.86 ? 180 HIS A CE1 1 ATOM 1449 N NE2 . HIS A 1 180 ? 44.087 -19.601 17.206 1.00 82.74 ? 180 HIS A NE2 1 ATOM 1450 N N . PRO A 1 181 ? 43.559 -15.198 22.546 1.00 94.12 ? 181 PRO A N 1 ATOM 1451 C CA . PRO A 1 181 ? 43.611 -13.922 23.250 1.00 96.76 ? 181 PRO A CA 1 ATOM 1452 C C . PRO A 1 181 ? 45.029 -13.371 23.398 1.00 97.79 ? 181 PRO A C 1 ATOM 1453 O O . PRO A 1 181 ? 46.003 -14.072 23.127 1.00 96.51 ? 181 PRO A O 1 ATOM 1454 C CB . PRO A 1 181 ? 43.031 -14.276 24.616 1.00 99.47 ? 181 PRO A CB 1 ATOM 1455 C CG . PRO A 1 181 ? 43.451 -15.696 24.834 1.00 99.15 ? 181 PRO A CG 1 ATOM 1456 C CD . PRO A 1 181 ? 43.644 -16.333 23.479 1.00 95.91 ? 181 PRO A CD 1 ATOM 1457 N N . ASN A 1 182 ? 45.124 -12.129 23.863 1.00 101.11 ? 182 ASN A N 1 ATOM 1458 C CA . ASN A 1 182 ? 46.403 -11.418 23.979 1.00 103.14 ? 182 ASN A CA 1 ATOM 1459 C C . ASN A 1 182 ? 47.350 -11.877 25.078 1.00 104.03 ? 182 ASN A C 1 ATOM 1460 O O . ASN A 1 182 ? 48.550 -12.013 24.833 1.00 103.03 ? 182 ASN A O 1 ATOM 1461 C CB . ASN A 1 182 ? 46.137 -9.928 24.132 1.00 105.71 ? 182 ASN A CB 1 ATOM 1462 C CG . ASN A 1 182 ? 45.743 -9.308 22.826 1.00 106.49 ? 182 ASN A CG 1 ATOM 1463 O OD1 . ASN A 1 182 ? 46.599 -9.051 21.993 1.00 108.23 ? 182 ASN A OD1 1 ATOM 1464 N ND2 . ASN A 1 182 ? 44.445 -9.126 22.604 1.00 106.98 ? 182 ASN A ND2 1 ATOM 1465 N N . ASP A 1 183 ? 46.810 -12.099 26.277 1.00 105.90 ? 183 ASP A N 1 ATOM 1466 C CA . ASP A 1 183 ? 47.612 -12.482 27.453 1.00 108.03 ? 183 ASP A CA 1 ATOM 1467 C C . ASP A 1 183 ? 46.826 -13.339 28.452 1.00 107.70 ? 183 ASP A C 1 ATOM 1468 O O . ASP A 1 183 ? 45.624 -13.559 28.288 1.00 105.53 ? 183 ASP A O 1 ATOM 1469 C CB . ASP A 1 183 ? 48.174 -11.230 28.145 1.00 110.97 ? 183 ASP A CB 1 ATOM 1470 C CG . ASP A 1 183 ? 47.111 -10.179 28.416 1.00 112.36 ? 183 ASP A CG 1 ATOM 1471 O OD1 . ASP A 1 183 ? 46.072 -10.504 29.032 1.00 114.06 ? 183 ASP A OD1 1 ATOM 1472 O OD2 . ASP A 1 183 ? 47.322 -9.019 28.018 1.00 112.68 ? 183 ASP A OD2 1 ATOM 1473 N N . ALA A 1 184 ? 47.519 -13.822 29.482 1.00 109.46 ? 184 ALA A N 1 ATOM 1474 C CA . ALA A 1 184 ? 46.898 -14.640 30.531 1.00 110.57 ? 184 ALA A CA 1 ATOM 1475 C C . ALA A 1 184 ? 45.713 -13.933 31.194 1.00 112.01 ? 184 ALA A C 1 ATOM 1476 O O . ALA A 1 184 ? 44.721 -14.575 31.542 1.00 110.89 ? 184 ALA A O 1 ATOM 1477 C CB . ALA A 1 184 ? 47.931 -15.034 31.578 1.00 112.62 ? 184 ALA A CB 1 ATOM 1478 N N . ALA A 1 185 ? 45.818 -12.615 31.356 1.00 113.81 ? 185 ALA A N 1 ATOM 1479 C CA . ALA A 1 185 ? 44.770 -11.823 32.006 1.00 116.05 ? 185 ALA A CA 1 ATOM 1480 C C . ALA A 1 185 ? 43.473 -11.781 31.192 1.00 112.78 ? 185 ALA A C 1 ATOM 1481 O O . ALA A 1 185 ? 42.379 -11.837 31.749 1.00 113.33 ? 185 ALA A O 1 ATOM 1482 C CB . ALA A 1 185 ? 45.270 -10.411 32.290 1.00 118.62 ? 185 ALA A CB 1 ATOM 1483 N N . GLU A 1 186 ? 43.595 -11.693 29.875 1.00 109.78 ? 186 GLU A N 1 ATOM 1484 C CA . GLU A 1 186 ? 42.415 -11.683 29.008 1.00 107.66 ? 186 GLU A CA 1 ATOM 1485 C C . GLU A 1 186 ? 41.713 -13.048 28.975 1.00 105.96 ? 186 GLU A C 1 ATOM 1486 O O . GLU A 1 186 ? 40.483 -13.119 28.946 1.00 104.76 ? 186 GLU A O 1 ATOM 1487 C CB . GLU A 1 186 ? 42.796 -11.251 27.596 1.00 104.95 ? 186 GLU A CB 1 ATOM 1488 C CG . GLU A 1 186 ? 41.611 -10.824 26.746 1.00 103.61 ? 186 GLU A CG 1 ATOM 1489 C CD . GLU A 1 186 ? 42.035 -10.231 25.415 1.00 101.14 ? 186 GLU A CD 1 ATOM 1490 O OE1 . GLU A 1 186 ? 42.462 -10.995 24.514 1.00 98.95 ? 186 GLU A OE1 1 ATOM 1491 O OE2 . GLU A 1 186 ? 41.926 -8.996 25.274 1.00 101.39 ? 186 GLU A OE2 1 ATOM 1492 N N . GLN A 1 187 ? 42.501 -14.121 28.980 1.00 105.49 ? 187 GLN A N 1 ATOM 1493 C CA . GLN A 1 187 ? 41.968 -15.484 29.026 1.00 104.81 ? 187 GLN A CA 1 ATOM 1494 C C . GLN A 1 187 ? 40.992 -15.674 30.202 1.00 108.13 ? 187 GLN A C 1 ATOM 1495 O O . GLN A 1 187 ? 39.817 -15.991 30.001 1.00 107.33 ? 187 GLN A O 1 ATOM 1496 C CB . GLN A 1 187 ? 43.122 -16.492 29.112 1.00 104.18 ? 187 GLN A CB 1 ATOM 1497 C CG . GLN A 1 187 ? 42.699 -17.945 29.273 1.00 103.65 ? 187 GLN A CG 1 ATOM 1498 C CD . GLN A 1 187 ? 41.853 -18.444 28.115 1.00 100.48 ? 187 GLN A CD 1 ATOM 1499 O OE1 . GLN A 1 187 ? 42.040 -18.036 26.968 1.00 97.39 ? 187 GLN A OE1 1 ATOM 1500 N NE2 . GLN A 1 187 ? 40.919 -19.338 28.415 1.00 100.49 ? 187 GLN A NE2 1 ATOM 1501 N N . THR A 1 188 ? 41.476 -15.469 31.425 1.00 111.87 ? 188 THR A N 1 ATOM 1502 C CA . THR A 1 188 ? 40.635 -15.646 32.608 1.00 114.97 ? 188 THR A CA 1 ATOM 1503 C C . THR A 1 188 ? 39.488 -14.620 32.627 1.00 115.29 ? 188 THR A C 1 ATOM 1504 O O . THR A 1 188 ? 38.373 -14.935 33.041 1.00 116.93 ? 188 THR A O 1 ATOM 1505 C CB . THR A 1 188 ? 41.455 -15.582 33.923 1.00 119.54 ? 188 THR A CB 1 ATOM 1506 O OG1 . THR A 1 188 ? 42.087 -14.302 34.053 1.00 121.31 ? 188 THR A OG1 1 ATOM 1507 C CG2 . THR A 1 188 ? 42.525 -16.685 33.961 1.00 119.19 ? 188 THR A CG2 1 ATOM 1508 N N . LYS A 1 189 ? 39.757 -13.407 32.151 1.00 113.67 ? 189 LYS A N 1 ATOM 1509 C CA . LYS A 1 189 ? 38.739 -12.360 32.078 1.00 114.15 ? 189 LYS A CA 1 ATOM 1510 C C . LYS A 1 189 ? 37.516 -12.762 31.233 1.00 112.59 ? 189 LYS A C 1 ATOM 1511 O O . LYS A 1 189 ? 36.395 -12.398 31.577 1.00 114.36 ? 189 LYS A O 1 ATOM 1512 C CB . LYS A 1 189 ? 39.371 -11.070 31.543 1.00 113.93 ? 189 LYS A CB 1 ATOM 1513 C CG . LYS A 1 189 ? 38.425 -9.891 31.372 1.00 115.23 ? 189 LYS A CG 1 ATOM 1514 C CD . LYS A 1 189 ? 39.194 -8.648 30.942 1.00 115.78 ? 189 LYS A CD 1 ATOM 1515 C CE . LYS A 1 189 ? 38.279 -7.517 30.489 1.00 115.79 ? 189 LYS A CE 1 ATOM 1516 N NZ . LYS A 1 189 ? 37.844 -7.682 29.075 1.00 111.58 ? 189 LYS A NZ 1 ATOM 1517 N N . LEU A 1 190 ? 37.728 -13.510 30.147 1.00 108.90 ? 190 LEU A N 1 ATOM 1518 C CA . LEU A 1 190 ? 36.628 -13.954 29.274 1.00 107.81 ? 190 LEU A CA 1 ATOM 1519 C C . LEU A 1 190 ? 36.124 -15.368 29.582 1.00 107.57 ? 190 LEU A C 1 ATOM 1520 O O . LEU A 1 190 ? 34.921 -15.639 29.520 1.00 106.83 ? 190 LEU A O 1 ATOM 1521 C CB . LEU A 1 190 ? 37.055 -13.916 27.796 1.00 104.85 ? 190 LEU A CB 1 ATOM 1522 C CG . LEU A 1 190 ? 37.607 -12.603 27.234 1.00 105.54 ? 190 LEU A CG 1 ATOM 1523 C CD1 . LEU A 1 190 ? 37.707 -12.676 25.723 1.00 102.22 ? 190 LEU A CD1 1 ATOM 1524 C CD2 . LEU A 1 190 ? 36.775 -11.400 27.654 1.00 108.54 ? 190 LEU A CD2 1 ATOM 1525 N N . TYR A 1 191 ? 37.053 -16.268 29.888 1.00 107.99 ? 191 TYR A N 1 ATOM 1526 C CA . TYR A 1 191 ? 36.744 -17.690 30.000 1.00 107.86 ? 191 TYR A CA 1 ATOM 1527 C C . TYR A 1 191 ? 37.058 -18.313 31.366 1.00 111.71 ? 191 TYR A C 1 ATOM 1528 O O . TYR A 1 191 ? 36.774 -19.493 31.581 1.00 113.19 ? 191 TYR A O 1 ATOM 1529 C CB . TYR A 1 191 ? 37.509 -18.440 28.918 1.00 105.25 ? 191 TYR A CB 1 ATOM 1530 C CG . TYR A 1 191 ? 37.425 -17.778 27.555 1.00 102.61 ? 191 TYR A CG 1 ATOM 1531 C CD1 . TYR A 1 191 ? 36.217 -17.725 26.859 1.00 101.92 ? 191 TYR A CD1 1 ATOM 1532 C CD2 . TYR A 1 191 ? 38.546 -17.186 26.973 1.00 101.32 ? 191 TYR A CD2 1 ATOM 1533 C CE1 . TYR A 1 191 ? 36.129 -17.119 25.611 1.00 99.59 ? 191 TYR A CE1 1 ATOM 1534 C CE2 . TYR A 1 191 ? 38.468 -16.575 25.732 1.00 99.62 ? 191 TYR A CE2 1 ATOM 1535 C CZ . TYR A 1 191 ? 37.254 -16.544 25.056 1.00 98.00 ? 191 TYR A CZ 1 ATOM 1536 O OH . TYR A 1 191 ? 37.158 -15.931 23.837 1.00 94.67 ? 191 TYR A OH 1 ATOM 1537 N N . GLN A 1 192 ? 37.639 -17.535 32.278 1.00 113.95 ? 192 GLN A N 1 ATOM 1538 C CA . GLN A 1 192 ? 38.033 -18.019 33.607 1.00 117.11 ? 192 GLN A CA 1 ATOM 1539 C C . GLN A 1 192 ? 39.167 -19.053 33.550 1.00 115.61 ? 192 GLN A C 1 ATOM 1540 O O . GLN A 1 192 ? 40.278 -18.778 34.007 1.00 117.27 ? 192 GLN A O 1 ATOM 1541 C CB . GLN A 1 192 ? 36.821 -18.577 34.376 1.00 119.44 ? 192 GLN A CB 1 ATOM 1542 C CG . GLN A 1 192 ? 36.990 -18.602 35.894 1.00 123.82 ? 192 GLN A CG 1 ATOM 1543 C CD . GLN A 1 192 ? 36.449 -17.361 36.575 1.00 126.80 ? 192 GLN A CD 1 ATOM 1544 O OE1 . GLN A 1 192 ? 35.348 -16.911 36.283 1.00 126.94 ? 192 GLN A OE1 1 ATOM 1545 N NE2 . GLN A 1 192 ? 37.220 -16.812 37.498 1.00 130.01 ? 192 GLN A NE2 1 ATOM 1546 N N . ASN A 1 193 ? 38.880 -20.233 33.000 1.00 112.85 ? 193 ASN A N 1 ATOM 1547 C CA . ASN A 1 193 ? 39.854 -21.326 32.924 1.00 111.82 ? 193 ASN A CA 1 ATOM 1548 C C . ASN A 1 193 ? 41.104 -20.899 32.153 1.00 109.40 ? 193 ASN A C 1 ATOM 1549 O O . ASN A 1 193 ? 40.992 -20.388 31.044 1.00 107.20 ? 193 ASN A O 1 ATOM 1550 C CB . ASN A 1 193 ? 39.215 -22.551 32.264 1.00 110.19 ? 193 ASN A CB 1 ATOM 1551 C CG . ASN A 1 193 ? 37.966 -23.017 32.994 1.00 112.52 ? 193 ASN A CG 1 ATOM 1552 O OD1 . ASN A 1 193 ? 37.956 -23.102 34.223 1.00 117.17 ? 193 ASN A OD1 1 ATOM 1553 N ND2 . ASN A 1 193 ? 36.903 -23.305 32.247 1.00 110.19 ? 193 ASN A ND2 1 ATOM 1554 N N . PRO A 1 194 ? 42.295 -21.079 32.747 1.00 110.45 ? 194 PRO A N 1 ATOM 1555 C CA . PRO A 1 194 ? 43.513 -20.573 32.120 1.00 109.04 ? 194 PRO A CA 1 ATOM 1556 C C . PRO A 1 194 ? 44.038 -21.456 30.993 1.00 106.07 ? 194 PRO A C 1 ATOM 1557 O O . PRO A 1 194 ? 44.567 -20.935 30.017 1.00 103.22 ? 194 PRO A O 1 ATOM 1558 C CB . PRO A 1 194 ? 44.506 -20.535 33.278 1.00 112.50 ? 194 PRO A CB 1 ATOM 1559 C CG . PRO A 1 194 ? 44.066 -21.635 34.174 1.00 114.46 ? 194 PRO A CG 1 ATOM 1560 C CD . PRO A 1 194 ? 42.567 -21.684 34.062 1.00 113.87 ? 194 PRO A CD 1 ATOM 1561 N N . THR A 1 195 ? 43.910 -22.774 31.137 1.00 106.10 ? 195 THR A N 1 ATOM 1562 C CA . THR A 1 195 ? 44.322 -23.711 30.095 1.00 103.30 ? 195 THR A CA 1 ATOM 1563 C C . THR A 1 195 ? 43.071 -24.375 29.522 1.00 101.60 ? 195 THR A C 1 ATOM 1564 O O . THR A 1 195 ? 42.396 -25.131 30.218 1.00 101.90 ? 195 THR A O 1 ATOM 1565 C CB . THR A 1 195 ? 45.282 -24.786 30.648 1.00 104.54 ? 195 THR A CB 1 ATOM 1566 O OG1 . THR A 1 195 ? 46.243 -24.175 31.509 1.00 106.47 ? 195 THR A OG1 1 ATOM 1567 C CG2 . THR A 1 195 ? 46.018 -25.490 29.523 1.00 102.58 ? 195 THR A CG2 1 ATOM 1568 N N . THR A 1 196 ? 42.765 -24.086 28.256 1.00 99.39 ? 196 THR A N 1 ATOM 1569 C CA . THR A 1 196 ? 41.516 -24.545 27.639 1.00 97.61 ? 196 THR A CA 1 ATOM 1570 C C . THR A 1 196 ? 41.772 -25.245 26.317 1.00 94.75 ? 196 THR A C 1 ATOM 1571 O O . THR A 1 196 ? 42.910 -25.375 25.884 1.00 93.14 ? 196 THR A O 1 ATOM 1572 C CB . THR A 1 196 ? 40.553 -23.367 27.404 1.00 97.56 ? 196 THR A CB 1 ATOM 1573 O OG1 . THR A 1 196 ? 41.171 -22.419 26.532 1.00 96.17 ? 196 THR A OG1 1 ATOM 1574 C CG2 . THR A 1 196 ? 40.212 -22.689 28.724 1.00 100.95 ? 196 THR A CG2 1 ATOM 1575 N N . TYR A 1 197 ? 40.691 -25.700 25.692 1.00 94.04 ? 197 TYR A N 1 ATOM 1576 C CA . TYR A 1 197 ? 40.750 -26.455 24.455 1.00 91.35 ? 197 TYR A CA 1 ATOM 1577 C C . TYR A 1 197 ? 39.369 -26.558 23.817 1.00 90.71 ? 197 TYR A C 1 ATOM 1578 O O . TYR A 1 197 ? 38.354 -26.349 24.478 1.00 90.77 ? 197 TYR A O 1 ATOM 1579 C CB . TYR A 1 197 ? 41.254 -27.871 24.735 1.00 92.15 ? 197 TYR A CB 1 ATOM 1580 C CG . TYR A 1 197 ? 40.284 -28.700 25.549 1.00 93.65 ? 197 TYR A CG 1 ATOM 1581 C CD1 . TYR A 1 197 ? 40.214 -28.561 26.937 1.00 96.96 ? 197 TYR A CD1 1 ATOM 1582 C CD2 . TYR A 1 197 ? 39.429 -29.612 24.934 1.00 92.35 ? 197 TYR A CD2 1 ATOM 1583 C CE1 . TYR A 1 197 ? 39.329 -29.315 27.685 1.00 98.50 ? 197 TYR A CE1 1 ATOM 1584 C CE2 . TYR A 1 197 ? 38.541 -30.369 25.670 1.00 94.24 ? 197 TYR A CE2 1 ATOM 1585 C CZ . TYR A 1 197 ? 38.493 -30.215 27.048 1.00 97.77 ? 197 TYR A CZ 1 ATOM 1586 O OH . TYR A 1 197 ? 37.606 -30.960 27.791 1.00 99.72 ? 197 TYR A OH 1 ATOM 1587 N N . ILE A 1 198 ? 39.344 -26.888 22.529 1.00 89.38 ? 198 ILE A N 1 ATOM 1588 C CA . ILE A 1 198 ? 38.115 -27.283 21.855 1.00 89.23 ? 198 ILE A CA 1 ATOM 1589 C C . ILE A 1 198 ? 38.390 -28.592 21.140 1.00 88.98 ? 198 ILE A C 1 ATOM 1590 O O . ILE A 1 198 ? 39.286 -28.658 20.291 1.00 89.11 ? 198 ILE A O 1 ATOM 1591 C CB . ILE A 1 198 ? 37.669 -26.261 20.799 1.00 88.38 ? 198 ILE A CB 1 ATOM 1592 C CG1 . ILE A 1 198 ? 37.537 -24.866 21.399 1.00 89.02 ? 198 ILE A CG1 1 ATOM 1593 C CG2 . ILE A 1 198 ? 36.336 -26.676 20.182 1.00 88.38 ? 198 ILE A CG2 1 ATOM 1594 C CD1 . ILE A 1 198 ? 37.415 -23.795 20.341 1.00 88.06 ? 198 ILE A CD1 1 ATOM 1595 N N . SER A 1 199 ? 37.624 -29.627 21.472 1.00 89.18 ? 199 SER A N 1 ATOM 1596 C CA . SER A 1 199 ? 37.739 -30.900 20.781 1.00 88.29 ? 199 SER A CA 1 ATOM 1597 C C . SER A 1 199 ? 36.529 -31.103 19.884 1.00 87.11 ? 199 SER A C 1 ATOM 1598 O O . SER A 1 199 ? 35.393 -30.965 20.322 1.00 88.10 ? 199 SER A O 1 ATOM 1599 C CB . SER A 1 199 ? 37.889 -32.052 21.780 1.00 90.45 ? 199 SER A CB 1 ATOM 1600 O OG . SER A 1 199 ? 36.756 -32.190 22.610 1.00 91.57 ? 199 SER A OG 1 ATOM 1601 N N . VAL A 1 200 ? 36.785 -31.416 18.621 1.00 86.18 ? 200 VAL A N 1 ATOM 1602 C CA . VAL A 1 200 ? 35.728 -31.637 17.642 1.00 86.11 ? 200 VAL A CA 1 ATOM 1603 C C . VAL A 1 200 ? 35.915 -33.017 17.030 1.00 86.40 ? 200 VAL A C 1 ATOM 1604 O O . VAL A 1 200 ? 37.026 -33.390 16.639 1.00 85.85 ? 200 VAL A O 1 ATOM 1605 C CB . VAL A 1 200 ? 35.756 -30.574 16.522 1.00 84.56 ? 200 VAL A CB 1 ATOM 1606 C CG1 . VAL A 1 200 ? 34.487 -30.637 15.686 1.00 85.25 ? 200 VAL A CG1 1 ATOM 1607 C CG2 . VAL A 1 200 ? 35.911 -29.180 17.111 1.00 84.78 ? 200 VAL A CG2 1 ATOM 1608 N N . GLY A 1 201 ? 34.826 -33.773 16.945 1.00 87.37 ? 201 GLY A N 1 ATOM 1609 C CA . GLY A 1 201 ? 34.865 -35.105 16.357 1.00 88.18 ? 201 GLY A CA 1 ATOM 1610 C C . GLY A 1 201 ? 33.652 -35.410 15.500 1.00 88.05 ? 201 GLY A C 1 ATOM 1611 O O . GLY A 1 201 ? 32.538 -35.008 15.825 1.00 90.25 ? 201 GLY A O 1 ATOM 1612 N N . THR A 1 202 ? 33.884 -36.113 14.396 1.00 87.10 ? 202 THR A N 1 ATOM 1613 C CA . THR A 1 202 ? 32.822 -36.674 13.565 1.00 86.88 ? 202 THR A CA 1 ATOM 1614 C C . THR A 1 202 ? 33.195 -38.111 13.240 1.00 88.19 ? 202 THR A C 1 ATOM 1615 O O . THR A 1 202 ? 34.107 -38.678 13.842 1.00 89.40 ? 202 THR A O 1 ATOM 1616 C CB . THR A 1 202 ? 32.650 -35.912 12.228 1.00 85.25 ? 202 THR A CB 1 ATOM 1617 O OG1 . THR A 1 202 ? 33.796 -36.129 11.394 1.00 83.03 ? 202 THR A OG1 1 ATOM 1618 C CG2 . THR A 1 202 ? 32.451 -34.436 12.463 1.00 84.75 ? 202 THR A CG2 1 ATOM 1619 N N . SER A 1 203 ? 32.481 -38.697 12.286 1.00 89.08 ? 203 SER A N 1 ATOM 1620 C CA . SER A 1 203 ? 32.861 -39.977 11.701 1.00 90.00 ? 203 SER A CA 1 ATOM 1621 C C . SER A 1 203 ? 34.342 -40.026 11.340 1.00 88.81 ? 203 SER A C 1 ATOM 1622 O O . SER A 1 203 ? 34.986 -41.051 11.526 1.00 89.09 ? 203 SER A O 1 ATOM 1623 C CB . SER A 1 203 ? 32.027 -40.241 10.446 1.00 90.38 ? 203 SER A CB 1 ATOM 1624 O OG . SER A 1 203 ? 32.778 -40.934 9.469 1.00 92.30 ? 203 SER A OG 1 ATOM 1625 N N . THR A 1 204 ? 34.862 -38.923 10.805 1.00 87.90 ? 204 THR A N 1 ATOM 1626 C CA . THR A 1 204 ? 36.236 -38.867 10.298 1.00 87.19 ? 204 THR A CA 1 ATOM 1627 C C . THR A 1 204 ? 37.102 -37.851 11.029 1.00 87.75 ? 204 THR A C 1 ATOM 1628 O O . THR A 1 204 ? 38.293 -38.083 11.201 1.00 91.18 ? 204 THR A O 1 ATOM 1629 C CB . THR A 1 204 ? 36.267 -38.511 8.797 1.00 85.13 ? 204 THR A CB 1 ATOM 1630 O OG1 . THR A 1 204 ? 35.735 -37.194 8.599 1.00 82.72 ? 204 THR A OG1 1 ATOM 1631 C CG2 . THR A 1 204 ? 35.453 -39.507 7.993 1.00 86.01 ? 204 THR A CG2 1 ATOM 1632 N N . LEU A 1 205 ? 36.516 -36.730 11.444 1.00 86.65 ? 205 LEU A N 1 ATOM 1633 C CA . LEU A 1 205 ? 37.276 -35.660 12.083 1.00 85.59 ? 205 LEU A CA 1 ATOM 1634 C C . LEU A 1 205 ? 37.708 -36.037 13.511 1.00 86.01 ? 205 LEU A C 1 ATOM 1635 O O . LEU A 1 205 ? 36.931 -36.621 14.281 1.00 87.01 ? 205 LEU A O 1 ATOM 1636 C CB . LEU A 1 205 ? 36.451 -34.365 12.097 1.00 85.54 ? 205 LEU A CB 1 ATOM 1637 C CG . LEU A 1 205 ? 37.177 -33.077 12.506 1.00 85.28 ? 205 LEU A CG 1 ATOM 1638 C CD1 . LEU A 1 205 ? 38.313 -32.769 11.539 1.00 84.20 ? 205 LEU A CD1 1 ATOM 1639 C CD2 . LEU A 1 205 ? 36.208 -31.908 12.570 1.00 84.66 ? 205 LEU A CD2 1 ATOM 1640 N N . ASN A 1 206 ? 38.953 -35.702 13.845 1.00 84.20 ? 206 ASN A N 1 ATOM 1641 C CA . ASN A 1 206 ? 39.507 -35.952 15.172 1.00 84.52 ? 206 ASN A CA 1 ATOM 1642 C C . ASN A 1 206 ? 40.359 -34.772 15.623 1.00 83.20 ? 206 ASN A C 1 ATOM 1643 O O . ASN A 1 206 ? 41.576 -34.866 15.732 1.00 82.74 ? 206 ASN A O 1 ATOM 1644 C CB . ASN A 1 206 ? 40.344 -37.230 15.163 1.00 85.70 ? 206 ASN A CB 1 ATOM 1645 C CG . ASN A 1 206 ? 40.807 -37.631 16.545 1.00 86.74 ? 206 ASN A CG 1 ATOM 1646 O OD1 . ASN A 1 206 ? 40.190 -37.276 17.540 1.00 86.61 ? 206 ASN A OD1 1 ATOM 1647 N ND2 . ASN A 1 206 ? 41.905 -38.374 16.610 1.00 88.85 ? 206 ASN A ND2 1 ATOM 1648 N N . GLN A 1 207 ? 39.703 -33.661 15.906 1.00 82.38 ? 207 GLN A N 1 ATOM 1649 C CA . GLN A 1 207 ? 40.404 -32.416 16.161 1.00 82.44 ? 207 GLN A CA 1 ATOM 1650 C C . GLN A 1 207 ? 40.489 -32.091 17.658 1.00 85.00 ? 207 GLN A C 1 ATOM 1651 O O . GLN A 1 207 ? 39.637 -32.498 18.447 1.00 86.46 ? 207 GLN A O 1 ATOM 1652 C CB . GLN A 1 207 ? 39.693 -31.303 15.403 1.00 79.95 ? 207 GLN A CB 1 ATOM 1653 C CG . GLN A 1 207 ? 40.314 -29.932 15.526 1.00 79.03 ? 207 GLN A CG 1 ATOM 1654 C CD . GLN A 1 207 ? 39.536 -28.910 14.736 1.00 78.18 ? 207 GLN A CD 1 ATOM 1655 O OE1 . GLN A 1 207 ? 38.789 -28.114 15.294 1.00 78.56 ? 207 GLN A OE1 1 ATOM 1656 N NE2 . GLN A 1 207 ? 39.685 -28.948 13.418 1.00 78.06 ? 207 GLN A NE2 1 ATOM 1657 N N . ARG A 1 208 ? 41.545 -31.374 18.035 1.00 86.51 ? 208 ARG A N 1 ATOM 1658 C CA . ARG A 1 208 ? 41.646 -30.764 19.361 1.00 89.67 ? 208 ARG A CA 1 ATOM 1659 C C . ARG A 1 208 ? 42.468 -29.485 19.255 1.00 89.41 ? 208 ARG A C 1 ATOM 1660 O O . ARG A 1 208 ? 43.683 -29.532 19.071 1.00 89.88 ? 208 ARG A O 1 ATOM 1661 C CB . ARG A 1 208 ? 42.286 -31.714 20.376 1.00 92.57 ? 208 ARG A CB 1 ATOM 1662 C CG . ARG A 1 208 ? 42.223 -31.213 21.811 1.00 95.05 ? 208 ARG A CG 1 ATOM 1663 C CD . ARG A 1 208 ? 43.184 -31.979 22.707 1.00 97.59 ? 208 ARG A CD 1 ATOM 1664 N NE . ARG A 1 208 ? 42.979 -31.694 24.126 1.00 99.56 ? 208 ARG A NE 1 ATOM 1665 C CZ . ARG A 1 208 ? 41.984 -32.184 24.865 1.00 101.85 ? 208 ARG A CZ 1 ATOM 1666 N NH1 . ARG A 1 208 ? 41.065 -32.986 24.333 1.00 100.54 ? 208 ARG A NH1 1 ATOM 1667 N NH2 . ARG A 1 208 ? 41.900 -31.863 26.156 1.00 105.73 ? 208 ARG A NH2 1 ATOM 1668 N N . LEU A 1 209 ? 41.797 -28.345 19.363 1.00 88.90 ? 209 LEU A N 1 ATOM 1669 C CA . LEU A 1 209 ? 42.455 -27.060 19.225 1.00 88.04 ? 209 LEU A CA 1 ATOM 1670 C C . LEU A 1 209 ? 42.765 -26.525 20.611 1.00 90.21 ? 209 LEU A C 1 ATOM 1671 O O . LEU A 1 209 ? 41.996 -26.729 21.545 1.00 89.17 ? 209 LEU A O 1 ATOM 1672 C CB . LEU A 1 209 ? 41.556 -26.077 18.474 1.00 87.11 ? 209 LEU A CB 1 ATOM 1673 C CG . LEU A 1 209 ? 40.919 -26.551 17.159 1.00 86.10 ? 209 LEU A CG 1 ATOM 1674 C CD1 . LEU A 1 209 ? 39.789 -25.612 16.750 1.00 85.36 ? 209 LEU A CD1 1 ATOM 1675 C CD2 . LEU A 1 209 ? 41.955 -26.688 16.045 1.00 84.87 ? 209 LEU A CD2 1 ATOM 1676 N N . VAL A 1 210 ? 43.907 -25.860 20.735 1.00 92.22 ? 210 VAL A N 1 ATOM 1677 C CA . VAL A 1 210 ? 44.263 -25.146 21.949 1.00 96.58 ? 210 VAL A CA 1 ATOM 1678 C C . VAL A 1 210 ? 44.556 -23.694 21.574 1.00 95.57 ? 210 VAL A C 1 ATOM 1679 O O . VAL A 1 210 ? 45.209 -23.439 20.557 1.00 93.88 ? 210 VAL A O 1 ATOM 1680 C CB . VAL A 1 210 ? 45.464 -25.793 22.704 1.00 99.94 ? 210 VAL A CB 1 ATOM 1681 C CG1 . VAL A 1 210 ? 45.157 -27.247 23.036 1.00 100.11 ? 210 VAL A CG1 1 ATOM 1682 C CG2 . VAL A 1 210 ? 46.765 -25.696 21.913 1.00 100.31 ? 210 VAL A CG2 1 ATOM 1683 N N . PRO A 1 211 ? 44.063 -22.738 22.383 1.00 97.60 ? 211 PRO A N 1 ATOM 1684 C CA . PRO A 1 211 ? 44.358 -21.333 22.102 1.00 97.65 ? 211 PRO A CA 1 ATOM 1685 C C . PRO A 1 211 ? 45.844 -21.014 22.258 1.00 99.14 ? 211 PRO A C 1 ATOM 1686 O O . PRO A 1 211 ? 46.572 -21.703 22.988 1.00 99.26 ? 211 PRO A O 1 ATOM 1687 C CB . PRO A 1 211 ? 43.539 -20.563 23.149 1.00 99.25 ? 211 PRO A CB 1 ATOM 1688 C CG . PRO A 1 211 ? 42.614 -21.551 23.760 1.00 99.69 ? 211 PRO A CG 1 ATOM 1689 C CD . PRO A 1 211 ? 43.247 -22.896 23.598 1.00 99.07 ? 211 PRO A CD 1 ATOM 1690 N N . ARG A 1 212 ? 46.261 -19.939 21.605 1.00 98.50 ? 212 ARG A N 1 ATOM 1691 C CA . ARG A 1 212 ? 47.658 -19.617 21.431 1.00 99.29 ? 212 ARG A CA 1 ATOM 1692 C C . ARG A 1 212 ? 47.868 -18.156 21.766 1.00 101.56 ? 212 ARG A C 1 ATOM 1693 O O . ARG A 1 212 ? 47.341 -17.271 21.083 1.00 99.80 ? 212 ARG A O 1 ATOM 1694 C CB . ARG A 1 212 ? 48.114 -19.960 20.008 1.00 96.84 ? 212 ARG A CB 1 ATOM 1695 C CG . ARG A 1 212 ? 48.778 -21.330 19.952 1.00 97.72 ? 212 ARG A CG 1 ATOM 1696 C CD . ARG A 1 212 ? 48.515 -22.100 18.677 1.00 95.30 ? 212 ARG A CD 1 ATOM 1697 N NE . ARG A 1 212 ? 48.936 -21.359 17.496 1.00 93.44 ? 212 ARG A NE 1 ATOM 1698 C CZ . ARG A 1 212 ? 48.153 -21.070 16.461 1.00 92.43 ? 212 ARG A CZ 1 ATOM 1699 N NH1 . ARG A 1 212 ? 46.884 -21.462 16.418 1.00 90.35 ? 212 ARG A NH1 1 ATOM 1700 N NH2 . ARG A 1 212 ? 48.648 -20.392 15.441 1.00 94.03 ? 212 ARG A NH2 1 ATOM 1701 N N . ILE A 1 213 ? 48.625 -17.928 22.841 1.00 105.92 ? 213 ILE A N 1 ATOM 1702 C CA . ILE A 1 213 ? 48.923 -16.585 23.328 1.00 108.12 ? 213 ILE A CA 1 ATOM 1703 C C . ILE A 1 213 ? 50.191 -16.080 22.646 1.00 109.07 ? 213 ILE A C 1 ATOM 1704 O O . ILE A 1 213 ? 51.199 -16.793 22.574 1.00 110.15 ? 213 ILE A O 1 ATOM 1705 C CB . ILE A 1 213 ? 49.146 -16.534 24.861 1.00 110.83 ? 213 ILE A CB 1 ATOM 1706 C CG1 . ILE A 1 213 ? 48.093 -17.354 25.628 1.00 111.41 ? 213 ILE A CG1 1 ATOM 1707 C CG2 . ILE A 1 213 ? 49.143 -15.088 25.341 1.00 112.28 ? 213 ILE A CG2 1 ATOM 1708 C CD1 . ILE A 1 213 ? 46.661 -16.944 25.362 1.00 110.71 ? 213 ILE A CD1 1 ATOM 1709 N N . ALA A 1 214 ? 50.124 -14.851 22.146 1.00 108.75 ? 214 ALA A N 1 ATOM 1710 C CA . ALA A 1 214 ? 51.284 -14.160 21.602 1.00 108.97 ? 214 ALA A CA 1 ATOM 1711 C C . ALA A 1 214 ? 50.939 -12.688 21.473 1.00 108.74 ? 214 ALA A C 1 ATOM 1712 O O . ALA A 1 214 ? 49.763 -12.320 21.376 1.00 107.13 ? 214 ALA A O 1 ATOM 1713 C CB . ALA A 1 214 ? 51.679 -14.737 20.251 1.00 107.80 ? 214 ALA A CB 1 ATOM 1714 N N . THR A 1 215 ? 51.963 -11.846 21.490 1.00 110.05 ? 215 THR A N 1 ATOM 1715 C CA . THR A 1 215 ? 51.763 -10.411 21.375 1.00 110.58 ? 215 THR A CA 1 ATOM 1716 C C . THR A 1 215 ? 51.740 -10.072 19.901 1.00 107.39 ? 215 THR A C 1 ATOM 1717 O O . THR A 1 215 ? 52.687 -10.369 19.174 1.00 107.80 ? 215 THR A O 1 ATOM 1718 C CB . THR A 1 215 ? 52.877 -9.630 22.083 1.00 113.47 ? 215 THR A CB 1 ATOM 1719 O OG1 . THR A 1 215 ? 53.044 -10.155 23.401 1.00 114.40 ? 215 THR A OG1 1 ATOM 1720 C CG2 . THR A 1 215 ? 52.534 -8.143 22.160 1.00 115.27 ? 215 THR A CG2 1 ATOM 1721 N N . ARG A 1 216 ? 50.651 -9.460 19.462 1.00 104.20 ? 216 ARG A N 1 ATOM 1722 C CA . ARG A 1 216 ? 50.406 -9.287 18.047 1.00 100.35 ? 216 ARG A CA 1 ATOM 1723 C C . ARG A 1 216 ? 50.080 -7.840 17.739 1.00 100.35 ? 216 ARG A C 1 ATOM 1724 O O . ARG A 1 216 ? 49.439 -7.160 18.536 1.00 98.69 ? 216 ARG A O 1 ATOM 1725 C CB . ARG A 1 216 ? 49.241 -10.182 17.626 1.00 97.99 ? 216 ARG A CB 1 ATOM 1726 C CG . ARG A 1 216 ? 49.497 -11.665 17.831 1.00 96.75 ? 216 ARG A CG 1 ATOM 1727 C CD . ARG A 1 216 ? 48.266 -12.487 17.510 1.00 94.51 ? 216 ARG A CD 1 ATOM 1728 N NE . ARG A 1 216 ? 47.355 -12.615 18.650 1.00 95.47 ? 216 ARG A NE 1 ATOM 1729 C CZ . ARG A 1 216 ? 47.317 -13.644 19.501 1.00 95.54 ? 216 ARG A CZ 1 ATOM 1730 N NH1 . ARG A 1 216 ? 48.147 -14.675 19.388 1.00 94.72 ? 216 ARG A NH1 1 ATOM 1731 N NH2 . ARG A 1 216 ? 46.431 -13.643 20.486 1.00 97.32 ? 216 ARG A NH2 1 ATOM 1732 N N . SER A 1 217 ? 50.526 -7.380 16.573 1.00 99.50 ? 217 SER A N 1 ATOM 1733 C CA . SER A 1 217 ? 50.144 -6.074 16.060 1.00 99.77 ? 217 SER A CA 1 ATOM 1734 C C . SER A 1 217 ? 48.627 -5.980 15.994 1.00 99.18 ? 217 SER A C 1 ATOM 1735 O O . SER A 1 217 ? 47.946 -6.979 15.774 1.00 97.73 ? 217 SER A O 1 ATOM 1736 C CB . SER A 1 217 ? 50.728 -5.861 14.664 1.00 98.94 ? 217 SER A CB 1 ATOM 1737 O OG . SER A 1 217 ? 52.101 -6.205 14.625 1.00 100.71 ? 217 SER A OG 1 ATOM 1738 N N . LYS A 1 218 ? 48.097 -4.781 16.192 1.00 100.57 ? 218 LYS A N 1 ATOM 1739 C CA . LYS A 1 218 ? 46.662 -4.572 16.075 1.00 100.66 ? 218 LYS A CA 1 ATOM 1740 C C . LYS A 1 218 ? 46.241 -4.554 14.609 1.00 99.47 ? 218 LYS A C 1 ATOM 1741 O O . LYS A 1 218 ? 46.963 -4.051 13.749 1.00 99.94 ? 218 LYS A O 1 ATOM 1742 C CB . LYS A 1 218 ? 46.232 -3.282 16.781 1.00 103.22 ? 218 LYS A CB 1 ATOM 1743 C CG . LYS A 1 218 ? 46.208 -3.438 18.286 1.00 104.97 ? 218 LYS A CG 1 ATOM 1744 C CD . LYS A 1 218 ? 45.873 -2.156 19.015 1.00 107.67 ? 218 LYS A CD 1 ATOM 1745 C CE . LYS A 1 218 ? 46.097 -2.351 20.506 1.00 110.66 ? 218 LYS A CE 1 ATOM 1746 N NZ . LYS A 1 218 ? 45.511 -1.242 21.298 1.00 114.49 ? 218 LYS A NZ 1 ATOM 1747 N N . VAL A 1 219 ? 45.079 -5.137 14.336 1.00 97.99 ? 219 VAL A N 1 ATOM 1748 C CA . VAL A 1 219 ? 44.503 -5.157 13.003 1.00 94.55 ? 219 VAL A CA 1 ATOM 1749 C C . VAL A 1 219 ? 43.004 -4.955 13.166 1.00 93.32 ? 219 VAL A C 1 ATOM 1750 O O . VAL A 1 219 ? 42.343 -5.748 13.821 1.00 92.15 ? 219 VAL A O 1 ATOM 1751 C CB . VAL A 1 219 ? 44.793 -6.495 12.304 1.00 93.79 ? 219 VAL A CB 1 ATOM 1752 C CG1 . VAL A 1 219 ? 44.154 -6.527 10.922 1.00 92.67 ? 219 VAL A CG1 1 ATOM 1753 C CG2 . VAL A 1 219 ? 46.295 -6.733 12.205 1.00 94.38 ? 219 VAL A CG2 1 ATOM 1754 N N . ASN A 1 220 ? 42.477 -3.882 12.585 1.00 94.02 ? 220 ASN A N 1 ATOM 1755 C CA . ASN A 1 220 ? 41.108 -3.432 12.863 1.00 94.59 ? 220 ASN A CA 1 ATOM 1756 C C . ASN A 1 220 ? 40.845 -3.292 14.368 1.00 94.56 ? 220 ASN A C 1 ATOM 1757 O O . ASN A 1 220 ? 39.794 -3.695 14.869 1.00 94.61 ? 220 ASN A O 1 ATOM 1758 C CB . ASN A 1 220 ? 40.069 -4.359 12.205 1.00 94.72 ? 220 ASN A CB 1 ATOM 1759 C CG . ASN A 1 220 ? 40.204 -4.421 10.683 1.00 94.74 ? 220 ASN A CG 1 ATOM 1760 O OD1 . ASN A 1 220 ? 40.119 -5.493 10.079 1.00 90.59 ? 220 ASN A OD1 1 ATOM 1761 N ND2 . ASN A 1 220 ? 40.404 -3.264 10.057 1.00 96.80 ? 220 ASN A ND2 1 ATOM 1762 N N . GLY A 1 221 ? 41.817 -2.720 15.077 1.00 95.00 ? 221 GLY A N 1 ATOM 1763 C CA . GLY A 1 221 ? 41.681 -2.387 16.494 1.00 95.73 ? 221 GLY A CA 1 ATOM 1764 C C . GLY A 1 221 ? 41.887 -3.533 17.470 1.00 94.80 ? 221 GLY A C 1 ATOM 1765 O O . GLY A 1 221 ? 41.777 -3.342 18.678 1.00 96.30 ? 221 GLY A O 1 ATOM 1766 N N . GLN A 1 222 ? 42.188 -4.724 16.966 1.00 92.34 ? 222 GLN A N 1 ATOM 1767 C CA . GLN A 1 222 ? 42.309 -5.897 17.821 1.00 92.78 ? 222 GLN A CA 1 ATOM 1768 C C . GLN A 1 222 ? 43.658 -6.558 17.634 1.00 93.52 ? 222 GLN A C 1 ATOM 1769 O O . GLN A 1 222 ? 44.179 -6.620 16.514 1.00 93.13 ? 222 GLN A O 1 ATOM 1770 C CB . GLN A 1 222 ? 41.217 -6.923 17.509 1.00 91.03 ? 222 GLN A CB 1 ATOM 1771 C CG . GLN A 1 222 ? 39.819 -6.351 17.302 1.00 91.58 ? 222 GLN A CG 1 ATOM 1772 C CD . GLN A 1 222 ? 39.291 -5.556 18.485 1.00 93.87 ? 222 GLN A CD 1 ATOM 1773 O OE1 . GLN A 1 222 ? 39.659 -5.797 19.643 1.00 93.91 ? 222 GLN A OE1 1 ATOM 1774 N NE2 . GLN A 1 222 ? 38.403 -4.603 18.195 1.00 94.63 ? 222 GLN A NE2 1 ATOM 1775 N N . SER A 1 223 ? 44.215 -7.051 18.739 1.00 95.37 ? 223 SER A N 1 ATOM 1776 C CA . SER A 1 223 ? 45.429 -7.868 18.707 1.00 95.19 ? 223 SER A CA 1 ATOM 1777 C C . SER A 1 223 ? 45.113 -9.346 18.936 1.00 93.49 ? 223 SER A C 1 ATOM 1778 O O . SER A 1 223 ? 45.941 -10.217 18.663 1.00 92.10 ? 223 SER A O 1 ATOM 1779 C CB . SER A 1 223 ? 46.435 -7.360 19.738 1.00 98.67 ? 223 SER A CB 1 ATOM 1780 O OG . SER A 1 223 ? 47.056 -6.168 19.295 1.00 100.25 ? 223 SER A OG 1 ATOM 1781 N N . GLY A 1 224 ? 43.910 -9.619 19.435 1.00 93.72 ? 224 GLY A N 1 ATOM 1782 C CA . GLY A 1 224 ? 43.397 -10.980 19.508 1.00 92.34 ? 224 GLY A CA 1 ATOM 1783 C C . GLY A 1 224 ? 43.018 -11.486 18.129 1.00 88.93 ? 224 GLY A C 1 ATOM 1784 O O . GLY A 1 224 ? 42.770 -10.695 17.221 1.00 88.51 ? 224 GLY A O 1 ATOM 1785 N N . ARG A 1 225 ? 42.958 -12.808 17.984 1.00 87.24 ? 225 ARG A N 1 ATOM 1786 C CA . ARG A 1 225 ? 42.726 -13.446 16.690 1.00 85.44 ? 225 ARG A CA 1 ATOM 1787 C C . ARG A 1 225 ? 41.623 -14.496 16.765 1.00 84.73 ? 225 ARG A C 1 ATOM 1788 O O . ARG A 1 225 ? 41.395 -15.092 17.810 1.00 86.31 ? 225 ARG A O 1 ATOM 1789 C CB . ARG A 1 225 ? 44.019 -14.105 16.196 1.00 83.98 ? 225 ARG A CB 1 ATOM 1790 C CG . ARG A 1 225 ? 45.171 -13.141 15.943 1.00 83.99 ? 225 ARG A CG 1 ATOM 1791 C CD . ARG A 1 225 ? 44.992 -12.380 14.640 1.00 82.38 ? 225 ARG A CD 1 ATOM 1792 N NE . ARG A 1 225 ? 46.111 -11.471 14.380 1.00 82.43 ? 225 ARG A NE 1 ATOM 1793 C CZ . ARG A 1 225 ? 46.192 -10.208 14.804 1.00 82.95 ? 225 ARG A CZ 1 ATOM 1794 N NH1 . ARG A 1 225 ? 45.221 -9.658 15.541 1.00 83.43 ? 225 ARG A NH1 1 ATOM 1795 N NH2 . ARG A 1 225 ? 47.264 -9.488 14.492 1.00 83.49 ? 225 ARG A NH2 1 ATOM 1796 N N . MET A 1 226 ? 40.928 -14.697 15.652 1.00 82.66 ? 226 MET A N 1 ATOM 1797 C CA . MET A 1 226 ? 39.995 -15.800 15.519 1.00 82.90 ? 226 MET A CA 1 ATOM 1798 C C . MET A 1 226 ? 40.524 -16.694 14.417 1.00 82.39 ? 226 MET A C 1 ATOM 1799 O O . MET A 1 226 ? 40.979 -16.207 13.385 1.00 82.52 ? 226 MET A O 1 ATOM 1800 C CB . MET A 1 226 ? 38.604 -15.304 15.140 1.00 83.93 ? 226 MET A CB 1 ATOM 1801 C CG . MET A 1 226 ? 37.919 -14.462 16.210 1.00 87.25 ? 226 MET A CG 1 ATOM 1802 S SD . MET A 1 226 ? 37.180 -15.410 17.558 1.00 89.66 ? 226 MET A SD 1 ATOM 1803 C CE . MET A 1 226 ? 36.427 -14.052 18.450 1.00 92.81 ? 226 MET A CE 1 ATOM 1804 N N . GLU A 1 227 ? 40.473 -18.001 14.636 1.00 81.77 ? 227 GLU A N 1 ATOM 1805 C CA . GLU A 1 227 ? 40.877 -18.967 13.629 1.00 80.27 ? 227 GLU A CA 1 ATOM 1806 C C . GLU A 1 227 ? 39.673 -19.848 13.350 1.00 79.28 ? 227 GLU A C 1 ATOM 1807 O O . GLU A 1 227 ? 39.173 -20.517 14.254 1.00 81.24 ? 227 GLU A O 1 ATOM 1808 C CB . GLU A 1 227 ? 42.063 -19.781 14.136 1.00 81.33 ? 227 GLU A CB 1 ATOM 1809 C CG . GLU A 1 227 ? 42.761 -20.599 13.066 1.00 81.69 ? 227 GLU A CG 1 ATOM 1810 C CD . GLU A 1 227 ? 44.062 -21.213 13.551 1.00 82.75 ? 227 GLU A CD 1 ATOM 1811 O OE1 . GLU A 1 227 ? 44.349 -21.125 14.763 1.00 82.87 ? 227 GLU A OE1 1 ATOM 1812 O OE2 . GLU A 1 227 ? 44.803 -21.777 12.715 1.00 82.95 ? 227 GLU A OE2 1 ATOM 1813 N N . PHE A 1 228 ? 39.181 -19.826 12.117 1.00 77.06 ? 228 PHE A N 1 ATOM 1814 C CA . PHE A 1 228 ? 37.947 -20.529 11.800 1.00 75.64 ? 228 PHE A CA 1 ATOM 1815 C C . PHE A 1 228 ? 38.230 -21.821 11.077 1.00 73.50 ? 228 PHE A C 1 ATOM 1816 O O . PHE A 1 228 ? 39.164 -21.902 10.293 1.00 73.08 ? 228 PHE A O 1 ATOM 1817 C CB . PHE A 1 228 ? 37.019 -19.637 10.994 1.00 76.24 ? 228 PHE A CB 1 ATOM 1818 C CG . PHE A 1 228 ? 36.518 -18.460 11.772 1.00 77.12 ? 228 PHE A CG 1 ATOM 1819 C CD1 . PHE A 1 228 ? 35.440 -18.591 12.630 1.00 78.22 ? 228 PHE A CD1 1 ATOM 1820 C CD2 . PHE A 1 228 ? 37.149 -17.234 11.674 1.00 77.21 ? 228 PHE A CD2 1 ATOM 1821 C CE1 . PHE A 1 228 ? 34.989 -17.515 13.364 1.00 79.95 ? 228 PHE A CE1 1 ATOM 1822 C CE2 . PHE A 1 228 ? 36.701 -16.151 12.399 1.00 78.88 ? 228 PHE A CE2 1 ATOM 1823 C CZ . PHE A 1 228 ? 35.624 -16.291 13.252 1.00 80.13 ? 228 PHE A CZ 1 ATOM 1824 N N . PHE A 1 229 ? 37.420 -22.828 11.384 1.00 72.50 ? 229 PHE A N 1 ATOM 1825 C CA . PHE A 1 229 ? 37.562 -24.167 10.841 1.00 71.83 ? 229 PHE A CA 1 ATOM 1826 C C . PHE A 1 229 ? 36.229 -24.640 10.301 1.00 71.52 ? 229 PHE A C 1 ATOM 1827 O O . PHE A 1 229 ? 35.177 -24.084 10.623 1.00 71.11 ? 229 PHE A O 1 ATOM 1828 C CB . PHE A 1 229 ? 38.031 -25.140 11.921 1.00 72.90 ? 229 PHE A CB 1 ATOM 1829 C CG . PHE A 1 229 ? 39.414 -24.859 12.422 1.00 73.36 ? 229 PHE A CG 1 ATOM 1830 C CD1 . PHE A 1 229 ? 39.622 -23.932 13.432 1.00 74.94 ? 229 PHE A CD1 1 ATOM 1831 C CD2 . PHE A 1 229 ? 40.509 -25.520 11.885 1.00 73.57 ? 229 PHE A CD2 1 ATOM 1832 C CE1 . PHE A 1 229 ? 40.904 -23.665 13.901 1.00 75.64 ? 229 PHE A CE1 1 ATOM 1833 C CE2 . PHE A 1 229 ? 41.791 -25.256 12.341 1.00 74.82 ? 229 PHE A CE2 1 ATOM 1834 C CZ . PHE A 1 229 ? 41.992 -24.327 13.356 1.00 75.56 ? 229 PHE A CZ 1 ATOM 1835 N N . TRP A 1 230 ? 36.283 -25.670 9.469 1.00 71.49 ? 230 TRP A N 1 ATOM 1836 C CA . TRP A 1 230 ? 35.079 -26.211 8.874 1.00 71.32 ? 230 TRP A CA 1 ATOM 1837 C C . TRP A 1 230 ? 35.188 -27.697 8.626 1.00 71.04 ? 230 TRP A C 1 ATOM 1838 O O . TRP A 1 230 ? 36.274 -28.254 8.638 1.00 69.80 ? 230 TRP A O 1 ATOM 1839 C CB . TRP A 1 230 ? 34.790 -25.508 7.549 1.00 70.59 ? 230 TRP A CB 1 ATOM 1840 C CG . TRP A 1 230 ? 35.881 -25.619 6.532 1.00 69.39 ? 230 TRP A CG 1 ATOM 1841 C CD1 . TRP A 1 230 ? 36.981 -24.822 6.427 1.00 68.96 ? 230 TRP A CD1 1 ATOM 1842 C CD2 . TRP A 1 230 ? 35.962 -26.556 5.459 1.00 69.13 ? 230 TRP A CD2 1 ATOM 1843 N NE1 . TRP A 1 230 ? 37.750 -25.213 5.369 1.00 68.40 ? 230 TRP A NE1 1 ATOM 1844 C CE2 . TRP A 1 230 ? 37.145 -26.276 4.754 1.00 69.08 ? 230 TRP A CE2 1 ATOM 1845 C CE3 . TRP A 1 230 ? 35.153 -27.613 5.029 1.00 70.30 ? 230 TRP A CE3 1 ATOM 1846 C CZ2 . TRP A 1 230 ? 37.540 -27.011 3.638 1.00 70.40 ? 230 TRP A CZ2 1 ATOM 1847 C CZ3 . TRP A 1 230 ? 35.544 -28.344 3.920 1.00 71.11 ? 230 TRP A CZ3 1 ATOM 1848 C CH2 . TRP A 1 230 ? 36.729 -28.044 3.238 1.00 70.91 ? 230 TRP A CH2 1 ATOM 1849 N N . THR A 1 231 ? 34.041 -28.328 8.410 1.00 71.22 ? 231 THR A N 1 ATOM 1850 C CA . THR A 1 231 ? 33.996 -29.684 7.897 1.00 71.26 ? 231 THR A CA 1 ATOM 1851 C C . THR A 1 231 ? 32.711 -29.883 7.113 1.00 72.44 ? 231 THR A C 1 ATOM 1852 O O . THR A 1 231 ? 31.812 -29.038 7.140 1.00 73.14 ? 231 THR A O 1 ATOM 1853 C CB . THR A 1 231 ? 34.086 -30.719 9.032 1.00 71.98 ? 231 THR A CB 1 ATOM 1854 O OG1 . THR A 1 231 ? 34.439 -31.998 8.497 1.00 71.05 ? 231 THR A OG1 1 ATOM 1855 C CG2 . THR A 1 231 ? 32.768 -30.838 9.777 1.00 72.92 ? 231 THR A CG2 1 ATOM 1856 N N . ILE A 1 232 ? 32.641 -31.000 6.406 1.00 73.71 ? 232 ILE A N 1 ATOM 1857 C CA . ILE A 1 232 ? 31.423 -31.433 5.738 1.00 75.17 ? 232 ILE A CA 1 ATOM 1858 C C . ILE A 1 232 ? 30.922 -32.631 6.520 1.00 75.99 ? 232 ILE A C 1 ATOM 1859 O O . ILE A 1 232 ? 31.559 -33.674 6.537 1.00 77.21 ? 232 ILE A O 1 ATOM 1860 C CB . ILE A 1 232 ? 31.687 -31.804 4.254 1.00 75.91 ? 232 ILE A CB 1 ATOM 1861 C CG1 . ILE A 1 232 ? 31.381 -30.622 3.338 1.00 75.15 ? 232 ILE A CG1 1 ATOM 1862 C CG2 . ILE A 1 232 ? 30.813 -32.965 3.794 1.00 77.73 ? 232 ILE A CG2 1 ATOM 1863 C CD1 . ILE A 1 232 ? 32.080 -29.353 3.727 1.00 74.36 ? 232 ILE A CD1 1 ATOM 1864 N N . LEU A 1 233 ? 29.790 -32.472 7.183 1.00 77.50 ? 233 LEU A N 1 ATOM 1865 C CA . LEU A 1 233 ? 29.196 -33.554 7.948 1.00 78.85 ? 233 LEU A CA 1 ATOM 1866 C C . LEU A 1 233 ? 28.310 -34.363 7.009 1.00 80.15 ? 233 LEU A C 1 ATOM 1867 O O . LEU A 1 233 ? 27.352 -33.831 6.459 1.00 80.16 ? 233 LEU A O 1 ATOM 1868 C CB . LEU A 1 233 ? 28.374 -32.960 9.092 1.00 79.50 ? 233 LEU A CB 1 ATOM 1869 C CG . LEU A 1 233 ? 27.960 -33.845 10.271 1.00 81.15 ? 233 LEU A CG 1 ATOM 1870 C CD1 . LEU A 1 233 ? 29.175 -34.340 11.046 1.00 80.79 ? 233 LEU A CD1 1 ATOM 1871 C CD2 . LEU A 1 233 ? 27.017 -33.071 11.186 1.00 81.81 ? 233 LEU A CD2 1 ATOM 1872 N N . LYS A 1 234 ? 28.636 -35.635 6.810 1.00 82.57 ? 234 LYS A N 1 ATOM 1873 C CA . LYS A 1 234 ? 27.845 -36.500 5.918 1.00 87.47 ? 234 LYS A CA 1 ATOM 1874 C C . LYS A 1 234 ? 26.424 -36.694 6.484 1.00 89.76 ? 234 LYS A C 1 ATOM 1875 O O . LYS A 1 234 ? 26.141 -36.242 7.598 1.00 91.35 ? 234 LYS A O 1 ATOM 1876 C CB . LYS A 1 234 ? 28.541 -37.868 5.729 1.00 90.88 ? 234 LYS A CB 1 ATOM 1877 C CG . LYS A 1 234 ? 29.934 -37.878 5.072 1.00 90.84 ? 234 LYS A CG 1 ATOM 1878 C CD . LYS A 1 234 ? 30.087 -36.997 3.836 1.00 91.60 ? 234 LYS A CD 1 ATOM 1879 C CE . LYS A 1 234 ? 29.096 -37.301 2.711 1.00 95.61 ? 234 LYS A CE 1 ATOM 1880 N NZ . LYS A 1 234 ? 29.350 -38.558 1.954 1.00 98.71 ? 234 LYS A NZ 1 ATOM 1881 N N . PRO A 1 235 ? 25.513 -37.348 5.726 1.00 91.56 ? 235 PRO A N 1 ATOM 1882 C CA . PRO A 1 235 ? 24.198 -37.599 6.336 1.00 91.89 ? 235 PRO A CA 1 ATOM 1883 C C . PRO A 1 235 ? 24.289 -38.711 7.374 1.00 93.11 ? 235 PRO A C 1 ATOM 1884 O O . PRO A 1 235 ? 25.196 -39.541 7.292 1.00 91.87 ? 235 PRO A O 1 ATOM 1885 C CB . PRO A 1 235 ? 23.314 -38.010 5.158 1.00 93.35 ? 235 PRO A CB 1 ATOM 1886 C CG . PRO A 1 235 ? 24.225 -38.299 4.016 1.00 92.88 ? 235 PRO A CG 1 ATOM 1887 C CD . PRO A 1 235 ? 25.630 -37.945 4.382 1.00 91.27 ? 235 PRO A CD 1 ATOM 1888 N N . ASN A 1 236 ? 23.381 -38.708 8.353 1.00 94.76 ? 236 ASN A N 1 ATOM 1889 C CA . ASN A 1 236 ? 23.410 -39.671 9.453 1.00 96.40 ? 236 ASN A CA 1 ATOM 1890 C C . ASN A 1 236 ? 24.662 -39.593 10.330 1.00 96.05 ? 236 ASN A C 1 ATOM 1891 O O . ASN A 1 236 ? 24.847 -40.442 11.202 1.00 98.73 ? 236 ASN A O 1 ATOM 1892 C CB . ASN A 1 236 ? 23.273 -41.110 8.928 1.00 98.72 ? 236 ASN A CB 1 ATOM 1893 C CG . ASN A 1 236 ? 21.897 -41.693 9.148 1.00 102.52 ? 236 ASN A CG 1 ATOM 1894 O OD1 . ASN A 1 236 ? 21.234 -41.434 10.158 1.00 104.52 ? 236 ASN A OD1 1 ATOM 1895 N ND2 . ASN A 1 236 ? 21.471 -42.523 8.209 1.00 104.78 ? 236 ASN A ND2 1 ATOM 1896 N N . ASP A 1 237 ? 25.527 -38.608 10.112 1.00 93.32 ? 237 ASP A N 1 ATOM 1897 C CA . ASP A 1 237 ? 26.714 -38.487 10.941 1.00 92.35 ? 237 ASP A CA 1 ATOM 1898 C C . ASP A 1 237 ? 26.493 -37.411 11.989 1.00 91.08 ? 237 ASP A C 1 ATOM 1899 O O . ASP A 1 237 ? 25.638 -36.534 11.837 1.00 89.76 ? 237 ASP A O 1 ATOM 1900 C CB . ASP A 1 237 ? 27.940 -38.169 10.097 1.00 91.70 ? 237 ASP A CB 1 ATOM 1901 C CG . ASP A 1 237 ? 29.247 -38.392 10.848 1.00 91.35 ? 237 ASP A CG 1 ATOM 1902 O OD1 . ASP A 1 237 ? 29.320 -39.299 11.716 1.00 92.04 ? 237 ASP A OD1 1 ATOM 1903 O OD2 . ASP A 1 237 ? 30.208 -37.649 10.558 1.00 89.81 ? 237 ASP A OD2 1 ATOM 1904 N N . ALA A 1 238 ? 27.263 -37.503 13.062 1.00 91.10 ? 238 ALA A N 1 ATOM 1905 C CA . ALA A 1 238 ? 27.111 -36.611 14.197 1.00 92.42 ? 238 ALA A CA 1 ATOM 1906 C C . ALA A 1 238 ? 28.388 -35.829 14.389 1.00 90.47 ? 238 ALA A C 1 ATOM 1907 O O . ALA A 1 238 ? 29.474 -36.400 14.278 1.00 91.15 ? 238 ALA A O 1 ATOM 1908 C CB . ALA A 1 238 ? 26.801 -37.419 15.448 1.00 94.37 ? 238 ALA A CB 1 ATOM 1909 N N . ILE A 1 239 ? 28.267 -34.530 14.651 1.00 89.13 ? 239 ILE A N 1 ATOM 1910 C CA . ILE A 1 239 ? 29.424 -33.740 15.080 1.00 87.32 ? 239 ILE A CA 1 ATOM 1911 C C . ILE A 1 239 ? 29.360 -33.523 16.599 1.00 89.53 ? 239 ILE A C 1 ATOM 1912 O O . ILE A 1 239 ? 28.285 -33.288 17.156 1.00 89.54 ? 239 ILE A O 1 ATOM 1913 C CB . ILE A 1 239 ? 29.556 -32.403 14.318 1.00 85.18 ? 239 ILE A CB 1 ATOM 1914 C CG1 . ILE A 1 239 ? 30.957 -31.812 14.528 1.00 84.42 ? 239 ILE A CG1 1 ATOM 1915 C CG2 . ILE A 1 239 ? 28.482 -31.409 14.733 1.00 85.24 ? 239 ILE A CG2 1 ATOM 1916 C CD1 . ILE A 1 239 ? 31.349 -30.772 13.502 1.00 82.40 ? 239 ILE A CD1 1 ATOM 1917 N N . ASN A 1 240 ? 30.519 -33.623 17.251 1.00 89.86 ? 240 ASN A N 1 ATOM 1918 C CA . ASN A 1 240 ? 30.618 -33.588 18.706 1.00 91.93 ? 240 ASN A CA 1 ATOM 1919 C C . ASN A 1 240 ? 31.604 -32.528 19.158 1.00 90.70 ? 240 ASN A C 1 ATOM 1920 O O . ASN A 1 240 ? 32.781 -32.585 18.801 1.00 90.35 ? 240 ASN A O 1 ATOM 1921 C CB . ASN A 1 240 ? 31.102 -34.931 19.228 1.00 93.99 ? 240 ASN A CB 1 ATOM 1922 C CG . ASN A 1 240 ? 30.123 -36.054 18.953 1.00 96.70 ? 240 ASN A CG 1 ATOM 1923 O OD1 . ASN A 1 240 ? 28.940 -35.956 19.287 1.00 96.67 ? 240 ASN A OD1 1 ATOM 1924 N ND2 . ASN A 1 240 ? 30.615 -37.139 18.345 1.00 97.71 ? 240 ASN A ND2 1 ATOM 1925 N N . PHE A 1 241 ? 31.128 -31.578 19.954 1.00 89.73 ? 241 PHE A N 1 ATOM 1926 C CA . PHE A 1 241 ? 31.979 -30.541 20.502 1.00 88.60 ? 241 PHE A CA 1 ATOM 1927 C C . PHE A 1 241 ? 32.201 -30.764 21.994 1.00 91.07 ? 241 PHE A C 1 ATOM 1928 O O . PHE A 1 241 ? 31.327 -31.266 22.702 1.00 92.08 ? 241 PHE A O 1 ATOM 1929 C CB . PHE A 1 241 ? 31.361 -29.170 20.258 1.00 87.56 ? 241 PHE A CB 1 ATOM 1930 C CG . PHE A 1 241 ? 31.330 -28.780 18.818 1.00 86.01 ? 241 PHE A CG 1 ATOM 1931 C CD1 . PHE A 1 241 ? 32.441 -28.200 18.222 1.00 84.92 ? 241 PHE A CD1 1 ATOM 1932 C CD2 . PHE A 1 241 ? 30.203 -29.007 18.048 1.00 86.44 ? 241 PHE A CD2 1 ATOM 1933 C CE1 . PHE A 1 241 ? 32.428 -27.845 16.885 1.00 84.18 ? 241 PHE A CE1 1 ATOM 1934 C CE2 . PHE A 1 241 ? 30.177 -28.651 16.705 1.00 85.14 ? 241 PHE A CE2 1 ATOM 1935 C CZ . PHE A 1 241 ? 31.293 -28.069 16.121 1.00 83.77 ? 241 PHE A CZ 1 ATOM 1936 N N . GLU A 1 242 ? 33.398 -30.421 22.447 1.00 91.43 ? 242 GLU A N 1 ATOM 1937 C CA . GLU A 1 242 ? 33.691 -30.308 23.861 1.00 94.16 ? 242 GLU A CA 1 ATOM 1938 C C . GLU A 1 242 ? 34.690 -29.165 24.026 1.00 93.65 ? 242 GLU A C 1 ATOM 1939 O O . GLU A 1 242 ? 35.716 -29.133 23.336 1.00 92.10 ? 242 GLU A O 1 ATOM 1940 C CB . GLU A 1 242 ? 34.247 -31.619 24.435 1.00 95.87 ? 242 GLU A CB 1 ATOM 1941 C CG . GLU A 1 242 ? 34.353 -31.614 25.955 1.00 99.17 ? 242 GLU A CG 1 ATOM 1942 C CD . GLU A 1 242 ? 35.091 -32.816 26.514 1.00 101.57 ? 242 GLU A CD 1 ATOM 1943 O OE1 . GLU A 1 242 ? 34.663 -33.964 26.271 1.00 103.18 ? 242 GLU A OE1 1 ATOM 1944 O OE2 . GLU A 1 242 ? 36.094 -32.615 27.225 1.00 102.95 ? 242 GLU A OE2 1 ATOM 1945 N N . SER A 1 243 ? 34.393 -28.224 24.920 1.00 94.86 ? 243 SER A N 1 ATOM 1946 C CA . SER A 1 243 ? 35.314 -27.116 25.156 1.00 94.87 ? 243 SER A CA 1 ATOM 1947 C C . SER A 1 243 ? 35.377 -26.619 26.593 1.00 98.01 ? 243 SER A C 1 ATOM 1948 O O . SER A 1 243 ? 34.496 -26.882 27.400 1.00 100.56 ? 243 SER A O 1 ATOM 1949 C CB . SER A 1 243 ? 34.989 -25.941 24.242 1.00 92.36 ? 243 SER A CB 1 ATOM 1950 O OG . SER A 1 243 ? 35.931 -24.898 24.428 1.00 91.33 ? 243 SER A OG 1 ATOM 1951 N N . ASN A 1 244 ? 36.451 -25.879 26.861 1.00 99.75 ? 244 ASN A N 1 ATOM 1952 C CA . ASN A 1 244 ? 36.755 -25.256 28.151 1.00 102.37 ? 244 ASN A CA 1 ATOM 1953 C C . ASN A 1 244 ? 36.648 -23.736 28.163 1.00 101.50 ? 244 ASN A C 1 ATOM 1954 O O . ASN A 1 244 ? 36.695 -23.114 29.223 1.00 102.80 ? 244 ASN A O 1 ATOM 1955 C CB . ASN A 1 244 ? 38.191 -25.601 28.521 1.00 103.33 ? 244 ASN A CB 1 ATOM 1956 C CG . ASN A 1 244 ? 38.274 -26.428 29.757 1.00 107.47 ? 244 ASN A CG 1 ATOM 1957 O OD1 . ASN A 1 244 ? 37.265 -26.938 30.238 1.00 109.43 ? 244 ASN A OD1 1 ATOM 1958 N ND2 . ASN A 1 244 ? 39.479 -26.560 30.297 1.00 109.77 ? 244 ASN A ND2 1 ATOM 1959 N N . GLY A 1 245 ? 36.502 -23.164 26.974 1.00 99.03 ? 245 GLY A N 1 ATOM 1960 C CA . GLY A 1 245 ? 36.646 -21.736 26.737 1.00 98.56 ? 245 GLY A CA 1 ATOM 1961 C C . GLY A 1 245 ? 37.221 -21.513 25.346 1.00 95.69 ? 245 GLY A C 1 ATOM 1962 O O . GLY A 1 245 ? 37.755 -22.443 24.726 1.00 94.37 ? 245 GLY A O 1 ATOM 1963 N N . ASN A 1 246 ? 37.113 -20.278 24.861 1.00 94.34 ? 246 ASN A N 1 ATOM 1964 C CA . ASN A 1 246 ? 37.696 -19.857 23.575 1.00 91.49 ? 246 ASN A CA 1 ATOM 1965 C C . ASN A 1 246 ? 36.957 -20.426 22.371 1.00 87.87 ? 246 ASN A C 1 ATOM 1966 O O . ASN A 1 246 ? 37.430 -20.318 21.252 1.00 86.83 ? 246 ASN A O 1 ATOM 1967 C CB . ASN A 1 246 ? 39.195 -20.201 23.469 1.00 91.08 ? 246 ASN A CB 1 ATOM 1968 C CG . ASN A 1 246 ? 40.016 -19.646 24.623 1.00 93.33 ? 246 ASN A CG 1 ATOM 1969 O OD1 . ASN A 1 246 ? 40.713 -18.646 24.474 1.00 93.98 ? 246 ASN A OD1 1 ATOM 1970 N ND2 . ASN A 1 246 ? 39.960 -20.308 25.765 1.00 94.80 ? 246 ASN A ND2 1 ATOM 1971 N N . PHE A 1 247 ? 35.779 -20.990 22.608 1.00 88.23 ? 247 PHE A N 1 ATOM 1972 C CA . PHE A 1 247 ? 35.015 -21.687 21.584 1.00 85.96 ? 247 PHE A CA 1 ATOM 1973 C C . PHE A 1 247 ? 34.069 -20.723 20.890 1.00 85.16 ? 247 PHE A C 1 ATOM 1974 O O . PHE A 1 247 ? 33.346 -19.972 21.538 1.00 86.45 ? 247 PHE A O 1 ATOM 1975 C CB . PHE A 1 247 ? 34.251 -22.839 22.243 1.00 87.45 ? 247 PHE A CB 1 ATOM 1976 C CG . PHE A 1 247 ? 33.422 -23.668 21.304 1.00 86.99 ? 247 PHE A CG 1 ATOM 1977 C CD1 . PHE A 1 247 ? 33.926 -24.113 20.094 1.00 85.03 ? 247 PHE A CD1 1 ATOM 1978 C CD2 . PHE A 1 247 ? 32.139 -24.056 21.668 1.00 89.29 ? 247 PHE A CD2 1 ATOM 1979 C CE1 . PHE A 1 247 ? 33.159 -24.893 19.248 1.00 84.87 ? 247 PHE A CE1 1 ATOM 1980 C CE2 . PHE A 1 247 ? 31.369 -24.844 20.829 1.00 88.25 ? 247 PHE A CE2 1 ATOM 1981 C CZ . PHE A 1 247 ? 31.878 -25.260 19.616 1.00 86.45 ? 247 PHE A CZ 1 ATOM 1982 N N . ILE A 1 248 ? 34.111 -20.716 19.565 1.00 83.25 ? 248 ILE A N 1 ATOM 1983 C CA . ILE A 1 248 ? 33.161 -19.955 18.785 1.00 82.33 ? 248 ILE A CA 1 ATOM 1984 C C . ILE A 1 248 ? 32.234 -21.005 18.215 1.00 82.27 ? 248 ILE A C 1 ATOM 1985 O O . ILE A 1 248 ? 32.590 -21.734 17.295 1.00 80.97 ? 248 ILE A O 1 ATOM 1986 C CB . ILE A 1 248 ? 33.851 -19.135 17.688 1.00 80.86 ? 248 ILE A CB 1 ATOM 1987 C CG1 . ILE A 1 248 ? 35.103 -18.444 18.227 1.00 80.98 ? 248 ILE A CG1 1 ATOM 1988 C CG2 . ILE A 1 248 ? 32.894 -18.099 17.129 1.00 81.35 ? 248 ILE A CG2 1 ATOM 1989 C CD1 . ILE A 1 248 ? 34.862 -17.581 19.445 1.00 83.88 ? 248 ILE A CD1 1 ATOM 1990 N N . ALA A 1 249 ? 31.058 -21.124 18.811 1.00 84.79 ? 249 ALA A N 1 ATOM 1991 C CA . ALA A 1 249 ? 30.190 -22.260 18.532 1.00 86.11 ? 249 ALA A CA 1 ATOM 1992 C C . ALA A 1 249 ? 29.344 -22.022 17.288 1.00 85.32 ? 249 ALA A C 1 ATOM 1993 O O . ALA A 1 249 ? 28.958 -20.893 17.016 1.00 85.25 ? 249 ALA A O 1 ATOM 1994 C CB . ALA A 1 249 ? 29.291 -22.535 19.723 1.00 88.83 ? 249 ALA A CB 1 ATOM 1995 N N . PRO A 1 250 ? 29.060 -23.084 16.523 1.00 85.61 ? 250 PRO A N 1 ATOM 1996 C CA . PRO A 1 250 ? 28.122 -22.897 15.418 1.00 85.71 ? 250 PRO A CA 1 ATOM 1997 C C . PRO A 1 250 ? 26.729 -22.532 15.918 1.00 87.97 ? 250 PRO A C 1 ATOM 1998 O O . PRO A 1 250 ? 26.296 -23.067 16.934 1.00 91.37 ? 250 PRO A O 1 ATOM 1999 C CB . PRO A 1 250 ? 28.083 -24.270 14.729 1.00 84.64 ? 250 PRO A CB 1 ATOM 2000 C CG . PRO A 1 250 ? 28.846 -25.215 15.595 1.00 84.63 ? 250 PRO A CG 1 ATOM 2001 C CD . PRO A 1 250 ? 29.719 -24.403 16.493 1.00 85.03 ? 250 PRO A CD 1 ATOM 2002 N N . GLU A 1 251 ? 26.056 -21.609 15.236 1.00 87.94 ? 251 GLU A N 1 ATOM 2003 C CA . GLU A 1 251 ? 24.605 -21.474 15.359 1.00 90.05 ? 251 GLU A CA 1 ATOM 2004 C C . GLU A 1 251 ? 23.955 -21.997 14.087 1.00 89.41 ? 251 GLU A C 1 ATOM 2005 O O . GLU A 1 251 ? 23.080 -22.872 14.134 1.00 89.56 ? 251 GLU A O 1 ATOM 2006 C CB . GLU A 1 251 ? 24.180 -20.023 15.604 1.00 92.33 ? 251 GLU A CB 1 ATOM 2007 C CG . GLU A 1 251 ? 22.758 -19.904 16.158 1.00 95.41 ? 251 GLU A CG 1 ATOM 2008 C CD . GLU A 1 251 ? 22.263 -18.474 16.262 1.00 97.65 ? 251 GLU A CD 1 ATOM 2009 O OE1 . GLU A 1 251 ? 23.074 -17.532 16.066 1.00 98.18 ? 251 GLU A OE1 1 ATOM 2010 O OE2 . GLU A 1 251 ? 21.059 -18.296 16.551 1.00 99.10 ? 251 GLU A OE2 1 ATOM 2011 N N . TYR A 1 252 ? 24.405 -21.452 12.956 1.00 87.57 ? 252 TYR A N 1 ATOM 2012 C CA . TYR A 1 252 ? 23.909 -21.834 11.646 1.00 87.21 ? 252 TYR A CA 1 ATOM 2013 C C . TYR A 1 252 ? 24.974 -22.572 10.831 1.00 85.33 ? 252 TYR A C 1 ATOM 2014 O O . TYR A 1 252 ? 26.151 -22.220 10.843 1.00 81.94 ? 252 TYR A O 1 ATOM 2015 C CB . TYR A 1 252 ? 23.449 -20.599 10.870 1.00 87.58 ? 252 TYR A CB 1 ATOM 2016 C CG . TYR A 1 252 ? 22.343 -19.820 11.535 1.00 90.38 ? 252 TYR A CG 1 ATOM 2017 C CD1 . TYR A 1 252 ? 21.011 -20.197 11.382 1.00 92.55 ? 252 TYR A CD1 1 ATOM 2018 C CD2 . TYR A 1 252 ? 22.624 -18.700 12.317 1.00 90.68 ? 252 TYR A CD2 1 ATOM 2019 C CE1 . TYR A 1 252 ? 19.992 -19.483 11.991 1.00 94.10 ? 252 TYR A CE1 1 ATOM 2020 C CE2 . TYR A 1 252 ? 21.610 -17.979 12.926 1.00 92.51 ? 252 TYR A CE2 1 ATOM 2021 C CZ . TYR A 1 252 ? 20.293 -18.374 12.759 1.00 94.61 ? 252 TYR A CZ 1 ATOM 2022 O OH . TYR A 1 252 ? 19.271 -17.665 13.365 1.00 96.63 ? 252 TYR A OH 1 ATOM 2023 N N . ALA A 1 253 ? 24.531 -23.604 10.125 1.00 86.20 ? 253 ALA A N 1 ATOM 2024 C CA . ALA A 1 253 ? 25.351 -24.308 9.157 1.00 85.21 ? 253 ALA A CA 1 ATOM 2025 C C . ALA A 1 253 ? 24.595 -24.318 7.817 1.00 85.80 ? 253 ALA A C 1 ATOM 2026 O O . ALA A 1 253 ? 23.380 -24.089 7.779 1.00 87.28 ? 253 ALA A O 1 ATOM 2027 C CB . ALA A 1 253 ? 25.621 -25.724 9.651 1.00 85.87 ? 253 ALA A CB 1 ATOM 2028 N N . TYR A 1 254 ? 25.308 -24.574 6.726 1.00 84.77 ? 254 TYR A N 1 ATOM 2029 C CA . TYR A 1 254 ? 24.706 -24.511 5.396 1.00 84.49 ? 254 TYR A CA 1 ATOM 2030 C C . TYR A 1 254 ? 24.426 -25.891 4.825 1.00 85.05 ? 254 TYR A C 1 ATOM 2031 O O . TYR A 1 254 ? 25.292 -26.763 4.801 1.00 83.65 ? 254 TYR A O 1 ATOM 2032 C CB . TYR A 1 254 ? 25.610 -23.763 4.442 1.00 83.28 ? 254 TYR A CB 1 ATOM 2033 C CG . TYR A 1 254 ? 25.777 -22.302 4.755 1.00 82.76 ? 254 TYR A CG 1 ATOM 2034 C CD1 . TYR A 1 254 ? 24.926 -21.350 4.198 1.00 84.04 ? 254 TYR A CD1 1 ATOM 2035 C CD2 . TYR A 1 254 ? 26.811 -21.866 5.568 1.00 82.54 ? 254 TYR A CD2 1 ATOM 2036 C CE1 . TYR A 1 254 ? 25.087 -20.002 4.457 1.00 84.76 ? 254 TYR A CE1 1 ATOM 2037 C CE2 . TYR A 1 254 ? 26.988 -20.521 5.838 1.00 83.48 ? 254 TYR A CE2 1 ATOM 2038 C CZ . TYR A 1 254 ? 26.119 -19.589 5.280 1.00 84.99 ? 254 TYR A CZ 1 ATOM 2039 O OH . TYR A 1 254 ? 26.278 -18.246 5.542 1.00 87.25 ? 254 TYR A OH 1 ATOM 2040 N N . LYS A 1 255 ? 23.203 -26.079 4.354 1.00 87.13 ? 255 LYS A N 1 ATOM 2041 C CA . LYS A 1 255 ? 22.812 -27.325 3.723 1.00 88.06 ? 255 LYS A CA 1 ATOM 2042 C C . LYS A 1 255 ? 23.181 -27.218 2.245 1.00 86.99 ? 255 LYS A C 1 ATOM 2043 O O . LYS A 1 255 ? 22.949 -26.189 1.610 1.00 85.91 ? 255 LYS A O 1 ATOM 2044 C CB . LYS A 1 255 ? 21.311 -27.567 3.924 1.00 90.77 ? 255 LYS A CB 1 ATOM 2045 C CG . LYS A 1 255 ? 20.980 -28.863 4.640 1.00 92.08 ? 255 LYS A CG 1 ATOM 2046 C CD . LYS A 1 255 ? 19.591 -28.838 5.257 1.00 94.12 ? 255 LYS A CD 1 ATOM 2047 C CE . LYS A 1 255 ? 18.482 -28.800 4.225 1.00 96.10 ? 255 LYS A CE 1 ATOM 2048 N NZ . LYS A 1 255 ? 17.210 -29.252 4.854 1.00 99.88 ? 255 LYS A NZ 1 ATOM 2049 N N . ILE A 1 256 ? 23.788 -28.275 1.718 1.00 86.89 ? 256 ILE A N 1 ATOM 2050 C CA . ILE A 1 256 ? 24.199 -28.323 0.315 1.00 86.66 ? 256 ILE A CA 1 ATOM 2051 C C . ILE A 1 256 ? 23.106 -28.985 -0.516 1.00 87.52 ? 256 ILE A C 1 ATOM 2052 O O . ILE A 1 256 ? 23.091 -30.205 -0.687 1.00 86.80 ? 256 ILE A O 1 ATOM 2053 C CB . ILE A 1 256 ? 25.530 -29.090 0.147 1.00 85.55 ? 256 ILE A CB 1 ATOM 2054 C CG1 . ILE A 1 256 ? 26.598 -28.471 1.057 1.00 83.81 ? 256 ILE A CG1 1 ATOM 2055 C CG2 . ILE A 1 256 ? 25.966 -29.086 -1.315 1.00 85.86 ? 256 ILE A CG2 1 ATOM 2056 C CD1 . ILE A 1 256 ? 28.003 -29.009 0.866 1.00 82.82 ? 256 ILE A CD1 1 ATOM 2057 N N . VAL A 1 257 ? 22.204 -28.171 -1.047 1.00 89.03 ? 257 VAL A N 1 ATOM 2058 C CA . VAL A 1 257 ? 21.035 -28.709 -1.743 1.00 93.13 ? 257 VAL A CA 1 ATOM 2059 C C . VAL A 1 257 ? 21.307 -29.020 -3.208 1.00 95.17 ? 257 VAL A C 1 ATOM 2060 O O . VAL A 1 257 ? 20.873 -30.065 -3.719 1.00 98.04 ? 257 VAL A O 1 ATOM 2061 C CB . VAL A 1 257 ? 19.784 -27.809 -1.601 1.00 95.11 ? 257 VAL A CB 1 ATOM 2062 C CG1 . VAL A 1 257 ? 19.336 -27.780 -0.153 1.00 95.86 ? 257 VAL A CG1 1 ATOM 2063 C CG2 . VAL A 1 257 ? 20.020 -26.392 -2.104 1.00 94.35 ? 257 VAL A CG2 1 ATOM 2064 N N . LYS A 1 258 ? 22.029 -28.127 -3.880 1.00 94.54 ? 258 LYS A N 1 ATOM 2065 C CA . LYS A 1 258 ? 22.330 -28.318 -5.296 1.00 95.56 ? 258 LYS A CA 1 ATOM 2066 C C . LYS A 1 258 ? 23.829 -28.320 -5.576 1.00 93.68 ? 258 LYS A C 1 ATOM 2067 O O . LYS A 1 258 ? 24.515 -27.329 -5.322 1.00 91.38 ? 258 LYS A O 1 ATOM 2068 C CB . LYS A 1 258 ? 21.642 -27.249 -6.135 1.00 96.55 ? 258 LYS A CB 1 ATOM 2069 C CG . LYS A 1 258 ? 21.600 -27.617 -7.600 1.00 99.41 ? 258 LYS A CG 1 ATOM 2070 C CD . LYS A 1 258 ? 20.725 -26.675 -8.398 1.00 102.21 ? 258 LYS A CD 1 ATOM 2071 C CE . LYS A 1 258 ? 20.802 -27.027 -9.873 1.00 104.74 ? 258 LYS A CE 1 ATOM 2072 N NZ . LYS A 1 258 ? 19.721 -26.377 -10.657 1.00 108.05 ? 258 LYS A NZ 1 ATOM 2073 N N . LYS A 1 259 ? 24.317 -29.447 -6.092 1.00 94.77 ? 259 LYS A N 1 ATOM 2074 C CA . LYS A 1 259 ? 25.684 -29.571 -6.578 1.00 94.38 ? 259 LYS A CA 1 ATOM 2075 C C . LYS A 1 259 ? 25.698 -29.466 -8.099 1.00 96.16 ? 259 LYS A C 1 ATOM 2076 O O . LYS A 1 259 ? 24.865 -30.063 -8.770 1.00 98.93 ? 259 LYS A O 1 ATOM 2077 C CB . LYS A 1 259 ? 26.288 -30.911 -6.144 1.00 95.07 ? 259 LYS A CB 1 ATOM 2078 C CG . LYS A 1 259 ? 26.892 -30.882 -4.754 1.00 94.96 ? 259 LYS A CG 1 ATOM 2079 C CD . LYS A 1 259 ? 27.416 -32.243 -4.306 1.00 96.58 ? 259 LYS A CD 1 ATOM 2080 C CE . LYS A 1 259 ? 27.724 -32.233 -2.810 1.00 97.39 ? 259 LYS A CE 1 ATOM 2081 N NZ . LYS A 1 259 ? 27.580 -33.563 -2.158 1.00 99.01 ? 259 LYS A NZ 1 ATOM 2082 N N . GLY A 1 260 ? 26.646 -28.717 -8.650 1.00 95.73 ? 260 GLY A N 1 ATOM 2083 C CA . GLY A 1 260 ? 26.793 -28.650 -10.107 1.00 97.08 ? 260 GLY A CA 1 ATOM 2084 C C . GLY A 1 260 ? 27.913 -27.749 -10.592 1.00 95.37 ? 260 GLY A C 1 ATOM 2085 O O . GLY A 1 260 ? 28.791 -27.365 -9.824 1.00 94.51 ? 260 GLY A O 1 ATOM 2086 N N . ASP A 1 261 ? 27.876 -27.418 -11.876 1.00 96.42 ? 261 ASP A N 1 ATOM 2087 C CA . ASP A 1 261 ? 28.885 -26.563 -12.479 1.00 95.51 ? 261 ASP A CA 1 ATOM 2088 C C . ASP A 1 261 ? 28.746 -25.139 -11.985 1.00 91.91 ? 261 ASP A C 1 ATOM 2089 O O . ASP A 1 261 ? 27.696 -24.526 -12.125 1.00 92.87 ? 261 ASP A O 1 ATOM 2090 C CB . ASP A 1 261 ? 28.782 -26.601 -14.012 1.00 98.80 ? 261 ASP A CB 1 ATOM 2091 C CG . ASP A 1 261 ? 29.299 -27.900 -14.591 1.00 102.05 ? 261 ASP A CG 1 ATOM 2092 O OD1 . ASP A 1 261 ? 29.993 -28.622 -13.840 1.00 102.04 ? 261 ASP A OD1 1 ATOM 2093 O OD2 . ASP A 1 261 ? 29.021 -28.201 -15.781 1.00 104.77 ? 261 ASP A OD2 1 ATOM 2094 N N . SER A 1 262 ? 29.820 -24.626 -11.409 1.00 88.68 ? 262 SER A N 1 ATOM 2095 C CA . SER A 1 262 ? 29.868 -23.255 -10.935 1.00 87.40 ? 262 SER A CA 1 ATOM 2096 C C . SER A 1 262 ? 31.323 -22.806 -10.978 1.00 85.93 ? 262 SER A C 1 ATOM 2097 O O . SER A 1 262 ? 32.203 -23.575 -11.384 1.00 87.08 ? 262 SER A O 1 ATOM 2098 C CB . SER A 1 262 ? 29.292 -23.157 -9.523 1.00 85.74 ? 262 SER A CB 1 ATOM 2099 O OG . SER A 1 262 ? 29.534 -21.887 -8.939 1.00 85.45 ? 262 SER A OG 1 ATOM 2100 N N . THR A 1 263 ? 31.570 -21.557 -10.602 1.00 78.45 ? 263 THR A N 1 ATOM 2101 C CA . THR A 1 263 ? 32.917 -21.018 -10.597 1.00 74.93 ? 263 THR A CA 1 ATOM 2102 C C . THR A 1 263 ? 32.941 -19.741 -9.787 1.00 72.77 ? 263 THR A C 1 ATOM 2103 O O . THR A 1 263 ? 31.954 -19.009 -9.740 1.00 72.11 ? 263 THR A O 1 ATOM 2104 C CB . THR A 1 263 ? 33.449 -20.747 -12.034 1.00 72.54 ? 263 THR A CB 1 ATOM 2105 O OG1 . THR A 1 263 ? 34.854 -20.535 -11.991 1.00 70.95 ? 263 THR A OG1 1 ATOM 2106 C CG2 . THR A 1 263 ? 32.820 -19.514 -12.665 1.00 71.43 ? 263 THR A CG2 1 ATOM 2107 N N . ILE A 1 264 ? 34.071 -19.492 -9.134 1.00 72.18 ? 264 ILE A N 1 ATOM 2108 C CA . ILE A 1 264 ? 34.309 -18.221 -8.475 1.00 69.96 ? 264 ILE A CA 1 ATOM 2109 C C . ILE A 1 264 ? 35.128 -17.391 -9.429 1.00 68.38 ? 264 ILE A C 1 ATOM 2110 O O . ILE A 1 264 ? 36.275 -17.718 -9.733 1.00 69.20 ? 264 ILE A O 1 ATOM 2111 C CB . ILE A 1 264 ? 35.043 -18.384 -7.150 1.00 70.12 ? 264 ILE A CB 1 ATOM 2112 C CG1 . ILE A 1 264 ? 34.269 -19.359 -6.268 1.00 72.89 ? 264 ILE A CG1 1 ATOM 2113 C CG2 . ILE A 1 264 ? 35.186 -17.031 -6.471 1.00 69.25 ? 264 ILE A CG2 1 ATOM 2114 C CD1 . ILE A 1 264 ? 34.959 -19.693 -4.973 1.00 74.90 ? 264 ILE A CD1 1 ATOM 2115 N N . MET A 1 265 ? 34.521 -16.320 -9.902 1.00 67.50 ? 265 MET A N 1 ATOM 2116 C CA . MET A 1 265 ? 35.098 -15.477 -10.923 1.00 67.08 ? 265 MET A CA 1 ATOM 2117 C C . MET A 1 265 ? 35.590 -14.211 -10.234 1.00 68.04 ? 265 MET A C 1 ATOM 2118 O O . MET A 1 265 ? 34.892 -13.651 -9.400 1.00 69.01 ? 265 MET A O 1 ATOM 2119 C CB . MET A 1 265 ? 34.003 -15.169 -11.928 1.00 67.02 ? 265 MET A CB 1 ATOM 2120 C CG . MET A 1 265 ? 34.417 -14.467 -13.188 1.00 66.46 ? 265 MET A CG 1 ATOM 2121 S SD . MET A 1 265 ? 32.940 -14.228 -14.191 1.00 67.79 ? 265 MET A SD 1 ATOM 2122 C CE . MET A 1 265 ? 32.693 -15.894 -14.814 1.00 67.22 ? 265 MET A CE 1 ATOM 2123 N N . LYS A 1 266 ? 36.810 -13.789 -10.541 1.00 70.15 ? 266 LYS A N 1 ATOM 2124 C CA . LYS A 1 266 ? 37.388 -12.610 -9.907 1.00 72.39 ? 266 LYS A CA 1 ATOM 2125 C C . LYS A 1 266 ? 37.239 -11.436 -10.865 1.00 72.59 ? 266 LYS A C 1 ATOM 2126 O O . LYS A 1 266 ? 37.734 -11.468 -12.000 1.00 71.90 ? 266 LYS A O 1 ATOM 2127 C CB . LYS A 1 266 ? 38.857 -12.840 -9.523 1.00 75.65 ? 266 LYS A CB 1 ATOM 2128 C CG . LYS A 1 266 ? 39.122 -14.099 -8.691 1.00 78.80 ? 266 LYS A CG 1 ATOM 2129 C CD . LYS A 1 266 ? 38.725 -13.961 -7.223 1.00 80.91 ? 266 LYS A CD 1 ATOM 2130 C CE . LYS A 1 266 ? 39.841 -13.343 -6.388 1.00 85.16 ? 266 LYS A CE 1 ATOM 2131 N NZ . LYS A 1 266 ? 39.333 -12.719 -5.113 1.00 89.46 ? 266 LYS A NZ 1 ATOM 2132 N N . SER A 1 267 ? 36.531 -10.411 -10.400 1.00 75.12 ? 267 SER A N 1 ATOM 2133 C CA . SER A 1 267 ? 36.168 -9.259 -11.215 1.00 76.82 ? 267 SER A CA 1 ATOM 2134 C C . SER A 1 267 ? 35.742 -8.095 -10.333 1.00 78.40 ? 267 SER A C 1 ATOM 2135 O O . SER A 1 267 ? 35.192 -8.292 -9.250 1.00 80.17 ? 267 SER A O 1 ATOM 2136 C CB . SER A 1 267 ? 35.017 -9.630 -12.148 1.00 78.38 ? 267 SER A CB 1 ATOM 2137 O OG . SER A 1 267 ? 34.508 -8.488 -12.814 1.00 82.27 ? 267 SER A OG 1 ATOM 2138 N N . GLU A 1 268 ? 35.991 -6.882 -10.809 1.00 79.42 ? 268 GLU A N 1 ATOM 2139 C CA . GLU A 1 268 ? 35.544 -5.680 -10.120 1.00 81.57 ? 268 GLU A CA 1 ATOM 2140 C C . GLU A 1 268 ? 34.157 -5.231 -10.577 1.00 83.29 ? 268 GLU A C 1 ATOM 2141 O O . GLU A 1 268 ? 33.553 -4.376 -9.943 1.00 89.39 ? 268 GLU A O 1 ATOM 2142 C CB . GLU A 1 268 ? 36.540 -4.547 -10.345 1.00 82.79 ? 268 GLU A CB 1 ATOM 2143 C CG . GLU A 1 268 ? 37.977 -4.893 -9.987 1.00 82.62 ? 268 GLU A CG 1 ATOM 2144 C CD . GLU A 1 268 ? 38.124 -5.458 -8.583 1.00 82.79 ? 268 GLU A CD 1 ATOM 2145 O OE1 . GLU A 1 268 ? 37.732 -4.771 -7.606 1.00 80.42 ? 268 GLU A OE1 1 ATOM 2146 O OE2 . GLU A 1 268 ? 38.635 -6.603 -8.471 1.00 81.58 ? 268 GLU A OE2 1 ATOM 2147 N N . LEU A 1 269 ? 33.645 -5.822 -11.652 1.00 82.76 ? 269 LEU A N 1 ATOM 2148 C CA . LEU A 1 269 ? 32.409 -5.358 -12.274 1.00 85.09 ? 269 LEU A CA 1 ATOM 2149 C C . LEU A 1 269 ? 31.195 -5.716 -11.436 1.00 87.13 ? 269 LEU A C 1 ATOM 2150 O O . LEU A 1 269 ? 31.210 -6.700 -10.706 1.00 84.02 ? 269 LEU A O 1 ATOM 2151 C CB . LEU A 1 269 ? 32.258 -5.956 -13.676 1.00 84.35 ? 269 LEU A CB 1 ATOM 2152 C CG . LEU A 1 269 ? 33.354 -5.610 -14.689 1.00 83.99 ? 269 LEU A CG 1 ATOM 2153 C CD1 . LEU A 1 269 ? 33.289 -6.516 -15.908 1.00 83.59 ? 269 LEU A CD1 1 ATOM 2154 C CD2 . LEU A 1 269 ? 33.252 -4.155 -15.113 1.00 87.69 ? 269 LEU A CD2 1 ATOM 2155 N N . GLU A 1 270 ? 30.156 -4.889 -11.541 1.00 93.85 ? 270 GLU A N 1 ATOM 2156 C CA . GLU A 1 270 ? 28.869 -5.141 -10.886 1.00 98.58 ? 270 GLU A CA 1 ATOM 2157 C C . GLU A 1 270 ? 27.904 -5.849 -11.862 1.00 95.94 ? 270 GLU A C 1 ATOM 2158 O O . GLU A 1 270 ? 28.289 -6.213 -12.971 1.00 94.77 ? 270 GLU A O 1 ATOM 2159 C CB . GLU A 1 270 ? 28.258 -3.822 -10.362 1.00 105.67 ? 270 GLU A CB 1 ATOM 2160 C CG . GLU A 1 270 ? 29.197 -2.933 -9.532 1.00 109.54 ? 270 GLU A CG 1 ATOM 2161 C CD . GLU A 1 270 ? 29.359 -3.366 -8.067 1.00 111.01 ? 270 GLU A CD 1 ATOM 2162 O OE1 . GLU A 1 270 ? 29.545 -4.576 -7.788 1.00 109.26 ? 270 GLU A OE1 1 ATOM 2163 O OE2 . GLU A 1 270 ? 29.310 -2.481 -7.182 1.00 112.54 ? 270 GLU A OE2 1 ATOM 2164 N N . TYR A 1 271 ? 26.660 -6.052 -11.435 1.00 95.78 ? 271 TYR A N 1 ATOM 2165 C CA . TYR A 1 271 ? 25.645 -6.719 -12.252 1.00 95.30 ? 271 TYR A CA 1 ATOM 2166 C C . TYR A 1 271 ? 25.214 -5.828 -13.413 1.00 98.31 ? 271 TYR A C 1 ATOM 2167 O O . TYR A 1 271 ? 25.029 -4.624 -13.240 1.00 99.77 ? 271 TYR A O 1 ATOM 2168 C CB . TYR A 1 271 ? 24.440 -7.053 -11.377 1.00 96.86 ? 271 TYR A CB 1 ATOM 2169 C CG . TYR A 1 271 ? 23.354 -7.887 -12.023 1.00 96.76 ? 271 TYR A CG 1 ATOM 2170 C CD1 . TYR A 1 271 ? 23.613 -9.168 -12.490 1.00 92.46 ? 271 TYR A CD1 1 ATOM 2171 C CD2 . TYR A 1 271 ? 22.045 -7.409 -12.106 1.00 100.64 ? 271 TYR A CD2 1 ATOM 2172 C CE1 . TYR A 1 271 ? 22.612 -9.938 -13.051 1.00 94.19 ? 271 TYR A CE1 1 ATOM 2173 C CE2 . TYR A 1 271 ? 21.037 -8.173 -12.666 1.00 101.94 ? 271 TYR A CE2 1 ATOM 2174 C CZ . TYR A 1 271 ? 21.324 -9.436 -13.136 1.00 98.98 ? 271 TYR A CZ 1 ATOM 2175 O OH . TYR A 1 271 ? 20.316 -10.186 -13.681 1.00 100.17 ? 271 TYR A OH 1 ATOM 2176 N N . GLY A 1 272 ? 25.054 -6.423 -14.593 1.00 99.09 ? 272 GLY A N 1 ATOM 2177 C CA . GLY A 1 272 ? 24.719 -5.671 -15.803 1.00 102.34 ? 272 GLY A CA 1 ATOM 2178 C C . GLY A 1 272 ? 23.246 -5.617 -16.201 1.00 106.94 ? 272 GLY A C 1 ATOM 2179 O O . GLY A 1 272 ? 22.913 -4.911 -17.153 1.00 108.56 ? 272 GLY A O 1 ATOM 2180 N N . ASN A 1 273 ? 22.380 -6.355 -15.494 1.00 108.79 ? 273 ASN A N 1 ATOM 2181 C CA . ASN A 1 273 ? 20.948 -6.502 -15.852 1.00 114.60 ? 273 ASN A CA 1 ATOM 2182 C C . ASN A 1 273 ? 20.827 -7.057 -17.253 1.00 113.05 ? 273 ASN A C 1 ATOM 2183 O O . ASN A 1 273 ? 20.609 -6.322 -18.207 1.00 116.39 ? 273 ASN A O 1 ATOM 2184 C CB . ASN A 1 273 ? 20.202 -5.174 -15.741 1.00 119.65 ? 273 ASN A CB 1 ATOM 2185 C CG . ASN A 1 273 ? 20.219 -4.624 -14.338 1.00 123.09 ? 273 ASN A CG 1 ATOM 2186 O OD1 . ASN A 1 273 ? 20.919 -3.655 -14.057 1.00 125.26 ? 273 ASN A OD1 1 ATOM 2187 N ND2 . ASN A 1 273 ? 19.464 -5.253 -13.439 1.00 125.49 ? 273 ASN A ND2 1 ATOM 2188 N N . CYS A 1 274 ? 20.948 -8.370 -17.365 1.00 110.27 ? 274 CYS A N 1 ATOM 2189 C CA . CYS A 1 274 ? 21.699 -8.930 -18.472 1.00 106.83 ? 274 CYS A CA 1 ATOM 2190 C C . CYS A 1 274 ? 21.548 -10.437 -18.562 1.00 104.73 ? 274 CYS A C 1 ATOM 2191 O O . CYS A 1 274 ? 21.430 -11.094 -17.537 1.00 105.75 ? 274 CYS A O 1 ATOM 2192 C CB . CYS A 1 274 ? 23.151 -8.617 -18.138 1.00 104.71 ? 274 CYS A CB 1 ATOM 2193 S SG . CYS A 1 274 ? 24.293 -8.533 -19.493 1.00 105.05 ? 274 CYS A SG 1 ATOM 2194 N N . ASN A 1 275 ? 21.603 -10.998 -19.764 1.00 105.30 ? 275 ASN A N 1 ATOM 2195 C CA . ASN A 1 275 ? 21.565 -12.462 -19.927 1.00 108.43 ? 275 ASN A CA 1 ATOM 2196 C C . ASN A 1 275 ? 22.478 -12.938 -21.055 1.00 102.00 ? 275 ASN A C 1 ATOM 2197 O O . ASN A 1 275 ? 22.550 -12.302 -22.101 1.00 103.69 ? 275 ASN A O 1 ATOM 2198 C CB . ASN A 1 275 ? 20.120 -12.938 -20.166 1.00 120.63 ? 275 ASN A CB 1 ATOM 2199 C CG . ASN A 1 275 ? 20.001 -14.458 -20.216 1.00 122.92 ? 275 ASN A CG 1 ATOM 2200 O OD1 . ASN A 1 275 ? 20.320 -15.154 -19.253 1.00 122.62 ? 275 ASN A OD1 1 ATOM 2201 N ND2 . ASN A 1 275 ? 19.546 -14.978 -21.345 1.00 126.71 ? 275 ASN A ND2 1 ATOM 2202 N N . THR A 1 276 ? 23.172 -14.055 -20.842 1.00 95.51 ? 276 THR A N 1 ATOM 2203 C CA . THR A 1 276 ? 24.164 -14.559 -21.797 1.00 87.09 ? 276 THR A CA 1 ATOM 2204 C C . THR A 1 276 ? 24.223 -16.073 -21.708 1.00 84.99 ? 276 THR A C 1 ATOM 2205 O O . THR A 1 276 ? 23.680 -16.652 -20.792 1.00 86.32 ? 276 THR A O 1 ATOM 2206 C CB . THR A 1 276 ? 25.566 -13.979 -21.485 1.00 84.78 ? 276 THR A CB 1 ATOM 2207 O OG1 . THR A 1 276 ? 26.502 -14.320 -22.517 1.00 81.19 ? 276 THR A OG1 1 ATOM 2208 C CG2 . THR A 1 276 ? 26.107 -14.496 -20.121 1.00 84.42 ? 276 THR A CG2 1 ATOM 2209 N N . LYS A 1 277 ? 24.900 -16.708 -22.653 1.00 84.18 ? 277 LYS A N 1 ATOM 2210 C CA . LYS A 1 277 ? 25.184 -18.145 -22.586 1.00 85.77 ? 277 LYS A CA 1 ATOM 2211 C C . LYS A 1 277 ? 26.647 -18.424 -22.288 1.00 79.63 ? 277 LYS A C 1 ATOM 2212 O O . LYS A 1 277 ? 27.047 -19.578 -22.137 1.00 79.12 ? 277 LYS A O 1 ATOM 2213 C CB . LYS A 1 277 ? 24.815 -18.825 -23.910 1.00 91.55 ? 277 LYS A CB 1 ATOM 2214 C CG . LYS A 1 277 ? 23.331 -19.155 -24.045 1.00 100.65 ? 277 LYS A CG 1 ATOM 2215 C CD . LYS A 1 277 ? 23.077 -20.171 -25.164 1.00 104.35 ? 277 LYS A CD 1 ATOM 2216 C CE . LYS A 1 277 ? 21.598 -20.530 -25.287 1.00 110.64 ? 277 LYS A CE 1 ATOM 2217 N NZ . LYS A 1 277 ? 20.989 -20.905 -23.974 1.00 114.51 ? 277 LYS A NZ 1 ATOM 2218 N N . CYS A 1 278 ? 27.446 -17.365 -22.232 1.00 75.93 ? 278 CYS A N 1 ATOM 2219 C CA . CYS A 1 278 ? 28.882 -17.487 -22.043 1.00 72.58 ? 278 CYS A CA 1 ATOM 2220 C C . CYS A 1 278 ? 29.375 -16.244 -21.330 1.00 69.56 ? 278 CYS A C 1 ATOM 2221 O O . CYS A 1 278 ? 29.221 -15.129 -21.844 1.00 70.14 ? 278 CYS A O 1 ATOM 2222 C CB . CYS A 1 278 ? 29.580 -17.623 -23.392 1.00 71.84 ? 278 CYS A CB 1 ATOM 2223 S SG . CYS A 1 278 ? 31.393 -17.646 -23.306 1.00 72.08 ? 278 CYS A SG 1 ATOM 2224 N N . GLN A 1 279 ? 29.950 -16.416 -20.145 1.00 66.80 ? 279 GLN A N 1 ATOM 2225 C CA . GLN A 1 279 ? 30.377 -15.258 -19.367 1.00 66.75 ? 279 GLN A CA 1 ATOM 2226 C C . GLN A 1 279 ? 31.862 -15.275 -19.111 1.00 64.10 ? 279 GLN A C 1 ATOM 2227 O O . GLN A 1 279 ? 32.431 -16.333 -18.868 1.00 62.57 ? 279 GLN A O 1 ATOM 2228 C CB . GLN A 1 279 ? 29.638 -15.192 -18.030 1.00 68.81 ? 279 GLN A CB 1 ATOM 2229 C CG . GLN A 1 279 ? 29.941 -13.936 -17.226 1.00 69.00 ? 279 GLN A CG 1 ATOM 2230 C CD . GLN A 1 279 ? 29.282 -12.700 -17.801 1.00 71.42 ? 279 GLN A CD 1 ATOM 2231 O OE1 . GLN A 1 279 ? 28.078 -12.685 -18.027 1.00 75.14 ? 279 GLN A OE1 1 ATOM 2232 N NE2 . GLN A 1 279 ? 30.062 -11.656 -18.033 1.00 71.12 ? 279 GLN A NE2 1 ATOM 2233 N N . THR A 1 280 ? 32.465 -14.089 -19.147 1.00 63.82 ? 280 THR A N 1 ATOM 2234 C CA . THR A 1 280 ? 33.848 -13.893 -18.747 1.00 63.30 ? 280 THR A CA 1 ATOM 2235 C C . THR A 1 280 ? 33.940 -12.803 -17.682 1.00 65.84 ? 280 THR A C 1 ATOM 2236 O O . THR A 1 280 ? 33.018 -11.997 -17.532 1.00 67.71 ? 280 THR A O 1 ATOM 2237 C CB . THR A 1 280 ? 34.733 -13.473 -19.937 1.00 62.72 ? 280 THR A CB 1 ATOM 2238 O OG1 . THR A 1 280 ? 34.755 -12.043 -20.057 1.00 62.21 ? 280 THR A OG1 1 ATOM 2239 C CG2 . THR A 1 280 ? 34.251 -14.103 -21.236 1.00 62.26 ? 280 THR A CG2 1 ATOM 2240 N N . PRO A 1 281 ? 35.073 -12.744 -16.961 1.00 67.63 ? 281 PRO A N 1 ATOM 2241 C CA . PRO A 1 281 ? 35.293 -11.693 -15.950 1.00 69.05 ? 281 PRO A CA 1 ATOM 2242 C C . PRO A 1 281 ? 35.308 -10.265 -16.491 1.00 71.51 ? 281 PRO A C 1 ATOM 2243 O O . PRO A 1 281 ? 35.214 -9.310 -15.708 1.00 73.86 ? 281 PRO A O 1 ATOM 2244 C CB . PRO A 1 281 ? 36.668 -12.030 -15.383 1.00 69.09 ? 281 PRO A CB 1 ATOM 2245 C CG . PRO A 1 281 ? 36.888 -13.471 -15.696 1.00 67.77 ? 281 PRO A CG 1 ATOM 2246 C CD . PRO A 1 281 ? 36.155 -13.747 -16.964 1.00 66.13 ? 281 PRO A CD 1 ATOM 2247 N N . MET A 1 282 ? 35.439 -10.112 -17.806 1.00 73.26 ? 282 MET A N 1 ATOM 2248 C CA . MET A 1 282 ? 35.414 -8.791 -18.437 1.00 75.63 ? 282 MET A CA 1 ATOM 2249 C C . MET A 1 282 ? 34.087 -8.458 -19.102 1.00 74.63 ? 282 MET A C 1 ATOM 2250 O O . MET A 1 282 ? 33.818 -7.289 -19.403 1.00 76.40 ? 282 MET A O 1 ATOM 2251 C CB . MET A 1 282 ? 36.490 -8.711 -19.494 1.00 78.57 ? 282 MET A CB 1 ATOM 2252 C CG . MET A 1 282 ? 37.900 -8.796 -18.950 1.00 82.18 ? 282 MET A CG 1 ATOM 2253 S SD . MET A 1 282 ? 38.991 -9.012 -20.356 1.00 89.06 ? 282 MET A SD 1 ATOM 2254 C CE . MET A 1 282 ? 38.604 -7.556 -21.343 1.00 89.29 ? 282 MET A CE 1 ATOM 2255 N N . GLY A 1 283 ? 33.263 -9.475 -19.340 1.00 71.02 ? 283 GLY A N 1 ATOM 2256 C CA . GLY A 1 283 ? 31.991 -9.265 -20.024 1.00 71.51 ? 283 GLY A CA 1 ATOM 2257 C C . GLY A 1 283 ? 31.466 -10.549 -20.626 1.00 69.32 ? 283 GLY A C 1 ATOM 2258 O O . GLY A 1 283 ? 32.155 -11.560 -20.644 1.00 67.43 ? 283 GLY A O 1 ATOM 2259 N N . ALA A 1 284 ? 30.242 -10.504 -21.126 1.00 70.53 ? 284 ALA A N 1 ATOM 2260 C CA . ALA A 1 284 ? 29.607 -11.679 -21.696 1.00 70.55 ? 284 ALA A CA 1 ATOM 2261 C C . ALA A 1 284 ? 29.878 -11.749 -23.198 1.00 70.61 ? 284 ALA A C 1 ATOM 2262 O O . ALA A 1 284 ? 30.196 -10.742 -23.846 1.00 69.35 ? 284 ALA A O 1 ATOM 2263 C CB . ALA A 1 284 ? 28.112 -11.636 -21.437 1.00 74.36 ? 284 ALA A CB 1 ATOM 2264 N N . ILE A 1 285 ? 29.703 -12.948 -23.741 1.00 70.00 ? 285 ILE A N 1 ATOM 2265 C CA . ILE A 1 285 ? 29.991 -13.239 -25.142 1.00 70.14 ? 285 ILE A CA 1 ATOM 2266 C C . ILE A 1 285 ? 28.744 -13.790 -25.822 1.00 73.44 ? 285 ILE A C 1 ATOM 2267 O O . ILE A 1 285 ? 28.087 -14.683 -25.289 1.00 74.17 ? 285 ILE A O 1 ATOM 2268 C CB . ILE A 1 285 ? 31.139 -14.276 -25.251 1.00 65.94 ? 285 ILE A CB 1 ATOM 2269 C CG1 . ILE A 1 285 ? 32.485 -13.570 -25.198 1.00 63.26 ? 285 ILE A CG1 1 ATOM 2270 C CG2 . ILE A 1 285 ? 31.055 -15.090 -26.526 1.00 64.24 ? 285 ILE A CG2 1 ATOM 2271 C CD1 . ILE A 1 285 ? 33.626 -14.516 -24.908 1.00 61.72 ? 285 ILE A CD1 1 ATOM 2272 N N . ASN A 1 286 ? 28.429 -13.247 -26.995 1.00 76.61 ? 286 ASN A N 1 ATOM 2273 C CA . ASN A 1 286 ? 27.375 -13.791 -27.848 1.00 80.87 ? 286 ASN A CA 1 ATOM 2274 C C . ASN A 1 286 ? 27.884 -13.903 -29.267 1.00 79.38 ? 286 ASN A C 1 ATOM 2275 O O . ASN A 1 286 ? 27.899 -12.922 -30.003 1.00 78.53 ? 286 ASN A O 1 ATOM 2276 C CB . ASN A 1 286 ? 26.130 -12.897 -27.822 1.00 86.61 ? 286 ASN A CB 1 ATOM 2277 C CG . ASN A 1 286 ? 24.927 -13.558 -28.472 1.00 92.54 ? 286 ASN A CG 1 ATOM 2278 O OD1 . ASN A 1 286 ? 24.888 -14.786 -28.630 1.00 93.87 ? 286 ASN A OD1 1 ATOM 2279 N ND2 . ASN A 1 286 ? 23.933 -12.750 -28.850 1.00 96.01 ? 286 ASN A ND2 1 ATOM 2280 N N . SER A 1 287 ? 28.330 -15.093 -29.646 1.00 78.73 ? 287 SER A N 1 ATOM 2281 C CA . SER A 1 287 ? 28.739 -15.319 -31.026 1.00 79.63 ? 287 SER A CA 1 ATOM 2282 C C . SER A 1 287 ? 28.759 -16.794 -31.399 1.00 78.21 ? 287 SER A C 1 ATOM 2283 O O . SER A 1 287 ? 28.732 -17.666 -30.540 1.00 77.51 ? 287 SER A O 1 ATOM 2284 C CB . SER A 1 287 ? 30.104 -14.655 -31.316 1.00 78.61 ? 287 SER A CB 1 ATOM 2285 O OG . SER A 1 287 ? 31.196 -15.381 -30.779 1.00 76.02 ? 287 SER A OG 1 ATOM 2286 N N . SER A 1 288 ? 28.800 -17.052 -32.701 1.00 78.87 ? 288 SER A N 1 ATOM 2287 C CA . SER A 1 288 ? 28.921 -18.409 -33.230 1.00 78.89 ? 288 SER A CA 1 ATOM 2288 C C . SER A 1 288 ? 30.346 -18.729 -33.671 1.00 71.89 ? 288 SER A C 1 ATOM 2289 O O . SER A 1 288 ? 30.617 -19.833 -34.138 1.00 71.19 ? 288 SER A O 1 ATOM 2290 C CB . SER A 1 288 ? 27.959 -18.597 -34.400 1.00 85.27 ? 288 SER A CB 1 ATOM 2291 O OG . SER A 1 288 ? 26.620 -18.334 -33.987 1.00 93.53 ? 288 SER A OG 1 ATOM 2292 N N . MET A 1 289 ? 31.264 -17.786 -33.492 1.00 66.77 ? 289 MET A N 1 ATOM 2293 C CA . MET A 1 289 ? 32.663 -18.022 -33.828 1.00 64.39 ? 289 MET A CA 1 ATOM 2294 C C . MET A 1 289 ? 33.184 -19.195 -33.014 1.00 63.27 ? 289 MET A C 1 ATOM 2295 O O . MET A 1 289 ? 32.858 -19.321 -31.844 1.00 64.35 ? 289 MET A O 1 ATOM 2296 C CB . MET A 1 289 ? 33.537 -16.823 -33.489 1.00 65.78 ? 289 MET A CB 1 ATOM 2297 C CG . MET A 1 289 ? 33.157 -15.514 -34.137 1.00 68.79 ? 289 MET A CG 1 ATOM 2298 S SD . MET A 1 289 ? 33.463 -15.583 -35.889 1.00 70.41 ? 289 MET A SD 1 ATOM 2299 C CE . MET A 1 289 ? 33.641 -13.808 -36.157 1.00 67.68 ? 289 MET A CE 1 ATOM 2300 N N . PRO A 1 290 ? 34.013 -20.054 -33.623 1.00 60.64 ? 290 PRO A N 1 ATOM 2301 C CA . PRO A 1 290 ? 34.590 -21.144 -32.843 1.00 59.59 ? 290 PRO A CA 1 ATOM 2302 C C . PRO A 1 290 ? 35.657 -20.699 -31.846 1.00 58.36 ? 290 PRO A C 1 ATOM 2303 O O . PRO A 1 290 ? 36.020 -21.475 -30.976 1.00 60.53 ? 290 PRO A O 1 ATOM 2304 C CB . PRO A 1 290 ? 35.215 -22.034 -33.914 1.00 58.77 ? 290 PRO A CB 1 ATOM 2305 C CG . PRO A 1 290 ? 35.544 -21.093 -35.017 1.00 58.13 ? 290 PRO A CG 1 ATOM 2306 C CD . PRO A 1 290 ? 34.402 -20.124 -35.041 1.00 58.07 ? 290 PRO A CD 1 ATOM 2307 N N . PHE A 1 291 ? 36.159 -19.474 -31.972 1.00 56.74 ? 291 PHE A N 1 ATOM 2308 C CA . PHE A 1 291 ? 37.244 -18.984 -31.127 1.00 56.78 ? 291 PHE A CA 1 ATOM 2309 C C . PHE A 1 291 ? 36.927 -17.598 -30.611 1.00 55.96 ? 291 PHE A C 1 ATOM 2310 O O . PHE A 1 291 ? 36.170 -16.876 -31.240 1.00 55.47 ? 291 PHE A O 1 ATOM 2311 C CB . PHE A 1 291 ? 38.522 -18.815 -31.933 1.00 57.66 ? 291 PHE A CB 1 ATOM 2312 C CG . PHE A 1 291 ? 39.199 -20.088 -32.311 1.00 60.17 ? 291 PHE A CG 1 ATOM 2313 C CD1 . PHE A 1 291 ? 39.835 -20.858 -31.356 1.00 63.77 ? 291 PHE A CD1 1 ATOM 2314 C CD2 . PHE A 1 291 ? 39.264 -20.481 -33.634 1.00 62.10 ? 291 PHE A CD2 1 ATOM 2315 C CE1 . PHE A 1 291 ? 40.500 -22.015 -31.711 1.00 65.27 ? 291 PHE A CE1 1 ATOM 2316 C CE2 . PHE A 1 291 ? 39.925 -21.640 -33.998 1.00 62.98 ? 291 PHE A CE2 1 ATOM 2317 C CZ . PHE A 1 291 ? 40.541 -22.404 -33.036 1.00 64.43 ? 291 PHE A CZ 1 ATOM 2318 N N . HIS A 1 292 ? 37.561 -17.220 -29.500 1.00 55.08 ? 292 HIS A N 1 ATOM 2319 C CA . HIS A 1 292 ? 37.587 -15.826 -29.048 1.00 54.60 ? 292 HIS A CA 1 ATOM 2320 C C . HIS A 1 292 ? 38.901 -15.517 -28.340 1.00 54.16 ? 292 HIS A C 1 ATOM 2321 O O . HIS A 1 292 ? 39.677 -16.434 -28.032 1.00 54.11 ? 292 HIS A O 1 ATOM 2322 C CB . HIS A 1 292 ? 36.432 -15.551 -28.101 1.00 56.89 ? 292 HIS A CB 1 ATOM 2323 C CG . HIS A 1 292 ? 36.597 -16.182 -26.756 1.00 57.65 ? 292 HIS A CG 1 ATOM 2324 N ND1 . HIS A 1 292 ? 37.175 -15.522 -25.701 1.00 57.79 ? 292 HIS A ND1 1 ATOM 2325 C CD2 . HIS A 1 292 ? 36.278 -17.415 -26.299 1.00 59.37 ? 292 HIS A CD2 1 ATOM 2326 C CE1 . HIS A 1 292 ? 37.202 -16.316 -24.649 1.00 59.62 ? 292 HIS A CE1 1 ATOM 2327 N NE2 . HIS A 1 292 ? 36.677 -17.479 -24.988 1.00 59.97 ? 292 HIS A NE2 1 ATOM 2328 N N . ASN A 1 293 ? 39.142 -14.236 -28.071 1.00 52.68 ? 293 ASN A N 1 ATOM 2329 C CA . ASN A 1 293 ? 40.344 -13.817 -27.351 1.00 53.72 ? 293 ASN A CA 1 ATOM 2330 C C . ASN A 1 293 ? 40.102 -12.883 -26.163 1.00 55.69 ? 293 ASN A C 1 ATOM 2331 O O . ASN A 1 293 ? 40.972 -12.095 -25.800 1.00 57.50 ? 293 ASN A O 1 ATOM 2332 C CB . ASN A 1 293 ? 41.318 -13.169 -28.333 1.00 54.34 ? 293 ASN A CB 1 ATOM 2333 C CG . ASN A 1 293 ? 40.800 -11.869 -28.909 1.00 54.64 ? 293 ASN A CG 1 ATOM 2334 O OD1 . ASN A 1 293 ? 39.677 -11.454 -28.656 1.00 55.11 ? 293 ASN A OD1 1 ATOM 2335 N ND2 . ASN A 1 293 ? 41.620 -11.224 -29.693 1.00 56.04 ? 293 ASN A ND2 1 ATOM 2336 N N . ILE A 1 294 ? 38.921 -12.975 -25.559 1.00 56.89 ? 294 ILE A N 1 ATOM 2337 C CA . ILE A 1 294 ? 38.511 -12.082 -24.469 1.00 58.85 ? 294 ILE A CA 1 ATOM 2338 C C . ILE A 1 294 ? 39.215 -12.379 -23.140 1.00 59.34 ? 294 ILE A C 1 ATOM 2339 O O . ILE A 1 294 ? 39.891 -11.513 -22.587 1.00 61.23 ? 294 ILE A O 1 ATOM 2340 C CB . ILE A 1 294 ? 36.985 -12.150 -24.243 1.00 60.49 ? 294 ILE A CB 1 ATOM 2341 C CG1 . ILE A 1 294 ? 36.212 -11.957 -25.560 1.00 60.60 ? 294 ILE A CG1 1 ATOM 2342 C CG2 . ILE A 1 294 ? 36.546 -11.090 -23.246 1.00 62.58 ? 294 ILE A CG2 1 ATOM 2343 C CD1 . ILE A 1 294 ? 36.647 -10.748 -26.358 1.00 61.70 ? 294 ILE A CD1 1 ATOM 2344 N N . HIS A 1 295 ? 39.041 -13.594 -22.629 1.00 58.80 ? 295 HIS A N 1 ATOM 2345 C CA . HIS A 1 295 ? 39.628 -14.013 -21.352 1.00 60.15 ? 295 HIS A CA 1 ATOM 2346 C C . HIS A 1 295 ? 39.600 -15.548 -21.267 1.00 58.46 ? 295 HIS A C 1 ATOM 2347 O O . HIS A 1 295 ? 38.631 -16.158 -21.699 1.00 55.21 ? 295 HIS A O 1 ATOM 2348 C CB . HIS A 1 295 ? 38.810 -13.418 -20.200 1.00 62.50 ? 295 HIS A CB 1 ATOM 2349 C CG . HIS A 1 295 ? 39.534 -13.373 -18.891 1.00 65.66 ? 295 HIS A CG 1 ATOM 2350 N ND1 . HIS A 1 295 ? 39.821 -14.503 -18.164 1.00 66.67 ? 295 HIS A ND1 1 ATOM 2351 C CD2 . HIS A 1 295 ? 40.001 -12.332 -18.163 1.00 68.75 ? 295 HIS A CD2 1 ATOM 2352 C CE1 . HIS A 1 295 ? 40.456 -14.167 -17.056 1.00 69.37 ? 295 HIS A CE1 1 ATOM 2353 N NE2 . HIS A 1 295 ? 40.578 -12.854 -17.031 1.00 70.79 ? 295 HIS A NE2 1 ATOM 2354 N N . PRO A 1 296 ? 40.647 -16.174 -20.699 1.00 59.63 ? 296 PRO A N 1 ATOM 2355 C CA . PRO A 1 296 ? 40.664 -17.645 -20.629 1.00 59.86 ? 296 PRO A CA 1 ATOM 2356 C C . PRO A 1 296 ? 39.638 -18.247 -19.675 1.00 60.78 ? 296 PRO A C 1 ATOM 2357 O O . PRO A 1 296 ? 39.161 -19.343 -19.902 1.00 59.93 ? 296 PRO A O 1 ATOM 2358 C CB . PRO A 1 296 ? 42.085 -17.964 -20.138 1.00 61.45 ? 296 PRO A CB 1 ATOM 2359 C CG . PRO A 1 296 ? 42.547 -16.726 -19.457 1.00 62.84 ? 296 PRO A CG 1 ATOM 2360 C CD . PRO A 1 296 ? 41.919 -15.594 -20.229 1.00 61.51 ? 296 PRO A CD 1 ATOM 2361 N N . LEU A 1 297 ? 39.323 -17.551 -18.594 1.00 63.66 ? 297 LEU A N 1 ATOM 2362 C CA . LEU A 1 297 ? 38.404 -18.082 -17.572 1.00 66.71 ? 297 LEU A CA 1 ATOM 2363 C C . LEU A 1 297 ? 36.941 -17.788 -17.880 1.00 65.41 ? 297 LEU A C 1 ATOM 2364 O O . LEU A 1 297 ? 36.412 -16.776 -17.457 1.00 69.00 ? 297 LEU A O 1 ATOM 2365 C CB . LEU A 1 297 ? 38.789 -17.540 -16.186 1.00 68.13 ? 297 LEU A CB 1 ATOM 2366 C CG . LEU A 1 297 ? 40.219 -17.890 -15.752 1.00 70.71 ? 297 LEU A CG 1 ATOM 2367 C CD1 . LEU A 1 297 ? 40.580 -17.275 -14.400 1.00 72.86 ? 297 LEU A CD1 1 ATOM 2368 C CD2 . LEU A 1 297 ? 40.395 -19.400 -15.699 1.00 73.08 ? 297 LEU A CD2 1 ATOM 2369 N N . THR A 1 298 ? 36.291 -18.677 -18.616 1.00 64.63 ? 298 THR A N 1 ATOM 2370 C CA . THR A 1 298 ? 34.899 -18.482 -18.999 1.00 63.18 ? 298 THR A CA 1 ATOM 2371 C C . THR A 1 298 ? 34.018 -19.536 -18.364 1.00 63.95 ? 298 THR A C 1 ATOM 2372 O O . THR A 1 298 ? 34.498 -20.555 -17.885 1.00 63.59 ? 298 THR A O 1 ATOM 2373 C CB . THR A 1 298 ? 34.720 -18.526 -20.529 1.00 62.32 ? 298 THR A CB 1 ATOM 2374 O OG1 . THR A 1 298 ? 34.769 -19.880 -20.997 1.00 63.24 ? 298 THR A OG1 1 ATOM 2375 C CG2 . THR A 1 298 ? 35.808 -17.735 -21.195 1.00 61.89 ? 298 THR A CG2 1 ATOM 2376 N N . ILE A 1 299 ? 32.720 -19.272 -18.366 1.00 65.93 ? 299 ILE A N 1 ATOM 2377 C CA . ILE A 1 299 ? 31.727 -20.215 -17.855 1.00 70.61 ? 299 ILE A CA 1 ATOM 2378 C C . ILE A 1 299 ? 30.606 -20.197 -18.877 1.00 71.67 ? 299 ILE A C 1 ATOM 2379 O O . ILE A 1 299 ? 30.253 -19.123 -19.385 1.00 69.36 ? 299 ILE A O 1 ATOM 2380 C CB . ILE A 1 299 ? 31.231 -19.823 -16.424 1.00 74.11 ? 299 ILE A CB 1 ATOM 2381 C CG1 . ILE A 1 299 ? 30.082 -20.714 -15.920 1.00 78.55 ? 299 ILE A CG1 1 ATOM 2382 C CG2 . ILE A 1 299 ? 30.768 -18.374 -16.365 1.00 73.71 ? 299 ILE A CG2 1 ATOM 2383 C CD1 . ILE A 1 299 ? 30.454 -22.169 -15.714 1.00 81.84 ? 299 ILE A CD1 1 ATOM 2384 N N . GLY A 1 300 ? 30.081 -21.385 -19.193 1.00 75.15 ? 300 GLY A N 1 ATOM 2385 C CA . GLY A 1 300 ? 28.953 -21.540 -20.118 1.00 78.10 ? 300 GLY A CA 1 ATOM 2386 C C . GLY A 1 300 ? 29.316 -22.230 -21.429 1.00 80.05 ? 300 GLY A C 1 ATOM 2387 O O . GLY A 1 300 ? 30.286 -22.994 -21.505 1.00 78.76 ? 300 GLY A O 1 ATOM 2388 N N . GLU A 1 301 ? 28.533 -21.951 -22.468 1.00 83.26 ? 301 GLU A N 1 ATOM 2389 C CA . GLU A 1 301 ? 28.744 -22.556 -23.778 1.00 85.48 ? 301 GLU A CA 1 ATOM 2390 C C . GLU A 1 301 ? 29.558 -21.579 -24.588 1.00 79.16 ? 301 GLU A C 1 ATOM 2391 O O . GLU A 1 301 ? 29.015 -20.643 -25.165 1.00 77.29 ? 301 GLU A O 1 ATOM 2392 C CB . GLU A 1 301 ? 27.407 -22.862 -24.464 1.00 93.86 ? 301 GLU A CB 1 ATOM 2393 C CG . GLU A 1 301 ? 27.436 -24.102 -25.349 1.00 101.18 ? 301 GLU A CG 1 ATOM 2394 C CD . GLU A 1 301 ? 27.746 -25.372 -24.563 1.00 108.10 ? 301 GLU A CD 1 ATOM 2395 O OE1 . GLU A 1 301 ? 26.860 -25.879 -23.830 1.00 113.26 ? 301 GLU A OE1 1 ATOM 2396 O OE2 . GLU A 1 301 ? 28.894 -25.857 -24.670 1.00 111.84 ? 301 GLU A OE2 1 ATOM 2397 N N . CYS A 1 302 ? 30.867 -21.803 -24.622 1.00 75.29 ? 302 CYS A N 1 ATOM 2398 C CA . CYS A 1 302 ? 31.787 -20.790 -25.102 1.00 71.76 ? 302 CYS A CA 1 ATOM 2399 C C . CYS A 1 302 ? 32.633 -21.220 -26.298 1.00 69.32 ? 302 CYS A C 1 ATOM 2400 O O . CYS A 1 302 ? 32.920 -22.398 -26.487 1.00 67.78 ? 302 CYS A O 1 ATOM 2401 C CB . CYS A 1 302 ? 32.717 -20.371 -23.970 1.00 71.81 ? 302 CYS A CB 1 ATOM 2402 S SG . CYS A 1 302 ? 31.880 -19.538 -22.602 1.00 75.14 ? 302 CYS A SG 1 ATOM 2403 N N . PRO A 1 303 ? 33.046 -20.241 -27.107 1.00 66.67 ? 303 PRO A N 1 ATOM 2404 C CA . PRO A 1 303 ? 34.112 -20.496 -28.051 1.00 65.43 ? 303 PRO A CA 1 ATOM 2405 C C . PRO A 1 303 ? 35.405 -20.813 -27.300 1.00 65.94 ? 303 PRO A C 1 ATOM 2406 O O . PRO A 1 303 ? 35.511 -20.515 -26.110 1.00 67.90 ? 303 PRO A O 1 ATOM 2407 C CB . PRO A 1 303 ? 34.247 -19.173 -28.823 1.00 64.47 ? 303 PRO A CB 1 ATOM 2408 C CG . PRO A 1 303 ? 33.081 -18.332 -28.436 1.00 65.01 ? 303 PRO A CG 1 ATOM 2409 C CD . PRO A 1 303 ? 32.589 -18.844 -27.125 1.00 65.67 ? 303 PRO A CD 1 ATOM 2410 N N . LYS A 1 304 ? 36.379 -21.398 -27.993 1.00 65.46 ? 304 LYS A N 1 ATOM 2411 C CA . LYS A 1 304 ? 37.665 -21.732 -27.389 1.00 65.34 ? 304 LYS A CA 1 ATOM 2412 C C . LYS A 1 304 ? 38.540 -20.501 -27.344 1.00 60.94 ? 304 LYS A C 1 ATOM 2413 O O . LYS A 1 304 ? 38.569 -19.718 -28.281 1.00 59.53 ? 304 LYS A O 1 ATOM 2414 C CB . LYS A 1 304 ? 38.359 -22.837 -28.174 1.00 68.43 ? 304 LYS A CB 1 ATOM 2415 C CG . LYS A 1 304 ? 37.510 -24.099 -28.317 1.00 75.46 ? 304 LYS A CG 1 ATOM 2416 C CD . LYS A 1 304 ? 37.294 -24.816 -26.987 1.00 81.63 ? 304 LYS A CD 1 ATOM 2417 C CE . LYS A 1 304 ? 35.900 -25.412 -26.861 1.00 85.58 ? 304 LYS A CE 1 ATOM 2418 N NZ . LYS A 1 304 ? 35.862 -26.350 -25.701 1.00 90.27 ? 304 LYS A NZ 1 ATOM 2419 N N . TYR A 1 305 ? 39.245 -20.330 -26.241 1.00 59.37 ? 305 TYR A N 1 ATOM 2420 C CA . TYR A 1 305 ? 40.051 -19.152 -26.046 1.00 58.07 ? 305 TYR A CA 1 ATOM 2421 C C . TYR A 1 305 ? 41.417 -19.335 -26.695 1.00 57.79 ? 305 TYR A C 1 ATOM 2422 O O . TYR A 1 305 ? 42.089 -20.338 -26.485 1.00 60.02 ? 305 TYR A O 1 ATOM 2423 C CB . TYR A 1 305 ? 40.216 -18.846 -24.549 1.00 59.01 ? 305 TYR A CB 1 ATOM 2424 C CG . TYR A 1 305 ? 41.178 -17.715 -24.303 1.00 58.64 ? 305 TYR A CG 1 ATOM 2425 C CD1 . TYR A 1 305 ? 40.787 -16.398 -24.480 1.00 58.18 ? 305 TYR A CD1 1 ATOM 2426 C CD2 . TYR A 1 305 ? 42.487 -17.960 -23.958 1.00 60.16 ? 305 TYR A CD2 1 ATOM 2427 C CE1 . TYR A 1 305 ? 41.670 -15.355 -24.290 1.00 58.97 ? 305 TYR A CE1 1 ATOM 2428 C CE2 . TYR A 1 305 ? 43.379 -16.922 -23.753 1.00 61.78 ? 305 TYR A CE2 1 ATOM 2429 C CZ . TYR A 1 305 ? 42.968 -15.620 -23.926 1.00 60.65 ? 305 TYR A CZ 1 ATOM 2430 O OH . TYR A 1 305 ? 43.851 -14.583 -23.738 1.00 60.88 ? 305 TYR A OH 1 ATOM 2431 N N . VAL A 1 306 ? 41.833 -18.343 -27.472 1.00 57.45 ? 306 VAL A N 1 ATOM 2432 C CA . VAL A 1 306 ? 43.189 -18.269 -27.989 1.00 56.33 ? 306 VAL A CA 1 ATOM 2433 C C . VAL A 1 306 ? 43.724 -16.871 -27.744 1.00 57.57 ? 306 VAL A C 1 ATOM 2434 O O . VAL A 1 306 ? 42.960 -15.913 -27.645 1.00 57.72 ? 306 VAL A O 1 ATOM 2435 C CB . VAL A 1 306 ? 43.260 -18.588 -29.497 1.00 55.90 ? 306 VAL A CB 1 ATOM 2436 C CG1 . VAL A 1 306 ? 42.932 -20.037 -29.764 1.00 55.47 ? 306 VAL A CG1 1 ATOM 2437 C CG2 . VAL A 1 306 ? 42.314 -17.710 -30.300 1.00 55.02 ? 306 VAL A CG2 1 ATOM 2438 N N . LYS A 1 307 ? 45.042 -16.759 -27.672 1.00 60.09 ? 307 LYS A N 1 ATOM 2439 C CA . LYS A 1 307 ? 45.726 -15.475 -27.549 1.00 64.05 ? 307 LYS A CA 1 ATOM 2440 C C . LYS A 1 307 ? 45.912 -14.691 -28.871 1.00 65.45 ? 307 LYS A C 1 ATOM 2441 O O . LYS A 1 307 ? 46.701 -13.752 -28.912 1.00 72.52 ? 307 LYS A O 1 ATOM 2442 C CB . LYS A 1 307 ? 47.121 -15.686 -26.929 1.00 67.69 ? 307 LYS A CB 1 ATOM 2443 C CG . LYS A 1 307 ? 47.153 -15.728 -25.418 1.00 70.50 ? 307 LYS A CG 1 ATOM 2444 C CD . LYS A 1 307 ? 48.581 -15.891 -24.946 1.00 76.37 ? 307 LYS A CD 1 ATOM 2445 C CE . LYS A 1 307 ? 48.658 -16.183 -23.460 1.00 81.54 ? 307 LYS A CE 1 ATOM 2446 N NZ . LYS A 1 307 ? 50.036 -16.625 -23.077 1.00 87.89 ? 307 LYS A NZ 1 ATOM 2447 N N . SER A 1 308 ? 45.218 -15.047 -29.949 1.00 62.61 ? 308 SER A N 1 ATOM 2448 C CA . SER A 1 308 ? 45.414 -14.359 -31.228 1.00 59.65 ? 308 SER A CA 1 ATOM 2449 C C . SER A 1 308 ? 44.721 -13.019 -31.269 1.00 60.11 ? 308 SER A C 1 ATOM 2450 O O . SER A 1 308 ? 43.664 -12.831 -30.672 1.00 58.35 ? 308 SER A O 1 ATOM 2451 C CB . SER A 1 308 ? 44.875 -15.194 -32.391 1.00 57.21 ? 308 SER A CB 1 ATOM 2452 O OG . SER A 1 308 ? 45.345 -16.516 -32.323 1.00 56.88 ? 308 SER A OG 1 ATOM 2453 N N . ASN A 1 309 ? 45.316 -12.103 -32.022 1.00 64.75 ? 309 ASN A N 1 ATOM 2454 C CA . ASN A 1 309 ? 44.657 -10.860 -32.425 1.00 68.06 ? 309 ASN A CA 1 ATOM 2455 C C . ASN A 1 309 ? 43.775 -11.036 -33.655 1.00 65.52 ? 309 ASN A C 1 ATOM 2456 O O . ASN A 1 309 ? 42.873 -10.241 -33.873 1.00 66.21 ? 309 ASN A O 1 ATOM 2457 C CB . ASN A 1 309 ? 45.698 -9.771 -32.711 1.00 73.39 ? 309 ASN A CB 1 ATOM 2458 C CG . ASN A 1 309 ? 46.313 -9.198 -31.441 1.00 79.90 ? 309 ASN A CG 1 ATOM 2459 O OD1 . ASN A 1 309 ? 45.696 -9.202 -30.362 1.00 79.90 ? 309 ASN A OD1 1 ATOM 2460 N ND2 . ASN A 1 309 ? 47.539 -8.688 -31.564 1.00 86.62 ? 309 ASN A ND2 1 ATOM 2461 N N . ARG A 1 310 ? 44.027 -12.079 -34.447 1.00 63.91 ? 310 ARG A N 1 ATOM 2462 C CA . ARG A 1 310 ? 43.378 -12.232 -35.752 1.00 63.83 ? 310 ARG A CA 1 ATOM 2463 C C . ARG A 1 310 ? 43.435 -13.666 -36.270 1.00 59.88 ? 310 ARG A C 1 ATOM 2464 O O . ARG A 1 310 ? 44.505 -14.249 -36.373 1.00 61.23 ? 310 ARG A O 1 ATOM 2465 C CB . ARG A 1 310 ? 44.077 -11.309 -36.754 1.00 69.45 ? 310 ARG A CB 1 ATOM 2466 C CG . ARG A 1 310 ? 43.333 -11.047 -38.049 1.00 71.74 ? 310 ARG A CG 1 ATOM 2467 C CD . ARG A 1 310 ? 44.194 -10.231 -39.003 1.00 76.70 ? 310 ARG A CD 1 ATOM 2468 N NE . ARG A 1 310 ? 43.854 -10.490 -40.406 1.00 81.02 ? 310 ARG A NE 1 ATOM 2469 C CZ . ARG A 1 310 ? 42.804 -9.976 -41.047 1.00 83.90 ? 310 ARG A CZ 1 ATOM 2470 N NH1 . ARG A 1 310 ? 41.958 -9.158 -40.431 1.00 87.52 ? 310 ARG A NH1 1 ATOM 2471 N NH2 . ARG A 1 310 ? 42.596 -10.272 -42.321 1.00 85.21 ? 310 ARG A NH2 1 ATOM 2472 N N . LEU A 1 311 ? 42.278 -14.239 -36.580 1.00 56.59 ? 311 LEU A N 1 ATOM 2473 C CA . LEU A 1 311 ? 42.214 -15.525 -37.280 1.00 55.10 ? 311 LEU A CA 1 ATOM 2474 C C . LEU A 1 311 ? 41.173 -15.431 -38.401 1.00 53.63 ? 311 LEU A C 1 ATOM 2475 O O . LEU A 1 311 ? 39.971 -15.371 -38.140 1.00 52.28 ? 311 LEU A O 1 ATOM 2476 C CB . LEU A 1 311 ? 41.864 -16.686 -36.336 1.00 53.97 ? 311 LEU A CB 1 ATOM 2477 C CG . LEU A 1 311 ? 42.832 -17.061 -35.217 1.00 55.29 ? 311 LEU A CG 1 ATOM 2478 C CD1 . LEU A 1 311 ? 42.223 -18.096 -34.294 1.00 55.27 ? 311 LEU A CD1 1 ATOM 2479 C CD2 . LEU A 1 311 ? 44.128 -17.618 -35.761 1.00 57.18 ? 311 LEU A CD2 1 ATOM 2480 N N . VAL A 1 312 ? 41.651 -15.428 -39.642 1.00 51.85 ? 312 VAL A N 1 ATOM 2481 C CA . VAL A 1 312 ? 40.795 -15.320 -40.824 1.00 49.80 ? 312 VAL A CA 1 ATOM 2482 C C . VAL A 1 312 ? 41.198 -16.360 -41.860 1.00 48.16 ? 312 VAL A C 1 ATOM 2483 O O . VAL A 1 312 ? 42.348 -16.372 -42.313 1.00 47.24 ? 312 VAL A O 1 ATOM 2484 C CB . VAL A 1 312 ? 40.944 -13.935 -41.460 1.00 50.63 ? 312 VAL A CB 1 ATOM 2485 C CG1 . VAL A 1 312 ? 40.169 -13.842 -42.768 1.00 49.82 ? 312 VAL A CG1 1 ATOM 2486 C CG2 . VAL A 1 312 ? 40.519 -12.870 -40.458 1.00 51.68 ? 312 VAL A CG2 1 ATOM 2487 N N . LEU A 1 313 ? 40.242 -17.211 -42.223 1.00 47.16 ? 313 LEU A N 1 ATOM 2488 C CA . LEU A 1 313 ? 40.417 -18.266 -43.217 1.00 46.58 ? 313 LEU A CA 1 ATOM 2489 C C . LEU A 1 313 ? 40.021 -17.797 -44.602 1.00 47.21 ? 313 LEU A C 1 ATOM 2490 O O . LEU A 1 313 ? 38.926 -17.240 -44.777 1.00 49.11 ? 313 LEU A O 1 ATOM 2491 C CB . LEU A 1 313 ? 39.527 -19.463 -42.905 1.00 46.13 ? 313 LEU A CB 1 ATOM 2492 C CG . LEU A 1 313 ? 39.966 -20.408 -41.800 1.00 47.87 ? 313 LEU A CG 1 ATOM 2493 C CD1 . LEU A 1 313 ? 38.804 -21.300 -41.389 1.00 49.00 ? 313 LEU A CD1 1 ATOM 2494 C CD2 . LEU A 1 313 ? 41.149 -21.274 -42.218 1.00 48.89 ? 313 LEU A CD2 1 ATOM 2495 N N . ALA A 1 314 ? 40.886 -18.060 -45.582 1.00 46.07 ? 314 ALA A N 1 ATOM 2496 C CA . ALA A 1 314 ? 40.529 -17.929 -46.996 1.00 46.27 ? 314 ALA A CA 1 ATOM 2497 C C . ALA A 1 314 ? 39.446 -18.930 -47.321 1.00 46.23 ? 314 ALA A C 1 ATOM 2498 O O . ALA A 1 314 ? 39.522 -20.093 -46.912 1.00 46.26 ? 314 ALA A O 1 ATOM 2499 C CB . ALA A 1 314 ? 41.728 -18.194 -47.884 1.00 47.38 ? 314 ALA A CB 1 ATOM 2500 N N . THR A 1 315 ? 38.413 -18.451 -48.007 1.00 47.32 ? 315 THR A N 1 ATOM 2501 C CA . THR A 1 315 ? 37.402 -19.309 -48.632 1.00 47.03 ? 315 THR A CA 1 ATOM 2502 C C . THR A 1 315 ? 37.491 -19.131 -50.137 1.00 45.47 ? 315 THR A C 1 ATOM 2503 O O . THR A 1 315 ? 37.550 -20.093 -50.874 1.00 46.18 ? 315 THR A O 1 ATOM 2504 C CB . THR A 1 315 ? 35.967 -18.942 -48.184 1.00 49.22 ? 315 THR A CB 1 ATOM 2505 O OG1 . THR A 1 315 ? 35.799 -17.515 -48.179 1.00 48.53 ? 315 THR A OG1 1 ATOM 2506 C CG2 . THR A 1 315 ? 35.689 -19.483 -46.775 1.00 50.56 ? 315 THR A CG2 1 ATOM 2507 N N . GLY A 1 316 ? 37.508 -17.890 -50.583 1.00 44.41 ? 316 GLY A N 1 ATOM 2508 C CA . GLY A 1 316 ? 37.645 -17.604 -51.982 1.00 45.29 ? 316 GLY A CA 1 ATOM 2509 C C . GLY A 1 316 ? 39.088 -17.610 -52.446 1.00 45.57 ? 316 GLY A C 1 ATOM 2510 O O . GLY A 1 316 ? 39.976 -18.216 -51.812 1.00 43.33 ? 316 GLY A O 1 ATOM 2511 N N . LEU A 1 317 ? 39.331 -16.889 -53.534 1.00 46.28 ? 317 LEU A N 1 ATOM 2512 C CA . LEU A 1 317 ? 40.598 -16.989 -54.210 1.00 47.39 ? 317 LEU A CA 1 ATOM 2513 C C . LEU A 1 317 ? 41.262 -15.632 -54.270 1.00 48.35 ? 317 LEU A C 1 ATOM 2514 O O . LEU A 1 317 ? 40.670 -14.621 -53.892 1.00 48.30 ? 317 LEU A O 1 ATOM 2515 C CB . LEU A 1 317 ? 40.437 -17.645 -55.595 1.00 48.53 ? 317 LEU A CB 1 ATOM 2516 C CG . LEU A 1 317 ? 39.367 -17.092 -56.519 1.00 50.17 ? 317 LEU A CG 1 ATOM 2517 C CD1 . LEU A 1 317 ? 39.830 -15.763 -57.069 1.00 53.10 ? 317 LEU A CD1 1 ATOM 2518 C CD2 . LEU A 1 317 ? 39.091 -18.049 -57.657 1.00 50.06 ? 317 LEU A CD2 1 ATOM 2519 N N . ARG A 1 318 ? 42.510 -15.639 -54.723 1.00 48.14 ? 318 ARG A N 1 ATOM 2520 C CA . ARG A 1 318 ? 43.326 -14.443 -54.793 1.00 50.67 ? 318 ARG A CA 1 ATOM 2521 C C . ARG A 1 318 ? 42.652 -13.406 -55.649 1.00 51.79 ? 318 ARG A C 1 ATOM 2522 O O . ARG A 1 318 ? 42.436 -13.623 -56.833 1.00 52.85 ? 318 ARG A O 1 ATOM 2523 C CB . ARG A 1 318 ? 44.706 -14.805 -55.355 1.00 51.65 ? 318 ARG A CB 1 ATOM 2524 C CG . ARG A 1 318 ? 45.738 -13.694 -55.286 1.00 56.16 ? 318 ARG A CG 1 ATOM 2525 C CD . ARG A 1 318 ? 47.063 -14.165 -55.857 1.00 58.84 ? 318 ARG A CD 1 ATOM 2526 N NE . ARG A 1 318 ? 47.840 -14.881 -54.851 1.00 58.92 ? 318 ARG A NE 1 ATOM 2527 C CZ . ARG A 1 318 ? 48.748 -14.308 -54.072 1.00 61.43 ? 318 ARG A CZ 1 ATOM 2528 N NH1 . ARG A 1 318 ? 49.002 -13.000 -54.175 1.00 65.20 ? 318 ARG A NH1 1 ATOM 2529 N NH2 . ARG A 1 318 ? 49.399 -15.042 -53.176 1.00 61.77 ? 318 ARG A NH2 1 ATOM 2530 N N . ASN A 1 319 ? 42.314 -12.280 -55.043 1.00 55.75 ? 319 ASN A N 1 ATOM 2531 C CA . ASN A 1 319 ? 41.576 -11.233 -55.735 1.00 59.34 ? 319 ASN A CA 1 ATOM 2532 C C . ASN A 1 319 ? 42.491 -10.312 -56.515 1.00 66.61 ? 319 ASN A C 1 ATOM 2533 O O . ASN A 1 319 ? 43.543 -9.909 -56.047 1.00 69.08 ? 319 ASN A O 1 ATOM 2534 C CB . ASN A 1 319 ? 40.723 -10.440 -54.765 1.00 59.41 ? 319 ASN A CB 1 ATOM 2535 C CG . ASN A 1 319 ? 39.674 -9.604 -55.465 1.00 62.22 ? 319 ASN A CG 1 ATOM 2536 O OD1 . ASN A 1 319 ? 39.480 -9.732 -56.653 1.00 62.86 ? 319 ASN A OD1 1 ATOM 2537 N ND2 . ASN A 1 319 ? 39.005 -8.730 -54.728 1.00 64.44 ? 319 ASN A ND2 1 ATOM 2538 N N . SER A 1 320 ? 42.056 -9.971 -57.718 1.00 75.50 ? 320 SER A N 1 ATOM 2539 C CA . SER A 1 320 ? 42.852 -9.205 -58.675 1.00 82.67 ? 320 SER A CA 1 ATOM 2540 C C . SER A 1 320 ? 42.742 -7.684 -58.446 1.00 89.39 ? 320 SER A C 1 ATOM 2541 O O . SER A 1 320 ? 41.717 -7.217 -57.969 1.00 86.54 ? 320 SER A O 1 ATOM 2542 C CB . SER A 1 320 ? 42.389 -9.567 -60.085 1.00 82.45 ? 320 SER A CB 1 ATOM 2543 O OG . SER A 1 320 ? 42.159 -10.970 -60.153 1.00 81.18 ? 320 SER A OG 1 ATOM 2544 N N . PRO A 1 321 ? 43.807 -6.919 -58.774 1.00 96.47 ? 321 PRO A N 1 ATOM 2545 C CA . PRO A 1 321 ? 43.790 -5.468 -58.604 1.00 106.75 ? 321 PRO A CA 1 ATOM 2546 C C . PRO A 1 321 ? 43.338 -4.729 -59.865 1.00 111.16 ? 321 PRO A C 1 ATOM 2547 O O . PRO A 1 321 ? 42.187 -4.850 -60.276 1.00 112.84 ? 321 PRO A O 1 ATOM 2548 C CB . PRO A 1 321 ? 45.256 -5.153 -58.310 1.00 109.59 ? 321 PRO A CB 1 ATOM 2549 C CG . PRO A 1 321 ? 46.000 -6.156 -59.132 1.00 106.23 ? 321 PRO A CG 1 ATOM 2550 C CD . PRO A 1 321 ? 45.146 -7.393 -59.179 1.00 99.31 ? 321 PRO A CD 1 ATOM 2551 N N . GLY B 2 1 ? 51.066 -18.738 -58.063 1.00 50.50 ? 1 GLY B N 1 ATOM 2552 C CA . GLY B 2 1 ? 50.655 -19.965 -57.331 1.00 47.08 ? 1 GLY B CA 1 ATOM 2553 C C . GLY B 2 1 ? 51.257 -21.244 -57.892 1.00 46.79 ? 1 GLY B C 1 ATOM 2554 O O . GLY B 2 1 ? 51.782 -21.283 -59.006 1.00 46.99 ? 1 GLY B O 1 ATOM 2555 N N . LEU B 2 2 ? 51.146 -22.320 -57.129 1.00 44.82 ? 2 LEU B N 1 ATOM 2556 C CA . LEU B 2 2 ? 51.835 -23.537 -57.497 1.00 44.92 ? 2 LEU B CA 1 ATOM 2557 C C . LEU B 2 2 ? 51.413 -24.046 -58.875 1.00 44.10 ? 2 LEU B C 1 ATOM 2558 O O . LEU B 2 2 ? 52.213 -24.636 -59.561 1.00 43.55 ? 2 LEU B O 1 ATOM 2559 C CB . LEU B 2 2 ? 51.558 -24.613 -56.460 1.00 43.68 ? 2 LEU B CB 1 ATOM 2560 C CG . LEU B 2 2 ? 52.248 -24.466 -55.146 1.00 43.39 ? 2 LEU B CG 1 ATOM 2561 C CD1 . LEU B 2 2 ? 51.785 -25.599 -54.258 1.00 43.13 ? 2 LEU B CD1 1 ATOM 2562 C CD2 . LEU B 2 2 ? 53.747 -24.462 -55.314 1.00 46.43 ? 2 LEU B CD2 1 ATOM 2563 N N . PHE B 2 3 ? 50.163 -23.796 -59.269 1.00 41.05 ? 3 PHE B N 1 ATOM 2564 C CA . PHE B 2 3 ? 49.621 -24.356 -60.506 1.00 42.08 ? 3 PHE B CA 1 ATOM 2565 C C . PHE B 2 3 ? 49.671 -23.440 -61.714 1.00 43.64 ? 3 PHE B C 1 ATOM 2566 O O . PHE B 2 3 ? 49.264 -23.842 -62.810 1.00 46.07 ? 3 PHE B O 1 ATOM 2567 C CB . PHE B 2 3 ? 48.192 -24.896 -60.242 1.00 40.84 ? 3 PHE B CB 1 ATOM 2568 C CG . PHE B 2 3 ? 48.204 -26.036 -59.267 1.00 39.64 ? 3 PHE B CG 1 ATOM 2569 C CD1 . PHE B 2 3 ? 48.444 -27.313 -59.698 1.00 39.00 ? 3 PHE B CD1 1 ATOM 2570 C CD2 . PHE B 2 3 ? 48.111 -25.796 -57.912 1.00 39.74 ? 3 PHE B CD2 1 ATOM 2571 C CE1 . PHE B 2 3 ? 48.520 -28.343 -58.805 1.00 41.10 ? 3 PHE B CE1 1 ATOM 2572 C CE2 . PHE B 2 3 ? 48.213 -26.831 -57.001 1.00 39.10 ? 3 PHE B CE2 1 ATOM 2573 C CZ . PHE B 2 3 ? 48.420 -28.097 -57.447 1.00 39.97 ? 3 PHE B CZ 1 ATOM 2574 N N . GLY B 2 4 ? 50.197 -22.231 -61.527 1.00 42.93 ? 4 GLY B N 1 ATOM 2575 C CA . GLY B 2 4 ? 50.517 -21.349 -62.635 1.00 43.46 ? 4 GLY B CA 1 ATOM 2576 C C . GLY B 2 4 ? 49.376 -20.625 -63.331 1.00 43.44 ? 4 GLY B C 1 ATOM 2577 O O . GLY B 2 4 ? 49.637 -19.820 -64.222 1.00 47.33 ? 4 GLY B O 1 ATOM 2578 N N . ALA B 2 5 ? 48.126 -20.886 -62.942 1.00 40.59 ? 5 ALA B N 1 ATOM 2579 C CA . ALA B 2 5 ? 46.961 -20.348 -63.652 1.00 39.91 ? 5 ALA B CA 1 ATOM 2580 C C . ALA B 2 5 ? 46.577 -18.999 -63.102 1.00 40.43 ? 5 ALA B C 1 ATOM 2581 O O . ALA B 2 5 ? 46.713 -17.992 -63.787 1.00 41.54 ? 5 ALA B O 1 ATOM 2582 C CB . ALA B 2 5 ? 45.768 -21.312 -63.570 1.00 38.90 ? 5 ALA B CB 1 ATOM 2583 N N . ILE B 2 6 ? 46.103 -18.977 -61.860 1.00 40.75 ? 6 ILE B N 1 ATOM 2584 C CA . ILE B 2 6 ? 45.678 -17.732 -61.221 1.00 42.80 ? 6 ILE B CA 1 ATOM 2585 C C . ILE B 2 6 ? 46.834 -16.745 -61.083 1.00 43.72 ? 6 ILE B C 1 ATOM 2586 O O . ILE B 2 6 ? 47.874 -17.071 -60.517 1.00 43.46 ? 6 ILE B O 1 ATOM 2587 C CB . ILE B 2 6 ? 45.040 -18.007 -59.853 1.00 44.13 ? 6 ILE B CB 1 ATOM 2588 C CG1 . ILE B 2 6 ? 43.646 -18.577 -60.067 1.00 45.29 ? 6 ILE B CG1 1 ATOM 2589 C CG2 . ILE B 2 6 ? 44.949 -16.734 -59.033 1.00 45.71 ? 6 ILE B CG2 1 ATOM 2590 C CD1 . ILE B 2 6 ? 43.042 -19.242 -58.857 1.00 48.12 ? 6 ILE B CD1 1 ATOM 2591 N N . ALA B 2 7 ? 46.656 -15.535 -61.615 1.00 45.47 ? 7 ALA B N 1 ATOM 2592 C CA . ALA B 2 7 ? 47.711 -14.518 -61.561 1.00 48.89 ? 7 ALA B CA 1 ATOM 2593 C C . ALA B 2 7 ? 48.995 -15.068 -62.140 1.00 52.33 ? 7 ALA B C 1 ATOM 2594 O O . ALA B 2 7 ? 50.072 -14.773 -61.651 1.00 58.23 ? 7 ALA B O 1 ATOM 2595 C CB . ALA B 2 7 ? 47.938 -14.075 -60.120 1.00 48.63 ? 7 ALA B CB 1 ATOM 2596 N N . GLY B 2 8 ? 48.860 -15.909 -63.157 1.00 53.63 ? 8 GLY B N 1 ATOM 2597 C CA . GLY B 2 8 ? 49.984 -16.529 -63.843 1.00 54.40 ? 8 GLY B CA 1 ATOM 2598 C C . GLY B 2 8 ? 49.755 -16.360 -65.336 1.00 55.77 ? 8 GLY B C 1 ATOM 2599 O O . GLY B 2 8 ? 49.843 -15.257 -65.835 1.00 58.94 ? 8 GLY B O 1 ATOM 2600 N N . PHE B 2 9 ? 49.431 -17.433 -66.051 1.00 53.18 ? 9 PHE B N 1 ATOM 2601 C CA . PHE B 2 9 ? 49.194 -17.310 -67.480 1.00 53.34 ? 9 PHE B CA 1 ATOM 2602 C C . PHE B 2 9 ? 47.815 -16.712 -67.702 1.00 52.19 ? 9 PHE B C 1 ATOM 2603 O O . PHE B 2 9 ? 47.576 -16.093 -68.733 1.00 54.78 ? 9 PHE B O 1 ATOM 2604 C CB . PHE B 2 9 ? 49.429 -18.632 -68.239 1.00 53.83 ? 9 PHE B CB 1 ATOM 2605 C CG . PHE B 2 9 ? 48.381 -19.684 -68.016 1.00 51.00 ? 9 PHE B CG 1 ATOM 2606 C CD1 . PHE B 2 9 ? 47.208 -19.685 -68.752 1.00 50.78 ? 9 PHE B CD1 1 ATOM 2607 C CD2 . PHE B 2 9 ? 48.589 -20.692 -67.105 1.00 50.21 ? 9 PHE B CD2 1 ATOM 2608 C CE1 . PHE B 2 9 ? 46.246 -20.658 -68.552 1.00 49.37 ? 9 PHE B CE1 1 ATOM 2609 C CE2 . PHE B 2 9 ? 47.640 -21.672 -66.896 1.00 48.82 ? 9 PHE B CE2 1 ATOM 2610 C CZ . PHE B 2 9 ? 46.457 -21.647 -67.618 1.00 48.86 ? 9 PHE B CZ 1 ATOM 2611 N N . ILE B 2 10 ? 46.918 -16.874 -66.732 1.00 50.02 ? 10 ILE B N 1 ATOM 2612 C CA . ILE B 2 10 ? 45.697 -16.087 -66.712 1.00 50.32 ? 10 ILE B CA 1 ATOM 2613 C C . ILE B 2 10 ? 45.946 -14.888 -65.815 1.00 53.59 ? 10 ILE B C 1 ATOM 2614 O O . ILE B 2 10 ? 45.957 -14.995 -64.602 1.00 56.12 ? 10 ILE B O 1 ATOM 2615 C CB . ILE B 2 10 ? 44.489 -16.890 -66.247 1.00 46.73 ? 10 ILE B CB 1 ATOM 2616 C CG1 . ILE B 2 10 ? 44.351 -18.146 -67.089 1.00 46.75 ? 10 ILE B CG1 1 ATOM 2617 C CG2 . ILE B 2 10 ? 43.235 -16.057 -66.403 1.00 47.17 ? 10 ILE B CG2 1 ATOM 2618 C CD1 . ILE B 2 10 ? 43.354 -19.121 -66.529 1.00 45.90 ? 10 ILE B CD1 1 ATOM 2619 N N . GLU B 2 11 ? 46.160 -13.746 -66.446 1.00 59.92 ? 11 GLU B N 1 ATOM 2620 C CA . GLU B 2 11 ? 46.717 -12.547 -65.795 1.00 64.46 ? 11 GLU B CA 1 ATOM 2621 C C . GLU B 2 11 ? 45.912 -12.047 -64.609 1.00 60.13 ? 11 GLU B C 1 ATOM 2622 O O . GLU B 2 11 ? 46.479 -11.638 -63.605 1.00 61.42 ? 11 GLU B O 1 ATOM 2623 C CB . GLU B 2 11 ? 46.800 -11.402 -66.806 1.00 72.72 ? 11 GLU B CB 1 ATOM 2624 C CG . GLU B 2 11 ? 48.190 -10.920 -67.160 1.00 80.65 ? 11 GLU B CG 1 ATOM 2625 C CD . GLU B 2 11 ? 48.162 -9.458 -67.609 1.00 87.60 ? 11 GLU B CD 1 ATOM 2626 O OE1 . GLU B 2 11 ? 47.268 -9.082 -68.415 1.00 87.72 ? 11 GLU B OE1 1 ATOM 2627 O OE2 . GLU B 2 11 ? 49.020 -8.679 -67.139 1.00 93.50 ? 11 GLU B OE2 1 ATOM 2628 N N . GLY B 2 12 ? 44.593 -12.033 -64.759 1.00 56.62 ? 12 GLY B N 1 ATOM 2629 C CA . GLY B 2 12 ? 43.692 -11.507 -63.732 1.00 55.00 ? 12 GLY B CA 1 ATOM 2630 C C . GLY B 2 12 ? 42.290 -12.086 -63.791 1.00 52.39 ? 12 GLY B C 1 ATOM 2631 O O . GLY B 2 12 ? 41.912 -12.747 -64.766 1.00 50.94 ? 12 GLY B O 1 ATOM 2632 N N . GLY B 2 13 ? 41.515 -11.840 -62.742 1.00 51.71 ? 13 GLY B N 1 ATOM 2633 C CA . GLY B 2 13 ? 40.159 -12.373 -62.640 1.00 51.31 ? 13 GLY B CA 1 ATOM 2634 C C . GLY B 2 13 ? 39.131 -11.509 -63.367 1.00 52.90 ? 13 GLY B C 1 ATOM 2635 O O . GLY B 2 13 ? 39.469 -10.498 -63.948 1.00 56.32 ? 13 GLY B O 1 ATOM 2636 N N . TRP B 2 14 ? 37.869 -11.911 -63.305 1.00 52.21 ? 14 TRP B N 1 ATOM 2637 C CA . TRP B 2 14 ? 36.791 -11.265 -64.041 1.00 54.39 ? 14 TRP B CA 1 ATOM 2638 C C . TRP B 2 14 ? 35.734 -10.710 -63.104 1.00 58.18 ? 14 TRP B C 1 ATOM 2639 O O . TRP B 2 14 ? 34.929 -11.459 -62.563 1.00 56.91 ? 14 TRP B O 1 ATOM 2640 C CB . TRP B 2 14 ? 36.129 -12.269 -64.996 1.00 51.28 ? 14 TRP B CB 1 ATOM 2641 C CG . TRP B 2 14 ? 36.994 -12.680 -66.140 1.00 49.69 ? 14 TRP B CG 1 ATOM 2642 C CD1 . TRP B 2 14 ? 38.008 -11.960 -66.694 1.00 50.67 ? 14 TRP B CD1 1 ATOM 2643 C CD2 . TRP B 2 14 ? 36.899 -13.887 -66.909 1.00 48.30 ? 14 TRP B CD2 1 ATOM 2644 N NE1 . TRP B 2 14 ? 38.559 -12.644 -67.744 1.00 49.57 ? 14 TRP B NE1 1 ATOM 2645 C CE2 . TRP B 2 14 ? 37.893 -13.825 -67.905 1.00 48.45 ? 14 TRP B CE2 1 ATOM 2646 C CE3 . TRP B 2 14 ? 36.070 -15.004 -66.858 1.00 47.47 ? 14 TRP B CE3 1 ATOM 2647 C CZ2 . TRP B 2 14 ? 38.091 -14.840 -68.827 1.00 49.23 ? 14 TRP B CZ2 1 ATOM 2648 C CZ3 . TRP B 2 14 ? 36.272 -16.017 -67.769 1.00 48.13 ? 14 TRP B CZ3 1 ATOM 2649 C CH2 . TRP B 2 14 ? 37.277 -15.932 -68.741 1.00 48.61 ? 14 TRP B CH2 1 ATOM 2650 N N . GLN B 2 15 ? 35.725 -9.389 -62.936 1.00 64.16 ? 15 GLN B N 1 ATOM 2651 C CA . GLN B 2 15 ? 34.638 -8.706 -62.229 1.00 69.04 ? 15 GLN B CA 1 ATOM 2652 C C . GLN B 2 15 ? 33.288 -9.050 -62.854 1.00 66.20 ? 15 GLN B C 1 ATOM 2653 O O . GLN B 2 15 ? 32.273 -9.054 -62.175 1.00 67.39 ? 15 GLN B O 1 ATOM 2654 C CB . GLN B 2 15 ? 34.817 -7.181 -62.278 1.00 75.45 ? 15 GLN B CB 1 ATOM 2655 C CG . GLN B 2 15 ? 36.069 -6.628 -61.608 1.00 78.84 ? 15 GLN B CG 1 ATOM 2656 C CD . GLN B 2 15 ? 35.877 -6.272 -60.143 1.00 82.77 ? 15 GLN B CD 1 ATOM 2657 O OE1 . GLN B 2 15 ? 36.699 -6.640 -59.313 1.00 86.10 ? 15 GLN B OE1 1 ATOM 2658 N NE2 . GLN B 2 15 ? 34.804 -5.548 -59.820 1.00 86.34 ? 15 GLN B NE2 1 ATOM 2659 N N . GLY B 2 16 ? 33.286 -9.304 -64.157 1.00 64.62 ? 16 GLY B N 1 ATOM 2660 C CA . GLY B 2 16 ? 32.062 -9.605 -64.895 1.00 65.65 ? 16 GLY B CA 1 ATOM 2661 C C . GLY B 2 16 ? 31.478 -10.998 -64.718 1.00 64.17 ? 16 GLY B C 1 ATOM 2662 O O . GLY B 2 16 ? 30.313 -11.218 -65.061 1.00 65.83 ? 16 GLY B O 1 ATOM 2663 N N . MET B 2 17 ? 32.265 -11.946 -64.207 1.00 58.44 ? 17 MET B N 1 ATOM 2664 C CA . MET B 2 17 ? 31.739 -13.280 -63.929 1.00 58.66 ? 17 MET B CA 1 ATOM 2665 C C . MET B 2 17 ? 31.285 -13.364 -62.489 1.00 59.10 ? 17 MET B C 1 ATOM 2666 O O . MET B 2 17 ? 32.090 -13.498 -61.575 1.00 59.39 ? 17 MET B O 1 ATOM 2667 C CB . MET B 2 17 ? 32.774 -14.373 -64.173 1.00 57.59 ? 17 MET B CB 1 ATOM 2668 C CG . MET B 2 17 ? 32.192 -15.753 -63.925 1.00 58.27 ? 17 MET B CG 1 ATOM 2669 S SD . MET B 2 17 ? 33.257 -17.016 -64.591 1.00 56.10 ? 17 MET B SD 1 ATOM 2670 C CE . MET B 2 17 ? 34.689 -16.593 -63.611 1.00 58.91 ? 17 MET B CE 1 ATOM 2671 N N . VAL B 2 18 ? 29.979 -13.345 -62.300 1.00 61.78 ? 18 VAL B N 1 ATOM 2672 C CA . VAL B 2 18 ? 29.393 -13.043 -61.010 1.00 63.77 ? 18 VAL B CA 1 ATOM 2673 C C . VAL B 2 18 ? 28.805 -14.260 -60.316 1.00 64.20 ? 18 VAL B C 1 ATOM 2674 O O . VAL B 2 18 ? 28.630 -14.268 -59.115 1.00 66.38 ? 18 VAL B O 1 ATOM 2675 C CB . VAL B 2 18 ? 28.328 -11.947 -61.206 1.00 68.87 ? 18 VAL B CB 1 ATOM 2676 C CG1 . VAL B 2 18 ? 26.959 -12.364 -60.693 1.00 72.51 ? 18 VAL B CG1 1 ATOM 2677 C CG2 . VAL B 2 18 ? 28.809 -10.649 -60.589 1.00 71.18 ? 18 VAL B CG2 1 ATOM 2678 N N . ASP B 2 19 ? 28.505 -15.299 -61.069 1.00 65.83 ? 19 ASP B N 1 ATOM 2679 C CA . ASP B 2 19 ? 27.740 -16.419 -60.540 1.00 67.83 ? 19 ASP B CA 1 ATOM 2680 C C . ASP B 2 19 ? 28.578 -17.691 -60.438 1.00 62.34 ? 19 ASP B C 1 ATOM 2681 O O . ASP B 2 19 ? 28.048 -18.779 -60.385 1.00 67.38 ? 19 ASP B O 1 ATOM 2682 C CB . ASP B 2 19 ? 26.495 -16.641 -61.416 1.00 72.59 ? 19 ASP B CB 1 ATOM 2683 C CG . ASP B 2 19 ? 26.835 -16.785 -62.892 1.00 74.13 ? 19 ASP B CG 1 ATOM 2684 O OD1 . ASP B 2 19 ? 28.025 -16.631 -63.253 1.00 67.85 ? 19 ASP B OD1 1 ATOM 2685 O OD2 . ASP B 2 19 ? 25.903 -17.033 -63.693 1.00 82.09 ? 19 ASP B OD2 1 ATOM 2686 N N . GLY B 2 20 ? 29.888 -17.569 -60.404 1.00 57.27 ? 20 GLY B N 1 ATOM 2687 C CA . GLY B 2 20 ? 30.685 -18.729 -60.058 1.00 55.83 ? 20 GLY B CA 1 ATOM 2688 C C . GLY B 2 20 ? 32.121 -18.377 -59.825 1.00 52.61 ? 20 GLY B C 1 ATOM 2689 O O . GLY B 2 20 ? 32.538 -17.251 -60.083 1.00 53.50 ? 20 GLY B O 1 ATOM 2690 N N . TRP B 2 21 ? 32.898 -19.339 -59.342 1.00 51.48 ? 21 TRP B N 1 ATOM 2691 C CA . TRP B 2 21 ? 34.303 -19.058 -59.080 1.00 48.45 ? 21 TRP B CA 1 ATOM 2692 C C . TRP B 2 21 ? 35.138 -19.172 -60.334 1.00 44.96 ? 21 TRP B C 1 ATOM 2693 O O . TRP B 2 21 ? 36.125 -18.447 -60.508 1.00 44.30 ? 21 TRP B O 1 ATOM 2694 C CB . TRP B 2 21 ? 34.844 -19.941 -57.968 1.00 50.40 ? 21 TRP B CB 1 ATOM 2695 C CG . TRP B 2 21 ? 34.753 -19.318 -56.582 1.00 52.39 ? 21 TRP B CG 1 ATOM 2696 C CD1 . TRP B 2 21 ? 34.890 -17.994 -56.240 1.00 54.03 ? 21 TRP B CD1 1 ATOM 2697 C CD2 . TRP B 2 21 ? 34.588 -20.019 -55.372 1.00 54.75 ? 21 TRP B CD2 1 ATOM 2698 N NE1 . TRP B 2 21 ? 34.796 -17.833 -54.881 1.00 55.09 ? 21 TRP B NE1 1 ATOM 2699 C CE2 . TRP B 2 21 ? 34.603 -19.067 -54.324 1.00 55.48 ? 21 TRP B CE2 1 ATOM 2700 C CE3 . TRP B 2 21 ? 34.455 -21.372 -55.060 1.00 58.86 ? 21 TRP B CE3 1 ATOM 2701 C CZ2 . TRP B 2 21 ? 34.460 -19.426 -52.999 1.00 59.01 ? 21 TRP B CZ2 1 ATOM 2702 C CZ3 . TRP B 2 21 ? 34.328 -21.738 -53.735 1.00 61.49 ? 21 TRP B CZ3 1 ATOM 2703 C CH2 . TRP B 2 21 ? 34.322 -20.766 -52.715 1.00 62.73 ? 21 TRP B CH2 1 ATOM 2704 N N . TYR B 2 22 ? 34.730 -20.069 -61.217 1.00 43.35 ? 22 TYR B N 1 ATOM 2705 C CA . TYR B 2 22 ? 35.460 -20.317 -62.435 1.00 42.93 ? 22 TYR B CA 1 ATOM 2706 C C . TYR B 2 22 ? 34.491 -20.505 -63.563 1.00 42.90 ? 22 TYR B C 1 ATOM 2707 O O . TYR B 2 22 ? 33.395 -21.044 -63.378 1.00 46.21 ? 22 TYR B O 1 ATOM 2708 C CB . TYR B 2 22 ? 36.333 -21.585 -62.340 1.00 41.12 ? 22 TYR B CB 1 ATOM 2709 C CG . TYR B 2 22 ? 36.771 -21.974 -60.947 1.00 41.22 ? 22 TYR B CG 1 ATOM 2710 C CD1 . TYR B 2 22 ? 37.704 -21.226 -60.259 1.00 42.12 ? 22 TYR B CD1 1 ATOM 2711 C CD2 . TYR B 2 22 ? 36.267 -23.115 -60.328 1.00 43.57 ? 22 TYR B CD2 1 ATOM 2712 C CE1 . TYR B 2 22 ? 38.135 -21.594 -58.985 1.00 42.53 ? 22 TYR B CE1 1 ATOM 2713 C CE2 . TYR B 2 22 ? 36.674 -23.482 -59.056 1.00 43.64 ? 22 TYR B CE2 1 ATOM 2714 C CZ . TYR B 2 22 ? 37.612 -22.726 -58.398 1.00 43.91 ? 22 TYR B CZ 1 ATOM 2715 O OH . TYR B 2 22 ? 38.024 -23.077 -57.146 1.00 44.90 ? 22 TYR B OH 1 ATOM 2716 N N . GLY B 2 23 ? 34.915 -20.109 -64.753 1.00 43.06 ? 23 GLY B N 1 ATOM 2717 C CA . GLY B 2 23 ? 34.081 -20.329 -65.918 1.00 45.32 ? 23 GLY B CA 1 ATOM 2718 C C . GLY B 2 23 ? 34.735 -19.843 -67.178 1.00 46.79 ? 23 GLY B C 1 ATOM 2719 O O . GLY B 2 23 ? 35.968 -19.764 -67.256 1.00 44.83 ? 23 GLY B O 1 ATOM 2720 N N . TYR B 2 24 ? 33.887 -19.500 -68.148 1.00 50.19 ? 24 TYR B N 1 ATOM 2721 C CA . TYR B 2 24 ? 34.307 -19.201 -69.519 1.00 50.86 ? 24 TYR B CA 1 ATOM 2722 C C . TYR B 2 24 ? 33.869 -17.825 -69.963 1.00 51.06 ? 24 TYR B C 1 ATOM 2723 O O . TYR B 2 24 ? 32.854 -17.321 -69.514 1.00 53.62 ? 24 TYR B O 1 ATOM 2724 C CB . TYR B 2 24 ? 33.668 -20.181 -70.491 1.00 54.51 ? 24 TYR B CB 1 ATOM 2725 C CG . TYR B 2 24 ? 33.696 -21.607 -70.046 1.00 55.79 ? 24 TYR B CG 1 ATOM 2726 C CD1 . TYR B 2 24 ? 32.776 -22.070 -69.135 1.00 55.89 ? 24 TYR B CD1 1 ATOM 2727 C CD2 . TYR B 2 24 ? 34.652 -22.496 -70.537 1.00 58.93 ? 24 TYR B CD2 1 ATOM 2728 C CE1 . TYR B 2 24 ? 32.784 -23.382 -68.720 1.00 60.30 ? 24 TYR B CE1 1 ATOM 2729 C CE2 . TYR B 2 24 ? 34.684 -23.819 -70.115 1.00 60.94 ? 24 TYR B CE2 1 ATOM 2730 C CZ . TYR B 2 24 ? 33.738 -24.254 -69.208 1.00 62.23 ? 24 TYR B CZ 1 ATOM 2731 O OH . TYR B 2 24 ? 33.711 -25.549 -68.771 1.00 65.79 ? 24 TYR B OH 1 ATOM 2732 N N . HIS B 2 25 ? 34.624 -17.235 -70.876 1.00 50.68 ? 25 HIS B N 1 ATOM 2733 C CA . HIS B 2 25 ? 34.178 -16.047 -71.577 1.00 52.16 ? 25 HIS B CA 1 ATOM 2734 C C . HIS B 2 25 ? 34.266 -16.295 -73.063 1.00 53.48 ? 25 HIS B C 1 ATOM 2735 O O . HIS B 2 25 ? 35.290 -16.740 -73.530 1.00 51.89 ? 25 HIS B O 1 ATOM 2736 C CB . HIS B 2 25 ? 35.057 -14.860 -71.238 1.00 51.12 ? 25 HIS B CB 1 ATOM 2737 C CG . HIS B 2 25 ? 34.616 -13.599 -71.897 1.00 53.87 ? 25 HIS B CG 1 ATOM 2738 N ND1 . HIS B 2 25 ? 35.219 -13.111 -73.036 1.00 54.19 ? 25 HIS B ND1 1 ATOM 2739 C CD2 . HIS B 2 25 ? 33.600 -12.747 -71.606 1.00 55.65 ? 25 HIS B CD2 1 ATOM 2740 C CE1 . HIS B 2 25 ? 34.614 -11.994 -73.399 1.00 57.52 ? 25 HIS B CE1 1 ATOM 2741 N NE2 . HIS B 2 25 ? 33.625 -11.755 -72.554 1.00 57.59 ? 25 HIS B NE2 1 ATOM 2742 N N . HIS B 2 26 ? 33.207 -15.992 -73.807 1.00 56.46 ? 26 HIS B N 1 ATOM 2743 C CA . HIS B 2 26 ? 33.212 -16.238 -75.256 1.00 59.46 ? 26 HIS B CA 1 ATOM 2744 C C . HIS B 2 26 ? 33.048 -14.956 -76.058 1.00 62.01 ? 26 HIS B C 1 ATOM 2745 O O . HIS B 2 26 ? 32.473 -14.004 -75.568 1.00 62.16 ? 26 HIS B O 1 ATOM 2746 C CB . HIS B 2 26 ? 32.125 -17.240 -75.639 1.00 60.01 ? 26 HIS B CB 1 ATOM 2747 C CG . HIS B 2 26 ? 30.759 -16.679 -75.598 1.00 62.55 ? 26 HIS B CG 1 ATOM 2748 N ND1 . HIS B 2 26 ? 30.009 -16.641 -74.444 1.00 64.31 ? 26 HIS B ND1 1 ATOM 2749 C CD2 . HIS B 2 26 ? 30.001 -16.115 -76.561 1.00 66.07 ? 26 HIS B CD2 1 ATOM 2750 C CE1 . HIS B 2 26 ? 28.838 -16.087 -74.698 1.00 65.61 ? 26 HIS B CE1 1 ATOM 2751 N NE2 . HIS B 2 26 ? 28.803 -15.766 -75.978 1.00 68.52 ? 26 HIS B NE2 1 ATOM 2752 N N . SER B 2 27 ? 33.563 -14.962 -77.285 1.00 64.69 ? 27 SER B N 1 ATOM 2753 C CA . SER B 2 27 ? 33.495 -13.834 -78.234 1.00 67.42 ? 27 SER B CA 1 ATOM 2754 C C . SER B 2 27 ? 33.272 -14.378 -79.627 1.00 68.78 ? 27 SER B C 1 ATOM 2755 O O . SER B 2 27 ? 34.105 -15.118 -80.135 1.00 69.24 ? 27 SER B O 1 ATOM 2756 C CB . SER B 2 27 ? 34.833 -13.095 -78.267 1.00 68.05 ? 27 SER B CB 1 ATOM 2757 O OG . SER B 2 27 ? 34.790 -11.910 -77.520 1.00 71.42 ? 27 SER B OG 1 ATOM 2758 N N . ASN B 2 28 ? 32.172 -14.018 -80.256 1.00 72.14 ? 28 ASN B N 1 ATOM 2759 C CA . ASN B 2 28 ? 31.929 -14.411 -81.629 1.00 73.68 ? 28 ASN B CA 1 ATOM 2760 C C . ASN B 2 28 ? 31.049 -13.354 -82.291 1.00 78.10 ? 28 ASN B C 1 ATOM 2761 O O . ASN B 2 28 ? 30.784 -12.315 -81.685 1.00 78.90 ? 28 ASN B O 1 ATOM 2762 C CB . ASN B 2 28 ? 31.328 -15.820 -81.671 1.00 73.86 ? 28 ASN B CB 1 ATOM 2763 C CG . ASN B 2 28 ? 29.967 -15.899 -81.027 1.00 74.24 ? 28 ASN B CG 1 ATOM 2764 O OD1 . ASN B 2 28 ? 29.286 -14.899 -80.902 1.00 78.10 ? 28 ASN B OD1 1 ATOM 2765 N ND2 . ASN B 2 28 ? 29.551 -17.098 -80.642 1.00 73.56 ? 28 ASN B ND2 1 ATOM 2766 N N . GLU B 2 29 ? 30.604 -13.593 -83.517 1.00 80.63 ? 29 GLU B N 1 ATOM 2767 C CA . GLU B 2 29 ? 29.892 -12.564 -84.238 1.00 86.07 ? 29 GLU B CA 1 ATOM 2768 C C . GLU B 2 29 ? 28.540 -12.229 -83.590 1.00 88.16 ? 29 GLU B C 1 ATOM 2769 O O . GLU B 2 29 ? 27.980 -11.159 -83.836 1.00 89.43 ? 29 GLU B O 1 ATOM 2770 C CB . GLU B 2 29 ? 29.671 -12.975 -85.699 1.00 91.51 ? 29 GLU B CB 1 ATOM 2771 C CG . GLU B 2 29 ? 30.949 -13.204 -86.499 1.00 92.13 ? 29 GLU B CG 1 ATOM 2772 C CD . GLU B 2 29 ? 30.713 -13.335 -88.009 1.00 97.58 ? 29 GLU B CD 1 ATOM 2773 O OE1 . GLU B 2 29 ? 29.609 -13.002 -88.523 1.00 99.44 ? 29 GLU B OE1 1 ATOM 2774 O OE2 . GLU B 2 29 ? 31.659 -13.780 -88.696 1.00 100.44 ? 29 GLU B OE2 1 ATOM 2775 N N . GLN B 2 30 ? 28.001 -13.143 -82.790 1.00 87.52 ? 30 GLN B N 1 ATOM 2776 C CA . GLN B 2 30 ? 26.701 -12.914 -82.153 1.00 90.60 ? 30 GLN B CA 1 ATOM 2777 C C . GLN B 2 30 ? 26.828 -12.109 -80.864 1.00 85.43 ? 30 GLN B C 1 ATOM 2778 O O . GLN B 2 30 ? 25.829 -11.621 -80.336 1.00 87.47 ? 30 GLN B O 1 ATOM 2779 C CB . GLN B 2 30 ? 25.989 -14.239 -81.857 1.00 94.61 ? 30 GLN B CB 1 ATOM 2780 C CG . GLN B 2 30 ? 25.571 -15.048 -83.084 1.00 99.19 ? 30 GLN B CG 1 ATOM 2781 C CD . GLN B 2 30 ? 25.528 -16.554 -82.794 1.00 101.26 ? 30 GLN B CD 1 ATOM 2782 O OE1 . GLN B 2 30 ? 26.544 -17.167 -82.436 1.00 97.01 ? 30 GLN B OE1 1 ATOM 2783 N NE2 . GLN B 2 30 ? 24.349 -17.156 -82.952 1.00 106.36 ? 30 GLN B NE2 1 ATOM 2784 N N . GLY B 2 31 ? 28.045 -11.971 -80.360 1.00 79.04 ? 31 GLY B N 1 ATOM 2785 C CA . GLY B 2 31 ? 28.275 -11.227 -79.133 1.00 76.28 ? 31 GLY B CA 1 ATOM 2786 C C . GLY B 2 31 ? 29.319 -11.835 -78.220 1.00 70.37 ? 31 GLY B C 1 ATOM 2787 O O . GLY B 2 31 ? 30.244 -12.497 -78.670 1.00 69.39 ? 31 GLY B O 1 ATOM 2788 N N . SER B 2 32 ? 29.174 -11.596 -76.925 1.00 67.30 ? 32 SER B N 1 ATOM 2789 C CA . SER B 2 32 ? 30.142 -12.087 -75.961 1.00 62.72 ? 32 SER B CA 1 ATOM 2790 C C . SER B 2 32 ? 29.539 -12.201 -74.583 1.00 61.86 ? 32 SER B C 1 ATOM 2791 O O . SER B 2 32 ? 28.481 -11.651 -74.319 1.00 64.42 ? 32 SER B O 1 ATOM 2792 C CB . SER B 2 32 ? 31.360 -11.169 -75.916 1.00 61.68 ? 32 SER B CB 1 ATOM 2793 O OG . SER B 2 32 ? 31.026 -9.922 -75.369 1.00 62.60 ? 32 SER B OG 1 ATOM 2794 N N . GLY B 2 33 ? 30.195 -12.947 -73.707 1.00 59.67 ? 33 GLY B N 1 ATOM 2795 C CA . GLY B 2 33 ? 29.757 -12.990 -72.326 1.00 60.78 ? 33 GLY B CA 1 ATOM 2796 C C . GLY B 2 33 ? 30.404 -14.019 -71.438 1.00 58.38 ? 33 GLY B C 1 ATOM 2797 O O . GLY B 2 33 ? 31.242 -14.794 -71.871 1.00 59.42 ? 33 GLY B O 1 ATOM 2798 N N . TYR B 2 34 ? 30.001 -14.006 -70.174 1.00 60.26 ? 34 TYR B N 1 ATOM 2799 C CA . TYR B 2 34 ? 30.567 -14.881 -69.155 1.00 57.15 ? 34 TYR B CA 1 ATOM 2800 C C . TYR B 2 34 ? 29.600 -15.984 -68.814 1.00 58.93 ? 34 TYR B C 1 ATOM 2801 O O . TYR B 2 34 ? 28.379 -15.786 -68.802 1.00 61.98 ? 34 TYR B O 1 ATOM 2802 C CB . TYR B 2 34 ? 30.886 -14.097 -67.894 1.00 56.53 ? 34 TYR B CB 1 ATOM 2803 C CG . TYR B 2 34 ? 31.840 -12.943 -68.101 1.00 56.68 ? 34 TYR B CG 1 ATOM 2804 C CD1 . TYR B 2 34 ? 33.212 -13.125 -68.038 1.00 54.63 ? 34 TYR B CD1 1 ATOM 2805 C CD2 . TYR B 2 34 ? 31.365 -11.664 -68.338 1.00 60.82 ? 34 TYR B CD2 1 ATOM 2806 C CE1 . TYR B 2 34 ? 34.082 -12.062 -68.225 1.00 55.69 ? 34 TYR B CE1 1 ATOM 2807 C CE2 . TYR B 2 34 ? 32.227 -10.596 -68.525 1.00 60.94 ? 34 TYR B CE2 1 ATOM 2808 C CZ . TYR B 2 34 ? 33.578 -10.801 -68.466 1.00 60.18 ? 34 TYR B CZ 1 ATOM 2809 O OH . TYR B 2 34 ? 34.431 -9.738 -68.642 1.00 63.84 ? 34 TYR B OH 1 ATOM 2810 N N . ALA B 2 35 ? 30.150 -17.159 -68.548 1.00 59.02 ? 35 ALA B N 1 ATOM 2811 C CA . ALA B 2 35 ? 29.356 -18.283 -68.070 1.00 61.41 ? 35 ALA B CA 1 ATOM 2812 C C . ALA B 2 35 ? 30.157 -19.086 -67.038 1.00 60.22 ? 35 ALA B C 1 ATOM 2813 O O . ALA B 2 35 ? 31.228 -19.608 -67.330 1.00 57.67 ? 35 ALA B O 1 ATOM 2814 C CB . ALA B 2 35 ? 28.941 -19.163 -69.229 1.00 62.59 ? 35 ALA B CB 1 ATOM 2815 N N . ALA B 2 36 ? 29.621 -19.165 -65.830 1.00 62.14 ? 36 ALA B N 1 ATOM 2816 C CA . ALA B 2 36 ? 30.198 -19.960 -64.760 1.00 61.48 ? 36 ALA B CA 1 ATOM 2817 C C . ALA B 2 36 ? 30.150 -21.460 -65.092 1.00 61.70 ? 36 ALA B C 1 ATOM 2818 O O . ALA B 2 36 ? 29.148 -21.952 -65.598 1.00 65.77 ? 36 ALA B O 1 ATOM 2819 C CB . ALA B 2 36 ? 29.434 -19.694 -63.461 1.00 64.13 ? 36 ALA B CB 1 ATOM 2820 N N . ASP B 2 37 ? 31.237 -22.167 -64.796 1.00 59.76 ? 37 ASP B N 1 ATOM 2821 C CA . ASP B 2 37 ? 31.271 -23.626 -64.817 1.00 60.96 ? 37 ASP B CA 1 ATOM 2822 C C . ASP B 2 37 ? 30.748 -24.125 -63.461 1.00 64.43 ? 37 ASP B C 1 ATOM 2823 O O . ASP B 2 37 ? 31.436 -24.044 -62.430 1.00 60.90 ? 37 ASP B O 1 ATOM 2824 C CB . ASP B 2 37 ? 32.706 -24.106 -65.030 1.00 59.78 ? 37 ASP B CB 1 ATOM 2825 C CG . ASP B 2 37 ? 32.792 -25.593 -65.237 1.00 61.26 ? 37 ASP B CG 1 ATOM 2826 O OD1 . ASP B 2 37 ? 32.427 -26.063 -66.336 1.00 63.62 ? 37 ASP B OD1 1 ATOM 2827 O OD2 . ASP B 2 37 ? 33.238 -26.291 -64.309 1.00 60.93 ? 37 ASP B OD2 1 ATOM 2828 N N . LYS B 2 38 ? 29.521 -24.627 -63.472 1.00 72.65 ? 38 LYS B N 1 ATOM 2829 C CA . LYS B 2 38 ? 28.806 -25.015 -62.259 1.00 78.08 ? 38 LYS B CA 1 ATOM 2830 C C . LYS B 2 38 ? 29.500 -26.161 -61.522 1.00 75.46 ? 38 LYS B C 1 ATOM 2831 O O . LYS B 2 38 ? 29.655 -26.116 -60.305 1.00 72.61 ? 38 LYS B O 1 ATOM 2832 C CB . LYS B 2 38 ? 27.369 -25.384 -62.623 1.00 87.47 ? 38 LYS B CB 1 ATOM 2833 C CG . LYS B 2 38 ? 26.464 -25.727 -61.447 1.00 98.17 ? 38 LYS B CG 1 ATOM 2834 C CD . LYS B 2 38 ? 26.212 -27.233 -61.298 1.00 104.01 ? 38 LYS B CD 1 ATOM 2835 C CE . LYS B 2 38 ? 25.205 -27.769 -62.316 1.00 107.71 ? 38 LYS B CE 1 ATOM 2836 N NZ . LYS B 2 38 ? 23.810 -27.326 -62.034 1.00 113.27 ? 38 LYS B NZ 1 ATOM 2837 N N . GLU B 2 39 ? 29.948 -27.165 -62.266 1.00 75.41 ? 39 GLU B N 1 ATOM 2838 C CA . GLU B 2 39 ? 30.525 -28.364 -61.665 1.00 75.39 ? 39 GLU B CA 1 ATOM 2839 C C . GLU B 2 39 ? 31.784 -28.071 -60.867 1.00 67.67 ? 39 GLU B C 1 ATOM 2840 O O . GLU B 2 39 ? 31.908 -28.522 -59.731 1.00 66.81 ? 39 GLU B O 1 ATOM 2841 C CB . GLU B 2 39 ? 30.820 -29.434 -62.729 1.00 81.30 ? 39 GLU B CB 1 ATOM 2842 C CG . GLU B 2 39 ? 31.811 -30.510 -62.276 1.00 86.39 ? 39 GLU B CG 1 ATOM 2843 C CD . GLU B 2 39 ? 31.884 -31.701 -63.216 1.00 93.93 ? 39 GLU B CD 1 ATOM 2844 O OE1 . GLU B 2 39 ? 30.920 -32.501 -63.241 1.00 99.75 ? 39 GLU B OE1 1 ATOM 2845 O OE2 . GLU B 2 39 ? 32.906 -31.837 -63.927 1.00 94.15 ? 39 GLU B OE2 1 ATOM 2846 N N . SER B 2 40 ? 32.726 -27.339 -61.460 1.00 61.63 ? 40 SER B N 1 ATOM 2847 C CA . SER B 2 40 ? 33.996 -27.111 -60.798 1.00 55.80 ? 40 SER B CA 1 ATOM 2848 C C . SER B 2 40 ? 33.813 -26.100 -59.665 1.00 54.54 ? 40 SER B C 1 ATOM 2849 O O . SER B 2 40 ? 34.507 -26.177 -58.635 1.00 50.86 ? 40 SER B O 1 ATOM 2850 C CB . SER B 2 40 ? 35.091 -26.685 -61.782 1.00 52.05 ? 40 SER B CB 1 ATOM 2851 O OG . SER B 2 40 ? 34.851 -25.413 -62.315 1.00 54.51 ? 40 SER B OG 1 ATOM 2852 N N . THR B 2 41 ? 32.874 -25.168 -59.850 1.00 52.54 ? 41 THR B N 1 ATOM 2853 C CA . THR B 2 41 ? 32.538 -24.213 -58.805 1.00 52.05 ? 41 THR B CA 1 ATOM 2854 C C . THR B 2 41 ? 31.993 -24.954 -57.588 1.00 51.80 ? 41 THR B C 1 ATOM 2855 O O . THR B 2 41 ? 32.444 -24.748 -56.473 1.00 48.56 ? 41 THR B O 1 ATOM 2856 C CB . THR B 2 41 ? 31.486 -23.168 -59.287 1.00 55.25 ? 41 THR B CB 1 ATOM 2857 O OG1 . THR B 2 41 ? 32.055 -22.320 -60.290 1.00 55.29 ? 41 THR B OG1 1 ATOM 2858 C CG2 . THR B 2 41 ? 31.029 -22.281 -58.151 1.00 57.17 ? 41 THR B CG2 1 ATOM 2859 N N . GLN B 2 42 ? 31.024 -25.826 -57.808 1.00 55.41 ? 42 GLN B N 1 ATOM 2860 C CA . GLN B 2 42 ? 30.374 -26.514 -56.694 1.00 60.00 ? 42 GLN B CA 1 ATOM 2861 C C . GLN B 2 42 ? 31.358 -27.427 -55.978 1.00 56.86 ? 42 GLN B C 1 ATOM 2862 O O . GLN B 2 42 ? 31.312 -27.556 -54.769 1.00 57.45 ? 42 GLN B O 1 ATOM 2863 C CB . GLN B 2 42 ? 29.165 -27.322 -57.171 1.00 65.53 ? 42 GLN B CB 1 ATOM 2864 C CG . GLN B 2 42 ? 28.357 -27.943 -56.046 1.00 71.76 ? 42 GLN B CG 1 ATOM 2865 C CD . GLN B 2 42 ? 27.746 -26.911 -55.107 1.00 75.89 ? 42 GLN B CD 1 ATOM 2866 O OE1 . GLN B 2 42 ? 28.032 -26.912 -53.916 1.00 80.57 ? 42 GLN B OE1 1 ATOM 2867 N NE2 . GLN B 2 42 ? 26.895 -26.036 -55.635 1.00 76.82 ? 42 GLN B NE2 1 ATOM 2868 N N . LYS B 2 43 ? 32.230 -28.067 -56.736 1.00 55.40 ? 43 LYS B N 1 ATOM 2869 C CA . LYS B 2 43 ? 33.323 -28.845 -56.160 1.00 57.68 ? 43 LYS B CA 1 ATOM 2870 C C . LYS B 2 43 ? 34.187 -28.023 -55.208 1.00 53.85 ? 43 LYS B C 1 ATOM 2871 O O . LYS B 2 43 ? 34.609 -28.516 -54.149 1.00 54.21 ? 43 LYS B O 1 ATOM 2872 C CB . LYS B 2 43 ? 34.220 -29.356 -57.278 1.00 62.33 ? 43 LYS B CB 1 ATOM 2873 C CG . LYS B 2 43 ? 34.749 -30.757 -57.060 1.00 71.21 ? 43 LYS B CG 1 ATOM 2874 C CD . LYS B 2 43 ? 34.777 -31.528 -58.375 1.00 77.28 ? 43 LYS B CD 1 ATOM 2875 C CE . LYS B 2 43 ? 35.027 -33.003 -58.145 1.00 81.49 ? 43 LYS B CE 1 ATOM 2876 N NZ . LYS B 2 43 ? 34.699 -33.718 -59.399 1.00 88.01 ? 43 LYS B NZ 1 ATOM 2877 N N . ALA B 2 44 ? 34.461 -26.780 -55.603 1.00 47.13 ? 44 ALA B N 1 ATOM 2878 C CA . ALA B 2 44 ? 35.252 -25.913 -54.794 1.00 46.52 ? 44 ALA B CA 1 ATOM 2879 C C . ALA B 2 44 ? 34.486 -25.533 -53.554 1.00 47.72 ? 44 ALA B C 1 ATOM 2880 O O . ALA B 2 44 ? 35.044 -25.482 -52.480 1.00 48.99 ? 44 ALA B O 1 ATOM 2881 C CB . ALA B 2 44 ? 35.676 -24.662 -55.570 1.00 46.34 ? 44 ALA B CB 1 ATOM 2882 N N . ILE B 2 45 ? 33.205 -25.244 -53.700 1.00 50.18 ? 45 ILE B N 1 ATOM 2883 C CA . ILE B 2 45 ? 32.398 -24.863 -52.555 1.00 53.06 ? 45 ILE B CA 1 ATOM 2884 C C . ILE B 2 45 ? 32.326 -25.990 -51.529 1.00 54.58 ? 45 ILE B C 1 ATOM 2885 O O . ILE B 2 45 ? 32.451 -25.747 -50.341 1.00 57.67 ? 45 ILE B O 1 ATOM 2886 C CB . ILE B 2 45 ? 30.988 -24.442 -52.992 1.00 57.86 ? 45 ILE B CB 1 ATOM 2887 C CG1 . ILE B 2 45 ? 31.066 -23.105 -53.727 1.00 56.63 ? 45 ILE B CG1 1 ATOM 2888 C CG2 . ILE B 2 45 ? 30.032 -24.377 -51.798 1.00 59.82 ? 45 ILE B CG2 1 ATOM 2889 C CD1 . ILE B 2 45 ? 29.739 -22.727 -54.342 1.00 62.91 ? 45 ILE B CD1 1 ATOM 2890 N N . ASP B 2 46 ? 32.133 -27.218 -51.985 1.00 55.32 ? 46 ASP B N 1 ATOM 2891 C CA . ASP B 2 46 ? 32.137 -28.384 -51.086 1.00 57.31 ? 46 ASP B CA 1 ATOM 2892 C C . ASP B 2 46 ? 33.471 -28.592 -50.366 1.00 54.37 ? 46 ASP B C 1 ATOM 2893 O O . ASP B 2 46 ? 33.496 -28.941 -49.190 1.00 57.40 ? 46 ASP B O 1 ATOM 2894 C CB . ASP B 2 46 ? 31.776 -29.662 -51.847 1.00 59.41 ? 46 ASP B CB 1 ATOM 2895 C CG . ASP B 2 46 ? 30.380 -29.613 -52.445 1.00 63.18 ? 46 ASP B CG 1 ATOM 2896 O OD1 . ASP B 2 46 ? 29.643 -28.626 -52.209 1.00 62.52 ? 46 ASP B OD1 1 ATOM 2897 O OD2 . ASP B 2 46 ? 30.032 -30.566 -53.171 1.00 67.18 ? 46 ASP B OD2 1 ATOM 2898 N N . GLY B 2 47 ? 34.574 -28.372 -51.059 1.00 50.41 ? 47 GLY B N 1 ATOM 2899 C CA . GLY B 2 47 ? 35.886 -28.593 -50.467 1.00 49.42 ? 47 GLY B CA 1 ATOM 2900 C C . GLY B 2 47 ? 36.224 -27.598 -49.378 1.00 48.58 ? 47 GLY B C 1 ATOM 2901 O O . GLY B 2 47 ? 36.595 -27.966 -48.264 1.00 48.85 ? 47 GLY B O 1 ATOM 2902 N N . VAL B 2 48 ? 36.074 -26.323 -49.701 1.00 49.41 ? 48 VAL B N 1 ATOM 2903 C CA . VAL B 2 48 ? 36.350 -25.242 -48.776 1.00 47.82 ? 48 VAL B CA 1 ATOM 2904 C C . VAL B 2 48 ? 35.407 -25.325 -47.573 1.00 50.01 ? 48 VAL B C 1 ATOM 2905 O O . VAL B 2 48 ? 35.837 -25.152 -46.449 1.00 51.66 ? 48 VAL B O 1 ATOM 2906 C CB . VAL B 2 48 ? 36.234 -23.902 -49.510 1.00 48.55 ? 48 VAL B CB 1 ATOM 2907 C CG1 . VAL B 2 48 ? 36.196 -22.737 -48.537 1.00 49.87 ? 48 VAL B CG1 1 ATOM 2908 C CG2 . VAL B 2 48 ? 37.395 -23.761 -50.498 1.00 47.34 ? 48 VAL B CG2 1 ATOM 2909 N N . THR B 2 49 ? 34.142 -25.646 -47.807 1.00 50.38 ? 49 THR B N 1 ATOM 2910 C CA . THR B 2 49 ? 33.178 -25.800 -46.728 1.00 53.42 ? 49 THR B CA 1 ATOM 2911 C C . THR B 2 49 ? 33.533 -26.944 -45.793 1.00 56.19 ? 49 THR B C 1 ATOM 2912 O O . THR B 2 49 ? 33.418 -26.817 -44.569 1.00 58.73 ? 49 THR B O 1 ATOM 2913 C CB . THR B 2 49 ? 31.768 -26.032 -47.289 1.00 55.79 ? 49 THR B CB 1 ATOM 2914 O OG1 . THR B 2 49 ? 31.427 -24.939 -48.146 1.00 53.31 ? 49 THR B OG1 1 ATOM 2915 C CG2 . THR B 2 49 ? 30.742 -26.134 -46.181 1.00 59.62 ? 49 THR B CG2 1 ATOM 2916 N N . ASN B 2 50 ? 33.965 -28.068 -46.358 1.00 56.52 ? 50 ASN B N 1 ATOM 2917 C CA . ASN B 2 50 ? 34.414 -29.189 -45.531 1.00 57.58 ? 50 ASN B CA 1 ATOM 2918 C C . ASN B 2 50 ? 35.666 -28.830 -44.744 1.00 55.73 ? 50 ASN B C 1 ATOM 2919 O O . ASN B 2 50 ? 35.801 -29.215 -43.592 1.00 57.71 ? 50 ASN B O 1 ATOM 2920 C CB . ASN B 2 50 ? 34.647 -30.438 -46.386 1.00 58.38 ? 50 ASN B CB 1 ATOM 2921 C CG . ASN B 2 50 ? 33.347 -31.046 -46.888 1.00 62.64 ? 50 ASN B CG 1 ATOM 2922 O OD1 . ASN B 2 50 ? 32.287 -30.786 -46.333 1.00 66.06 ? 50 ASN B OD1 1 ATOM 2923 N ND2 . ASN B 2 50 ? 33.421 -31.848 -47.943 1.00 62.74 ? 50 ASN B ND2 1 ATOM 2924 N N . LYS B 2 51 ? 36.573 -28.082 -45.373 1.00 52.65 ? 51 LYS B N 1 ATOM 2925 C CA . LYS B 2 51 ? 37.799 -27.614 -44.716 1.00 51.02 ? 51 LYS B CA 1 ATOM 2926 C C . LYS B 2 51 ? 37.478 -26.773 -43.479 1.00 53.01 ? 51 LYS B C 1 ATOM 2927 O O . LYS B 2 51 ? 37.975 -27.037 -42.383 1.00 55.33 ? 51 LYS B O 1 ATOM 2928 C CB . LYS B 2 51 ? 38.637 -26.794 -45.697 1.00 47.50 ? 51 LYS B CB 1 ATOM 2929 C CG . LYS B 2 51 ? 39.865 -26.178 -45.074 1.00 47.89 ? 51 LYS B CG 1 ATOM 2930 C CD . LYS B 2 51 ? 40.666 -25.400 -46.092 1.00 47.22 ? 51 LYS B CD 1 ATOM 2931 C CE . LYS B 2 51 ? 41.371 -26.334 -47.051 1.00 46.97 ? 51 LYS B CE 1 ATOM 2932 N NZ . LYS B 2 51 ? 42.587 -25.664 -47.569 1.00 47.84 ? 51 LYS B NZ 1 ATOM 2933 N N . VAL B 2 52 ? 36.613 -25.782 -43.651 1.00 51.96 ? 52 VAL B N 1 ATOM 2934 C CA . VAL B 2 52 ? 36.289 -24.894 -42.558 1.00 52.67 ? 52 VAL B CA 1 ATOM 2935 C C . VAL B 2 52 ? 35.663 -25.710 -41.414 1.00 55.40 ? 52 VAL B C 1 ATOM 2936 O O . VAL B 2 52 ? 36.082 -25.593 -40.252 1.00 57.46 ? 52 VAL B O 1 ATOM 2937 C CB . VAL B 2 52 ? 35.373 -23.734 -43.026 1.00 53.09 ? 52 VAL B CB 1 ATOM 2938 C CG1 . VAL B 2 52 ? 35.090 -22.788 -41.872 1.00 56.27 ? 52 VAL B CG1 1 ATOM 2939 C CG2 . VAL B 2 52 ? 36.026 -22.962 -44.164 1.00 49.59 ? 52 VAL B CG2 1 ATOM 2940 N N . ASN B 2 53 ? 34.702 -26.565 -41.737 1.00 56.27 ? 53 ASN B N 1 ATOM 2941 C CA . ASN B 2 53 ? 34.067 -27.404 -40.715 1.00 60.58 ? 53 ASN B CA 1 ATOM 2942 C C . ASN B 2 53 ? 35.040 -28.392 -40.062 1.00 60.57 ? 53 ASN B C 1 ATOM 2943 O O . ASN B 2 53 ? 34.959 -28.633 -38.876 1.00 62.86 ? 53 ASN B O 1 ATOM 2944 C CB . ASN B 2 53 ? 32.861 -28.145 -41.290 1.00 63.77 ? 53 ASN B CB 1 ATOM 2945 C CG . ASN B 2 53 ? 31.730 -27.215 -41.657 1.00 66.57 ? 53 ASN B CG 1 ATOM 2946 O OD1 . ASN B 2 53 ? 31.573 -26.159 -41.061 1.00 69.74 ? 53 ASN B OD1 1 ATOM 2947 N ND2 . ASN B 2 53 ? 30.922 -27.611 -42.626 1.00 68.66 ? 53 ASN B ND2 1 ATOM 2948 N N . SER B 2 54 ? 35.965 -28.944 -40.843 1.00 59.36 ? 54 SER B N 1 ATOM 2949 C CA . SER B 2 54 ? 37.028 -29.784 -40.301 1.00 60.46 ? 54 SER B CA 1 ATOM 2950 C C . SER B 2 54 ? 37.870 -28.994 -39.315 1.00 60.96 ? 54 SER B C 1 ATOM 2951 O O . SER B 2 54 ? 38.197 -29.501 -38.240 1.00 61.16 ? 54 SER B O 1 ATOM 2952 C CB . SER B 2 54 ? 37.944 -30.345 -41.414 1.00 58.33 ? 54 SER B CB 1 ATOM 2953 O OG . SER B 2 54 ? 37.355 -31.452 -42.070 1.00 60.33 ? 54 SER B OG 1 ATOM 2954 N N . ILE B 2 55 ? 38.236 -27.765 -39.696 1.00 60.11 ? 55 ILE B N 1 ATOM 2955 C CA . ILE B 2 55 ? 39.062 -26.916 -38.842 1.00 61.63 ? 55 ILE B CA 1 ATOM 2956 C C . ILE B 2 55 ? 38.342 -26.560 -37.554 1.00 67.02 ? 55 ILE B C 1 ATOM 2957 O O . ILE B 2 55 ? 38.901 -26.699 -36.471 1.00 70.39 ? 55 ILE B O 1 ATOM 2958 C CB . ILE B 2 55 ? 39.482 -25.629 -39.576 1.00 62.23 ? 55 ILE B CB 1 ATOM 2959 C CG1 . ILE B 2 55 ? 40.570 -25.968 -40.589 1.00 59.22 ? 55 ILE B CG1 1 ATOM 2960 C CG2 . ILE B 2 55 ? 39.978 -24.567 -38.598 1.00 65.18 ? 55 ILE B CG2 1 ATOM 2961 C CD1 . ILE B 2 55 ? 40.968 -24.833 -41.476 1.00 58.27 ? 55 ILE B CD1 1 ATOM 2962 N N . ILE B 2 56 ? 37.102 -26.102 -37.663 1.00 69.32 ? 56 ILE B N 1 ATOM 2963 C CA . ILE B 2 56 ? 36.324 -25.773 -36.478 1.00 72.21 ? 56 ILE B CA 1 ATOM 2964 C C . ILE B 2 56 ? 36.227 -26.997 -35.566 1.00 77.91 ? 56 ILE B C 1 ATOM 2965 O O . ILE B 2 56 ? 36.435 -26.895 -34.350 1.00 82.01 ? 56 ILE B O 1 ATOM 2966 C CB . ILE B 2 56 ? 34.904 -25.334 -36.863 1.00 74.61 ? 56 ILE B CB 1 ATOM 2967 C CG1 . ILE B 2 56 ? 34.937 -24.005 -37.621 1.00 72.70 ? 56 ILE B CG1 1 ATOM 2968 C CG2 . ILE B 2 56 ? 34.008 -25.240 -35.631 1.00 79.05 ? 56 ILE B CG2 1 ATOM 2969 C CD1 . ILE B 2 56 ? 33.605 -23.647 -38.241 1.00 74.94 ? 56 ILE B CD1 1 ATOM 2970 N N . ASP B 2 57 ? 35.909 -28.151 -36.156 1.00 79.53 ? 57 ASP B N 1 ATOM 2971 C CA . ASP B 2 57 ? 35.618 -29.373 -35.391 1.00 83.73 ? 57 ASP B CA 1 ATOM 2972 C C . ASP B 2 57 ? 36.841 -29.909 -34.633 1.00 82.39 ? 57 ASP B C 1 ATOM 2973 O O . ASP B 2 57 ? 36.736 -30.308 -33.483 1.00 83.40 ? 57 ASP B O 1 ATOM 2974 C CB . ASP B 2 57 ? 35.058 -30.458 -36.318 1.00 84.70 ? 57 ASP B CB 1 ATOM 2975 C CG . ASP B 2 57 ? 34.708 -31.730 -35.575 1.00 91.48 ? 57 ASP B CG 1 ATOM 2976 O OD1 . ASP B 2 57 ? 33.816 -31.679 -34.691 1.00 98.87 ? 57 ASP B OD1 1 ATOM 2977 O OD2 . ASP B 2 57 ? 35.325 -32.780 -35.864 1.00 91.36 ? 57 ASP B OD2 1 ATOM 2978 N N . LYS B 2 58 ? 37.997 -29.904 -35.288 1.00 78.80 ? 58 LYS B N 1 ATOM 2979 C CA . LYS B 2 58 ? 39.234 -30.370 -34.676 1.00 78.92 ? 58 LYS B CA 1 ATOM 2980 C C . LYS B 2 58 ? 39.621 -29.557 -33.448 1.00 82.46 ? 58 LYS B C 1 ATOM 2981 O O . LYS B 2 58 ? 40.206 -30.096 -32.516 1.00 83.12 ? 58 LYS B O 1 ATOM 2982 C CB . LYS B 2 58 ? 40.375 -30.373 -35.716 1.00 76.65 ? 58 LYS B CB 1 ATOM 2983 C CG . LYS B 2 58 ? 40.792 -31.753 -36.237 1.00 77.25 ? 58 LYS B CG 1 ATOM 2984 C CD . LYS B 2 58 ? 39.815 -32.859 -35.848 1.00 80.90 ? 58 LYS B CD 1 ATOM 2985 C CE . LYS B 2 58 ? 39.990 -34.087 -36.706 1.00 81.31 ? 58 LYS B CE 1 ATOM 2986 N NZ . LYS B 2 58 ? 39.294 -35.272 -36.132 1.00 85.27 ? 58 LYS B NZ 1 ATOM 2987 N N . MET B 2 59 ? 39.272 -28.276 -33.438 1.00 84.90 ? 59 MET B N 1 ATOM 2988 C CA . MET B 2 59 ? 39.551 -27.406 -32.298 1.00 89.22 ? 59 MET B CA 1 ATOM 2989 C C . MET B 2 59 ? 38.488 -27.520 -31.191 1.00 95.93 ? 59 MET B C 1 ATOM 2990 O O . MET B 2 59 ? 38.654 -26.936 -30.128 1.00 99.57 ? 59 MET B O 1 ATOM 2991 C CB . MET B 2 59 ? 39.667 -25.956 -32.763 1.00 89.04 ? 59 MET B CB 1 ATOM 2992 C CG . MET B 2 59 ? 40.616 -25.736 -33.939 1.00 85.37 ? 59 MET B CG 1 ATOM 2993 S SD . MET B 2 59 ? 42.375 -25.998 -33.629 1.00 86.04 ? 59 MET B SD 1 ATOM 2994 C CE . MET B 2 59 ? 42.618 -25.272 -32.007 1.00 90.26 ? 59 MET B CE 1 ATOM 2995 N N . ASN B 2 60 ? 37.415 -28.277 -31.444 1.00 99.84 ? 60 ASN B N 1 ATOM 2996 C CA . ASN B 2 60 ? 36.340 -28.541 -30.463 1.00 104.88 ? 60 ASN B CA 1 ATOM 2997 C C . ASN B 2 60 ? 36.851 -28.964 -29.081 1.00 106.08 ? 60 ASN B C 1 ATOM 2998 O O . ASN B 2 60 ? 36.578 -28.300 -28.080 1.00 107.05 ? 60 ASN B O 1 ATOM 2999 C CB . ASN B 2 60 ? 35.377 -29.604 -31.023 1.00 107.50 ? 60 ASN B CB 1 ATOM 3000 C CG . ASN B 2 60 ? 34.211 -29.900 -30.097 1.00 116.63 ? 60 ASN B CG 1 ATOM 3001 O OD1 . ASN B 2 60 ? 34.125 -30.984 -29.517 1.00 120.10 ? 60 ASN B OD1 1 ATOM 3002 N ND2 . ASN B 2 60 ? 33.303 -28.939 -29.957 1.00 120.20 ? 60 ASN B ND2 1 ATOM 3003 N N . THR B 2 61 ? 37.572 -30.078 -29.021 1.00 122.38 ? 61 THR B N 1 ATOM 3004 C CA . THR B 2 61 ? 38.220 -30.467 -27.784 1.00 117.13 ? 61 THR B CA 1 ATOM 3005 C C . THR B 2 61 ? 39.488 -29.653 -27.732 1.00 110.69 ? 61 THR B C 1 ATOM 3006 O O . THR B 2 61 ? 40.268 -29.653 -28.682 1.00 113.25 ? 61 THR B O 1 ATOM 3007 C CB . THR B 2 61 ? 38.587 -31.958 -27.710 1.00 120.96 ? 61 THR B CB 1 ATOM 3008 O OG1 . THR B 2 61 ? 37.484 -32.768 -28.142 1.00 128.28 ? 61 THR B OG1 1 ATOM 3009 C CG2 . THR B 2 61 ? 38.951 -32.327 -26.275 1.00 118.61 ? 61 THR B CG2 1 ATOM 3010 N N . GLN B 2 62 ? 39.672 -28.956 -26.623 1.00 103.21 ? 62 GLN B N 1 ATOM 3011 C CA . GLN B 2 62 ? 40.796 -28.055 -26.436 1.00 98.43 ? 62 GLN B CA 1 ATOM 3012 C C . GLN B 2 62 ? 40.770 -27.530 -24.989 1.00 94.33 ? 62 GLN B C 1 ATOM 3013 O O . GLN B 2 62 ? 39.691 -27.387 -24.394 1.00 99.16 ? 62 GLN B O 1 ATOM 3014 C CB . GLN B 2 62 ? 40.731 -26.901 -27.444 1.00 99.55 ? 62 GLN B CB 1 ATOM 3015 C CG . GLN B 2 62 ? 41.487 -25.641 -27.023 1.00 96.05 ? 62 GLN B CG 1 ATOM 3016 C CD . GLN B 2 62 ? 41.487 -24.563 -28.090 1.00 98.39 ? 62 GLN B CD 1 ATOM 3017 O OE1 . GLN B 2 62 ? 41.191 -24.822 -29.257 1.00 101.63 ? 62 GLN B OE1 1 ATOM 3018 N NE2 . GLN B 2 62 ? 41.817 -23.340 -27.689 1.00 96.61 ? 62 GLN B NE2 1 ATOM 3019 N N . PHE B 2 63 ? 41.950 -27.232 -24.454 1.00 86.10 ? 63 PHE B N 1 ATOM 3020 C CA . PHE B 2 63 ? 42.124 -26.874 -23.043 1.00 82.11 ? 63 PHE B CA 1 ATOM 3021 C C . PHE B 2 63 ? 41.237 -25.716 -22.554 1.00 84.42 ? 63 PHE B C 1 ATOM 3022 O O . PHE B 2 63 ? 41.067 -24.706 -23.240 1.00 88.96 ? 63 PHE B O 1 ATOM 3023 C CB . PHE B 2 63 ? 43.587 -26.540 -22.769 1.00 75.45 ? 63 PHE B CB 1 ATOM 3024 C CG . PHE B 2 63 ? 43.903 -26.388 -21.322 1.00 71.65 ? 63 PHE B CG 1 ATOM 3025 C CD1 . PHE B 2 63 ? 44.116 -27.507 -20.524 1.00 69.75 ? 63 PHE B CD1 1 ATOM 3026 C CD2 . PHE B 2 63 ? 43.987 -25.121 -20.740 1.00 70.43 ? 63 PHE B CD2 1 ATOM 3027 C CE1 . PHE B 2 63 ? 44.398 -27.368 -19.175 1.00 66.40 ? 63 PHE B CE1 1 ATOM 3028 C CE2 . PHE B 2 63 ? 44.272 -24.978 -19.386 1.00 66.15 ? 63 PHE B CE2 1 ATOM 3029 C CZ . PHE B 2 63 ? 44.472 -26.100 -18.608 1.00 64.62 ? 63 PHE B CZ 1 ATOM 3030 N N . GLU B 2 64 ? 40.670 -25.896 -21.363 1.00 84.77 ? 64 GLU B N 1 ATOM 3031 C CA . GLU B 2 64 ? 39.841 -24.892 -20.705 1.00 87.38 ? 64 GLU B CA 1 ATOM 3032 C C . GLU B 2 64 ? 40.444 -24.569 -19.345 1.00 83.70 ? 64 GLU B C 1 ATOM 3033 O O . GLU B 2 64 ? 40.690 -25.465 -18.534 1.00 81.28 ? 64 GLU B O 1 ATOM 3034 C CB . GLU B 2 64 ? 38.415 -25.417 -20.513 1.00 92.36 ? 64 GLU B CB 1 ATOM 3035 C CG . GLU B 2 64 ? 37.720 -25.860 -21.795 1.00 97.91 ? 64 GLU B CG 1 ATOM 3036 C CD . GLU B 2 64 ? 36.279 -26.296 -21.556 1.00 106.36 ? 64 GLU B CD 1 ATOM 3037 O OE1 . GLU B 2 64 ? 35.802 -26.162 -20.405 1.00 109.79 ? 64 GLU B OE1 1 ATOM 3038 O OE2 . GLU B 2 64 ? 35.618 -26.769 -22.511 1.00 108.58 ? 64 GLU B OE2 1 ATOM 3039 N N . ALA B 2 65 ? 40.681 -23.288 -19.089 1.00 84.48 ? 65 ALA B N 1 ATOM 3040 C CA . ALA B 2 65 ? 41.271 -22.873 -17.821 1.00 82.40 ? 65 ALA B CA 1 ATOM 3041 C C . ALA B 2 65 ? 40.217 -22.831 -16.714 1.00 86.49 ? 65 ALA B C 1 ATOM 3042 O O . ALA B 2 65 ? 39.061 -22.453 -16.955 1.00 88.78 ? 65 ALA B O 1 ATOM 3043 C CB . ALA B 2 65 ? 41.950 -21.523 -17.968 1.00 82.43 ? 65 ALA B CB 1 ATOM 3044 N N . VAL B 2 66 ? 40.634 -23.241 -15.514 1.00 86.59 ? 66 VAL B N 1 ATOM 3045 C CA . VAL B 2 66 ? 39.795 -23.216 -14.314 1.00 91.75 ? 66 VAL B CA 1 ATOM 3046 C C . VAL B 2 66 ? 40.467 -22.368 -13.244 1.00 87.90 ? 66 VAL B C 1 ATOM 3047 O O . VAL B 2 66 ? 41.685 -22.424 -13.093 1.00 84.54 ? 66 VAL B O 1 ATOM 3048 C CB . VAL B 2 66 ? 39.577 -24.632 -13.729 1.00 94.77 ? 66 VAL B CB 1 ATOM 3049 C CG1 . VAL B 2 66 ? 38.521 -24.602 -12.621 1.00 100.39 ? 66 VAL B CG1 1 ATOM 3050 C CG2 . VAL B 2 66 ? 39.166 -25.614 -14.824 1.00 97.94 ? 66 VAL B CG2 1 ATOM 3051 N N . GLY B 2 67 ? 39.667 -21.613 -12.489 1.00 89.83 ? 67 GLY B N 1 ATOM 3052 C CA . GLY B 2 67 ? 40.167 -20.839 -11.349 1.00 88.20 ? 67 GLY B CA 1 ATOM 3053 C C . GLY B 2 67 ? 40.596 -21.710 -10.173 1.00 84.46 ? 67 GLY B C 1 ATOM 3054 O O . GLY B 2 67 ? 39.844 -22.564 -9.714 1.00 85.24 ? 67 GLY B O 1 ATOM 3055 N N . ARG B 2 68 ? 41.816 -21.496 -9.694 1.00 78.66 ? 68 ARG B N 1 ATOM 3056 C CA . ARG B 2 68 ? 42.339 -22.209 -8.532 1.00 76.50 ? 68 ARG B CA 1 ATOM 3057 C C . ARG B 2 68 ? 43.085 -21.221 -7.665 1.00 75.82 ? 68 ARG B C 1 ATOM 3058 O O . ARG B 2 68 ? 43.932 -20.480 -8.161 1.00 77.67 ? 68 ARG B O 1 ATOM 3059 C CB . ARG B 2 68 ? 43.317 -23.291 -8.960 1.00 72.31 ? 68 ARG B CB 1 ATOM 3060 C CG . ARG B 2 68 ? 42.681 -24.557 -9.494 1.00 72.96 ? 68 ARG B CG 1 ATOM 3061 C CD . ARG B 2 68 ? 43.726 -25.603 -9.864 1.00 67.74 ? 68 ARG B CD 1 ATOM 3062 N NE . ARG B 2 68 ? 43.190 -26.401 -10.944 1.00 69.44 ? 68 ARG B NE 1 ATOM 3063 C CZ . ARG B 2 68 ? 43.327 -26.112 -12.234 1.00 69.28 ? 68 ARG B CZ 1 ATOM 3064 N NH1 . ARG B 2 68 ? 44.070 -25.093 -12.646 1.00 66.78 ? 68 ARG B NH1 1 ATOM 3065 N NH2 . ARG B 2 68 ? 42.729 -26.873 -13.136 1.00 73.63 ? 68 ARG B NH2 1 ATOM 3066 N N . GLU B 2 69 ? 42.816 -21.227 -6.368 1.00 76.63 ? 69 GLU B N 1 ATOM 3067 C CA . GLU B 2 69 ? 43.411 -20.236 -5.489 1.00 75.28 ? 69 GLU B CA 1 ATOM 3068 C C . GLU B 2 69 ? 44.364 -20.869 -4.518 1.00 69.86 ? 69 GLU B C 1 ATOM 3069 O O . GLU B 2 69 ? 44.186 -22.005 -4.113 1.00 67.35 ? 69 GLU B O 1 ATOM 3070 C CB . GLU B 2 69 ? 42.326 -19.448 -4.766 1.00 83.33 ? 69 GLU B CB 1 ATOM 3071 C CG . GLU B 2 69 ? 41.800 -18.315 -5.621 1.00 88.60 ? 69 GLU B CG 1 ATOM 3072 C CD . GLU B 2 69 ? 40.435 -17.852 -5.198 1.00 98.63 ? 69 GLU B CD 1 ATOM 3073 O OE1 . GLU B 2 69 ? 39.437 -18.479 -5.631 1.00 103.96 ? 69 GLU B OE1 1 ATOM 3074 O OE2 . GLU B 2 69 ? 40.366 -16.868 -4.433 1.00 103.88 ? 69 GLU B OE2 1 ATOM 3075 N N . PHE B 2 70 ? 45.392 -20.111 -4.163 1.00 68.74 ? 70 PHE B N 1 ATOM 3076 C CA . PHE B 2 70 ? 46.450 -20.587 -3.288 1.00 65.86 ? 70 PHE B CA 1 ATOM 3077 C C . PHE B 2 70 ? 46.836 -19.526 -2.275 1.00 67.13 ? 70 PHE B C 1 ATOM 3078 O O . PHE B 2 70 ? 46.703 -18.335 -2.531 1.00 69.01 ? 70 PHE B O 1 ATOM 3079 C CB . PHE B 2 70 ? 47.662 -20.967 -4.115 1.00 61.34 ? 70 PHE B CB 1 ATOM 3080 C CG . PHE B 2 70 ? 47.347 -21.899 -5.235 1.00 59.15 ? 70 PHE B CG 1 ATOM 3081 C CD1 . PHE B 2 70 ? 46.951 -21.401 -6.474 1.00 59.71 ? 70 PHE B CD1 1 ATOM 3082 C CD2 . PHE B 2 70 ? 47.435 -23.272 -5.057 1.00 56.21 ? 70 PHE B CD2 1 ATOM 3083 C CE1 . PHE B 2 70 ? 46.637 -22.269 -7.513 1.00 58.27 ? 70 PHE B CE1 1 ATOM 3084 C CE2 . PHE B 2 70 ? 47.138 -24.135 -6.096 1.00 55.48 ? 70 PHE B CE2 1 ATOM 3085 C CZ . PHE B 2 70 ? 46.735 -23.635 -7.323 1.00 55.47 ? 70 PHE B CZ 1 ATOM 3086 N N . ASN B 2 71 ? 47.299 -19.968 -1.115 1.00 67.47 ? 71 ASN B N 1 ATOM 3087 C CA . ASN B 2 71 ? 47.653 -19.041 -0.044 1.00 71.18 ? 71 ASN B CA 1 ATOM 3088 C C . ASN B 2 71 ? 49.106 -18.582 -0.189 1.00 67.61 ? 71 ASN B C 1 ATOM 3089 O O . ASN B 2 71 ? 49.800 -18.990 -1.116 1.00 61.81 ? 71 ASN B O 1 ATOM 3090 C CB . ASN B 2 71 ? 47.340 -19.638 1.353 1.00 74.08 ? 71 ASN B CB 1 ATOM 3091 C CG . ASN B 2 71 ? 48.317 -20.729 1.779 1.00 71.72 ? 71 ASN B CG 1 ATOM 3092 O OD1 . ASN B 2 71 ? 49.522 -20.625 1.570 1.00 68.91 ? 71 ASN B OD1 1 ATOM 3093 N ND2 . ASN B 2 71 ? 47.792 -21.779 2.397 1.00 74.82 ? 71 ASN B ND2 1 ATOM 3094 N N . ASN B 2 72 ? 49.554 -17.745 0.741 1.00 71.70 ? 72 ASN B N 1 ATOM 3095 C CA . ASN B 2 72 ? 50.860 -17.100 0.648 1.00 72.03 ? 72 ASN B CA 1 ATOM 3096 C C . ASN B 2 72 ? 52.077 -18.041 0.723 1.00 67.54 ? 72 ASN B C 1 ATOM 3097 O O . ASN B 2 72 ? 53.164 -17.674 0.283 1.00 66.05 ? 72 ASN B O 1 ATOM 3098 C CB . ASN B 2 72 ? 50.976 -16.037 1.728 1.00 78.59 ? 72 ASN B CB 1 ATOM 3099 C CG . ASN B 2 72 ? 52.120 -15.088 1.475 1.00 82.71 ? 72 ASN B CG 1 ATOM 3100 O OD1 . ASN B 2 72 ? 52.399 -14.733 0.330 1.00 84.89 ? 72 ASN B OD1 1 ATOM 3101 N ND2 . ASN B 2 72 ? 52.791 -14.667 2.539 1.00 86.39 ? 72 ASN B ND2 1 ATOM 3102 N N . LEU B 2 73 ? 51.896 -19.229 1.301 1.00 65.39 ? 73 LEU B N 1 ATOM 3103 C CA . LEU B 2 73 ? 52.948 -20.242 1.381 1.00 62.71 ? 73 LEU B CA 1 ATOM 3104 C C . LEU B 2 73 ? 52.628 -21.452 0.484 1.00 59.87 ? 73 LEU B C 1 ATOM 3105 O O . LEU B 2 73 ? 53.053 -22.575 0.749 1.00 57.79 ? 73 LEU B O 1 ATOM 3106 C CB . LEU B 2 73 ? 53.152 -20.672 2.841 1.00 65.72 ? 73 LEU B CB 1 ATOM 3107 C CG . LEU B 2 73 ? 53.769 -19.634 3.809 1.00 69.16 ? 73 LEU B CG 1 ATOM 3108 C CD1 . LEU B 2 73 ? 53.720 -20.130 5.247 1.00 71.32 ? 73 LEU B CD1 1 ATOM 3109 C CD2 . LEU B 2 73 ? 55.200 -19.290 3.421 1.00 68.12 ? 73 LEU B CD2 1 ATOM 3110 N N . GLU B 2 74 ? 51.892 -21.200 -0.592 1.00 58.92 ? 74 GLU B N 1 ATOM 3111 C CA . GLU B 2 74 ? 51.669 -22.181 -1.637 1.00 57.34 ? 74 GLU B CA 1 ATOM 3112 C C . GLU B 2 74 ? 52.095 -21.602 -2.985 1.00 57.05 ? 74 GLU B C 1 ATOM 3113 O O . GLU B 2 74 ? 51.464 -21.877 -4.009 1.00 55.44 ? 74 GLU B O 1 ATOM 3114 C CB . GLU B 2 74 ? 50.191 -22.556 -1.677 1.00 57.68 ? 74 GLU B CB 1 ATOM 3115 C CG . GLU B 2 74 ? 49.746 -23.419 -0.527 1.00 58.08 ? 74 GLU B CG 1 ATOM 3116 C CD . GLU B 2 74 ? 48.279 -23.725 -0.600 1.00 60.98 ? 74 GLU B CD 1 ATOM 3117 O OE1 . GLU B 2 74 ? 47.502 -22.832 -0.982 1.00 63.58 ? 74 GLU B OE1 1 ATOM 3118 O OE2 . GLU B 2 74 ? 47.888 -24.856 -0.279 1.00 63.64 ? 74 GLU B OE2 1 ATOM 3119 N N . ARG B 2 75 ? 53.156 -20.790 -2.975 1.00 57.67 ? 75 ARG B N 1 ATOM 3120 C CA . ARG B 2 75 ? 53.611 -20.097 -4.169 1.00 57.04 ? 75 ARG B CA 1 ATOM 3121 C C . ARG B 2 75 ? 54.123 -21.050 -5.231 1.00 54.92 ? 75 ARG B C 1 ATOM 3122 O O . ARG B 2 75 ? 54.007 -20.772 -6.418 1.00 54.27 ? 75 ARG B O 1 ATOM 3123 C CB . ARG B 2 75 ? 54.728 -19.099 -3.837 1.00 61.44 ? 75 ARG B CB 1 ATOM 3124 C CG . ARG B 2 75 ? 54.319 -17.911 -2.983 1.00 67.79 ? 75 ARG B CG 1 ATOM 3125 C CD . ARG B 2 75 ? 53.231 -17.100 -3.659 1.00 72.78 ? 75 ARG B CD 1 ATOM 3126 N NE . ARG B 2 75 ? 52.701 -16.044 -2.804 1.00 82.97 ? 75 ARG B NE 1 ATOM 3127 C CZ . ARG B 2 75 ? 51.589 -15.355 -3.064 1.00 91.20 ? 75 ARG B CZ 1 ATOM 3128 N NH1 . ARG B 2 75 ? 50.878 -15.608 -4.167 1.00 91.96 ? 75 ARG B NH1 1 ATOM 3129 N NH2 . ARG B 2 75 ? 51.179 -14.405 -2.221 1.00 96.94 ? 75 ARG B NH2 1 ATOM 3130 N N . ARG B 2 76 ? 54.730 -22.159 -4.824 1.00 54.66 ? 76 ARG B N 1 ATOM 3131 C CA . ARG B 2 76 ? 55.306 -23.063 -5.814 1.00 52.22 ? 76 ARG B CA 1 ATOM 3132 C C . ARG B 2 76 ? 54.217 -23.697 -6.661 1.00 50.39 ? 76 ARG B C 1 ATOM 3133 O O . ARG B 2 76 ? 54.290 -23.629 -7.879 1.00 49.42 ? 76 ARG B O 1 ATOM 3134 C CB . ARG B 2 76 ? 56.144 -24.130 -5.150 1.00 52.81 ? 76 ARG B CB 1 ATOM 3135 C CG . ARG B 2 76 ? 57.447 -23.611 -4.593 1.00 54.37 ? 76 ARG B CG 1 ATOM 3136 C CD . ARG B 2 76 ? 58.050 -24.677 -3.713 1.00 55.00 ? 76 ARG B CD 1 ATOM 3137 N NE . ARG B 2 76 ? 57.147 -25.012 -2.612 1.00 52.41 ? 76 ARG B NE 1 ATOM 3138 C CZ . ARG B 2 76 ? 57.124 -26.181 -1.984 1.00 52.41 ? 76 ARG B CZ 1 ATOM 3139 N NH1 . ARG B 2 76 ? 57.953 -27.151 -2.337 1.00 53.35 ? 76 ARG B NH1 1 ATOM 3140 N NH2 . ARG B 2 76 ? 56.247 -26.391 -1.013 1.00 51.99 ? 76 ARG B NH2 1 ATOM 3141 N N . ILE B 2 77 ? 53.213 -24.307 -6.025 1.00 50.62 ? 77 ILE B N 1 ATOM 3142 C CA . ILE B 2 77 ? 52.097 -24.875 -6.773 1.00 50.79 ? 77 ILE B CA 1 ATOM 3143 C C . ILE B 2 77 ? 51.241 -23.805 -7.464 1.00 52.85 ? 77 ILE B C 1 ATOM 3144 O O . ILE B 2 77 ? 50.696 -24.057 -8.534 1.00 53.73 ? 77 ILE B O 1 ATOM 3145 C CB . ILE B 2 77 ? 51.220 -25.840 -5.966 1.00 51.91 ? 77 ILE B CB 1 ATOM 3146 C CG1 . ILE B 2 77 ? 50.619 -25.176 -4.751 1.00 55.39 ? 77 ILE B CG1 1 ATOM 3147 C CG2 . ILE B 2 77 ? 52.020 -27.057 -5.536 1.00 53.64 ? 77 ILE B CG2 1 ATOM 3148 C CD1 . ILE B 2 77 ? 49.665 -26.094 -4.005 1.00 58.87 ? 77 ILE B CD1 1 ATOM 3149 N N . GLU B 2 78 ? 51.147 -22.606 -6.905 1.00 52.66 ? 78 GLU B N 1 ATOM 3150 C CA . GLU B 2 78 ? 50.461 -21.548 -7.622 1.00 53.91 ? 78 GLU B CA 1 ATOM 3151 C C . GLU B 2 78 ? 51.172 -21.268 -8.947 1.00 52.47 ? 78 GLU B C 1 ATOM 3152 O O . GLU B 2 78 ? 50.531 -21.010 -9.969 1.00 50.21 ? 78 GLU B O 1 ATOM 3153 C CB . GLU B 2 78 ? 50.385 -20.265 -6.806 1.00 58.84 ? 78 GLU B CB 1 ATOM 3154 C CG . GLU B 2 78 ? 49.894 -19.052 -7.587 1.00 64.68 ? 78 GLU B CG 1 ATOM 3155 C CD . GLU B 2 78 ? 49.707 -17.849 -6.696 1.00 74.31 ? 78 GLU B CD 1 ATOM 3156 O OE1 . GLU B 2 78 ? 50.663 -17.459 -5.978 1.00 78.61 ? 78 GLU B OE1 1 ATOM 3157 O OE2 . GLU B 2 78 ? 48.591 -17.300 -6.702 1.00 83.49 ? 78 GLU B OE2 1 ATOM 3158 N N . ASN B 2 79 ? 52.496 -21.303 -8.915 1.00 51.07 ? 79 ASN B N 1 ATOM 3159 C CA . ASN B 2 79 ? 53.284 -20.935 -10.068 1.00 52.08 ? 79 ASN B CA 1 ATOM 3160 C C . ASN B 2 79 ? 53.236 -22.065 -11.093 1.00 50.42 ? 79 ASN B C 1 ATOM 3161 O O . ASN B 2 79 ? 53.257 -21.836 -12.287 1.00 50.39 ? 79 ASN B O 1 ATOM 3162 C CB . ASN B 2 79 ? 54.711 -20.644 -9.641 1.00 54.59 ? 79 ASN B CB 1 ATOM 3163 C CG . ASN B 2 79 ? 55.611 -20.307 -10.808 1.00 58.71 ? 79 ASN B CG 1 ATOM 3164 O OD1 . ASN B 2 79 ? 55.513 -19.229 -11.391 1.00 63.52 ? 79 ASN B OD1 1 ATOM 3165 N ND2 . ASN B 2 79 ? 56.514 -21.205 -11.133 1.00 59.13 ? 79 ASN B ND2 1 ATOM 3166 N N . LEU B 2 80 ? 53.153 -23.285 -10.591 1.00 49.64 ? 80 LEU B N 1 ATOM 3167 C CA . LEU B 2 80 ? 53.016 -24.469 -11.404 1.00 50.60 ? 80 LEU B CA 1 ATOM 3168 C C . LEU B 2 80 ? 51.703 -24.375 -12.148 1.00 51.08 ? 80 LEU B C 1 ATOM 3169 O O . LEU B 2 80 ? 51.656 -24.540 -13.363 1.00 52.21 ? 80 LEU B O 1 ATOM 3170 C CB . LEU B 2 80 ? 53.023 -25.709 -10.507 1.00 51.13 ? 80 LEU B CB 1 ATOM 3171 C CG . LEU B 2 80 ? 53.253 -27.059 -11.167 1.00 53.31 ? 80 LEU B CG 1 ATOM 3172 C CD1 . LEU B 2 80 ? 53.364 -28.159 -10.119 1.00 54.55 ? 80 LEU B CD1 1 ATOM 3173 C CD2 . LEU B 2 80 ? 52.132 -27.355 -12.137 1.00 55.89 ? 80 LEU B CD2 1 ATOM 3174 N N . ASN B 2 81 ? 50.643 -24.087 -11.403 1.00 50.50 ? 81 ASN B N 1 ATOM 3175 C CA . ASN B 2 81 ? 49.314 -23.878 -11.967 1.00 51.17 ? 81 ASN B CA 1 ATOM 3176 C C . ASN B 2 81 ? 49.279 -22.851 -13.085 1.00 52.27 ? 81 ASN B C 1 ATOM 3177 O O . ASN B 2 81 ? 48.614 -23.046 -14.090 1.00 53.27 ? 81 ASN B O 1 ATOM 3178 C CB . ASN B 2 81 ? 48.359 -23.392 -10.896 1.00 51.83 ? 81 ASN B CB 1 ATOM 3179 C CG . ASN B 2 81 ? 46.940 -23.416 -11.369 1.00 54.47 ? 81 ASN B CG 1 ATOM 3180 O OD1 . ASN B 2 81 ? 46.447 -24.466 -11.759 1.00 56.16 ? 81 ASN B OD1 1 ATOM 3181 N ND2 . ASN B 2 81 ? 46.279 -22.270 -11.368 1.00 56.18 ? 81 ASN B ND2 1 ATOM 3182 N N . LYS B 2 82 ? 49.991 -21.753 -12.889 1.00 52.92 ? 82 LYS B N 1 ATOM 3183 C CA . LYS B 2 82 ? 49.992 -20.669 -13.838 1.00 57.88 ? 82 LYS B CA 1 ATOM 3184 C C . LYS B 2 82 ? 50.734 -21.106 -15.091 1.00 58.76 ? 82 LYS B C 1 ATOM 3185 O O . LYS B 2 82 ? 50.246 -20.918 -16.200 1.00 58.53 ? 82 LYS B O 1 ATOM 3186 C CB . LYS B 2 82 ? 50.640 -19.429 -13.228 1.00 61.94 ? 82 LYS B CB 1 ATOM 3187 C CG . LYS B 2 82 ? 50.658 -18.188 -14.128 1.00 69.35 ? 82 LYS B CG 1 ATOM 3188 C CD . LYS B 2 82 ? 51.668 -17.181 -13.570 1.00 76.13 ? 82 LYS B CD 1 ATOM 3189 C CE . LYS B 2 82 ? 51.656 -15.818 -14.259 1.00 83.66 ? 82 LYS B CE 1 ATOM 3190 N NZ . LYS B 2 82 ? 51.853 -15.901 -15.737 1.00 85.94 ? 82 LYS B NZ 1 ATOM 3191 N N . LYS B 2 83 ? 51.901 -21.712 -14.903 1.00 57.91 ? 83 LYS B N 1 ATOM 3192 C CA . LYS B 2 83 ? 52.709 -22.169 -16.033 1.00 61.05 ? 83 LYS B CA 1 ATOM 3193 C C . LYS B 2 83 ? 51.982 -23.243 -16.844 1.00 57.99 ? 83 LYS B C 1 ATOM 3194 O O . LYS B 2 83 ? 52.009 -23.244 -18.076 1.00 56.53 ? 83 LYS B O 1 ATOM 3195 C CB . LYS B 2 83 ? 54.097 -22.646 -15.573 1.00 64.12 ? 83 LYS B CB 1 ATOM 3196 C CG . LYS B 2 83 ? 55.187 -21.624 -15.877 1.00 72.36 ? 83 LYS B CG 1 ATOM 3197 C CD . LYS B 2 83 ? 55.017 -20.330 -15.082 1.00 76.94 ? 83 LYS B CD 1 ATOM 3198 C CE . LYS B 2 83 ? 54.935 -19.080 -15.960 1.00 84.65 ? 83 LYS B CE 1 ATOM 3199 N NZ . LYS B 2 83 ? 56.084 -18.910 -16.896 1.00 89.57 ? 83 LYS B NZ 1 ATOM 3200 N N . MET B 2 84 ? 51.311 -24.137 -16.139 1.00 55.79 ? 84 MET B N 1 ATOM 3201 C CA . MET B 2 84 ? 50.465 -25.124 -16.786 1.00 56.90 ? 84 MET B CA 1 ATOM 3202 C C . MET B 2 84 ? 49.383 -24.471 -17.643 1.00 55.69 ? 84 MET B C 1 ATOM 3203 O O . MET B 2 84 ? 49.292 -24.763 -18.836 1.00 55.89 ? 84 MET B O 1 ATOM 3204 C CB . MET B 2 84 ? 49.839 -26.059 -15.755 1.00 57.00 ? 84 MET B CB 1 ATOM 3205 C CG . MET B 2 84 ? 49.440 -27.394 -16.340 1.00 60.53 ? 84 MET B CG 1 ATOM 3206 S SD . MET B 2 84 ? 47.800 -27.874 -15.829 1.00 66.97 ? 84 MET B SD 1 ATOM 3207 C CE . MET B 2 84 ? 46.900 -26.492 -16.499 1.00 68.45 ? 84 MET B CE 1 ATOM 3208 N N . GLU B 2 85 ? 48.599 -23.562 -17.070 1.00 65.78 ? 85 GLU B N 1 ATOM 3209 C CA . GLU B 2 85 ? 47.479 -22.989 -17.822 1.00 64.73 ? 85 GLU B CA 1 ATOM 3210 C C . GLU B 2 85 ? 47.962 -22.181 -19.014 1.00 62.13 ? 85 GLU B C 1 ATOM 3211 O O . GLU B 2 85 ? 47.448 -22.324 -20.125 1.00 59.05 ? 85 GLU B O 1 ATOM 3212 C CB . GLU B 2 85 ? 46.533 -22.203 -16.916 1.00 69.26 ? 85 GLU B CB 1 ATOM 3213 C CG . GLU B 2 85 ? 45.889 -23.120 -15.874 1.00 73.88 ? 85 GLU B CG 1 ATOM 3214 C CD . GLU B 2 85 ? 44.436 -22.818 -15.549 1.00 79.60 ? 85 GLU B CD 1 ATOM 3215 O OE1 . GLU B 2 85 ? 44.130 -21.663 -15.178 1.00 85.45 ? 85 GLU B OE1 1 ATOM 3216 O OE2 . GLU B 2 85 ? 43.608 -23.758 -15.630 1.00 80.01 ? 85 GLU B OE2 1 ATOM 3217 N N . ASP B 2 86 ? 48.989 -21.376 -18.793 1.00 63.50 ? 86 ASP B N 1 ATOM 3218 C CA . ASP B 2 86 ? 49.610 -20.590 -19.858 1.00 63.56 ? 86 ASP B CA 1 ATOM 3219 C C . ASP B 2 86 ? 50.207 -21.430 -20.964 1.00 59.63 ? 86 ASP B C 1 ATOM 3220 O O . ASP B 2 86 ? 50.129 -21.063 -22.134 1.00 56.88 ? 86 ASP B O 1 ATOM 3221 C CB . ASP B 2 86 ? 50.739 -19.717 -19.295 1.00 68.28 ? 86 ASP B CB 1 ATOM 3222 C CG . ASP B 2 86 ? 50.307 -18.312 -19.047 1.00 73.06 ? 86 ASP B CG 1 ATOM 3223 O OD1 . ASP B 2 86 ? 49.718 -17.724 -20.001 1.00 77.24 ? 86 ASP B OD1 1 ATOM 3224 O OD2 . ASP B 2 86 ? 50.569 -17.797 -17.927 1.00 76.09 ? 86 ASP B OD2 1 ATOM 3225 N N . GLY B 2 87 ? 50.872 -22.508 -20.567 1.00 58.60 ? 87 GLY B N 1 ATOM 3226 C CA . GLY B 2 87 ? 51.521 -23.399 -21.500 1.00 57.59 ? 87 GLY B CA 1 ATOM 3227 C C . GLY B 2 87 ? 50.544 -24.002 -22.484 1.00 55.51 ? 87 GLY B C 1 ATOM 3228 O O . GLY B 2 87 ? 50.827 -24.055 -23.697 1.00 53.65 ? 87 GLY B O 1 ATOM 3229 N N . PHE B 2 88 ? 49.389 -24.444 -21.986 1.00 53.47 ? 88 PHE B N 1 ATOM 3230 C CA . PHE B 2 88 ? 48.385 -24.994 -22.875 1.00 51.75 ? 88 PHE B CA 1 ATOM 3231 C C . PHE B 2 88 ? 47.791 -23.912 -23.791 1.00 52.40 ? 88 PHE B C 1 ATOM 3232 O O . PHE B 2 88 ? 47.569 -24.169 -24.960 1.00 51.98 ? 88 PHE B O 1 ATOM 3233 C CB . PHE B 2 88 ? 47.302 -25.701 -22.090 1.00 52.56 ? 88 PHE B CB 1 ATOM 3234 C CG . PHE B 2 88 ? 47.700 -27.061 -21.585 1.00 53.99 ? 88 PHE B CG 1 ATOM 3235 C CD1 . PHE B 2 88 ? 48.032 -28.080 -22.462 1.00 53.45 ? 88 PHE B CD1 1 ATOM 3236 C CD2 . PHE B 2 88 ? 47.705 -27.336 -20.234 1.00 55.88 ? 88 PHE B CD2 1 ATOM 3237 C CE1 . PHE B 2 88 ? 48.373 -29.333 -22.001 1.00 54.37 ? 88 PHE B CE1 1 ATOM 3238 C CE2 . PHE B 2 88 ? 48.048 -28.591 -19.765 1.00 57.43 ? 88 PHE B CE2 1 ATOM 3239 C CZ . PHE B 2 88 ? 48.379 -29.586 -20.652 1.00 57.58 ? 88 PHE B CZ 1 ATOM 3240 N N . LEU B 2 89 ? 47.558 -22.700 -23.289 1.00 55.54 ? 89 LEU B N 1 ATOM 3241 C CA . LEU B 2 89 ? 47.131 -21.593 -24.166 1.00 56.78 ? 89 LEU B CA 1 ATOM 3242 C C . LEU B 2 89 ? 48.105 -21.340 -25.303 1.00 53.64 ? 89 LEU B C 1 ATOM 3243 O O . LEU B 2 89 ? 47.701 -21.112 -26.422 1.00 50.29 ? 89 LEU B O 1 ATOM 3244 C CB . LEU B 2 89 ? 47.001 -20.277 -23.418 1.00 62.62 ? 89 LEU B CB 1 ATOM 3245 C CG . LEU B 2 89 ? 46.028 -20.213 -22.252 1.00 70.13 ? 89 LEU B CG 1 ATOM 3246 C CD1 . LEU B 2 89 ? 46.106 -18.801 -21.659 1.00 74.22 ? 89 LEU B CD1 1 ATOM 3247 C CD2 . LEU B 2 89 ? 44.601 -20.626 -22.662 1.00 70.49 ? 89 LEU B CD2 1 ATOM 3248 N N . ASP B 2 90 ? 49.394 -21.351 -24.992 1.00 54.79 ? 90 ASP B N 1 ATOM 3249 C CA . ASP B 2 90 ? 50.427 -21.154 -25.995 1.00 54.34 ? 90 ASP B CA 1 ATOM 3250 C C . ASP B 2 90 ? 50.419 -22.276 -27.049 1.00 50.90 ? 90 ASP B C 1 ATOM 3251 O O . ASP B 2 90 ? 50.515 -22.025 -28.228 1.00 50.97 ? 90 ASP B O 1 ATOM 3252 C CB . ASP B 2 90 ? 51.790 -21.046 -25.323 1.00 58.29 ? 90 ASP B CB 1 ATOM 3253 C CG . ASP B 2 90 ? 51.968 -19.740 -24.576 1.00 64.65 ? 90 ASP B CG 1 ATOM 3254 O OD1 . ASP B 2 90 ? 51.153 -18.812 -24.788 1.00 65.71 ? 90 ASP B OD1 1 ATOM 3255 O OD2 . ASP B 2 90 ? 52.937 -19.637 -23.780 1.00 71.41 ? 90 ASP B OD2 1 ATOM 3256 N N . VAL B 2 91 ? 50.272 -23.509 -26.607 1.00 50.47 ? 91 VAL B N 1 ATOM 3257 C CA . VAL B 2 91 ? 50.159 -24.647 -27.497 1.00 49.21 ? 91 VAL B CA 1 ATOM 3258 C C . VAL B 2 91 ? 48.942 -24.541 -28.419 1.00 48.65 ? 91 VAL B C 1 ATOM 3259 O O . VAL B 2 91 ? 49.055 -24.778 -29.618 1.00 49.10 ? 91 VAL B O 1 ATOM 3260 C CB . VAL B 2 91 ? 50.077 -25.960 -26.688 1.00 49.95 ? 91 VAL B CB 1 ATOM 3261 C CG1 . VAL B 2 91 ? 49.660 -27.117 -27.576 1.00 49.20 ? 91 VAL B CG1 1 ATOM 3262 C CG2 . VAL B 2 91 ? 51.421 -26.252 -26.015 1.00 52.88 ? 91 VAL B CG2 1 ATOM 3263 N N . TRP B 2 92 ? 47.785 -24.187 -27.877 1.00 47.99 ? 92 TRP B N 1 ATOM 3264 C CA . TRP B 2 92 ? 46.587 -24.075 -28.706 1.00 47.06 ? 92 TRP B CA 1 ATOM 3265 C C . TRP B 2 92 ? 46.555 -22.800 -29.529 1.00 46.72 ? 92 TRP B C 1 ATOM 3266 O O . TRP B 2 92 ? 46.015 -22.787 -30.606 1.00 46.57 ? 92 TRP B O 1 ATOM 3267 C CB . TRP B 2 92 ? 45.325 -24.200 -27.863 1.00 47.71 ? 92 TRP B CB 1 ATOM 3268 C CG . TRP B 2 92 ? 45.119 -25.604 -27.385 1.00 49.94 ? 92 TRP B CG 1 ATOM 3269 C CD1 . TRP B 2 92 ? 45.272 -26.065 -26.110 1.00 52.44 ? 92 TRP B CD1 1 ATOM 3270 C CD2 . TRP B 2 92 ? 44.746 -26.737 -28.170 1.00 49.98 ? 92 TRP B CD2 1 ATOM 3271 N NE1 . TRP B 2 92 ? 44.984 -27.404 -26.046 1.00 53.41 ? 92 TRP B NE1 1 ATOM 3272 C CE2 . TRP B 2 92 ? 44.664 -27.843 -27.300 1.00 52.23 ? 92 TRP B CE2 1 ATOM 3273 C CE3 . TRP B 2 92 ? 44.454 -26.924 -29.518 1.00 50.16 ? 92 TRP B CE3 1 ATOM 3274 C CZ2 . TRP B 2 92 ? 44.307 -29.115 -27.736 1.00 54.51 ? 92 TRP B CZ2 1 ATOM 3275 C CZ3 . TRP B 2 92 ? 44.087 -28.192 -29.947 1.00 51.21 ? 92 TRP B CZ3 1 ATOM 3276 C CH2 . TRP B 2 92 ? 44.018 -29.269 -29.060 1.00 53.35 ? 92 TRP B CH2 1 ATOM 3277 N N . THR B 2 93 ? 47.151 -21.723 -29.046 1.00 50.10 ? 93 THR B N 1 ATOM 3278 C CA . THR B 2 93 ? 47.223 -20.535 -29.857 1.00 50.96 ? 93 THR B CA 1 ATOM 3279 C C . THR B 2 93 ? 48.050 -20.883 -31.096 1.00 50.79 ? 93 THR B C 1 ATOM 3280 O O . THR B 2 93 ? 47.653 -20.547 -32.221 1.00 50.58 ? 93 THR B O 1 ATOM 3281 C CB . THR B 2 93 ? 47.827 -19.357 -29.101 1.00 53.88 ? 93 THR B CB 1 ATOM 3282 O OG1 . THR B 2 93 ? 46.890 -18.920 -28.121 1.00 56.87 ? 93 THR B OG1 1 ATOM 3283 C CG2 . THR B 2 93 ? 48.097 -18.214 -30.031 1.00 56.04 ? 93 THR B CG2 1 ATOM 3284 N N . TYR B 2 94 ? 49.165 -21.587 -30.876 1.00 49.60 ? 94 TYR B N 1 ATOM 3285 C CA . TYR B 2 94 ? 50.096 -21.946 -31.943 1.00 49.42 ? 94 TYR B CA 1 ATOM 3286 C C . TYR B 2 94 ? 49.398 -22.855 -32.929 1.00 46.13 ? 94 TYR B C 1 ATOM 3287 O O . TYR B 2 94 ? 49.374 -22.580 -34.111 1.00 44.27 ? 94 TYR B O 1 ATOM 3288 C CB . TYR B 2 94 ? 51.377 -22.593 -31.376 1.00 52.13 ? 94 TYR B CB 1 ATOM 3289 C CG . TYR B 2 94 ? 52.234 -23.325 -32.388 1.00 51.74 ? 94 TYR B CG 1 ATOM 3290 C CD1 . TYR B 2 94 ? 51.945 -24.634 -32.766 1.00 51.21 ? 94 TYR B CD1 1 ATOM 3291 C CD2 . TYR B 2 94 ? 53.332 -22.722 -32.953 1.00 53.77 ? 94 TYR B CD2 1 ATOM 3292 C CE1 . TYR B 2 94 ? 52.718 -25.295 -33.703 1.00 52.40 ? 94 TYR B CE1 1 ATOM 3293 C CE2 . TYR B 2 94 ? 54.118 -23.381 -33.882 1.00 54.95 ? 94 TYR B CE2 1 ATOM 3294 C CZ . TYR B 2 94 ? 53.803 -24.664 -34.258 1.00 54.36 ? 94 TYR B CZ 1 ATOM 3295 O OH . TYR B 2 94 ? 54.584 -25.325 -35.177 1.00 57.86 ? 94 TYR B OH 1 ATOM 3296 N N . ASN B 2 95 ? 48.772 -23.907 -32.435 1.00 46.80 ? 95 ASN B N 1 ATOM 3297 C CA . ASN B 2 95 ? 47.993 -24.777 -33.296 1.00 46.36 ? 95 ASN B CA 1 ATOM 3298 C C . ASN B 2 95 ? 47.041 -23.989 -34.185 1.00 47.45 ? 95 ASN B C 1 ATOM 3299 O O . ASN B 2 95 ? 47.021 -24.195 -35.397 1.00 50.86 ? 95 ASN B O 1 ATOM 3300 C CB . ASN B 2 95 ? 47.231 -25.833 -32.501 1.00 45.81 ? 95 ASN B CB 1 ATOM 3301 C CG . ASN B 2 95 ? 48.149 -26.904 -31.925 1.00 48.25 ? 95 ASN B CG 1 ATOM 3302 O OD1 . ASN B 2 95 ? 49.328 -26.961 -32.247 1.00 49.69 ? 95 ASN B OD1 1 ATOM 3303 N ND2 . ASN B 2 95 ? 47.603 -27.759 -31.066 1.00 51.85 ? 95 ASN B ND2 1 ATOM 3304 N N . ALA B 2 96 ? 46.271 -23.079 -33.604 1.00 47.47 ? 96 ALA B N 1 ATOM 3305 C CA . ALA B 2 96 ? 45.256 -22.367 -34.382 1.00 47.10 ? 96 ALA B CA 1 ATOM 3306 C C . ALA B 2 96 ? 45.907 -21.451 -35.436 1.00 47.42 ? 96 ALA B C 1 ATOM 3307 O O . ALA B 2 96 ? 45.510 -21.444 -36.591 1.00 46.77 ? 96 ALA B O 1 ATOM 3308 C CB . ALA B 2 96 ? 44.344 -21.574 -33.463 1.00 47.68 ? 96 ALA B CB 1 ATOM 3309 N N . GLU B 2 97 ? 46.917 -20.685 -35.056 1.00 48.04 ? 97 GLU B N 1 ATOM 3310 C CA . GLU B 2 97 ? 47.540 -19.808 -36.037 1.00 51.05 ? 97 GLU B CA 1 ATOM 3311 C C . GLU B 2 97 ? 48.200 -20.604 -37.169 1.00 50.52 ? 97 GLU B C 1 ATOM 3312 O O . GLU B 2 97 ? 48.067 -20.251 -38.346 1.00 51.97 ? 97 GLU B O 1 ATOM 3313 C CB . GLU B 2 97 ? 48.507 -18.840 -35.355 1.00 54.21 ? 97 GLU B CB 1 ATOM 3314 C CG . GLU B 2 97 ? 47.720 -17.851 -34.503 1.00 57.98 ? 97 GLU B CG 1 ATOM 3315 C CD . GLU B 2 97 ? 48.554 -16.927 -33.666 1.00 62.65 ? 97 GLU B CD 1 ATOM 3316 O OE1 . GLU B 2 97 ? 49.795 -17.021 -33.689 1.00 67.88 ? 97 GLU B OE1 1 ATOM 3317 O OE2 . GLU B 2 97 ? 47.950 -16.090 -32.979 1.00 67.02 ? 97 GLU B OE2 1 ATOM 3318 N N . LEU B 2 98 ? 48.883 -21.693 -36.823 1.00 50.22 ? 98 LEU B N 1 ATOM 3319 C CA . LEU B 2 98 ? 49.635 -22.438 -37.812 1.00 49.22 ? 98 LEU B CA 1 ATOM 3320 C C . LEU B 2 98 ? 48.673 -23.115 -38.745 1.00 45.75 ? 98 LEU B C 1 ATOM 3321 O O . LEU B 2 98 ? 48.896 -23.124 -39.939 1.00 45.39 ? 98 LEU B O 1 ATOM 3322 C CB . LEU B 2 98 ? 50.560 -23.463 -37.178 1.00 52.07 ? 98 LEU B CB 1 ATOM 3323 C CG . LEU B 2 98 ? 51.533 -24.143 -38.143 1.00 53.08 ? 98 LEU B CG 1 ATOM 3324 C CD1 . LEU B 2 98 ? 52.577 -23.142 -38.610 1.00 54.58 ? 98 LEU B CD1 1 ATOM 3325 C CD2 . LEU B 2 98 ? 52.191 -25.351 -37.489 1.00 54.93 ? 98 LEU B CD2 1 ATOM 3326 N N . LEU B 2 99 ? 47.586 -23.652 -38.218 1.00 44.81 ? 99 LEU B N 1 ATOM 3327 C CA . LEU B 2 99 ? 46.623 -24.317 -39.070 1.00 45.30 ? 99 LEU B CA 1 ATOM 3328 C C . LEU B 2 99 ? 46.050 -23.316 -40.064 1.00 45.39 ? 99 LEU B C 1 ATOM 3329 O O . LEU B 2 99 ? 45.940 -23.601 -41.259 1.00 48.46 ? 99 LEU B O 1 ATOM 3330 C CB . LEU B 2 99 ? 45.500 -24.925 -38.248 1.00 49.22 ? 99 LEU B CB 1 ATOM 3331 C CG . LEU B 2 99 ? 44.448 -25.750 -38.997 1.00 51.99 ? 99 LEU B CG 1 ATOM 3332 C CD1 . LEU B 2 99 ? 45.027 -27.054 -39.476 1.00 52.78 ? 99 LEU B CD1 1 ATOM 3333 C CD2 . LEU B 2 99 ? 43.265 -26.054 -38.089 1.00 56.47 ? 99 LEU B CD2 1 ATOM 3334 N N . VAL B 2 100 ? 45.676 -22.138 -39.578 1.00 43.84 ? 100 VAL B N 1 ATOM 3335 C CA . VAL B 2 100 ? 45.091 -21.160 -40.463 1.00 41.70 ? 100 VAL B CA 1 ATOM 3336 C C . VAL B 2 100 ? 46.080 -20.746 -41.572 1.00 41.41 ? 100 VAL B C 1 ATOM 3337 O O . VAL B 2 100 ? 45.678 -20.670 -42.730 1.00 39.88 ? 100 VAL B O 1 ATOM 3338 C CB . VAL B 2 100 ? 44.545 -19.959 -39.685 1.00 43.16 ? 100 VAL B CB 1 ATOM 3339 C CG1 . VAL B 2 100 ? 44.330 -18.751 -40.610 1.00 44.36 ? 100 VAL B CG1 1 ATOM 3340 C CG2 . VAL B 2 100 ? 43.242 -20.372 -38.995 1.00 42.88 ? 100 VAL B CG2 1 ATOM 3341 N N . LEU B 2 101 ? 47.347 -20.496 -41.225 1.00 40.39 ? 101 LEU B N 1 ATOM 3342 C CA . LEU B 2 101 ? 48.347 -20.135 -42.225 1.00 40.83 ? 101 LEU B CA 1 ATOM 3343 C C . LEU B 2 101 ? 48.473 -21.244 -43.283 1.00 41.89 ? 101 LEU B C 1 ATOM 3344 O O . LEU B 2 101 ? 48.384 -20.990 -44.486 1.00 43.20 ? 101 LEU B O 1 ATOM 3345 C CB . LEU B 2 101 ? 49.709 -19.916 -41.573 1.00 41.96 ? 101 LEU B CB 1 ATOM 3346 C CG . LEU B 2 101 ? 49.907 -18.669 -40.719 1.00 45.73 ? 101 LEU B CG 1 ATOM 3347 C CD1 . LEU B 2 101 ? 51.344 -18.586 -40.236 1.00 48.64 ? 101 LEU B CD1 1 ATOM 3348 C CD2 . LEU B 2 101 ? 49.553 -17.399 -41.475 1.00 47.75 ? 101 LEU B CD2 1 ATOM 3349 N N . MET B 2 102 ? 48.701 -22.470 -42.822 1.00 41.52 ? 102 MET B N 1 ATOM 3350 C CA . MET B 2 102 ? 48.924 -23.589 -43.707 1.00 41.53 ? 102 MET B CA 1 ATOM 3351 C C . MET B 2 102 ? 47.728 -23.849 -44.604 1.00 41.69 ? 102 MET B C 1 ATOM 3352 O O . MET B 2 102 ? 47.902 -24.088 -45.810 1.00 42.36 ? 102 MET B O 1 ATOM 3353 C CB . MET B 2 102 ? 49.231 -24.843 -42.899 1.00 43.31 ? 102 MET B CB 1 ATOM 3354 C CG . MET B 2 102 ? 50.618 -24.872 -42.279 1.00 47.79 ? 102 MET B CG 1 ATOM 3355 S SD . MET B 2 102 ? 50.813 -26.415 -41.353 1.00 52.42 ? 102 MET B SD 1 ATOM 3356 C CE . MET B 2 102 ? 52.596 -26.407 -41.198 1.00 56.05 ? 102 MET B CE 1 ATOM 3357 N N . GLU B 2 103 ? 46.522 -23.823 -44.041 1.00 39.05 ? 103 GLU B N 1 ATOM 3358 C CA . GLU B 2 103 ? 45.367 -24.178 -44.849 1.00 41.79 ? 103 GLU B CA 1 ATOM 3359 C C . GLU B 2 103 ? 44.970 -23.039 -45.783 1.00 41.00 ? 103 GLU B C 1 ATOM 3360 O O . GLU B 2 103 ? 44.457 -23.281 -46.860 1.00 41.22 ? 103 GLU B O 1 ATOM 3361 C CB . GLU B 2 103 ? 44.207 -24.640 -43.991 1.00 41.04 ? 103 GLU B CB 1 ATOM 3362 C CG . GLU B 2 103 ? 44.482 -25.985 -43.352 1.00 46.25 ? 103 GLU B CG 1 ATOM 3363 C CD . GLU B 2 103 ? 44.550 -27.141 -44.355 1.00 48.58 ? 103 GLU B CD 1 ATOM 3364 O OE1 . GLU B 2 103 ? 43.908 -27.083 -45.424 1.00 52.33 ? 103 GLU B OE1 1 ATOM 3365 O OE2 . GLU B 2 103 ? 45.249 -28.131 -44.067 1.00 53.31 ? 103 GLU B OE2 1 ATOM 3366 N N . ASN B 2 104 ? 45.197 -21.802 -45.370 1.00 41.07 ? 104 ASN B N 1 ATOM 3367 C CA . ASN B 2 104 ? 44.973 -20.680 -46.254 1.00 40.31 ? 104 ASN B CA 1 ATOM 3368 C C . ASN B 2 104 ? 45.847 -20.845 -47.486 1.00 42.35 ? 104 ASN B C 1 ATOM 3369 O O . ASN B 2 104 ? 45.375 -20.675 -48.598 1.00 38.59 ? 104 ASN B O 1 ATOM 3370 C CB . ASN B 2 104 ? 45.309 -19.369 -45.562 1.00 42.20 ? 104 ASN B CB 1 ATOM 3371 C CG . ASN B 2 104 ? 44.213 -18.906 -44.634 1.00 43.59 ? 104 ASN B CG 1 ATOM 3372 O OD1 . ASN B 2 104 ? 43.111 -19.457 -44.630 1.00 41.29 ? 104 ASN B OD1 1 ATOM 3373 N ND2 . ASN B 2 104 ? 44.511 -17.886 -43.834 1.00 46.29 ? 104 ASN B ND2 1 ATOM 3374 N N . GLU B 2 105 ? 47.121 -21.196 -47.293 1.00 43.62 ? 105 GLU B N 1 ATOM 3375 C CA . GLU B 2 105 ? 47.983 -21.446 -48.432 1.00 43.93 ? 105 GLU B CA 1 ATOM 3376 C C . GLU B 2 105 ? 47.417 -22.557 -49.300 1.00 40.86 ? 105 GLU B C 1 ATOM 3377 O O . GLU B 2 105 ? 47.364 -22.455 -50.510 1.00 38.75 ? 105 GLU B O 1 ATOM 3378 C CB . GLU B 2 105 ? 49.368 -21.841 -47.989 1.00 47.84 ? 105 GLU B CB 1 ATOM 3379 C CG . GLU B 2 105 ? 50.375 -21.687 -49.095 1.00 55.38 ? 105 GLU B CG 1 ATOM 3380 C CD . GLU B 2 105 ? 51.752 -21.533 -48.548 1.00 67.77 ? 105 GLU B CD 1 ATOM 3381 O OE1 . GLU B 2 105 ? 52.254 -22.572 -48.040 1.00 75.42 ? 105 GLU B OE1 1 ATOM 3382 O OE2 . GLU B 2 105 ? 52.298 -20.381 -48.595 1.00 67.73 ? 105 GLU B OE2 1 ATOM 3383 N N . ARG B 2 106 ? 46.978 -23.628 -48.678 1.00 41.71 ? 106 ARG B N 1 ATOM 3384 C CA . ARG B 2 106 ? 46.402 -24.714 -49.459 1.00 43.20 ? 106 ARG B CA 1 ATOM 3385 C C . ARG B 2 106 ? 45.121 -24.316 -50.176 1.00 40.76 ? 106 ARG B C 1 ATOM 3386 O O . ARG B 2 106 ? 44.888 -24.742 -51.279 1.00 42.94 ? 106 ARG B O 1 ATOM 3387 C CB . ARG B 2 106 ? 46.187 -25.940 -48.595 1.00 46.48 ? 106 ARG B CB 1 ATOM 3388 C CG . ARG B 2 106 ? 47.509 -26.543 -48.109 1.00 51.00 ? 106 ARG B CG 1 ATOM 3389 C CD . ARG B 2 106 ? 47.434 -28.063 -47.946 1.00 59.24 ? 106 ARG B CD 1 ATOM 3390 N NE . ARG B 2 106 ? 47.855 -28.829 -49.150 1.00 63.74 ? 106 ARG B NE 1 ATOM 3391 C CZ . ARG B 2 106 ? 47.320 -29.989 -49.545 1.00 68.11 ? 106 ARG B CZ 1 ATOM 3392 N NH1 . ARG B 2 106 ? 46.306 -30.530 -48.887 1.00 73.10 ? 106 ARG B NH1 1 ATOM 3393 N NH2 . ARG B 2 106 ? 47.772 -30.620 -50.625 1.00 76.21 ? 106 ARG B NH2 1 ATOM 3394 N N . THR B 2 107 ? 44.303 -23.469 -49.571 1.00 41.83 ? 107 THR B N 1 ATOM 3395 C CA . THR B 2 107 ? 43.057 -23.033 -50.186 1.00 36.49 ? 107 THR B CA 1 ATOM 3396 C C . THR B 2 107 ? 43.340 -22.206 -51.443 1.00 38.38 ? 107 THR B C 1 ATOM 3397 O O . THR B 2 107 ? 42.714 -22.416 -52.472 1.00 37.37 ? 107 THR B O 1 ATOM 3398 C CB . THR B 2 107 ? 42.200 -22.239 -49.194 1.00 36.51 ? 107 THR B CB 1 ATOM 3399 O OG1 . THR B 2 107 ? 41.777 -23.098 -48.133 1.00 37.36 ? 107 THR B OG1 1 ATOM 3400 C CG2 . THR B 2 107 ? 40.959 -21.673 -49.876 1.00 37.76 ? 107 THR B CG2 1 ATOM 3401 N N . LEU B 2 108 ? 44.285 -21.280 -51.372 1.00 37.59 ? 108 LEU B N 1 ATOM 3402 C CA . LEU B 2 108 ? 44.630 -20.516 -52.542 1.00 39.62 ? 108 LEU B CA 1 ATOM 3403 C C . LEU B 2 108 ? 45.136 -21.405 -53.689 1.00 39.90 ? 108 LEU B C 1 ATOM 3404 O O . LEU B 2 108 ? 44.734 -21.226 -54.837 1.00 39.02 ? 108 LEU B O 1 ATOM 3405 C CB . LEU B 2 108 ? 45.659 -19.440 -52.202 1.00 40.59 ? 108 LEU B CB 1 ATOM 3406 C CG . LEU B 2 108 ? 45.147 -18.399 -51.189 1.00 43.92 ? 108 LEU B CG 1 ATOM 3407 C CD1 . LEU B 2 108 ? 46.156 -17.286 -50.986 1.00 45.64 ? 108 LEU B CD1 1 ATOM 3408 C CD2 . LEU B 2 108 ? 43.792 -17.812 -51.563 1.00 44.92 ? 108 LEU B CD2 1 ATOM 3409 N N . ASP B 2 109 ? 46.011 -22.355 -53.379 1.00 40.18 ? 109 ASP B N 1 ATOM 3410 C CA . ASP B 2 109 ? 46.480 -23.297 -54.372 1.00 39.53 ? 109 ASP B CA 1 ATOM 3411 C C . ASP B 2 109 ? 45.327 -24.199 -54.926 1.00 38.38 ? 109 ASP B C 1 ATOM 3412 O O . ASP B 2 109 ? 45.322 -24.575 -56.086 1.00 42.43 ? 109 ASP B O 1 ATOM 3413 C CB . ASP B 2 109 ? 47.583 -24.145 -53.762 1.00 41.85 ? 109 ASP B CB 1 ATOM 3414 C CG . ASP B 2 109 ? 48.871 -23.330 -53.432 1.00 46.27 ? 109 ASP B CG 1 ATOM 3415 O OD1 . ASP B 2 109 ? 49.175 -22.353 -54.150 1.00 46.86 ? 109 ASP B OD1 1 ATOM 3416 O OD2 . ASP B 2 109 ? 49.598 -23.711 -52.465 1.00 50.40 ? 109 ASP B OD2 1 ATOM 3417 N N . PHE B 2 110 ? 44.359 -24.549 -54.105 1.00 35.60 ? 110 PHE B N 1 ATOM 3418 C CA . PHE B 2 110 ? 43.245 -25.427 -54.527 1.00 34.48 ? 110 PHE B CA 1 ATOM 3419 C C . PHE B 2 110 ? 42.522 -24.745 -55.682 1.00 36.31 ? 110 PHE B C 1 ATOM 3420 O O . PHE B 2 110 ? 42.284 -25.367 -56.723 1.00 38.22 ? 110 PHE B O 1 ATOM 3421 C CB . PHE B 2 110 ? 42.342 -25.693 -53.316 1.00 33.43 ? 110 PHE B CB 1 ATOM 3422 C CG . PHE B 2 110 ? 41.065 -26.448 -53.609 1.00 35.09 ? 110 PHE B CG 1 ATOM 3423 C CD1 . PHE B 2 110 ? 41.081 -27.697 -54.180 1.00 37.33 ? 110 PHE B CD1 1 ATOM 3424 C CD2 . PHE B 2 110 ? 39.862 -25.930 -53.233 1.00 34.00 ? 110 PHE B CD2 1 ATOM 3425 C CE1 . PHE B 2 110 ? 39.911 -28.377 -54.421 1.00 39.08 ? 110 PHE B CE1 1 ATOM 3426 C CE2 . PHE B 2 110 ? 38.677 -26.607 -53.469 1.00 37.60 ? 110 PHE B CE2 1 ATOM 3427 C CZ . PHE B 2 110 ? 38.700 -27.835 -54.065 1.00 39.31 ? 110 PHE B CZ 1 ATOM 3428 N N . HIS B 2 111 ? 42.225 -23.454 -55.509 1.00 34.80 ? 111 HIS B N 1 ATOM 3429 C CA . HIS B 2 111 ? 41.582 -22.663 -56.521 1.00 36.31 ? 111 HIS B CA 1 ATOM 3430 C C . HIS B 2 111 ? 42.413 -22.578 -57.799 1.00 36.89 ? 111 HIS B C 1 ATOM 3431 O O . HIS B 2 111 ? 41.894 -22.740 -58.921 1.00 36.57 ? 111 HIS B O 1 ATOM 3432 C CB . HIS B 2 111 ? 41.313 -21.229 -56.012 1.00 39.04 ? 111 HIS B CB 1 ATOM 3433 C CG . HIS B 2 111 ? 40.227 -21.142 -54.989 1.00 38.90 ? 111 HIS B CG 1 ATOM 3434 N ND1 . HIS B 2 111 ? 38.943 -21.556 -55.247 1.00 40.38 ? 111 HIS B ND1 1 ATOM 3435 C CD2 . HIS B 2 111 ? 40.229 -20.677 -53.713 1.00 38.86 ? 111 HIS B CD2 1 ATOM 3436 C CE1 . HIS B 2 111 ? 38.196 -21.351 -54.173 1.00 42.82 ? 111 HIS B CE1 1 ATOM 3437 N NE2 . HIS B 2 111 ? 38.959 -20.829 -53.225 1.00 40.96 ? 111 HIS B NE2 1 ATOM 3438 N N . ASP B 2 112 ? 43.698 -22.313 -57.626 1.00 34.72 ? 112 ASP B N 1 ATOM 3439 C CA . ASP B 2 112 ? 44.611 -22.229 -58.733 1.00 34.70 ? 112 ASP B CA 1 ATOM 3440 C C . ASP B 2 112 ? 44.498 -23.526 -59.520 1.00 34.87 ? 112 ASP B C 1 ATOM 3441 O O . ASP B 2 112 ? 44.362 -23.523 -60.746 1.00 37.40 ? 112 ASP B O 1 ATOM 3442 C CB . ASP B 2 112 ? 46.042 -22.021 -58.207 1.00 35.97 ? 112 ASP B CB 1 ATOM 3443 C CG . ASP B 2 112 ? 47.000 -21.613 -59.287 1.00 38.76 ? 112 ASP B CG 1 ATOM 3444 O OD1 . ASP B 2 112 ? 46.541 -21.348 -60.425 1.00 40.10 ? 112 ASP B OD1 1 ATOM 3445 O OD2 . ASP B 2 112 ? 48.215 -21.556 -58.995 1.00 41.13 ? 112 ASP B OD2 1 ATOM 3446 N N . SER B 2 113 ? 44.530 -24.639 -58.801 1.00 33.74 ? 113 SER B N 1 ATOM 3447 C CA . SER B 2 113 ? 44.480 -25.947 -59.408 1.00 34.26 ? 113 SER B CA 1 ATOM 3448 C C . SER B 2 113 ? 43.153 -26.163 -60.112 1.00 35.02 ? 113 SER B C 1 ATOM 3449 O O . SER B 2 113 ? 43.097 -26.710 -61.218 1.00 38.42 ? 113 SER B O 1 ATOM 3450 C CB . SER B 2 113 ? 44.695 -27.029 -58.344 1.00 34.43 ? 113 SER B CB 1 ATOM 3451 O OG . SER B 2 113 ? 44.239 -28.291 -58.785 1.00 37.02 ? 113 SER B OG 1 ATOM 3452 N N . ASN B 2 114 ? 42.060 -25.776 -59.482 1.00 34.26 ? 114 ASN B N 1 ATOM 3453 C CA . ASN B 2 114 ? 40.791 -25.931 -60.166 1.00 35.61 ? 114 ASN B CA 1 ATOM 3454 C C . ASN B 2 114 ? 40.759 -25.155 -61.478 1.00 35.23 ? 114 ASN B C 1 ATOM 3455 O O . ASN B 2 114 ? 40.148 -25.615 -62.431 1.00 37.19 ? 114 ASN B O 1 ATOM 3456 C CB . ASN B 2 114 ? 39.634 -25.530 -59.285 1.00 36.88 ? 114 ASN B CB 1 ATOM 3457 C CG . ASN B 2 114 ? 39.513 -26.406 -58.080 1.00 38.30 ? 114 ASN B CG 1 ATOM 3458 O OD1 . ASN B 2 114 ? 39.799 -27.611 -58.121 1.00 37.08 ? 114 ASN B OD1 1 ATOM 3459 N ND2 . ASN B 2 114 ? 39.100 -25.807 -56.986 1.00 40.74 ? 114 ASN B ND2 1 ATOM 3460 N N . VAL B 2 115 ? 41.431 -24.007 -61.542 1.00 34.35 ? 115 VAL B N 1 ATOM 3461 C CA . VAL B 2 115 ? 41.424 -23.220 -62.771 1.00 36.86 ? 115 VAL B CA 1 ATOM 3462 C C . VAL B 2 115 ? 42.269 -23.906 -63.830 1.00 37.63 ? 115 VAL B C 1 ATOM 3463 O O . VAL B 2 115 ? 41.829 -24.047 -64.956 1.00 39.39 ? 115 VAL B O 1 ATOM 3464 C CB . VAL B 2 115 ? 41.907 -21.771 -62.551 1.00 38.65 ? 115 VAL B CB 1 ATOM 3465 C CG1 . VAL B 2 115 ? 42.097 -21.056 -63.879 1.00 40.92 ? 115 VAL B CG1 1 ATOM 3466 C CG2 . VAL B 2 115 ? 40.890 -21.006 -61.722 1.00 40.11 ? 115 VAL B CG2 1 ATOM 3467 N N . LYS B 2 116 ? 43.477 -24.324 -63.458 1.00 37.16 ? 116 LYS B N 1 ATOM 3468 C CA . LYS B 2 116 ? 44.360 -25.013 -64.358 1.00 38.48 ? 116 LYS B CA 1 ATOM 3469 C C . LYS B 2 116 ? 43.680 -26.233 -64.942 1.00 41.29 ? 116 LYS B C 1 ATOM 3470 O O . LYS B 2 116 ? 43.810 -26.489 -66.138 1.00 42.65 ? 116 LYS B O 1 ATOM 3471 C CB . LYS B 2 116 ? 45.643 -25.371 -63.611 1.00 41.64 ? 116 LYS B CB 1 ATOM 3472 C CG . LYS B 2 116 ? 46.660 -26.222 -64.326 1.00 44.36 ? 116 LYS B CG 1 ATOM 3473 C CD . LYS B 2 116 ? 47.106 -25.591 -65.623 1.00 50.38 ? 116 LYS B CD 1 ATOM 3474 C CE . LYS B 2 116 ? 48.519 -26.066 -65.998 1.00 55.10 ? 116 LYS B CE 1 ATOM 3475 N NZ . LYS B 2 116 ? 49.514 -25.078 -65.470 1.00 58.55 ? 116 LYS B NZ 1 ATOM 3476 N N . ASN B 2 117 ? 42.923 -26.966 -64.127 1.00 41.26 ? 117 ASN B N 1 ATOM 3477 C CA . ASN B 2 117 ? 42.267 -28.179 -64.599 1.00 45.08 ? 117 ASN B CA 1 ATOM 3478 C C . ASN B 2 117 ? 41.092 -27.912 -65.537 1.00 46.47 ? 117 ASN B C 1 ATOM 3479 O O . ASN B 2 117 ? 40.781 -28.736 -66.400 1.00 50.35 ? 117 ASN B O 1 ATOM 3480 C CB . ASN B 2 117 ? 41.803 -29.043 -63.416 1.00 47.29 ? 117 ASN B CB 1 ATOM 3481 C CG . ASN B 2 117 ? 42.956 -29.680 -62.663 1.00 48.75 ? 117 ASN B CG 1 ATOM 3482 O OD1 . ASN B 2 117 ? 44.084 -29.719 -63.137 1.00 52.40 ? 117 ASN B OD1 1 ATOM 3483 N ND2 . ASN B 2 117 ? 42.674 -30.176 -61.479 1.00 48.89 ? 117 ASN B ND2 1 ATOM 3484 N N . LEU B 2 118 ? 40.413 -26.787 -65.358 1.00 45.36 ? 118 LEU B N 1 ATOM 3485 C CA . LEU B 2 118 ? 39.313 -26.442 -66.248 1.00 45.76 ? 118 LEU B CA 1 ATOM 3486 C C . LEU B 2 118 ? 39.915 -25.996 -67.580 1.00 45.83 ? 118 LEU B C 1 ATOM 3487 O O . LEU B 2 118 ? 39.495 -26.443 -68.647 1.00 48.25 ? 118 LEU B O 1 ATOM 3488 C CB . LEU B 2 118 ? 38.435 -25.370 -65.609 1.00 46.71 ? 118 LEU B CB 1 ATOM 3489 C CG . LEU B 2 118 ? 37.277 -24.846 -66.415 1.00 49.07 ? 118 LEU B CG 1 ATOM 3490 C CD1 . LEU B 2 118 ? 36.285 -25.960 -66.700 1.00 54.37 ? 118 LEU B CD1 1 ATOM 3491 C CD2 . LEU B 2 118 ? 36.619 -23.717 -65.655 1.00 50.03 ? 118 LEU B CD2 1 ATOM 3492 N N . TYR B 2 119 ? 40.949 -25.165 -67.523 1.00 43.06 ? 119 TYR B N 1 ATOM 3493 C CA . TYR B 2 119 ? 41.682 -24.811 -68.732 1.00 42.02 ? 119 TYR B CA 1 ATOM 3494 C C . TYR B 2 119 ? 42.154 -26.060 -69.498 1.00 46.27 ? 119 TYR B C 1 ATOM 3495 O O . TYR B 2 119 ? 41.989 -26.147 -70.710 1.00 49.25 ? 119 TYR B O 1 ATOM 3496 C CB . TYR B 2 119 ? 42.862 -23.911 -68.391 1.00 39.16 ? 119 TYR B CB 1 ATOM 3497 C CG . TYR B 2 119 ? 43.686 -23.511 -69.596 1.00 41.34 ? 119 TYR B CG 1 ATOM 3498 C CD1 . TYR B 2 119 ? 43.298 -22.459 -70.434 1.00 41.50 ? 119 TYR B CD1 1 ATOM 3499 C CD2 . TYR B 2 119 ? 44.880 -24.164 -69.885 1.00 41.37 ? 119 TYR B CD2 1 ATOM 3500 C CE1 . TYR B 2 119 ? 44.080 -22.085 -71.528 1.00 43.03 ? 119 TYR B CE1 1 ATOM 3501 C CE2 . TYR B 2 119 ? 45.660 -23.794 -70.962 1.00 42.90 ? 119 TYR B CE2 1 ATOM 3502 C CZ . TYR B 2 119 ? 45.259 -22.769 -71.779 1.00 45.04 ? 119 TYR B CZ 1 ATOM 3503 O OH . TYR B 2 119 ? 46.048 -22.456 -72.843 1.00 47.11 ? 119 TYR B OH 1 ATOM 3504 N N . ASP B 2 120 ? 42.735 -27.033 -68.810 1.00 45.86 ? 120 ASP B N 1 ATOM 3505 C CA . ASP B 2 120 ? 43.209 -28.230 -69.511 1.00 48.79 ? 120 ASP B CA 1 ATOM 3506 C C . ASP B 2 120 ? 42.048 -29.029 -70.090 1.00 49.20 ? 120 ASP B C 1 ATOM 3507 O O . ASP B 2 120 ? 42.104 -29.489 -71.221 1.00 51.85 ? 120 ASP B O 1 ATOM 3508 C CB . ASP B 2 120 ? 44.076 -29.107 -68.593 1.00 49.92 ? 120 ASP B CB 1 ATOM 3509 C CG . ASP B 2 120 ? 45.424 -28.487 -68.313 1.00 50.02 ? 120 ASP B CG 1 ATOM 3510 O OD1 . ASP B 2 120 ? 45.992 -27.881 -69.233 1.00 53.08 ? 120 ASP B OD1 1 ATOM 3511 O OD2 . ASP B 2 120 ? 45.922 -28.588 -67.172 1.00 51.22 ? 120 ASP B OD2 1 ATOM 3512 N N . LYS B 2 121 ? 40.992 -29.187 -69.321 1.00 49.98 ? 121 LYS B N 1 ATOM 3513 C CA . LYS B 2 121 ? 39.794 -29.874 -69.809 1.00 55.41 ? 121 LYS B CA 1 ATOM 3514 C C . LYS B 2 121 ? 39.353 -29.347 -71.178 1.00 56.19 ? 121 LYS B C 1 ATOM 3515 O O . LYS B 2 121 ? 39.058 -30.123 -72.066 1.00 60.82 ? 121 LYS B O 1 ATOM 3516 C CB . LYS B 2 121 ? 38.673 -29.676 -68.800 1.00 57.72 ? 121 LYS B CB 1 ATOM 3517 C CG . LYS B 2 121 ? 37.398 -30.435 -69.052 1.00 64.16 ? 121 LYS B CG 1 ATOM 3518 C CD . LYS B 2 121 ? 36.392 -30.102 -67.945 1.00 67.04 ? 121 LYS B CD 1 ATOM 3519 C CE . LYS B 2 121 ? 35.116 -30.931 -68.043 1.00 75.44 ? 121 LYS B CE 1 ATOM 3520 N NZ . LYS B 2 121 ? 34.439 -30.779 -69.377 1.00 82.54 ? 121 LYS B NZ 1 ATOM 3521 N N . VAL B 2 122 ? 39.313 -28.023 -71.325 1.00 52.38 ? 122 VAL B N 1 ATOM 3522 C CA . VAL B 2 122 ? 38.982 -27.374 -72.580 1.00 51.43 ? 122 VAL B CA 1 ATOM 3523 C C . VAL B 2 122 ? 40.067 -27.576 -73.618 1.00 52.49 ? 122 VAL B C 1 ATOM 3524 O O . VAL B 2 122 ? 39.774 -27.894 -74.764 1.00 54.92 ? 122 VAL B O 1 ATOM 3525 C CB . VAL B 2 122 ? 38.689 -25.865 -72.376 1.00 49.83 ? 122 VAL B CB 1 ATOM 3526 C CG1 . VAL B 2 122 ? 38.642 -25.108 -73.702 1.00 50.54 ? 122 VAL B CG1 1 ATOM 3527 C CG2 . VAL B 2 122 ? 37.371 -25.707 -71.631 1.00 50.21 ? 122 VAL B CG2 1 ATOM 3528 N N . ARG B 2 123 ? 41.317 -27.395 -73.233 1.00 51.93 ? 123 ARG B N 1 ATOM 3529 C CA . ARG B 2 123 ? 42.426 -27.631 -74.147 1.00 54.09 ? 123 ARG B CA 1 ATOM 3530 C C . ARG B 2 123 ? 42.386 -29.025 -74.755 1.00 58.21 ? 123 ARG B C 1 ATOM 3531 O O . ARG B 2 123 ? 42.533 -29.169 -75.966 1.00 60.37 ? 123 ARG B O 1 ATOM 3532 C CB . ARG B 2 123 ? 43.745 -27.442 -73.424 1.00 55.03 ? 123 ARG B CB 1 ATOM 3533 C CG . ARG B 2 123 ? 44.940 -27.436 -74.348 1.00 57.83 ? 123 ARG B CG 1 ATOM 3534 C CD . ARG B 2 123 ? 46.226 -27.254 -73.555 1.00 60.86 ? 123 ARG B CD 1 ATOM 3535 N NE . ARG B 2 123 ? 46.379 -28.232 -72.459 1.00 61.33 ? 123 ARG B NE 1 ATOM 3536 C CZ . ARG B 2 123 ? 46.772 -29.500 -72.621 1.00 63.81 ? 123 ARG B CZ 1 ATOM 3537 N NH1 . ARG B 2 123 ? 47.039 -30.004 -73.835 1.00 66.22 ? 123 ARG B NH1 1 ATOM 3538 N NH2 . ARG B 2 123 ? 46.885 -30.278 -71.560 1.00 62.80 ? 123 ARG B NH2 1 ATOM 3539 N N . LEU B 2 124 ? 42.166 -30.048 -73.927 1.00 60.37 ? 124 LEU B N 1 ATOM 3540 C CA . LEU B 2 124 ? 42.138 -31.446 -74.404 1.00 65.60 ? 124 LEU B CA 1 ATOM 3541 C C . LEU B 2 124 ? 40.958 -31.786 -75.338 1.00 67.54 ? 124 LEU B C 1 ATOM 3542 O O . LEU B 2 124 ? 40.986 -32.805 -76.023 1.00 72.56 ? 124 LEU B O 1 ATOM 3543 C CB . LEU B 2 124 ? 42.155 -32.431 -73.222 1.00 68.19 ? 124 LEU B CB 1 ATOM 3544 C CG . LEU B 2 124 ? 43.400 -32.387 -72.309 1.00 70.17 ? 124 LEU B CG 1 ATOM 3545 C CD1 . LEU B 2 124 ? 43.135 -32.923 -70.891 1.00 70.30 ? 124 LEU B CD1 1 ATOM 3546 C CD2 . LEU B 2 124 ? 44.569 -33.120 -72.965 1.00 74.65 ? 124 LEU B CD2 1 ATOM 3547 N N . GLN B 2 125 ? 39.917 -30.960 -75.344 1.00 65.84 ? 125 GLN B N 1 ATOM 3548 C CA . GLN B 2 125 ? 38.795 -31.136 -76.277 1.00 68.87 ? 125 GLN B CA 1 ATOM 3549 C C . GLN B 2 125 ? 39.114 -30.523 -77.613 1.00 66.39 ? 125 GLN B C 1 ATOM 3550 O O . GLN B 2 125 ? 38.960 -31.158 -78.649 1.00 72.68 ? 125 GLN B O 1 ATOM 3551 C CB . GLN B 2 125 ? 37.533 -30.465 -75.762 1.00 69.52 ? 125 GLN B CB 1 ATOM 3552 C CG . GLN B 2 125 ? 36.939 -31.122 -74.537 1.00 72.95 ? 125 GLN B CG 1 ATOM 3553 C CD . GLN B 2 125 ? 35.605 -30.507 -74.184 1.00 75.12 ? 125 GLN B CD 1 ATOM 3554 O OE1 . GLN B 2 125 ? 34.590 -30.812 -74.819 1.00 81.36 ? 125 GLN B OE1 1 ATOM 3555 N NE2 . GLN B 2 125 ? 35.596 -29.626 -73.181 1.00 71.56 ? 125 GLN B NE2 1 ATOM 3556 N N . LEU B 2 126 ? 39.555 -29.279 -77.572 1.00 60.75 ? 126 LEU B N 1 ATOM 3557 C CA . LEU B 2 126 ? 39.832 -28.519 -78.766 1.00 62.77 ? 126 LEU B CA 1 ATOM 3558 C C . LEU B 2 126 ? 41.010 -29.053 -79.556 1.00 67.23 ? 126 LEU B C 1 ATOM 3559 O O . LEU B 2 126 ? 41.046 -28.896 -80.759 1.00 70.35 ? 126 LEU B O 1 ATOM 3560 C CB . LEU B 2 126 ? 40.072 -27.039 -78.429 1.00 59.65 ? 126 LEU B CB 1 ATOM 3561 C CG . LEU B 2 126 ? 38.921 -26.346 -77.695 1.00 56.86 ? 126 LEU B CG 1 ATOM 3562 C CD1 . LEU B 2 126 ? 39.182 -24.862 -77.608 1.00 55.12 ? 126 LEU B CD1 1 ATOM 3563 C CD2 . LEU B 2 126 ? 37.591 -26.621 -78.379 1.00 59.45 ? 126 LEU B CD2 1 ATOM 3564 N N . ARG B 2 127 ? 41.976 -29.675 -78.893 1.00 72.28 ? 127 ARG B N 1 ATOM 3565 C CA . ARG B 2 127 ? 43.121 -30.268 -79.599 1.00 77.98 ? 127 ARG B CA 1 ATOM 3566 C C . ARG B 2 127 ? 43.695 -29.265 -80.626 1.00 77.75 ? 127 ARG B C 1 ATOM 3567 O O . ARG B 2 127 ? 44.052 -28.153 -80.244 1.00 75.20 ? 127 ARG B O 1 ATOM 3568 C CB . ARG B 2 127 ? 42.727 -31.625 -80.227 1.00 83.56 ? 127 ARG B CB 1 ATOM 3569 C CG . ARG B 2 127 ? 42.471 -32.729 -79.197 1.00 85.69 ? 127 ARG B CG 1 ATOM 3570 C CD . ARG B 2 127 ? 41.590 -33.851 -79.725 1.00 91.03 ? 127 ARG B CD 1 ATOM 3571 N NE . ARG B 2 127 ? 42.230 -34.606 -80.804 1.00 99.42 ? 127 ARG B NE 1 ATOM 3572 C CZ . ARG B 2 127 ? 41.746 -35.736 -81.322 1.00 107.73 ? 127 ARG B CZ 1 ATOM 3573 N NH1 . ARG B 2 127 ? 40.605 -36.239 -80.862 1.00 110.94 ? 127 ARG B NH1 1 ATOM 3574 N NH2 . ARG B 2 127 ? 42.394 -36.370 -82.306 1.00 112.99 ? 127 ARG B NH2 1 ATOM 3575 N N . ASP B 2 128 ? 43.748 -29.618 -81.910 1.00 79.69 ? 128 ASP B N 1 ATOM 3576 C CA . ASP B 2 128 ? 44.331 -28.721 -82.909 1.00 81.57 ? 128 ASP B CA 1 ATOM 3577 C C . ASP B 2 128 ? 43.281 -27.908 -83.722 1.00 79.65 ? 128 ASP B C 1 ATOM 3578 O O . ASP B 2 128 ? 43.621 -27.271 -84.717 1.00 81.46 ? 128 ASP B O 1 ATOM 3579 C CB . ASP B 2 128 ? 45.253 -29.515 -83.840 1.00 88.57 ? 128 ASP B CB 1 ATOM 3580 C CG . ASP B 2 128 ? 44.539 -30.666 -84.532 1.00 95.03 ? 128 ASP B CG 1 ATOM 3581 O OD1 . ASP B 2 128 ? 43.291 -30.709 -84.517 1.00 95.02 ? 128 ASP B OD1 1 ATOM 3582 O OD2 . ASP B 2 128 ? 45.225 -31.536 -85.098 1.00 105.47 ? 128 ASP B OD2 1 ATOM 3583 N N . ASN B 2 129 ? 42.019 -27.932 -83.295 1.00 75.85 ? 129 ASN B N 1 ATOM 3584 C CA . ASN B 2 129 ? 40.978 -27.104 -83.899 1.00 73.99 ? 129 ASN B CA 1 ATOM 3585 C C . ASN B 2 129 ? 40.948 -25.631 -83.415 1.00 70.75 ? 129 ASN B C 1 ATOM 3586 O O . ASN B 2 129 ? 40.063 -24.882 -83.836 1.00 71.68 ? 129 ASN B O 1 ATOM 3587 C CB . ASN B 2 129 ? 39.603 -27.753 -83.664 1.00 75.59 ? 129 ASN B CB 1 ATOM 3588 C CG . ASN B 2 129 ? 39.385 -29.005 -84.502 1.00 80.92 ? 129 ASN B CG 1 ATOM 3589 O OD1 . ASN B 2 129 ? 40.306 -29.526 -85.134 1.00 86.35 ? 129 ASN B OD1 1 ATOM 3590 N ND2 . ASN B 2 129 ? 38.154 -29.493 -84.511 1.00 81.71 ? 129 ASN B ND2 1 ATOM 3591 N N . ALA B 2 130 ? 41.901 -25.219 -82.565 1.00 67.13 ? 130 ALA B N 1 ATOM 3592 C CA . ALA B 2 130 ? 41.992 -23.840 -82.045 1.00 63.09 ? 130 ALA B CA 1 ATOM 3593 C C . ALA B 2 130 ? 43.431 -23.474 -81.739 1.00 65.22 ? 130 ALA B C 1 ATOM 3594 O O . ALA B 2 130 ? 44.204 -24.361 -81.407 1.00 68.75 ? 130 ALA B O 1 ATOM 3595 C CB . ALA B 2 130 ? 41.193 -23.722 -80.770 1.00 60.56 ? 130 ALA B CB 1 ATOM 3596 N N . LYS B 2 131 ? 43.785 -22.186 -81.818 1.00 65.83 ? 131 LYS B N 1 ATOM 3597 C CA . LYS B 2 131 ? 45.121 -21.701 -81.419 1.00 67.57 ? 131 LYS B CA 1 ATOM 3598 C C . LYS B 2 131 ? 45.158 -21.414 -79.915 1.00 63.84 ? 131 LYS B C 1 ATOM 3599 O O . LYS B 2 131 ? 44.299 -20.722 -79.392 1.00 63.09 ? 131 LYS B O 1 ATOM 3600 C CB . LYS B 2 131 ? 45.497 -20.411 -82.147 1.00 73.50 ? 131 LYS B CB 1 ATOM 3601 C CG . LYS B 2 131 ? 45.590 -20.517 -83.661 1.00 83.47 ? 131 LYS B CG 1 ATOM 3602 C CD . LYS B 2 131 ? 45.416 -19.157 -84.353 1.00 92.35 ? 131 LYS B CD 1 ATOM 3603 C CE . LYS B 2 131 ? 46.219 -19.035 -85.650 1.00 101.66 ? 131 LYS B CE 1 ATOM 3604 N NZ . LYS B 2 131 ? 47.695 -18.885 -85.422 1.00 106.79 ? 131 LYS B NZ 1 ATOM 3605 N N . GLU B 2 132 ? 46.156 -21.940 -79.222 1.00 61.31 ? 132 GLU B N 1 ATOM 3606 C CA . GLU B 2 132 ? 46.330 -21.661 -77.819 1.00 57.94 ? 132 GLU B CA 1 ATOM 3607 C C . GLU B 2 132 ? 47.082 -20.343 -77.694 1.00 60.20 ? 132 GLU B C 1 ATOM 3608 O O . GLU B 2 132 ? 48.281 -20.275 -77.953 1.00 64.26 ? 132 GLU B O 1 ATOM 3609 C CB . GLU B 2 132 ? 47.096 -22.795 -77.164 1.00 58.69 ? 132 GLU B CB 1 ATOM 3610 C CG . GLU B 2 132 ? 47.082 -22.766 -75.654 1.00 56.89 ? 132 GLU B CG 1 ATOM 3611 C CD . GLU B 2 132 ? 47.729 -23.980 -75.014 1.00 58.94 ? 132 GLU B CD 1 ATOM 3612 O OE1 . GLU B 2 132 ? 48.335 -24.821 -75.716 1.00 66.00 ? 132 GLU B OE1 1 ATOM 3613 O OE2 . GLU B 2 132 ? 47.636 -24.087 -73.783 1.00 57.58 ? 132 GLU B OE2 1 ATOM 3614 N N . LEU B 2 133 ? 46.382 -19.287 -77.300 1.00 58.51 ? 133 LEU B N 1 ATOM 3615 C CA . LEU B 2 133 ? 46.963 -17.945 -77.336 1.00 60.18 ? 133 LEU B CA 1 ATOM 3616 C C . LEU B 2 133 ? 47.992 -17.650 -76.251 1.00 60.73 ? 133 LEU B C 1 ATOM 3617 O O . LEU B 2 133 ? 48.818 -16.756 -76.422 1.00 64.02 ? 133 LEU B O 1 ATOM 3618 C CB . LEU B 2 133 ? 45.856 -16.898 -77.287 1.00 60.75 ? 133 LEU B CB 1 ATOM 3619 C CG . LEU B 2 133 ? 44.933 -16.836 -78.509 1.00 61.44 ? 133 LEU B CG 1 ATOM 3620 C CD1 . LEU B 2 133 ? 43.993 -15.658 -78.339 1.00 63.00 ? 133 LEU B CD1 1 ATOM 3621 C CD2 . LEU B 2 133 ? 45.729 -16.690 -79.803 1.00 65.06 ? 133 LEU B CD2 1 ATOM 3622 N N . GLY B 2 134 ? 47.935 -18.383 -75.142 1.00 57.38 ? 134 GLY B N 1 ATOM 3623 C CA . GLY B 2 134 ? 48.886 -18.218 -74.053 1.00 59.26 ? 134 GLY B CA 1 ATOM 3624 C C . GLY B 2 134 ? 48.375 -17.457 -72.843 1.00 59.56 ? 134 GLY B C 1 ATOM 3625 O O . GLY B 2 134 ? 49.141 -17.215 -71.894 1.00 61.07 ? 134 GLY B O 1 ATOM 3626 N N . ASN B 2 135 ? 47.091 -17.090 -72.856 1.00 58.34 ? 135 ASN B N 1 ATOM 3627 C CA . ASN B 2 135 ? 46.541 -16.184 -71.843 1.00 58.02 ? 135 ASN B CA 1 ATOM 3628 C C . ASN B 2 135 ? 45.238 -16.668 -71.243 1.00 54.14 ? 135 ASN B C 1 ATOM 3629 O O . ASN B 2 135 ? 44.543 -15.915 -70.563 1.00 56.10 ? 135 ASN B O 1 ATOM 3630 C CB . ASN B 2 135 ? 46.327 -14.802 -72.451 1.00 62.14 ? 135 ASN B CB 1 ATOM 3631 C CG . ASN B 2 135 ? 45.317 -14.815 -73.577 1.00 62.90 ? 135 ASN B CG 1 ATOM 3632 O OD1 . ASN B 2 135 ? 44.896 -15.871 -74.059 1.00 61.80 ? 135 ASN B OD1 1 ATOM 3633 N ND2 . ASN B 2 135 ? 44.934 -13.639 -74.014 1.00 66.78 ? 135 ASN B ND2 1 ATOM 3634 N N . GLY B 2 136 ? 44.904 -17.924 -71.495 1.00 50.96 ? 136 GLY B N 1 ATOM 3635 C CA . GLY B 2 136 ? 43.645 -18.482 -71.037 1.00 47.38 ? 136 GLY B CA 1 ATOM 3636 C C . GLY B 2 136 ? 42.683 -18.702 -72.180 1.00 47.21 ? 136 GLY B C 1 ATOM 3637 O O . GLY B 2 136 ? 41.682 -19.396 -72.019 1.00 47.38 ? 136 GLY B O 1 ATOM 3638 N N . CYS B 2 137 ? 42.999 -18.147 -73.340 1.00 50.22 ? 137 CYS B N 1 ATOM 3639 C CA . CYS B 2 137 ? 42.069 -18.121 -74.446 1.00 52.82 ? 137 CYS B CA 1 ATOM 3640 C C . CYS B 2 137 ? 42.491 -19.067 -75.571 1.00 53.74 ? 137 CYS B C 1 ATOM 3641 O O . CYS B 2 137 ? 43.686 -19.346 -75.784 1.00 55.07 ? 137 CYS B O 1 ATOM 3642 C CB . CYS B 2 137 ? 41.922 -16.695 -74.980 1.00 56.42 ? 137 CYS B CB 1 ATOM 3643 S SG . CYS B 2 137 ? 41.274 -15.470 -73.805 1.00 60.83 ? 137 CYS B SG 1 ATOM 3644 N N . PHE B 2 138 ? 41.477 -19.545 -76.283 1.00 53.06 ? 138 PHE B N 1 ATOM 3645 C CA . PHE B 2 138 ? 41.643 -20.352 -77.465 1.00 53.19 ? 138 PHE B CA 1 ATOM 3646 C C . PHE B 2 138 ? 40.953 -19.628 -78.588 1.00 55.27 ? 138 PHE B C 1 ATOM 3647 O O . PHE B 2 138 ? 39.790 -19.289 -78.466 1.00 56.40 ? 138 PHE B O 1 ATOM 3648 C CB . PHE B 2 138 ? 40.998 -21.727 -77.276 1.00 51.58 ? 138 PHE B CB 1 ATOM 3649 C CG . PHE B 2 138 ? 41.649 -22.545 -76.203 1.00 50.42 ? 138 PHE B CG 1 ATOM 3650 C CD1 . PHE B 2 138 ? 42.823 -23.250 -76.455 1.00 51.32 ? 138 PHE B CD1 1 ATOM 3651 C CD2 . PHE B 2 138 ? 41.110 -22.572 -74.928 1.00 50.10 ? 138 PHE B CD2 1 ATOM 3652 C CE1 . PHE B 2 138 ? 43.427 -23.986 -75.454 1.00 52.39 ? 138 PHE B CE1 1 ATOM 3653 C CE2 . PHE B 2 138 ? 41.705 -23.296 -73.919 1.00 50.15 ? 138 PHE B CE2 1 ATOM 3654 C CZ . PHE B 2 138 ? 42.880 -23.992 -74.175 1.00 52.02 ? 138 PHE B CZ 1 ATOM 3655 N N . GLU B 2 139 ? 41.664 -19.405 -79.682 1.00 56.86 ? 139 GLU B N 1 ATOM 3656 C CA . GLU B 2 139 ? 41.097 -18.774 -80.829 1.00 60.20 ? 139 GLU B CA 1 ATOM 3657 C C . GLU B 2 139 ? 40.818 -19.848 -81.875 1.00 61.07 ? 139 GLU B C 1 ATOM 3658 O O . GLU B 2 139 ? 41.727 -20.527 -82.340 1.00 62.38 ? 139 GLU B O 1 ATOM 3659 C CB . GLU B 2 139 ? 42.062 -17.728 -81.343 1.00 64.82 ? 139 GLU B CB 1 ATOM 3660 C CG . GLU B 2 139 ? 41.563 -16.952 -82.545 1.00 69.30 ? 139 GLU B CG 1 ATOM 3661 C CD . GLU B 2 139 ? 42.663 -16.084 -83.104 1.00 76.56 ? 139 GLU B CD 1 ATOM 3662 O OE1 . GLU B 2 139 ? 43.186 -15.232 -82.351 1.00 80.16 ? 139 GLU B OE1 1 ATOM 3663 O OE2 . GLU B 2 139 ? 43.023 -16.268 -84.287 1.00 83.37 ? 139 GLU B OE2 1 ATOM 3664 N N . PHE B 2 140 ? 39.552 -19.997 -82.238 1.00 62.61 ? 140 PHE B N 1 ATOM 3665 C CA . PHE B 2 140 ? 39.106 -21.087 -83.102 1.00 64.68 ? 140 PHE B CA 1 ATOM 3666 C C . PHE B 2 140 ? 39.516 -20.940 -84.566 1.00 67.93 ? 140 PHE B C 1 ATOM 3667 O O . PHE B 2 140 ? 39.636 -19.825 -85.074 1.00 69.68 ? 140 PHE B O 1 ATOM 3668 C CB . PHE B 2 140 ? 37.586 -21.193 -83.053 1.00 64.04 ? 140 PHE B CB 1 ATOM 3669 C CG . PHE B 2 140 ? 37.059 -21.684 -81.759 1.00 61.79 ? 140 PHE B CG 1 ATOM 3670 C CD1 . PHE B 2 140 ? 36.739 -20.802 -80.754 1.00 61.51 ? 140 PHE B CD1 1 ATOM 3671 C CD2 . PHE B 2 140 ? 36.863 -23.037 -81.550 1.00 61.95 ? 140 PHE B CD2 1 ATOM 3672 C CE1 . PHE B 2 140 ? 36.227 -21.257 -79.554 1.00 59.87 ? 140 PHE B CE1 1 ATOM 3673 C CE2 . PHE B 2 140 ? 36.346 -23.505 -80.353 1.00 61.14 ? 140 PHE B CE2 1 ATOM 3674 C CZ . PHE B 2 140 ? 36.029 -22.613 -79.353 1.00 59.62 ? 140 PHE B CZ 1 ATOM 3675 N N . TYR B 2 141 ? 39.695 -22.071 -85.251 1.00 70.26 ? 141 TYR B N 1 ATOM 3676 C CA . TYR B 2 141 ? 39.941 -22.038 -86.703 1.00 74.77 ? 141 TYR B CA 1 ATOM 3677 C C . TYR B 2 141 ? 38.647 -21.898 -87.465 1.00 74.90 ? 141 TYR B C 1 ATOM 3678 O O . TYR B 2 141 ? 38.580 -21.153 -88.420 1.00 80.62 ? 141 TYR B O 1 ATOM 3679 C CB . TYR B 2 141 ? 40.729 -23.258 -87.178 1.00 76.80 ? 141 TYR B CB 1 ATOM 3680 C CG . TYR B 2 141 ? 42.140 -23.219 -86.669 1.00 77.32 ? 141 TYR B CG 1 ATOM 3681 C CD1 . TYR B 2 141 ? 42.993 -22.196 -87.048 1.00 80.35 ? 141 TYR B CD1 1 ATOM 3682 C CD2 . TYR B 2 141 ? 42.604 -24.163 -85.767 1.00 77.47 ? 141 TYR B CD2 1 ATOM 3683 C CE1 . TYR B 2 141 ? 44.280 -22.130 -86.575 1.00 82.49 ? 141 TYR B CE1 1 ATOM 3684 C CE2 . TYR B 2 141 ? 43.895 -24.109 -85.280 1.00 79.05 ? 141 TYR B CE2 1 ATOM 3685 C CZ . TYR B 2 141 ? 44.733 -23.091 -85.695 1.00 82.17 ? 141 TYR B CZ 1 ATOM 3686 O OH . TYR B 2 141 ? 46.026 -23.010 -85.227 1.00 87.15 ? 141 TYR B OH 1 ATOM 3687 N N . HIS B 2 142 ? 37.617 -22.607 -87.030 1.00 93.36 ? 142 HIS B N 1 ATOM 3688 C CA . HIS B 2 142 ? 36.287 -22.447 -87.600 1.00 93.28 ? 142 HIS B CA 1 ATOM 3689 C C . HIS B 2 142 ? 35.547 -21.328 -86.883 1.00 89.38 ? 142 HIS B C 1 ATOM 3690 O O . HIS B 2 142 ? 35.978 -20.867 -85.831 1.00 85.24 ? 142 HIS B O 1 ATOM 3691 C CB . HIS B 2 142 ? 35.500 -23.755 -87.481 1.00 93.38 ? 142 HIS B CB 1 ATOM 3692 C CG . HIS B 2 142 ? 35.472 -24.325 -86.098 1.00 87.74 ? 142 HIS B CG 1 ATOM 3693 N ND1 . HIS B 2 142 ? 34.431 -24.104 -85.222 1.00 84.25 ? 142 HIS B ND1 1 ATOM 3694 C CD2 . HIS B 2 142 ? 36.366 -25.097 -85.434 1.00 86.26 ? 142 HIS B CD2 1 ATOM 3695 C CE1 . HIS B 2 142 ? 34.680 -24.727 -84.083 1.00 80.39 ? 142 HIS B CE1 1 ATOM 3696 N NE2 . HIS B 2 142 ? 35.847 -25.336 -84.186 1.00 81.66 ? 142 HIS B NE2 1 ATOM 3697 N N . LYS B 2 143 ? 34.435 -20.877 -87.454 1.00 93.18 ? 143 LYS B N 1 ATOM 3698 C CA . LYS B 2 143 ? 33.515 -20.025 -86.707 1.00 90.76 ? 143 LYS B CA 1 ATOM 3699 C C . LYS B 2 143 ? 32.847 -20.886 -85.657 1.00 86.23 ? 143 LYS B C 1 ATOM 3700 O O . LYS B 2 143 ? 32.594 -22.072 -85.892 1.00 86.90 ? 143 LYS B O 1 ATOM 3701 C CB . LYS B 2 143 ? 32.452 -19.399 -87.591 1.00 96.93 ? 143 LYS B CB 1 ATOM 3702 C CG . LYS B 2 143 ? 32.922 -18.187 -88.380 1.00 104.00 ? 143 LYS B CG 1 ATOM 3703 C CD . LYS B 2 143 ? 31.841 -17.114 -88.438 1.00 108.05 ? 143 LYS B CD 1 ATOM 3704 C CE . LYS B 2 143 ? 30.512 -17.633 -88.986 1.00 113.42 ? 143 LYS B CE 1 ATOM 3705 N NZ . LYS B 2 143 ? 29.386 -17.304 -88.057 1.00 111.44 ? 143 LYS B NZ 1 ATOM 3706 N N . CYS B 2 144 ? 32.582 -20.288 -84.498 1.00 80.64 ? 144 CYS B N 1 ATOM 3707 C CA . CYS B 2 144 ? 32.034 -21.012 -83.364 1.00 76.77 ? 144 CYS B CA 1 ATOM 3708 C C . CYS B 2 144 ? 30.875 -20.206 -82.798 1.00 77.21 ? 144 CYS B C 1 ATOM 3709 O O . CYS B 2 144 ? 31.069 -19.367 -81.926 1.00 78.22 ? 144 CYS B O 1 ATOM 3710 C CB . CYS B 2 144 ? 33.129 -21.226 -82.309 1.00 72.78 ? 144 CYS B CB 1 ATOM 3711 S SG . CYS B 2 144 ? 32.761 -22.433 -81.007 1.00 70.63 ? 144 CYS B SG 1 ATOM 3712 N N . ASP B 2 145 ? 29.669 -20.459 -83.309 1.00 80.23 ? 145 ASP B N 1 ATOM 3713 C CA . ASP B 2 145 ? 28.462 -19.764 -82.856 1.00 79.97 ? 145 ASP B CA 1 ATOM 3714 C C . ASP B 2 145 ? 28.104 -20.178 -81.418 1.00 75.86 ? 145 ASP B C 1 ATOM 3715 O O . ASP B 2 145 ? 28.815 -20.968 -80.813 1.00 73.68 ? 145 ASP B O 1 ATOM 3716 C CB . ASP B 2 145 ? 27.291 -20.011 -83.834 1.00 85.20 ? 145 ASP B CB 1 ATOM 3717 C CG . ASP B 2 145 ? 26.910 -21.480 -83.953 1.00 87.69 ? 145 ASP B CG 1 ATOM 3718 O OD1 . ASP B 2 145 ? 27.405 -22.304 -83.169 1.00 85.70 ? 145 ASP B OD1 1 ATOM 3719 O OD2 . ASP B 2 145 ? 26.113 -21.819 -84.844 1.00 94.11 ? 145 ASP B OD2 1 ATOM 3720 N N . ASN B 2 146 ? 27.002 -19.662 -80.878 1.00 76.79 ? 146 ASN B N 1 ATOM 3721 C CA . ASN B 2 146 ? 26.653 -19.929 -79.482 1.00 74.20 ? 146 ASN B CA 1 ATOM 3722 C C . ASN B 2 146 ? 26.474 -21.402 -79.172 1.00 77.42 ? 146 ASN B C 1 ATOM 3723 O O . ASN B 2 146 ? 26.936 -21.875 -78.138 1.00 76.17 ? 146 ASN B O 1 ATOM 3724 C CB . ASN B 2 146 ? 25.419 -19.135 -79.064 1.00 75.11 ? 146 ASN B CB 1 ATOM 3725 C CG . ASN B 2 146 ? 25.668 -17.636 -79.055 1.00 72.85 ? 146 ASN B CG 1 ATOM 3726 O OD1 . ASN B 2 146 ? 26.800 -17.169 -78.941 1.00 67.98 ? 146 ASN B OD1 1 ATOM 3727 N ND2 . ASN B 2 146 ? 24.607 -16.876 -79.171 1.00 77.05 ? 146 ASN B ND2 1 ATOM 3728 N N . GLU B 2 147 ? 25.839 -22.136 -80.075 1.00 85.33 ? 147 GLU B N 1 ATOM 3729 C CA . GLU B 2 147 ? 25.712 -23.592 -79.923 1.00 91.29 ? 147 GLU B CA 1 ATOM 3730 C C . GLU B 2 147 ? 27.084 -24.283 -79.886 1.00 84.42 ? 147 GLU B C 1 ATOM 3731 O O . GLU B 2 147 ? 27.311 -25.205 -79.104 1.00 83.14 ? 147 GLU B O 1 ATOM 3732 C CB . GLU B 2 147 ? 24.875 -24.196 -81.055 1.00 101.41 ? 147 GLU B CB 1 ATOM 3733 C CG . GLU B 2 147 ? 23.451 -23.672 -81.125 1.00 111.89 ? 147 GLU B CG 1 ATOM 3734 C CD . GLU B 2 147 ? 23.320 -22.456 -82.032 1.00 116.07 ? 147 GLU B CD 1 ATOM 3735 O OE1 . GLU B 2 147 ? 23.853 -21.374 -81.678 1.00 112.10 ? 147 GLU B OE1 1 ATOM 3736 O OE2 . GLU B 2 147 ? 22.683 -22.591 -83.103 1.00 125.19 ? 147 GLU B OE2 1 ATOM 3737 N N . CYS B 2 148 ? 27.984 -23.836 -80.749 1.00 80.28 ? 148 CYS B N 1 ATOM 3738 C CA . CYS B 2 148 ? 29.360 -24.315 -80.750 1.00 77.93 ? 148 CYS B CA 1 ATOM 3739 C C . CYS B 2 148 ? 30.012 -24.021 -79.391 1.00 71.83 ? 148 CYS B C 1 ATOM 3740 O O . CYS B 2 148 ? 30.514 -24.925 -78.716 1.00 70.87 ? 148 CYS B O 1 ATOM 3741 C CB . CYS B 2 148 ? 30.116 -23.632 -81.890 1.00 78.93 ? 148 CYS B CB 1 ATOM 3742 S SG . CYS B 2 148 ? 31.875 -23.987 -82.007 1.00 81.48 ? 148 CYS B SG 1 ATOM 3743 N N . MET B 2 149 ? 29.963 -22.761 -78.970 1.00 67.07 ? 149 MET B N 1 ATOM 3744 C CA . MET B 2 149 ? 30.526 -22.384 -77.684 1.00 63.17 ? 149 MET B CA 1 ATOM 3745 C C . MET B 2 149 ? 29.970 -23.252 -76.566 1.00 65.10 ? 149 MET B C 1 ATOM 3746 O O . MET B 2 149 ? 30.716 -23.707 -75.694 1.00 64.20 ? 149 MET B O 1 ATOM 3747 C CB . MET B 2 149 ? 30.258 -20.918 -77.382 1.00 61.13 ? 149 MET B CB 1 ATOM 3748 C CG . MET B 2 149 ? 30.981 -19.950 -78.291 1.00 60.33 ? 149 MET B CG 1 ATOM 3749 S SD . MET B 2 149 ? 32.775 -20.119 -78.242 1.00 60.36 ? 149 MET B SD 1 ATOM 3750 C CE . MET B 2 149 ? 33.211 -18.751 -79.315 1.00 61.40 ? 149 MET B CE 1 ATOM 3751 N N . GLU B 2 150 ? 28.664 -23.491 -76.598 1.00 70.19 ? 150 GLU B N 1 ATOM 3752 C CA . GLU B 2 150 ? 28.001 -24.269 -75.552 1.00 74.39 ? 150 GLU B CA 1 ATOM 3753 C C . GLU B 2 150 ? 28.524 -25.699 -75.486 1.00 75.51 ? 150 GLU B C 1 ATOM 3754 O O . GLU B 2 150 ? 28.597 -26.267 -74.403 1.00 77.91 ? 150 GLU B O 1 ATOM 3755 C CB . GLU B 2 150 ? 26.474 -24.228 -75.740 1.00 81.37 ? 150 GLU B CB 1 ATOM 3756 C CG . GLU B 2 150 ? 25.645 -25.176 -74.870 1.00 89.33 ? 150 GLU B CG 1 ATOM 3757 C CD . GLU B 2 150 ? 25.670 -24.866 -73.379 1.00 91.15 ? 150 GLU B CD 1 ATOM 3758 O OE1 . GLU B 2 150 ? 26.358 -23.919 -72.940 1.00 89.60 ? 150 GLU B OE1 1 ATOM 3759 O OE2 . GLU B 2 150 ? 24.982 -25.590 -72.630 1.00 98.40 ? 150 GLU B OE2 1 ATOM 3760 N N . SER B 2 151 ? 28.898 -26.271 -76.628 1.00 75.12 ? 151 SER B N 1 ATOM 3761 C CA . SER B 2 151 ? 29.402 -27.645 -76.660 1.00 78.63 ? 151 SER B CA 1 ATOM 3762 C C . SER B 2 151 ? 30.796 -27.757 -76.028 1.00 76.90 ? 151 SER B C 1 ATOM 3763 O O . SER B 2 151 ? 31.158 -28.805 -75.483 1.00 81.16 ? 151 SER B O 1 ATOM 3764 C CB . SER B 2 151 ? 29.441 -28.178 -78.092 1.00 81.26 ? 151 SER B CB 1 ATOM 3765 O OG . SER B 2 151 ? 30.513 -27.606 -78.818 1.00 78.01 ? 151 SER B OG 1 ATOM 3766 N N . VAL B 2 152 ? 31.578 -26.681 -76.113 1.00 72.54 ? 152 VAL B N 1 ATOM 3767 C CA . VAL B 2 152 ? 32.868 -26.604 -75.426 1.00 69.56 ? 152 VAL B CA 1 ATOM 3768 C C . VAL B 2 152 ? 32.632 -26.627 -73.911 1.00 70.55 ? 152 VAL B C 1 ATOM 3769 O O . VAL B 2 152 ? 33.291 -27.370 -73.188 1.00 69.43 ? 152 VAL B O 1 ATOM 3770 C CB . VAL B 2 152 ? 33.660 -25.347 -75.842 1.00 65.37 ? 152 VAL B CB 1 ATOM 3771 C CG1 . VAL B 2 152 ? 35.016 -25.320 -75.172 1.00 65.35 ? 152 VAL B CG1 1 ATOM 3772 C CG2 . VAL B 2 152 ? 33.851 -25.317 -77.347 1.00 66.37 ? 152 VAL B CG2 1 ATOM 3773 N N . ARG B 2 153 ? 31.662 -25.844 -73.447 1.00 71.41 ? 153 ARG B N 1 ATOM 3774 C CA . ARG B 2 153 ? 31.301 -25.845 -72.029 1.00 75.25 ? 153 ARG B CA 1 ATOM 3775 C C . ARG B 2 153 ? 30.587 -27.115 -71.600 1.00 82.45 ? 153 ARG B C 1 ATOM 3776 O O . ARG B 2 153 ? 30.625 -27.461 -70.426 1.00 84.14 ? 153 ARG B O 1 ATOM 3777 C CB . ARG B 2 153 ? 30.388 -24.673 -71.701 1.00 75.07 ? 153 ARG B CB 1 ATOM 3778 C CG . ARG B 2 153 ? 30.922 -23.311 -72.075 1.00 70.92 ? 153 ARG B CG 1 ATOM 3779 C CD . ARG B 2 153 ? 30.010 -22.252 -71.492 1.00 73.27 ? 153 ARG B CD 1 ATOM 3780 N NE . ARG B 2 153 ? 29.929 -21.109 -72.387 1.00 73.55 ? 153 ARG B NE 1 ATOM 3781 C CZ . ARG B 2 153 ? 28.978 -20.904 -73.293 1.00 75.09 ? 153 ARG B CZ 1 ATOM 3782 N NH1 . ARG B 2 153 ? 27.964 -21.752 -73.435 1.00 78.58 ? 153 ARG B NH1 1 ATOM 3783 N NH2 . ARG B 2 153 ? 29.042 -19.825 -74.066 1.00 76.46 ? 153 ARG B NH2 1 ATOM 3784 N N . ASN B 2 154 ? 29.888 -27.755 -72.543 1.00 89.19 ? 154 ASN B N 1 ATOM 3785 C CA . ASN B 2 154 ? 29.235 -29.055 -72.336 1.00 98.63 ? 154 ASN B CA 1 ATOM 3786 C C . ASN B 2 154 ? 30.204 -30.153 -71.946 1.00 99.98 ? 154 ASN B C 1 ATOM 3787 O O . ASN B 2 154 ? 29.907 -30.968 -71.077 1.00 107.17 ? 154 ASN B O 1 ATOM 3788 C CB . ASN B 2 154 ? 28.565 -29.541 -73.632 1.00 105.84 ? 154 ASN B CB 1 ATOM 3789 C CG . ASN B 2 154 ? 27.129 -29.090 -73.775 1.00 117.25 ? 154 ASN B CG 1 ATOM 3790 O OD1 . ASN B 2 154 ? 26.630 -28.280 -72.999 1.00 117.27 ? 154 ASN B OD1 1 ATOM 3791 N ND2 . ASN B 2 154 ? 26.450 -29.624 -74.783 1.00 132.59 ? 154 ASN B ND2 1 ATOM 3792 N N . GLY B 2 155 ? 31.356 -30.172 -72.614 1.00 94.42 ? 155 GLY B N 1 ATOM 3793 C CA . GLY B 2 155 ? 32.225 -31.346 -72.663 1.00 95.29 ? 155 GLY B CA 1 ATOM 3794 C C . GLY B 2 155 ? 31.980 -32.113 -73.954 1.00 95.56 ? 155 GLY B C 1 ATOM 3795 O O . GLY B 2 155 ? 32.541 -33.186 -74.166 1.00 99.74 ? 155 GLY B O 1 ATOM 3796 N N . THR B 2 156 ? 31.169 -31.532 -74.832 1.00 92.11 ? 156 THR B N 1 ATOM 3797 C CA . THR B 2 156 ? 30.603 -32.230 -75.982 1.00 95.22 ? 156 THR B CA 1 ATOM 3798 C C . THR B 2 156 ? 31.238 -31.799 -77.291 1.00 90.85 ? 156 THR B C 1 ATOM 3799 O O . THR B 2 156 ? 30.882 -32.312 -78.336 1.00 94.27 ? 156 THR B O 1 ATOM 3800 C CB . THR B 2 156 ? 29.081 -31.960 -76.042 1.00 98.80 ? 156 THR B CB 1 ATOM 3801 O OG1 . THR B 2 156 ? 28.436 -32.678 -74.983 1.00 103.47 ? 156 THR B OG1 1 ATOM 3802 C CG2 . THR B 2 156 ? 28.450 -32.367 -77.378 1.00 103.86 ? 156 THR B CG2 1 ATOM 3803 N N . TYR B 2 157 ? 32.183 -30.870 -77.241 1.00 85.52 ? 157 TYR B N 1 ATOM 3804 C CA . TYR B 2 157 ? 32.741 -30.284 -78.463 1.00 83.51 ? 157 TYR B CA 1 ATOM 3805 C C . TYR B 2 157 ? 33.143 -31.349 -79.467 1.00 90.17 ? 157 TYR B C 1 ATOM 3806 O O . TYR B 2 157 ? 34.111 -32.085 -79.250 1.00 91.00 ? 157 TYR B O 1 ATOM 3807 C CB . TYR B 2 157 ? 33.958 -29.419 -78.156 1.00 77.16 ? 157 TYR B CB 1 ATOM 3808 C CG . TYR B 2 157 ? 34.612 -28.852 -79.399 1.00 74.83 ? 157 TYR B CG 1 ATOM 3809 C CD1 . TYR B 2 157 ? 34.030 -27.794 -80.094 1.00 72.80 ? 157 TYR B CD1 1 ATOM 3810 C CD2 . TYR B 2 157 ? 35.805 -29.374 -79.884 1.00 75.47 ? 157 TYR B CD2 1 ATOM 3811 C CE1 . TYR B 2 157 ? 34.624 -27.263 -81.227 1.00 71.82 ? 157 TYR B CE1 1 ATOM 3812 C CE2 . TYR B 2 157 ? 36.399 -28.850 -81.019 1.00 75.57 ? 157 TYR B CE2 1 ATOM 3813 C CZ . TYR B 2 157 ? 35.805 -27.795 -81.680 1.00 72.96 ? 157 TYR B CZ 1 ATOM 3814 O OH . TYR B 2 157 ? 36.403 -27.270 -82.792 1.00 73.18 ? 157 TYR B OH 1 ATOM 3815 N N . ASP B 2 158 ? 32.402 -31.412 -80.568 1.00 96.65 ? 158 ASP B N 1 ATOM 3816 C CA . ASP B 2 158 ? 32.603 -32.461 -81.562 1.00 105.48 ? 158 ASP B CA 1 ATOM 3817 C C . ASP B 2 158 ? 33.793 -32.105 -82.452 1.00 106.43 ? 158 ASP B C 1 ATOM 3818 O O . ASP B 2 158 ? 33.680 -31.322 -83.405 1.00 106.15 ? 158 ASP B O 1 ATOM 3819 C CB . ASP B 2 158 ? 31.330 -32.709 -82.377 1.00 109.86 ? 158 ASP B CB 1 ATOM 3820 C CG . ASP B 2 158 ? 31.321 -34.067 -83.016 1.00 117.66 ? 158 ASP B CG 1 ATOM 3821 O OD1 . ASP B 2 158 ? 32.330 -34.419 -83.657 1.00 119.21 ? 158 ASP B OD1 1 ATOM 3822 O OD2 . ASP B 2 158 ? 30.316 -34.791 -82.865 1.00 124.11 ? 158 ASP B OD2 1 ATOM 3823 N N . TYR B 2 159 ? 34.937 -32.692 -82.110 1.00 108.16 ? 159 TYR B N 1 ATOM 3824 C CA . TYR B 2 159 ? 36.195 -32.373 -82.755 1.00 107.80 ? 159 TYR B CA 1 ATOM 3825 C C . TYR B 2 159 ? 36.199 -32.791 -84.233 1.00 116.93 ? 159 TYR B C 1 ATOM 3826 O O . TYR B 2 159 ? 36.526 -31.969 -85.094 1.00 118.40 ? 159 TYR B O 1 ATOM 3827 C CB . TYR B 2 159 ? 37.357 -32.991 -81.971 1.00 106.68 ? 159 TYR B CB 1 ATOM 3828 C CG . TYR B 2 159 ? 38.670 -33.004 -82.708 1.00 107.55 ? 159 TYR B CG 1 ATOM 3829 C CD1 . TYR B 2 159 ? 39.554 -31.937 -82.604 1.00 102.96 ? 159 TYR B CD1 1 ATOM 3830 C CD2 . TYR B 2 159 ? 39.030 -34.086 -83.511 1.00 113.66 ? 159 TYR B CD2 1 ATOM 3831 C CE1 . TYR B 2 159 ? 40.758 -31.947 -83.276 1.00 107.01 ? 159 TYR B CE1 1 ATOM 3832 C CE2 . TYR B 2 159 ? 40.234 -34.105 -84.187 1.00 116.34 ? 159 TYR B CE2 1 ATOM 3833 C CZ . TYR B 2 159 ? 41.094 -33.035 -84.065 1.00 113.10 ? 159 TYR B CZ 1 ATOM 3834 O OH . TYR B 2 159 ? 42.289 -33.058 -84.733 1.00 116.78 ? 159 TYR B OH 1 ATOM 3835 N N . PRO B 2 160 ? 35.830 -34.058 -84.537 1.00 125.82 ? 160 PRO B N 1 ATOM 3836 C CA . PRO B 2 160 ? 35.748 -34.446 -85.962 1.00 133.77 ? 160 PRO B CA 1 ATOM 3837 C C . PRO B 2 160 ? 34.830 -33.554 -86.826 1.00 133.53 ? 160 PRO B C 1 ATOM 3838 O O . PRO B 2 160 ? 35.147 -33.302 -87.990 1.00 136.31 ? 160 PRO B O 1 ATOM 3839 C CB . PRO B 2 160 ? 35.226 -35.890 -85.908 1.00 140.30 ? 160 PRO B CB 1 ATOM 3840 C CG . PRO B 2 160 ? 35.677 -36.399 -84.581 1.00 137.80 ? 160 PRO B CG 1 ATOM 3841 C CD . PRO B 2 160 ? 35.621 -35.219 -83.645 1.00 128.21 ? 160 PRO B CD 1 ATOM 3842 N N . GLN B 2 161 ? 33.726 -33.066 -86.257 1.00 130.54 ? 161 GLN B N 1 ATOM 3843 C CA . GLN B 2 161 ? 32.811 -32.169 -86.983 1.00 131.24 ? 161 GLN B CA 1 ATOM 3844 C C . GLN B 2 161 ? 33.510 -30.896 -87.488 1.00 125.32 ? 161 GLN B C 1 ATOM 3845 O O . GLN B 2 161 ? 33.082 -30.307 -88.480 1.00 129.85 ? 161 GLN B O 1 ATOM 3846 C CB . GLN B 2 161 ? 31.606 -31.792 -86.110 1.00 130.12 ? 161 GLN B CB 1 ATOM 3847 C CG . GLN B 2 161 ? 30.445 -31.163 -86.874 1.00 134.67 ? 161 GLN B CG 1 ATOM 3848 C CD . GLN B 2 161 ? 29.363 -30.618 -85.957 1.00 133.23 ? 161 GLN B CD 1 ATOM 3849 O OE1 . GLN B 2 161 ? 29.024 -31.231 -84.946 1.00 133.84 ? 161 GLN B OE1 1 ATOM 3850 N NE2 . GLN B 2 161 ? 28.815 -29.460 -86.307 1.00 132.64 ? 161 GLN B NE2 1 ATOM 3851 N N . TYR B 2 162 ? 34.571 -30.475 -86.805 1.00 116.06 ? 162 TYR B N 1 ATOM 3852 C CA . TYR B 2 162 ? 35.399 -29.379 -87.277 1.00 111.60 ? 162 TYR B CA 1 ATOM 3853 C C . TYR B 2 162 ? 36.820 -29.871 -87.501 1.00 111.65 ? 162 TYR B C 1 ATOM 3854 O O . TYR B 2 162 ? 37.548 -29.325 -88.321 1.00 111.64 ? 162 TYR B O 1 ATOM 3855 C CB . TYR B 2 162 ? 35.390 -28.236 -86.268 1.00 104.39 ? 162 TYR B CB 1 ATOM 3856 C CG . TYR B 2 162 ? 34.010 -27.801 -85.804 1.00 102.07 ? 162 TYR B CG 1 ATOM 3857 C CD1 . TYR B 2 162 ? 33.239 -26.913 -86.560 1.00 104.17 ? 162 TYR B CD1 1 ATOM 3858 C CD2 . TYR B 2 162 ? 33.482 -28.263 -84.594 1.00 98.93 ? 162 TYR B CD2 1 ATOM 3859 C CE1 . TYR B 2 162 ? 31.980 -26.501 -86.123 1.00 102.75 ? 162 TYR B CE1 1 ATOM 3860 C CE2 . TYR B 2 162 ? 32.225 -27.864 -84.150 1.00 97.71 ? 162 TYR B CE2 1 ATOM 3861 C CZ . TYR B 2 162 ? 31.475 -26.981 -84.912 1.00 99.57 ? 162 TYR B CZ 1 ATOM 3862 O OH . TYR B 2 162 ? 30.224 -26.591 -84.465 1.00 98.14 ? 162 TYR B OH 1 HETATM 3863 C C1 . NAG C 3 . ? 49.631 -6.338 -43.194 1.00 67.83 ? 1023 NAG A C1 1 HETATM 3864 C C2 . NAG C 3 . ? 50.981 -5.701 -42.877 1.00 79.66 ? 1023 NAG A C2 1 HETATM 3865 C C3 . NAG C 3 . ? 50.988 -5.020 -41.508 1.00 83.25 ? 1023 NAG A C3 1 HETATM 3866 C C4 . NAG C 3 . ? 49.749 -4.149 -41.315 1.00 84.58 ? 1023 NAG A C4 1 HETATM 3867 C C5 . NAG C 3 . ? 48.548 -5.082 -41.467 1.00 83.41 ? 1023 NAG A C5 1 HETATM 3868 C C6 . NAG C 3 . ? 47.213 -4.489 -40.993 1.00 81.41 ? 1023 NAG A C6 1 HETATM 3869 C C7 . NAG C 3 . ? 52.963 -6.875 -43.792 1.00 83.32 ? 1023 NAG A C7 1 HETATM 3870 C C8 . NAG C 3 . ? 53.962 -7.992 -43.620 1.00 81.37 ? 1023 NAG A C8 1 HETATM 3871 N N2 . NAG C 3 . ? 52.013 -6.737 -42.855 1.00 86.51 ? 1023 NAG A N2 1 HETATM 3872 O O3 . NAG C 3 . ? 52.172 -4.272 -41.359 1.00 88.34 ? 1023 NAG A O3 1 HETATM 3873 O O4 . NAG C 3 . ? 49.780 -3.535 -40.042 1.00 88.99 ? 1023 NAG A O4 1 HETATM 3874 O O5 . NAG C 3 . ? 48.523 -5.517 -42.824 1.00 74.44 ? 1023 NAG A O5 1 HETATM 3875 O O6 . NAG C 3 . ? 46.665 -3.645 -41.974 1.00 88.17 ? 1023 NAG A O6 1 HETATM 3876 O O7 . NAG C 3 . ? 53.045 -6.145 -44.776 1.00 82.72 ? 1023 NAG A O7 1 HETATM 3877 C C1 . NAG D 3 . ? 21.831 -40.010 14.082 1.00 82.05 ? 1165 NAG A C1 1 HETATM 3878 C C2 . NAG D 3 . ? 22.686 -41.234 14.389 1.00 88.32 ? 1165 NAG A C2 1 HETATM 3879 C C3 . NAG D 3 . ? 22.265 -42.345 13.413 1.00 89.67 ? 1165 NAG A C3 1 HETATM 3880 C C4 . NAG D 3 . ? 20.767 -42.637 13.599 1.00 93.98 ? 1165 NAG A C4 1 HETATM 3881 C C5 . NAG D 3 . ? 19.954 -41.352 13.398 1.00 96.87 ? 1165 NAG A C5 1 HETATM 3882 C C6 . NAG D 3 . ? 18.452 -41.534 13.668 1.00 104.77 ? 1165 NAG A C6 1 HETATM 3883 C C7 . NAG D 3 . ? 25.166 -41.571 14.671 1.00 105.82 ? 1165 NAG A C7 1 HETATM 3884 C C8 . NAG D 3 . ? 25.026 -43.012 15.069 1.00 105.54 ? 1165 NAG A C8 1 HETATM 3885 N N2 . NAG D 3 . ? 24.090 -40.815 14.369 1.00 95.18 ? 1165 NAG A N2 1 HETATM 3886 O O3 . NAG D 3 . ? 22.961 -43.561 13.561 1.00 94.22 ? 1165 NAG A O3 1 HETATM 3887 O O4 . NAG D 3 . ? 20.342 -43.677 12.735 1.00 93.52 ? 1165 NAG A O4 1 HETATM 3888 O O5 . NAG D 3 . ? 20.465 -40.351 14.257 1.00 89.69 ? 1165 NAG A O5 1 HETATM 3889 O O6 . NAG D 3 . ? 17.884 -40.392 14.290 1.00 102.88 ? 1165 NAG A O6 1 HETATM 3890 O O7 . NAG D 3 . ? 26.314 -41.119 14.633 1.00 107.33 ? 1165 NAG A O7 1 HETATM 3891 C C1 . SIA E 4 . ? 36.272 -5.309 21.589 1.00 90.68 ? 1322 SIA A C1 1 HETATM 3892 C C2 . SIA E 4 . ? 36.530 -5.442 23.084 1.00 86.22 ? 1322 SIA A C2 1 HETATM 3893 C C3 . SIA E 4 . ? 35.205 -5.287 23.836 1.00 80.49 ? 1322 SIA A C3 1 HETATM 3894 C C4 . SIA E 4 . ? 34.358 -6.530 23.662 1.00 82.56 ? 1322 SIA A C4 1 HETATM 3895 C C5 . SIA E 4 . ? 35.164 -7.715 24.157 1.00 81.81 ? 1322 SIA A C5 1 HETATM 3896 C C6 . SIA E 4 . ? 36.439 -7.852 23.321 1.00 77.19 ? 1322 SIA A C6 1 HETATM 3897 C C7 . SIA E 4 . ? 37.403 -8.974 23.699 1.00 75.88 ? 1322 SIA A C7 1 HETATM 3898 C C8 . SIA E 4 . ? 38.762 -8.846 22.985 1.00 74.26 ? 1322 SIA A C8 1 HETATM 3899 C C9 . SIA E 4 . ? 39.574 -10.141 23.016 1.00 73.37 ? 1322 SIA A C9 1 HETATM 3900 C C10 . SIA E 4 . ? 34.347 -9.961 24.533 1.00 95.64 ? 1322 SIA A C10 1 HETATM 3901 C C11 . SIA E 4 . ? 33.342 -11.003 24.135 1.00 97.32 ? 1322 SIA A C11 1 HETATM 3902 N N5 . SIA E 4 . ? 34.262 -8.818 23.879 1.00 88.37 ? 1322 SIA A N5 1 HETATM 3903 O O1A . SIA E 4 . ? 35.621 -4.330 21.157 1.00 90.58 ? 1322 SIA A O1A 1 HETATM 3904 O O1B . SIA E 4 . ? 36.724 -6.179 20.817 1.00 98.89 ? 1322 SIA A O1B 1 HETATM 3905 O O4 . SIA E 4 . ? 33.113 -6.433 24.365 1.00 80.01 ? 1322 SIA A O4 1 HETATM 3906 O O6 . SIA E 4 . ? 37.195 -6.661 23.430 1.00 76.59 ? 1322 SIA A O6 1 HETATM 3907 O O7 . SIA E 4 . ? 37.558 -8.962 25.110 1.00 75.83 ? 1322 SIA A O7 1 HETATM 3908 O O8 . SIA E 4 . ? 38.566 -8.517 21.600 1.00 78.68 ? 1322 SIA A O8 1 HETATM 3909 O O9 . SIA E 4 . ? 40.862 -9.966 22.388 1.00 69.12 ? 1322 SIA A O9 1 HETATM 3910 O O10 . SIA E 4 . ? 35.198 -10.152 25.386 1.00 96.35 ? 1322 SIA A O10 1 HETATM 3911 C C1 . GAL F 5 . ? 38.399 -0.613 23.012 1.00 126.24 ? 1323 GAL A C1 1 HETATM 3912 C C2 . GAL F 5 . ? 39.537 -0.160 22.074 1.00 123.69 ? 1323 GAL A C2 1 HETATM 3913 C C3 . GAL F 5 . ? 39.937 -1.223 21.027 1.00 114.01 ? 1323 GAL A C3 1 HETATM 3914 C C4 . GAL F 5 . ? 39.996 -2.646 21.601 1.00 108.14 ? 1323 GAL A C4 1 HETATM 3915 C C5 . GAL F 5 . ? 38.716 -2.908 22.372 1.00 105.50 ? 1323 GAL A C5 1 HETATM 3916 C C6 . GAL F 5 . ? 38.680 -4.313 22.935 1.00 96.10 ? 1323 GAL A C6 1 HETATM 3917 O O1 . GAL F 5 . ? 38.283 0.250 24.157 1.00 119.14 ? 1323 GAL A O1 1 HETATM 3918 O O2 . GAL F 5 . ? 39.131 1.029 21.378 1.00 123.10 ? 1323 GAL A O2 1 HETATM 3919 O O3 . GAL F 5 . ? 41.195 -0.883 20.429 1.00 105.89 ? 1323 GAL A O3 1 HETATM 3920 O O4 . GAL F 5 . ? 41.110 -2.848 22.484 1.00 97.87 ? 1323 GAL A O4 1 HETATM 3921 O O5 . GAL F 5 . ? 38.620 -1.964 23.451 1.00 123.12 ? 1323 GAL A O5 1 HETATM 3922 O O6 . GAL F 5 . ? 37.398 -4.413 23.548 1.00 91.66 ? 1323 GAL A O6 1 HETATM 3923 C C1 . NAG G 3 . ? 25.074 -29.295 -75.029 1.00 90.33 ? 1154 NAG B C1 1 HETATM 3924 C C2 . NAG G 3 . ? 24.092 -30.479 -75.067 1.00 96.67 ? 1154 NAG B C2 1 HETATM 3925 C C3 . NAG G 3 . ? 23.615 -30.921 -76.459 1.00 103.86 ? 1154 NAG B C3 1 HETATM 3926 C C4 . NAG G 3 . ? 23.495 -29.734 -77.411 1.00 113.01 ? 1154 NAG B C4 1 HETATM 3927 C C5 . NAG G 3 . ? 24.846 -29.006 -77.396 1.00 111.87 ? 1154 NAG B C5 1 HETATM 3928 C C6 . NAG G 3 . ? 24.956 -27.889 -78.431 1.00 111.58 ? 1154 NAG B C6 1 HETATM 3929 C C7 . NAG G 3 . ? 24.748 -31.596 -73.009 1.00 92.38 ? 1154 NAG B C7 1 HETATM 3930 C C8 . NAG G 3 . ? 25.354 -32.799 -72.334 1.00 87.61 ? 1154 NAG B C8 1 HETATM 3931 N N2 . NAG G 3 . ? 24.666 -31.603 -74.342 1.00 93.86 ? 1154 NAG B N2 1 HETATM 3932 O O3 . NAG G 3 . ? 22.358 -31.548 -76.355 1.00 104.16 ? 1154 NAG B O3 1 HETATM 3933 O O4 . NAG G 3 . ? 23.048 -30.136 -78.707 1.00 111.23 ? 1154 NAG B O4 1 HETATM 3934 O O5 . NAG G 3 . ? 24.988 -28.408 -76.123 1.00 101.40 ? 1154 NAG B O5 1 HETATM 3935 O O6 . NAG G 3 . ? 24.262 -26.768 -77.932 1.00 109.18 ? 1154 NAG B O6 1 HETATM 3936 O O7 . NAG G 3 . ? 24.350 -30.646 -72.334 1.00 89.12 ? 1154 NAG B O7 1 HETATM 3937 N N1 . EPE H 6 . ? 41.172 -11.885 -71.750 1.00 84.40 ? 1163 EPE B N1 1 HETATM 3938 C C2 . EPE H 6 . ? 41.098 -11.317 -73.085 1.00 97.21 ? 1163 EPE B C2 1 HETATM 3939 C C3 . EPE H 6 . ? 42.473 -10.987 -73.656 1.00 99.19 ? 1163 EPE B C3 1 HETATM 3940 N N4 . EPE H 6 . ? 43.450 -10.585 -72.646 1.00 95.19 ? 1163 EPE B N4 1 HETATM 3941 C C5 . EPE H 6 . ? 43.511 -11.186 -71.324 1.00 86.22 ? 1163 EPE B C5 1 HETATM 3942 C C6 . EPE H 6 . ? 42.113 -11.383 -70.755 1.00 89.35 ? 1163 EPE B C6 1 HETATM 3943 C C7 . EPE H 6 . ? 44.453 -9.599 -73.041 1.00 94.45 ? 1163 EPE B C7 1 HETATM 3944 C C8 . EPE H 6 . ? 45.235 -10.163 -74.246 1.00 90.34 ? 1163 EPE B C8 1 HETATM 3945 O O8 . EPE H 6 . ? 46.286 -11.082 -73.862 1.00 88.58 ? 1163 EPE B O8 1 HETATM 3946 C C9 . EPE H 6 . ? 40.193 -12.894 -71.379 1.00 83.92 ? 1163 EPE B C9 1 HETATM 3947 C C10 . EPE H 6 . ? 38.817 -12.463 -71.910 1.00 92.65 ? 1163 EPE B C10 1 HETATM 3948 S S . EPE H 6 . ? 38.151 -11.147 -71.113 1.00 111.24 ? 1163 EPE B S 1 HETATM 3949 O O1S . EPE H 6 . ? 37.530 -10.151 -72.034 1.00 109.99 ? 1163 EPE B O1S 1 HETATM 3950 O O2S . EPE H 6 . ? 39.173 -10.462 -70.272 1.00 120.09 ? 1163 EPE B O2S 1 HETATM 3951 O O3S . EPE H 6 . ? 37.071 -11.650 -70.237 1.00 112.69 ? 1163 EPE B O3S 1 HETATM 3952 O O . HOH I 7 . ? 37.612 -17.964 -85.200 1.00 64.85 ? 2001 HOH A O 1 HETATM 3953 O O . HOH I 7 . ? 38.486 -14.214 -82.248 1.00 53.14 ? 2002 HOH A O 1 HETATM 3954 O O . HOH I 7 . ? 36.157 -13.996 -75.353 1.00 62.64 ? 2003 HOH A O 1 HETATM 3955 O O . HOH I 7 . ? 42.613 -13.055 -76.289 1.00 61.67 ? 2004 HOH A O 1 HETATM 3956 O O . HOH I 7 . ? 39.208 -10.345 -79.122 1.00 69.58 ? 2005 HOH A O 1 HETATM 3957 O O . HOH I 7 . ? 39.305 -7.411 -61.929 1.00 80.50 ? 2006 HOH A O 1 HETATM 3958 O O . HOH I 7 . ? 41.430 -16.025 -70.019 1.00 45.18 ? 2007 HOH A O 1 HETATM 3959 O O . HOH I 7 . ? 40.065 -14.586 -65.289 1.00 46.39 ? 2008 HOH A O 1 HETATM 3960 O O . HOH I 7 . ? 44.277 -12.880 -59.186 1.00 65.99 ? 2009 HOH A O 1 HETATM 3961 O O . HOH I 7 . ? 55.402 -11.011 -50.662 1.00 72.69 ? 2010 HOH A O 1 HETATM 3962 O O . HOH I 7 . ? 40.344 -12.633 -58.692 1.00 46.84 ? 2011 HOH A O 1 HETATM 3963 O O . HOH I 7 . ? 31.238 -11.804 -54.518 1.00 64.07 ? 2012 HOH A O 1 HETATM 3964 O O . HOH I 7 . ? 39.338 -7.505 -58.392 1.00 72.54 ? 2013 HOH A O 1 HETATM 3965 O O . HOH I 7 . ? 36.379 -3.894 -57.476 1.00 78.99 ? 2014 HOH A O 1 HETATM 3966 O O . HOH I 7 . ? 32.232 -6.880 -55.854 1.00 59.80 ? 2015 HOH A O 1 HETATM 3967 O O . HOH I 7 . ? 32.693 -2.240 -57.500 1.00 69.76 ? 2016 HOH A O 1 HETATM 3968 O O . HOH I 7 . ? 40.307 -5.263 -54.004 1.00 65.58 ? 2017 HOH A O 1 HETATM 3969 O O . HOH I 7 . ? 34.038 -10.689 -49.426 1.00 71.86 ? 2018 HOH A O 1 HETATM 3970 O O . HOH I 7 . ? 36.490 -6.208 -48.378 1.00 68.11 ? 2019 HOH A O 1 HETATM 3971 O O . HOH I 7 . ? 42.629 -5.736 -49.234 1.00 66.28 ? 2020 HOH A O 1 HETATM 3972 O O . HOH I 7 . ? 40.702 -7.955 -44.050 1.00 67.80 ? 2021 HOH A O 1 HETATM 3973 O O . HOH I 7 . ? 45.984 -10.609 -43.684 1.00 56.99 ? 2022 HOH A O 1 HETATM 3974 O O . HOH I 7 . ? 46.013 -7.782 -42.614 1.00 69.23 ? 2023 HOH A O 1 HETATM 3975 O O . HOH I 7 . ? 44.825 -15.010 -42.144 1.00 41.85 ? 2024 HOH A O 1 HETATM 3976 O O . HOH I 7 . ? 49.583 -9.601 -41.380 1.00 64.50 ? 2025 HOH A O 1 HETATM 3977 O O . HOH I 7 . ? 46.562 -12.763 -39.320 1.00 53.11 ? 2026 HOH A O 1 HETATM 3978 O O . HOH I 7 . ? 50.450 -14.209 -39.971 1.00 62.26 ? 2027 HOH A O 1 HETATM 3979 O O . HOH I 7 . ? 51.546 -18.573 -50.499 1.00 52.56 ? 2028 HOH A O 1 HETATM 3980 O O . HOH I 7 . ? 56.131 -14.181 -51.053 1.00 62.26 ? 2029 HOH A O 1 HETATM 3981 O O . HOH I 7 . ? 52.265 -16.488 -51.933 1.00 48.67 ? 2030 HOH A O 1 HETATM 3982 O O . HOH I 7 . ? 54.052 -11.258 -47.418 1.00 67.56 ? 2031 HOH A O 1 HETATM 3983 O O . HOH I 7 . ? 52.598 -7.844 -47.779 1.00 74.73 ? 2032 HOH A O 1 HETATM 3984 O O . HOH I 7 . ? 18.489 -16.640 9.301 1.00 75.07 ? 2033 HOH A O 1 HETATM 3985 O O . HOH I 7 . ? 45.678 -10.373 -53.849 1.00 70.65 ? 2034 HOH A O 1 HETATM 3986 O O . HOH I 7 . ? 31.812 -18.316 -50.549 1.00 65.90 ? 2035 HOH A O 1 HETATM 3987 O O . HOH I 7 . ? 33.994 -12.720 -47.333 1.00 59.82 ? 2036 HOH A O 1 HETATM 3988 O O . HOH I 7 . ? 32.272 -14.650 -43.755 1.00 78.14 ? 2037 HOH A O 1 HETATM 3989 O O . HOH I 7 . ? 32.471 -18.289 -45.468 1.00 67.32 ? 2038 HOH A O 1 HETATM 3990 O O . HOH I 7 . ? 31.071 -22.311 -40.600 1.00 69.56 ? 2039 HOH A O 1 HETATM 3991 O O . HOH I 7 . ? 33.787 -13.394 -42.036 1.00 62.96 ? 2040 HOH A O 1 HETATM 3992 O O . HOH I 7 . ? 40.063 -12.314 -36.774 1.00 49.41 ? 2041 HOH A O 1 HETATM 3993 O O . HOH I 7 . ? 39.946 -9.766 -37.798 1.00 60.26 ? 2042 HOH A O 1 HETATM 3994 O O . HOH I 7 . ? 47.722 -28.999 -1.222 1.00 52.53 ? 2043 HOH A O 1 HETATM 3995 O O . HOH I 7 . ? 34.151 -10.313 -33.569 1.00 72.83 ? 2044 HOH A O 1 HETATM 3996 O O . HOH I 7 . ? 39.483 -9.061 -28.145 1.00 74.54 ? 2045 HOH A O 1 HETATM 3997 O O . HOH I 7 . ? 30.593 -11.380 -27.933 1.00 58.98 ? 2046 HOH A O 1 HETATM 3998 O O . HOH I 7 . ? 28.208 -4.939 -15.637 1.00 69.72 ? 2047 HOH A O 1 HETATM 3999 O O . HOH I 7 . ? 17.653 -11.769 -13.124 1.00 71.49 ? 2048 HOH A O 1 HETATM 4000 O O . HOH I 7 . ? 22.758 -21.250 -16.395 1.00 84.74 ? 2049 HOH A O 1 HETATM 4001 O O . HOH I 7 . ? 24.448 -21.105 -20.969 1.00 73.62 ? 2050 HOH A O 1 HETATM 4002 O O . HOH I 7 . ? 33.535 -9.427 -3.447 1.00 65.98 ? 2051 HOH A O 1 HETATM 4003 O O . HOH I 7 . ? 25.769 -5.591 -8.148 1.00 80.95 ? 2052 HOH A O 1 HETATM 4004 O O . HOH I 7 . ? 35.431 -4.615 -1.514 1.00 72.21 ? 2053 HOH A O 1 HETATM 4005 O O . HOH I 7 . ? 26.084 -25.736 27.367 1.00 79.16 ? 2054 HOH A O 1 HETATM 4006 O O . HOH I 7 . ? 25.495 -13.858 5.612 1.00 66.37 ? 2055 HOH A O 1 HETATM 4007 O O . HOH I 7 . ? 25.349 -6.960 2.970 1.00 69.19 ? 2056 HOH A O 1 HETATM 4008 O O . HOH I 7 . ? 20.932 -5.821 7.778 1.00 76.72 ? 2057 HOH A O 1 HETATM 4009 O O . HOH I 7 . ? 26.386 -5.061 0.103 1.00 76.34 ? 2058 HOH A O 1 HETATM 4010 O O . HOH I 7 . ? 21.917 -9.890 -3.109 1.00 79.03 ? 2059 HOH A O 1 HETATM 4011 O O . HOH I 7 . ? 16.773 -16.029 -1.513 1.00 91.59 ? 2060 HOH A O 1 HETATM 4012 O O . HOH I 7 . ? 17.768 -18.321 8.606 1.00 72.34 ? 2061 HOH A O 1 HETATM 4013 O O . HOH I 7 . ? 22.431 -15.756 -5.055 1.00 80.27 ? 2062 HOH A O 1 HETATM 4014 O O . HOH I 7 . ? 38.231 -14.525 -0.330 1.00 57.63 ? 2063 HOH A O 1 HETATM 4015 O O . HOH I 7 . ? 39.738 -14.954 4.526 1.00 71.47 ? 2064 HOH A O 1 HETATM 4016 O O . HOH I 7 . ? 41.239 -7.795 20.894 1.00 66.21 ? 2065 HOH A O 1 HETATM 4017 O O . HOH I 7 . ? 45.159 -17.229 13.865 1.00 71.94 ? 2066 HOH A O 1 HETATM 4018 O O . HOH I 7 . ? 43.361 -18.681 5.649 1.00 78.50 ? 2067 HOH A O 1 HETATM 4019 O O . HOH I 7 . ? 44.926 -23.463 6.009 1.00 76.44 ? 2068 HOH A O 1 HETATM 4020 O O . HOH I 7 . ? 39.268 -26.465 8.655 1.00 75.27 ? 2069 HOH A O 1 HETATM 4021 O O . HOH I 7 . ? 44.758 -27.825 11.426 1.00 85.34 ? 2070 HOH A O 1 HETATM 4022 O O . HOH I 7 . ? 43.148 -24.705 1.558 1.00 53.93 ? 2071 HOH A O 1 HETATM 4023 O O . HOH I 7 . ? 40.672 -22.913 -4.627 1.00 70.04 ? 2072 HOH A O 1 HETATM 4024 O O . HOH I 7 . ? 45.277 -29.007 -2.878 1.00 50.20 ? 2073 HOH A O 1 HETATM 4025 O O . HOH I 7 . ? 43.651 -13.362 -14.927 1.00 79.28 ? 2074 HOH A O 1 HETATM 4026 O O . HOH I 7 . ? 50.931 -14.775 -57.360 1.00 66.95 ? 2075 HOH A O 1 HETATM 4027 O O . HOH I 7 . ? 28.216 -14.157 24.897 1.00 73.28 ? 2076 HOH A O 1 HETATM 4028 O O . HOH I 7 . ? 27.203 -13.198 21.580 1.00 74.82 ? 2077 HOH A O 1 HETATM 4029 O O . HOH I 7 . ? 29.097 -14.137 19.471 1.00 77.67 ? 2078 HOH A O 1 HETATM 4030 O O . HOH I 7 . ? 37.951 -1.712 17.019 1.00 70.35 ? 2079 HOH A O 1 HETATM 4031 O O . HOH I 7 . ? 28.272 0.524 11.839 1.00 67.04 ? 2080 HOH A O 1 HETATM 4032 O O . HOH I 7 . ? 27.806 -0.643 20.932 1.00 74.77 ? 2081 HOH A O 1 HETATM 4033 O O . HOH I 7 . ? 20.031 -9.522 11.316 1.00 70.22 ? 2082 HOH A O 1 HETATM 4034 O O . HOH I 7 . ? 19.609 -10.563 14.071 1.00 75.72 ? 2083 HOH A O 1 HETATM 4035 O O . HOH I 7 . ? 24.310 -15.200 40.148 1.00 73.81 ? 2084 HOH A O 1 HETATM 4036 O O . HOH I 7 . ? 26.824 -28.212 27.556 1.00 69.13 ? 2085 HOH A O 1 HETATM 4037 O O . HOH I 7 . ? 35.815 -34.354 30.222 1.00 74.26 ? 2086 HOH A O 1 HETATM 4038 O O . HOH I 7 . ? 24.272 -37.175 18.163 1.00 71.13 ? 2087 HOH A O 1 HETATM 4039 O O . HOH I 7 . ? 23.958 -35.247 4.251 1.00 65.78 ? 2088 HOH A O 1 HETATM 4040 O O . HOH I 7 . ? 17.252 -31.567 10.406 1.00 67.96 ? 2089 HOH A O 1 HETATM 4041 O O . HOH I 7 . ? 44.130 -21.204 26.876 1.00 82.45 ? 2090 HOH A O 1 HETATM 4042 O O . HOH I 7 . ? 33.113 -34.649 9.137 1.00 61.64 ? 2091 HOH A O 1 HETATM 4043 O O . HOH I 7 . ? 41.694 -35.566 12.067 1.00 70.61 ? 2092 HOH A O 1 HETATM 4044 O O . HOH I 7 . ? 43.678 -31.183 16.048 1.00 73.73 ? 2093 HOH A O 1 HETATM 4045 O O . HOH I 7 . ? 44.069 -1.693 14.173 1.00 79.81 ? 2094 HOH A O 1 HETATM 4046 O O . HOH I 7 . ? 39.626 -13.215 -13.294 1.00 64.55 ? 2095 HOH A O 1 HETATM 4047 O O . HOH I 7 . ? 18.103 -7.372 -14.978 1.00 69.77 ? 2096 HOH A O 1 HETATM 4048 O O . HOH I 7 . ? 18.216 -9.143 -17.597 1.00 82.14 ? 2097 HOH A O 1 HETATM 4049 O O . HOH I 7 . ? 25.747 -15.547 -25.378 1.00 66.27 ? 2098 HOH A O 1 HETATM 4050 O O . HOH I 7 . ? 27.373 -10.660 -25.078 1.00 81.11 ? 2099 HOH A O 1 HETATM 4051 O O . HOH I 7 . ? 24.658 -15.758 -31.629 1.00 75.10 ? 2100 HOH A O 1 HETATM 4052 O O . HOH I 7 . ? 23.049 -10.885 -32.310 1.00 90.76 ? 2101 HOH A O 1 HETATM 4053 O O . HOH I 7 . ? 28.453 -15.261 -34.367 1.00 75.86 ? 2102 HOH A O 1 HETATM 4054 O O . HOH I 7 . ? 36.630 -19.562 -23.327 1.00 67.79 ? 2103 HOH A O 1 HETATM 4055 O O . HOH I 7 . ? 42.589 -9.259 -26.090 1.00 67.94 ? 2104 HOH A O 1 HETATM 4056 O O . HOH I 7 . ? 40.471 -8.937 -24.258 1.00 79.70 ? 2105 HOH A O 1 HETATM 4057 O O . HOH I 7 . ? 41.403 -8.566 -31.013 1.00 64.55 ? 2106 HOH A O 1 HETATM 4058 O O . HOH I 7 . ? 43.364 -11.583 -20.522 1.00 73.52 ? 2107 HOH A O 1 HETATM 4059 O O . HOH I 7 . ? 42.254 -10.418 -15.640 1.00 68.73 ? 2108 HOH A O 1 HETATM 4060 O O . HOH I 7 . ? 37.095 -28.691 -24.986 1.00 75.76 ? 2109 HOH A O 1 HETATM 4061 O O . HOH I 7 . ? 45.221 -10.024 -22.745 1.00 70.43 ? 2110 HOH A O 1 HETATM 4062 O O . HOH I 7 . ? 45.150 -10.909 -27.336 1.00 81.57 ? 2111 HOH A O 1 HETATM 4063 O O . HOH I 7 . ? 47.799 -12.651 -33.518 1.00 68.57 ? 2112 HOH A O 1 HETATM 4064 O O . HOH I 7 . ? 45.692 -6.097 -32.912 1.00 75.97 ? 2113 HOH A O 1 HETATM 4065 O O . HOH I 7 . ? 45.195 -15.396 -39.466 1.00 51.99 ? 2114 HOH A O 1 HETATM 4066 O O . HOH I 7 . ? 41.583 -21.665 -45.860 1.00 40.55 ? 2115 HOH A O 1 HETATM 4067 O O . HOH I 7 . ? 44.055 -18.288 -55.469 1.00 35.75 ? 2116 HOH A O 1 HETATM 4068 O O . HOH I 7 . ? 46.704 -18.120 -56.024 1.00 49.54 ? 2117 HOH A O 1 HETATM 4069 O O . HOH I 7 . ? 48.297 -17.007 -57.720 1.00 47.62 ? 2118 HOH A O 1 HETATM 4070 O O . HOH I 7 . ? 45.712 -10.447 -58.502 1.00 75.22 ? 2119 HOH A O 1 HETATM 4071 O O . HOH I 7 . ? 40.852 -2.661 -59.415 1.00 76.23 ? 2120 HOH A O 1 HETATM 4072 O O . HOH I 7 . ? 24.035 -44.357 17.572 1.00 79.52 ? 2121 HOH A O 1 HETATM 4073 O O . HOH I 7 . ? 41.673 -1.713 25.225 1.00 83.36 ? 2122 HOH A O 1 HETATM 4074 O O . HOH J 7 . ? 49.295 -19.476 -60.289 1.00 45.50 ? 2001 HOH B O 1 HETATM 4075 O O . HOH J 7 . ? 52.728 -26.070 -62.012 1.00 56.02 ? 2002 HOH B O 1 HETATM 4076 O O . HOH J 7 . ? 42.542 -9.763 -67.341 1.00 74.52 ? 2003 HOH B O 1 HETATM 4077 O O . HOH J 7 . ? 50.653 -13.069 -64.704 1.00 57.71 ? 2004 HOH B O 1 HETATM 4078 O O . HOH J 7 . ? 49.392 -11.893 -63.594 1.00 72.29 ? 2005 HOH B O 1 HETATM 4079 O O . HOH J 7 . ? 49.583 -14.505 -70.074 1.00 71.77 ? 2006 HOH B O 1 HETATM 4080 O O . HOH J 7 . ? 45.178 -13.375 -69.382 1.00 59.00 ? 2007 HOH B O 1 HETATM 4081 O O . HOH J 7 . ? 43.218 -12.491 -67.687 1.00 59.94 ? 2008 HOH B O 1 HETATM 4082 O O . HOH J 7 . ? 41.433 -9.187 -64.913 1.00 58.52 ? 2009 HOH B O 1 HETATM 4083 O O . HOH J 7 . ? 41.408 -13.819 -68.312 1.00 53.68 ? 2010 HOH B O 1 HETATM 4084 O O . HOH J 7 . ? 35.179 -9.068 -66.122 1.00 58.00 ? 2011 HOH B O 1 HETATM 4085 O O . HOH J 7 . ? 28.062 -13.049 -64.659 1.00 64.18 ? 2012 HOH B O 1 HETATM 4086 O O . HOH J 7 . ? 32.297 -20.453 -49.184 1.00 58.48 ? 2013 HOH B O 1 HETATM 4087 O O . HOH J 7 . ? 24.241 -15.311 -59.747 1.00 76.52 ? 2014 HOH B O 1 HETATM 4088 O O . HOH J 7 . ? 26.825 -17.941 -66.006 1.00 72.46 ? 2015 HOH B O 1 HETATM 4089 O O . HOH J 7 . ? 28.516 -15.489 -65.361 1.00 56.33 ? 2016 HOH B O 1 HETATM 4090 O O . HOH J 7 . ? 24.879 -18.003 -58.363 1.00 76.99 ? 2017 HOH B O 1 HETATM 4091 O O . HOH J 7 . ? 28.123 -19.557 -56.378 1.00 77.15 ? 2018 HOH B O 1 HETATM 4092 O O . HOH J 7 . ? 30.960 -17.571 -55.948 1.00 54.92 ? 2019 HOH B O 1 HETATM 4093 O O . HOH J 7 . ? 30.664 -17.738 -72.123 1.00 63.40 ? 2020 HOH B O 1 HETATM 4094 O O . HOH J 7 . ? 27.782 -14.656 -78.573 1.00 56.97 ? 2021 HOH B O 1 HETATM 4095 O O . HOH J 7 . ? 27.286 -17.736 -72.291 1.00 57.63 ? 2022 HOH B O 1 HETATM 4096 O O . HOH J 7 . ? 25.538 -14.267 -75.174 0.50 59.17 ? 2023 HOH B O 1 HETATM 4097 O O . HOH J 7 . ? 31.587 -9.876 -79.610 1.00 69.32 ? 2024 HOH B O 1 HETATM 4098 O O . HOH J 7 . ? 50.657 -29.262 -46.161 0.33 74.00 ? 2025 HOH B O 1 HETATM 4099 O O . HOH J 7 . ? 37.392 -28.700 -64.128 1.00 62.79 ? 2026 HOH B O 1 HETATM 4100 O O . HOH J 7 . ? 28.719 -26.349 -65.489 1.00 72.37 ? 2027 HOH B O 1 HETATM 4101 O O . HOH J 7 . ? 28.783 -28.291 -64.907 1.00 77.85 ? 2028 HOH B O 1 HETATM 4102 O O . HOH J 7 . ? 25.297 -28.952 -50.856 1.00 78.54 ? 2029 HOH B O 1 HETATM 4103 O O . HOH J 7 . ? 35.013 -31.242 -53.567 1.00 63.76 ? 2030 HOH B O 1 HETATM 4104 O O . HOH J 7 . ? 32.565 -21.713 -47.262 1.00 57.47 ? 2031 HOH B O 1 HETATM 4105 O O . HOH J 7 . ? 27.598 -26.030 -49.463 1.00 78.54 ? 2032 HOH B O 1 HETATM 4106 O O . HOH J 7 . ? 29.802 -29.267 -48.503 1.00 78.26 ? 2033 HOH B O 1 HETATM 4107 O O . HOH J 7 . ? 31.266 -29.975 -43.677 1.00 77.42 ? 2034 HOH B O 1 HETATM 4108 O O . HOH J 7 . ? 42.901 -27.468 -49.726 1.00 48.47 ? 2035 HOH B O 1 HETATM 4109 O O . HOH J 7 . ? 31.965 -27.394 -38.015 1.00 71.85 ? 2036 HOH B O 1 HETATM 4110 O O . HOH J 7 . ? 28.309 -26.499 -43.220 1.00 72.48 ? 2037 HOH B O 1 HETATM 4111 O O . HOH J 7 . ? 28.054 -27.645 -39.438 1.00 75.27 ? 2038 HOH B O 1 HETATM 4112 O O . HOH J 7 . ? 34.082 -31.916 -40.694 1.00 72.98 ? 2039 HOH B O 1 HETATM 4113 O O . HOH J 7 . ? 37.219 -34.102 -42.461 1.00 56.89 ? 2040 HOH B O 1 HETATM 4114 O O . HOH J 7 . ? 35.694 -25.943 -31.894 1.00 76.23 ? 2041 HOH B O 1 HETATM 4115 O O . HOH J 7 . ? 37.916 -29.237 -22.243 1.00 66.75 ? 2042 HOH B O 1 HETATM 4116 O O . HOH J 7 . ? 42.309 -26.180 -16.044 1.00 70.00 ? 2043 HOH B O 1 HETATM 4117 O O . HOH J 7 . ? 43.604 -20.912 -12.536 1.00 70.81 ? 2044 HOH B O 1 HETATM 4118 O O . HOH J 7 . ? 43.746 -16.336 -3.476 1.00 83.91 ? 2045 HOH B O 1 HETATM 4119 O O . HOH J 7 . ? 46.019 -18.015 -5.914 1.00 72.14 ? 2046 HOH B O 1 HETATM 4120 O O . HOH J 7 . ? 46.703 -15.436 -1.528 1.00 86.81 ? 2047 HOH B O 1 HETATM 4121 O O . HOH J 7 . ? 49.977 -23.474 3.946 1.00 66.45 ? 2048 HOH B O 1 HETATM 4122 O O . HOH J 7 . ? 55.699 -14.132 2.478 1.00 68.85 ? 2049 HOH B O 1 HETATM 4123 O O . HOH J 7 . ? 53.877 -24.913 0.222 1.00 52.09 ? 2050 HOH B O 1 HETATM 4124 O O . HOH J 7 . ? 53.764 -18.040 -7.185 1.00 67.66 ? 2051 HOH B O 1 HETATM 4125 O O . HOH J 7 . ? 47.745 -19.857 -10.306 1.00 56.55 ? 2052 HOH B O 1 HETATM 4126 O O . HOH J 7 . ? 54.350 -21.872 -19.330 1.00 63.53 ? 2053 HOH B O 1 HETATM 4127 O O . HOH J 7 . ? 44.636 -21.889 -20.076 1.00 77.63 ? 2054 HOH B O 1 HETATM 4128 O O . HOH J 7 . ? 53.415 -24.132 -23.906 1.00 54.66 ? 2055 HOH B O 1 HETATM 4129 O O . HOH J 7 . ? 51.804 -19.739 -29.102 1.00 60.94 ? 2056 HOH B O 1 HETATM 4130 O O . HOH J 7 . ? 47.563 -26.845 -36.003 1.00 44.90 ? 2057 HOH B O 1 HETATM 4131 O O . HOH J 7 . ? 50.667 -29.253 -30.879 0.33 53.53 ? 2058 HOH B O 1 HETATM 4132 O O . HOH J 7 . ? 49.717 -27.823 -34.821 1.00 51.46 ? 2059 HOH B O 1 HETATM 4133 O O . HOH J 7 . ? 47.149 -17.520 -38.675 1.00 48.61 ? 2060 HOH B O 1 HETATM 4134 O O . HOH J 7 . ? 52.091 -18.981 -31.812 1.00 60.56 ? 2061 HOH B O 1 HETATM 4135 O O . HOH J 7 . ? 48.900 -20.298 -51.445 1.00 53.40 ? 2062 HOH B O 1 HETATM 4136 O O . HOH J 7 . ? 52.249 -24.297 -45.610 1.00 58.62 ? 2063 HOH B O 1 HETATM 4137 O O . HOH J 7 . ? 46.004 -27.199 -52.118 1.00 40.08 ? 2064 HOH B O 1 HETATM 4138 O O . HOH J 7 . ? 48.218 -31.142 -46.565 1.00 61.36 ? 2065 HOH B O 1 HETATM 4139 O O . HOH J 7 . ? 44.796 -29.441 -51.161 1.00 45.87 ? 2066 HOH B O 1 HETATM 4140 O O . HOH J 7 . ? 49.743 -31.908 -52.289 1.00 48.40 ? 2067 HOH B O 1 HETATM 4141 O O . HOH J 7 . ? 51.788 -22.334 -52.445 1.00 44.41 ? 2068 HOH B O 1 HETATM 4142 O O . HOH J 7 . ? 42.132 -29.051 -57.611 1.00 42.16 ? 2069 HOH B O 1 HETATM 4143 O O . HOH J 7 . ? 38.346 -27.531 -62.276 1.00 50.15 ? 2070 HOH B O 1 HETATM 4144 O O . HOH J 7 . ? 37.576 -29.455 -57.380 1.00 58.07 ? 2071 HOH B O 1 HETATM 4145 O O . HOH J 7 . ? 41.822 -31.463 -66.474 1.00 64.38 ? 2072 HOH B O 1 HETATM 4146 O O . HOH J 7 . ? 45.001 -30.475 -65.447 1.00 49.67 ? 2073 HOH B O 1 HETATM 4147 O O . HOH J 7 . ? 45.701 -19.926 -73.614 1.00 45.52 ? 2074 HOH B O 1 HETATM 4148 O O . HOH J 7 . ? 38.425 -32.593 -71.851 1.00 60.78 ? 2075 HOH B O 1 HETATM 4149 O O . HOH J 7 . ? 43.969 -27.518 -77.471 1.00 67.35 ? 2076 HOH B O 1 HETATM 4150 O O . HOH J 7 . ? 37.600 -33.913 -78.542 1.00 73.38 ? 2077 HOH B O 1 HETATM 4151 O O . HOH J 7 . ? 46.618 -26.388 -80.911 1.00 69.02 ? 2078 HOH B O 1 HETATM 4152 O O . HOH J 7 . ? 42.985 -26.583 -89.009 1.00 73.94 ? 2079 HOH B O 1 HETATM 4153 O O . HOH J 7 . ? 48.178 -23.516 -80.698 1.00 66.23 ? 2080 HOH B O 1 HETATM 4154 O O . HOH J 7 . ? 50.228 -20.941 -76.113 1.00 82.35 ? 2081 HOH B O 1 HETATM 4155 O O . HOH J 7 . ? 49.515 -27.656 -75.395 1.00 58.57 ? 2082 HOH B O 1 HETATM 4156 O O . HOH J 7 . ? 48.679 -25.315 -71.757 1.00 55.51 ? 2083 HOH B O 1 HETATM 4157 O O . HOH J 7 . ? 50.172 -13.996 -73.111 1.00 68.87 ? 2084 HOH B O 1 HETATM 4158 O O . HOH J 7 . ? 51.641 -16.767 -70.083 1.00 68.30 ? 2085 HOH B O 1 HETATM 4159 O O . HOH J 7 . ? 30.975 -36.190 -76.633 1.00 79.14 ? 2086 HOH B O 1 HETATM 4160 O O . HOH J 7 . ? 38.651 -31.643 -89.217 1.00 86.16 ? 2087 HOH B O 1 HETATM 4161 O O . HOH J 7 . ? 46.254 -11.204 -20.323 1.00 83.07 ? 2088 HOH B O 1 HETATM 4162 O O . HOH J 7 . ? 19.410 -10.594 -34.163 1.00 83.97 ? 2089 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASP A 1 ? 0.7176 0.8018 0.7511 0.2375 -0.1301 -0.0026 1 ASP A N 2 C CA . ASP A 1 ? 0.7086 0.8300 0.7588 0.2311 -0.1289 -0.0091 1 ASP A CA 3 C C . ASP A 1 ? 0.6946 0.7910 0.7537 0.2065 -0.1258 -0.0107 1 ASP A C 4 O O . ASP A 1 ? 0.6554 0.7318 0.7177 0.1889 -0.1258 -0.0096 1 ASP A O 5 C CB . ASP A 1 ? 0.6883 0.8711 0.7568 0.2224 -0.1321 -0.0152 1 ASP A CB 6 C CG . ASP A 1 ? 0.7077 0.9268 0.7695 0.2483 -0.1354 -0.0143 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.7275 0.9151 0.7675 0.2728 -0.1355 -0.0079 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.7532 1.0326 0.8287 0.2437 -0.1378 -0.0199 1 ASP A OD2 9 N N . GLN A 2 ? 0.6980 0.7974 0.7595 0.2075 -0.1230 -0.0131 2 GLN A N 10 C CA . GLN A 2 ? 0.6626 0.7392 0.7303 0.1873 -0.1199 -0.0144 2 GLN A CA 11 C C . GLN A 2 ? 0.6378 0.7413 0.7157 0.1834 -0.1177 -0.0196 2 GLN A C 12 O O . GLN A 2 ? 0.6186 0.7521 0.6953 0.2012 -0.1179 -0.0215 2 GLN A O 13 C CB . GLN A 2 ? 0.7006 0.7231 0.7510 0.1907 -0.1175 -0.0088 2 GLN A CB 14 C CG . GLN A 2 ? 0.7627 0.7661 0.7938 0.2120 -0.1154 -0.0067 2 GLN A CG 15 C CD . GLN A 2 ? 0.8145 0.7634 0.8272 0.2062 -0.1124 -0.0025 2 GLN A CD 16 O OE1 . GLN A 2 ? 0.8921 0.8229 0.8940 0.2113 -0.1094 -0.0029 2 GLN A OE1 17 N NE2 . GLN A 2 ? 0.7997 0.7249 0.8076 0.1948 -0.1129 0.0013 2 GLN A NE2 18 N N . ILE A 3 ? 0.6020 0.6960 0.6885 0.1610 -0.1155 -0.0220 3 ILE A N 19 C CA . ILE A 3 ? 0.5861 0.6957 0.6799 0.1544 -0.1127 -0.0262 3 ILE A CA 20 C C . ILE A 3 ? 0.5854 0.6520 0.6746 0.1460 -0.1096 -0.0238 3 ILE A C 21 O O . ILE A 3 ? 0.5959 0.6358 0.6832 0.1344 -0.1096 -0.0213 3 ILE A O 22 C CB . ILE A 3 ? 0.5901 0.7386 0.6962 0.1333 -0.1127 -0.0327 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.5977 0.7669 0.7098 0.1273 -0.1096 -0.0370 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.5701 0.6938 0.6749 0.1107 -0.1122 -0.0328 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.6012 0.8237 0.7218 0.1117 -0.1098 -0.0439 3 ILE A CD1 26 N N . CYS A 4 ? 0.5907 0.6535 0.6773 0.1531 -0.1070 -0.0245 4 CYS A N 27 C CA . CYS A 4 ? 0.5962 0.6211 0.6772 0.1463 -0.1041 -0.0224 4 CYS A CA 28 C C . CYS A 4 ? 0.5661 0.6054 0.6559 0.1354 -0.1012 -0.0267 4 CYS A C 29 O O . CYS A 4 ? 0.5463 0.6217 0.6425 0.1399 -0.1010 -0.0307 4 CYS A O 30 C CB . CYS A 4 ? 0.6427 0.6386 0.7054 0.1647 -0.1030 -0.0189 4 CYS A CB 31 S SG . CYS A 4 ? 0.7025 0.6772 0.7475 0.1795 -0.1056 -0.0135 4 CYS A SG 32 N N . ILE A 5 ? 0.5437 0.5579 0.6332 0.1217 -0.0991 -0.0257 5 ILE A N 33 C CA . ILE A 5 ? 0.5350 0.5557 0.6294 0.1127 -0.0960 -0.0290 5 ILE A CA 34 C C . ILE A 5 ? 0.5599 0.5554 0.6456 0.1211 -0.0938 -0.0271 5 ILE A C 35 O O . ILE A 5 ? 0.5563 0.5201 0.6320 0.1220 -0.0939 -0.0230 5 ILE A O 36 C CB . ILE A 5 ? 0.5387 0.5475 0.6345 0.0931 -0.0946 -0.0293 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.5570 0.5824 0.6550 0.0833 -0.0963 -0.0314 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.5264 0.5387 0.6242 0.0838 -0.0911 -0.0322 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.5919 0.6594 0.6968 0.0820 -0.0967 -0.0365 5 ILE A CD1 40 N N . GLY A 6 ? 0.5566 0.5673 0.6442 0.1258 -0.0916 -0.0303 6 GLY A N 41 C CA . GLY A 6 ? 0.5742 0.5602 0.6503 0.1346 -0.0894 -0.0292 6 GLY A CA 42 C C . GLY A 6 ? 0.5635 0.5660 0.6448 0.1329 -0.0864 -0.0332 6 GLY A C 43 O O . GLY A 6 ? 0.5886 0.6221 0.6823 0.1226 -0.0858 -0.0367 6 GLY A O 44 N N . TYR A 7 ? 0.5724 0.5524 0.6412 0.1418 -0.0842 -0.0328 7 TYR A N 45 C CA . TYR A 7 ? 0.5717 0.5625 0.6440 0.1398 -0.0811 -0.0362 7 TYR A CA 46 C C . TYR A 7 ? 0.5934 0.5772 0.6498 0.1619 -0.0794 -0.0372 7 TYR A C 47 O O . TYR A 7 ? 0.6038 0.5611 0.6408 0.1770 -0.0801 -0.0346 7 TYR A O 48 C CB . TYR A 7 ? 0.5731 0.5395 0.6456 0.1227 -0.0793 -0.0350 7 TYR A CB 49 C CG . TYR A 7 ? 0.5886 0.5143 0.6453 0.1221 -0.0795 -0.0311 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.5856 0.4986 0.6414 0.1153 -0.0818 -0.0275 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.6223 0.5233 0.6632 0.1263 -0.0770 -0.0316 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.6295 0.5103 0.6696 0.1118 -0.0816 -0.0243 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.6332 0.4982 0.6564 0.1212 -0.0767 -0.0287 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.6369 0.4939 0.6602 0.1132 -0.0790 -0.0251 7 TYR A CZ 55 O OH . TYR A 7 ? 0.6718 0.4978 0.6762 0.1053 -0.0784 -0.0226 7 TYR A OH 56 N N . HIS A 8 ? 0.5980 0.6036 0.6596 0.1638 -0.0768 -0.0410 8 HIS A N 57 C CA . HIS A 8 ? 0.6370 0.6425 0.6833 0.1869 -0.0746 -0.0429 8 HIS A CA 58 C C . HIS A 8 ? 0.6642 0.6146 0.6847 0.1912 -0.0725 -0.0410 8 HIS A C 59 O O . HIS A 8 ? 0.6601 0.5858 0.6814 0.1722 -0.0717 -0.0398 8 HIS A O 60 C CB . HIS A 8 ? 0.6378 0.6830 0.6987 0.1822 -0.0721 -0.0476 8 HIS A CB 61 C CG . HIS A 8 ? 0.6692 0.7231 0.7164 0.2069 -0.0695 -0.0503 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.6973 0.7808 0.7379 0.2340 -0.0703 -0.0513 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.6735 0.7141 0.7119 0.2101 -0.0660 -0.0523 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.6991 0.7847 0.7252 0.2548 -0.0672 -0.0537 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.6810 0.7397 0.7057 0.2398 -0.0645 -0.0545 8 HIS A NE2 66 N N . ALA A 9 ? 0.7057 0.6366 0.6997 0.2169 -0.0713 -0.0408 9 ALA A N 67 C CA . ALA A 9 ? 0.7339 0.6118 0.6965 0.2220 -0.0682 -0.0404 9 ALA A CA 68 C C . ALA A 9 ? 0.7686 0.6527 0.7120 0.2523 -0.0655 -0.0433 9 ALA A C 69 O O . ALA A 9 ? 0.8029 0.7314 0.7554 0.2713 -0.0667 -0.0447 9 ALA A O 70 C CB . ALA A 9 ? 0.7525 0.5783 0.6878 0.2211 -0.0690 -0.0361 9 ALA A CB 71 N N . ASN A 10 ? 0.7836 0.6271 0.6997 0.2570 -0.0618 -0.0446 10 ASN A N 72 C CA . ASN A 10 ? 0.8236 0.6684 0.7166 0.2885 -0.0588 -0.0474 10 ASN A CA 73 C C . ASN A 10 ? 0.8832 0.6576 0.7310 0.2929 -0.0547 -0.0477 10 ASN A C 74 O O . ASN A 10 ? 0.8970 0.6253 0.7311 0.2712 -0.0546 -0.0454 10 ASN A O 75 C CB . ASN A 10 ? 0.7936 0.7009 0.7176 0.2880 -0.0579 -0.0519 10 ASN A CB 76 C CG . ASN A 10 ? 0.7846 0.6823 0.7194 0.2625 -0.0558 -0.0539 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.7979 0.6428 0.7130 0.2496 -0.0546 -0.0526 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.7644 0.7151 0.7291 0.2540 -0.0553 -0.0571 10 ASN A ND2 79 N N . ASN A 11 ? 0.9470 0.7145 0.7693 0.3206 -0.0511 -0.0506 11 ASN A N 80 C CA . ASN A 11 ? 1.0372 0.7309 0.8071 0.3281 -0.0466 -0.0513 11 ASN A CA 81 C C . ASN A 11 ? 1.0185 0.7044 0.7947 0.3060 -0.0441 -0.0549 11 ASN A C 82 O O . ASN A 11 ? 1.0779 0.7085 0.8111 0.3122 -0.0398 -0.0568 11 ASN A O 83 C CB . ASN A 11 ? 1.1066 0.7850 0.8342 0.3750 -0.0436 -0.0522 11 ASN A CB 84 C CG . ASN A 11 ? 1.1471 0.8877 0.8952 0.3958 -0.0423 -0.0568 11 ASN A CG 85 O OD1 . ASN A 11 ? 1.1459 0.9312 0.9348 0.3727 -0.0429 -0.0595 11 ASN A OD1 86 N ND2 . ASN A 11 ? 1.2173 0.9623 0.9348 0.4409 -0.0402 -0.0575 11 ASN A ND2 87 N N . SER A 12 ? 0.9297 0.6664 0.7552 0.2799 -0.0464 -0.0557 12 SER A N 88 C CA . SER A 12 ? 0.8983 0.6373 0.7344 0.2605 -0.0443 -0.0588 12 SER A CA 89 C C . SER A 12 ? 0.9357 0.6145 0.7460 0.2357 -0.0430 -0.0580 12 SER A C 90 O O . SER A 12 ? 0.9040 0.5622 0.7119 0.2189 -0.0452 -0.0544 12 SER A O 91 C CB . SER A 12 ? 0.8441 0.6457 0.7337 0.2382 -0.0469 -0.0590 12 SER A CB 92 O OG . SER A 12 ? 0.8067 0.6137 0.7063 0.2220 -0.0448 -0.0618 12 SER A OG 93 N N . THR A 13 ? 0.9778 0.6320 0.7682 0.2333 -0.0392 -0.0616 13 THR A N 94 C CA . THR A 13 ? 1.0040 0.6123 0.7733 0.2057 -0.0378 -0.0621 13 THR A CA 95 C C . THR A 13 ? 0.9768 0.6175 0.7766 0.1855 -0.0376 -0.0645 13 THR A C 96 O O . THR A 13 ? 1.0043 0.6139 0.7860 0.1656 -0.0358 -0.0661 13 THR A O 97 C CB . THR A 13 ? 1.0843 0.6215 0.7909 0.2187 -0.0327 -0.0648 13 THR A CB 98 O OG1 . THR A 13 ? 1.1065 0.6576 0.8085 0.2429 -0.0296 -0.0690 13 THR A OG1 99 C CG2 . THR A 13 ? 1.1324 0.6233 0.7970 0.2392 -0.0320 -0.0620 13 THR A CG2 100 N N . GLU A 14 ? 0.9307 0.6323 0.7728 0.1895 -0.0390 -0.0650 14 GLU A N 101 C CA . GLU A 14 ? 0.9311 0.6632 0.8024 0.1690 -0.0390 -0.0663 14 GLU A CA 102 C C . GLU A 14 ? 0.8926 0.6224 0.7782 0.1392 -0.0419 -0.0630 14 GLU A C 103 O O . GLU A 14 ? 0.8819 0.6161 0.7768 0.1352 -0.0450 -0.0593 14 GLU A O 104 C CB . GLU A 14 ? 0.9487 0.7437 0.8595 0.1751 -0.0400 -0.0668 14 GLU A CB 105 C CG . GLU A 14 ? 1.0153 0.8307 0.9190 0.2041 -0.0373 -0.0704 14 GLU A CG 106 C CD . GLU A 14 ? 1.1297 0.9301 1.0157 0.2079 -0.0331 -0.0746 14 GLU A CD 107 O OE1 . GLU A 14 ? 1.1340 0.9482 1.0386 0.1867 -0.0327 -0.0753 14 GLU A OE1 108 O OE2 . GLU A 14 ? 1.2438 1.0160 1.0943 0.2334 -0.0300 -0.0773 14 GLU A OE2 109 N N . GLN A 15 ? 0.8714 0.5978 0.7585 0.1198 -0.0409 -0.0642 15 GLN A N 110 C CA . GLN A 15 ? 0.8219 0.5506 0.7195 0.0938 -0.0433 -0.0613 15 GLN A CA 111 C C . GLN A 15 ? 0.7667 0.5332 0.6945 0.0821 -0.0438 -0.0612 15 GLN A C 112 O O . GLN A 15 ? 0.7449 0.5204 0.6743 0.0873 -0.0412 -0.0643 15 GLN A O 113 C CB . GLN A 15 ? 0.8691 0.5522 0.7296 0.0790 -0.0415 -0.0630 15 GLN A CB 114 C CG . GLN A 15 ? 0.9347 0.5668 0.7537 0.0874 -0.0401 -0.0632 15 GLN A CG 115 C CD . GLN A 15 ? 0.9967 0.5829 0.7761 0.0651 -0.0380 -0.0650 15 GLN A CD 116 O OE1 . GLN A 15 ? 1.0524 0.6039 0.8043 0.0577 -0.0379 -0.0634 15 GLN A OE1 117 N NE2 . GLN A 15 ? 1.0190 0.6052 0.7935 0.0526 -0.0360 -0.0686 15 GLN A NE2 118 N N . VAL A 16 ? 0.7300 0.5165 0.6782 0.0673 -0.0467 -0.0574 16 VAL A N 119 C CA . VAL A 16 ? 0.6866 0.5022 0.6566 0.0573 -0.0468 -0.0565 16 VAL A CA 120 C C . VAL A 16 ? 0.6955 0.5107 0.6633 0.0390 -0.0487 -0.0540 16 VAL A C 121 O O . VAL A 16 ? 0.7131 0.5144 0.6707 0.0333 -0.0504 -0.0522 16 VAL A O 122 C CB . VAL A 16 ? 0.6495 0.4977 0.6473 0.0618 -0.0482 -0.0540 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.6543 0.5133 0.6556 0.0781 -0.0465 -0.0567 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.6416 0.4926 0.6469 0.0586 -0.0516 -0.0498 16 VAL A CG2 125 N N . ASP A 17 ? 0.6860 0.5191 0.6624 0.0305 -0.0482 -0.0537 17 ASP A N 126 C CA . ASP A 17 ? 0.6673 0.5122 0.6445 0.0157 -0.0502 -0.0511 17 ASP A CA 127 C C . ASP A 17 ? 0.6279 0.5004 0.6270 0.0184 -0.0521 -0.0464 17 ASP A C 128 O O . ASP A 17 ? 0.5942 0.4767 0.6056 0.0263 -0.0509 -0.0461 17 ASP A O 129 C CB . ASP A 17 ? 0.6915 0.5390 0.6594 0.0059 -0.0485 -0.0537 17 ASP A CB 130 C CG . ASP A 17 ? 0.7498 0.5643 0.6883 -0.0009 -0.0463 -0.0586 17 ASP A CG 131 O OD1 . ASP A 17 ? 0.7777 0.5662 0.6985 -0.0028 -0.0466 -0.0589 17 ASP A OD1 132 O OD2 . ASP A 17 ? 0.7782 0.5897 0.7078 -0.0046 -0.0440 -0.0621 17 ASP A OD2 133 N N . THR A 18 ? 0.6342 0.5176 0.6345 0.0114 -0.0546 -0.0430 18 THR A N 134 C CA . THR A 18 ? 0.6104 0.5173 0.6241 0.0149 -0.0562 -0.0383 18 THR A CA 135 C C . THR A 18 ? 0.6100 0.5373 0.6185 0.0056 -0.0573 -0.0369 18 THR A C 136 O O . THR A 18 ? 0.6316 0.5549 0.6272 -0.0066 -0.0569 -0.0398 18 THR A O 137 C CB . THR A 18 ? 0.5969 0.5039 0.6169 0.0191 -0.0586 -0.0351 18 THR A CB 138 O OG1 . THR A 18 ? 0.6528 0.5555 0.6627 0.0096 -0.0603 -0.0350 18 THR A OG1 139 C CG2 . THR A 18 ? 0.5841 0.4774 0.6087 0.0274 -0.0580 -0.0367 18 THR A CG2 140 N N . ILE A 19 ? 0.6118 0.5608 0.6268 0.0117 -0.0583 -0.0326 19 ILE A N 141 C CA . ILE A 19 ? 0.6018 0.5799 0.6126 0.0065 -0.0596 -0.0307 19 ILE A CA 142 C C . ILE A 19 ? 0.6057 0.5944 0.6105 -0.0065 -0.0618 -0.0309 19 ILE A C 143 O O . ILE A 19 ? 0.5951 0.6017 0.5912 -0.0204 -0.0620 -0.0327 19 ILE A O 144 C CB . ILE A 19 ? 0.6280 0.6238 0.6426 0.0212 -0.0603 -0.0253 19 ILE A CB 145 C CG1 . ILE A 19 ? 0.6677 0.6521 0.6817 0.0311 -0.0575 -0.0247 19 ILE A CG1 146 C CG2 . ILE A 19 ? 0.6391 0.6725 0.6494 0.0204 -0.0620 -0.0228 19 ILE A CG2 147 C CD1 . ILE A 19 ? 0.6636 0.6609 0.6722 0.0286 -0.0561 -0.0260 19 ILE A CD1 148 N N . MET A 20 ? 0.6228 0.6019 0.6311 -0.0036 -0.0631 -0.0291 20 MET A N 149 C CA . MET A 20 ? 0.6469 0.6369 0.6496 -0.0152 -0.0651 -0.0283 20 MET A CA 150 C C . MET A 20 ? 0.6685 0.6270 0.6564 -0.0297 -0.0641 -0.0322 20 MET A C 151 O O . MET A 20 ? 0.6673 0.6313 0.6448 -0.0445 -0.0650 -0.0321 20 MET A O 152 C CB . MET A 20 ? 0.6256 0.6210 0.6376 -0.0034 -0.0670 -0.0239 20 MET A CB 153 C CG . MET A 20 ? 0.6269 0.6582 0.6435 0.0075 -0.0684 -0.0194 20 MET A CG 154 S SD . MET A 20 ? 0.6703 0.7027 0.6925 0.0192 -0.0704 -0.0150 20 MET A SD 155 C CE . MET A 20 ? 0.6926 0.7736 0.7123 0.0297 -0.0716 -0.0107 20 MET A CE 156 N N . GLU A 21 ? 0.6653 0.5907 0.6496 -0.0246 -0.0621 -0.0353 21 GLU A N 157 C CA . GLU A 21 ? 0.7108 0.5985 0.6762 -0.0315 -0.0607 -0.0385 21 GLU A CA 158 C C . GLU A 21 ? 0.7278 0.5890 0.6850 -0.0258 -0.0578 -0.0429 21 GLU A C 159 O O . GLU A 21 ? 0.7228 0.5883 0.6954 -0.0109 -0.0572 -0.0427 21 GLU A O 160 C CB . GLU A 21 ? 0.7110 0.5846 0.6811 -0.0216 -0.0621 -0.0360 21 GLU A CB 161 C CG . GLU A 21 ? 0.7794 0.6146 0.7233 -0.0298 -0.0609 -0.0381 21 GLU A CG 162 C CD . GLU A 21 ? 0.8259 0.6492 0.7724 -0.0206 -0.0625 -0.0353 21 GLU A CD 163 O OE1 . GLU A 21 ? 0.7450 0.5920 0.7150 -0.0097 -0.0648 -0.0319 21 GLU A OE1 164 O OE2 . GLU A 21 ? 0.8624 0.6489 0.7832 -0.0246 -0.0612 -0.0365 21 GLU A OE2 165 N N . LYS A 22 ? 0.7668 0.6000 0.6969 -0.0387 -0.0556 -0.0470 22 LYS A N 166 C CA . LYS A 22 ? 0.8085 0.6132 0.7249 -0.0326 -0.0525 -0.0516 22 LYS A CA 167 C C . LYS A 22 ? 0.8113 0.5719 0.7059 -0.0240 -0.0509 -0.0531 22 LYS A C 168 O O . LYS A 22 ? 0.8225 0.5676 0.7036 -0.0306 -0.0518 -0.0514 22 LYS A O 169 C CB . LYS A 22 ? 0.8873 0.6899 0.7839 -0.0517 -0.0507 -0.0555 22 LYS A CB 170 C CG . LYS A 22 ? 0.9168 0.7666 0.8357 -0.0544 -0.0522 -0.0537 22 LYS A CG 171 C CD . LYS A 22 ? 1.0134 0.8734 0.9147 -0.0769 -0.0514 -0.0571 22 LYS A CD 172 C CE . LYS A 22 ? 1.0802 0.9167 0.9667 -0.0764 -0.0481 -0.0624 22 LYS A CE 173 N NZ . LYS A 22 ? 1.0644 0.9239 0.9425 -0.0950 -0.0478 -0.0652 22 LYS A NZ 174 N N . ASN A 23 ? 0.7908 0.5338 0.6815 -0.0074 -0.0486 -0.0559 23 ASN A N 175 C CA . ASN A 23 ? 0.8418 0.5430 0.7073 0.0060 -0.0467 -0.0575 23 ASN A CA 176 C C . ASN A 23 ? 0.8148 0.5181 0.6905 0.0177 -0.0491 -0.0536 23 ASN A C 177 O O . ASN A 23 ? 0.8414 0.5089 0.6894 0.0184 -0.0483 -0.0533 23 ASN A O 178 C CB . ASN A 23 ? 0.9245 0.5774 0.7429 -0.0102 -0.0438 -0.0608 23 ASN A CB 179 C CG . ASN A 23 ? 1.0063 0.6492 0.8086 -0.0182 -0.0408 -0.0658 23 ASN A CG 180 O OD1 . ASN A 23 ? 1.0047 0.6749 0.8309 -0.0082 -0.0408 -0.0667 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.1655 0.7674 0.9245 -0.0376 -0.0381 -0.0693 23 ASN A ND2 182 N N . VAL A 24 ? 0.7687 0.5109 0.6808 0.0266 -0.0516 -0.0507 24 VAL A N 183 C CA . VAL A 24 ? 0.7309 0.4806 0.6560 0.0380 -0.0540 -0.0473 24 VAL A CA 184 C C . VAL A 24 ? 0.7332 0.4740 0.6546 0.0615 -0.0526 -0.0493 24 VAL A C 185 O O . VAL A 24 ? 0.7034 0.4642 0.6393 0.0706 -0.0514 -0.0514 24 VAL A O 186 C CB . VAL A 24 ? 0.6865 0.4784 0.6469 0.0369 -0.0567 -0.0440 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.6843 0.4842 0.6572 0.0472 -0.0591 -0.0411 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.6730 0.4801 0.6364 0.0185 -0.0581 -0.0419 24 VAL A CG2 189 N N . THR A 25 ? 0.7517 0.4642 0.6515 0.0720 -0.0525 -0.0487 25 THR A N 190 C CA . THR A 25 ? 0.7605 0.4699 0.6550 0.0980 -0.0512 -0.0503 25 THR A CA 191 C C . THR A 25 ? 0.7224 0.4770 0.6531 0.1069 -0.0540 -0.0485 25 THR A C 192 O O . THR A 25 ? 0.7221 0.4888 0.6672 0.0996 -0.0570 -0.0450 25 THR A O 193 C CB . THR A 25 ? 0.8079 0.4723 0.6648 0.1096 -0.0503 -0.0496 25 THR A CB 194 O OG1 . THR A 25 ? 0.8697 0.4859 0.6870 0.0955 -0.0474 -0.0513 25 THR A OG1 195 C CG2 . THR A 25 ? 0.8450 0.5067 0.6906 0.1403 -0.0484 -0.0518 25 THR A CG2 196 N N . VAL A 26 ? 0.6973 0.4775 0.6407 0.1212 -0.0527 -0.0512 26 VAL A N 197 C CA . VAL A 26 ? 0.6514 0.4762 0.6262 0.1251 -0.0547 -0.0504 26 VAL A CA 198 C C . VAL A 26 ? 0.6890 0.5288 0.6599 0.1500 -0.0537 -0.0527 26 VAL A C 199 O O . VAL A 26 ? 0.7559 0.5752 0.7024 0.1657 -0.0509 -0.0553 26 VAL A O 200 C CB . VAL A 26 ? 0.6097 0.4645 0.6087 0.1115 -0.0540 -0.0513 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.5933 0.4402 0.5968 0.0911 -0.0554 -0.0483 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.6290 0.4833 0.6204 0.1165 -0.0504 -0.0553 26 VAL A CG2 203 N N . THR A 27 ? 0.6692 0.5456 0.6617 0.1539 -0.0560 -0.0519 27 THR A N 204 C CA . THR A 27 ? 0.6606 0.5620 0.6519 0.1776 -0.0558 -0.0537 27 THR A CA 205 C C . THR A 27 ? 0.6614 0.5981 0.6627 0.1836 -0.0529 -0.0580 27 THR A C 206 O O . THR A 27 ? 0.7178 0.6678 0.7080 0.2079 -0.0514 -0.0605 27 THR A O 207 C CB . THR A 27 ? 0.6506 0.5856 0.6628 0.1760 -0.0592 -0.0520 27 THR A CB 208 O OG1 . THR A 27 ? 0.6106 0.5782 0.6502 0.1548 -0.0597 -0.0525 27 THR A OG1 209 C CG2 . THR A 27 ? 0.6665 0.5686 0.6688 0.1712 -0.0620 -0.0476 27 THR A CG2 210 N N . HIS A 28 ? 0.6434 0.5963 0.6637 0.1627 -0.0521 -0.0587 28 HIS A N 211 C CA . HIS A 28 ? 0.6428 0.6288 0.6728 0.1633 -0.0490 -0.0626 28 HIS A CA 212 C C . HIS A 28 ? 0.6440 0.6170 0.6785 0.1425 -0.0473 -0.0625 28 HIS A C 213 O O . HIS A 28 ? 0.6399 0.6001 0.6816 0.1239 -0.0491 -0.0593 28 HIS A O 214 C CB . HIS A 28 ? 0.6346 0.6758 0.6885 0.1580 -0.0497 -0.0639 28 HIS A CB 215 C CG . HIS A 28 ? 0.6476 0.7113 0.7008 0.1767 -0.0519 -0.0639 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.6482 0.6992 0.7026 0.1738 -0.0555 -0.0605 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.6517 0.7516 0.7017 0.2007 -0.0509 -0.0669 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.6467 0.7239 0.6989 0.1943 -0.0568 -0.0613 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.6437 0.7524 0.6930 0.2118 -0.0542 -0.0651 28 HIS A NE2 220 N N . ALA A 29 ? 0.6557 0.6353 0.6855 0.1475 -0.0439 -0.0658 29 ALA A N 221 C CA . ALA A 29 ? 0.6618 0.6299 0.6932 0.1308 -0.0420 -0.0660 29 ALA A CA 222 C C . ALA A 29 ? 0.6760 0.6749 0.7122 0.1352 -0.0382 -0.0701 29 ALA A C 223 O O . ALA A 29 ? 0.7363 0.7621 0.7710 0.1539 -0.0370 -0.0730 29 ALA A O 224 C CB . ALA A 29 ? 0.6825 0.6020 0.6905 0.1309 -0.0417 -0.0655 29 ALA A CB 225 N N . GLN A 30 ? 0.6695 0.6671 0.7106 0.1190 -0.0363 -0.0702 30 GLN A N 226 C CA . GLN A 30 ? 0.6893 0.7161 0.7353 0.1197 -0.0325 -0.0738 30 GLN A CA 227 C C . GLN A 30 ? 0.6812 0.6818 0.7170 0.1128 -0.0304 -0.0743 30 GLN A C 228 O O . GLN A 30 ? 0.6168 0.6066 0.6574 0.0945 -0.0309 -0.0716 30 GLN A O 229 C CB . GLN A 30 ? 0.6974 0.7627 0.7627 0.1018 -0.0316 -0.0734 30 GLN A CB 230 C CG . GLN A 30 ? 0.7331 0.8318 0.8024 0.0993 -0.0272 -0.0772 30 GLN A CG 231 C CD . GLN A 30 ? 0.7359 0.8726 0.8187 0.0794 -0.0256 -0.0775 30 GLN A CD 232 O OE1 . GLN A 30 ? 0.7633 0.9169 0.8533 0.0748 -0.0276 -0.0768 30 GLN A OE1 233 N NE2 . GLN A 30 ? 0.7695 0.9180 0.8527 0.0661 -0.0217 -0.0787 30 GLN A NE2 234 N N . ASP A 31 ? 0.7142 0.7044 0.7333 0.1292 -0.0280 -0.0779 31 ASP A N 235 C CA . ASP A 31 ? 0.7441 0.7157 0.7528 0.1238 -0.0255 -0.0797 31 ASP A CA 236 C C . ASP A 31 ? 0.7296 0.7374 0.7553 0.1112 -0.0227 -0.0804 31 ASP A C 237 O O . ASP A 31 ? 0.7285 0.7775 0.7651 0.1161 -0.0209 -0.0825 31 ASP A O 238 C CB . ASP A 31 ? 0.7814 0.7348 0.7650 0.1465 -0.0229 -0.0840 31 ASP A CB 239 C CG . ASP A 31 ? 0.8126 0.7344 0.7786 0.1401 -0.0209 -0.0859 31 ASP A CG 240 O OD1 . ASP A 31 ? 0.7631 0.6896 0.7408 0.1202 -0.0209 -0.0843 31 ASP A OD1 241 O OD2 . ASP A 31 ? 0.8670 0.7571 0.8039 0.1560 -0.0190 -0.0892 31 ASP A OD2 242 N N . ILE A 32 ? 0.6895 0.6835 0.7157 0.0945 -0.0221 -0.0787 32 ILE A N 243 C CA . ILE A 32 ? 0.6568 0.6762 0.6931 0.0817 -0.0190 -0.0789 32 ILE A CA 244 C C . ILE A 32 ? 0.6498 0.6576 0.6758 0.0808 -0.0162 -0.0810 32 ILE A C 245 O O . ILE A 32 ? 0.6105 0.6333 0.6417 0.0693 -0.0136 -0.0806 32 ILE A O 246 C CB . ILE A 32 ? 0.6453 0.6623 0.6904 0.0619 -0.0205 -0.0738 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.6371 0.6193 0.6745 0.0567 -0.0235 -0.0703 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.6568 0.6909 0.7120 0.0603 -0.0224 -0.0725 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.6321 0.6108 0.6728 0.0417 -0.0241 -0.0653 32 ILE A CD1 250 N N . LEU A 33 ? 0.6654 0.6439 0.6734 0.0918 -0.0165 -0.0834 33 LEU A N 251 C CA . LEU A 33 ? 0.6987 0.6622 0.6933 0.0908 -0.0141 -0.0861 33 LEU A CA 252 C C . LEU A 33 ? 0.7539 0.7180 0.7332 0.1119 -0.0109 -0.0918 33 LEU A C 253 O O . LEU A 33 ? 0.8019 0.7428 0.7635 0.1277 -0.0116 -0.0935 33 LEU A O 254 C CB . LEU A 33 ? 0.7144 0.6388 0.6941 0.0828 -0.0167 -0.0849 33 LEU A CB 255 C CG . LEU A 33 ? 0.7332 0.6412 0.6976 0.0777 -0.0147 -0.0877 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.7165 0.6467 0.6951 0.0644 -0.0135 -0.0852 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.7667 0.6394 0.7129 0.0686 -0.0173 -0.0874 33 LEU A CD2 258 N N . GLU A 34 ? 0.7764 0.7645 0.7588 0.1131 -0.0070 -0.0946 34 GLU A N 259 C CA . GLU A 34 ? 0.7908 0.7802 0.7563 0.1347 -0.0034 -0.1002 34 GLU A CA 260 C C . GLU A 34 ? 0.8099 0.7538 0.7485 0.1346 -0.0026 -0.1028 34 GLU A C 261 O O . GLU A 34 ? 0.8126 0.7525 0.7540 0.1178 -0.0022 -0.1021 34 GLU A O 262 C CB . GLU A 34 ? 0.7986 0.8356 0.7780 0.1345 0.0006 -0.1023 34 GLU A CB 263 C CG . GLU A 34 ? 0.8220 0.8674 0.7842 0.1599 0.0046 -0.1082 34 GLU A CG 264 C CD . GLU A 34 ? 0.8552 0.8942 0.8031 0.1870 0.0037 -0.1098 34 GLU A CD 265 O OE1 . GLU A 34 ? 0.8825 0.9597 0.8479 0.1910 0.0025 -0.1084 34 GLU A OE1 266 O OE2 . GLU A 34 ? 0.8991 0.8920 0.8152 0.2035 0.0044 -0.1124 34 GLU A OE2 267 N N . LYS A 35 ? 0.8596 0.7680 0.7688 0.1530 -0.0020 -0.1060 35 LYS A N 268 C CA . LYS A 35 ? 0.8905 0.7486 0.7664 0.1507 -0.0008 -0.1093 35 LYS A CA 269 C C . LYS A 35 ? 0.9028 0.7517 0.7522 0.1728 0.0041 -0.1155 35 LYS A C 270 O O . LYS A 35 ? 0.9086 0.7192 0.7303 0.1680 0.0059 -0.1190 35 LYS A O 271 C CB . LYS A 35 ? 0.9171 0.7253 0.7673 0.1504 -0.0032 -0.1084 35 LYS A CB 272 C CG . LYS A 35 ? 0.9032 0.7152 0.7744 0.1282 -0.0081 -0.1027 35 LYS A CG 273 C CD . LYS A 35 ? 0.9516 0.7211 0.7985 0.1307 -0.0101 -0.1018 35 LYS A CD 274 C CE . LYS A 35 ? 0.9439 0.7364 0.8169 0.1294 -0.0140 -0.0965 35 LYS A CE 275 N NZ . LYS A 35 ? 0.9201 0.7585 0.8167 0.1469 -0.0134 -0.0960 35 LYS A NZ 276 N N . THR A 36 ? 0.8929 0.7792 0.7497 0.1962 0.0065 -0.1172 36 THR A N 277 C CA . THR A 36 ? 0.9606 0.8403 0.7895 0.2230 0.0114 -0.1231 36 THR A CA 278 C C . THR A 36 ? 0.9432 0.8755 0.7935 0.2222 0.0147 -0.1250 36 THR A C 279 O O . THR A 36 ? 0.8809 0.8657 0.7679 0.2087 0.0138 -0.1219 36 THR A O 280 C CB . THR A 36 ? 0.9950 0.8786 0.8071 0.2584 0.0125 -0.1244 36 THR A CB 281 O OG1 . THR A 36 ? 0.9914 0.9436 0.8421 0.2605 0.0112 -0.1218 36 THR A OG1 282 C CG2 . THR A 36 ? 1.0265 0.8521 0.8107 0.2615 0.0099 -0.1225 36 THR A CG2 283 N N . HIS A 37 ? 0.9720 0.8861 0.7948 0.2361 0.0190 -0.1304 37 HIS A N 284 C CA . HIS A 37 ? 0.9705 0.9320 0.8058 0.2417 0.0232 -0.1334 37 HIS A CA 285 C C . HIS A 37 ? 1.0374 0.9848 0.8347 0.2801 0.0279 -0.1395 37 HIS A C 286 O O . HIS A 37 ? 1.0834 0.9735 0.8410 0.2975 0.0281 -0.1412 37 HIS A O 287 C CB . HIS A 37 ? 0.9381 0.8891 0.7781 0.2149 0.0237 -0.1335 37 HIS A CB 288 C CG . HIS A 37 ? 0.9862 0.8694 0.7864 0.2125 0.0242 -0.1370 37 HIS A CG 289 N ND1 . HIS A 37 ? 1.0415 0.9017 0.8076 0.2306 0.0289 -0.1433 37 HIS A ND1 290 C CD2 . HIS A 37 ? 1.0028 0.8371 0.7889 0.1929 0.0209 -0.1354 37 HIS A CD2 291 C CE1 . HIS A 37 ? 1.0719 0.8685 0.8030 0.2202 0.0285 -0.1457 37 HIS A CE1 292 N NE2 . HIS A 37 ? 1.0612 0.8438 0.8045 0.1964 0.0237 -0.1410 37 HIS A NE2 293 N N . ASN A 38 ? 1.0469 1.0442 0.8526 0.2938 0.0321 -0.1427 38 ASN A N 294 C CA . ASN A 38 ? 1.0998 1.0911 0.8692 0.3349 0.0370 -0.1485 38 ASN A CA 295 C C . ASN A 38 ? 1.1507 1.0901 0.8819 0.3381 0.0408 -0.1538 38 ASN A C 296 O O . ASN A 38 ? 1.2364 1.1599 0.9301 0.3729 0.0453 -0.1590 38 ASN A O 297 C CB . ASN A 38 ? 1.0630 1.1426 0.8580 0.3532 0.0399 -0.1499 38 ASN A CB 298 C CG . ASN A 38 ? 1.0201 1.1426 0.8376 0.3342 0.0429 -0.1513 38 ASN A CG 299 O OD1 . ASN A 38 ? 1.0216 1.1096 0.8376 0.3086 0.0425 -0.1510 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.9953 1.1966 0.8334 0.3460 0.0460 -0.1529 38 ASN A ND2 301 N N . GLY A 39 ? 1.1286 1.0454 0.8682 0.3032 0.0392 -0.1528 39 GLY A N 302 C CA . GLY A 39 ? 1.1554 1.0169 0.8570 0.3003 0.0420 -0.1578 39 GLY A CA 303 C C . GLY A 39 ? 1.1446 1.0422 0.8479 0.3104 0.0471 -0.1622 39 GLY A C 304 O O . GLY A 39 ? 1.1330 0.9863 0.7982 0.3171 0.0504 -0.1676 39 GLY A O 305 N N . LYS A 40 ? 1.1139 1.0912 0.8597 0.3090 0.0478 -0.1600 40 LYS A N 306 C CA . LYS A 40 ? 1.1184 1.1428 0.8684 0.3216 0.0530 -0.1640 40 LYS A CA 307 C C . LYS A 40 ? 1.0744 1.1559 0.8695 0.2892 0.0526 -0.1604 40 LYS A C 308 O O . LYS A 40 ? 1.0490 1.1519 0.8770 0.2644 0.0488 -0.1545 40 LYS A O 309 C CB . LYS A 40 ? 1.1482 1.2235 0.8967 0.3606 0.0559 -0.1660 40 LYS A CB 310 C CG . LYS A 40 ? 1.2314 1.2505 0.9250 0.4023 0.0582 -0.1705 40 LYS A CG 311 C CD . LYS A 40 ? 1.2472 1.3179 0.9417 0.4415 0.0595 -0.1709 40 LYS A CD 312 C CE . LYS A 40 ? 1.3510 1.3549 0.9821 0.4859 0.0623 -0.1749 40 LYS A CE 313 N NZ . LYS A 40 ? 1.3884 1.4332 1.0170 0.5253 0.0624 -0.1740 40 LYS A NZ 314 N N . LEU A 41 ? 1.0967 1.1996 0.8893 0.2905 0.0571 -0.1639 41 LEU A N 315 C CA . LEU A 41 ? 1.0738 1.2373 0.9037 0.2654 0.0584 -0.1611 41 LEU A CA 316 C C . LEU A 41 ? 1.0377 1.2814 0.8848 0.2843 0.0622 -0.1626 41 LEU A C 317 O O . LEU A 41 ? 1.0647 1.3206 0.8891 0.3200 0.0662 -0.1682 41 LEU A O 318 C CB . LEU A 41 ? 1.1075 1.2541 0.9254 0.2549 0.0614 -0.1639 41 LEU A CB 319 C CG . LEU A 41 ? 1.1476 1.2241 0.9486 0.2340 0.0577 -0.1629 41 LEU A CG 320 C CD1 . LEU A 41 ? 1.1731 1.2372 0.9593 0.2277 0.0609 -0.1667 41 LEU A CD1 321 C CD2 . LEU A 41 ? 1.1175 1.1964 0.9488 0.2004 0.0525 -0.1552 41 LEU A CD2 322 N N . CYS A 42 ? 0.9726 1.2712 0.8566 0.2607 0.0611 -0.1579 42 CYS A N 323 C CA . CYS A 42 ? 0.9739 1.3538 0.8759 0.2740 0.0639 -0.1592 42 CYS A CA 324 C C . CYS A 42 ? 0.9154 1.3580 0.8468 0.2428 0.0667 -0.1569 42 CYS A C 325 O O . CYS A 42 ? 0.8963 1.3158 0.8369 0.2094 0.0657 -0.1528 42 CYS A O 326 C CB . CYS A 42 ? 0.9856 1.3745 0.8990 0.2783 0.0595 -0.1561 42 CYS A CB 327 S SG . CYS A 42 ? 1.0242 1.3286 0.9029 0.3056 0.0553 -0.1566 42 CYS A SG 328 N N . ASP A 43 ? 0.9106 1.4342 0.8546 0.2536 0.0705 -0.1596 43 ASP A N 329 C CA . ASP A 43 ? 0.8868 1.4755 0.8568 0.2202 0.0736 -0.1576 43 ASP A CA 330 C C . ASP A 43 ? 0.8615 1.4361 0.8499 0.1867 0.0691 -0.1511 43 ASP A C 331 O O . ASP A 43 ? 0.8598 1.4176 0.8492 0.1977 0.0646 -0.1498 43 ASP A O 332 C CB . ASP A 43 ? 0.9014 1.5876 0.8818 0.2369 0.0779 -0.1619 43 ASP A CB 333 C CG . ASP A 43 ? 0.9269 1.6358 0.8877 0.2745 0.0829 -0.1685 43 ASP A CG 334 O OD1 . ASP A 43 ? 0.9411 1.5954 0.8820 0.2801 0.0841 -0.1700 43 ASP A OD1 335 O OD2 . ASP A 43 ? 0.9403 1.7254 0.9046 0.2997 0.0858 -0.1725 43 ASP A OD2 336 N N . LEU A 44 ? 0.8792 1.4562 0.8783 0.1473 0.0707 -0.1471 44 LEU A N 337 C CA . LEU A 44 ? 0.8838 1.4496 0.8962 0.1140 0.0676 -0.1411 44 LEU A CA 338 C C . LEU A 44 ? 0.9377 1.5860 0.9660 0.0942 0.0717 -0.1420 44 LEU A C 339 O O . LEU A 44 ? 0.9574 1.6406 0.9864 0.0739 0.0773 -0.1427 44 LEU A O 340 C CB . LEU A 44 ? 0.8676 1.3783 0.8744 0.0843 0.0673 -0.1358 44 LEU A CB 341 C CG . LEU A 44 ? 0.8640 1.3504 0.8772 0.0504 0.0647 -0.1289 44 LEU A CG 342 C CD1 . LEU A 44 ? 0.8696 1.3168 0.8853 0.0609 0.0580 -0.1265 44 LEU A CD1 343 C CD2 . LEU A 44 ? 0.8569 1.2962 0.8596 0.0276 0.0656 -0.1240 44 LEU A CD2 344 N N . ASP A 45 ? 1.0153 1.6969 1.0545 0.0992 0.0692 -0.1424 45 ASP A N 345 C CA . ASP A 45 ? 1.0297 1.7971 1.0832 0.0799 0.0729 -0.1442 45 ASP A CA 346 C C . ASP A 45 ? 0.9960 1.8369 1.0498 0.0920 0.0792 -0.1500 45 ASP A C 347 O O . ASP A 45 ? 0.9710 1.8604 1.0293 0.0600 0.0846 -0.1504 45 ASP A O 348 C CB . ASP A 45 ? 1.1088 1.8645 1.1641 0.0286 0.0745 -0.1392 45 ASP A CB 349 C CG . ASP A 45 ? 1.1827 1.9588 1.2479 0.0111 0.0717 -0.1376 45 ASP A CG 350 O OD1 . ASP A 45 ? 1.1877 1.9026 1.2515 0.0122 0.0660 -0.1333 45 ASP A OD1 351 O OD2 . ASP A 45 ? 1.2239 2.0806 1.2979 -0.0042 0.0754 -0.1408 45 ASP A OD2 352 N N . GLY A 46 ? 1.0027 1.8473 1.0479 0.1383 0.0790 -0.1545 46 GLY A N 353 C CA . GLY A 46 ? 0.9740 1.8911 1.0173 0.1602 0.0847 -0.1606 46 GLY A CA 354 C C . GLY A 46 ? 0.9728 1.8710 1.0056 0.1524 0.0894 -0.1614 46 GLY A C 355 O O . GLY A 46 ? 0.9848 1.9276 1.0114 0.1786 0.0938 -0.1667 46 GLY A O 356 N N . VAL A 47 ? 0.9501 1.7835 0.9794 0.1186 0.0886 -0.1561 47 VAL A N 357 C CA . VAL A 47 ? 0.9162 1.7292 0.9354 0.1065 0.0928 -0.1560 47 VAL A CA 358 C C . VAL A 47 ? 0.9166 1.6468 0.9176 0.1328 0.0895 -0.1562 47 VAL A C 359 O O . VAL A 47 ? 0.9089 1.5667 0.9058 0.1237 0.0844 -0.1517 47 VAL A O 360 C CB . VAL A 47 ? 0.9009 1.6908 0.9217 0.0554 0.0944 -0.1499 47 VAL A CB 361 C CG1 . VAL A 47 ? 0.9261 1.6995 0.9353 0.0449 0.0990 -0.1496 47 VAL A CG1 362 C CG2 . VAL A 47 ? 0.8829 1.7466 0.9158 0.0233 0.0980 -0.1499 47 VAL A CG2 363 N N . LYS A 48 ? 0.9323 1.6754 0.9205 0.1639 0.0928 -0.1619 48 LYS A N 364 C CA . LYS A 48 ? 0.9534 1.6223 0.9185 0.1911 0.0905 -0.1638 48 LYS A CA 365 C C . LYS A 48 ? 0.9236 1.5262 0.8822 0.1636 0.0893 -0.1595 48 LYS A C 366 O O . LYS A 48 ? 0.8973 1.5195 0.8634 0.1319 0.0927 -0.1566 48 LYS A O 367 C CB . LYS A 48 ? 1.0171 1.7226 0.9672 0.2272 0.0958 -0.1711 48 LYS A CB 368 C CG . LYS A 48 ? 1.0819 1.7180 1.0005 0.2621 0.0947 -0.1751 48 LYS A CG 369 C CD . LYS A 48 ? 1.1379 1.8175 1.0410 0.2943 0.1011 -0.1822 48 LYS A CD 370 C CE . LYS A 48 ? 1.1914 1.7958 1.0576 0.3213 0.1013 -0.1865 48 LYS A CE 371 N NZ . LYS A 48 ? 1.2323 1.7747 1.0735 0.3512 0.0971 -0.1876 48 LYS A NZ 372 N N . PRO A 49 ? 0.9206 1.4446 0.8627 0.1751 0.0846 -0.1590 49 PRO A N 373 C CA . PRO A 49 ? 0.8943 1.3618 0.8280 0.1542 0.0834 -0.1558 49 PRO A CA 374 C C . PRO A 49 ? 0.8789 1.3451 0.7952 0.1683 0.0879 -0.1610 49 PRO A C 375 O O . PRO A 49 ? 0.8900 1.3775 0.7938 0.2013 0.0907 -0.1675 49 PRO A O 376 C CB . PRO A 49 ? 0.8958 1.2901 0.8172 0.1630 0.0769 -0.1546 49 PRO A CB 377 C CG . PRO A 49 ? 0.9260 1.3260 0.8350 0.2011 0.0768 -0.1600 49 PRO A CG 378 C CD . PRO A 49 ? 0.9266 1.4104 0.8553 0.2049 0.0801 -0.1609 49 PRO A CD 379 N N . LEU A 50 ? 0.8526 1.2929 0.7657 0.1450 0.0886 -0.1582 50 LEU A N 380 C CA . LEU A 50 ? 0.8588 1.2836 0.7529 0.1559 0.0918 -0.1628 50 LEU A CA 381 C C . LEU A 50 ? 0.8917 1.2427 0.7623 0.1708 0.0872 -0.1652 50 LEU A C 382 O O . LEU A 50 ? 0.9144 1.2187 0.7846 0.1511 0.0827 -0.1607 50 LEU A O 383 C CB . LEU A 50 ? 0.8422 1.2687 0.7410 0.1241 0.0941 -0.1582 50 LEU A CB 384 C CG . LEU A 50 ? 0.8578 1.2688 0.7386 0.1295 0.0973 -0.1620 50 LEU A CG 385 C CD1 . LEU A 50 ? 0.8675 1.3338 0.7439 0.1523 0.1038 -0.1689 50 LEU A CD1 386 C CD2 . LEU A 50 ? 0.8462 1.2514 0.7307 0.0969 0.0985 -0.1557 50 LEU A CD2 387 N N . ILE A 51 ? 0.9379 1.2776 0.7856 0.2055 0.0887 -0.1724 51 ILE A N 388 C CA . ILE A 51 ? 0.9798 1.2448 0.7973 0.2177 0.0854 -0.1758 51 ILE A CA 389 C C . ILE A 51 ? 0.9978 1.2436 0.7925 0.2209 0.0890 -0.1808 51 ILE A C 390 O O . ILE A 51 ? 1.0204 1.2826 0.7967 0.2485 0.0940 -0.1874 51 ILE A O 391 C CB . ILE A 51 ? 1.0254 1.2730 0.8219 0.2533 0.0849 -0.1803 51 ILE A CB 392 C CG1 . ILE A 51 ? 1.0265 1.2943 0.8476 0.2472 0.0810 -0.1749 51 ILE A CG1 393 C CG2 . ILE A 51 ? 1.0693 1.2327 0.8271 0.2618 0.0824 -0.1841 51 ILE A CG2 394 C CD1 . ILE A 51 ? 1.0775 1.3106 0.8766 0.2764 0.0787 -0.1774 51 ILE A CD1 395 N N . LEU A 52 ? 0.9765 1.1888 0.7712 0.1941 0.0863 -0.1776 52 LEU A N 396 C CA . LEU A 52 ? 0.9865 1.1826 0.7622 0.1918 0.0891 -0.1817 52 LEU A CA 397 C C . LEU A 52 ? 1.0494 1.1876 0.7822 0.2143 0.0896 -0.1901 52 LEU A C 398 O O . LEU A 52 ? 1.0821 1.2057 0.7942 0.2159 0.0924 -0.1949 52 LEU A O 399 C CB . LEU A 52 ? 0.9510 1.1308 0.7381 0.1578 0.0857 -0.1755 52 LEU A CB 400 C CG . LEU A 52 ? 0.9059 1.1331 0.7249 0.1340 0.0866 -0.1673 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.8832 1.0854 0.7068 0.1062 0.0828 -0.1606 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.9186 1.1990 0.7418 0.1378 0.0938 -0.1695 52 LEU A CD2 403 N N . ARG A 53 ? 1.0850 1.1868 0.8009 0.2305 0.0870 -0.1920 53 ARG A N 404 C CA . ARG A 53 ? 1.1813 1.2225 0.8484 0.2543 0.0885 -0.2002 53 ARG A CA 405 C C . ARG A 53 ? 1.2167 1.2017 0.8595 0.2324 0.0865 -0.2027 53 ARG A C 406 O O . ARG A 53 ? 1.2295 1.1859 0.8784 0.2076 0.0808 -0.1987 53 ARG A O 407 C CB . ARG A 53 ? 1.2614 1.3299 0.9094 0.2905 0.0956 -0.2069 53 ARG A CB 408 C CG . ARG A 53 ? 1.3680 1.3775 0.9619 0.3263 0.0979 -0.2147 53 ARG A CG 409 C CD . ARG A 53 ? 1.4342 1.4731 1.0069 0.3637 0.1053 -0.2214 53 ARG A CD 410 N NE . ARG A 53 ? 1.4873 1.5366 1.0439 0.4055 0.1075 -0.2234 53 ARG A NE 411 C CZ . ARG A 53 ? 1.4537 1.5757 1.0477 0.4140 0.1071 -0.2189 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.3843 1.5709 1.0322 0.3817 0.1051 -0.2122 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.4856 1.6142 1.0594 0.4553 0.1091 -0.2212 53 ARG A NH2 414 N N . ASP A 54 ? 1.2443 1.2164 0.8595 0.2407 0.0909 -0.2095 54 ASP A N 415 C CA . ASP A 54 ? 1.2606 1.1869 0.8533 0.2177 0.0891 -0.2124 54 ASP A CA 416 C C . ASP A 54 ? 1.2103 1.1781 0.8325 0.1927 0.0889 -0.2082 54 ASP A C 417 O O . ASP A 54 ? 1.2285 1.1686 0.8331 0.1757 0.0879 -0.2109 54 ASP A O 418 C CB . ASP A 54 ? 1.3426 1.2169 0.8783 0.2398 0.0940 -0.2232 54 ASP A CB 419 C CG . ASP A 54 ? 1.4016 1.2127 0.8939 0.2604 0.0941 -0.2276 54 ASP A CG 420 O OD1 . ASP A 54 ? 1.3648 1.1481 0.8608 0.2430 0.0888 -0.2239 54 ASP A OD1 421 O OD2 . ASP A 54 ? 1.4681 1.2549 0.9188 0.2949 0.0997 -0.2349 54 ASP A OD2 422 N N . CYS A 55 ? 1.1488 1.1811 0.8119 0.1896 0.0901 -0.2017 55 CYS A N 423 C CA . CYS A 55 ? 1.1088 1.1771 0.7965 0.1662 0.0904 -0.1966 55 CYS A CA 424 C C . CYS A 55 ? 1.0460 1.1213 0.7641 0.1381 0.0846 -0.1867 55 CYS A C 425 O O . CYS A 55 ? 1.0284 1.1027 0.7602 0.1382 0.0814 -0.1828 55 CYS A O 426 C CB . CYS A 55 ? 1.0947 1.2276 0.8019 0.1767 0.0966 -0.1957 55 CYS A CB 427 S SG . CYS A 55 ? 1.1685 1.3038 0.8410 0.2121 0.1042 -0.2069 55 CYS A SG 428 N N . SER A 56 ? 1.0148 1.0968 0.7406 0.1161 0.0834 -0.1828 56 SER A N 429 C CA . SER A 56 ? 0.9651 1.0574 0.7163 0.0925 0.0789 -0.1728 56 SER A CA 430 C C . SER A 56 ? 0.9264 1.0688 0.7027 0.0857 0.0828 -0.1663 56 SER A C 431 O O . SER A 56 ? 0.9332 1.1060 0.7084 0.0958 0.0888 -0.1696 56 SER A O 432 C CB . SER A 56 ? 0.9772 1.0478 0.7173 0.0743 0.0754 -0.1721 56 SER A CB 433 O OG . SER A 56 ? 0.9693 1.0638 0.7087 0.0704 0.0796 -0.1718 56 SER A OG 434 N N . VAL A 57 ? 0.9039 1.0537 0.6993 0.0675 0.0798 -0.1570 57 VAL A N 435 C CA . VAL A 57 ? 0.8870 1.0753 0.6990 0.0561 0.0839 -0.1503 57 VAL A CA 436 C C . VAL A 57 ? 0.9046 1.1044 0.7064 0.0508 0.0881 -0.1510 57 VAL A C 437 O O . VAL A 57 ? 0.9074 1.1437 0.7147 0.0486 0.0942 -0.1501 57 VAL A O 438 C CB . VAL A 57 ? 0.8666 1.0484 0.6924 0.0383 0.0799 -0.1400 57 VAL A CB 439 C CG1 . VAL A 57 ? 0.8637 1.0722 0.6960 0.0226 0.0847 -0.1328 57 VAL A CG1 440 C CG2 . VAL A 57 ? 0.8603 1.0404 0.6986 0.0439 0.0771 -0.1395 57 VAL A CG2 441 N N . ALA A 58 ? 0.9029 1.0745 0.6891 0.0478 0.0850 -0.1529 58 ALA A N 442 C CA . ALA A 58 ? 0.9173 1.0970 0.6919 0.0438 0.0883 -0.1541 58 ALA A CA 443 C C . ALA A 58 ? 0.9407 1.1355 0.7039 0.0613 0.0943 -0.1637 58 ALA A C 444 O O . ALA A 58 ? 0.9287 1.1564 0.6946 0.0601 0.1002 -0.1631 58 ALA A O 445 C CB . ALA A 58 ? 0.9258 1.0753 0.6859 0.0366 0.0831 -0.1547 58 ALA A CB 446 N N . GLY A 59 ? 0.9648 1.1343 0.7124 0.0781 0.0930 -0.1724 59 GLY A N 447 C CA . GLY A 59 ? 0.9791 1.1579 0.7110 0.1006 0.0986 -0.1817 59 GLY A CA 448 C C . GLY A 59 ? 0.9804 1.2126 0.7313 0.1081 0.1043 -0.1799 59 GLY A C 449 O O . GLY A 59 ? 0.9922 1.2570 0.7402 0.1139 0.1104 -0.1827 59 GLY A O 450 N N . TRP A 60 ? 0.9584 1.2032 0.7288 0.1062 0.1024 -0.1752 60 TRP A N 451 C CA . TRP A 60 ? 0.9428 1.2429 0.7318 0.1090 0.1073 -0.1734 60 TRP A CA 452 C C . TRP A 60 ? 0.9499 1.2850 0.7479 0.0882 0.1120 -0.1679 60 TRP A C 453 O O . TRP A 60 ? 0.9880 1.3648 0.7847 0.0951 0.1185 -0.1715 60 TRP A O 454 C CB . TRP A 60 ? 0.9281 1.2320 0.7364 0.1036 0.1036 -0.1681 60 TRP A CB 455 C CG . TRP A 60 ? 0.9056 1.2676 0.7349 0.0953 0.1080 -0.1644 60 TRP A CG 456 C CD1 . TRP A 60 ? 0.9320 1.3496 0.7641 0.1047 0.1149 -0.1684 60 TRP A CD1 457 C CD2 . TRP A 60 ? 0.8860 1.2574 0.7339 0.0746 0.1061 -0.1563 60 TRP A CD2 458 N NE1 . TRP A 60 ? 0.9179 1.3820 0.7697 0.0881 0.1174 -0.1636 60 TRP A NE1 459 C CE2 . TRP A 60 ? 0.8934 1.3264 0.7537 0.0691 0.1121 -0.1562 60 TRP A CE2 460 C CE3 . TRP A 60 ? 0.8795 1.2141 0.7330 0.0598 0.1000 -0.1495 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 0.8859 1.3400 0.7614 0.0470 0.1124 -0.1497 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 0.8589 1.2123 0.7273 0.0413 0.1003 -0.1429 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 0.8520 1.2624 0.7302 0.0339 0.1064 -0.1431 60 TRP A CH2 464 N N . LEU A 61 ? 0.9394 1.2564 0.7430 0.0639 0.1089 -0.1593 61 LEU A N 465 C CA . LEU A 61 ? 0.9287 1.2727 0.7374 0.0418 0.1136 -0.1523 61 LEU A CA 466 C C . LEU A 61 ? 0.9429 1.2944 0.7373 0.0412 0.1180 -0.1548 61 LEU A C 467 O O . LEU A 61 ? 0.9356 1.3267 0.7320 0.0324 0.1248 -0.1535 61 LEU A O 468 C CB . LEU A 61 ? 0.9109 1.2258 0.7226 0.0203 0.1092 -0.1420 61 LEU A CB 469 C CG . LEU A 61 ? 0.8955 1.2123 0.7225 0.0148 0.1066 -0.1378 61 LEU A CG 470 C CD1 . LEU A 61 ? 0.9056 1.1846 0.7301 -0.0006 0.1016 -0.1285 61 LEU A CD1 471 C CD2 . LEU A 61 ? 0.8832 1.2489 0.7201 0.0035 0.1132 -0.1362 61 LEU A CD2 472 N N . LEU A 62 ? 0.9633 1.2778 0.7423 0.0484 0.1144 -0.1584 62 LEU A N 473 C CA . LEU A 62 ? 0.9715 1.2897 0.7347 0.0508 0.1180 -0.1623 62 LEU A CA 474 C C . LEU A 62 ? 0.9910 1.3361 0.7470 0.0738 0.1234 -0.1726 62 LEU A C 475 O O . LEU A 62 ? 1.0099 1.3725 0.7560 0.0757 0.1284 -0.1756 62 LEU A O 476 C CB . LEU A 62 ? 0.9719 1.2444 0.7190 0.0505 0.1121 -0.1641 62 LEU A CB 477 C CG . LEU A 62 ? 0.9544 1.2082 0.7044 0.0304 0.1077 -0.1538 62 LEU A CG 478 C CD1 . LEU A 62 ? 0.9577 1.1732 0.6951 0.0311 0.1007 -0.1564 62 LEU A CD1 479 C CD2 . LEU A 62 ? 0.9637 1.2363 0.7087 0.0172 0.1127 -0.1478 62 LEU A CD2 480 N N . GLY A 63 ? 0.9960 1.3444 0.7550 0.0932 0.1227 -0.1777 63 GLY A N 481 C CA . GLY A 63 ? 1.0162 1.3904 0.7652 0.1204 0.1279 -0.1872 63 GLY A CA 482 C C . GLY A 63 ? 1.0442 1.3735 0.7628 0.1390 0.1267 -0.1963 63 GLY A C 483 O O . GLY A 63 ? 1.0573 1.4005 0.7605 0.1520 0.1319 -0.2025 63 GLY A O 484 N N . ASN A 64 ? 1.0533 1.3279 0.7610 0.1384 0.1202 -0.1972 64 ASN A N 485 C CA . ASN A 64 ? 1.0980 1.3233 0.7710 0.1552 0.1192 -0.2069 64 ASN A CA 486 C C . ASN A 64 ? 1.1323 1.3728 0.7890 0.1900 0.1249 -0.2154 64 ASN A C 487 O O . ASN A 64 ? 1.1118 1.3723 0.7802 0.2036 0.1251 -0.2144 64 ASN A O 488 C CB . ASN A 64 ? 1.1042 1.2764 0.7702 0.1489 0.1118 -0.2061 64 ASN A CB 489 C CG . ASN A 64 ? 1.1513 1.2645 0.7751 0.1608 0.1110 -0.2163 64 ASN A CG 490 O OD1 . ASN A 64 ? 1.1871 1.2914 0.7847 0.1879 0.1157 -0.2247 64 ASN A OD1 491 N ND2 . ASN A 64 ? 1.1563 1.2287 0.7702 0.1403 0.1052 -0.2156 64 ASN A ND2 492 N N . PRO A 65 ? 1.1928 1.4247 0.8204 0.2065 0.1296 -0.2239 65 PRO A N 493 C CA . PRO A 65 ? 1.2286 1.4841 0.8392 0.2434 0.1361 -0.2317 65 PRO A CA 494 C C . PRO A 65 ? 1.2706 1.4879 0.8568 0.2727 0.1349 -0.2370 65 PRO A C 495 O O . PRO A 65 ? 1.2987 1.5439 0.8751 0.3063 0.1399 -0.2417 65 PRO A O 496 C CB . PRO A 65 ? 1.2625 1.5003 0.8411 0.2512 0.1403 -0.2395 65 PRO A CB 497 C CG . PRO A 65 ? 1.2656 1.4479 0.8327 0.2240 0.1346 -0.2386 65 PRO A CG 498 C CD . PRO A 65 ? 1.2212 1.4198 0.8272 0.1933 0.1289 -0.2271 65 PRO A CD 499 N N . MET A 66 ? 1.2834 1.4397 0.8586 0.2605 0.1285 -0.2360 66 MET A N 500 C CA . MET A 66 ? 1.3090 1.4261 0.8637 0.2825 0.1267 -0.2389 66 MET A CA 501 C C . MET A 66 ? 1.2515 1.4110 0.8462 0.2791 0.1239 -0.2309 66 MET A C 502 O O . MET A 66 ? 1.2475 1.3808 0.8307 0.2958 0.1219 -0.2318 66 MET A O 503 C CB . MET A 66 ? 1.3499 1.3858 0.8757 0.2656 0.1211 -0.2411 66 MET A CB 504 C CG . MET A 66 ? 1.4240 1.4086 0.9033 0.2663 0.1234 -0.2502 66 MET A CG 505 S SD . MET A 66 ? 1.5550 1.4689 0.9643 0.3082 0.1282 -0.2623 66 MET A SD 506 C CE . MET A 66 ? 1.6050 1.4544 0.9639 0.2920 0.1294 -0.2716 66 MET A CE 507 N N . CYS A 67 ? 1.1962 1.4171 0.8340 0.2564 0.1240 -0.2229 67 CYS A N 508 C CA . CYS A 67 ? 1.1526 1.4121 0.8278 0.2461 0.1213 -0.2149 67 CYS A CA 509 C C . CYS A 67 ? 1.1401 1.4839 0.8396 0.2542 0.1273 -0.2137 67 CYS A C 510 O O . CYS A 67 ? 1.0901 1.4789 0.8242 0.2310 0.1266 -0.2060 67 CYS A O 511 C CB . CYS A 67 ? 1.1025 1.3514 0.8027 0.2061 0.1158 -0.2058 67 CYS A CB 512 S SG . CYS A 67 ? 1.1211 1.2832 0.7951 0.1945 0.1086 -0.2074 67 CYS A SG 513 N N . ASP A 68 ? 1.1715 1.5357 0.8491 0.2871 0.1333 -0.2216 68 ASP A N 514 C CA . ASP A 68 ? 1.1624 1.6133 0.8586 0.2987 0.1397 -0.2220 68 ASP A CA 515 C C . ASP A 68 ? 1.1542 1.6483 0.8714 0.3093 0.1386 -0.2194 68 ASP A C 516 O O . ASP A 68 ? 1.1400 1.7129 0.8856 0.3004 0.1420 -0.2164 68 ASP A O 517 C CB . ASP A 68 ? 1.2033 1.6626 0.8665 0.3367 0.1462 -0.2317 68 ASP A CB 518 C CG . ASP A 68 ? 1.2116 1.6496 0.8602 0.3230 0.1485 -0.2342 68 ASP A CG 519 O OD1 . ASP A 68 ? 1.1995 1.6195 0.8644 0.2852 0.1449 -0.2279 68 ASP A OD1 520 O OD2 . ASP A 68 ? 1.2314 1.6705 0.8507 0.3515 0.1539 -0.2422 68 ASP A OD2 521 N N . GLU A 69 ? 1.1767 1.6205 0.8788 0.3260 0.1340 -0.2204 69 GLU A N 522 C CA . GLU A 69 ? 1.1640 1.6425 0.8868 0.3332 0.1319 -0.2171 69 GLU A CA 523 C C . GLU A 69 ? 1.1128 1.6405 0.8801 0.2916 0.1302 -0.2080 69 GLU A C 524 O O . GLU A 69 ? 1.0837 1.6803 0.8742 0.2930 0.1319 -0.2062 69 GLU A O 525 C CB . GLU A 69 ? 1.1887 1.5913 0.8909 0.3443 0.1259 -0.2173 69 GLU A CB 526 C CG . GLU A 69 ? 1.1844 1.6196 0.9034 0.3574 0.1238 -0.2146 69 GLU A CG 527 C CD . GLU A 69 ? 1.2087 1.5665 0.9058 0.3665 0.1181 -0.2144 69 GLU A CD 528 O OE1 . GLU A 69 ? 1.2416 1.5201 0.9073 0.3632 0.1162 -0.2171 69 GLU A OE1 529 O OE2 . GLU A 69 ? 1.2045 1.5821 0.9146 0.3757 0.1157 -0.2117 69 GLU A OE2 530 N N . PHE A 70 ? 1.0988 1.5910 0.8740 0.2550 0.1272 -0.2027 70 PHE A N 531 C CA . PHE A 70 ? 1.0586 1.5771 0.8663 0.2152 0.1255 -0.1936 70 PHE A CA 532 C C . PHE A 70 ? 1.0539 1.6192 0.8724 0.1912 0.1311 -0.1913 70 PHE A C 533 O O . PHE A 70 ? 1.0186 1.5798 0.8514 0.1554 0.1300 -0.1836 70 PHE A O 534 C CB . PHE A 70 ? 1.0401 1.4867 0.8470 0.1931 0.1182 -0.1882 70 PHE A CB 535 C CG . PHE A 70 ? 1.0458 1.4364 0.8341 0.2155 0.1132 -0.1915 70 PHE A CG 536 C CD1 . PHE A 70 ? 1.0241 1.4305 0.8229 0.2276 0.1111 -0.1904 70 PHE A CD1 537 C CD2 . PHE A 70 ? 1.0688 1.3913 0.8259 0.2239 0.1112 -0.1961 70 PHE A CD2 538 C CE1 . PHE A 70 ? 1.0427 1.3948 0.8210 0.2480 0.1070 -0.1932 70 PHE A CE1 539 C CE2 . PHE A 70 ? 1.0954 1.3627 0.8299 0.2419 0.1074 -0.1993 70 PHE A CE2 540 C CZ . PHE A 70 ? 1.0795 1.3602 0.8242 0.2546 0.1054 -0.1976 70 PHE A CZ 541 N N . ILE A 71 ? 1.0917 1.7013 0.9007 0.2121 0.1376 -0.1976 71 ILE A N 542 C CA . ILE A 71 ? 1.1107 1.7644 0.9263 0.1911 0.1436 -0.1961 71 ILE A CA 543 C C . ILE A 71 ? 1.0966 1.8182 0.9393 0.1615 0.1466 -0.1903 71 ILE A C 544 O O . ILE A 71 ? 1.0768 1.8117 0.9247 0.1291 0.1498 -0.1854 71 ILE A O 545 C CB . ILE A 71 ? 1.1526 1.8408 0.9500 0.2227 0.1502 -0.2050 71 ILE A CB 546 C CG1 . ILE A 71 ? 1.1457 1.8523 0.9428 0.1993 0.1552 -0.2033 71 ILE A CG1 547 C CG2 . ILE A 71 ? 1.1372 1.9083 0.9437 0.2482 0.1548 -0.2092 71 ILE A CG2 548 C CD1 . ILE A 71 ? 1.1795 1.8708 0.9487 0.2272 0.1587 -0.2116 71 ILE A CD1 549 N N . ASN A 72 ? 1.1096 1.8728 0.9660 0.1719 0.1460 -0.1910 72 ASN A N 550 C CA . ASN A 72 ? 1.1095 1.9263 0.9895 0.1389 0.1476 -0.1853 72 ASN A CA 551 C C . ASN A 72 ? 1.0944 1.9109 0.9865 0.1462 0.1424 -0.1840 72 ASN A C 552 O O . ASN A 72 ? 1.0983 1.9685 0.9952 0.1732 0.1437 -0.1889 72 ASN A O 553 C CB . ASN A 72 ? 1.1386 2.0534 1.0265 0.1356 0.1561 -0.1886 72 ASN A CB 554 C CG . ASN A 72 ? 1.1719 2.0923 1.0559 0.1012 0.1613 -0.1850 72 ASN A CG 555 O OD1 . ASN A 72 ? 1.1853 2.0550 1.0677 0.0679 0.1591 -0.1774 72 ASN A OD1 556 N ND2 . ASN A 72 ? 1.1924 2.1735 1.0723 0.1109 0.1685 -0.1901 72 ASN A ND2 557 N N . VAL A 73 ? 1.0960 1.8530 0.9922 0.1232 0.1365 -0.1772 73 VAL A N 558 C CA . VAL A 73 ? 1.0645 1.8080 0.9703 0.1298 0.1307 -0.1756 73 VAL A CA 559 C C . VAL A 73 ? 1.0268 1.8246 0.9529 0.0987 0.1324 -0.1712 73 VAL A C 560 O O . VAL A 73 ? 1.0086 1.8066 0.9369 0.0595 0.1349 -0.1654 73 VAL A O 561 C CB . VAL A 73 ? 1.0745 1.7267 0.9734 0.1225 0.1232 -0.1709 73 VAL A CB 562 C CG1 . VAL A 73 ? 1.0935 1.6903 0.9689 0.1486 0.1216 -0.1758 73 VAL A CG1 563 C CG2 . VAL A 73 ? 1.0775 1.7042 0.9806 0.0797 0.1228 -0.1622 73 VAL A CG2 564 N N . PRO A 74 ? 1.0105 1.8513 0.9478 0.1157 0.1311 -0.1738 74 PRO A N 565 C CA . PRO A 74 ? 0.9993 1.8891 0.9544 0.0840 0.1321 -0.1700 74 PRO A CA 566 C C . PRO A 74 ? 0.9534 1.7753 0.9108 0.0585 0.1260 -0.1624 74 PRO A C 567 O O . PRO A 74 ? 0.9352 1.6789 0.8830 0.0676 0.1207 -0.1603 74 PRO A O 568 C CB . PRO A 74 ? 0.9970 1.9513 0.9614 0.1169 0.1318 -0.1757 74 PRO A CB 569 C CG . PRO A 74 ? 1.0184 1.9151 0.9672 0.1628 0.1272 -0.1794 74 PRO A CG 570 C CD . PRO A 74 ? 1.0296 1.8705 0.9601 0.1641 0.1285 -0.1799 74 PRO A CD 571 N N . GLU A 75 ? 0.9364 1.7916 0.9048 0.0260 0.1271 -0.1588 75 GLU A N 572 C CA . GLU A 75 ? 0.9292 1.7290 0.8990 0.0029 0.1220 -0.1519 75 GLU A CA 573 C C . GLU A 75 ? 0.8974 1.6454 0.8688 0.0351 0.1139 -0.1526 75 GLU A C 574 O O . GLU A 75 ? 0.8715 1.6511 0.8478 0.0691 0.1127 -0.1581 75 GLU A O 575 C CB . GLU A 75 ? 0.9426 1.8000 0.9230 -0.0277 0.1246 -0.1506 75 GLU A CB 576 C CG . GLU A 75 ? 0.9584 1.7599 0.9371 -0.0535 0.1200 -0.1436 75 GLU A CG 577 C CD . GLU A 75 ? 0.9617 1.8175 0.9465 -0.0868 0.1230 -0.1430 75 GLU A CD 578 O OE1 . GLU A 75 ? 0.9777 1.9150 0.9662 -0.0998 0.1296 -0.1471 75 GLU A OE1 579 O OE2 . GLU A 75 ? 0.9568 1.7751 0.9416 -0.1007 0.1188 -0.1387 75 GLU A OE2 580 N N . TRP A 76 ? 0.8855 1.5546 0.8502 0.0250 0.1087 -0.1468 76 TRP A N 581 C CA . TRP A 76 ? 0.8754 1.4913 0.8396 0.0492 0.1011 -0.1468 76 TRP A CA 582 C C . TRP A 76 ? 0.8786 1.4652 0.8496 0.0263 0.0967 -0.1402 76 TRP A C 583 O O . TRP A 76 ? 0.8967 1.4860 0.8667 -0.0085 0.0992 -0.1351 76 TRP A O 584 C CB . TRP A 76 ? 0.8615 1.4100 0.8098 0.0631 0.0984 -0.1470 76 TRP A CB 585 C CG . TRP A 76 ? 0.8521 1.3555 0.7928 0.0337 0.0981 -0.1401 76 TRP A CG 586 C CD1 . TRP A 76 ? 0.8386 1.2881 0.7778 0.0190 0.0929 -0.1335 76 TRP A CD1 587 C CD2 . TRP A 76 ? 0.8494 1.3584 0.7805 0.0183 0.1033 -0.1390 76 TRP A CD2 588 N NE1 . TRP A 76 ? 0.8315 1.2532 0.7594 -0.0025 0.0946 -0.1281 76 TRP A NE1 589 C CE2 . TRP A 76 ? 0.8415 1.2971 0.7641 -0.0040 0.1009 -0.1313 76 TRP A CE2 590 C CE3 . TRP A 76 ? 0.8647 1.4198 0.7924 0.0225 0.1099 -0.1436 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 0.8596 1.3041 0.7691 -0.0216 0.1049 -0.1278 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 0.8617 1.4060 0.7781 0.0024 0.1139 -0.1404 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 0.8624 1.3508 0.7691 -0.0192 0.1113 -0.1324 76 TRP A CH2 594 N N . SER A 77 ? 0.8838 1.4394 0.8578 0.0465 0.0904 -0.1406 77 SER A N 595 C CA . SER A 77 ? 0.8578 1.3833 0.8379 0.0302 0.0855 -0.1349 77 SER A CA 596 C C . SER A 77 ? 0.8452 1.2926 0.8152 0.0276 0.0804 -0.1302 77 SER A C 597 O O . SER A 77 ? 0.8411 1.2581 0.8096 0.0040 0.0786 -0.1236 77 SER A O 598 C CB . SER A 77 ? 0.8568 1.4009 0.8464 0.0548 0.0817 -0.1381 77 SER A CB 599 O OG . SER A 77 ? 0.8803 1.4009 0.8597 0.0918 0.0797 -0.1430 77 SER A OG 600 N N . TYR A 78 ? 0.8320 1.2481 0.7924 0.0530 0.0782 -0.1339 78 TYR A N 601 C CA . TYR A 78 ? 0.7935 1.1450 0.7424 0.0506 0.0740 -0.1308 78 TYR A CA 602 C C . TYR A 78 ? 0.7905 1.1305 0.7246 0.0712 0.0756 -0.1368 78 TYR A C 603 O O . TYR A 78 ? 0.7899 1.1672 0.7222 0.0905 0.0795 -0.1430 78 TYR A O 604 C CB . TYR A 78 ? 0.7766 1.0866 0.7273 0.0574 0.0670 -0.1286 78 TYR A CB 605 C CG . TYR A 78 ? 0.7700 1.0829 0.7187 0.0876 0.0650 -0.1345 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.7523 1.1099 0.7132 0.0959 0.0658 -0.1360 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.7861 1.0553 0.7168 0.1074 0.0626 -0.1384 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.7555 1.1131 0.7102 0.1270 0.0642 -0.1409 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.7960 1.0588 0.7169 0.1360 0.0615 -0.1434 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.7812 1.0875 0.7140 0.1477 0.0623 -0.1443 78 TYR A CZ 611 O OH . TYR A 78 ? 0.7959 1.0922 0.7144 0.1799 0.0613 -0.1489 78 TYR A OH 612 N N . ILE A 79 ? 0.7887 1.0792 0.7107 0.0678 0.0728 -0.1352 79 ILE A N 613 C CA . ILE A 79 ? 0.8139 1.0880 0.7184 0.0835 0.0743 -0.1411 79 ILE A CA 614 C C . ILE A 79 ? 0.8336 1.0541 0.7237 0.0970 0.0688 -0.1436 79 ILE A C 615 O O . ILE A 79 ? 0.8324 1.0219 0.7260 0.0856 0.0636 -0.1388 79 ILE A O 616 C CB . ILE A 79 ? 0.8204 1.0861 0.7190 0.0648 0.0763 -0.1378 79 ILE A CB 617 C CG1 . ILE A 79 ? 0.8197 1.1365 0.7263 0.0509 0.0830 -0.1362 79 ILE A CG1 618 C CG2 . ILE A 79 ? 0.8500 1.0912 0.7289 0.0783 0.0768 -0.1438 79 ILE A CG2 619 C CD1 . ILE A 79 ? 0.8291 1.1348 0.7284 0.0293 0.0852 -0.1310 79 ILE A CD1 620 N N . VAL A 80 ? 0.8631 1.0706 0.7334 0.1205 0.0704 -0.1513 80 VAL A N 621 C CA . VAL A 80 ? 0.8914 1.0418 0.7402 0.1299 0.0661 -0.1544 80 VAL A CA 622 C C . VAL A 80 ? 0.9185 1.0396 0.7426 0.1314 0.0675 -0.1594 80 VAL A C 623 O O . VAL A 80 ? 0.9342 1.0695 0.7453 0.1478 0.0725 -0.1653 80 VAL A O 624 C CB . VAL A 80 ? 0.9108 1.0537 0.7474 0.1582 0.0661 -0.1593 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.9449 1.0220 0.7544 0.1626 0.0621 -0.1620 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.8910 1.0680 0.7526 0.1568 0.0646 -0.1547 80 VAL A CG2 627 N N . GLU A 81 ? 0.9318 1.0141 0.7485 0.1147 0.0631 -0.1573 81 GLU A N 628 C CA . GLU A 81 ? 0.9638 1.0181 0.7570 0.1108 0.0636 -0.1618 81 GLU A CA 629 C C . GLU A 81 ? 0.9968 0.9966 0.7659 0.1092 0.0592 -0.1650 81 GLU A C 630 O O . GLU A 81 ? 1.0051 0.9929 0.7842 0.0980 0.0542 -0.1602 81 GLU A O 631 C CB . GLU A 81 ? 0.9546 1.0233 0.7617 0.0871 0.0626 -0.1555 81 GLU A CB 632 C CG . GLU A 81 ? 0.9804 1.0310 0.7665 0.0817 0.0634 -0.1598 81 GLU A CG 633 C CD . GLU A 81 ? 0.9699 1.0361 0.7683 0.0614 0.0622 -0.1527 81 GLU A CD 634 O OE1 . GLU A 81 ? 0.9382 1.0013 0.7497 0.0485 0.0577 -0.1455 81 GLU A OE1 635 O OE2 . GLU A 81 ? 0.9674 1.0482 0.7602 0.0601 0.0661 -0.1543 81 GLU A OE2 636 N N . LYS A 82 ? 1.0668 1.0322 0.8011 0.1192 0.0614 -0.1733 82 LYS A N 637 C CA . LYS A 82 ? 1.1221 1.0322 0.8269 0.1120 0.0579 -0.1770 82 LYS A CA 638 C C . LYS A 82 ? 1.1105 1.0179 0.8225 0.0828 0.0532 -0.1732 82 LYS A C 639 O O . LYS A 82 ? 1.0530 0.9944 0.7860 0.0720 0.0533 -0.1686 82 LYS A O 640 C CB . LYS A 82 ? 1.1840 1.0526 0.8423 0.1284 0.0623 -0.1874 82 LYS A CB 641 C CG . LYS A 82 ? 1.2168 1.0811 0.8603 0.1622 0.0664 -0.1913 82 LYS A CG 642 C CD . LYS A 82 ? 1.2946 1.1065 0.8831 0.1807 0.0710 -0.2016 82 LYS A CD 643 C CE . LYS A 82 ? 1.3519 1.1431 0.9156 0.2157 0.0740 -0.2048 82 LYS A CE 644 N NZ . LYS A 82 ? 1.3476 1.2040 0.9407 0.2407 0.0773 -0.2026 82 LYS A NZ 645 N N . ALA A 83 ? 1.1600 1.0282 0.8526 0.0705 0.0492 -0.1750 83 ALA A N 646 C CA . ALA A 83 ? 1.1669 1.0361 0.8631 0.0438 0.0444 -0.1722 83 ALA A CA 647 C C . ALA A 83 ? 1.1930 1.0632 0.8722 0.0353 0.0464 -0.1769 83 ALA A C 648 O O . ALA A 83 ? 1.2001 1.1002 0.8975 0.0214 0.0442 -0.1719 83 ALA A O 649 C CB . ALA A 83 ? 1.1780 1.0073 0.8528 0.0314 0.0404 -0.1744 83 ALA A CB 650 N N . ASN A 84 ? 1.2334 1.0697 0.8754 0.0453 0.0507 -0.1865 84 ASN A N 651 C CA . ASN A 84 ? 1.2700 1.1060 0.8936 0.0392 0.0533 -0.1919 84 ASN A CA 652 C C . ASN A 84 ? 1.2635 1.0936 0.8689 0.0644 0.0602 -0.1983 84 ASN A C 653 O O . ASN A 84 ? 1.2967 1.0799 0.8576 0.0716 0.0633 -0.2076 84 ASN A O 654 C CB . ASN A 84 ? 1.3470 1.1416 0.9325 0.0172 0.0510 -0.1987 84 ASN A CB 655 C CG . ASN A 84 ? 1.3620 1.1759 0.9671 -0.0085 0.0441 -0.1925 84 ASN A CG 656 O OD1 . ASN A 84 ? 1.3516 1.2058 0.9797 -0.0194 0.0417 -0.1873 84 ASN A OD1 657 N ND2 . ASN A 84 ? 1.3841 1.1701 0.9781 -0.0167 0.0411 -0.1928 84 ASN A ND2 658 N N . PRO A 85 ? 1.2106 1.0878 0.8470 0.0777 0.0631 -0.1936 85 PRO A N 659 C CA . PRO A 85 ? 1.2444 1.1256 0.8659 0.1029 0.0699 -0.1995 85 PRO A CA 660 C C . PRO A 85 ? 1.2702 1.1312 0.8593 0.0988 0.0728 -0.2074 85 PRO A C 661 O O . PRO A 85 ? 1.2747 1.1513 0.8734 0.0774 0.0703 -0.2050 85 PRO A O 662 C CB . PRO A 85 ? 1.1960 1.1401 0.8602 0.1068 0.0718 -0.1919 85 PRO A CB 663 C CG . PRO A 85 ? 1.1388 1.0997 0.8356 0.0900 0.0663 -0.1822 85 PRO A CG 664 C CD . PRO A 85 ? 1.1495 1.0770 0.8311 0.0689 0.0609 -0.1830 85 PRO A CD 665 N N . VAL A 86 ? 1.3062 1.1325 0.8550 0.1205 0.0779 -0.2167 86 VAL A N 666 C CA . VAL A 86 ? 1.3387 1.1395 0.8507 0.1174 0.0811 -0.2253 86 VAL A CA 667 C C . VAL A 86 ? 1.2986 1.1497 0.8311 0.1230 0.0850 -0.2241 86 VAL A C 668 O O . VAL A 86 ? 1.2959 1.1431 0.8148 0.1094 0.0855 -0.2276 86 VAL A O 669 C CB . VAL A 86 ? 1.4210 1.1588 0.8740 0.1407 0.0861 -0.2361 86 VAL A CB 670 C CG1 . VAL A 86 ? 1.4458 1.1272 0.8719 0.1340 0.0830 -0.2374 86 VAL A CG1 671 C CG2 . VAL A 86 ? 1.4382 1.2001 0.8935 0.1798 0.0922 -0.2373 86 VAL A CG2 672 N N . ASN A 87 ? 1.2420 1.1411 0.8051 0.1416 0.0880 -0.2194 87 ASN A N 673 C CA . ASN A 87 ? 1.2182 1.1672 0.7995 0.1462 0.0924 -0.2181 87 ASN A CA 674 C C . ASN A 87 ? 1.1705 1.1671 0.7970 0.1235 0.0893 -0.2072 87 ASN A C 675 O O . ASN A 87 ? 1.1556 1.1956 0.8139 0.1278 0.0905 -0.2008 87 ASN A O 676 C CB . ASN A 87 ? 1.2218 1.1996 0.8045 0.1788 0.0986 -0.2205 87 ASN A CB 677 C CG . ASN A 87 ? 1.2898 1.2209 0.8207 0.2066 0.1032 -0.2317 87 ASN A CG 678 O OD1 . ASN A 87 ? 1.3437 1.2409 0.8407 0.2026 0.1049 -0.2386 87 ASN A OD1 679 N ND2 . ASN A 87 ? 1.3210 1.2487 0.8419 0.2363 0.1055 -0.2336 87 ASN A ND2 680 N N . ASP A 88 ? 1.1701 1.1571 0.7951 0.0993 0.0854 -0.2053 88 ASP A N 681 C CA . ASP A 88 ? 1.1289 1.1524 0.7877 0.0794 0.0825 -0.1950 88 ASP A CA 682 C C . ASP A 88 ? 1.1406 1.1882 0.7968 0.0761 0.0864 -0.1958 88 ASP A C 683 O O . ASP A 88 ? 1.1249 1.1942 0.7793 0.0922 0.0927 -0.1990 88 ASP A O 684 C CB . ASP A 88 ? 1.1203 1.1214 0.7790 0.0577 0.0751 -0.1917 88 ASP A CB 685 C CG . ASP A 88 ? 1.0847 1.1183 0.7766 0.0429 0.0716 -0.1797 88 ASP A CG 686 O OD1 . ASP A 88 ? 1.0951 1.1613 0.8098 0.0474 0.0747 -0.1735 88 ASP A OD1 687 O OD2 . ASP A 88 ? 1.0880 1.1145 0.7803 0.0265 0.0660 -0.1764 88 ASP A OD2 688 N N . LEU A 89 ? 1.1414 1.1885 0.7967 0.0565 0.0829 -0.1929 89 LEU A N 689 C CA . LEU A 89 ? 1.1455 1.2106 0.7946 0.0525 0.0861 -0.1939 89 LEU A CA 690 C C . LEU A 89 ? 1.1879 1.2199 0.7981 0.0588 0.0883 -0.2064 89 LEU A C 691 O O . LEU A 89 ? 1.2204 1.2235 0.8094 0.0448 0.0842 -0.2106 89 LEU A O 692 C CB . LEU A 89 ? 1.1221 1.1997 0.7822 0.0317 0.0812 -0.1858 89 LEU A CB 693 C CG . LEU A 89 ? 1.0776 1.1794 0.7684 0.0255 0.0792 -0.1731 89 LEU A CG 694 C CD1 . LEU A 89 ? 1.0735 1.1816 0.7668 0.0098 0.0741 -0.1659 89 LEU A CD1 695 C CD2 . LEU A 89 ? 1.0498 1.1845 0.7558 0.0317 0.0858 -0.1685 89 LEU A CD2 696 N N . CYS A 90 ? 1.1913 1.2292 0.7901 0.0794 0.0951 -0.2124 90 CYS A N 697 C CA . CYS A 90 ? 1.2257 1.2273 0.7822 0.0902 0.0984 -0.2248 90 CYS A CA 698 C C . CYS A 90 ? 1.2077 1.2079 0.7491 0.0738 0.0977 -0.2276 90 CYS A C 699 O O . CYS A 90 ? 1.2479 1.2065 0.7537 0.0664 0.0963 -0.2361 90 CYS A O 700 C CB . CYS A 90 ? 1.2707 1.2878 0.8204 0.1197 0.1061 -0.2296 90 CYS A CB 701 S SG . CYS A 90 ? 1.2673 1.3561 0.8516 0.1215 0.1114 -0.2224 90 CYS A SG 702 N N . TYR A 91 ? 1.1573 1.2015 0.7227 0.0673 0.0991 -0.2205 91 TYR A N 703 C CA . TYR A 91 ? 1.1527 1.2036 0.7119 0.0490 0.0968 -0.2197 91 TYR A CA 704 C C . TYR A 91 ? 1.1246 1.1814 0.7034 0.0288 0.0892 -0.2108 91 TYR A C 705 O O . TYR A 91 ? 1.1010 1.1821 0.7103 0.0283 0.0881 -0.2004 91 TYR A O 706 C CB . TYR A 91 ? 1.1453 1.2392 0.7195 0.0520 0.1019 -0.2149 91 TYR A CB 707 C CG . TYR A 91 ? 1.1735 1.2695 0.7310 0.0401 0.1014 -0.2176 91 TYR A CG 708 C CD1 . TYR A 91 ? 1.1647 1.2723 0.7318 0.0207 0.0956 -0.2103 91 TYR A CD1 709 C CD2 . TYR A 91 ? 1.1998 1.2868 0.7295 0.0499 0.1066 -0.2277 91 TYR A CD2 710 C CE1 . TYR A 91 ? 1.1788 1.2924 0.7301 0.0107 0.0948 -0.2128 91 TYR A CE1 711 C CE2 . TYR A 91 ? 1.2108 1.3005 0.7245 0.0383 0.1061 -0.2305 91 TYR A CE2 712 C CZ . TYR A 91 ? 1.1968 1.3011 0.7220 0.0183 0.1000 -0.2231 91 TYR A CZ 713 O OH . TYR A 91 ? 1.2082 1.3192 0.7171 0.0077 0.0993 -0.2260 91 TYR A OH 714 N N . PRO A 92 ? 1.1364 1.1727 0.6960 0.0118 0.0841 -0.2148 92 PRO A N 715 C CA . PRO A 92 ? 1.1070 1.1512 0.6837 -0.0043 0.0768 -0.2070 92 PRO A CA 716 C C . PRO A 92 ? 1.0846 1.1703 0.6889 -0.0090 0.0752 -0.1943 92 PRO A C 717 O O . PRO A 92 ? 1.0818 1.1884 0.6865 -0.0059 0.0791 -0.1925 92 PRO A O 718 C CB . PRO A 92 ? 1.1383 1.1609 0.6848 -0.0230 0.0726 -0.2154 92 PRO A CB 719 C CG . PRO A 92 ? 1.1731 1.1912 0.6945 -0.0198 0.0775 -0.2237 92 PRO A CG 720 C CD . PRO A 92 ? 1.1806 1.1922 0.7023 0.0047 0.0849 -0.2262 92 PRO A CD 721 N N . GLY A 93 ? 1.0930 1.1873 0.7168 -0.0156 0.0699 -0.1855 93 GLY A N 722 C CA . GLY A 93 ? 1.0878 1.2132 0.7307 -0.0185 0.0682 -0.1729 93 GLY A CA 723 C C . GLY A 93 ? 1.0848 1.2135 0.7490 -0.0192 0.0641 -0.1632 93 GLY A C 724 O O . GLY A 93 ? 1.0783 1.1919 0.7419 -0.0245 0.0595 -0.1658 93 GLY A O 725 N N . ASP A 94 ? 1.0762 1.2226 0.7558 -0.0150 0.0662 -0.1519 94 ASP A N 726 C CA . ASP A 94 ? 1.0581 1.2048 0.7554 -0.0141 0.0636 -0.1422 94 ASP A CA 727 C C . ASP A 94 ? 1.0270 1.1796 0.7359 -0.0083 0.0698 -0.1361 94 ASP A C 728 O O . ASP A 94 ? 1.0297 1.1923 0.7336 -0.0060 0.0759 -0.1375 94 ASP A O 729 C CB . ASP A 94 ? 1.0773 1.2382 0.7739 -0.0177 0.0586 -0.1326 94 ASP A CB 730 C CG . ASP A 94 ? 1.1209 1.2870 0.8065 -0.0263 0.0521 -0.1383 94 ASP A CG 731 O OD1 . ASP A 94 ? 1.1305 1.2866 0.8194 -0.0315 0.0476 -0.1417 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.1595 1.3414 0.8321 -0.0294 0.0515 -0.1394 94 ASP A OD2 733 N N . PHE A 95 ? 0.9969 1.1445 0.7201 -0.0077 0.0685 -0.1297 95 PHE A N 734 C CA . PHE A 95 ? 0.9498 1.1034 0.6827 -0.0067 0.0738 -0.1229 95 PHE A CA 735 C C . PHE A 95 ? 0.9362 1.0855 0.6697 -0.0096 0.0708 -0.1107 95 PHE A C 736 O O . PHE A 95 ? 0.9261 1.0664 0.6666 -0.0092 0.0654 -0.1084 95 PHE A O 737 C CB . PHE A 95 ? 0.9369 1.0861 0.6831 -0.0022 0.0749 -0.1279 95 PHE A CB 738 C CG . PHE A 95 ? 0.9289 1.0929 0.6839 -0.0026 0.0816 -0.1246 95 PHE A CG 739 C CD1 . PHE A 95 ? 0.9349 1.0989 0.6930 -0.0102 0.0828 -0.1139 95 PHE A CD1 740 C CD2 . PHE A 95 ? 0.9337 1.1120 0.6910 0.0042 0.0868 -0.1326 95 PHE A CD2 741 C CE1 . PHE A 95 ? 0.9497 1.1288 0.7134 -0.0153 0.0893 -0.1115 95 PHE A CE1 742 C CE2 . PHE A 95 ? 0.9370 1.1377 0.7031 0.0019 0.0930 -0.1301 95 PHE A CE2 743 C CZ . PHE A 95 ? 0.9350 1.1367 0.7045 -0.0102 0.0943 -0.1197 95 PHE A CZ 744 N N . ASN A 96 ? 0.9366 1.0898 0.6587 -0.0115 0.0746 -0.1026 96 ASN A N 745 C CA . ASN A 96 ? 0.9412 1.0847 0.6547 -0.0108 0.0724 -0.0906 96 ASN A CA 746 C C . ASN A 96 ? 0.9234 1.0535 0.6448 -0.0134 0.0737 -0.0845 96 ASN A C 747 O O . ASN A 96 ? 0.8947 1.0277 0.6218 -0.0192 0.0796 -0.0859 96 ASN A O 748 C CB . ASN A 96 ? 0.9769 1.1218 0.6695 -0.0113 0.0772 -0.0837 96 ASN A CB 749 C CG . ASN A 96 ? 1.0039 1.1370 0.6793 -0.0052 0.0743 -0.0719 96 ASN A CG 750 O OD1 . ASN A 96 ? 1.0082 1.1499 0.6817 0.0015 0.0676 -0.0718 96 ASN A OD1 751 N ND2 . ASN A 96 ? 1.0306 1.1440 0.6904 -0.0076 0.0795 -0.0619 96 ASN A ND2 752 N N . ASP A 97 ? 0.9319 1.0506 0.6522 -0.0094 0.0684 -0.0780 97 ASP A N 753 C CA . ASP A 97 ? 0.9274 1.0300 0.6529 -0.0113 0.0685 -0.0722 97 ASP A CA 754 C C . ASP A 97 ? 0.8812 0.9896 0.6287 -0.0155 0.0696 -0.0802 97 ASP A C 755 O O . ASP A 97 ? 0.8534 0.9578 0.6038 -0.0221 0.0741 -0.0776 97 ASP A O 756 C CB . ASP A 97 ? 0.9859 1.0709 0.6897 -0.0162 0.0752 -0.0618 97 ASP A CB 757 C CG . ASP A 97 ? 1.0342 1.1033 0.7118 -0.0068 0.0732 -0.0512 97 ASP A CG 758 O OD1 . ASP A 97 ? 1.0613 1.1329 0.7425 0.0033 0.0660 -0.0497 97 ASP A OD1 759 O OD2 . ASP A 97 ? 1.0936 1.1482 0.7449 -0.0089 0.0791 -0.0441 97 ASP A OD2 760 N N . TYR A 98 ? 0.8530 0.9701 0.6123 -0.0120 0.0657 -0.0900 98 TYR A N 761 C CA . TYR A 98 ? 0.8453 0.9670 0.6204 -0.0114 0.0669 -0.0986 98 TYR A CA 762 C C . TYR A 98 ? 0.8328 0.9450 0.6203 -0.0121 0.0645 -0.0950 98 TYR A C 763 O O . TYR A 98 ? 0.8323 0.9506 0.6292 -0.0145 0.0683 -0.0962 98 TYR A O 764 C CB . TYR A 98 ? 0.8446 0.9666 0.6200 -0.0070 0.0631 -0.1092 98 TYR A CB 765 C CG . TYR A 98 ? 0.8561 0.9782 0.6396 -0.0018 0.0650 -0.1188 98 TYR A CG 766 C CD1 . TYR A 98 ? 0.8672 1.0051 0.6550 0.0005 0.0718 -0.1212 98 TYR A CD1 767 C CD2 . TYR A 98 ? 0.8519 0.9592 0.6356 0.0014 0.0602 -0.1257 98 TYR A CD2 768 C CE1 . TYR A 98 ? 0.8660 1.0073 0.6586 0.0100 0.0735 -0.1297 98 TYR A CE1 769 C CE2 . TYR A 98 ? 0.8577 0.9600 0.6426 0.0099 0.0622 -0.1340 98 TYR A CE2 770 C CZ . TYR A 98 ? 0.8741 0.9948 0.6638 0.0161 0.0688 -0.1359 98 TYR A CZ 771 O OH . TYR A 98 ? 0.9043 1.0237 0.6930 0.0289 0.0710 -0.1439 98 TYR A OH 772 N N . GLU A 99 ? 0.8170 0.9180 0.6040 -0.0101 0.0583 -0.0904 99 GLU A N 773 C CA . GLU A 99 ? 0.8147 0.9058 0.6129 -0.0100 0.0554 -0.0875 99 GLU A CA 774 C C . GLU A 99 ? 0.8199 0.9032 0.6130 -0.0156 0.0600 -0.0789 99 GLU A C 775 O O . GLU A 99 ? 0.8072 0.8898 0.6115 -0.0190 0.0613 -0.0794 99 GLU A O 776 C CB . GLU A 99 ? 0.8177 0.9024 0.6148 -0.0064 0.0479 -0.0844 99 GLU A CB 777 C CG . GLU A 99 ? 0.8144 0.9039 0.6145 -0.0060 0.0431 -0.0936 99 GLU A CG 778 C CD . GLU A 99 ? 0.8493 0.9492 0.6365 -0.0071 0.0438 -0.0976 99 GLU A CD 779 O OE1 . GLU A 99 ? 0.8653 0.9709 0.6415 -0.0059 0.0463 -0.0914 99 GLU A OE1 780 O OE2 . GLU A 99 ? 0.8709 0.9705 0.6558 -0.0094 0.0422 -0.1071 99 GLU A OE2 781 N N . GLU A 100 ? 0.8308 0.9066 0.6036 -0.0174 0.0630 -0.0712 100 GLU A N 782 C CA . GLU A 100 ? 0.8405 0.9016 0.5993 -0.0258 0.0687 -0.0632 100 GLU A CA 783 C C . GLU A 100 ? 0.8538 0.9317 0.6204 -0.0369 0.0755 -0.0682 100 GLU A C 784 O O . GLU A 100 ? 0.8762 0.9482 0.6402 -0.0474 0.0793 -0.0649 100 GLU A O 785 C CB . GLU A 100 ? 0.8581 0.9035 0.5870 -0.0243 0.0713 -0.0544 100 GLU A CB 786 C CG . GLU A 100 ? 0.8771 0.9039 0.5921 -0.0125 0.0660 -0.0463 100 GLU A CG 787 C CD . GLU A 100 ? 0.8916 0.8924 0.5991 -0.0147 0.0663 -0.0397 100 GLU A CD 788 O OE1 . GLU A 100 ? 0.9217 0.9042 0.6127 -0.0270 0.0732 -0.0358 100 GLU A OE1 789 O OE2 . GLU A 100 ? 0.8775 0.8764 0.5940 -0.0056 0.0600 -0.0387 100 GLU A OE2 790 N N . LEU A 101 ? 0.8449 0.9458 0.6198 -0.0347 0.0774 -0.0765 101 LEU A N 791 C CA . LEU A 101 ? 0.8506 0.9759 0.6342 -0.0421 0.0837 -0.0818 101 LEU A CA 792 C C . LEU A 101 ? 0.8292 0.9660 0.6353 -0.0381 0.0812 -0.0876 101 LEU A C 793 O O . LEU A 101 ? 0.8092 0.9604 0.6210 -0.0472 0.0853 -0.0876 101 LEU A O 794 C CB . LEU A 101 ? 0.8554 1.0021 0.6388 -0.0376 0.0866 -0.0891 101 LEU A CB 795 C CG . LEU A 101 ? 0.8538 1.0336 0.6455 -0.0422 0.0935 -0.0951 101 LEU A CG 796 C CD1 . LEU A 101 ? 0.8628 1.0475 0.6426 -0.0616 0.1007 -0.0884 101 LEU A CD1 797 C CD2 . LEU A 101 ? 0.8766 1.0724 0.6647 -0.0344 0.0957 -0.1020 101 LEU A CD2 798 N N . LYS A 102 ? 0.8253 0.9563 0.6416 -0.0257 0.0747 -0.0927 102 LYS A N 799 C CA . LYS A 102 ? 0.8262 0.9623 0.6600 -0.0199 0.0720 -0.0976 102 LYS A CA 800 C C . LYS A 102 ? 0.8188 0.9452 0.6562 -0.0282 0.0712 -0.0906 102 LYS A C 801 O O . LYS A 102 ? 0.8053 0.9465 0.6553 -0.0296 0.0725 -0.0932 102 LYS A O 802 C CB . LYS A 102 ? 0.8437 0.9655 0.6806 -0.0086 0.0652 -0.1027 102 LYS A CB 803 C CG . LYS A 102 ? 0.8935 1.0220 0.7245 -0.0005 0.0665 -0.1117 102 LYS A CG 804 C CD . LYS A 102 ? 0.9306 1.0389 0.7563 0.0048 0.0601 -0.1164 102 LYS A CD 805 C CE . LYS A 102 ? 0.9548 1.0554 0.7846 0.0149 0.0586 -0.1241 102 LYS A CE 806 N NZ . LYS A 102 ? 0.9831 1.0607 0.7997 0.0163 0.0540 -0.1299 102 LYS A NZ 807 N N . HIS A 103 ? 0.8273 0.9291 0.6512 -0.0327 0.0693 -0.0819 103 HIS A N 808 C CA . HIS A 103 ? 0.8232 0.9095 0.6443 -0.0404 0.0691 -0.0750 103 HIS A CA 809 C C . HIS A 103 ? 0.8457 0.9435 0.6600 -0.0571 0.0770 -0.0733 103 HIS A C 810 O O . HIS A 103 ? 0.8479 0.9472 0.6674 -0.0653 0.0778 -0.0722 103 HIS A O 811 C CB . HIS A 103 ? 0.8248 0.8806 0.6258 -0.0385 0.0665 -0.0656 103 HIS A CB 812 C CG . HIS A 103 ? 0.8158 0.8492 0.6077 -0.0453 0.0669 -0.0585 103 HIS A CG 813 N ND1 . HIS A 103 ? 0.7993 0.8257 0.6042 -0.0395 0.0612 -0.0584 103 HIS A ND1 814 C CD2 . HIS A 103 ? 0.8281 0.8426 0.5964 -0.0589 0.0728 -0.0518 103 HIS A CD2 815 C CE1 . HIS A 103 ? 0.8036 0.8083 0.5944 -0.0477 0.0632 -0.0520 103 HIS A CE1 816 N NE2 . HIS A 103 ? 0.8375 0.8325 0.6043 -0.0603 0.0704 -0.0480 103 HIS A NE2 817 N N . LEU A 104 ? 0.8763 0.9833 0.6775 -0.0639 0.0828 -0.0730 104 LEU A N 818 C CA . LEU A 104 ? 0.9215 1.0439 0.7133 -0.0832 0.0911 -0.0721 104 LEU A CA 819 C C . LEU A 104 ? 0.9135 1.0798 0.7298 -0.0843 0.0929 -0.0805 104 LEU A C 820 O O . LEU A 104 ? 0.9192 1.1007 0.7339 -0.1015 0.0975 -0.0798 104 LEU A O 821 C CB . LEU A 104 ? 0.9571 1.0847 0.7320 -0.0873 0.0965 -0.0714 104 LEU A CB 822 C CG . LEU A 104 ? 0.9971 1.1086 0.7407 -0.1090 0.1044 -0.0640 104 LEU A CG 823 C CD1 . LEU A 104 ? 1.0282 1.0878 0.7445 -0.1104 0.1026 -0.0537 104 LEU A CD1 824 C CD2 . LEU A 104 ? 1.0169 1.1367 0.7479 -0.1087 0.1086 -0.0645 104 LEU A CD2 825 N N . LEU A 105 ? 0.9082 1.0936 0.7432 -0.0655 0.0895 -0.0886 105 LEU A N 826 C CA . LEU A 105 ? 0.8929 1.1185 0.7485 -0.0579 0.0905 -0.0970 105 LEU A CA 827 C C . LEU A 105 ? 0.8876 1.1139 0.7571 -0.0571 0.0868 -0.0970 105 LEU A C 828 O O . LEU A 105 ? 0.9341 1.1982 0.8175 -0.0552 0.0888 -0.1021 105 LEU A O 829 C CB . LEU A 105 ? 0.8853 1.1145 0.7487 -0.0347 0.0870 -0.1050 105 LEU A CB 830 C CG . LEU A 105 ? 0.8965 1.1504 0.7555 -0.0286 0.0918 -0.1109 105 LEU A CG 831 C CD1 . LEU A 105 ? 0.9029 1.1490 0.7648 -0.0052 0.0877 -0.1190 105 LEU A CD1 832 C CD2 . LEU A 105 ? 0.9219 1.2264 0.7882 -0.0354 0.0987 -0.1141 105 LEU A CD2 833 N N . SER A 106 ? 1.0674 1.3507 0.6554 0.0232 0.0882 -0.1258 106 SER A N 834 C CA A SER A 106 ? 1.0971 1.3805 0.6577 0.0226 0.0858 -0.1271 106 SER A CA 835 C CA B SER A 106 ? 1.0958 1.3803 0.6572 0.0226 0.0853 -0.1270 106 SER A CA 836 C C . SER A 106 ? 1.1306 1.4128 0.6683 0.0041 0.0816 -0.1432 106 SER A C 837 O O . SER A 106 ? 1.1672 1.4530 0.6785 0.0000 0.0752 -0.1470 106 SER A O 838 C CB A SER A 106 ? 1.1038 1.3582 0.6482 0.0321 0.1009 -0.1213 106 SER A CB 839 C CB B SER A 106 ? 1.1005 1.3580 0.6476 0.0333 0.0996 -0.1198 106 SER A CB 840 O OG A SER A 106 ? 1.1078 1.3318 0.6361 0.0244 0.1142 -0.1317 106 SER A OG 841 O OG B SER A 106 ? 1.0556 1.3154 0.6297 0.0478 0.1011 -0.1046 106 SER A OG 842 N N . ARG A 107 ? 1.1667 1.4420 0.7129 -0.0077 0.0848 -0.1522 107 ARG A N 843 C CA . ARG A 107 ? 1.2491 1.5228 0.7795 -0.0277 0.0798 -0.1675 107 ARG A CA 844 C C . ARG A 107 ? 1.1956 1.5040 0.7542 -0.0375 0.0676 -0.1687 107 ARG A C 845 O O . ARG A 107 ? 1.2104 1.5188 0.7668 -0.0558 0.0645 -0.1796 107 ARG A O 846 C CB . ARG A 107 ? 1.3391 1.5748 0.8582 -0.0356 0.0946 -0.1764 107 ARG A CB 847 C CG . ARG A 107 ? 1.4295 1.6292 0.9247 -0.0259 0.1104 -0.1760 107 ARG A CG 848 C CD . ARG A 107 ? 1.5156 1.6853 1.0211 -0.0256 0.1254 -0.1758 107 ARG A CD 849 N NE . ARG A 107 ? 1.6163 1.7495 1.1027 -0.0173 0.1429 -0.1766 107 ARG A NE 850 C CZ . ARG A 107 ? 1.6233 1.7304 1.1221 -0.0116 0.1569 -0.1716 107 ARG A CZ 851 N NH1 . ARG A 107 ? 1.5823 1.6938 1.1079 -0.0141 0.1544 -0.1654 107 ARG A NH1 852 N NH2 . ARG A 107 ? 1.5880 1.6647 1.0723 -0.0028 0.1740 -0.1720 107 ARG A NH2 853 N N . ILE A 108 ? 1.1260 1.4627 0.7123 -0.0254 0.0618 -0.1574 108 ILE A N 854 C CA . ILE A 108 ? 1.0759 1.4472 0.6931 -0.0308 0.0538 -0.1569 108 ILE A CA 855 C C . ILE A 108 ? 1.0587 1.4672 0.6910 -0.0225 0.0387 -0.1487 108 ILE A C 856 O O . ILE A 108 ? 1.0464 1.4554 0.6814 -0.0053 0.0385 -0.1381 108 ILE A O 857 C CB . ILE A 108 ? 1.0360 1.4036 0.6761 -0.0230 0.0645 -0.1518 108 ILE A CB 858 C CG1 . ILE A 108 ? 1.0358 1.3705 0.6645 -0.0331 0.0772 -0.1580 108 ILE A CG1 859 C CG2 . ILE A 108 ? 1.0064 1.4109 0.6783 -0.0250 0.0595 -0.1502 108 ILE A CG2 860 C CD1 . ILE A 108 ? 1.0128 1.3370 0.6550 -0.0253 0.0868 -0.1518 108 ILE A CD1 861 N N . ASN A 109 ? 1.0614 1.5015 0.7070 -0.0350 0.0256 -0.1523 109 ASN A N 862 C CA . ASN A 109 ? 1.0538 1.5335 0.7203 -0.0277 0.0098 -0.1430 109 ASN A CA 863 C C . ASN A 109 ? 1.0324 1.5466 0.7439 -0.0236 0.0099 -0.1384 109 ASN A C 864 O O . ASN A 109 ? 1.0019 1.5467 0.7373 -0.0120 0.0002 -0.1285 109 ASN A O 865 C CB . ASN A 109 ? 1.0935 1.5891 0.7448 -0.0441 -0.0085 -0.1482 109 ASN A CB 866 C CG . ASN A 109 ? 1.1316 1.5961 0.7342 -0.0454 -0.0093 -0.1522 109 ASN A CG 867 O OD1 . ASN A 109 ? 1.1194 1.5800 0.7102 -0.0297 -0.0101 -0.1419 109 ASN A OD1 868 N ND2 . ASN A 109 ? 1.1750 1.6155 0.7485 -0.0640 -0.0080 -0.1670 109 ASN A ND2 869 N N . HIS A 110 ? 1.0282 1.5378 0.7516 -0.0326 0.0216 -0.1446 110 HIS A N 870 C CA . HIS A 110 ? 1.0216 1.5642 0.7856 -0.0293 0.0248 -0.1409 110 HIS A CA 871 C C . HIS A 110 ? 1.0145 1.5399 0.7824 -0.0314 0.0434 -0.1447 110 HIS A C 872 O O . HIS A 110 ? 1.0036 1.5070 0.7553 -0.0472 0.0499 -0.1521 110 HIS A O 873 C CB . HIS A 110 ? 1.0567 1.6396 0.8445 -0.0454 0.0109 -0.1421 110 HIS A CB 874 C CG . HIS A 110 ? 1.0495 1.6751 0.8853 -0.0377 0.0127 -0.1350 110 HIS A CG 875 N ND1 . HIS A 110 ? 1.0544 1.7167 0.9225 -0.0533 0.0080 -0.1356 110 HIS A ND1 876 C CD2 . HIS A 110 ? 1.0324 1.6689 0.8906 -0.0156 0.0198 -0.1273 110 HIS A CD2 877 C CE1 . HIS A 110 ? 1.0415 1.7374 0.9511 -0.0399 0.0138 -0.1279 110 HIS A CE1 878 N NE2 . HIS A 110 ? 1.0239 1.7030 0.9264 -0.0167 0.0212 -0.1237 110 HIS A NE2 879 N N . PHE A 111 ? 1.0103 1.5441 0.7980 -0.0150 0.0518 -0.1392 111 PHE A N 880 C CA . PHE A 111 ? 1.0216 1.5443 0.8132 -0.0155 0.0686 -0.1415 111 PHE A CA 881 C C . PHE A 111 ? 1.0287 1.5931 0.8585 -0.0152 0.0723 -0.1394 111 PHE A C 882 O O . PHE A 111 ? 1.0321 1.6281 0.8874 -0.0049 0.0635 -0.1340 111 PHE A O 883 C CB . PHE A 111 ? 1.0012 1.4975 0.7820 0.0035 0.0763 -0.1381 111 PHE A CB 884 C CG . PHE A 111 ? 0.9957 1.4483 0.7438 0.0022 0.0791 -0.1392 111 PHE A CG 885 C CD1 . PHE A 111 ? 1.0005 1.4314 0.7314 -0.0141 0.0852 -0.1443 111 PHE A CD1 886 C CD2 . PHE A 111 ? 0.9700 1.4032 0.7087 0.0180 0.0765 -0.1338 111 PHE A CD2 887 C CE1 . PHE A 111 ? 0.9917 1.3840 0.6978 -0.0131 0.0888 -0.1439 111 PHE A CE1 888 C CE2 . PHE A 111 ? 0.9603 1.3572 0.6756 0.0177 0.0798 -0.1329 111 PHE A CE2 889 C CZ . PHE A 111 ? 0.9771 1.3540 0.6767 0.0028 0.0862 -0.1379 111 PHE A CZ 890 N N . GLU A 112 ? 1.0505 1.6150 0.8855 -0.0258 0.0862 -0.1424 112 GLU A N 891 C CA . GLU A 112 ? 1.0674 1.6696 0.9389 -0.0244 0.0955 -0.1398 112 GLU A CA 892 C C . GLU A 112 ? 1.0335 1.6138 0.8925 -0.0177 0.1159 -0.1411 112 GLU A C 893 O O . GLU A 112 ? 1.0126 1.5687 0.8513 -0.0311 0.1244 -0.1435 112 GLU A O 894 C CB . GLU A 112 ? 1.1102 1.7397 1.0025 -0.0482 0.0920 -0.1408 112 GLU A CB 895 C CG . GLU A 112 ? 1.1428 1.8277 1.0855 -0.0467 0.0902 -0.1349 112 GLU A CG 896 C CD . GLU A 112 ? 1.2057 1.9081 1.1714 -0.0523 0.1115 -0.1334 112 GLU A CD 897 O OE1 . GLU A 112 ? 1.2650 1.9518 1.2204 -0.0378 0.1301 -0.1338 112 GLU A OE1 898 O OE2 . GLU A 112 ? 1.2361 1.9672 1.2287 -0.0722 0.1095 -0.1316 112 GLU A OE2 899 N N . LYS A 113 ? 1.0078 1.5931 0.8759 0.0030 0.1227 -0.1394 113 LYS A N 900 C CA . LYS A 113 ? 1.0173 1.5775 0.8662 0.0109 0.1401 -0.1418 113 LYS A CA 901 C C . LYS A 113 ? 1.0156 1.5954 0.8784 0.0006 0.1584 -0.1417 113 LYS A C 902 O O . LYS A 113 ? 1.0016 1.6242 0.9031 0.0003 0.1619 -0.1390 113 LYS A O 903 C CB . LYS A 113 ? 1.0142 1.5732 0.8687 0.0357 0.1420 -0.1419 113 LYS A CB 904 C CG . LYS A 113 ? 1.0346 1.5647 0.8642 0.0443 0.1576 -0.1461 113 LYS A CG 905 C CD . LYS A 113 ? 1.0404 1.5367 0.8489 0.0603 0.1491 -0.1473 113 LYS A CD 906 C CE . LYS A 113 ? 1.0328 1.5474 0.8683 0.0800 0.1433 -0.1457 113 LYS A CE 907 N NZ . LYS A 113 ? 1.0389 1.5222 0.8579 0.0904 0.1300 -0.1441 113 LYS A NZ 908 N N . ILE A 114 ? 1.0230 1.5732 0.8565 -0.0082 0.1700 -0.1430 114 ILE A N 909 C CA . ILE A 114 ? 1.0573 1.6221 0.8988 -0.0158 0.1908 -0.1415 114 ILE A CA 910 C C . ILE A 114 ? 1.0870 1.6166 0.8908 -0.0097 0.2054 -0.1430 114 ILE A C 911 O O . ILE A 114 ? 1.1213 1.6103 0.8901 -0.0086 0.1976 -0.1440 114 ILE A O 912 C CB . ILE A 114 ? 1.0695 1.6439 0.9202 -0.0421 0.1916 -0.1384 114 ILE A CB 913 C CG1 . ILE A 114 ? 1.0886 1.6173 0.9012 -0.0544 0.1852 -0.1391 114 ILE A CG1 914 C CG2 . ILE A 114 ? 1.0517 1.6659 0.9417 -0.0505 0.1769 -0.1372 114 ILE A CG2 915 C CD1 . ILE A 114 ? 1.1176 1.6439 0.9302 -0.0776 0.1951 -0.1354 114 ILE A CD1 916 N N . GLN A 115 ? 1.0827 1.6295 0.8944 -0.0060 0.2269 -0.1426 115 GLN A N 917 C CA . GLN A 115 ? 1.0871 1.6037 0.8601 -0.0003 0.2426 -0.1444 115 GLN A CA 918 C C . GLN A 115 ? 1.0821 1.5797 0.8320 -0.0213 0.2492 -0.1386 115 GLN A C 919 O O . GLN A 115 ? 1.0690 1.5927 0.8429 -0.0370 0.2584 -0.1334 115 GLN A O 920 C CB . GLN A 115 ? 1.0920 1.6349 0.8812 0.0125 0.2660 -0.1465 115 GLN A CB 921 C CG . GLN A 115 ? 1.1237 1.6321 0.8662 0.0219 0.2812 -0.1511 115 GLN A CG 922 C CD . GLN A 115 ? 1.1343 1.6670 0.8891 0.0337 0.3091 -0.1539 115 GLN A CD 923 O OE1 . GLN A 115 ? 1.1379 1.6608 0.8833 0.0545 0.3147 -0.1624 115 GLN A OE1 924 N NE2 . GLN A 115 ? 1.1362 1.6997 0.9131 0.0207 0.3279 -0.1465 115 GLN A NE2 925 N N . ILE A 116 ? 1.0833 1.5360 0.7893 -0.0219 0.2439 -0.1382 116 ILE A N 926 C CA . ILE A 116 ? 1.1095 1.5401 0.7922 -0.0405 0.2491 -0.1307 116 ILE A CA 927 C C . ILE A 116 ? 1.1648 1.5732 0.8076 -0.0372 0.2658 -0.1287 116 ILE A C 928 O O . ILE A 116 ? 1.2054 1.6143 0.8403 -0.0514 0.2807 -0.1209 116 ILE A O 929 C CB . ILE A 116 ? 1.0860 1.4827 0.7524 -0.0481 0.2291 -0.1283 116 ILE A CB 930 C CG1 . ILE A 116 ? 1.0665 1.4362 0.7121 -0.0311 0.2144 -0.1326 116 ILE A CG1 931 C CG2 . ILE A 116 ? 1.0562 1.4728 0.7552 -0.0589 0.2176 -0.1293 116 ILE A CG2 932 C CD1 . ILE A 116 ? 1.0694 1.4009 0.6925 -0.0369 0.2007 -0.1276 116 ILE A CD1 933 N N . ILE A 117 ? 1.1930 1.5810 0.8094 -0.0195 0.2632 -0.1354 117 ILE A N 934 C CA . ILE A 117 ? 1.2410 1.6081 0.8150 -0.0148 0.2788 -0.1360 117 ILE A CA 935 C C . ILE A 117 ? 1.2470 1.6259 0.8234 0.0060 0.2900 -0.1473 117 ILE A C 936 O O . ILE A 117 ? 1.2244 1.5816 0.7861 0.0203 0.2766 -0.1551 117 ILE A O 937 C CB . ILE A 117 ? 1.2644 1.5825 0.7909 -0.0158 0.2630 -0.1332 117 ILE A CB 938 C CG1 . ILE A 117 ? 1.2497 1.5548 0.7794 -0.0337 0.2514 -0.1221 117 ILE A CG1 939 C CG2 . ILE A 117 ? 1.3222 1.6182 0.7993 -0.0145 0.2783 -0.1327 117 ILE A CG2 940 C CD1 . ILE A 117 ? 1.2714 1.5320 0.7604 -0.0357 0.2369 -0.1157 117 ILE A CD1 941 N N . PRO A 118 ? 1.2769 1.6895 0.8735 0.0080 0.3157 -0.1476 118 PRO A N 942 C CA . PRO A 118 ? 1.2879 1.7145 0.8931 0.0295 0.3300 -0.1583 118 PRO A CA 943 C C . PRO A 118 ? 1.3309 1.7133 0.8798 0.0427 0.3303 -0.1683 118 PRO A C 944 O O . PRO A 118 ? 1.3613 1.7112 0.8604 0.0338 0.3317 -0.1649 118 PRO A O 945 C CB . PRO A 118 ? 1.3045 1.7677 0.9304 0.0254 0.3618 -0.1536 118 PRO A CB 946 C CG . PRO A 118 ? 1.2865 1.7665 0.9344 0.0011 0.3587 -0.1404 118 PRO A CG 947 C CD . PRO A 118 ? 1.2932 1.7306 0.9059 -0.0097 0.3343 -0.1370 118 PRO A CD 948 N N . LYS A 119 ? 1.3408 1.7213 0.8979 0.0631 0.3275 -0.1800 119 LYS A N 949 C CA . LYS A 119 ? 1.3969 1.7339 0.9032 0.0758 0.3252 -0.1918 119 LYS A CA 950 C C . LYS A 119 ? 1.4662 1.7944 0.9315 0.0780 0.3555 -0.1961 119 LYS A C 951 O O . LYS A 119 ? 1.5098 1.7961 0.9140 0.0749 0.3529 -0.1993 119 LYS A O 952 C CB . LYS A 119 ? 1.3951 1.7355 0.9270 0.0975 0.3190 -0.2030 119 LYS A CB 953 C CG . LYS A 119 ? 1.4374 1.7280 0.9248 0.1074 0.3038 -0.2145 119 LYS A CG 954 C CD . LYS A 119 ? 1.4439 1.7400 0.9665 0.1263 0.2941 -0.2220 119 LYS A CD 955 C CE . LYS A 119 ? 1.4988 1.7455 0.9789 0.1379 0.2846 -0.2361 119 LYS A CE 956 N NZ . LYS A 119 ? 1.4968 1.7460 1.0128 0.1556 0.2742 -0.2416 119 LYS A NZ 957 N N . SER A 120 ? 1.4715 1.8407 0.9712 0.0827 0.3840 -0.1950 120 SER A N 958 C CA . SER A 120 ? 1.5251 1.8927 0.9918 0.0857 0.4184 -0.1978 120 SER A CA 959 C C . SER A 120 ? 1.5527 1.8990 0.9709 0.0650 0.4219 -0.1866 120 SER A C 960 O O . SER A 120 ? 1.6326 1.9533 0.9944 0.0674 0.4403 -0.1911 120 SER A O 961 C CB . SER A 120 ? 1.5076 1.9319 1.0336 0.0911 0.4478 -0.1935 120 SER A CB 962 O OG . SER A 120 ? 1.4714 1.9307 1.0377 0.0700 0.4448 -0.1767 120 SER A OG 963 N N . SER A 121 ? 1.5143 1.8687 0.9520 0.0450 0.4043 -0.1719 121 SER A N 964 C CA . SER A 121 ? 1.5268 1.8670 0.9295 0.0246 0.4097 -0.1578 121 SER A CA 965 C C . SER A 121 ? 1.5565 1.8403 0.8861 0.0206 0.3927 -0.1584 121 SER A C 966 O O . SER A 121 ? 1.5518 1.8209 0.8493 0.0045 0.3958 -0.1451 121 SER A O 967 C CB . SER A 121 ? 1.4738 1.8374 0.9222 0.0049 0.3963 -0.1429 121 SER A CB 968 O OG . SER A 121 ? 1.4335 1.7769 0.8866 0.0034 0.3620 -0.1440 121 SER A OG 969 N N . TRP A 122 ? 1.5611 1.8140 0.8663 0.0342 0.3739 -0.1722 122 TRP A N 970 C CA . TRP A 122 ? 1.5960 1.7966 0.8332 0.0306 0.3557 -0.1733 122 TRP A CA 971 C C . TRP A 122 ? 1.6747 1.8510 0.8486 0.0396 0.3785 -0.1846 122 TRP A C 972 O O . TRP A 122 ? 1.7058 1.8557 0.8525 0.0542 0.3723 -0.2019 122 TRP A O 973 C CB . TRP A 122 ? 1.5634 1.7411 0.8061 0.0386 0.3223 -0.1818 122 TRP A CB 974 C CG . TRP A 122 ? 1.5113 1.7028 0.8024 0.0298 0.2979 -0.1709 122 TRP A CG 975 C CD1 . TRP A 122 ? 1.4501 1.6676 0.7978 0.0375 0.2890 -0.1746 122 TRP A CD1 976 C CD2 . TRP A 122 ? 1.4949 1.6722 0.7789 0.0125 0.2796 -0.1547 122 TRP A CD2 977 N NE1 . TRP A 122 ? 1.4183 1.6377 0.7909 0.0258 0.2677 -0.1630 122 TRP A NE1 978 C CE2 . TRP A 122 ? 1.4358 1.6307 0.7723 0.0110 0.2622 -0.1510 122 TRP A CE2 979 C CE3 . TRP A 122 ? 1.5257 1.6763 0.7636 -0.0012 0.2767 -0.1422 122 TRP A CE3 980 C CZ2 . TRP A 122 ? 1.4131 1.5989 0.7583 -0.0027 0.2442 -0.1369 122 TRP A CZ2 981 C CZ3 . TRP A 122 ? 1.5064 1.6492 0.7567 -0.0148 0.2573 -0.1266 122 TRP A CZ3 982 C CH2 . TRP A 122 ? 1.4498 1.6095 0.7538 -0.0150 0.2422 -0.1249 122 TRP A CH2 983 N N . SER A 123 ? 1.7104 1.8935 0.8588 0.0303 0.4052 -0.1747 123 SER A N 984 C CA . SER A 123 ? 1.7913 1.9563 0.8796 0.0390 0.4341 -0.1848 123 SER A CA 985 C C . SER A 123 ? 1.8609 1.9687 0.8617 0.0339 0.4168 -0.1871 123 SER A C 986 O O . SER A 123 ? 1.9228 2.0031 0.8666 0.0452 0.4304 -0.2033 123 SER A O 987 C CB . SER A 123 ? 1.8048 2.0026 0.9023 0.0309 0.4724 -0.1714 123 SER A CB 988 O OG . SER A 123 ? 1.7790 1.9784 0.8785 0.0082 0.4624 -0.1486 123 SER A OG 989 N N . SER A 124 ? 1.8385 1.9283 0.8290 0.0173 0.3867 -0.1711 124 SER A N 990 C CA . SER A 124 ? 1.8834 1.9218 0.7973 0.0103 0.3642 -0.1695 124 SER A CA 991 C C . SER A 124 ? 1.8709 1.8783 0.7779 0.0177 0.3273 -0.1831 124 SER A C 992 O O . SER A 124 ? 1.9120 1.8773 0.7599 0.0119 0.3039 -0.1828 124 SER A O 993 C CB . SER A 124 ? 1.8725 1.9070 0.7821 -0.0107 0.3499 -0.1429 124 SER A CB 994 O OG . SER A 124 ? 1.8624 1.9298 0.7946 -0.0193 0.3813 -0.1285 124 SER A OG 995 N N . HIS A 125 ? 1.8189 1.8477 0.7874 0.0294 0.3209 -0.1934 125 HIS A N 996 C CA . HIS A 125 ? 1.8074 1.8107 0.7790 0.0362 0.2875 -0.2046 125 HIS A CA 997 C C . HIS A 125 ? 1.8130 1.8285 0.8157 0.0567 0.3001 -0.2257 125 HIS A C 998 O O . HIS A 125 ? 1.8130 1.8663 0.8544 0.0649 0.3301 -0.2279 125 HIS A O 999 C CB . HIS A 125 ? 1.7178 1.7337 0.7435 0.0272 0.2576 -0.1892 125 HIS A CB 1000 C CG . HIS A 125 ? 1.7108 1.7154 0.7166 0.0085 0.2434 -0.1669 125 HIS A CG 1001 N ND1 . HIS A 125 ? 1.6951 1.7256 0.7202 -0.0026 0.2616 -0.1499 125 HIS A ND1 1002 C CD2 . HIS A 125 ? 1.7281 1.6984 0.6998 -0.0008 0.2122 -0.1576 125 HIS A CD2 1003 C CE1 . HIS A 125 ? 1.7150 1.7254 0.7168 -0.0172 0.2433 -0.1314 125 HIS A CE1 1004 N NE2 . HIS A 125 ? 1.7328 1.7082 0.7031 -0.0161 0.2130 -0.1350 125 HIS A NE2 1005 N N . GLU A 126 ? 1.8277 1.8118 0.8176 0.0645 0.2758 -0.2396 126 GLU A N 1006 C CA . GLU A 126 ? 1.8103 1.8018 0.8340 0.0842 0.2828 -0.2580 126 GLU A CA 1007 C C . GLU A 126 ? 1.7308 1.7548 0.8329 0.0845 0.2655 -0.2480 126 GLU A C 1008 O O . GLU A 126 ? 1.7139 1.7259 0.8253 0.0749 0.2335 -0.2380 126 GLU A O 1009 C CB . GLU A 126 ? 1.8727 1.8125 0.8464 0.0912 0.2644 -0.2775 126 GLU A CB 1010 C CG . GLU A 126 ? 1.8756 1.8158 0.8792 0.1127 0.2726 -0.2975 126 GLU A CG 1011 C CD . GLU A 126 ? 1.8961 1.8641 0.9130 0.1286 0.3170 -0.3069 126 GLU A CD 1012 O OE1 . GLU A 126 ? 1.9226 1.8712 0.8789 0.1308 0.3418 -0.3167 126 GLU A OE1 1013 O OE2 . GLU A 126 ? 1.8447 1.8545 0.9332 0.1392 0.3268 -0.3038 126 GLU A OE2 1014 N N . ALA A 127 ? 1.6852 1.7511 0.8436 0.0957 0.2872 -0.2499 127 ALA A N 1015 C CA . ALA A 127 ? 1.5877 1.6893 0.8185 0.0952 0.2746 -0.2393 127 ALA A CA 1016 C C . ALA A 127 ? 1.5669 1.6807 0.8408 0.1150 0.2763 -0.2515 127 ALA A C 1017 O O . ALA A 127 ? 1.5208 1.6672 0.8541 0.1165 0.2688 -0.2434 127 ALA A O 1018 C CB . ALA A 127 ? 1.5473 1.6944 0.8141 0.0857 0.2940 -0.2246 127 ALA A CB 1019 N N . SER A 128 ? 1.6191 1.7043 0.8611 0.1301 0.2852 -0.2706 128 SER A N 1020 C CA . SER A 128 ? 1.6002 1.6939 0.8811 0.1513 0.2908 -0.2826 128 SER A CA 1021 C C . SER A 128 ? 1.6097 1.6535 0.8620 0.1592 0.2693 -0.2978 128 SER A C 1022 O O . SER A 128 ? 1.5986 1.6387 0.8722 0.1780 0.2756 -0.3102 128 SER A O 1023 C CB . SER A 128 ? 1.6455 1.7593 0.9290 0.1664 0.3312 -0.2927 128 SER A CB 1024 O OG . SER A 128 ? 1.6215 1.7865 0.9440 0.1586 0.3490 -0.2773 128 SER A OG 1025 N N . LEU A 129 ? 1.6156 1.6213 0.8229 0.1446 0.2430 -0.2956 129 LEU A N 1026 C CA . LEU A 129 ? 1.6398 1.5982 0.8227 0.1478 0.2176 -0.3076 129 LEU A CA 1027 C C . LEU A 129 ? 1.5953 1.5510 0.8005 0.1336 0.1810 -0.2911 129 LEU A C 1028 O O . LEU A 129 ? 1.6389 1.5540 0.8127 0.1269 0.1548 -0.2948 129 LEU A O 1029 C CB . LEU A 129 ? 1.7316 1.6403 0.8310 0.1437 0.2193 -0.3228 129 LEU A CB 1030 C CG . LEU A 129 ? 1.7899 1.6967 0.8525 0.1557 0.2593 -0.3386 129 LEU A CG 1031 C CD1 . LEU A 129 ? 1.8649 1.7157 0.8363 0.1494 0.2549 -0.3535 129 LEU A CD1 1032 C CD2 . LEU A 129 ? 1.7951 1.7107 0.8947 0.1805 0.2803 -0.3540 129 LEU A CD2 1033 N N . GLY A 130 ? 1.5250 1.5240 0.7850 0.1289 0.1799 -0.2731 130 GLY A N 1034 C CA . GLY A 130 ? 1.4695 1.4712 0.7565 0.1172 0.1503 -0.2563 130 GLY A CA 1035 C C . GLY A 130 ? 1.4263 1.4377 0.7662 0.1281 0.1384 -0.2552 130 GLY A C 1036 O O . GLY A 130 ? 1.3443 1.3906 0.7334 0.1268 0.1360 -0.2414 130 GLY A O 1037 N N . VAL A 131 ? 1.4545 1.4316 0.7806 0.1380 0.1299 -0.2696 131 VAL A N 1038 C CA . VAL A 131 ? 1.4204 1.4013 0.7926 0.1505 0.1210 -0.2698 131 VAL A CA 1039 C C . VAL A 131 ? 1.4390 1.3773 0.7989 0.1456 0.0903 -0.2714 131 VAL A C 1040 O O . VAL A 131 ? 1.4907 1.3943 0.8026 0.1341 0.0766 -0.2758 131 VAL A O 1041 C CB . VAL A 131 ? 1.4468 1.4301 0.8270 0.1717 0.1453 -0.2866 131 VAL A CB 1042 C CG1 . VAL A 131 ? 1.4278 1.4565 0.8253 0.1762 0.1759 -0.2838 131 VAL A CG1 1043 C CG2 . VAL A 131 ? 1.5159 1.4474 0.8374 0.1765 0.1481 -0.3091 131 VAL A CG2 1044 N N . SER A 132 ? 1.4144 1.3563 0.8188 0.1539 0.0794 -0.2670 132 SER A N 1045 C CA . SER A 132 ? 1.4210 1.3269 0.8257 0.1492 0.0504 -0.2659 132 SER A CA 1046 C C . SER A 132 ? 1.4195 1.3244 0.8669 0.1647 0.0484 -0.2673 132 SER A C 1047 O O . SER A 132 ? 1.3947 1.3367 0.8838 0.1762 0.0633 -0.2609 132 SER A O 1048 C CB . SER A 132 ? 1.3652 1.2825 0.7883 0.1328 0.0286 -0.2440 132 SER A CB 1049 O OG . SER A 132 ? 1.3489 1.2442 0.7927 0.1304 0.0033 -0.2382 132 SER A OG 1050 N N . SER A 133 ? 1.4571 1.3191 0.8949 0.1636 0.0280 -0.2742 133 SER A N 1051 C CA . SER A 133 ? 1.4631 1.3169 0.9403 0.1766 0.0228 -0.2739 133 SER A CA 1052 C C . SER A 133 ? 1.4146 1.2996 0.9474 0.1732 0.0103 -0.2484 133 SER A C 1053 O O . SER A 133 ? 1.3986 1.2900 0.9710 0.1852 0.0105 -0.2430 133 SER A O 1054 C CB . SER A 133 ? 1.5203 1.3157 0.9697 0.1735 0.0028 -0.2885 133 SER A CB 1055 O OG . SER A 133 ? 1.5305 1.3079 0.9595 0.1524 -0.0237 -0.2805 133 SER A OG 1056 N N . ALA A 134 ? 1.4016 1.3047 0.9361 0.1575 0.0004 -0.2324 134 ALA A N 1057 C CA . ALA A 134 ? 1.3625 1.2964 0.9446 0.1544 -0.0072 -0.2088 134 ALA A CA 1058 C C . ALA A 134 ? 1.3227 1.3048 0.9356 0.1647 0.0134 -0.2016 134 ALA A C 1059 O O . ALA A 134 ? 1.2705 1.2745 0.9234 0.1682 0.0099 -0.1857 134 ALA A O 1060 C CB . ALA A 134 ? 1.3508 1.2872 0.9250 0.1360 -0.0219 -0.1950 134 ALA A CB 1061 N N . CYS A 135 ? 1.3373 1.3359 0.9311 0.1688 0.0345 -0.2125 135 CYS A N 1062 C CA . CYS A 135 ? 1.3037 1.3486 0.9268 0.1774 0.0532 -0.2070 135 CYS A CA 1063 C C . CYS A 135 ? 1.2947 1.3425 0.9220 0.1960 0.0724 -0.2217 135 CYS A C 1064 O O . CYS A 135 ? 1.2903 1.3539 0.9026 0.1983 0.0925 -0.2307 135 CYS A O 1065 C CB . CYS A 135 ? 1.3130 1.3828 0.9201 0.1651 0.0631 -0.2035 135 CYS A CB 1066 S SG . CYS A 135 ? 1.3356 1.4025 0.9401 0.1454 0.0438 -0.1860 135 CYS A SG 1067 N N . PRO A 136 ? 1.2727 1.3057 0.9234 0.2100 0.0675 -0.2231 136 PRO A N 1068 C CA . PRO A 136 ? 1.2920 1.3221 0.9487 0.2299 0.0857 -0.2375 136 PRO A CA 1069 C C . PRO A 136 ? 1.2492 1.3315 0.9473 0.2416 0.1023 -0.2289 136 PRO A C 1070 O O . PRO A 136 ? 1.1893 1.3036 0.9187 0.2374 0.0941 -0.2105 136 PRO A O 1071 C CB . PRO A 136 ? 1.3115 1.3063 0.9837 0.2390 0.0710 -0.2381 136 PRO A CB 1072 C CG . PRO A 136 ? 1.2681 1.2745 0.9667 0.2281 0.0504 -0.2157 136 PRO A CG 1073 C CD . PRO A 136 ? 1.2531 1.2680 0.9259 0.2081 0.0454 -0.2110 136 PRO A CD 1074 N N . TYR A 137 ? 1.2765 1.3669 0.9740 0.2560 0.1254 -0.2422 137 TYR A N 1075 C CA . TYR A 137 ? 1.2562 1.3958 0.9987 0.2692 0.1404 -0.2343 137 TYR A CA 1076 C C . TYR A 137 ? 1.2894 1.4168 1.0440 0.2934 0.1581 -0.2480 137 TYR A C 1077 O O . TYR A 137 ? 1.3499 1.4579 1.0721 0.2983 0.1770 -0.2670 137 TYR A O 1078 C CB . TYR A 137 ? 1.2467 1.4260 0.9838 0.2591 0.1561 -0.2327 137 TYR A CB 1079 C CG . TYR A 137 ? 1.2263 1.4596 1.0129 0.2705 0.1695 -0.2238 137 TYR A CG 1080 C CD1 . TYR A 137 ? 1.1899 1.4563 1.0182 0.2699 0.1550 -0.2044 137 TYR A CD1 1081 C CD2 . TYR A 137 ? 1.2437 1.4959 1.0359 0.2816 0.1967 -0.2339 137 TYR A CD2 1082 C CE1 . TYR A 137 ? 1.1702 1.4869 1.0441 0.2791 0.1638 -0.1953 137 TYR A CE1 1083 C CE2 . TYR A 137 ? 1.2211 1.5259 1.0644 0.2914 0.2073 -0.2239 137 TYR A CE2 1084 C CZ . TYR A 137 ? 1.1795 1.5164 1.0635 0.2896 0.1891 -0.2046 137 TYR A CZ 1085 O OH . TYR A 137 ? 1.1603 1.5503 1.0951 0.2980 0.1962 -0.1939 137 TYR A OH 1086 N N . GLN A 138 ? 1.2677 1.4055 1.0681 0.3091 0.1528 -0.2378 138 GLN A N 1087 C CA . GLN A 138 ? 1.3023 1.4294 1.1231 0.3346 0.1691 -0.2482 138 GLN A CA 1088 C C . GLN A 138 ? 1.3660 1.4293 1.1388 0.3384 0.1736 -0.2730 138 GLN A C 1089 O O . GLN A 138 ? 1.4125 1.4654 1.1699 0.3518 0.1983 -0.2914 138 GLN A O 1090 C CB . GLN A 138 ? 1.2929 1.4683 1.1392 0.3460 0.1961 -0.2492 138 GLN A CB 1091 C CG . GLN A 138 ? 1.2380 1.4763 1.1277 0.3390 0.1893 -0.2260 138 GLN A CG 1092 C CD . GLN A 138 ? 1.2278 1.5173 1.1579 0.3525 0.2126 -0.2235 138 GLN A CD 1093 O OE1 . GLN A 138 ? 1.2422 1.5238 1.1660 0.3666 0.2383 -0.2393 138 GLN A OE1 1094 N NE2 . GLN A 138 ? 1.1870 1.5302 1.1593 0.3477 0.2036 -0.2032 138 GLN A NE2 1095 N N . GLY A 139 ? 1.3748 1.3957 1.1228 0.3255 0.1496 -0.2733 139 GLY A N 1096 C CA . GLY A 139 ? 1.4246 1.3799 1.1280 0.3267 0.1468 -0.2959 139 GLY A CA 1097 C C . GLY A 139 ? 1.4405 1.3718 1.0794 0.3104 0.1501 -0.3123 139 GLY A C 1098 O O . GLY A 139 ? 1.4719 1.3471 1.0676 0.3054 0.1403 -0.3290 139 GLY A O 1099 N N . LYS A 140 ? 1.4112 1.3837 1.0433 0.3010 0.1623 -0.3067 140 LYS A N 1100 C CA . LYS A 140 ? 1.4521 1.4080 1.0244 0.2878 0.1707 -0.3205 140 LYS A CA 1101 C C . LYS A 140 ? 1.4047 1.3767 0.9660 0.2626 0.1514 -0.3045 140 LYS A C 1102 O O . LYS A 140 ? 1.3502 1.3623 0.9532 0.2577 0.1428 -0.2837 140 LYS A O 1103 C CB . LYS A 140 ? 1.4692 1.4585 1.0422 0.2989 0.2058 -0.3276 140 LYS A CB 1104 C CG . LYS A 140 ? 1.5219 1.4985 1.1086 0.3265 0.2301 -0.3435 140 LYS A CG 1105 C CD . LYS A 140 ? 1.5128 1.5451 1.1352 0.3397 0.2618 -0.3391 140 LYS A CD 1106 C CE . LYS A 140 ? 1.5418 1.5714 1.1993 0.3702 0.2832 -0.3482 140 LYS A CE 1107 N NZ . LYS A 140 ? 1.6189 1.5880 1.2238 0.3824 0.2998 -0.3775 140 LYS A NZ 1108 N N . SER A 141 ? 1.4345 1.3743 0.9383 0.2471 0.1451 -0.3142 141 SER A N 1109 C CA . SER A 141 ? 1.3913 1.3418 0.8814 0.2238 0.1278 -0.2997 141 SER A CA 1110 C C . SER A 141 ? 1.3515 1.3551 0.8566 0.2189 0.1457 -0.2885 141 SER A C 1111 O O . SER A 141 ? 1.3682 1.3842 0.8585 0.2254 0.1721 -0.2981 141 SER A O 1112 C CB . SER A 141 ? 1.4422 1.3448 0.8658 0.2097 0.1171 -0.3127 141 SER A CB 1113 O OG . SER A 141 ? 1.4685 1.3210 0.8792 0.2107 0.0964 -0.3224 141 SER A OG 1114 N N . SER A 142 ? 1.3021 1.3360 0.8371 0.2072 0.1319 -0.2681 142 SER A N 1115 C CA . SER A 142 ? 1.2673 1.3499 0.8206 0.2006 0.1451 -0.2567 142 SER A CA 1116 C C . SER A 142 ? 1.2506 1.3347 0.7939 0.1793 0.1266 -0.2423 142 SER A C 1117 O O . SER A 142 ? 1.2663 1.3133 0.7799 0.1698 0.1080 -0.2436 142 SER A O 1118 C CB . SER A 142 ? 1.2296 1.3557 0.8427 0.2129 0.1505 -0.2461 142 SER A CB 1119 O OG . SER A 142 ? 1.2078 1.3803 0.8383 0.2084 0.1666 -0.2392 142 SER A OG 1120 N N . PHE A 143 ? 1.2168 1.3425 0.7857 0.1718 0.1314 -0.2288 143 PHE A N 1121 C CA . PHE A 143 ? 1.2000 1.3282 0.7624 0.1532 0.1172 -0.2152 143 PHE A CA 1122 C C . PHE A 143 ? 1.1587 1.3326 0.7587 0.1485 0.1215 -0.2017 143 PHE A C 1123 O O . PHE A 143 ? 1.1473 1.3544 0.7730 0.1567 0.1370 -0.2030 143 PHE A O 1124 C CB . PHE A 143 ? 1.2335 1.3443 0.7475 0.1406 0.1231 -0.2200 143 PHE A CB 1125 C CG . PHE A 143 ? 1.2198 1.3174 0.7204 0.1234 0.1042 -0.2076 143 PHE A CG 1126 C CD1 . PHE A 143 ? 1.2229 1.2875 0.7154 0.1202 0.0803 -0.2051 143 PHE A CD1 1127 C CD2 . PHE A 143 ? 1.1975 1.3149 0.6957 0.1102 0.1104 -0.1980 143 PHE A CD2 1128 C CE1 . PHE A 143 ? 1.2125 1.2673 0.6976 0.1056 0.0636 -0.1922 143 PHE A CE1 1129 C CE2 . PHE A 143 ? 1.1885 1.2925 0.6767 0.0962 0.0942 -0.1861 143 PHE A CE2 1130 C CZ . PHE A 143 ? 1.1926 1.2667 0.6755 0.0945 0.0711 -0.1828 143 PHE A CZ 1131 N N . PHE A 144 ? 1.1206 1.2952 0.7240 0.1354 0.1073 -0.1889 144 PHE A N 1132 C CA . PHE A 144 ? 1.0813 1.2919 0.7094 0.1275 0.1107 -0.1780 144 PHE A CA 1133 C C . PHE A 144 ? 1.0895 1.3282 0.7176 0.1256 0.1324 -0.1830 144 PHE A C 1134 O O . PHE A 144 ? 1.1326 1.3602 0.7296 0.1174 0.1415 -0.1869 144 PHE A O 1135 C CB . PHE A 144 ? 1.0665 1.2650 0.6814 0.1115 0.0993 -0.1677 144 PHE A CB 1136 C CG . PHE A 144 ? 1.0567 1.2329 0.6780 0.1119 0.0791 -0.1597 144 PHE A CG 1137 C CD1 . PHE A 144 ? 1.0205 1.2118 0.6745 0.1177 0.0722 -0.1512 144 PHE A CD1 1138 C CD2 . PHE A 144 ? 1.0771 1.2180 0.6718 0.1058 0.0665 -0.1594 144 PHE A CD2 1139 C CE1 . PHE A 144 ? 1.0103 1.1826 0.6725 0.1178 0.0559 -0.1421 144 PHE A CE1 1140 C CE2 . PHE A 144 ? 1.0595 1.1829 0.6660 0.1053 0.0480 -0.1503 144 PHE A CE2 1141 C CZ . PHE A 144 ? 1.0246 1.1640 0.6658 0.1115 0.0441 -0.1415 144 PHE A CZ 1142 N N . ARG A 145 ? 1.0738 1.3498 0.7382 0.1325 0.1401 -0.1810 145 ARG A N 1143 C CA . ARG A 145 ? 1.0770 1.3836 0.7510 0.1333 0.1614 -0.1853 145 ARG A CA 1144 C C . ARG A 145 ? 1.0961 1.4197 0.7648 0.1147 0.1680 -0.1795 145 ARG A C 1145 O O . ARG A 145 ? 1.1393 1.4842 0.8113 0.1126 0.1869 -0.1824 145 ARG A O 1146 C CB . ARG A 145 ? 1.0421 1.3872 0.7631 0.1454 0.1642 -0.1822 145 ARG A CB 1147 C CG . ARG A 145 ? 1.0446 1.3768 0.7780 0.1657 0.1606 -0.1869 145 ARG A CG 1148 C CD . ARG A 145 ? 1.0389 1.4127 0.8164 0.1787 0.1714 -0.1852 145 ARG A CD 1149 N NE . ARG A 145 ? 1.0555 1.4199 0.8522 0.1992 0.1673 -0.1871 145 ARG A NE 1150 C CZ . ARG A 145 ? 1.1047 1.4438 0.8887 0.2143 0.1788 -0.1999 145 ARG A CZ 1151 N NH1 . ARG A 145 ? 1.1446 1.4641 0.8914 0.2111 0.1951 -0.2124 145 ARG A NH1 1152 N NH2 . ARG A 145 ? 1.1241 1.4545 0.9301 0.2327 0.1740 -0.2002 145 ARG A NH2 1153 N N . ASN A 146 ? 1.0963 1.4112 0.7597 0.1016 0.1539 -0.1710 146 ASN A N 1154 C CA . ASN A 146 ? 1.0878 1.4184 0.7516 0.0840 0.1590 -0.1652 146 ASN A CA 1155 C C . ASN A 146 ? 1.1018 1.4038 0.7263 0.0719 0.1622 -0.1644 146 ASN A C 1156 O O . ASN A 146 ? 1.0859 1.3986 0.7071 0.0582 0.1718 -0.1608 146 ASN A O 1157 C CB . ASN A 146 ? 1.0641 1.4049 0.7477 0.0772 0.1444 -0.1567 146 ASN A CB 1158 C CG . ASN A 146 ? 1.0473 1.4243 0.7692 0.0852 0.1424 -0.1553 146 ASN A CG 1159 O OD1 . ASN A 146 ? 1.0588 1.4651 0.8008 0.0894 0.1546 -0.1583 146 ASN A OD1 1160 N ND2 . ASN A 146 ? 1.0260 1.4023 0.7591 0.0876 0.1271 -0.1494 146 ASN A ND2 1161 N N . VAL A 147 ? 1.1166 1.3819 0.7122 0.0763 0.1532 -0.1669 147 VAL A N 1162 C CA . VAL A 147 ? 1.1490 1.3852 0.7043 0.0661 0.1535 -0.1653 147 VAL A CA 1163 C C . VAL A 147 ? 1.1832 1.3977 0.7053 0.0749 0.1610 -0.1763 147 VAL A C 1164 O O . VAL A 147 ? 1.2079 1.4164 0.7358 0.0893 0.1584 -0.1846 147 VAL A O 1165 C CB . VAL A 147 ? 1.1443 1.3540 0.6918 0.0598 0.1328 -0.1563 147 VAL A CB 1166 C CG1 . VAL A 147 ? 1.1174 1.3446 0.6899 0.0503 0.1301 -0.1471 147 VAL A CG1 1167 C CG2 . VAL A 147 ? 1.1410 1.3346 0.6960 0.0718 0.1168 -0.1585 147 VAL A CG2 1168 N N . VAL A 148 ? 1.2084 1.4090 0.6937 0.0662 0.1708 -0.1762 148 VAL A N 1169 C CA . VAL A 148 ? 1.2465 1.4272 0.6929 0.0732 0.1824 -0.1878 148 VAL A CA 1170 C C . VAL A 148 ? 1.2726 1.4089 0.6726 0.0671 0.1647 -0.1866 148 VAL A C 1171 O O . VAL A 148 ? 1.2792 1.4060 0.6613 0.0531 0.1596 -0.1755 148 VAL A O 1172 C CB . VAL A 148 ? 1.2710 1.4705 0.7056 0.0675 0.2095 -0.1877 148 VAL A CB 1173 C CG1 . VAL A 148 ? 1.3407 1.5178 0.7297 0.0756 0.2245 -0.2004 148 VAL A CG1 1174 C CG2 . VAL A 148 ? 1.2405 1.4879 0.7264 0.0711 0.2251 -0.1867 148 VAL A CG2 1175 N N . TRP A 149 ? 1.2975 1.4064 0.6800 0.0773 0.1542 -0.1973 149 TRP A N 1176 C CA . TRP A 149 ? 1.3420 1.4081 0.6806 0.0712 0.1341 -0.1973 149 TRP A CA 1177 C C . TRP A 149 ? 1.4177 1.4628 0.6976 0.0693 0.1490 -0.2064 149 TRP A C 1178 O O . TRP A 149 ? 1.4564 1.4875 0.7141 0.0809 0.1593 -0.2231 149 TRP A O 1179 C CB . TRP A 149 ? 1.3382 1.3828 0.6862 0.0808 0.1142 -0.2045 149 TRP A CB 1180 C CG . TRP A 149 ? 1.3759 1.3773 0.6857 0.0740 0.0890 -0.2047 149 TRP A CG 1181 C CD1 . TRP A 149 ? 1.4072 1.3883 0.6773 0.0602 0.0793 -0.1967 149 TRP A CD1 1182 C CD2 . TRP A 149 ? 1.3791 1.3532 0.6903 0.0796 0.0681 -0.2116 149 TRP A CD2 1183 N NE1 . TRP A 149 ? 1.4342 1.3787 0.6808 0.0567 0.0524 -0.1986 149 TRP A NE1 1184 C CE2 . TRP A 149 ? 1.4143 1.3535 0.6862 0.0678 0.0453 -0.2081 149 TRP A CE2 1185 C CE3 . TRP A 149 ? 1.3653 1.3409 0.7085 0.0929 0.0656 -0.2193 149 TRP A CE3 1186 C CZ2 . TRP A 149 ? 1.4345 1.3408 0.6993 0.0677 0.0197 -0.2130 149 TRP A CZ2 1187 C CZ3 . TRP A 149 ? 1.3874 1.3284 0.7230 0.0933 0.0418 -0.2238 149 TRP A CZ3 1188 C CH2 . TRP A 149 ? 1.4191 1.3263 0.7165 0.0802 0.0189 -0.2211 149 TRP A CH2 1189 N N . LEU A 150 ? 1.4362 1.4780 0.6901 0.0550 0.1510 -0.1947 150 LEU A N 1190 C CA . LEU A 150 ? 1.4960 1.5218 0.6933 0.0513 0.1675 -0.1995 150 LEU A CA 1191 C C . LEU A 150 ? 1.5554 1.5336 0.6956 0.0474 0.1454 -0.2041 150 LEU A C 1192 O O . LEU A 150 ? 1.5470 1.5098 0.6910 0.0387 0.1167 -0.1926 150 LEU A O 1193 C CB . LEU A 150 ? 1.4962 1.5380 0.6912 0.0364 0.1778 -0.1823 150 LEU A CB 1194 C CG . LEU A 150 ? 1.4510 1.5387 0.6990 0.0357 0.1982 -0.1764 150 LEU A CG 1195 C CD1 . LEU A 150 ? 1.4492 1.5440 0.6961 0.0185 0.2011 -0.1579 150 LEU A CD1 1196 C CD2 . LEU A 150 ? 1.4672 1.5769 0.7173 0.0466 0.2302 -0.1890 150 LEU A CD2 1197 N N . ILE A 151 ? 1.6071 1.5625 0.6955 0.0538 0.1589 -0.2208 151 ILE A N 1198 C CA . ILE A 151 ? 1.6690 1.5760 0.6909 0.0483 0.1393 -0.2273 151 ILE A CA 1199 C C . ILE A 151 ? 1.7270 1.6200 0.6814 0.0435 0.1610 -0.2300 151 ILE A C 1200 O O . ILE A 151 ? 1.7077 1.6282 0.6693 0.0472 0.1946 -0.2299 151 ILE A O 1201 C CB . ILE A 151 ? 1.6915 1.5698 0.7040 0.0607 0.1284 -0.2489 151 ILE A CB 1202 C CG1 . ILE A 151 ? 1.7344 1.6138 0.7294 0.0771 0.1626 -0.2707 151 ILE A CG1 1203 C CG2 . ILE A 151 ? 1.6229 1.5174 0.7036 0.0661 0.1106 -0.2446 151 ILE A CG2 1204 C CD1 . ILE A 151 ? 1.7659 1.6130 0.7506 0.0903 0.1542 -0.2932 151 ILE A CD1 1205 N N . LYS A 152 ? 1.7987 1.6491 0.6877 0.0347 0.1408 -0.2315 152 LYS A N 1206 C CA . LYS A 152 ? 1.8815 1.7125 0.6958 0.0281 0.1569 -0.2319 152 LYS A CA 1207 C C . LYS A 152 ? 1.9522 1.7822 0.7357 0.0427 0.1959 -0.2539 152 LYS A C 1208 O O . LYS A 152 ? 1.9499 1.7735 0.7466 0.0580 0.2013 -0.2748 152 LYS A O 1209 C CB . LYS A 152 ? 1.9289 1.7107 0.6765 0.0169 0.1227 -0.2321 152 LYS A CB 1210 C CG . LYS A 152 ? 1.9787 1.7215 0.6923 0.0258 0.1110 -0.2589 152 LYS A CG 1211 C CD . LYS A 152 ? 2.0410 1.7361 0.6900 0.0118 0.0729 -0.2579 152 LYS A CD 1212 C CE . LYS A 152 ? 2.1029 1.7522 0.6982 0.0191 0.0676 -0.2883 152 LYS A CE 1213 N NZ . LYS A 152 ? 2.1749 1.7778 0.7050 0.0030 0.0276 -0.2868 152 LYS A NZ 1214 N N . LYS A 153 ? 2.0301 1.8655 0.7732 0.0382 0.2241 -0.2482 153 LYS A N 1215 C CA . LYS A 153 ? 2.1027 1.9390 0.8145 0.0518 0.2659 -0.2666 153 LYS A CA 1216 C C . LYS A 153 ? 2.1960 1.9906 0.8067 0.0448 0.2718 -0.2711 153 LYS A C 1217 O O . LYS A 153 ? 2.2151 2.0079 0.7962 0.0286 0.2664 -0.2500 153 LYS A O 1218 C CB . LYS A 153 ? 2.0793 1.9700 0.8462 0.0548 0.3029 -0.2551 153 LYS A CB 1219 C CG . LYS A 153 ? 2.1121 2.0188 0.8896 0.0752 0.3436 -0.2750 153 LYS A CG 1220 C CD . LYS A 153 ? 2.0928 2.0530 0.9176 0.0750 0.3805 -0.2612 153 LYS A CD 1221 C CE . LYS A 153 ? 2.1596 2.1120 0.9213 0.0648 0.4059 -0.2515 153 LYS A CE 1222 N NZ . LYS A 153 ? 2.1445 2.1472 0.9497 0.0669 0.4480 -0.2416 153 LYS A NZ 1223 N N . ASN A 154 ? 2.2742 2.0342 0.8314 0.0574 0.2833 -0.2986 154 ASN A N 1224 C CA . ASN A 154 ? 2.3768 2.0868 0.8262 0.0519 0.2846 -0.3088 154 ASN A CA 1225 C C . ASN A 154 ? 2.3862 2.0649 0.7943 0.0307 0.2371 -0.2926 154 ASN A C 1226 O O . ASN A 154 ? 2.4448 2.1052 0.7844 0.0182 0.2378 -0.2813 154 ASN A O 1227 C CB . ASN A 154 ? 2.4268 2.1525 0.8391 0.0533 0.3325 -0.3036 154 ASN A CB 1228 C CG . ASN A 154 ? 2.5614 2.2358 0.8628 0.0565 0.3477 -0.3245 154 ASN A CG 1229 O OD1 . ASN A 154 ? 2.6285 2.2585 0.8890 0.0635 0.3319 -0.3504 154 ASN A OD1 1230 N ND2 . ASN A 154 ? 2.6168 2.2954 0.8672 0.0511 0.3792 -0.3134 154 ASN A ND2 1231 N N . SER A 155 ? 2.3279 2.0020 0.7808 0.0272 0.1962 -0.2903 155 SER A N 1232 C CA . SER A 155 ? 2.3216 1.9726 0.7546 0.0083 0.1481 -0.2730 155 SER A CA 1233 C C . SER A 155 ? 2.2839 1.9617 0.7327 -0.0065 0.1465 -0.2389 155 SER A C 1234 O O . SER A 155 ? 2.3396 1.9923 0.7286 -0.0212 0.1273 -0.2250 155 SER A O 1235 C CB . SER A 155 ? 2.4215 2.0123 0.7502 0.0015 0.1288 -0.2886 155 SER A CB 1236 O OG . SER A 155 ? 2.4501 2.0111 0.7649 0.0145 0.1283 -0.3211 155 SER A OG 1237 N N . THR A 156 ? 2.1933 1.9206 0.7222 -0.0030 0.1655 -0.2252 156 THR A N 1238 C CA . THR A 156 ? 2.1547 1.9069 0.7064 -0.0165 0.1656 -0.1939 156 THR A CA 1239 C C . THR A 156 ? 2.0705 1.8691 0.7230 -0.0129 0.1690 -0.1836 156 THR A C 1240 O O . THR A 156 ? 2.0918 1.9214 0.7855 -0.0008 0.2003 -0.1941 156 THR A O 1241 C CB . THR A 156 ? 2.1851 1.9472 0.6949 -0.0185 0.2071 -0.1876 156 THR A CB 1242 O OG1 . THR A 156 ? 2.2809 1.9995 0.6907 -0.0193 0.2108 -0.2011 156 THR A OG1 1243 C CG2 . THR A 156 ? 2.1610 1.9390 0.6846 -0.0348 0.2023 -0.1541 156 THR A CG2 1244 N N . TYR A 157 ? 2.0186 1.8219 0.7107 -0.0227 0.1367 -0.1635 157 TYR A N 1245 C CA . TYR A 157 ? 1.9067 1.7513 0.6866 -0.0218 0.1403 -0.1509 157 TYR A CA 1246 C C . TYR A 157 ? 1.8930 1.7479 0.6745 -0.0362 0.1433 -0.1228 157 TYR A C 1247 O O . TYR A 157 ? 1.8722 1.7140 0.6562 -0.0464 0.1130 -0.1038 157 TYR A O 1248 C CB . TYR A 157 ? 1.8605 1.7030 0.6902 -0.0200 0.1050 -0.1500 157 TYR A CB 1249 C CG . TYR A 157 ? 1.7740 1.6574 0.6903 -0.0144 0.1130 -0.1458 157 TYR A CG 1250 C CD1 . TYR A 157 ? 1.7328 1.6391 0.6880 -0.0233 0.1157 -0.1238 157 TYR A CD1 1251 C CD2 . TYR A 157 ? 1.7391 1.6356 0.6955 -0.0004 0.1171 -0.1638 157 TYR A CD2 1252 C CE1 . TYR A 157 ? 1.6712 1.6114 0.6987 -0.0190 0.1220 -0.1217 157 TYR A CE1 1253 C CE2 . TYR A 157 ? 1.6679 1.6004 0.6975 0.0040 0.1228 -0.1595 157 TYR A CE2 1254 C CZ . TYR A 157 ? 1.6332 1.5872 0.6964 -0.0056 0.1251 -0.1392 157 TYR A CZ 1255 O OH . TYR A 157 ? 1.5459 1.5328 0.6760 -0.0019 0.1299 -0.1365 157 TYR A OH 1256 N N . PRO A 158 ? 1.8989 1.7766 0.6797 -0.0371 0.1804 -0.1191 158 PRO A N 1257 C CA . PRO A 158 ? 1.8910 1.7776 0.6764 -0.0514 0.1850 -0.0920 158 PRO A CA 1258 C C . PRO A 158 ? 1.7963 1.7114 0.6641 -0.0538 0.1771 -0.0797 158 PRO A C 1259 O O . PRO A 158 ? 1.7411 1.6771 0.6624 -0.0438 0.1774 -0.0932 158 PRO A O 1260 C CB . PRO A 158 ? 1.9262 1.8307 0.6914 -0.0507 0.2294 -0.0944 158 PRO A CB 1261 C CG . PRO A 158 ? 1.9060 1.8308 0.6996 -0.0340 0.2497 -0.1204 158 PRO A CG 1262 C CD . PRO A 158 ? 1.9159 1.8120 0.6936 -0.0254 0.2198 -0.1381 158 PRO A CD 1263 N N . THR A 159 ? 1.7834 1.6969 0.6587 -0.0668 0.1698 -0.0544 159 THR A N 1264 C CA . THR A 159 ? 1.7073 1.6415 0.6543 -0.0699 0.1620 -0.0426 159 THR A CA 1265 C C . THR A 159 ? 1.6703 1.6440 0.6687 -0.0659 0.1925 -0.0521 159 THR A C 1266 O O . THR A 159 ? 1.6901 1.6774 0.6729 -0.0687 0.2230 -0.0524 159 THR A O 1267 C CB . THR A 159 ? 1.7108 1.6339 0.6538 -0.0843 0.1541 -0.0134 159 THR A CB 1268 O OG1 . THR A 159 ? 1.7470 1.6352 0.6416 -0.0884 0.1241 -0.0023 159 THR A OG1 1269 C CG2 . THR A 159 ? 1.6397 1.5785 0.6538 -0.0861 0.1455 -0.0037 159 THR A CG2 1270 N N . ILE A 160 ? 1.6215 1.6139 0.6807 -0.0596 0.1835 -0.0591 160 ILE A N 1271 C CA . ILE A 160 ? 1.5763 1.6072 0.6916 -0.0572 0.2053 -0.0661 160 ILE A CA 1272 C C . ILE A 160 ? 1.5583 1.5981 0.7113 -0.0698 0.2052 -0.0476 160 ILE A C 1273 O O . ILE A 160 ? 1.5388 1.5620 0.7036 -0.0730 0.1819 -0.0360 160 ILE A O 1274 C CB . ILE A 160 ? 1.5177 1.5621 0.6755 -0.0437 0.1940 -0.0831 160 ILE A CB 1275 C CG1 . ILE A 160 ? 1.5438 1.5798 0.6693 -0.0304 0.1978 -0.1033 160 ILE A CG1 1276 C CG2 . ILE A 160 ? 1.4655 1.5489 0.6835 -0.0433 0.2101 -0.0867 160 ILE A CG2 1277 C CD1 . ILE A 160 ? 1.5053 1.5481 0.6661 -0.0169 0.1844 -0.1184 160 ILE A CD1 1278 N N . LYS A 161 ? 1.5664 1.6318 0.7402 -0.0770 0.2316 -0.0447 161 LYS A N 1279 C CA . LYS A 161 ? 1.5491 1.6230 0.7626 -0.0896 0.2330 -0.0304 161 LYS A CA 1280 C C . LYS A 161 ? 1.5141 1.6279 0.7772 -0.0903 0.2531 -0.0404 161 LYS A C 1281 O O . LYS A 161 ? 1.5438 1.6762 0.8052 -0.0969 0.2786 -0.0379 161 LYS A O 1282 C CB . LYS A 161 ? 1.6130 1.6704 0.7946 -0.1045 0.2425 -0.0088 161 LYS A CB 1283 C CG . LYS A 161 ? 1.6586 1.6779 0.8070 -0.1080 0.2178 0.0086 161 LYS A CG 1284 C CD . LYS A 161 ? 1.7121 1.7193 0.8424 -0.1239 0.2289 0.0326 161 LYS A CD 1285 C CE . LYS A 161 ? 1.7418 1.7150 0.8574 -0.1286 0.2034 0.0544 161 LYS A CE 1286 N NZ . LYS A 161 ? 1.8094 1.7559 0.8563 -0.1301 0.1955 0.0655 161 LYS A NZ 1287 N N . ARG A 162 ? 1.4671 1.5951 0.7747 -0.0840 0.2415 -0.0505 162 ARG A N 1288 C CA . ARG A 162 ? 1.4446 1.6113 0.7998 -0.0847 0.2559 -0.0599 162 ARG A CA 1289 C C . ARG A 162 ? 1.4202 1.5910 0.8174 -0.0941 0.2467 -0.0553 162 ARG A C 1290 O O . ARG A 162 ? 1.4134 1.5607 0.8117 -0.0929 0.2268 -0.0506 162 ARG A O 1291 C CB . ARG A 162 ? 1.4245 1.6088 0.7939 -0.0673 0.2528 -0.0788 162 ARG A CB 1292 C CG . ARG A 162 ? 1.4745 1.6557 0.8055 -0.0565 0.2655 -0.0875 162 ARG A CG 1293 C CD . ARG A 162 ? 1.5135 1.7137 0.8360 -0.0637 0.2963 -0.0830 162 ARG A CD 1294 N NE . ARG A 162 ? 1.5451 1.7587 0.8555 -0.0490 0.3140 -0.0977 162 ARG A NE 1295 C CZ . ARG A 162 ? 1.5185 1.7691 0.8726 -0.0399 0.3258 -0.1086 162 ARG A CZ 1296 N NH1 . ARG A 162 ? 1.4694 1.7486 0.8796 -0.0457 0.3203 -0.1069 162 ARG A NH1 1297 N NH2 . ARG A 162 ? 1.5469 1.8052 0.8877 -0.0248 0.3431 -0.1214 162 ARG A NH2 1298 N N . SER A 163 ? 1.3942 1.5954 0.8269 -0.1032 0.2616 -0.0571 163 SER A N 1299 C CA . SER A 163 ? 1.3525 1.5571 0.8217 -0.1144 0.2552 -0.0548 163 SER A CA 1300 C C . SER A 163 ? 1.3205 1.5669 0.8336 -0.1149 0.2623 -0.0668 163 SER A C 1301 O O . SER A 163 ? 1.3152 1.5902 0.8363 -0.1163 0.2811 -0.0683 163 SER A O 1302 C CB . SER A 163 ? 1.3764 1.5662 0.8388 -0.1333 0.2648 -0.0378 163 SER A CB 1303 O OG . SER A 163 ? 1.3875 1.5732 0.8816 -0.1446 0.2579 -0.0367 163 SER A OG 1304 N N . TYR A 164 ? 1.2873 1.5383 0.8284 -0.1129 0.2474 -0.0746 164 TYR A N 1305 C CA . TYR A 164 ? 1.2558 1.5453 0.8386 -0.1164 0.2505 -0.0838 164 TYR A CA 1306 C C . TYR A 164 ? 1.2657 1.5494 0.8713 -0.1325 0.2428 -0.0828 164 TYR A C 1307 O O . TYR A 164 ? 1.2586 1.5151 0.8580 -0.1300 0.2282 -0.0836 164 TYR A O 1308 C CB . TYR A 164 ? 1.2163 1.5227 0.8110 -0.0978 0.2403 -0.0967 164 TYR A CB 1309 C CG . TYR A 164 ? 1.2030 1.5477 0.8407 -0.1020 0.2391 -0.1042 164 TYR A CG 1310 C CD1 . TYR A 164 ? 1.2132 1.5981 0.8759 -0.1040 0.2547 -0.1053 164 TYR A CD1 1311 C CD2 . TYR A 164 ? 1.2010 1.5422 0.8544 -0.1045 0.2225 -0.1093 164 TYR A CD2 1312 C CE1 . TYR A 164 ? 1.2009 1.6232 0.9060 -0.1089 0.2506 -0.1103 164 TYR A CE1 1313 C CE2 . TYR A 164 ? 1.1869 1.5621 0.8758 -0.1097 0.2185 -0.1157 164 TYR A CE2 1314 C CZ . TYR A 164 ? 1.1859 1.6024 0.9020 -0.1124 0.2310 -0.1156 164 TYR A CZ 1315 O OH . TYR A 164 ? 1.1730 1.6247 0.9265 -0.1184 0.2238 -0.1204 164 TYR A OH 1316 N N . ASN A 165 ? 1.2986 1.6080 0.9315 -0.1489 0.2535 -0.0814 165 ASN A N 1317 C CA . ASN A 165 ? 1.3348 1.6399 0.9899 -0.1673 0.2474 -0.0823 165 ASN A CA 1318 C C . ASN A 165 ? 1.3044 1.6408 0.9913 -0.1653 0.2363 -0.0956 165 ASN A C 1319 O O . ASN A 165 ? 1.2922 1.6701 1.0041 -0.1636 0.2426 -0.0987 165 ASN A O 1320 C CB . ASN A 165 ? 1.3966 1.7116 1.0645 -0.1889 0.2640 -0.0718 165 ASN A CB 1321 C CG . ASN A 165 ? 1.4575 1.7586 1.1433 -0.2106 0.2579 -0.0719 165 ASN A CG 1322 O OD1 . ASN A 165 ? 1.4248 1.7294 1.1264 -0.2123 0.2437 -0.0836 165 ASN A OD1 1323 N ND2 . ASN A 165 ? 1.6055 1.8887 1.2867 -0.2275 0.2688 -0.0588 165 ASN A ND2 1324 N N . ASN A 166 ? 1.2942 1.6107 0.9797 -0.1650 0.2203 -0.1027 166 ASN A N 1325 C CA . ASN A 166 ? 1.2728 1.6148 0.9827 -0.1650 0.2079 -0.1145 166 ASN A CA 1326 C C . ASN A 166 ? 1.2767 1.6372 1.0146 -0.1893 0.2087 -0.1160 166 ASN A C 1327 O O . ASN A 166 ? 1.2691 1.6046 1.0040 -0.2032 0.2013 -0.1199 166 ASN A O 1328 C CB . ASN A 166 ? 1.2617 1.5748 0.9565 -0.1566 0.1926 -0.1216 166 ASN A CB 1329 C CG . ASN A 166 ? 1.2559 1.5956 0.9683 -0.1524 0.1794 -0.1326 166 ASN A CG 1330 O OD1 . ASN A 166 ? 1.2316 1.6126 0.9673 -0.1495 0.1800 -0.1340 166 ASN A OD1 1331 N ND2 . ASN A 166 ? 1.2666 1.5832 0.9680 -0.1514 0.1679 -0.1395 166 ASN A ND2 1332 N N . THR A 167 ? 1.2752 1.6788 1.0415 -0.1944 0.2180 -0.1130 167 THR A N 1333 C CA . THR A 167 ? 1.2967 1.7241 1.0963 -0.2191 0.2187 -0.1124 167 THR A CA 1334 C C . THR A 167 ? 1.3051 1.7646 1.1322 -0.2218 0.2006 -0.1231 167 THR A C 1335 O O . THR A 167 ? 1.3345 1.8048 1.1842 -0.2444 0.1934 -0.1258 167 THR A O 1336 C CB . THR A 167 ? 1.2863 1.7463 1.1080 -0.2259 0.2398 -0.1008 167 THR A CB 1337 O OG1 . THR A 167 ? 1.2384 1.7337 1.0705 -0.2050 0.2460 -0.1017 167 THR A OG1 1338 C CG2 . THR A 167 ? 1.3049 1.7293 1.0962 -0.2292 0.2559 -0.0887 167 THR A CG2 1339 N N . ASN A 168 ? 1.2713 1.7451 1.0959 -0.1998 0.1921 -0.1287 168 ASN A N 1340 C CA . ASN A 168 ? 1.2336 1.7308 1.0758 -0.2006 0.1720 -0.1379 168 ASN A CA 1341 C C . ASN A 168 ? 1.1995 1.6569 1.0163 -0.2094 0.1569 -0.1475 168 ASN A C 1342 O O . ASN A 168 ? 1.2084 1.6205 0.9952 -0.2086 0.1621 -0.1468 168 ASN A O 1343 C CB . ASN A 168 ? 1.2110 1.7332 1.0586 -0.1747 0.1668 -0.1396 168 ASN A CB 1344 C CG . ASN A 168 ? 1.2083 1.7110 1.0309 -0.1525 0.1797 -0.1357 168 ASN A CG 1345 O OD1 . ASN A 168 ? 1.2055 1.7356 1.0423 -0.1367 0.1872 -0.1332 168 ASN A OD1 1346 N ND2 . ASN A 168 ? 1.2159 1.6708 1.0020 -0.1508 0.1814 -0.1352 168 ASN A ND2 1347 N N . GLN A 169 ? 1.1838 1.6585 1.0127 -0.2179 0.1385 -0.1559 169 GLN A N 1348 C CA . GLN A 169 ? 1.2184 1.6562 1.0220 -0.2292 0.1251 -0.1672 169 GLN A CA 1349 C C . GLN A 169 ? 1.1875 1.5949 0.9563 -0.2084 0.1195 -0.1727 169 GLN A C 1350 O O . GLN A 169 ? 1.1907 1.5545 0.9314 -0.2127 0.1179 -0.1795 169 GLN A O 1351 C CB . GLN A 169 ? 1.2558 1.7223 1.0803 -0.2478 0.1055 -0.1750 169 GLN A CB 1352 C CG . GLN A 169 ? 1.3042 1.7622 1.1412 -0.2792 0.1046 -0.1774 169 GLN A CG 1353 C CD . GLN A 169 ? 1.3365 1.8128 1.2017 -0.2863 0.1239 -0.1638 169 GLN A CD 1354 O OE1 . GLN A 169 ? 1.3528 1.7945 1.1998 -0.2851 0.1404 -0.1582 169 GLN A OE1 1355 N NE2 . GLN A 169 ? 1.3571 1.8895 1.2675 -0.2922 0.1230 -0.1569 169 GLN A NE2 1356 N N . GLU A 170 ? 1.1374 1.5680 0.9107 -0.1859 0.1176 -0.1691 170 GLU A N 1357 C CA . GLU A 170 ? 1.1051 1.5171 0.8531 -0.1663 0.1105 -0.1727 170 GLU A CA 1358 C C . GLU A 170 ? 1.0960 1.4750 0.8225 -0.1491 0.1230 -0.1668 170 GLU A C 1359 O O . GLU A 170 ? 1.1036 1.4932 0.8391 -0.1414 0.1340 -0.1588 170 GLU A O 1360 C CB . GLU A 170 ? 1.0744 1.5287 0.8420 -0.1513 0.1011 -0.1702 170 GLU A CB 1361 C CG . GLU A 170 ? 1.0843 1.5798 0.8799 -0.1666 0.0863 -0.1729 170 GLU A CG 1362 C CD . GLU A 170 ? 1.0720 1.6089 0.9091 -0.1743 0.0945 -0.1655 170 GLU A CD 1363 O OE1 . GLU A 170 ? 1.0995 1.6248 0.9370 -0.1762 0.1128 -0.1604 170 GLU A OE1 1364 O OE2 . GLU A 170 ? 1.0476 1.6295 0.9174 -0.1783 0.0830 -0.1636 170 GLU A OE2 1365 N N . ASP A 171 ? 1.1076 1.4470 0.8059 -0.1433 0.1213 -0.1705 171 ASP A N 1366 C CA . ASP A 171 ? 1.0902 1.4004 0.7711 -0.1258 0.1292 -0.1638 171 ASP A CA 1367 C C . ASP A 171 ? 1.0570 1.3931 0.7493 -0.1075 0.1304 -0.1571 171 ASP A C 1368 O O . ASP A 171 ? 1.0287 1.3974 0.7358 -0.1006 0.1224 -0.1587 171 ASP A O 1369 C CB . ASP A 171 ? 1.1146 1.3958 0.7730 -0.1154 0.1241 -0.1680 171 ASP A CB 1370 C CG . ASP A 171 ? 1.1655 1.4076 0.8061 -0.1289 0.1272 -0.1749 171 ASP A CG 1371 O OD1 . ASP A 171 ? 1.2025 1.4333 0.8469 -0.1456 0.1333 -0.1748 171 ASP A OD1 1372 O OD2 . ASP A 171 ? 1.1967 1.4178 0.8188 -0.1223 0.1247 -0.1803 171 ASP A OD2 1373 N N . LEU A 172 ? 1.0638 1.3832 0.7477 -0.0993 0.1397 -0.1495 172 LEU A N 1374 C CA . LEU A 172 ? 1.0672 1.4044 0.7571 -0.0829 0.1421 -0.1449 172 LEU A CA 1375 C C . LEU A 172 ? 1.0444 1.3533 0.7161 -0.0656 0.1397 -0.1405 172 LEU A C 1376 O O . LEU A 172 ? 1.0438 1.3200 0.6997 -0.0675 0.1434 -0.1357 172 LEU A O 1377 C CB . LEU A 172 ? 1.1025 1.4487 0.7973 -0.0898 0.1553 -0.1399 172 LEU A CB 1378 C CG . LEU A 172 ? 1.1180 1.4860 0.8191 -0.0746 0.1608 -0.1378 172 LEU A CG 1379 C CD1 . LEU A 172 ? 1.1142 1.5266 0.8454 -0.0709 0.1570 -0.1418 172 LEU A CD1 1380 C CD2 . LEU A 172 ? 1.1497 1.5155 0.8441 -0.0808 0.1766 -0.1322 172 LEU A CD2 1381 N N . LEU A 173 ? 1.0186 1.3411 0.6959 -0.0493 0.1327 -0.1410 173 LEU A N 1382 C CA . LEU A 173 ? 1.0099 1.3111 0.6758 -0.0331 0.1295 -0.1360 173 LEU A CA 1383 C C . LEU A 173 ? 1.0235 1.3258 0.6855 -0.0263 0.1351 -0.1330 173 LEU A C 1384 O O . LEU A 173 ? 1.0321 1.3602 0.7063 -0.0190 0.1367 -0.1357 173 LEU A O 1385 C CB . LEU A 173 ? 0.9995 1.3132 0.6735 -0.0193 0.1196 -0.1370 173 LEU A CB 1386 C CG . LEU A 173 ? 0.9945 1.2899 0.6625 -0.0029 0.1151 -0.1312 173 LEU A CG 1387 C CD1 . LEU A 173 ? 1.0015 1.2618 0.6557 -0.0045 0.1157 -0.1257 173 LEU A CD1 1388 C CD2 . LEU A 173 ? 0.9859 1.2954 0.6641 0.0093 0.1063 -0.1306 173 LEU A CD2 1389 N N . VAL A 174 ? 1.0297 1.3028 0.6736 -0.0280 0.1382 -0.1271 174 VAL A N 1390 C CA . VAL A 174 ? 1.0214 1.2892 0.6525 -0.0227 0.1427 -0.1246 174 VAL A CA 1391 C C . VAL A 174 ? 1.0099 1.2553 0.6309 -0.0091 0.1325 -0.1207 174 VAL A C 1392 O O . VAL A 174 ? 0.9972 1.2194 0.6142 -0.0094 0.1264 -0.1147 174 VAL A O 1393 C CB . VAL A 174 ? 1.0419 1.2925 0.6566 -0.0359 0.1517 -0.1187 174 VAL A CB 1394 C CG1 . VAL A 174 ? 1.0720 1.3199 0.6685 -0.0312 0.1578 -0.1173 174 VAL A CG1 1395 C CG2 . VAL A 174 ? 1.0404 1.3086 0.6682 -0.0524 0.1605 -0.1210 174 VAL A CG2 1396 N N . LEU A 175 ? 1.0058 1.2580 0.6251 0.0026 0.1310 -0.1240 175 LEU A N 1397 C CA . LEU A 175 ? 0.9973 1.2281 0.6074 0.0142 0.1202 -0.1211 175 LEU A CA 1398 C C . LEU A 175 ? 1.0323 1.2472 0.6165 0.0144 0.1229 -0.1212 175 LEU A C 1399 O O . LEU A 175 ? 1.0466 1.2756 0.6248 0.0131 0.1349 -0.1268 175 LEU A O 1400 C CB . LEU A 175 ? 0.9811 1.2276 0.6078 0.0282 0.1147 -0.1260 175 LEU A CB 1401 C CG . LEU A 175 ? 0.9626 1.2251 0.6110 0.0302 0.1100 -0.1252 175 LEU A CG 1402 C CD1 . LEU A 175 ? 0.9641 1.2541 0.6308 0.0406 0.1098 -0.1305 175 LEU A CD1 1403 C CD2 . LEU A 175 ? 0.9493 1.1906 0.5987 0.0353 0.0996 -0.1176 175 LEU A CD2 1404 N N . TRP A 176 ? 1.0464 1.2324 0.6152 0.0158 0.1119 -0.1144 176 TRP A N 1405 C CA . TRP A 176 ? 1.0771 1.2438 0.6160 0.0168 0.1098 -0.1149 176 TRP A CA 1406 C C . TRP A 176 ? 1.0859 1.2281 0.6208 0.0231 0.0911 -0.1098 176 TRP A C 1407 O O . TRP A 176 ? 1.0579 1.2002 0.6156 0.0268 0.0825 -0.1047 176 TRP A O 1408 C CB . TRP A 176 ? 1.1105 1.2654 0.6268 0.0038 0.1169 -0.1079 176 TRP A CB 1409 C CG . TRP A 176 ? 1.1101 1.2446 0.6284 -0.0027 0.1075 -0.0946 176 TRP A CG 1410 C CD1 . TRP A 176 ? 1.1259 1.2333 0.6274 -0.0034 0.0937 -0.0846 176 TRP A CD1 1411 C CD2 . TRP A 176 ? 1.0917 1.2305 0.6308 -0.0092 0.1114 -0.0897 176 TRP A CD2 1412 N NE1 . TRP A 176 ? 1.1142 1.2108 0.6291 -0.0085 0.0899 -0.0725 176 TRP A NE1 1413 C CE2 . TRP A 176 ? 1.1040 1.2174 0.6400 -0.0119 0.1017 -0.0764 176 TRP A CE2 1414 C CE3 . TRP A 176 ? 1.0674 1.2281 0.6269 -0.0133 0.1215 -0.0956 176 TRP A CE3 1415 C CZ2 . TRP A 176 ? 1.1044 1.2117 0.6571 -0.0168 0.1045 -0.0699 176 TRP A CZ2 1416 C CZ3 . TRP A 176 ? 1.0689 1.2218 0.6403 -0.0200 0.1226 -0.0904 176 TRP A CZ3 1417 C CH2 . TRP A 176 ? 1.0876 1.2130 0.6555 -0.0209 0.1155 -0.0782 176 TRP A CH2 1418 N N . GLY A 177 ? 1.1356 1.2566 0.6407 0.0235 0.0847 -0.1109 177 GLY A N 1419 C CA . GLY A 177 ? 1.1488 1.2467 0.6513 0.0277 0.0642 -0.1062 177 GLY A CA 1420 C C . GLY A 177 ? 1.1766 1.2462 0.6411 0.0222 0.0536 -0.1029 177 GLY A C 1421 O O . GLY A 177 ? 1.2146 1.2807 0.6482 0.0164 0.0641 -0.1055 177 GLY A O 1422 N N . ILE A 178 ? 1.1809 1.2312 0.6486 0.0235 0.0322 -0.0963 178 ILE A N 1423 C CA . ILE A 178 ? 1.2188 1.2404 0.6516 0.0176 0.0155 -0.0921 178 ILE A CA 1424 C C . ILE A 178 ? 1.2316 1.2383 0.6615 0.0243 -0.0004 -0.1008 178 ILE A C 1425 O O . ILE A 178 ? 1.1879 1.2031 0.6535 0.0313 -0.0055 -0.1002 178 ILE A O 1426 C CB . ILE A 178 ? 1.2197 1.2307 0.6647 0.0102 0.0005 -0.0715 178 ILE A CB 1427 C CG1 . ILE A 178 ? 1.2686 1.2517 0.6757 0.0024 -0.0188 -0.0648 178 ILE A CG1 1428 C CG2 . ILE A 178 ? 1.1908 1.2060 0.6802 0.0156 -0.0119 -0.0631 178 ILE A CG2 1429 C CD1 . ILE A 178 ? 1.3038 1.2804 0.6792 -0.0070 -0.0110 -0.0566 178 ILE A CD1 1430 N N . HIS A 179 ? 1.2890 1.2718 0.6745 0.0218 -0.0080 -0.1091 179 HIS A N 1431 C CA . HIS A 179 ? 1.3236 1.2850 0.7010 0.0258 -0.0261 -0.1181 179 HIS A CA 1432 C C . HIS A 179 ? 1.3437 1.2792 0.7095 0.0162 -0.0563 -0.1057 179 HIS A C 1433 O O . HIS A 179 ? 1.3898 1.3094 0.7165 0.0071 -0.0626 -0.1009 179 HIS A O 1434 C CB . HIS A 179 ? 1.3715 1.3203 0.7054 0.0308 -0.0143 -0.1394 179 HIS A CB 1435 C CG . HIS A 179 ? 1.4154 1.3345 0.7325 0.0334 -0.0335 -0.1508 179 HIS A CG 1436 N ND1 . HIS A 179 ? 1.4933 1.3786 0.7539 0.0271 -0.0454 -0.1590 179 HIS A ND1 1437 C CD2 . HIS A 179 ? 1.4082 1.3241 0.7563 0.0407 -0.0438 -0.1550 179 HIS A CD2 1438 C CE1 . HIS A 179 ? 1.5194 1.3806 0.7769 0.0300 -0.0626 -0.1696 179 HIS A CE1 1439 N NE2 . HIS A 179 ? 1.4785 1.3579 0.7906 0.0383 -0.0617 -0.1667 179 HIS A NE2 1440 N N . HIS A 180 ? 1.3244 1.2568 0.7259 0.0179 -0.0752 -0.0992 180 HIS A N 1441 C CA . HIS A 180 ? 1.3522 1.2636 0.7534 0.0088 -0.1065 -0.0864 180 HIS A CA 1442 C C . HIS A 180 ? 1.4066 1.2892 0.7801 0.0085 -0.1234 -0.1025 180 HIS A C 1443 O O . HIS A 180 ? 1.4002 1.2843 0.8002 0.0161 -0.1236 -0.1100 180 HIS A O 1444 C CB . HIS A 180 ? 1.3045 1.2317 0.7677 0.0104 -0.1158 -0.0679 180 HIS A CB 1445 C CG . HIS A 180 ? 1.2640 1.2154 0.7552 0.0115 -0.0990 -0.0537 180 HIS A CG 1446 N ND1 . HIS A 180 ? 1.2823 1.2304 0.7597 0.0037 -0.1012 -0.0403 180 HIS A ND1 1447 C CD2 . HIS A 180 ? 1.2219 1.1985 0.7519 0.0192 -0.0802 -0.0512 180 HIS A CD2 1448 C CE1 . HIS A 180 ? 1.2366 1.2051 0.7443 0.0068 -0.0836 -0.0313 180 HIS A CE1 1449 N NE2 . HIS A 180 ? 1.2066 1.1925 0.7444 0.0158 -0.0709 -0.0384 180 HIS A NE2 1450 N N . PRO A 181 ? 1.4679 1.3219 0.7860 -0.0003 -0.1378 -0.1078 181 PRO A N 1451 C CA . PRO A 181 ? 1.5239 1.3450 0.8075 -0.0012 -0.1530 -0.1265 181 PRO A CA 1452 C C . PRO A 181 ? 1.5374 1.3395 0.8387 -0.0111 -0.1914 -0.1158 181 PRO A C 1453 O O . PRO A 181 ? 1.5054 1.3198 0.8414 -0.0178 -0.2067 -0.0920 181 PRO A O 1454 C CB . PRO A 181 ? 1.5901 1.3896 0.7996 -0.0067 -0.1481 -0.1373 181 PRO A CB 1455 C CG . PRO A 181 ? 1.5815 1.3934 0.7922 -0.0157 -0.1515 -0.1142 181 PRO A CG 1456 C CD . PRO A 181 ? 1.5052 1.3530 0.7857 -0.0102 -0.1404 -0.0973 181 PRO A CD 1457 N N . ASN A 182 ? 1.5976 1.3687 0.8753 -0.0123 -0.2066 -0.1333 182 ASN A N 1458 C CA . ASN A 182 ? 1.6234 1.3748 0.9206 -0.0228 -0.2442 -0.1255 182 ASN A CA 1459 C C . ASN A 182 ? 1.6523 1.3831 0.9170 -0.0400 -0.2777 -0.1138 182 ASN A C 1460 O O . ASN A 182 ? 1.6229 1.3605 0.9310 -0.0487 -0.3044 -0.0919 182 ASN A O 1461 C CB . ASN A 182 ? 1.6717 1.3926 0.9521 -0.0191 -0.2495 -0.1499 182 ASN A CB 1462 C CG . ASN A 182 ? 1.6556 1.3982 0.9919 -0.0048 -0.2301 -0.1515 182 ASN A CG 1463 O OD1 . ASN A 182 ? 1.6542 1.4092 1.0487 -0.0067 -0.2434 -0.1349 182 ASN A OD1 1464 N ND2 . ASN A 182 ? 1.6642 1.4146 0.9860 0.0095 -0.1976 -0.1690 182 ASN A ND2 1465 N N . ASP A 183 ? 1.7091 1.4158 0.8985 -0.0446 -0.2760 -0.1273 183 ASP A N 1466 C CA . ASP A 183 ? 1.7587 1.4415 0.9044 -0.0616 -0.3094 -0.1178 183 ASP A CA 1467 C C . ASP A 183 ? 1.7809 1.4557 0.8555 -0.0631 -0.2930 -0.1226 183 ASP A C 1468 O O . ASP A 183 ? 1.7548 1.4412 0.8134 -0.0514 -0.2554 -0.1354 183 ASP A O 1469 C CB . ASP A 183 ? 1.8207 1.4607 0.9349 -0.0719 -0.3432 -0.1338 183 ASP A CB 1470 C CG . ASP A 183 ? 1.8633 1.4755 0.9304 -0.0623 -0.3228 -0.1690 183 ASP A CG 1471 O OD1 . ASP A 183 ? 1.9066 1.5119 0.9152 -0.0563 -0.2965 -0.1841 183 ASP A OD1 1472 O OD2 . ASP A 183 ? 1.8646 1.4616 0.9552 -0.0603 -0.3323 -0.1809 183 ASP A OD2 1473 N N . ALA A 184 ? 1.8230 1.4790 0.8569 -0.0782 -0.3222 -0.1104 184 ALA A N 1474 C CA . ALA A 184 ? 1.8647 1.5098 0.8263 -0.0819 -0.3105 -0.1116 184 ALA A CA 1475 C C . ALA A 184 ? 1.9163 1.5343 0.8053 -0.0752 -0.2861 -0.1453 184 ALA A C 1476 O O . ALA A 184 ? 1.9121 1.5370 0.7641 -0.0698 -0.2544 -0.1496 184 ALA A O 1477 C CB . ALA A 184 ? 1.9100 1.5336 0.8353 -0.1002 -0.3525 -0.0941 184 ALA A CB 1478 N N . ALA A 185 ? 1.9551 1.5423 0.8267 -0.0753 -0.2996 -0.1687 185 ALA A N 1479 C CA . ALA A 185 ? 2.0165 1.5729 0.8197 -0.0677 -0.2773 -0.2027 185 ALA A CA 1480 C C . ALA A 185 ? 1.9558 1.5409 0.7883 -0.0475 -0.2284 -0.2147 185 ALA A C 1481 O O . ALA A 185 ? 1.9827 1.5605 0.7629 -0.0398 -0.1972 -0.2317 185 ALA A O 1482 C CB . ALA A 185 ? 2.0695 1.5835 0.8538 -0.0727 -0.3052 -0.2244 185 ALA A CB 1483 N N . GLU A 186 ? 1.8787 1.4973 0.7950 -0.0390 -0.2218 -0.2046 186 GLU A N 1484 C CA . GLU A 186 ? 1.8302 1.4798 0.7806 -0.0209 -0.1795 -0.2131 186 GLU A CA 1485 C C . GLU A 186 ? 1.7979 1.4803 0.7476 -0.0190 -0.1511 -0.1989 186 GLU A C 1486 O O . GLU A 186 ? 1.7827 1.4778 0.7198 -0.0076 -0.1145 -0.2117 186 GLU A O 1487 C CB . GLU A 186 ? 1.7585 1.4340 0.7949 -0.0138 -0.1827 -0.2042 186 GLU A CB 1488 C CG . GLU A 186 ? 1.7241 1.4222 0.7904 0.0050 -0.1458 -0.2179 186 GLU A CG 1489 C CD . GLU A 186 ? 1.6609 1.3782 0.8035 0.0115 -0.1519 -0.2101 186 GLU A CD 1490 O OE1 . GLU A 186 ? 1.6036 1.3549 0.8008 0.0101 -0.1525 -0.1871 186 GLU A OE1 1491 O OE2 . GLU A 186 ? 1.6699 1.3664 0.8160 0.0183 -0.1549 -0.2271 186 GLU A OE2 1492 N N . GLN A 187 ? 1.7819 1.4777 0.7482 -0.0302 -0.1682 -0.1718 187 GLN A N 1493 C CA . GLN A 187 ? 1.7656 1.4871 0.7296 -0.0311 -0.1455 -0.1562 187 GLN A CA 1494 C C . GLN A 187 ? 1.8404 1.5438 0.7242 -0.0314 -0.1235 -0.1704 187 GLN A C 1495 O O . GLN A 187 ? 1.8228 1.5474 0.7079 -0.0221 -0.0859 -0.1771 187 GLN A O 1496 C CB . GLN A 187 ? 1.7494 1.4764 0.7323 -0.0442 -0.1733 -0.1257 187 GLN A CB 1497 C CG . GLN A 187 ? 1.7382 1.4849 0.7151 -0.0471 -0.1540 -0.1075 187 GLN A CG 1498 C CD . GLN A 187 ? 1.6668 1.4525 0.6984 -0.0360 -0.1192 -0.1063 187 GLN A CD 1499 O OE1 . GLN A 187 ? 1.6011 1.4058 0.6935 -0.0284 -0.1184 -0.1069 187 GLN A OE1 1500 N NE2 . GLN A 187 ? 1.6704 1.4679 0.6796 -0.0360 -0.0910 -0.1039 187 GLN A NE2 1501 N N . THR A 188 ? 1.9240 1.5886 0.7379 -0.0426 -0.1469 -0.1744 188 THR A N 1502 C CA . THR A 188 ? 1.9980 1.6420 0.7283 -0.0436 -0.1265 -0.1868 188 THR A CA 1503 C C . THR A 188 ? 2.0118 1.6472 0.7213 -0.0282 -0.0944 -0.2191 188 THR A C 1504 O O . THR A 188 ? 2.0414 1.6837 0.7176 -0.0217 -0.0582 -0.2272 188 THR A O 1505 C CB . THR A 188 ? 2.0961 1.6965 0.7493 -0.0597 -0.1617 -0.1850 188 THR A CB 1506 O OG1 . THR A 188 ? 2.1335 1.7004 0.7752 -0.0619 -0.1906 -0.2035 188 THR A OG1 1507 C CG2 . THR A 188 ? 2.0803 1.6919 0.7561 -0.0738 -0.1918 -0.1499 188 THR A CG2 1508 N N . LYS A 189 ? 1.9876 1.6096 0.7216 -0.0217 -0.1066 -0.2360 189 LYS A N 1509 C CA . LYS A 189 ? 2.0004 1.6133 0.7236 -0.0052 -0.0779 -0.2657 189 LYS A CA 1510 C C . LYS A 189 ? 1.9485 1.6079 0.7213 0.0100 -0.0344 -0.2643 189 LYS A C 1511 O O . LYS A 189 ? 1.9810 1.6381 0.7257 0.0221 -0.0007 -0.2837 189 LYS A O 1512 C CB . LYS A 189 ? 1.9935 1.5866 0.7484 -0.0019 -0.1021 -0.2786 189 LYS A CB 1513 C CG . LYS A 189 ? 2.0148 1.5960 0.7674 0.0164 -0.0758 -0.3081 189 LYS A CG 1514 C CD . LYS A 189 ? 2.0213 1.5767 0.8011 0.0166 -0.1047 -0.3184 189 LYS A CD 1515 C CE . LYS A 189 ? 2.0169 1.5675 0.8151 0.0371 -0.0782 -0.3427 189 LYS A CE 1516 N NZ . LYS A 189 ? 1.9170 1.5190 0.8032 0.0496 -0.0600 -0.3288 189 LYS A NZ 1517 N N . LEU A 190 ? 1.8637 1.5645 0.7093 0.0091 -0.0352 -0.2417 190 LEU A N 1518 C CA . LEU A 190 ? 1.8181 1.5643 0.7138 0.0209 0.0012 -0.2388 190 LEU A CA 1519 C C . LEU A 190 ? 1.8111 1.5807 0.6951 0.0139 0.0210 -0.2216 190 LEU A C 1520 O O . LEU A 190 ? 1.7926 1.5860 0.6804 0.0221 0.0572 -0.2267 190 LEU A O 1521 C CB . LEU A 190 ? 1.7415 1.5188 0.7232 0.0248 -0.0085 -0.2261 190 LEU A CB 1522 C CG . LEU A 190 ? 1.7462 1.5074 0.7564 0.0312 -0.0282 -0.2372 190 LEU A CG 1523 C CD1 . LEU A 190 ? 1.6641 1.4631 0.7567 0.0374 -0.0268 -0.2242 190 LEU A CD1 1524 C CD2 . LEU A 190 ? 1.8023 1.5405 0.7813 0.0449 -0.0106 -0.2663 190 LEU A CD2 1525 N N . TYR A 191 ? 1.8216 1.5855 0.6961 -0.0011 -0.0030 -0.1997 191 TYR A N 1526 C CA . TYR A 191 ? 1.8119 1.5984 0.6879 -0.0088 0.0116 -0.1789 191 TYR A CA 1527 C C . TYR A 191 ? 1.8950 1.6531 0.6960 -0.0222 0.0020 -0.1698 191 TYR A C 1528 O O . TYR A 191 ? 1.9105 1.6833 0.7067 -0.0291 0.0150 -0.1518 191 TYR A O 1529 C CB . TYR A 191 ? 1.7470 1.5590 0.6928 -0.0134 -0.0044 -0.1556 191 TYR A CB 1530 C CG . TYR A 191 ? 1.6825 1.5182 0.6979 -0.0018 -0.0015 -0.1622 191 TYR A CG 1531 C CD1 . TYR A 191 ? 1.6528 1.5198 0.6997 0.0093 0.0312 -0.1713 191 TYR A CD1 1532 C CD2 . TYR A 191 ? 1.6573 1.4849 0.7072 -0.0024 -0.0320 -0.1581 191 TYR A CD2 1533 C CE1 . TYR A 191 ? 1.5960 1.4844 0.7033 0.0197 0.0326 -0.1758 191 TYR A CE1 1534 C CE2 . TYR A 191 ? 1.6088 1.4572 0.7190 0.0079 -0.0285 -0.1625 191 TYR A CE2 1535 C CZ . TYR A 191 ? 1.5696 1.4476 0.7061 0.0191 0.0034 -0.1714 191 TYR A CZ 1536 O OH . TYR A 191 ? 1.5021 1.4002 0.6946 0.0293 0.0056 -0.1745 191 TYR A OH 1537 N N . GLN A 192 ? 1.9572 1.6735 0.6987 -0.0265 -0.0213 -0.1817 192 GLN A N 1538 C CA . GLN A 192 ? 2.0336 1.7189 0.6969 -0.0400 -0.0357 -0.1734 192 GLN A CA 1539 C C . GLN A 192 ? 2.0058 1.6957 0.6909 -0.0542 -0.0675 -0.1411 192 GLN A C 1540 O O . GLN A 192 ? 2.0430 1.7060 0.7067 -0.0641 -0.1070 -0.1355 192 GLN A O 1541 C CB . GLN A 192 ? 2.0791 1.7683 0.6908 -0.0382 0.0043 -0.1766 192 GLN A CB 1542 C CG . GLN A 192 ? 2.1823 1.8297 0.6923 -0.0483 -0.0044 -0.1791 192 GLN A CG 1543 C CD . GLN A 192 ? 2.2521 1.8663 0.6992 -0.0392 0.0085 -0.2132 192 GLN A CD 1544 O OE1 . GLN A 192 ? 2.2442 1.8737 0.7052 -0.0242 0.0464 -0.2316 192 GLN A OE1 1545 N NE2 . GLN A 192 ? 2.3316 1.8992 0.7090 -0.0483 -0.0231 -0.2218 192 GLN A NE2 1546 N N . ASN A 193 ? 1.9453 1.6682 0.6740 -0.0553 -0.0505 -0.1201 193 ASN A N 1547 C CA . ASN A 193 ? 1.9224 1.6506 0.6756 -0.0666 -0.0751 -0.0885 193 ASN A CA 1548 C C . ASN A 193 ? 1.8722 1.6018 0.6827 -0.0672 -0.1110 -0.0813 193 ASN A C 1549 O O . ASN A 193 ? 1.8175 1.5676 0.6879 -0.0573 -0.1035 -0.0904 193 ASN A O 1550 C CB . ASN A 193 ? 1.8746 1.6380 0.6738 -0.0654 -0.0464 -0.0720 193 ASN A CB 1551 C CG . ASN A 193 ? 1.9198 1.6856 0.6698 -0.0659 -0.0095 -0.0762 193 ASN A CG 1552 O OD1 . ASN A 193 ? 2.0128 1.7515 0.6874 -0.0732 -0.0129 -0.0744 193 ASN A OD1 1553 N ND2 . ASN A 193 ? 1.8655 1.6640 0.6571 -0.0585 0.0257 -0.0814 193 ASN A ND2 1554 N N . PRO A 194 ? 1.8983 1.6070 0.6910 -0.0790 -0.1505 -0.0640 194 PRO A N 1555 C CA . PRO A 194 ? 1.8626 1.5718 0.7084 -0.0803 -0.1855 -0.0571 194 PRO A CA 1556 C C . PRO A 194 ? 1.7859 1.5278 0.7162 -0.0777 -0.1854 -0.0329 194 PRO A C 1557 O O . PRO A 194 ? 1.7251 1.4802 0.7165 -0.0722 -0.1945 -0.0340 194 PRO A O 1558 C CB . PRO A 194 ? 1.9352 1.6115 0.7275 -0.0950 -0.2271 -0.0459 194 PRO A CB 1559 C CG . PRO A 194 ? 1.9796 1.6506 0.7187 -0.1017 -0.2148 -0.0309 194 PRO A CG 1560 C CD . PRO A 194 ? 1.9741 1.6573 0.6950 -0.0919 -0.1657 -0.0497 194 PRO A CD 1561 N N . THR A 195 ? 1.7821 1.5347 0.7145 -0.0817 -0.1746 -0.0110 195 THR A N 1562 C CA . THR A 195 ? 1.7124 1.4924 0.7200 -0.0785 -0.1702 0.0103 195 THR A CA 1563 C C . THR A 195 ? 1.6783 1.4815 0.7003 -0.0720 -0.1270 0.0043 195 THR A C 1564 O O . THR A 195 ? 1.6974 1.4963 0.6781 -0.0771 -0.1099 0.0097 195 THR A O 1565 C CB . THR A 195 ? 1.7307 1.5029 0.7382 -0.0883 -0.1950 0.0433 195 THR A CB 1566 O OG1 . THR A 195 ? 1.7747 1.5217 0.7489 -0.0973 -0.2359 0.0477 195 THR A OG1 1567 C CG2 . THR A 195 ? 1.6701 1.4657 0.7617 -0.0834 -0.1973 0.0638 195 THR A CG2 1568 N N . THR A 196 ? 1.6227 1.4506 0.7028 -0.0618 -0.1103 -0.0059 196 THR A N 1569 C CA . THR A 196 ? 1.5871 1.4386 0.6830 -0.0562 -0.0715 -0.0149 196 THR A CA 1570 C C . THR A 196 ? 1.5185 1.3947 0.6866 -0.0518 -0.0640 -0.0035 196 THR A C 1571 O O . THR A 196 ? 1.4854 1.3611 0.6923 -0.0516 -0.0858 0.0114 196 THR A O 1572 C CB . THR A 196 ? 1.5877 1.4452 0.6735 -0.0469 -0.0530 -0.0443 196 THR A CB 1573 O OG1 . THR A 196 ? 1.5540 1.4163 0.6835 -0.0396 -0.0681 -0.0516 196 THR A OG1 1574 C CG2 . THR A 196 ? 1.6654 1.4953 0.6746 -0.0500 -0.0557 -0.0585 196 THR A CG2 1575 N N . TYR A 197 ? 1.4966 1.3943 0.6821 -0.0484 -0.0324 -0.0110 197 TYR A N 1576 C CA . TYR A 197 ? 1.4357 1.3544 0.6807 -0.0453 -0.0214 -0.0031 197 TYR A CA 1577 C C . TYR A 197 ? 1.4158 1.3584 0.6723 -0.0418 0.0111 -0.0186 197 TYR A C 1578 O O . TYR A 197 ? 1.4288 1.3723 0.6475 -0.0433 0.0280 -0.0300 197 TYR A O 1579 C CB . TYR A 197 ? 1.4468 1.3575 0.6969 -0.0533 -0.0252 0.0223 197 TYR A CB 1580 C CG . TYR A 197 ? 1.4806 1.3877 0.6901 -0.0617 -0.0050 0.0257 197 TYR A CG 1581 C CD1 . TYR A 197 ? 1.5505 1.4369 0.6966 -0.0685 -0.0125 0.0289 197 TYR A CD1 1582 C CD2 . TYR A 197 ? 1.4507 1.3743 0.6837 -0.0638 0.0216 0.0260 197 TYR A CD2 1583 C CE1 . TYR A 197 ? 1.5833 1.4670 0.6921 -0.0762 0.0080 0.0339 197 TYR A CE1 1584 C CE2 . TYR A 197 ? 1.4864 1.4078 0.6865 -0.0725 0.0408 0.0309 197 TYR A CE2 1585 C CZ . TYR A 197 ? 1.5580 1.4603 0.6965 -0.0783 0.0350 0.0355 197 TYR A CZ 1586 O OH . TYR A 197 ? 1.5944 1.4950 0.6993 -0.0871 0.0561 0.0421 197 TYR A OH 1587 N N . ILE A 198 ? 1.3751 1.3370 0.6837 -0.0374 0.0199 -0.0186 198 ILE A N 1588 C CA . ILE A 198 ? 1.3599 1.3453 0.6849 -0.0372 0.0478 -0.0285 198 ILE A CA 1589 C C . ILE A 198 ? 1.3443 1.3330 0.7034 -0.0418 0.0530 -0.0140 198 ILE A C 1590 O O . ILE A 198 ? 1.3338 1.3224 0.7296 -0.0370 0.0423 -0.0079 198 ILE A O 1591 C CB . ILE A 198 ? 1.3322 1.3388 0.6869 -0.0265 0.0540 -0.0468 198 ILE A CB 1592 C CG1 . ILE A 198 ? 1.3521 1.3514 0.6787 -0.0200 0.0471 -0.0617 198 ILE A CG1 1593 C CG2 . ILE A 198 ? 1.3183 1.3509 0.6886 -0.0277 0.0804 -0.0560 198 ILE A CG2 1594 C CD1 . ILE A 198 ? 1.3234 1.3386 0.6836 -0.0086 0.0470 -0.0752 198 ILE A CD1 1595 N N . SER A 199 ? 1.3500 1.3405 0.6977 -0.0510 0.0704 -0.0087 199 SER A N 1596 C CA . SER A 199 ? 1.3283 1.3192 0.7068 -0.0561 0.0779 0.0022 199 SER A CA 1597 C C . SER A 199 ? 1.2979 1.3135 0.6982 -0.0578 0.1005 -0.0118 199 SER A C 1598 O O . SER A 199 ? 1.3122 1.3407 0.6942 -0.0619 0.1164 -0.0203 199 SER A O 1599 C CB . SER A 199 ? 1.3706 1.3413 0.7246 -0.0669 0.0782 0.0223 199 SER A CB 1600 O OG . SER A 199 ? 1.3948 1.3703 0.7141 -0.0748 0.0955 0.0187 199 SER A OG 1601 N N . VAL A 200 ? 1.2709 1.2934 0.7102 -0.0547 0.1017 -0.0141 200 VAL A N 1602 C CA . VAL A 200 ? 1.2550 1.3002 0.7166 -0.0574 0.1189 -0.0272 200 VAL A CA 1603 C C . VAL A 200 ? 1.2552 1.2897 0.7377 -0.0651 0.1249 -0.0188 200 VAL A C 1604 O O . VAL A 200 ? 1.2486 1.2662 0.7469 -0.0606 0.1152 -0.0092 200 VAL A O 1605 C CB . VAL A 200 ? 1.2211 1.2847 0.7068 -0.0459 0.1149 -0.0417 200 VAL A CB 1606 C CG1 . VAL A 200 ? 1.2153 1.3059 0.7178 -0.0494 0.1305 -0.0556 200 VAL A CG1 1607 C CG2 . VAL A 200 ? 1.2293 1.2947 0.6970 -0.0366 0.1048 -0.0482 200 VAL A CG2 1608 N N . GLY A 201 ? 1.2637 1.3077 0.7481 -0.0766 0.1415 -0.0222 201 GLY A N 1609 C CA . GLY A 201 ? 1.2722 1.3034 0.7749 -0.0857 0.1483 -0.0168 201 GLY A CA 1610 C C . GLY A 201 ? 1.2576 1.3103 0.7775 -0.0944 0.1622 -0.0310 201 GLY A C 1611 O O . GLY A 201 ? 1.2795 1.3559 0.7934 -0.0990 0.1714 -0.0382 201 GLY A O 1612 N N . THR A 202 ? 1.2412 1.2853 0.7829 -0.0966 0.1635 -0.0349 202 THR A N 1613 C CA . THR A 202 ? 1.2286 1.2865 0.7857 -0.1086 0.1740 -0.0467 202 THR A CA 1614 C C . THR A 202 ? 1.2528 1.2799 0.8178 -0.1180 0.1782 -0.0403 202 THR A C 1615 O O . THR A 202 ? 1.2796 1.2785 0.8384 -0.1157 0.1751 -0.0245 202 THR A O 1616 C CB . THR A 202 ? 1.1956 1.2742 0.7691 -0.1008 0.1701 -0.0638 202 THR A CB 1617 O OG1 . THR A 202 ? 1.1720 1.2289 0.7538 -0.0919 0.1642 -0.0631 202 THR A OG1 1618 C CG2 . THR A 202 ? 1.1823 1.2866 0.7511 -0.0887 0.1648 -0.0694 202 THR A CG2 1619 N N . SER A 203 ? 1.2579 1.2896 0.8370 -0.1287 0.1844 -0.0524 203 SER A N 1620 C CA . SER A 203 ? 1.2776 1.2771 0.8649 -0.1361 0.1883 -0.0515 203 SER A CA 1621 C C . SER A 203 ? 1.2705 1.2429 0.8609 -0.1202 0.1824 -0.0456 203 SER A C 1622 O O . SER A 203 ? 1.2842 1.2232 0.8774 -0.1220 0.1854 -0.0347 203 SER A O 1623 C CB . SER A 203 ? 1.2748 1.2851 0.8739 -0.1463 0.1913 -0.0707 203 SER A CB 1624 O OG . SER A 203 ? 1.3079 1.2876 0.9113 -0.1434 0.1918 -0.0764 203 SER A OG 1625 N N . THR A 204 ? 1.2531 1.2404 0.8461 -0.1046 0.1748 -0.0518 204 THR A N 1626 C CA . THR A 204 ? 1.2480 1.2153 0.8495 -0.0889 0.1705 -0.0470 204 THR A CA 1627 C C . THR A 204 ? 1.2535 1.2279 0.8526 -0.0747 0.1589 -0.0349 204 THR A C 1628 O O . THR A 204 ? 1.3010 1.2548 0.9085 -0.0652 0.1545 -0.0213 204 THR A O 1629 C CB . THR A 204 ? 1.2168 1.1917 0.8258 -0.0827 0.1721 -0.0644 204 THR A CB 1630 O OG1 . THR A 204 ? 1.1753 1.1855 0.7820 -0.0778 0.1657 -0.0731 204 THR A OG1 1631 C CG2 . THR A 204 ? 1.2315 1.1966 0.8399 -0.0979 0.1810 -0.0784 204 THR A CG2 1632 N N . LEU A 205 ? 1.2334 1.2359 0.8228 -0.0731 0.1536 -0.0397 205 LEU A N 1633 C CA . LEU A 205 ? 1.2196 1.2276 0.8045 -0.0608 0.1410 -0.0314 205 LEU A CA 1634 C C . LEU A 205 ? 1.2357 1.2265 0.8057 -0.0640 0.1353 -0.0125 205 LEU A C 1635 O O . LEU A 205 ? 1.2540 1.2429 0.8088 -0.0764 0.1420 -0.0089 205 LEU A O 1636 C CB . LEU A 205 ? 1.2109 1.2506 0.7886 -0.0580 0.1384 -0.0439 205 LEU A CB 1637 C CG . LEU A 205 ? 1.2068 1.2522 0.7811 -0.0449 0.1247 -0.0402 205 LEU A CG 1638 C CD1 . LEU A 205 ? 1.1882 1.2275 0.7836 -0.0326 0.1188 -0.0381 205 LEU A CD1 1639 C CD2 . LEU A 205 ? 1.1922 1.2655 0.7590 -0.0428 0.1250 -0.0533 205 LEU A CD2 1640 N N . ASN A 206 ? 1.2150 1.1941 0.7900 -0.0534 0.1223 0.0006 206 ASN A N 1641 C CA . ASN A 206 ? 1.2296 1.1924 0.7892 -0.0554 0.1122 0.0201 206 ASN A CA 1642 C C . ASN A 206 ? 1.2122 1.1801 0.7688 -0.0450 0.0937 0.0253 206 ASN A C 1643 O O . ASN A 206 ? 1.2058 1.1603 0.7777 -0.0379 0.0816 0.0405 206 ASN A O 1644 C CB . ASN A 206 ? 1.2487 1.1830 0.8243 -0.0557 0.1135 0.0372 206 ASN A CB 1645 C CG . ASN A 206 ? 1.2732 1.1905 0.8317 -0.0597 0.1027 0.0597 206 ASN A CG 1646 O OD1 . ASN A 206 ? 1.2799 1.2036 0.8073 -0.0668 0.1001 0.0606 206 ASN A OD1 1647 N ND2 . ASN A 206 ? 1.3009 1.1960 0.8789 -0.0544 0.0968 0.0787 206 ASN A ND2 1648 N N . GLN A 207 ? 1.2015 1.1883 0.7400 -0.0444 0.0912 0.0129 207 GLN A N 1649 C CA . GLN A 207 ? 1.2014 1.1927 0.7381 -0.0351 0.0740 0.0134 207 GLN A CA 1650 C C . GLN A 207 ? 1.2489 1.2305 0.7501 -0.0395 0.0614 0.0221 207 GLN A C 1651 O O . GLN A 207 ? 1.2775 1.2574 0.7501 -0.0489 0.0703 0.0218 207 GLN A O 1652 C CB . GLN A 207 ? 1.1604 1.1759 0.7014 -0.0297 0.0789 -0.0067 207 GLN A CB 1653 C CG . GLN A 207 ? 1.1470 1.1667 0.6888 -0.0203 0.0626 -0.0087 207 GLN A CG 1654 C CD . GLN A 207 ? 1.1266 1.1691 0.6746 -0.0146 0.0690 -0.0273 207 GLN A CD 1655 O OE1 . GLN A 207 ? 1.1355 1.1867 0.6627 -0.0146 0.0696 -0.0375 207 GLN A OE1 1656 N NE2 . GLN A 207 ? 1.1127 1.1644 0.6886 -0.0092 0.0748 -0.0314 207 GLN A NE2 1657 N N . ARG A 208 ? 1.2699 1.2444 0.7727 -0.0335 0.0404 0.0304 208 ARG A N 1658 C CA . ARG A 208 ? 1.3258 1.2910 0.7902 -0.0369 0.0250 0.0341 208 ARG A CA 1659 C C . ARG A 208 ? 1.3186 1.2858 0.7926 -0.0289 0.0050 0.0311 208 ARG A C 1660 O O . ARG A 208 ? 1.3177 1.2782 0.8188 -0.0248 -0.0110 0.0458 208 ARG A O 1661 C CB . ARG A 208 ? 1.3748 1.3181 0.8242 -0.0438 0.0140 0.0574 208 ARG A CB 1662 C CG . ARG A 208 ? 1.4270 1.3585 0.8257 -0.0497 0.0000 0.0604 208 ARG A CG 1663 C CD . ARG A 208 ? 1.4694 1.3794 0.8591 -0.0547 -0.0189 0.0871 208 ARG A CD 1664 N NE . ARG A 208 ? 1.5183 1.4145 0.8500 -0.0625 -0.0298 0.0905 208 ARG A NE 1665 C CZ . ARG A 208 ? 1.5624 1.4544 0.8530 -0.0710 -0.0133 0.0895 208 ARG A CZ 1666 N NH1 . ARG A 208 ? 1.5379 1.4396 0.8425 -0.0739 0.0135 0.0853 208 ARG A NH1 1667 N NH2 . ARG A 208 ? 1.6354 1.5127 0.8691 -0.0772 -0.0238 0.0927 208 ARG A NH2 1668 N N . LEU A 209 ? 1.3155 1.2919 0.7704 -0.0264 0.0065 0.0128 209 LEU A N 1669 C CA . LEU A 209 ? 1.3013 1.2782 0.7653 -0.0195 -0.0111 0.0079 209 LEU A CA 1670 C C . LEU A 209 ? 1.3495 1.3073 0.7708 -0.0247 -0.0312 0.0106 209 LEU A C 1671 O O . LEU A 209 ? 1.3533 1.3041 0.7306 -0.0310 -0.0238 0.0062 209 LEU A O 1672 C CB . LEU A 209 ? 1.2814 1.2770 0.7513 -0.0126 0.0017 -0.0138 209 LEU A CB 1673 C CG . LEU A 209 ? 1.2516 1.2675 0.7520 -0.0093 0.0229 -0.0205 209 LEU A CG 1674 C CD1 . LEU A 209 ? 1.2374 1.2720 0.7336 -0.0043 0.0348 -0.0409 209 LEU A CD1 1675 C CD2 . LEU A 209 ? 1.2204 1.2391 0.7650 -0.0028 0.0180 -0.0110 209 LEU A CD2 1676 N N . VAL A 210 ? 1.3735 1.3225 0.8077 -0.0229 -0.0566 0.0184 210 VAL A N 1677 C CA . VAL A 210 ? 1.4489 1.3782 0.8423 -0.0282 -0.0798 0.0179 210 VAL A CA 1678 C C . VAL A 210 ? 1.4314 1.3620 0.8376 -0.0223 -0.0920 0.0049 210 VAL A C 1679 O O . VAL A 210 ? 1.3895 1.3319 0.8455 -0.0161 -0.0954 0.0100 210 VAL A O 1680 C CB . VAL A 210 ? 1.4970 1.4101 0.8899 -0.0352 -0.1059 0.0436 210 VAL A CB 1681 C CG1 . VAL A 210 ? 1.5036 1.4136 0.8863 -0.0405 -0.0928 0.0579 210 VAL A CG1 1682 C CG2 . VAL A 210 ? 1.4794 1.3996 0.9322 -0.0303 -0.1222 0.0591 210 VAL A CG2 1683 N N . PRO A 211 ? 1.4768 1.3939 0.8375 -0.0239 -0.0969 -0.0120 211 PRO A N 1684 C CA . PRO A 211 ? 1.4751 1.3885 0.8465 -0.0190 -0.1099 -0.0244 211 PRO A CA 1685 C C . PRO A 211 ? 1.4901 1.3922 0.8846 -0.0236 -0.1439 -0.0080 211 PRO A C 1686 O O . PRO A 211 ? 1.4986 1.3898 0.8829 -0.0318 -0.1621 0.0102 211 PRO A O 1687 C CB . PRO A 211 ? 1.5222 1.4170 0.8318 -0.0207 -0.1077 -0.0453 211 PRO A CB 1688 C CG . PRO A 211 ? 1.5395 1.4361 0.8121 -0.0246 -0.0865 -0.0451 211 PRO A CG 1689 C CD . PRO A 211 ? 1.5216 1.4240 0.8184 -0.0300 -0.0900 -0.0202 211 PRO A CD 1690 N N . ARG A 212 ? 1.4703 1.3756 0.8963 -0.0186 -0.1529 -0.0136 212 ARG A N 1691 C CA . ARG A 212 ? 1.4681 1.3707 0.9338 -0.0218 -0.1812 0.0035 212 ARG A CA 1692 C C . ARG A 212 ? 1.5073 1.3918 0.9597 -0.0239 -0.2012 -0.0105 212 ARG A C 1693 O O . ARG A 212 ? 1.4791 1.3692 0.9435 -0.0157 -0.1886 -0.0261 212 ARG A O 1694 C CB . ARG A 212 ? 1.4058 1.3343 0.9391 -0.0133 -0.1686 0.0163 212 ARG A CB 1695 C CG . ARG A 212 ? 1.4065 1.3421 0.9642 -0.0152 -0.1687 0.0405 212 ARG A CG 1696 C CD . ARG A 212 ? 1.3554 1.3132 0.9521 -0.0059 -0.1400 0.0441 212 ARG A CD 1697 N NE . ARG A 212 ? 1.3110 1.2835 0.9556 0.0021 -0.1365 0.0444 212 ARG A NE 1698 C CZ . ARG A 212 ? 1.2903 1.2775 0.9441 0.0105 -0.1129 0.0306 212 ARG A CZ 1699 N NH1 . ARG A 212 ? 1.2727 1.2641 0.8959 0.0118 -0.0907 0.0149 212 ARG A NH1 1700 N NH2 . ARG A 212 ? 1.2927 1.2916 0.9884 0.0172 -0.1118 0.0342 212 ARG A NH2 1701 N N . ILE A 213 ? 1.5790 1.4402 1.0050 -0.0354 -0.2334 -0.0046 213 ILE A N 1702 C CA . ILE A 213 ? 1.6212 1.4583 1.0284 -0.0405 -0.2574 -0.0181 213 ILE A CA 1703 C C . ILE A 213 ? 1.6085 1.4541 1.0812 -0.0425 -0.2802 -0.0011 213 ILE A C 1704 O O . ILE A 213 ? 1.6060 1.4628 1.1160 -0.0470 -0.2952 0.0247 213 ILE A O 1705 C CB . ILE A 213 ? 1.6884 1.4930 1.0296 -0.0540 -0.2846 -0.0211 213 ILE A CB 1706 C CG1 . ILE A 213 ? 1.7184 1.5172 0.9975 -0.0539 -0.2628 -0.0291 213 ILE A CG1 1707 C CG2 . ILE A 213 ? 1.7270 1.5016 1.0376 -0.0580 -0.3027 -0.0432 213 ILE A CG2 1708 C CD1 . ILE A 213 ? 1.7165 1.5187 0.9712 -0.0428 -0.2272 -0.0555 213 ILE A CD1 1709 N N . ALA A 214 ? 1.6007 1.4414 1.0897 -0.0387 -0.2814 -0.0145 214 ALA A N 1710 C CA . ALA A 214 ? 1.5827 1.4277 1.1299 -0.0423 -0.3042 -0.0002 214 ALA A CA 1711 C C . ALA A 214 ? 1.5888 1.4151 1.1275 -0.0403 -0.3072 -0.0220 214 ALA A C 1712 O O . ALA A 214 ? 1.5806 1.4021 1.0876 -0.0310 -0.2829 -0.0448 214 ALA A O 1713 C CB . ALA A 214 ? 1.5325 1.4129 1.1504 -0.0327 -0.2854 0.0198 214 ALA A CB 1714 N N . THR A 215 ? 1.5986 1.4143 1.1683 -0.0493 -0.3374 -0.0140 215 THR A N 1715 C CA . THR A 215 ? 1.6137 1.4077 1.1799 -0.0488 -0.3435 -0.0328 215 THR A CA 1716 C C . THR A 215 ? 1.5430 1.3642 1.1728 -0.0365 -0.3218 -0.0247 215 THR A C 1717 O O . THR A 215 ? 1.5196 1.3646 1.2115 -0.0375 -0.3267 0.0006 215 THR A O 1718 C CB . THR A 215 ? 1.6578 1.4253 1.2280 -0.0663 -0.3879 -0.0281 215 THR A CB 1719 O OG1 . THR A 215 ? 1.6955 1.4421 1.2090 -0.0788 -0.4104 -0.0297 215 THR A OG1 1720 C CG2 . THR A 215 ? 1.6970 1.4325 1.2501 -0.0666 -0.3942 -0.0523 215 THR A CG2 1721 N N . ARG A 216 ? 1.5089 1.3272 1.1230 -0.0242 -0.2971 -0.0454 216 ARG A N 1722 C CA . ARG A 216 ? 1.4341 1.2803 1.0984 -0.0110 -0.2723 -0.0384 216 ARG A CA 1723 C C . ARG A 216 ? 1.4386 1.2663 1.1079 -0.0064 -0.2733 -0.0534 216 ARG A C 1724 O O . ARG A 216 ? 1.4443 1.2409 1.0644 -0.0068 -0.2772 -0.0777 216 ARG A O 1725 C CB . ARG A 216 ? 1.4028 1.2716 1.0486 0.0017 -0.2364 -0.0456 216 ARG A CB 1726 C CG . ARG A 216 ? 1.3821 1.2683 1.0257 -0.0016 -0.2320 -0.0305 216 ARG A CG 1727 C CD . ARG A 216 ? 1.3551 1.2592 0.9763 0.0085 -0.1983 -0.0402 216 ARG A CD 1728 N NE . ARG A 216 ? 1.3956 1.2803 0.9512 0.0063 -0.1946 -0.0602 216 ARG A NE 1729 C CZ . ARG A 216 ? 1.4091 1.2900 0.9307 -0.0005 -0.1964 -0.0565 216 ARG A CZ 1730 N NH1 . ARG A 216 ? 1.3857 1.2798 0.9333 -0.0055 -0.2033 -0.0335 216 ARG A NH1 1731 N NH2 . ARG A 216 ? 1.4578 1.3211 0.9187 -0.0016 -0.1900 -0.0752 216 ARG A NH2 1732 N N . SER A 217 ? 1.4021 1.2477 1.1304 -0.0016 -0.2685 -0.0381 217 SER A N 1733 C CA . SER A 217 ? 1.4060 1.2386 1.1463 0.0052 -0.2646 -0.0486 217 SER A CA 1734 C C . SER A 217 ? 1.4114 1.2439 1.1128 0.0201 -0.2363 -0.0720 217 SER A C 1735 O O . SER A 217 ? 1.3894 1.2460 1.0778 0.0272 -0.2134 -0.0724 217 SER A O 1736 C CB . SER A 217 ? 1.3636 1.2236 1.1721 0.0103 -0.2562 -0.0249 217 SER A CB 1737 O OG . SER A 217 ? 1.3683 1.2383 1.2200 -0.0014 -0.2762 0.0004 217 SER A OG 1738 N N . LYS A 218 ? 1.4436 1.2485 1.1288 0.0246 -0.2381 -0.0910 218 LYS A N 1739 C CA . LYS A 218 ? 1.4536 1.2603 1.1105 0.0404 -0.2109 -0.1116 218 LYS A CA 1740 C C . LYS A 218 ? 1.4121 1.2536 1.1137 0.0543 -0.1875 -0.0991 218 LYS A C 1741 O O . LYS A 218 ? 1.3996 1.2481 1.1494 0.0535 -0.1942 -0.0813 218 LYS A O 1742 C CB . LYS A 218 ? 1.5109 1.2742 1.1366 0.0425 -0.2191 -0.1364 218 LYS A CB 1743 C CG . LYS A 218 ? 1.5657 1.2950 1.1276 0.0323 -0.2333 -0.1556 218 LYS A CG 1744 C CD . LYS A 218 ? 1.6276 1.3084 1.1549 0.0337 -0.2421 -0.1819 218 LYS A CD 1745 C CE . LYS A 218 ? 1.6994 1.3442 1.1610 0.0202 -0.2612 -0.1981 218 LYS A CE 1746 N NZ . LYS A 218 ? 1.7802 1.3758 1.1939 0.0245 -0.2619 -0.2294 218 LYS A NZ 1747 N N . VAL A 219 ? 1.3915 1.2553 1.0762 0.0660 -0.1605 -0.1074 219 VAL A N 1748 C CA . VAL A 219 ? 1.3259 1.2223 1.0440 0.0791 -0.1387 -0.0983 219 VAL A CA 1749 C C . VAL A 219 ? 1.3191 1.2179 1.0088 0.0926 -0.1175 -0.1193 219 VAL A C 1750 O O . VAL A 219 ? 1.3142 1.2184 0.9685 0.0922 -0.1065 -0.1306 219 VAL A O 1751 C CB . VAL A 219 ? 1.2982 1.2306 1.0345 0.0769 -0.1277 -0.0801 219 VAL A CB 1752 C CG1 . VAL A 219 ? 1.2644 1.2285 1.0279 0.0895 -0.1062 -0.0723 219 VAL A CG1 1753 C CG2 . VAL A 219 ? 1.2956 1.2271 1.0633 0.0648 -0.1470 -0.0583 219 VAL A CG2 1754 N N . ASN A 220 ? 1.3230 1.2183 1.0309 0.1047 -0.1116 -0.1232 220 ASN A N 1755 C CA . ASN A 220 ? 1.3387 1.2308 1.0243 0.1187 -0.0941 -0.1438 220 ASN A CA 1756 C C . ASN A 220 ? 1.3677 1.2247 1.0004 0.1149 -0.0983 -0.1679 220 ASN A C 1757 O O . ASN A 220 ? 1.3759 1.2403 0.9784 0.1215 -0.0797 -0.1828 220 ASN A O 1758 C CB . ASN A 220 ? 1.3249 1.2599 1.0141 0.1271 -0.0693 -0.1412 220 ASN A CB 1759 C CG . ASN A 220 ? 1.2995 1.2665 1.0336 0.1321 -0.0641 -0.1199 220 ASN A CG 1760 O OD1 . ASN A 220 ? 1.2344 1.2326 0.9748 0.1296 -0.0542 -0.1098 220 ASN A OD1 1761 N ND2 . ASN A 220 ? 1.3192 1.2763 1.0822 0.1389 -0.0704 -0.1132 220 ASN A ND2 1762 N N . GLY A 221 ? 1.3897 1.2087 1.0112 0.1034 -0.1232 -0.1710 221 GLY A N 1763 C CA . GLY A 221 ? 1.4309 1.2085 0.9978 0.0990 -0.1309 -0.1950 221 GLY A CA 1764 C C . GLY A 221 ? 1.4335 1.2111 0.9574 0.0865 -0.1346 -0.1973 221 GLY A C 1765 O O . GLY A 221 ? 1.4812 1.2246 0.9531 0.0819 -0.1407 -0.2166 221 GLY A O 1766 N N . GLN A 222 ? 1.3840 1.1975 0.9270 0.0811 -0.1307 -0.1778 222 GLN A N 1767 C CA . GLN A 222 ? 1.4011 1.2173 0.9068 0.0705 -0.1320 -0.1773 222 GLN A CA 1768 C C . GLN A 222 ? 1.3994 1.2234 0.9305 0.0559 -0.1538 -0.1537 222 GLN A C 1769 O O . GLN A 222 ? 1.3691 1.2169 0.9523 0.0574 -0.1542 -0.1342 222 GLN A O 1770 C CB . GLN A 222 ? 1.3681 1.2209 0.8693 0.0785 -0.1023 -0.1773 222 GLN A CB 1771 C CG . GLN A 222 ? 1.3739 1.2344 0.8714 0.0957 -0.0767 -0.1941 222 GLN A CG 1772 C CD . GLN A 222 ? 1.4324 1.2541 0.8801 0.0997 -0.0746 -0.2201 222 GLN A CD 1773 O OE1 . GLN A 222 ? 1.4581 1.2522 0.8577 0.0888 -0.0860 -0.2282 222 GLN A OE1 1774 N NE2 . GLN A 222 ? 1.4395 1.2585 0.8973 0.1161 -0.0595 -0.2331 222 GLN A NE2 1775 N N . SER A 223 ? 1.4418 1.2461 0.9357 0.0423 -0.1714 -0.1547 223 SER A N 1776 C CA . SER A 223 ? 1.4286 1.2432 0.9448 0.0289 -0.1910 -0.1311 223 SER A CA 1777 C C . SER A 223 ? 1.4057 1.2427 0.9038 0.0269 -0.1767 -0.1239 223 SER A C 1778 O O . SER A 223 ? 1.3735 1.2273 0.8983 0.0200 -0.1846 -0.1023 223 SER A O 1779 C CB . SER A 223 ? 1.4926 1.2695 0.9867 0.0133 -0.2266 -0.1329 223 SER A CB 1780 O OG . SER A 223 ? 1.5059 1.2676 1.0353 0.0119 -0.2436 -0.1309 223 SER A OG 1781 N N . GLY A 224 ? 1.4229 1.2598 0.8780 0.0333 -0.1546 -0.1413 224 GLY A N 1782 C CA . GLY A 224 ? 1.4018 1.2624 0.8440 0.0327 -0.1359 -0.1351 224 GLY A CA 1783 C C . GLY A 224 ? 1.3295 1.2295 0.8198 0.0418 -0.1143 -0.1241 224 GLY A C 1784 O O . GLY A 224 ? 1.3105 1.2197 0.8325 0.0516 -0.1077 -0.1263 224 GLY A O 1785 N N . ARG A 225 ? 1.3001 1.2211 0.7933 0.0384 -0.1037 -0.1123 225 ARG A N 1786 C CA . ARG A 225 ? 1.2520 1.2073 0.7868 0.0446 -0.0856 -0.1013 225 ARG A CA 1787 C C . ARG A 225 ? 1.2434 1.2173 0.7585 0.0458 -0.0608 -0.1064 225 ARG A C 1788 O O . ARG A 225 ? 1.2804 1.2430 0.7559 0.0390 -0.0600 -0.1099 225 ARG A O 1789 C CB . ARG A 225 ? 1.2188 1.1815 0.7903 0.0382 -0.0987 -0.0777 225 ARG A CB 1790 C CG . ARG A 225 ? 1.2123 1.1632 0.8156 0.0362 -0.1219 -0.0683 225 ARG A CG 1791 C CD . ARG A 225 ? 1.1733 1.1405 0.8162 0.0468 -0.1117 -0.0669 225 ARG A CD 1792 N NE . ARG A 225 ? 1.1661 1.1226 0.8429 0.0439 -0.1327 -0.0558 225 ARG A NE 1793 C CZ . ARG A 225 ? 1.1834 1.1154 0.8528 0.0431 -0.1479 -0.0660 225 ARG A CZ 1794 N NH1 . ARG A 225 ? 1.2097 1.1234 0.8365 0.0466 -0.1434 -0.0891 225 ARG A NH1 1795 N NH2 . ARG A 225 ? 1.1803 1.1051 0.8866 0.0387 -0.1670 -0.0529 225 ARG A NH2 1796 N N . MET A 226 ? 1.1988 1.2008 0.7411 0.0536 -0.0414 -0.1062 226 MET A N 1797 C CA . MET A 226 ? 1.1975 1.2206 0.7315 0.0527 -0.0198 -0.1077 226 MET A CA 1798 C C . MET A 226 ? 1.1729 1.2148 0.7427 0.0511 -0.0164 -0.0916 226 MET A C 1799 O O . MET A 226 ? 1.1603 1.2108 0.7643 0.0567 -0.0196 -0.0850 226 MET A O 1800 C CB . MET A 226 ? 1.2043 1.2455 0.7389 0.0627 0.0000 -0.1226 226 MET A CB 1801 C CG . MET A 226 ? 1.2643 1.2877 0.7631 0.0667 0.0028 -0.1407 226 MET A CG 1802 S SD . MET A 226 ? 1.3136 1.3312 0.7617 0.0588 0.0165 -0.1475 226 MET A SD 1803 C CE . MET A 226 ? 1.3714 1.3683 0.7863 0.0689 0.0221 -0.1705 226 MET A CE 1804 N N . GLU A 227 ? 1.1666 1.2129 0.7272 0.0438 -0.0091 -0.0850 227 GLU A N 1805 C CA . GLU A 227 ? 1.1330 1.1938 0.7228 0.0426 -0.0025 -0.0722 227 GLU A CA 1806 C C . GLU A 227 ? 1.1171 1.1964 0.6988 0.0408 0.0189 -0.0792 227 GLU A C 1807 O O . GLU A 227 ? 1.1528 1.2270 0.7067 0.0340 0.0247 -0.0821 227 GLU A O 1808 C CB . GLU A 227 ? 1.1510 1.1965 0.7426 0.0349 -0.0155 -0.0556 227 GLU A CB 1809 C CG . GLU A 227 ? 1.1404 1.1960 0.7673 0.0362 -0.0102 -0.0413 227 GLU A CG 1810 C CD . GLU A 227 ? 1.1550 1.1962 0.7925 0.0310 -0.0250 -0.0228 227 GLU A CD 1811 O OE1 . GLU A 227 ? 1.1705 1.1944 0.7836 0.0246 -0.0407 -0.0207 227 GLU A OE1 1812 O OE2 . GLU A 227 ? 1.1448 1.1919 0.8148 0.0338 -0.0210 -0.0099 227 GLU A OE2 1813 N N . PHE A 228 ? 1.0740 1.1749 0.6790 0.0461 0.0300 -0.0816 228 PHE A N 1814 C CA . PHE A 228 ? 1.0511 1.1716 0.6513 0.0435 0.0481 -0.0895 228 PHE A CA 1815 C C . PHE A 228 ? 1.0185 1.1432 0.6309 0.0376 0.0552 -0.0812 228 PHE A C 1816 O O . PHE A 228 ? 1.0072 1.1288 0.6404 0.0406 0.0508 -0.0717 228 PHE A O 1817 C CB . PHE A 228 ? 1.0467 1.1891 0.6607 0.0523 0.0546 -0.0992 228 PHE A CB 1818 C CG . PHE A 228 ? 1.0640 1.2014 0.6645 0.0589 0.0520 -0.1099 228 PHE A CG 1819 C CD1 . PHE A 228 ? 1.0837 1.2261 0.6622 0.0571 0.0637 -0.1203 228 PHE A CD1 1820 C CD2 . PHE A 228 ? 1.0660 1.1916 0.6758 0.0669 0.0391 -0.1092 228 PHE A CD2 1821 C CE1 . PHE A 228 ? 1.1129 1.2478 0.6768 0.0646 0.0639 -0.1314 228 PHE A CE1 1822 C CE2 . PHE A 228 ? 1.0950 1.2112 0.6908 0.0733 0.0373 -0.1207 228 PHE A CE2 1823 C CZ . PHE A 228 ? 1.1177 1.2377 0.6891 0.0729 0.0503 -0.1325 228 PHE A CZ 1824 N N . PHE A 229 ? 1.0085 1.1386 0.6075 0.0293 0.0673 -0.0848 229 PHE A N 1825 C CA . PHE A 229 ? 0.9979 1.1271 0.6039 0.0221 0.0752 -0.0790 229 PHE A CA 1826 C C . PHE A 229 ? 0.9865 1.1375 0.5934 0.0172 0.0895 -0.0891 229 PHE A C 1827 O O . PHE A 229 ? 0.9780 1.1448 0.5788 0.0183 0.0943 -0.0985 229 PHE A O 1828 C CB . PHE A 229 ? 1.0240 1.1326 0.6130 0.0134 0.0732 -0.0698 229 PHE A CB 1829 C CG . PHE A 229 ? 1.0358 1.1240 0.6276 0.0163 0.0567 -0.0571 229 PHE A CG 1830 C CD1 . PHE A 229 ? 1.0650 1.1433 0.6391 0.0180 0.0438 -0.0584 229 PHE A CD1 1831 C CD2 . PHE A 229 ? 1.0346 1.1131 0.6475 0.0173 0.0539 -0.0440 229 PHE A CD2 1832 C CE1 . PHE A 229 ? 1.0783 1.1387 0.6568 0.0188 0.0253 -0.0461 229 PHE A CE1 1833 C CE2 . PHE A 229 ? 1.0524 1.1159 0.6743 0.0197 0.0375 -0.0303 229 PHE A CE2 1834 C CZ . PHE A 229 ? 1.0702 1.1252 0.6754 0.0196 0.0216 -0.0310 229 PHE A CZ 1835 N N . TRP A 230 ? 0.9830 1.1342 0.5988 0.0117 0.0962 -0.0873 230 TRP A N 1836 C CA . TRP A 230 ? 0.9737 1.1443 0.5919 0.0045 0.1070 -0.0964 230 TRP A CA 1837 C C . TRP A 230 ? 0.9748 1.1327 0.5914 -0.0065 0.1144 -0.0936 230 TRP A C 1838 O O . TRP A 230 ? 0.9660 1.1016 0.5842 -0.0056 0.1122 -0.0844 230 TRP A O 1839 C CB . TRP A 230 ? 0.9527 1.1429 0.5864 0.0117 0.1055 -0.1021 230 TRP A CB 1840 C CG . TRP A 230 ? 0.9382 1.1167 0.5814 0.0171 0.1027 -0.0960 230 TRP A CG 1841 C CD1 . TRP A 230 ? 0.9329 1.1021 0.5850 0.0276 0.0946 -0.0878 230 TRP A CD1 1842 C CD2 . TRP A 230 ? 0.9356 1.1105 0.5806 0.0123 0.1093 -0.0979 230 TRP A CD2 1843 N NE1 . TRP A 230 ? 0.9253 1.0872 0.5862 0.0305 0.0977 -0.0831 230 TRP A NE1 1844 C CE2 . TRP A 230 ? 0.9356 1.0993 0.5897 0.0217 0.1071 -0.0902 230 TRP A CE2 1845 C CE3 . TRP A 230 ? 0.9510 1.1296 0.5904 0.0003 0.1171 -0.1057 230 TRP A CE3 1846 C CZ2 . TRP A 230 ? 0.9551 1.1102 0.6093 0.0211 0.1146 -0.0909 230 TRP A CZ2 1847 C CZ3 . TRP A 230 ? 0.9654 1.1330 0.6035 -0.0014 0.1221 -0.1077 230 TRP A CZ3 1848 C CH2 . TRP A 230 ? 0.9650 1.1203 0.6087 0.0096 0.1219 -0.1008 230 TRP A CH2 1849 N N . THR A 231 ? 0.9724 1.1448 0.5885 -0.0170 0.1231 -0.1013 231 THR A N 1850 C CA . THR A 231 ? 0.9766 1.1374 0.5932 -0.0283 0.1300 -0.1019 231 THR A CA 1851 C C . THR A 231 ? 0.9812 1.1666 0.6043 -0.0371 0.1344 -0.1133 231 THR A C 1852 O O . THR A 231 ? 0.9788 1.1919 0.6081 -0.0344 0.1332 -0.1187 231 THR A O 1853 C CB . THR A 231 ? 0.9961 1.1373 0.6014 -0.0386 0.1350 -0.0939 231 THR A CB 1854 O OG1 . THR A 231 ? 0.9905 1.1108 0.5981 -0.0463 0.1404 -0.0923 231 THR A OG1 1855 C CG2 . THR A 231 ? 1.0036 1.1634 0.6034 -0.0489 0.1424 -0.0980 231 THR A CG2 1856 N N . ILE A 232 ? 1.0011 1.1754 0.6239 -0.0475 0.1389 -0.1169 232 ILE A N 1857 C CA . ILE A 232 ? 1.0113 1.2053 0.6395 -0.0603 0.1412 -0.1273 232 ILE A CA 1858 C C . ILE A 232 ? 1.0260 1.2096 0.6513 -0.0770 0.1493 -0.1251 232 ILE A C 1859 O O . ILE A 232 ? 1.0539 1.2069 0.6728 -0.0825 0.1533 -0.1216 232 ILE A O 1860 C CB . ILE A 232 ? 1.0241 1.2100 0.6499 -0.0614 0.1391 -0.1351 232 ILE A CB 1861 C CG1 . ILE A 232 ? 1.0037 1.2165 0.6351 -0.0515 0.1310 -0.1397 232 ILE A CG1 1862 C CG2 . ILE A 232 ? 1.0480 1.2325 0.6726 -0.0809 0.1423 -0.1442 232 ILE A CG2 1863 C CD1 . ILE A 232 ? 0.9910 1.2077 0.6265 -0.0336 0.1266 -0.1318 232 ILE A CD1 1864 N N . LEU A 233 ? 1.0346 1.2435 0.6664 -0.0844 0.1530 -0.1259 233 LEU A N 1865 C CA . LEU A 233 ? 1.0539 1.2568 0.6850 -0.1014 0.1621 -0.1221 233 LEU A CA 1866 C C . LEU A 233 ? 1.0637 1.2756 0.7057 -0.1185 0.1620 -0.1317 233 LEU A C 1867 O O . LEU A 233 ? 1.0478 1.2935 0.7041 -0.1207 0.1579 -0.1388 233 LEU A O 1868 C CB . LEU A 233 ? 1.0532 1.2807 0.6865 -0.1008 0.1684 -0.1181 233 LEU A CB 1869 C CG . LEU A 233 ? 1.0789 1.2983 0.7059 -0.1144 0.1800 -0.1092 233 LEU A CG 1870 C CD1 . LEU A 233 ? 1.0943 1.2746 0.7005 -0.1110 0.1798 -0.0974 233 LEU A CD1 1871 C CD2 . LEU A 233 ? 1.0762 1.3260 0.7061 -0.1116 0.1884 -0.1080 233 LEU A CD2 1872 N N . LYS A 234 ? 1.1066 1.2876 0.7428 -0.1307 0.1654 -0.1317 234 LYS A N 1873 C CA . LYS A 234 ? 1.1656 1.3487 0.8090 -0.1494 0.1639 -0.1422 234 LYS A CA 1874 C C . LYS A 234 ? 1.1778 1.3927 0.8397 -0.1660 0.1681 -0.1408 234 LYS A C 1875 O O . LYS A 234 ? 1.1916 1.4221 0.8569 -0.1618 0.1752 -0.1315 234 LYS A O 1876 C CB . LYS A 234 ? 1.2279 1.3647 0.8604 -0.1585 0.1686 -0.1424 234 LYS A CB 1877 C CG . LYS A 234 ? 1.2430 1.3469 0.8614 -0.1431 0.1674 -0.1437 234 LYS A CG 1878 C CD . LYS A 234 ? 1.2491 1.3676 0.8635 -0.1319 0.1592 -0.1542 234 LYS A CD 1879 C CE . LYS A 234 ? 1.2955 1.4273 0.9099 -0.1473 0.1528 -0.1697 234 LYS A CE 1880 N NZ . LYS A 234 ? 1.3522 1.4453 0.9530 -0.1592 0.1560 -0.1802 234 LYS A NZ 1881 N N . PRO A 235 ? 1.1932 1.4183 0.8672 -0.1853 0.1641 -0.1500 235 PRO A N 1882 C CA . PRO A 235 ? 1.1792 1.4355 0.8765 -0.2021 0.1695 -0.1459 235 PRO A CA 1883 C C . PRO A 235 ? 1.2049 1.4344 0.8984 -0.2152 0.1822 -0.1350 235 PRO A C 1884 O O . PRO A 235 ? 1.2096 1.3949 0.8862 -0.2165 0.1836 -0.1341 235 PRO A O 1885 C CB . PRO A 235 ? 1.1876 1.4596 0.8993 -0.2202 0.1581 -0.1583 235 PRO A CB 1886 C CG . PRO A 235 ? 1.2013 1.4384 0.8891 -0.2161 0.1495 -0.1697 235 PRO A CG 1887 C CD . PRO A 235 ? 1.1981 1.4052 0.8644 -0.1940 0.1552 -0.1636 235 PRO A CD 1888 N N . ASN A 236 ? 1.2116 1.4674 0.9211 -0.2235 0.1926 -0.1254 236 ASN A N 1889 C CA . ASN A 236 ? 1.2415 1.4750 0.9461 -0.2353 0.2060 -0.1119 236 ASN A CA 1890 C C . ASN A 236 ? 1.2581 1.4571 0.9342 -0.2193 0.2109 -0.1009 236 ASN A C 1891 O O . ASN A 236 ? 1.3028 1.4775 0.9707 -0.2280 0.2202 -0.0880 236 ASN A O 1892 C CB . ASN A 236 ? 1.2790 1.4831 0.9887 -0.2589 0.2044 -0.1154 236 ASN A CB 1893 C CG . ASN A 236 ? 1.3081 1.5397 1.0473 -0.2840 0.2099 -0.1120 236 ASN A CG 1894 O OD1 . ASN A 236 ? 1.3203 1.5794 1.0713 -0.2857 0.2226 -0.0998 236 ASN A OD1 1895 N ND2 . ASN A 236 ? 1.3359 1.5583 1.0867 -0.3045 0.2009 -0.1227 236 ASN A ND2 1896 N N . ASP A 237 ? 1.2290 1.4254 0.8911 -0.1970 0.2035 -0.1043 237 ASP A N 1897 C CA . ASP A 237 ? 1.2346 1.4013 0.8728 -0.1827 0.2051 -0.0932 237 ASP A CA 1898 C C . ASP A 237 ? 1.2134 1.4038 0.8435 -0.1706 0.2102 -0.0870 237 ASP A C 1899 O O . ASP A 237 ? 1.1792 1.4080 0.8231 -0.1668 0.2112 -0.0938 237 ASP A O 1900 C CB . ASP A 237 ? 1.2372 1.3811 0.8657 -0.1668 0.1942 -0.0992 237 ASP A CB 1901 C CG . ASP A 237 ? 1.2510 1.3587 0.8610 -0.1563 0.1941 -0.0858 237 ASP A CG 1902 O OD1 . ASP A 237 ? 1.2691 1.3555 0.8725 -0.1661 0.2012 -0.0728 237 ASP A OD1 1903 O OD2 . ASP A 237 ? 1.2356 1.3372 0.8395 -0.1385 0.1861 -0.0868 237 ASP A OD2 1904 N N . ALA A 238 ? 1.2293 1.3953 0.8364 -0.1646 0.2133 -0.0738 238 ALA A N 1905 C CA . ALA A 238 ? 1.2467 1.4269 0.8376 -0.1547 0.2190 -0.0681 238 ALA A CA 1906 C C . ALA A 238 ? 1.2354 1.3959 0.8059 -0.1354 0.2074 -0.0663 238 ALA A C 1907 O O . ALA A 238 ? 1.2574 1.3850 0.8207 -0.1335 0.2001 -0.0596 238 ALA A O 1908 C CB . ALA A 238 ? 1.2799 1.4489 0.8565 -0.1674 0.2324 -0.0523 238 ALA A CB 1909 N N . ILE A 239 ? 1.2139 1.3943 0.7783 -0.1211 0.2055 -0.0721 239 ILE A N 1910 C CA . ILE A 239 ? 1.2044 1.3658 0.7474 -0.1049 0.1944 -0.0690 239 ILE A CA 1911 C C . ILE A 239 ? 1.2451 1.3996 0.7568 -0.1043 0.2012 -0.0597 239 ILE A C 1912 O O . ILE A 239 ? 1.2385 1.4157 0.7477 -0.1079 0.2155 -0.0620 239 ILE A O 1913 C CB . ILE A 239 ? 1.1677 1.3471 0.7213 -0.0886 0.1850 -0.0815 239 ILE A CB 1914 C CG1 . ILE A 239 ? 1.1716 1.3260 0.7098 -0.0749 0.1704 -0.0769 239 ILE A CG1 1915 C CG2 . ILE A 239 ? 1.1574 1.3687 0.7125 -0.0833 0.1939 -0.0892 239 ILE A CG2 1916 C CD1 . ILE A 239 ? 1.1374 1.3020 0.6911 -0.0610 0.1597 -0.0863 239 ILE A CD1 1917 N N . ASN A 240 ? 1.2676 1.3909 0.7555 -0.0998 0.1909 -0.0487 240 ASN A N 1918 C CA . ASN A 240 ? 1.3107 1.4202 0.7616 -0.1011 0.1945 -0.0379 240 ASN A CA 1919 C C . ASN A 240 ? 1.3076 1.4029 0.7357 -0.0866 0.1784 -0.0388 240 ASN A C 1920 O O . ASN A 240 ? 1.3077 1.3835 0.7416 -0.0812 0.1618 -0.0334 240 ASN A O 1921 C CB . ASN A 240 ? 1.3499 1.4308 0.7905 -0.1131 0.1947 -0.0191 240 ASN A CB 1922 C CG . ASN A 240 ? 1.3747 1.4647 0.8348 -0.1302 0.2108 -0.0165 240 ASN A CG 1923 O OD1 . ASN A 240 ? 1.3657 1.4804 0.8268 -0.1369 0.2271 -0.0201 240 ASN A OD1 1924 N ND2 . ASN A 240 ? 1.3886 1.4579 0.8660 -0.1374 0.2068 -0.0102 240 ASN A ND2 1925 N N . PHE A 241 ? 1.3006 1.4048 0.7039 -0.0805 0.1838 -0.0456 241 PHE A N 1926 C CA . PHE A 241 ? 1.3004 1.3884 0.6776 -0.0688 0.1682 -0.0478 241 PHE A CA 1927 C C . PHE A 241 ? 1.3556 1.4206 0.6837 -0.0739 0.1684 -0.0363 241 PHE A C 1928 O O . PHE A 241 ? 1.3724 1.4432 0.6828 -0.0826 0.1872 -0.0320 241 PHE A O 1929 C CB . PHE A 241 ? 1.2783 1.3880 0.6604 -0.0564 0.1723 -0.0664 241 PHE A CB 1930 C CG . PHE A 241 ? 1.2380 1.3671 0.6630 -0.0497 0.1672 -0.0760 241 PHE A CG 1931 C CD1 . PHE A 241 ? 1.2246 1.3417 0.6600 -0.0403 0.1475 -0.0767 241 PHE A CD1 1932 C CD2 . PHE A 241 ? 1.2230 1.3829 0.6783 -0.0535 0.1815 -0.0830 241 PHE A CD2 1933 C CE1 . PHE A 241 ? 1.1978 1.3317 0.6689 -0.0342 0.1438 -0.0842 241 PHE A CE1 1934 C CE2 . PHE A 241 ? 1.1891 1.3660 0.6795 -0.0478 0.1752 -0.0911 241 PHE A CE2 1935 C CZ . PHE A 241 ? 1.1745 1.3376 0.6707 -0.0378 0.1572 -0.0916 241 PHE A CZ 1936 N N . GLU A 242 ? 1.3758 1.4151 0.6829 -0.0692 0.1466 -0.0298 242 GLU A N 1937 C CA . GLU A 242 ? 1.4359 1.4522 0.6895 -0.0719 0.1416 -0.0218 242 GLU A CA 1938 C C . GLU A 242 ? 1.4394 1.4400 0.6789 -0.0617 0.1173 -0.0279 242 GLU A C 1939 O O . GLU A 242 ? 1.4123 1.4067 0.6804 -0.0578 0.0979 -0.0229 242 GLU A O 1940 C CB . GLU A 242 ? 1.4692 1.4634 0.7098 -0.0837 0.1365 0.0022 242 GLU A CB 1941 C CG . GLU A 242 ? 1.5388 1.5110 0.7181 -0.0887 0.1340 0.0122 242 GLU A CG 1942 C CD . GLU A 242 ? 1.5811 1.5292 0.7486 -0.0987 0.1234 0.0389 242 GLU A CD 1943 O OE1 . GLU A 242 ? 1.5935 1.5453 0.7812 -0.1080 0.1377 0.0501 242 GLU A OE1 1944 O OE2 . GLU A 242 ? 1.6163 1.5407 0.7544 -0.0979 0.0998 0.0495 242 GLU A OE2 1945 N N . SER A 243 ? 1.4713 1.4647 0.6679 -0.0574 0.1190 -0.0388 243 SER A N 1946 C CA . SER A 243 ? 1.4832 1.4582 0.6633 -0.0496 0.0946 -0.0456 243 SER A CA 1947 C C . SER A 243 ? 1.5537 1.5034 0.6665 -0.0515 0.0896 -0.0481 243 SER A C 1948 O O . SER A 243 ? 1.5982 1.5484 0.6742 -0.0557 0.1108 -0.0492 243 SER A O 1949 C CB . SER A 243 ? 1.4351 1.4282 0.6460 -0.0369 0.0971 -0.0660 243 SER A CB 1950 O OG . SER A 243 ? 1.4325 1.4059 0.6315 -0.0308 0.0724 -0.0714 243 SER A OG 1951 N N . ASN A 244 ? 1.5882 1.5155 0.6862 -0.0488 0.0609 -0.0490 244 ASN A N 1952 C CA . ASN A 244 ? 1.6534 1.5507 0.6854 -0.0509 0.0479 -0.0533 244 ASN A CA 1953 C C . ASN A 244 ? 1.6491 1.5392 0.6681 -0.0404 0.0437 -0.0781 244 ASN A C 1954 O O . ASN A 244 ? 1.6942 1.5581 0.6534 -0.0413 0.0375 -0.0873 244 ASN A O 1955 C CB . ASN A 244 ? 1.6757 1.5495 0.7006 -0.0583 0.0124 -0.0333 244 ASN A CB 1956 C CG . ASN A 244 ? 1.7535 1.6070 0.7229 -0.0697 0.0097 -0.0161 244 ASN A CG 1957 O OD1 . ASN A 244 ? 1.7854 1.6445 0.7277 -0.0732 0.0371 -0.0161 244 ASN A OD1 1958 N ND2 . ASN A 244 ? 1.7957 1.6263 0.7486 -0.0761 -0.0238 0.0002 244 ASN A ND2 1959 N N . GLY A 245 ? 1.5925 1.5039 0.6661 -0.0306 0.0472 -0.0886 245 GLY A N 1960 C CA . GLY A 245 ? 1.5881 1.4920 0.6647 -0.0202 0.0378 -0.1083 245 GLY A CA 1961 C C . GLY A 245 ? 1.5231 1.4449 0.6677 -0.0145 0.0262 -0.1050 245 GLY A C 1962 O O . GLY A 245 ? 1.4907 1.4233 0.6715 -0.0194 0.0202 -0.0870 245 GLY A O 1963 N N . ASN A 246 ? 1.5003 1.4232 0.6607 -0.0038 0.0241 -0.1219 246 ASN A N 1964 C CA . ASN A 246 ? 1.4397 1.3766 0.6595 0.0023 0.0124 -0.1194 246 ASN A CA 1965 C C . ASN A 246 ? 1.3653 1.3385 0.6346 0.0065 0.0340 -0.1170 246 ASN A C 1966 O O . ASN A 246 ? 1.3321 1.3183 0.6485 0.0104 0.0267 -0.1120 246 ASN A O 1967 C CB . ASN A 246 ? 1.4332 1.3570 0.6701 -0.0050 -0.0182 -0.1003 246 ASN A CB 1968 C CG . ASN A 246 ? 1.4890 1.3773 0.6796 -0.0114 -0.0452 -0.1010 246 ASN A CG 1969 O OD1 . ASN A 246 ? 1.4982 1.3733 0.6990 -0.0090 -0.0661 -0.1062 246 ASN A OD1 1970 N ND2 . ASN A 246 ? 1.5301 1.4021 0.6696 -0.0206 -0.0462 -0.0948 246 ASN A ND2 1971 N N . PHE A 247 ? 1.3684 1.3578 0.6259 0.0054 0.0605 -0.1209 247 PHE A N 1972 C CA . PHE A 247 ? 1.3144 1.3372 0.6142 0.0059 0.0797 -0.1179 247 PHE A CA 1973 C C . PHE A 247 ? 1.2887 1.3339 0.6130 0.0185 0.0939 -0.1343 247 PHE A C 1974 O O . PHE A 247 ? 1.3147 1.3563 0.6136 0.0252 0.1057 -0.1486 247 PHE A O 1975 C CB . PHE A 247 ? 1.3387 1.3678 0.6162 -0.0039 0.0994 -0.1111 247 PHE A CB 1976 C CG . PHE A 247 ? 1.3088 1.3700 0.6264 -0.0067 0.1180 -0.1079 247 PHE A CG 1977 C CD1 . PHE A 247 ? 1.2657 1.3377 0.6273 -0.0074 0.1097 -0.1005 247 PHE A CD1 1978 C CD2 . PHE A 247 ? 1.3343 1.4141 0.6440 -0.0097 0.1442 -0.1119 247 PHE A CD2 1979 C CE1 . PHE A 247 ? 1.2443 1.3424 0.6377 -0.0117 0.1250 -0.0991 247 PHE A CE1 1980 C CE2 . PHE A 247 ? 1.2990 1.4079 0.6462 -0.0147 0.1587 -0.1087 247 PHE A CE2 1981 C CZ . PHE A 247 ? 1.2602 1.3769 0.6474 -0.0161 0.1480 -0.1031 247 PHE A CZ 1982 N N . ILE A 248 ? 1.2410 1.3079 0.6142 0.0225 0.0923 -0.1318 248 ILE A N 1983 C CA . ILE A 248 ? 1.2112 1.3038 0.6130 0.0337 0.1051 -0.1437 248 ILE A CA 1984 C C . ILE A 248 ? 1.1924 1.3159 0.6175 0.0275 0.1234 -0.1392 248 ILE A C 1985 O O . ILE A 248 ? 1.1635 1.2965 0.6163 0.0222 0.1184 -0.1298 248 ILE A O 1986 C CB . ILE A 248 ? 1.1804 1.2747 0.6172 0.0421 0.0889 -0.1433 248 ILE A CB 1987 C CG1 . ILE A 248 ? 1.1994 1.2598 0.6175 0.0425 0.0653 -0.1418 248 ILE A CG1 1988 C CG2 . ILE A 248 ? 1.1726 1.2871 0.6310 0.0556 0.0997 -0.1559 248 ILE A CG2 1989 C CD1 . ILE A 248 ? 1.2588 1.2952 0.6332 0.0463 0.0658 -0.1557 248 ILE A CD1 1990 N N . ALA A 249 ? 1.2238 1.3614 0.6362 0.0272 0.1451 -0.1456 249 ALA A N 1991 C CA . ALA A 249 ? 1.2262 1.3898 0.6557 0.0173 0.1620 -0.1397 249 ALA A CA 1992 C C . ALA A 249 ? 1.1883 1.3884 0.6649 0.0228 0.1686 -0.1443 249 ALA A C 1993 O O . ALA A 249 ? 1.1798 1.3899 0.6693 0.0363 0.1699 -0.1541 249 ALA A O 1994 C CB . ALA A 249 ? 1.2705 1.4358 0.6687 0.0136 0.1837 -0.1421 249 ALA A CB 1995 N N . PRO A 250 ? 1.1775 1.3961 0.6792 0.0120 0.1717 -0.1370 250 PRO A N 1996 C CA . PRO A 250 ? 1.1528 1.4080 0.6958 0.0153 0.1774 -0.1413 250 PRO A CA 1997 C C . PRO A 250 ? 1.1701 1.4525 0.7198 0.0196 0.1986 -0.1482 250 PRO A C 1998 O O . PRO A 250 ? 1.2215 1.5010 0.7492 0.0125 0.2140 -0.1461 250 PRO A O 1999 C CB . PRO A 250 ? 1.1311 1.3945 0.6903 -0.0005 0.1772 -0.1329 250 PRO A CB 2000 C CG . PRO A 250 ? 1.1514 1.3844 0.6797 -0.0113 0.1757 -0.1235 250 PRO A CG 2001 C CD . PRO A 250 ? 1.1770 1.3808 0.6729 -0.0024 0.1664 -0.1247 250 PRO A CD 2002 N N . GLU A 251 ? 1.1508 1.4591 0.7312 0.0319 0.2002 -0.1550 251 GLU A N 2003 C CA . GLU A 251 ? 1.1574 1.5026 0.7615 0.0347 0.2204 -0.1585 251 GLU A CA 2004 C C . GLU A 251 ? 1.1225 1.5037 0.7710 0.0272 0.2164 -0.1543 251 GLU A C 2005 O O . GLU A 251 ? 1.1109 1.5165 0.7754 0.0144 0.2284 -0.1502 251 GLU A O 2006 C CB . GLU A 251 ? 1.1829 1.5330 0.7920 0.0555 0.2266 -0.1688 251 GLU A CB 2007 C CG . GLU A 251 ? 1.2059 1.5880 0.8312 0.0599 0.2531 -0.1721 251 GLU A CG 2008 C CD . GLU A 251 ? 1.2280 1.6168 0.8655 0.0825 0.2606 -0.1823 251 GLU A CD 2009 O OE1 . GLU A 251 ? 1.2471 1.6096 0.8736 0.0940 0.2452 -0.1877 251 GLU A OE1 2010 O OE2 . GLU A 251 ? 1.2282 1.6483 0.8888 0.0888 0.2828 -0.1842 251 GLU A OE2 2011 N N . TYR A 252 ? 1.0924 1.4757 0.7592 0.0342 0.1986 -0.1548 252 TYR A N 2012 C CA . TYR A 252 ? 1.0658 1.4791 0.7685 0.0277 0.1907 -0.1516 252 TYR A CA 2013 C C . TYR A 252 ? 1.0525 1.4441 0.7455 0.0177 0.1741 -0.1471 252 TYR A C 2014 O O . TYR A 252 ? 1.0265 1.3873 0.6997 0.0237 0.1634 -0.1462 252 TYR A O 2015 C CB . TYR A 252 ? 1.0525 1.4894 0.7854 0.0446 0.1848 -0.1545 252 TYR A CB 2016 C CG . TYR A 252 ? 1.0744 1.5353 0.8243 0.0572 0.2023 -0.1589 252 TYR A CG 2017 C CD1 . TYR A 252 ? 1.0754 1.5799 0.8609 0.0517 0.2139 -0.1563 252 TYR A CD1 2018 C CD2 . TYR A 252 ? 1.0913 1.5309 0.8231 0.0747 0.2077 -0.1658 252 TYR A CD2 2019 C CE1 . TYR A 252 ? 1.0804 1.6090 0.8858 0.0649 0.2325 -0.1593 252 TYR A CE1 2020 C CE2 . TYR A 252 ? 1.1030 1.5622 0.8497 0.0881 0.2265 -0.1710 252 TYR A CE2 2021 C CZ . TYR A 252 ? 1.1015 1.6065 0.8865 0.0840 0.2400 -0.1672 252 TYR A CZ 2022 O OH . TYR A 252 ? 1.1134 1.6402 0.9177 0.0988 0.2614 -0.1713 252 TYR A OH 2023 N N . ALA A 253 ? 1.0527 1.4608 0.7614 0.0022 0.1729 -0.1443 253 ALA A N 2024 C CA . ALA A 253 ? 1.0474 1.4389 0.7510 -0.0063 0.1594 -0.1418 253 ALA A CA 2025 C C . ALA A 253 ? 1.0343 1.4581 0.7674 -0.0098 0.1511 -0.1432 253 ALA A C 2026 O O . ALA A 253 ? 1.0320 1.4922 0.7921 -0.0102 0.1565 -0.1441 253 ALA A O 2027 C CB . ALA A 253 ? 1.0682 1.4396 0.7546 -0.0242 0.1653 -0.1380 253 ALA A CB 2028 N N . TYR A 254 ? 1.0271 1.4383 0.7552 -0.0122 0.1382 -0.1427 254 TYR A N 2029 C CA . TYR A 254 ? 1.0080 1.4458 0.7565 -0.0152 0.1275 -0.1440 254 TYR A CA 2030 C C . TYR A 254 ? 1.0157 1.4529 0.7628 -0.0366 0.1256 -0.1462 254 TYR A C 2031 O O . TYR A 254 ? 1.0162 1.4207 0.7413 -0.0444 0.1262 -0.1464 254 TYR A O 2032 C CB . TYR A 254 ? 0.9992 1.4242 0.7405 -0.0027 0.1148 -0.1424 254 TYR A CB 2033 C CG . TYR A 254 ? 0.9894 1.4173 0.7375 0.0178 0.1135 -0.1404 254 TYR A CG 2034 C CD1 . TYR A 254 ? 0.9861 1.4466 0.7604 0.0278 0.1082 -0.1392 254 TYR A CD1 2035 C CD2 . TYR A 254 ? 1.0034 1.3999 0.7327 0.0269 0.1159 -0.1391 254 TYR A CD2 2036 C CE1 . TYR A 254 ? 0.9933 1.4526 0.7745 0.0471 0.1073 -0.1375 254 TYR A CE1 2037 C CE2 . TYR A 254 ? 1.0142 1.4090 0.7486 0.0445 0.1136 -0.1385 254 TYR A CE2 2038 C CZ . TYR A 254 ? 1.0146 1.4397 0.7749 0.0550 0.1102 -0.1381 254 TYR A CZ 2039 O OH . TYR A 254 ? 1.0427 1.4630 0.8094 0.0730 0.1085 -0.1377 254 TYR A OH 2040 N N . LYS A 255 ? 1.0214 1.4949 0.7942 -0.0462 0.1228 -0.1476 255 LYS A N 2041 C CA . LYS A 255 ? 1.0325 1.5071 0.8060 -0.0683 0.1184 -0.1510 255 LYS A CA 2042 C C . LYS A 255 ? 1.0233 1.4940 0.7876 -0.0677 0.1018 -0.1543 255 LYS A C 2043 O O . LYS A 255 ? 0.9984 1.4909 0.7746 -0.0551 0.0922 -0.1521 255 LYS A O 2044 C CB . LYS A 255 ? 1.0410 1.5583 0.8492 -0.0805 0.1215 -0.1500 255 LYS A CB 2045 C CG . LYS A 255 ? 1.0608 1.5694 0.8683 -0.1014 0.1329 -0.1497 255 LYS A CG 2046 C CD . LYS A 255 ? 1.0596 1.6116 0.9046 -0.1081 0.1427 -0.1454 255 LYS A CD 2047 C CE . LYS A 255 ? 1.0587 1.6535 0.9388 -0.1179 0.1279 -0.1461 255 LYS A CE 2048 N NZ . LYS A 255 ? 1.0818 1.7134 0.9997 -0.1321 0.1389 -0.1408 255 LYS A NZ 2049 N N . ILE A 256 ? 1.0400 1.4803 0.7811 -0.0804 0.0995 -0.1591 256 ILE A N 2050 C CA . ILE A 256 ? 1.0457 1.4766 0.7702 -0.0811 0.0865 -0.1636 256 ILE A CA 2051 C C . ILE A 256 ? 1.0455 1.4994 0.7804 -0.1013 0.0750 -0.1696 256 ILE A C 2052 O O . ILE A 256 ? 1.0471 1.4809 0.7699 -0.1202 0.0759 -0.1765 256 ILE A O 2053 C CB . ILE A 256 ? 1.0588 1.4408 0.7507 -0.0819 0.0921 -0.1665 256 ILE A CB 2054 C CG1 . ILE A 256 ? 1.0456 1.4071 0.7314 -0.0640 0.1011 -0.1590 256 ILE A CG1 2055 C CG2 . ILE A 256 ? 1.0732 1.4446 0.7443 -0.0810 0.0818 -0.1715 256 ILE A CG2 2056 C CD1 . ILE A 256 ? 1.0557 1.3739 0.7168 -0.0605 0.1059 -0.1586 256 ILE A CD1 2057 N N . VAL A 257 ? 1.0432 1.5380 0.8014 -0.0975 0.0629 -0.1665 257 VAL A N 2058 C CA . VAL A 257 ? 1.0798 1.6037 0.8548 -0.1175 0.0490 -0.1704 257 VAL A CA 2059 C C . VAL A 257 ? 1.1200 1.6299 0.8658 -0.1251 0.0324 -0.1778 257 VAL A C 2060 O O . VAL A 257 ? 1.1609 1.6650 0.8989 -0.1479 0.0245 -0.1865 257 VAL A O 2061 C CB . VAL A 257 ? 1.0713 1.6509 0.8914 -0.1122 0.0427 -0.1622 257 VAL A CB 2062 C CG1 . VAL A 257 ? 1.0676 1.6604 0.9143 -0.1098 0.0618 -0.1574 257 VAL A CG1 2063 C CG2 . VAL A 257 ? 1.0560 1.6494 0.8792 -0.0884 0.0348 -0.1552 257 VAL A CG2 2064 N N . LYS A 258 ? 1.1207 1.6229 0.8483 -0.1069 0.0275 -0.1744 258 LYS A N 2065 C CA . LYS A 258 ? 1.1492 1.6376 0.8437 -0.1119 0.0135 -0.1804 258 LYS A CA 2066 C C . LYS A 258 ? 1.1536 1.5961 0.8096 -0.0991 0.0242 -0.1821 258 LYS A C 2067 O O . LYS A 258 ? 1.1242 1.5646 0.7830 -0.0779 0.0302 -0.1729 258 LYS A O 2068 C CB . LYS A 258 ? 1.1437 1.6719 0.8527 -0.1041 -0.0055 -0.1724 258 LYS A CB 2069 C CG . LYS A 258 ? 1.1940 1.7145 0.8687 -0.1158 -0.0235 -0.1794 258 LYS A CG 2070 C CD . LYS A 258 ? 1.2087 1.7734 0.9013 -0.1117 -0.0459 -0.1697 258 LYS A CD 2071 C CE . LYS A 258 ? 1.2597 1.8117 0.9083 -0.1229 -0.0641 -0.1766 258 LYS A CE 2072 N NZ . LYS A 258 ? 1.2797 1.8781 0.9474 -0.1259 -0.0910 -0.1675 258 LYS A NZ 2073 N N . LYS A 259 ? 1.1908 1.5965 0.8133 -0.1124 0.0271 -0.1939 259 LYS A N 2074 C CA . LYS A 259 ? 1.2121 1.5756 0.7981 -0.1017 0.0374 -0.1963 259 LYS A CA 2075 C C . LYS A 259 ? 1.2471 1.6074 0.7992 -0.1040 0.0243 -0.2014 259 LYS A C 2076 O O . LYS A 259 ? 1.2829 1.6509 0.8249 -0.1233 0.0099 -0.2111 259 LYS A O 2077 C CB . LYS A 259 ? 1.2406 1.5610 0.8104 -0.1124 0.0521 -0.2058 259 LYS A CB 2078 C CG . LYS A 259 ? 1.2366 1.5459 0.8254 -0.1027 0.0684 -0.1975 259 LYS A CG 2079 C CD . LYS A 259 ? 1.2751 1.5432 0.8513 -0.1137 0.0816 -0.2046 259 LYS A CD 2080 C CE . LYS A 259 ? 1.2792 1.5440 0.8770 -0.1077 0.0938 -0.1946 259 LYS A CE 2081 N NZ . LYS A 259 ? 1.3073 1.5486 0.9057 -0.1249 0.1021 -0.1991 259 LYS A NZ 2082 N N . GLY A 260 ? 1.2518 1.6001 0.7851 -0.0855 0.0289 -0.1946 260 GLY A N 2083 C CA . GLY A 260 ? 1.2850 1.6250 0.7783 -0.0867 0.0197 -0.1988 260 GLY A CA 2084 C C . GLY A 260 ? 1.2727 1.6007 0.7501 -0.0645 0.0285 -0.1878 260 GLY A C 2085 O O . GLY A 260 ? 1.2600 1.5772 0.7538 -0.0493 0.0434 -0.1791 260 GLY A O 2086 N N . ASP A 261 ? 1.2961 1.6263 0.7411 -0.0637 0.0183 -0.1873 261 ASP A N 2087 C CA . ASP A 261 ? 1.2935 1.6138 0.7214 -0.0440 0.0267 -0.1753 261 ASP A CA 2088 C C . ASP A 261 ? 1.2237 1.5771 0.6913 -0.0271 0.0209 -0.1560 261 ASP A C 2089 O O . ASP A 261 ? 1.2172 1.6074 0.7038 -0.0294 0.0019 -0.1502 261 ASP A O 2090 C CB . ASP A 261 ? 1.3539 1.6682 0.7319 -0.0490 0.0167 -0.1795 261 ASP A CB 2091 C CG . ASP A 261 ? 1.4259 1.6954 0.7559 -0.0603 0.0290 -0.1989 261 ASP A CG 2092 O OD1 . ASP A 261 ? 1.4323 1.6735 0.7709 -0.0590 0.0485 -0.2049 261 ASP A OD1 2093 O OD2 . ASP A 261 ? 1.4790 1.7397 0.7619 -0.0700 0.0192 -0.2080 261 ASP A OD2 2094 N N . SER A 262 ? 1.1829 1.5220 0.6644 -0.0102 0.0370 -0.1460 262 SER A N 2095 C CA . SER A 262 ? 1.1475 1.5096 0.6635 0.0067 0.0335 -0.1286 262 SER A CA 2096 C C . SER A 262 ? 1.1391 1.4758 0.6498 0.0230 0.0503 -0.1181 262 SER A C 2097 O O . SER A 262 ? 1.1735 1.4788 0.6561 0.0215 0.0650 -0.1241 262 SER A O 2098 C CB . SER A 262 ? 1.1067 1.4857 0.6653 0.0057 0.0328 -0.1293 262 SER A CB 2099 O OG . SER A 262 ? 1.0888 1.4802 0.6777 0.0232 0.0330 -0.1150 262 SER A OG 2100 N N . THR A 263 ? 1.1296 1.1010 0.7500 -0.0818 0.1608 -0.0795 263 THR A N 2101 C CA . THR A 263 ? 1.0757 1.0465 0.7248 -0.0282 0.1453 -0.0733 263 THR A CA 2102 C C . THR A 263 ? 0.9966 1.0525 0.7157 -0.0153 0.1408 -0.0899 263 THR A C 2103 O O . THR A 263 ? 0.9499 1.0717 0.7182 -0.0332 0.1447 -0.1068 263 THR A O 2104 C CB . THR A 263 ? 1.0338 1.0008 0.7216 -0.0054 0.1346 -0.0704 263 THR A CB 2105 O OG1 . THR A 263 ? 1.0145 0.9745 0.7067 0.0390 0.1225 -0.0644 263 THR A OG1 2106 C CG2 . THR A 263 ? 0.9639 1.0103 0.7397 -0.0078 0.1313 -0.0880 263 THR A CG2 2107 N N . ILE A 264 ? 0.9893 1.0467 0.7065 0.0177 0.1331 -0.0871 264 ILE A N 2108 C CA . ILE A 264 ? 0.9166 1.0461 0.6955 0.0298 0.1294 -0.1042 264 ILE A CA 2109 C C . ILE A 264 ? 0.8745 1.0213 0.7022 0.0529 0.1200 -0.1097 264 ILE A C 2110 O O . ILE A 264 ? 0.8970 1.0253 0.7069 0.0770 0.1124 -0.1019 264 ILE A O 2111 C CB . ILE A 264 ? 0.9273 1.0621 0.6746 0.0454 0.1284 -0.1024 264 ILE A CB 2112 C CG1 . ILE A 264 ? 0.9979 1.0943 0.6772 0.0198 0.1397 -0.0938 264 ILE A CG1 2113 C CG2 . ILE A 264 ? 0.8715 1.0798 0.6798 0.0492 0.1273 -0.1234 264 ILE A CG2 2114 C CD1 . ILE A 264 ? 1.0419 1.1304 0.6734 0.0393 0.1389 -0.0884 264 ILE A CD1 2115 N N . MET A 265 ? 0.8336 1.0159 0.7150 0.0470 0.1212 -0.1243 265 MET A N 2116 C CA . MET A 265 ? 0.8160 1.0000 0.7327 0.0612 0.1159 -0.1300 265 MET A CA 2117 C C . MET A 265 ? 0.8077 1.0266 0.7506 0.0663 0.1177 -0.1485 265 MET A C 2118 O O . MET A 265 ? 0.8076 1.0536 0.7608 0.0599 0.1234 -0.1603 265 MET A O 2119 C CB . MET A 265 ? 0.8070 0.9927 0.7467 0.0547 0.1177 -0.1334 265 MET A CB 2120 C CG . MET A 265 ? 0.7976 0.9673 0.7601 0.0682 0.1133 -0.1354 265 MET A CG 2121 S SD . MET A 265 ? 0.8033 0.9879 0.7844 0.0678 0.1150 -0.1399 265 MET A SD 2122 C CE . MET A 265 ? 0.8152 0.9733 0.7652 0.0468 0.1146 -0.1217 265 MET A CE 2123 N N . LYS A 266 ? 0.8320 1.0533 0.7801 0.0744 0.1143 -0.1532 266 LYS A N 2124 C CA . LYS A 266 ? 0.8464 1.0961 0.8078 0.0691 0.1194 -0.1738 266 LYS A CA 2125 C C . LYS A 266 ? 0.8539 1.0755 0.8284 0.0653 0.1243 -0.1850 266 LYS A C 2126 O O . LYS A 266 ? 0.8527 1.0515 0.8275 0.0669 0.1213 -0.1801 266 LYS A O 2127 C CB . LYS A 266 ? 0.8796 1.1645 0.8302 0.0735 0.1154 -0.1779 266 LYS A CB 2128 C CG . LYS A 266 ? 0.9253 1.2239 0.8448 0.0903 0.1092 -0.1637 266 LYS A CG 2129 C CD . LYS A 266 ? 0.9447 1.2708 0.8585 0.0846 0.1141 -0.1706 266 LYS A CD 2130 C CE . LYS A 266 ? 0.9754 1.3657 0.8946 0.0841 0.1150 -0.1905 266 LYS A CE 2131 N NZ . LYS A 266 ? 1.0188 1.4350 0.9453 0.0705 0.1228 -0.2040 266 LYS A NZ 2132 N N . SER A 267 ? 0.8870 1.1037 0.8636 0.0636 0.1323 -0.1998 267 SER A N 2133 C CA . SER A 267 ? 0.9264 1.0970 0.8953 0.0688 0.1385 -0.2096 267 SER A CA 2134 C C . SER A 267 ? 0.9541 1.1165 0.9081 0.0698 0.1489 -0.2297 267 SER A C 2135 O O . SER A 267 ? 0.9607 1.1621 0.9232 0.0717 0.1491 -0.2331 267 SER A O 2136 C CB . SER A 267 ? 0.9474 1.1057 0.9249 0.0872 0.1332 -0.1977 267 SER A CB 2137 O OG . SER A 267 ? 1.0172 1.1310 0.9775 0.1044 0.1386 -0.2074 267 SER A OG 2138 N N . GLU A 268 ? 0.9975 1.1001 0.9198 0.0680 0.1589 -0.2433 268 GLU A N 2139 C CA . GLU A 268 ? 1.0468 1.1160 0.9364 0.0742 0.1707 -0.2629 268 GLU A CA 2140 C C . GLU A 268 ? 1.0825 1.1237 0.9582 0.1159 0.1694 -0.2624 268 GLU A C 2141 O O . GLU A 268 ? 1.1757 1.1976 1.0232 0.1342 0.1767 -0.2775 268 GLU A O 2142 C CB . GLU A 268 ? 1.1018 1.1027 0.9411 0.0474 0.1864 -0.2805 268 GLU A CB 2143 C CG . GLU A 268 ? 1.0792 1.1289 0.9309 0.0055 0.1884 -0.2873 268 GLU A CG 2144 C CD . GLU A 268 ? 1.0433 1.1770 0.9254 -0.0006 0.1841 -0.2909 268 GLU A CD 2145 O OE1 . GLU A 268 ? 1.0211 1.1483 0.8861 -0.0018 0.1929 -0.3062 268 GLU A OE1 2146 O OE2 . GLU A 268 ? 0.9944 1.1948 0.9102 -0.0006 0.1721 -0.2780 268 GLU A OE2 2147 N N . LEU A 269 ? 1.0681 1.1149 0.9613 0.1340 0.1598 -0.2469 269 LEU A N 2148 C CA . LEU A 269 ? 1.1082 1.1397 0.9850 0.1785 0.1576 -0.2488 269 LEU A CA 2149 C C . LEU A 269 ? 1.0974 1.2119 1.0010 0.1972 0.1529 -0.2544 269 LEU A C 2150 O O . LEU A 269 ? 1.0232 1.2046 0.9643 0.1716 0.1488 -0.2486 269 LEU A O 2151 C CB . LEU A 269 ? 1.0951 1.1232 0.9864 0.1877 0.1487 -0.2324 269 LEU A CB 2152 C CG . LEU A 269 ? 1.1257 1.0761 0.9893 0.1713 0.1532 -0.2270 269 LEU A CG 2153 C CD1 . LEU A 269 ? 1.1054 1.0732 0.9973 0.1734 0.1424 -0.2089 269 LEU A CD1 2154 C CD2 . LEU A 269 ? 1.2319 1.0787 1.0212 0.1958 0.1652 -0.2390 269 LEU A CD2 2155 N N . GLU A 270 ? 1.1943 1.3020 1.0694 0.2440 0.1543 -0.2669 270 GLU A N 2156 C CA . GLU A 270 ? 1.2142 1.4182 1.1131 0.2667 0.1497 -0.2770 270 GLU A CA 2157 C C . GLU A 270 ? 1.1488 1.4213 1.0751 0.2846 0.1397 -0.2709 270 GLU A C 2158 O O . GLU A 270 ? 1.1435 1.3837 1.0734 0.2779 0.1357 -0.2565 270 GLU A O 2159 C CB . GLU A 270 ? 1.3314 1.5047 1.1789 0.3153 0.1565 -0.2985 270 GLU A CB 2160 C CG . GLU A 270 ? 1.4236 1.5110 1.2272 0.2964 0.1699 -0.3083 270 GLU A CG 2161 C CD . GLU A 270 ? 1.4076 1.5630 1.2470 0.2614 0.1719 -0.3146 270 GLU A CD 2162 O OE1 . GLU A 270 ? 1.3429 1.5712 1.2374 0.2241 0.1653 -0.3019 270 GLU A OE1 2163 O OE2 . GLU A 270 ? 1.4487 1.5755 1.2516 0.2726 0.1811 -0.3322 270 GLU A OE2 2164 N N . TYR A 271 ? 1.1059 1.4821 1.0512 0.3037 0.1364 -0.2845 271 TYR A N 2165 C CA . TYR A 271 ? 1.0611 1.5275 1.0322 0.3143 0.1288 -0.2855 271 TYR A CA 2166 C C . TYR A 271 ? 1.1231 1.5549 1.0574 0.3790 0.1246 -0.2901 271 TYR A C 2167 O O . TYR A 271 ? 1.1757 1.5561 1.0590 0.4328 0.1276 -0.3025 271 TYR A O 2168 C CB . TYR A 271 ? 1.0280 1.6286 1.0236 0.3138 0.1289 -0.3052 271 TYR A CB 2169 C CG . TYR A 271 ? 0.9767 1.6985 1.0011 0.3064 0.1243 -0.3123 271 TYR A CG 2170 C CD1 . TYR A 271 ? 0.9119 1.6419 0.9590 0.2476 0.1249 -0.2962 271 TYR A CD1 2171 C CD2 . TYR A 271 ? 0.9882 1.8240 1.0113 0.3573 0.1206 -0.3383 271 TYR A CD2 2172 C CE1 . TYR A 271 ? 0.8905 1.7314 0.9568 0.2302 0.1240 -0.3063 271 TYR A CE1 2173 C CE2 . TYR A 271 ? 0.9516 1.9197 1.0017 0.3434 0.1180 -0.3503 271 TYR A CE2 2174 C CZ . TYR A 271 ? 0.9073 1.8749 0.9785 0.2746 0.1208 -0.3345 271 TYR A CZ 2175 O OH . TYR A 271 ? 0.8723 1.9704 0.9630 0.2516 0.1213 -0.3497 271 TYR A OH 2176 N N . GLY A 272 ? 1.1207 1.5728 1.0714 0.3758 0.1183 -0.2801 272 GLY A N 2177 C CA . GLY A 272 ? 1.1869 1.6019 1.0995 0.4373 0.1135 -0.2814 272 GLY A CA 2178 C C . GLY A 272 ? 1.1997 1.7449 1.1185 0.4906 0.1057 -0.3012 272 GLY A C 2179 O O . GLY A 272 ? 1.2437 1.7597 1.1211 0.5546 0.1009 -0.3036 272 GLY A O 2180 N N . ASN A 273 ? 1.1594 1.8506 1.1235 0.4644 0.1051 -0.3169 273 ASN A N 2181 C CA . ASN A 273 ? 1.1727 2.0282 1.1532 0.5007 0.0985 -0.3411 273 ASN A CA 2182 C C . ASN A 273 ? 1.1412 2.0189 1.1350 0.4964 0.0926 -0.3325 273 ASN A C 2183 O O . ASN A 273 ? 1.2047 2.0549 1.1625 0.5654 0.0858 -0.3336 273 ASN A O 2184 C CB . ASN A 273 ? 1.2486 2.1199 1.1776 0.6013 0.0942 -0.3629 273 ASN A CB 2185 C CG . ASN A 273 ? 1.3010 2.1604 1.2154 0.6070 0.1005 -0.3747 273 ASN A CG 2186 O OD1 . ASN A 273 ? 1.3956 2.1097 1.2540 0.6359 0.1055 -0.3678 273 ASN A OD1 2187 N ND2 . ASN A 273 ? 1.2662 2.2759 1.2260 0.5730 0.1022 -0.3940 273 ASN A ND2 2188 N N . CYS A 274 ? 1.0769 1.9988 1.1138 0.4162 0.0960 -0.3243 274 CYS A N 2189 C CA . CYS A 274 ? 1.0587 1.9008 1.0995 0.3876 0.0943 -0.3004 274 CYS A CA 2190 C C . CYS A 274 ? 0.9984 1.9065 1.0741 0.3038 0.0995 -0.2975 274 CYS A C 2191 O O . CYS A 274 ? 0.9945 1.9412 1.0820 0.2500 0.1077 -0.3024 274 CYS A O 2192 C CB . CYS A 274 ? 1.0947 1.7687 1.1149 0.3706 0.0983 -0.2758 274 CYS A CB 2193 S SG . CYS A 274 ? 1.1512 1.6878 1.1522 0.3723 0.0952 -0.2490 274 CYS A SG 2194 N N . ASN A 275 ? 1.0043 1.9100 1.0864 0.2900 0.0966 -0.2886 275 ASN A N 2195 C CA . ASN A 275 ? 1.0283 1.9655 1.1259 0.2066 0.1042 -0.2841 275 ASN A CA 2196 C C . ASN A 275 ? 0.9839 1.8159 1.0758 0.1907 0.1014 -0.2583 275 ASN A C 2197 O O . ASN A 275 ? 1.0147 1.8232 1.1018 0.2417 0.0928 -0.2543 275 ASN A O 2198 C CB . ASN A 275 ? 1.1160 2.2369 1.2303 0.1897 0.1071 -0.3157 275 ASN A CB 2199 C CG . ASN A 275 ? 1.1384 2.2815 1.2502 0.0920 0.1203 -0.3149 275 ASN A CG 2200 O OD1 . ASN A 275 ? 1.1542 2.2539 1.2510 0.0328 0.1314 -0.3081 275 ASN A OD1 2201 N ND2 . ASN A 275 ? 1.1651 2.3673 1.2817 0.0753 0.1203 -0.3222 275 ASN A ND2 2202 N N . THR A 276 ? 0.9262 1.6915 1.0109 0.1239 0.1089 -0.2410 276 THR A N 2203 C CA . THR A 276 ? 0.8579 1.5175 0.9336 0.1098 0.1063 -0.2161 276 THR A CA 2204 C C . THR A 276 ? 0.8420 1.4879 0.8991 0.0334 0.1171 -0.2097 276 THR A C 2205 O O . THR A 276 ? 0.8469 1.5407 0.8921 -0.0109 0.1277 -0.2212 276 THR A O 2206 C CB . THR A 276 ? 0.8761 1.4035 0.9414 0.1316 0.1025 -0.1943 276 THR A CB 2207 O OG1 . THR A 276 ? 0.8613 1.3033 0.9201 0.1272 0.0985 -0.1738 276 THR A OG1 2208 C CG2 . THR A 276 ? 0.8879 1.3782 0.9414 0.0929 0.1099 -0.1879 276 THR A CG2 2209 N N . LYS A 277 ? 0.8610 1.4315 0.9058 0.0181 0.1156 -0.1916 277 LYS A N 2210 C CA . LYS A 277 ? 0.9127 1.4275 0.9186 -0.0472 0.1266 -0.1810 277 LYS A CA 2211 C C . LYS A 277 ? 0.8880 1.2677 0.8697 -0.0425 0.1239 -0.1538 277 LYS A C 2212 O O . LYS A 277 ? 0.9206 1.2304 0.8551 -0.0833 0.1320 -0.1418 277 LYS A O 2213 C CB . LYS A 277 ? 0.9816 1.5154 0.9812 -0.0704 0.1284 -0.1834 277 LYS A CB 2214 C CG . LYS A 277 ? 1.0478 1.7246 1.0518 -0.1081 0.1380 -0.2143 277 LYS A CG 2215 C CD . LYS A 277 ? 1.1026 1.7792 1.0828 -0.1553 0.1455 -0.2165 277 LYS A CD 2216 C CE . LYS A 277 ? 1.1281 1.9651 1.1103 -0.2033 0.1576 -0.2527 277 LYS A CE 2217 N NZ . LYS A 277 ? 1.1697 2.0544 1.1265 -0.2562 0.1734 -0.2696 277 LYS A NZ 2218 N N . CYS A 278 ? 0.8456 1.1886 0.8507 0.0080 0.1133 -0.1459 278 CYS A N 2219 C CA . CYS A 278 ? 0.8425 1.0836 0.8316 0.0172 0.1094 -0.1251 278 CYS A CA 2220 C C . CYS A 278 ? 0.7994 1.0351 0.8085 0.0541 0.1047 -0.1282 278 CYS A C 2221 O O . CYS A 278 ? 0.7948 1.0456 0.8243 0.0915 0.0995 -0.1350 278 CYS A O 2222 C CB . CYS A 278 ? 0.8496 1.0397 0.8401 0.0308 0.1023 -0.1119 278 CYS A CB 2223 S SG . CYS A 278 ? 0.8894 0.9835 0.8657 0.0483 0.0960 -0.0922 278 CYS A SG 2224 N N . GLN A 279 ? 0.7786 0.9871 0.7724 0.0442 0.1079 -0.1241 279 GLN A N 2225 C CA . GLN A 279 ? 0.7735 0.9807 0.7817 0.0712 0.1060 -0.1304 279 GLN A CA 2226 C C . GLN A 279 ? 0.7649 0.9088 0.7616 0.0756 0.1030 -0.1183 279 GLN A C 2227 O O . GLN A 279 ? 0.7651 0.8768 0.7354 0.0588 0.1035 -0.1061 279 GLN A O 2228 C CB . GLN A 279 ? 0.7825 1.0418 0.7898 0.0590 0.1125 -0.1432 279 GLN A CB 2229 C CG . GLN A 279 ? 0.7812 1.0408 0.7995 0.0866 0.1120 -0.1529 279 GLN A CG 2230 C CD . GLN A 279 ? 0.7997 1.0835 0.8304 0.1264 0.1095 -0.1666 279 GLN A CD 2231 O OE1 . GLN A 279 ? 0.8199 1.1751 0.8598 0.1344 0.1096 -0.1792 279 GLN A OE1 2232 N NE2 . GLN A 279 ? 0.8184 1.0433 0.8404 0.1519 0.1083 -0.1662 279 GLN A NE2 2233 N N . THR A 280 ? 0.7634 0.8904 0.7708 0.0987 0.1012 -0.1239 280 THR A N 2234 C CA . THR A 280 ? 0.7706 0.8640 0.7702 0.0987 0.1003 -0.1205 280 THR A CA 2235 C C . THR A 280 ? 0.7987 0.9027 0.8000 0.1046 0.1054 -0.1352 280 THR A C 2236 O O . THR A 280 ? 0.8154 0.9364 0.8208 0.1185 0.1087 -0.1469 280 THR A O 2237 C CB . THR A 280 ? 0.7757 0.8312 0.7759 0.1077 0.0968 -0.1165 280 THR A CB 2238 O OG1 . THR A 280 ? 0.7766 0.8132 0.7738 0.1206 0.1014 -0.1290 280 THR A OG1 2239 C CG2 . THR A 280 ? 0.7712 0.8194 0.7747 0.1094 0.0924 -0.1068 280 THR A CG2 2240 N N . PRO A 281 ? 0.8258 0.9237 0.8198 0.0971 0.1064 -0.1366 281 PRO A N 2241 C CA . PRO A 281 ? 0.8425 0.9475 0.8336 0.0965 0.1130 -0.1527 281 PRO A CA 2242 C C . PRO A 281 ? 0.8910 0.9563 0.8696 0.1061 0.1194 -0.1653 281 PRO A C 2243 O O . PRO A 281 ? 0.9277 0.9857 0.8927 0.1074 0.1272 -0.1803 281 PRO A O 2244 C CB . PRO A 281 ? 0.8415 0.9575 0.8261 0.0853 0.1118 -0.1526 281 PRO A CB 2245 C CG . PRO A 281 ? 0.8268 0.9436 0.8042 0.0877 0.1039 -0.1344 281 PRO A CG 2246 C CD . PRO A 281 ? 0.8124 0.9050 0.7952 0.0915 0.1012 -0.1252 281 PRO A CD 2247 N N . MET A 282 ? 0.9268 0.9565 0.9000 0.1127 0.1174 -0.1594 282 MET A N 2248 C CA . MET A 282 ? 0.9871 0.9571 0.9292 0.1239 0.1251 -0.1691 282 MET A CA 2249 C C . MET A 282 ? 0.9794 0.9410 0.9150 0.1587 0.1226 -0.1681 282 MET A C 2250 O O . MET A 282 ? 1.0347 0.9390 0.9290 0.1809 0.1296 -0.1770 282 MET A O 2251 C CB . MET A 282 ? 1.0407 0.9736 0.9709 0.1088 0.1260 -0.1652 282 MET A CB 2252 C CG . MET A 282 ? 1.0796 1.0333 1.0094 0.0771 0.1297 -0.1730 282 MET A CG 2253 S SD . MET A 282 ? 1.1736 1.1111 1.0990 0.0623 0.1278 -0.1677 282 MET A SD 2254 C CE . MET A 282 ? 1.2283 1.0648 1.0994 0.0663 0.1407 -0.1743 282 MET A CE 2255 N N . GLY A 283 ? 0.9051 0.9217 0.8714 0.1643 0.1140 -0.1590 283 GLY A N 2256 C CA . GLY A 283 ? 0.9049 0.9417 0.8702 0.1972 0.1105 -0.1614 283 GLY A CA 2257 C C . GLY A 283 ? 0.8493 0.9397 0.8446 0.1855 0.1030 -0.1510 283 GLY A C 2258 O O . GLY A 283 ? 0.8224 0.9106 0.8289 0.1565 0.1007 -0.1393 283 GLY A O 2259 N N . ALA A 284 ? 0.8466 0.9858 0.8474 0.2097 0.0999 -0.1572 284 ALA A N 2260 C CA . ALA A 284 ? 0.8200 1.0172 0.8431 0.1913 0.0958 -0.1523 284 ALA A CA 2261 C C . ALA A 284 ? 0.8331 0.9964 0.8532 0.2011 0.0908 -0.1421 284 ALA A C 2262 O O . ALA A 284 ? 0.8431 0.9507 0.8408 0.2316 0.0905 -0.1417 284 ALA A O 2263 C CB . ALA A 284 ? 0.8322 1.1271 0.8657 0.2066 0.0958 -0.1697 284 ALA A CB 2264 N N . ILE A 285 ? 0.8116 1.0027 0.8454 0.1732 0.0886 -0.1347 285 ILE A N 2265 C CA . ILE A 285 ? 0.8222 0.9865 0.8562 0.1757 0.0839 -0.1243 285 ILE A CA 2266 C C . ILE A 285 ? 0.8329 1.0781 0.8792 0.1738 0.0823 -0.1326 285 ILE A C 2267 O O . ILE A 285 ? 0.8210 1.1243 0.8726 0.1396 0.0870 -0.1393 285 ILE A O 2268 C CB . ILE A 285 ? 0.7872 0.9008 0.8174 0.1418 0.0835 -0.1079 285 ILE A CB 2269 C CG1 . ILE A 285 ? 0.7790 0.8257 0.7989 0.1499 0.0833 -0.1024 285 ILE A CG1 2270 C CG2 . ILE A 285 ? 0.7657 0.8775 0.7976 0.1316 0.0801 -0.0997 285 ILE A CG2 2271 C CD1 . ILE A 285 ? 0.7705 0.7899 0.7846 0.1261 0.0823 -0.0914 285 ILE A CD1 2272 N N . ASN A 286 ? 0.8721 1.1220 0.9167 0.2076 0.0770 -0.1337 286 ASN A N 2273 C CA . ASN A 286 ? 0.8937 1.2279 0.9510 0.2054 0.0747 -0.1425 286 ASN A CA 2274 C C . ASN A 286 ? 0.8914 1.1793 0.9452 0.2128 0.0696 -0.1296 286 ASN A C 2275 O O . ASN A 286 ? 0.8942 1.1556 0.9340 0.2596 0.0649 -0.1287 286 ASN A O 2276 C CB . ASN A 286 ? 0.9364 1.3602 0.9938 0.2553 0.0718 -0.1635 286 ASN A CB 2277 C CG . ASN A 286 ? 0.9640 1.5130 1.0390 0.2447 0.0708 -0.1800 286 ASN A CG 2278 O OD1 . ASN A 286 ? 0.9711 1.5408 1.0547 0.1854 0.0762 -0.1785 286 ASN A OD1 2279 N ND2 . ASN A 286 ? 0.9807 1.6144 1.0528 0.3030 0.0648 -0.1977 286 ASN A ND2 2280 N N . SER A 287 ? 0.8889 1.1561 0.9460 0.1683 0.0713 -0.1193 287 SER A N 2281 C CA . SER A 287 ? 0.9117 1.1458 0.9678 0.1721 0.0665 -0.1087 287 SER A CA 2282 C C . SER A 287 ? 0.8938 1.1310 0.9467 0.1215 0.0704 -0.1043 287 SER A C 2283 O O . SER A 287 ? 0.8902 1.1245 0.9302 0.0817 0.0779 -0.1051 287 SER A O 2284 C CB . SER A 287 ? 0.9372 1.0691 0.9805 0.1896 0.0637 -0.0932 287 SER A CB 2285 O OG . SER A 287 ? 0.9236 1.0025 0.9621 0.1574 0.0661 -0.0821 287 SER A OG 2286 N N . SER A 288 ? 0.9027 1.1361 0.9576 0.1242 0.0665 -0.0997 288 SER A N 2287 C CA . SER A 288 ? 0.9134 1.1297 0.9541 0.0790 0.0710 -0.0948 288 SER A CA 2288 C C . SER A 288 ? 0.8629 0.9783 0.8899 0.0803 0.0672 -0.0745 288 SER A C 2289 O O . SER A 288 ? 0.8729 0.9539 0.8779 0.0514 0.0703 -0.0683 288 SER A O 2290 C CB . SER A 288 ? 0.9650 1.2583 1.0164 0.0770 0.0699 -0.1066 288 SER A CB 2291 O OG . SER A 288 ? 1.0260 1.4372 1.0904 0.0775 0.0730 -0.1300 288 SER A OG 2292 N N . MET A 289 ? 0.8114 0.8808 0.8445 0.1116 0.0619 -0.0665 289 MET A N 2293 C CA . MET A 289 ? 0.8093 0.8054 0.8317 0.1126 0.0585 -0.0520 289 MET A CA 2294 C C . MET A 289 ? 0.8167 0.7761 0.8112 0.0858 0.0628 -0.0460 289 MET A C 2295 O O . MET A 289 ? 0.8294 0.8004 0.8153 0.0742 0.0681 -0.0507 289 MET A O 2296 C CB . MET A 289 ? 0.8364 0.8001 0.8626 0.1373 0.0564 -0.0502 289 MET A CB 2297 C CG . MET A 289 ? 0.8725 0.8396 0.9016 0.1692 0.0547 -0.0546 289 MET A CG 2298 S SD . MET A 289 ? 0.9004 0.8464 0.9283 0.1776 0.0495 -0.0464 289 MET A SD 2299 C CE . MET A 289 ? 0.8902 0.7890 0.8922 0.2141 0.0517 -0.0486 289 MET A CE 2300 N N . PRO A 290 ? 0.8070 0.7172 0.7797 0.0807 0.0606 -0.0356 290 PRO A N 2301 C CA . PRO A 290 ? 0.8252 0.6852 0.7536 0.0682 0.0642 -0.0287 290 PRO A CA 2302 C C . PRO A 290 ? 0.8141 0.6607 0.7426 0.0883 0.0608 -0.0262 290 PRO A C 2303 O O . PRO A 290 ? 0.8660 0.6791 0.7546 0.0854 0.0636 -0.0217 290 PRO A O 2304 C CB . PRO A 290 ? 0.8395 0.6523 0.7410 0.0695 0.0613 -0.0198 290 PRO A CB 2305 C CG . PRO A 290 ? 0.8087 0.6468 0.7529 0.0897 0.0534 -0.0200 290 PRO A CG 2306 C CD . PRO A 290 ? 0.7771 0.6733 0.7560 0.0894 0.0551 -0.0301 290 PRO A CD 2307 N N . PHE A 291 ? 0.7745 0.6433 0.7380 0.1069 0.0563 -0.0300 291 PHE A N 2308 C CA . PHE A 291 ? 0.7749 0.6432 0.7391 0.1192 0.0545 -0.0320 291 PHE A CA 2309 C C . PHE A 291 ? 0.7475 0.6414 0.7371 0.1222 0.0577 -0.0421 291 PHE A C 2310 O O . PHE A 291 ? 0.7331 0.6368 0.7377 0.1268 0.0587 -0.0457 291 PHE A O 2311 C CB . PHE A 291 ? 0.7872 0.6491 0.7545 0.1319 0.0486 -0.0304 291 PHE A CB 2312 C CG . PHE A 291 ? 0.8389 0.6741 0.7733 0.1412 0.0439 -0.0220 291 PHE A CG 2313 C CD1 . PHE A 291 ? 0.9008 0.7233 0.7986 0.1544 0.0426 -0.0194 291 PHE A CD1 2314 C CD2 . PHE A 291 ? 0.8689 0.6887 0.8020 0.1429 0.0405 -0.0170 291 PHE A CD2 2315 C CE1 . PHE A 291 ? 0.9468 0.7341 0.7989 0.1742 0.0381 -0.0118 291 PHE A CE1 2316 C CE2 . PHE A 291 ? 0.9037 0.6915 0.7976 0.1570 0.0364 -0.0101 291 PHE A CE2 2317 C CZ . PHE A 291 ? 0.9433 0.7115 0.7929 0.1753 0.0352 -0.0075 291 PHE A CZ 2318 N N . HIS A 292 ? 0.7347 0.6362 0.7217 0.1237 0.0595 -0.0474 292 HIS A N 2319 C CA . HIS A 292 ? 0.7218 0.6319 0.7205 0.1254 0.0642 -0.0585 292 HIS A CA 2320 C C . HIS A 292 ? 0.7148 0.6349 0.7077 0.1218 0.0653 -0.0656 292 HIS A C 2321 O O . HIS A 292 ? 0.7142 0.6457 0.6960 0.1262 0.0606 -0.0618 292 HIS A O 2322 C CB . HIS A 292 ? 0.7432 0.6721 0.7462 0.1248 0.0687 -0.0641 292 HIS A CB 2323 C CG . HIS A 292 ? 0.7521 0.6934 0.7449 0.1170 0.0702 -0.0643 292 HIS A CG 2324 N ND1 . HIS A 292 ? 0.7504 0.7021 0.7431 0.1167 0.0733 -0.0729 292 HIS A ND1 2325 C CD2 . HIS A 292 ? 0.7817 0.7193 0.7545 0.1079 0.0703 -0.0571 292 HIS A CD2 2326 C CE1 . HIS A 292 ? 0.7751 0.7360 0.7540 0.1128 0.0735 -0.0701 292 HIS A CE1 2327 N NE2 . HIS A 292 ? 0.7908 0.7358 0.7519 0.1074 0.0723 -0.0598 292 HIS A NE2 2328 N N . ASN A 293 ? 0.6980 0.6137 0.6898 0.1151 0.0723 -0.0776 293 ASN A N 2329 C CA . ASN A 293 ? 0.7056 0.6444 0.6910 0.1027 0.0762 -0.0902 293 ASN A CA 2330 C C . ASN A 293 ? 0.7323 0.6722 0.7115 0.0942 0.0851 -0.1028 293 ASN A C 2331 O O . ASN A 293 ? 0.7564 0.7046 0.7235 0.0751 0.0930 -0.1180 293 ASN A O 2332 C CB . ASN A 293 ? 0.7192 0.6499 0.6954 0.0878 0.0801 -0.0978 293 ASN A CB 2333 C CG . ASN A 293 ? 0.7495 0.6220 0.7044 0.0805 0.0904 -0.1023 293 ASN A CG 2334 O OD1 . ASN A 293 ? 0.7664 0.6112 0.7163 0.0952 0.0925 -0.0997 293 ASN A OD1 2335 N ND2 . ASN A 293 ? 0.7808 0.6336 0.7146 0.0599 0.0975 -0.1102 293 ASN A ND2 2336 N N . ILE A 294 ? 0.7468 0.6834 0.7314 0.1049 0.0850 -0.0989 294 ILE A N 2337 C CA . ILE A 294 ? 0.7745 0.7095 0.7519 0.1021 0.0931 -0.1108 294 ILE A CA 2338 C C . ILE A 294 ? 0.7663 0.7423 0.7460 0.0923 0.0937 -0.1178 294 ILE A C 2339 O O . ILE A 294 ? 0.7928 0.7730 0.7607 0.0762 0.1020 -0.1335 294 ILE A O 2340 C CB . ILE A 294 ? 0.7917 0.7299 0.7765 0.1190 0.0919 -0.1071 294 ILE A CB 2341 C CG1 . ILE A 294 ? 0.8012 0.7168 0.7842 0.1355 0.0895 -0.1012 294 ILE A CG1 2342 C CG2 . ILE A 294 ? 0.8244 0.7565 0.7966 0.1227 0.1003 -0.1208 294 ILE A CG2 2343 C CD1 . ILE A 294 ? 0.8441 0.7026 0.7974 0.1389 0.0961 -0.1066 294 ILE A CD1 2344 N N . HIS A 295 ? 0.7491 0.7501 0.7349 0.1008 0.0864 -0.1073 295 HIS A N 2345 C CA . HIS A 295 ? 0.7559 0.7934 0.7360 0.1002 0.0855 -0.1114 295 HIS A CA 2346 C C . HIS A 295 ? 0.7404 0.7760 0.7046 0.1146 0.0774 -0.0949 295 HIS A C 2347 O O . HIS A 295 ? 0.7100 0.7181 0.6696 0.1147 0.0766 -0.0837 295 HIS A O 2348 C CB . HIS A 295 ? 0.7829 0.8262 0.7655 0.0957 0.0922 -0.1194 295 HIS A CB 2349 C CG . HIS A 295 ? 0.8116 0.8940 0.7889 0.0910 0.0940 -0.1294 295 HIS A CG 2350 N ND1 . HIS A 295 ? 0.8218 0.9256 0.7857 0.1027 0.0879 -0.1206 295 HIS A ND1 2351 C CD2 . HIS A 295 ? 0.8453 0.9456 0.8211 0.0762 0.1023 -0.1482 295 HIS A CD2 2352 C CE1 . HIS A 295 ? 0.8431 0.9881 0.8044 0.0993 0.0904 -0.1333 295 HIS A CE1 2353 N NE2 . HIS A 295 ? 0.8567 1.0043 0.8283 0.0797 0.0996 -0.1513 295 HIS A NE2 2354 N N . PRO A 296 ? 0.7523 0.8150 0.6982 0.1275 0.0724 -0.0952 296 PRO A N 2355 C CA . PRO A 296 ? 0.7771 0.8130 0.6842 0.1480 0.0662 -0.0784 296 PRO A CA 2356 C C . PRO A 296 ? 0.8065 0.8143 0.6884 0.1419 0.0709 -0.0701 296 PRO A C 2357 O O . PRO A 296 ? 0.8257 0.7834 0.6679 0.1436 0.0713 -0.0559 296 PRO A O 2358 C CB . PRO A 296 ? 0.7882 0.8705 0.6759 0.1731 0.0596 -0.0846 296 PRO A CB 2359 C CG . PRO A 296 ? 0.7755 0.9180 0.6940 0.1550 0.0650 -0.1061 296 PRO A CG 2360 C CD . PRO A 296 ? 0.7558 0.8751 0.7062 0.1260 0.0728 -0.1124 296 PRO A CD 2361 N N . LEU A 297 ? 0.8281 0.8651 0.7256 0.1311 0.0762 -0.0805 297 LEU A N 2362 C CA . LEU A 297 ? 0.8806 0.9010 0.7530 0.1218 0.0817 -0.0752 297 LEU A CA 2363 C C . LEU A 297 ? 0.8589 0.8739 0.7521 0.0978 0.0885 -0.0772 297 LEU A C 2364 O O . LEU A 297 ? 0.8828 0.9306 0.8081 0.0901 0.0925 -0.0900 297 LEU A O 2365 C CB . LEU A 297 ? 0.8826 0.9460 0.7600 0.1242 0.0836 -0.0865 297 LEU A CB 2366 C CG . LEU A 297 ? 0.9136 1.0052 0.7675 0.1520 0.0764 -0.0881 297 LEU A CG 2367 C CD1 . LEU A 297 ? 0.9198 1.0658 0.7826 0.1507 0.0789 -0.1024 297 LEU A CD1 2368 C CD2 . LEU A 297 ? 0.9853 1.0222 0.7691 0.1778 0.0722 -0.0688 297 LEU A CD2 2369 N N . THR A 298 ? 0.8692 0.8473 0.7389 0.0874 0.0901 -0.0667 298 THR A N 2370 C CA . THR A 298 ? 0.8388 0.8335 0.7280 0.0648 0.0961 -0.0722 298 THR A CA 2371 C C . THR A 298 ? 0.8708 0.8460 0.7128 0.0366 0.1056 -0.0682 298 THR A C 2372 O O . THR A 298 ? 0.9046 0.8255 0.6856 0.0371 0.1076 -0.0564 298 THR A O 2373 C CB . THR A 298 ? 0.8269 0.8101 0.7307 0.0656 0.0927 -0.0688 298 THR A CB 2374 O OG1 . THR A 298 ? 0.8735 0.8029 0.7265 0.0556 0.0943 -0.0556 298 THR A OG1 2375 C CG2 . THR A 298 ? 0.8122 0.7965 0.7426 0.0883 0.0851 -0.0703 298 THR A CG2 2376 N N . ILE A 299 ? 0.8741 0.8944 0.7364 0.0129 0.1123 -0.0797 299 ILE A N 2377 C CA . ILE A 299 ? 0.9503 0.9653 0.7671 -0.0278 0.1249 -0.0813 299 ILE A CA 2378 C C . ILE A 299 ? 0.9410 1.0020 0.7801 -0.0497 0.1286 -0.0920 299 ILE A C 2379 O O . ILE A 299 ? 0.8716 0.9945 0.7692 -0.0278 0.1221 -0.1033 299 ILE A O 2380 C CB . ILE A 299 ? 0.9781 1.0378 0.7997 -0.0383 0.1310 -0.0922 299 ILE A CB 2381 C CG1 . ILE A 299 ? 1.0479 1.1148 0.8218 -0.0905 0.1469 -0.0985 299 ILE A CG1 2382 C CG2 . ILE A 299 ? 0.9224 1.0639 0.8142 -0.0176 0.1261 -0.1100 299 ILE A CG2 2383 C CD1 . ILE A 299 ? 1.1582 1.1181 0.8332 -0.1147 0.1566 -0.0813 299 ILE A CD1 2384 N N . GLY A 300 ? 1.0155 1.0412 0.7986 -0.0913 0.1397 -0.0891 300 GLY A N 2385 C CA . GLY A 300 ? 1.0295 1.1116 0.8260 -0.1221 0.1457 -0.1029 300 GLY A CA 2386 C C . GLY A 300 ? 1.0818 1.1054 0.8543 -0.1253 0.1440 -0.0921 300 GLY A C 2387 O O . GLY A 300 ? 1.1175 1.0394 0.8354 -0.1166 0.1432 -0.0734 300 GLY A O 2388 N N . GLU A 301 ? 1.0867 1.1795 0.8973 -0.1327 0.1429 -0.1049 301 GLU A N 2389 C CA . GLU A 301 ? 1.1347 1.1851 0.9278 -0.1390 0.1419 -0.0975 301 GLU A CA 2390 C C . GLU A 301 ? 1.0342 1.0879 0.8856 -0.0813 0.1240 -0.0895 301 GLU A C 2391 O O . GLU A 301 ? 0.9659 1.0978 0.8729 -0.0601 0.1174 -0.1011 301 GLU A O 2392 C CB . GLU A 301 ? 1.2122 1.3452 1.0088 -0.1846 0.1522 -0.1186 301 GLU A CB 2393 C CG . GLU A 301 ? 1.3509 1.4107 1.0827 -0.2261 0.1627 -0.1131 301 GLU A CG 2394 C CD . GLU A 301 ? 1.5159 1.4518 1.1395 -0.2681 0.1797 -0.1021 301 GLU A CD 2395 O OE1 . GLU A 301 ? 1.5899 1.5460 1.1672 -0.3278 0.1987 -0.1168 301 GLU A OE1 2396 O OE2 . GLU A 301 ? 1.6182 1.4354 1.1957 -0.2389 0.1745 -0.0793 301 GLU A OE2 2397 N N . CYS A 302 ? 1.0204 0.9895 0.8507 -0.0547 0.1170 -0.0708 302 CYS A N 2398 C CA . CYS A 302 ? 0.9582 0.9309 0.8373 -0.0070 0.1026 -0.0655 302 CYS A CA 2399 C C . CYS A 302 ? 0.9489 0.8680 0.8167 0.0071 0.0960 -0.0530 302 CYS A C 2400 O O . CYS A 302 ? 0.9714 0.8233 0.7806 -0.0077 0.1006 -0.0433 302 CYS A O 2401 C CB . CYS A 302 ? 0.9655 0.9189 0.8438 0.0159 0.0989 -0.0609 302 CYS A CB 2402 S SG . CYS A 302 ? 0.9765 0.9980 0.8804 0.0100 0.1040 -0.0766 302 CYS A SG 2403 N N . PRO A 303 ? 0.8920 0.8336 0.8073 0.0369 0.0862 -0.0537 303 PRO A N 2404 C CA . PRO A 303 ? 0.8938 0.7901 0.8021 0.0548 0.0788 -0.0425 303 PRO A CA 2405 C C . PRO A 303 ? 0.9236 0.7782 0.8035 0.0731 0.0753 -0.0341 303 PRO A C 2406 O O . PRO A 303 ? 0.9445 0.8121 0.8233 0.0755 0.0772 -0.0376 303 PRO A O 2407 C CB . PRO A 303 ? 0.8536 0.7834 0.8123 0.0789 0.0719 -0.0476 303 PRO A CB 2408 C CG . PRO A 303 ? 0.8326 0.8203 0.8172 0.0790 0.0753 -0.0609 303 PRO A CG 2409 C CD . PRO A 303 ? 0.8433 0.8436 0.8083 0.0572 0.0828 -0.0652 303 PRO A CD 2410 N N . LYS A 304 ? 0.9386 0.7529 0.7953 0.0894 0.0696 -0.0249 304 LYS A N 2411 C CA . LYS A 304 ? 0.9543 0.7466 0.7815 0.1163 0.0643 -0.0196 304 LYS A CA 2412 C C . LYS A 304 ? 0.8645 0.7093 0.7416 0.1332 0.0579 -0.0285 304 LYS A C 2413 O O . LYS A 304 ? 0.8274 0.6922 0.7422 0.1317 0.0557 -0.0327 304 LYS A O 2414 C CB . LYS A 304 ? 1.0290 0.7654 0.8057 0.1333 0.0604 -0.0091 304 LYS A CB 2415 C CG . LYS A 304 ? 1.1649 0.8286 0.8734 0.1084 0.0706 -0.0017 304 LYS A CG 2416 C CD . LYS A 304 ? 1.2822 0.8971 0.9221 0.1015 0.0795 0.0024 304 LYS A CD 2417 C CE . LYS A 304 ? 1.3548 0.9392 0.9573 0.0483 0.0958 -0.0003 304 LYS A CE 2418 N NZ . LYS A 304 ? 1.4726 0.9776 0.9793 0.0411 0.1066 0.0066 304 LYS A NZ 2419 N N . TYR A 305 ? 0.8408 0.7046 0.7101 0.1461 0.0567 -0.0324 305 TYR A N 2420 C CA . TYR A 305 ? 0.7944 0.7100 0.7020 0.1507 0.0545 -0.0452 305 TYR A CA 2421 C C . TYR A 305 ? 0.7861 0.7213 0.6883 0.1711 0.0469 -0.0474 305 TYR A C 2422 O O . TYR A 305 ? 0.8316 0.7567 0.6922 0.1979 0.0412 -0.0416 305 TYR A O 2423 C CB . TYR A 305 ? 0.7984 0.7412 0.7022 0.1516 0.0574 -0.0525 305 TYR A CB 2424 C CG . TYR A 305 ? 0.7666 0.7629 0.6985 0.1497 0.0576 -0.0690 305 TYR A CG 2425 C CD1 . TYR A 305 ? 0.7484 0.7511 0.7108 0.1292 0.0646 -0.0798 305 TYR A CD1 2426 C CD2 . TYR A 305 ? 0.7757 0.8155 0.6944 0.1682 0.0522 -0.0759 305 TYR A CD2 2427 C CE1 . TYR A 305 ? 0.7438 0.7805 0.7163 0.1169 0.0690 -0.0971 305 TYR A CE1 2428 C CE2 . TYR A 305 ? 0.7689 0.8685 0.7096 0.1551 0.0553 -0.0958 305 TYR A CE2 2429 C CZ . TYR A 305 ? 0.7496 0.8403 0.7143 0.1242 0.0652 -0.1064 305 TYR A CZ 2430 O OH . TYR A 305 ? 0.7355 0.8708 0.7068 0.1011 0.0725 -0.1282 305 TYR A OH 2431 N N . VAL A 306 ? 0.7613 0.7238 0.6975 0.1602 0.0475 -0.0571 306 VAL A N 2432 C CA . VAL A 306 ? 0.7324 0.7377 0.6700 0.1706 0.0424 -0.0659 306 VAL A CA 2433 C C . VAL A 306 ? 0.7249 0.7748 0.6874 0.1451 0.0498 -0.0856 306 VAL A C 2434 O O . VAL A 306 ? 0.7313 0.7552 0.7065 0.1237 0.0584 -0.0885 306 VAL A O 2435 C CB . VAL A 306 ? 0.7336 0.7169 0.6734 0.1733 0.0384 -0.0590 306 VAL A CB 2436 C CG1 . VAL A 306 ? 0.7577 0.6911 0.6586 0.1961 0.0329 -0.0425 306 VAL A CG1 2437 C CG2 . VAL A 306 ? 0.7242 0.6770 0.6894 0.1491 0.0447 -0.0574 306 VAL A CG2 2438 N N . LYS A 307 ? 0.7349 0.8522 0.6958 0.1476 0.0477 -0.1011 307 LYS A N 2439 C CA . LYS A 307 ? 0.7663 0.9282 0.7388 0.1121 0.0582 -0.1244 307 LYS A CA 2440 C C . LYS A 307 ? 0.7897 0.9309 0.7660 0.0834 0.0652 -0.1299 307 LYS A C 2441 O O . LYS A 307 ? 0.8690 1.0460 0.8401 0.0480 0.0759 -0.1517 307 LYS A O 2442 C CB . LYS A 307 ? 0.7792 1.0457 0.7467 0.1208 0.0544 -0.1447 307 LYS A CB 2443 C CG . LYS A 307 ? 0.8052 1.1063 0.7670 0.1297 0.0547 -0.1510 307 LYS A CG 2444 C CD . LYS A 307 ? 0.8404 1.2638 0.7973 0.1415 0.0503 -0.1747 307 LYS A CD 2445 C CE . LYS A 307 ? 0.8968 1.3590 0.8422 0.1637 0.0472 -0.1781 307 LYS A CE 2446 N NZ . LYS A 307 ? 0.9375 1.5301 0.8718 0.1946 0.0383 -0.1991 307 LYS A NZ 2447 N N . SER A 308 ? 0.7721 0.8557 0.7509 0.0939 0.0610 -0.1121 308 SER A N 2448 C CA . SER A 308 ? 0.7432 0.8036 0.7194 0.0707 0.0671 -0.1158 308 SER A CA 2449 C C . SER A 308 ? 0.7760 0.7706 0.7370 0.0436 0.0816 -0.1193 308 SER A C 2450 O O . SER A 308 ? 0.7671 0.7213 0.7283 0.0542 0.0828 -0.1114 308 SER A O 2451 C CB . SER A 308 ? 0.7230 0.7458 0.7046 0.0934 0.0576 -0.0960 308 SER A CB 2452 O OG . SER A 308 ? 0.7083 0.7653 0.6875 0.1256 0.0450 -0.0899 308 SER A OG 2453 N N . ASN A 309 ? 0.8472 0.8270 0.7860 0.0101 0.0932 -0.1318 309 ASN A N 2454 C CA . ASN A 309 ? 0.9323 0.8196 0.8340 -0.0079 0.1076 -0.1317 309 ASN A CA 2455 C C . ASN A 309 ? 0.9199 0.7484 0.8212 0.0162 0.1015 -0.1117 309 ASN A C 2456 O O . ASN A 309 ? 0.9639 0.7159 0.8356 0.0243 0.1082 -0.1061 309 ASN A O 2457 C CB . ASN A 309 ? 1.0172 0.8964 0.8749 -0.0618 0.1269 -0.1551 309 ASN A CB 2458 C CG . ASN A 309 ? 1.0914 1.0095 0.9349 -0.0947 0.1390 -0.1789 309 ASN A CG 2459 O OD1 . ASN A 309 ? 1.0900 1.0026 0.9431 -0.0768 0.1368 -0.1759 309 ASN A OD1 2460 N ND2 . ASN A 309 ? 1.1690 1.1341 0.9880 -0.1475 0.1531 -0.2055 309 ASN A ND2 2461 N N . ARG A 310 ? 0.8778 0.7436 0.8066 0.0320 0.0886 -0.1020 310 ARG A N 2462 C CA . ARG A 310 ? 0.8921 0.7134 0.8197 0.0482 0.0839 -0.0865 310 ARG A CA 2463 C C . ARG A 310 ? 0.8169 0.6807 0.7776 0.0721 0.0679 -0.0745 310 ARG A C 2464 O O . ARG A 310 ? 0.8127 0.7321 0.7816 0.0685 0.0633 -0.0817 310 ARG A O 2465 C CB . ARG A 310 ? 0.9878 0.7737 0.8772 0.0163 0.0964 -0.0954 310 ARG A CB 2466 C CG . ARG A 310 ? 1.0451 0.7647 0.9158 0.0318 0.0957 -0.0809 310 ARG A CG 2467 C CD . ARG A 310 ? 1.1353 0.8189 0.9598 -0.0054 0.1096 -0.0906 310 ARG A CD 2468 N NE . ARG A 310 ? 1.1989 0.8564 1.0229 0.0113 0.1032 -0.0763 310 ARG A NE 2469 C CZ . ARG A 310 ? 1.2711 0.8521 1.0644 0.0381 0.1042 -0.0629 310 ARG A CZ 2470 N NH1 . ARG A 310 ? 1.3499 0.8689 1.1065 0.0559 0.1110 -0.0619 310 ARG A NH1 2471 N NH2 . ARG A 310 ? 1.2904 0.8610 1.0862 0.0519 0.0979 -0.0517 310 ARG A NH2 2472 N N . LEU A 311 ? 0.7789 0.6191 0.7520 0.0968 0.0604 -0.0587 311 LEU A N 2473 C CA . LEU A 311 ? 0.7493 0.6060 0.7381 0.1137 0.0489 -0.0475 311 LEU A CA 2474 C C . LEU A 311 ? 0.7422 0.5634 0.7320 0.1230 0.0474 -0.0367 311 LEU A C 2475 O O . LEU A 311 ? 0.7277 0.5376 0.7211 0.1340 0.0474 -0.0321 311 LEU A O 2476 C CB . LEU A 311 ? 0.7274 0.6008 0.7221 0.1293 0.0423 -0.0417 311 LEU A CB 2477 C CG . LEU A 311 ? 0.7328 0.6461 0.7218 0.1330 0.0406 -0.0501 311 LEU A CG 2478 C CD1 . LEU A 311 ? 0.7395 0.6424 0.7178 0.1484 0.0369 -0.0415 311 LEU A CD1 2479 C CD2 . LEU A 311 ? 0.7452 0.6985 0.7288 0.1416 0.0344 -0.0555 311 LEU A CD2 2480 N N . VAL A 312 ? 0.7228 0.5379 0.7091 0.1193 0.0459 -0.0347 312 VAL A N 2481 C CA . VAL A 312 ? 0.7063 0.4945 0.6913 0.1298 0.0439 -0.0254 312 VAL A CA 2482 C C . VAL A 312 ? 0.6764 0.4814 0.6721 0.1328 0.0358 -0.0197 312 VAL A C 2483 O O . VAL A 312 ? 0.6610 0.4811 0.6528 0.1228 0.0357 -0.0251 312 VAL A O 2484 C CB . VAL A 312 ? 0.7432 0.4845 0.6958 0.1217 0.0537 -0.0287 312 VAL A CB 2485 C CG1 . VAL A 312 ? 0.7431 0.4605 0.6890 0.1392 0.0504 -0.0189 312 VAL A CG1 2486 C CG2 . VAL A 312 ? 0.7757 0.4843 0.7036 0.1223 0.0632 -0.0349 312 VAL A CG2 2487 N N . LEU A 313 ? 0.6597 0.4667 0.6653 0.1439 0.0302 -0.0115 313 LEU A N 2488 C CA . LEU A 313 ? 0.6499 0.4617 0.6581 0.1468 0.0237 -0.0060 313 LEU A CA 2489 C C . LEU A 313 ? 0.6609 0.4622 0.6705 0.1494 0.0232 -0.0019 313 LEU A C 2490 O O . LEU A 313 ? 0.6863 0.4834 0.6962 0.1580 0.0249 -0.0003 313 LEU A O 2491 C CB . LEU A 313 ? 0.6453 0.4569 0.6505 0.1477 0.0216 -0.0018 313 LEU A CB 2492 C CG . LEU A 313 ? 0.6758 0.4807 0.6621 0.1493 0.0212 -0.0022 313 LEU A CG 2493 C CD1 . LEU A 313 ? 0.6999 0.4912 0.6704 0.1386 0.0248 0.0001 313 LEU A CD1 2494 C CD2 . LEU A 313 ? 0.6973 0.4961 0.6640 0.1619 0.0155 -0.0012 313 LEU A CD2 2495 N N . ALA A 314 ? 0.6464 0.4497 0.6542 0.1464 0.0201 -0.0013 314 ALA A N 2496 C CA . ALA A 314 ? 0.6516 0.4468 0.6597 0.1498 0.0182 0.0038 314 ALA A CA 2497 C C . ALA A 314 ? 0.6442 0.4511 0.6612 0.1548 0.0140 0.0081 314 ALA A C 2498 O O . ALA A 314 ? 0.6456 0.4539 0.6581 0.1508 0.0120 0.0080 314 ALA A O 2499 C CB . ALA A 314 ? 0.6636 0.4674 0.6692 0.1435 0.0157 0.0019 314 ALA A CB 2500 N N . THR A 315 ? 0.6549 0.4682 0.6748 0.1635 0.0140 0.0101 315 THR A N 2501 C CA . THR A 315 ? 0.6395 0.4800 0.6674 0.1616 0.0113 0.0100 315 THR A CA 2502 C C . THR A 315 ? 0.6196 0.4607 0.6474 0.1684 0.0078 0.0139 315 THR A C 2503 O O . THR A 315 ? 0.6253 0.4737 0.6553 0.1591 0.0052 0.0142 315 THR A O 2504 C CB . THR A 315 ? 0.6528 0.5303 0.6868 0.1698 0.0133 0.0045 315 THR A CB 2505 O OG1 . THR A 315 ? 0.6519 0.5163 0.6754 0.1954 0.0143 0.0057 315 THR A OG1 2506 C CG2 . THR A 315 ? 0.6674 0.5522 0.7012 0.1550 0.0174 -0.0004 315 THR A CG2 2507 N N . GLY A 316 ? 0.6158 0.4395 0.6318 0.1848 0.0091 0.0168 316 GLY A N 2508 C CA . GLY A 316 ? 0.6324 0.4482 0.6400 0.1926 0.0068 0.0215 316 GLY A CA 2509 C C . GLY A 316 ? 0.6476 0.4363 0.6476 0.1768 0.0078 0.0232 316 GLY A C 2510 O O . GLY A 316 ? 0.6151 0.4082 0.6228 0.1624 0.0077 0.0194 316 GLY A O 2511 N N . LEU A 317 ? 0.6715 0.4361 0.6508 0.1817 0.0094 0.0275 317 LEU A N 2512 C CA . LEU A 317 ? 0.6899 0.4465 0.6640 0.1631 0.0104 0.0265 317 LEU A CA 2513 C C . LEU A 317 ? 0.7337 0.4387 0.6645 0.1517 0.0213 0.0257 317 LEU A C 2514 O O . LEU A 317 ? 0.7591 0.4197 0.6561 0.1646 0.0277 0.0282 317 LEU A O 2515 C CB . LEU A 317 ? 0.6942 0.4706 0.6788 0.1673 0.0040 0.0303 317 LEU A CB 2516 C CG . LEU A 317 ? 0.7218 0.4924 0.6920 0.1902 0.0026 0.0368 317 LEU A CG 2517 C CD1 . LEU A 317 ? 0.7955 0.5058 0.7162 0.1921 0.0106 0.0417 317 LEU A CD1 2518 C CD2 . LEU A 317 ? 0.7011 0.5090 0.6920 0.1906 -0.0045 0.0374 317 LEU A CD2 2519 N N . ARG A 318 ? 0.7314 0.4419 0.6558 0.1259 0.0248 0.0199 318 ARG A N 2520 C CA . ARG A 318 ? 0.7956 0.4594 0.6702 0.0984 0.0392 0.0145 318 ARG A CA 2521 C C . ARG A 318 ? 0.8536 0.4420 0.6720 0.1124 0.0460 0.0250 318 ARG A C 2522 O O . ARG A 318 ? 0.8666 0.4570 0.6843 0.1233 0.0410 0.0321 318 ARG A O 2523 C CB . ARG A 318 ? 0.7907 0.4986 0.6732 0.0673 0.0406 0.0035 318 ARG A CB 2524 C CG . ARG A 318 ? 0.8744 0.5538 0.7054 0.0220 0.0588 -0.0091 318 ARG A CG 2525 C CD . ARG A 318 ? 0.8788 0.6314 0.7254 -0.0070 0.0587 -0.0242 318 ARG A CD 2526 N NE . ARG A 318 ? 0.8380 0.6767 0.7238 -0.0088 0.0528 -0.0397 318 ARG A NE 2527 C CZ . ARG A 318 ? 0.8655 0.7346 0.7336 -0.0458 0.0648 -0.0594 318 ARG A CZ 2528 N NH1 . ARG A 318 ? 0.9548 0.7624 0.7598 -0.0925 0.0861 -0.0665 318 ARG A NH1 2529 N NH2 . ARG A 318 ? 0.8286 0.7857 0.7326 -0.0363 0.0569 -0.0731 318 ARG A NH2 2530 N N . ASN A 319 ? 0.9459 0.4628 0.7095 0.1162 0.0574 0.0259 319 ASN A N 2531 C CA . ASN A 319 ? 1.0454 0.4735 0.7358 0.1433 0.0640 0.0368 319 ASN A CA 2532 C C . ASN A 319 ? 1.1905 0.5385 0.8018 0.1064 0.0817 0.0351 319 ASN A C 2533 O O . ASN A 319 ? 1.2353 0.5678 0.8215 0.0557 0.0962 0.0220 319 ASN A O 2534 C CB . ASN A 319 ? 1.0767 0.4520 0.7284 0.1731 0.0687 0.0385 319 ASN A CB 2535 C CG . ASN A 319 ? 1.1601 0.4626 0.7413 0.2262 0.0695 0.0506 319 ASN A CG 2536 O OD1 . ASN A 319 ? 1.1708 0.4743 0.7432 0.2422 0.0645 0.0585 319 ASN A OD1 2537 N ND2 . ASN A 319 ? 1.2279 0.4673 0.7532 0.2583 0.0756 0.0514 319 ASN A ND2 2538 N N . SER A 320 ? 1.3341 0.6338 0.9007 0.1302 0.0815 0.0470 320 SER A N 2539 C CA . SER A 320 ? 1.4787 0.6985 0.9639 0.0944 0.0984 0.0471 320 SER A CA 2540 C C . SER A 320 ? 1.6603 0.7239 1.0121 0.0920 0.1213 0.0500 320 SER A C 2541 O O . SER A 320 ? 1.6519 0.6660 0.9702 0.1451 0.1187 0.0580 320 SER A O 2542 C CB . SER A 320 ? 1.4690 0.7029 0.9606 0.1253 0.0874 0.0597 320 SER A CB 2543 O OG . SER A 320 ? 1.3727 0.7350 0.9767 0.1390 0.0663 0.0580 320 SER A OG 2544 N N . PRO A 321 ? 1.8041 0.7892 1.0719 0.0287 0.1453 0.0413 321 PRO A N 2545 C CA . PRO A 321 ? 2.0424 0.8538 1.1598 0.0166 0.1720 0.0427 321 PRO A CA 2546 C C . PRO A 321 ? 2.1797 0.8619 1.1817 0.0486 0.1800 0.0604 321 PRO A C 2547 O O . PRO A 321 ? 2.1993 0.8810 1.2069 0.1295 0.1627 0.0773 321 PRO A O 2548 C CB . PRO A 321 ? 2.0885 0.8989 1.1764 -0.0823 0.1961 0.0193 321 PRO A CB 2549 C CG . PRO A 321 ? 1.9721 0.9136 1.1503 -0.1103 0.1842 0.0130 321 PRO A CG 2550 C CD . PRO A 321 ? 1.8023 0.8633 1.1074 -0.0412 0.1508 0.0252 321 PRO A CD 2551 N N . GLY B 1 ? 0.4771 0.6410 0.8004 -0.0867 -0.1107 0.1409 1 GLY B N 2552 C CA . GLY B 1 ? 0.4450 0.5906 0.7532 -0.0609 -0.0983 0.1147 1 GLY B CA 2553 C C . GLY B 1 ? 0.4178 0.6194 0.7406 -0.0272 -0.0760 0.1224 1 GLY B C 2554 O O . GLY B 1 ? 0.3957 0.6527 0.7370 -0.0144 -0.0639 0.1423 1 GLY B O 2555 N N . LEU B 2 ? 0.4052 0.5863 0.7115 -0.0087 -0.0698 0.1064 2 LEU B N 2556 C CA . LEU B 2 ? 0.3926 0.6132 0.7009 0.0276 -0.0529 0.1143 2 LEU B CA 2557 C C . LEU B 2 ? 0.3860 0.6089 0.6805 0.0570 -0.0321 0.1047 2 LEU B C 2558 O O . LEU B 2 ? 0.3610 0.6337 0.6597 0.0889 -0.0188 0.1205 2 LEU B O 2559 C CB . LEU B 2 ? 0.4021 0.5759 0.6814 0.0418 -0.0508 0.0953 2 LEU B CB 2560 C CG . LEU B 2 ? 0.3927 0.5759 0.6800 0.0270 -0.0687 0.1079 2 LEU B CG 2561 C CD1 . LEU B 2 ? 0.4205 0.5477 0.6705 0.0441 -0.0626 0.0881 2 LEU B CD1 2562 C CD2 . LEU B 2 ? 0.3889 0.6623 0.7128 0.0358 -0.0730 0.1447 2 LEU B CD2 2563 N N . PHE B 3 ? 0.3705 0.5431 0.6458 0.0489 -0.0303 0.0794 3 PHE B N 2564 C CA . PHE B 3 ? 0.3937 0.5576 0.6474 0.0746 -0.0153 0.0650 3 PHE B CA 2565 C C . PHE B 3 ? 0.3962 0.5976 0.6643 0.0723 -0.0124 0.0795 3 PHE B C 2566 O O . PHE B 3 ? 0.4354 0.6326 0.6822 0.0953 -0.0015 0.0683 3 PHE B O 2567 C CB . PHE B 3 ? 0.4116 0.5055 0.6344 0.0690 -0.0157 0.0294 3 PHE B CB 2568 C CG . PHE B 3 ? 0.4169 0.4721 0.6171 0.0760 -0.0147 0.0190 3 PHE B CG 2569 C CD1 . PHE B 3 ? 0.4273 0.4604 0.5938 0.1075 -0.0056 0.0120 3 PHE B CD1 2570 C CD2 . PHE B 3 ? 0.4220 0.4599 0.6280 0.0545 -0.0239 0.0192 3 PHE B CD2 2571 C CE1 . PHE B 3 ? 0.4776 0.4668 0.6171 0.1146 -0.0060 0.0060 3 PHE B CE1 2572 C CE2 . PHE B 3 ? 0.4327 0.4368 0.6158 0.0620 -0.0226 0.0144 3 PHE B CE2 2573 C CZ . PHE B 3 ? 0.4629 0.4417 0.6138 0.0907 -0.0137 0.0089 3 PHE B CZ 2574 N N . GLY B 4 ? 0.3665 0.5995 0.6651 0.0436 -0.0243 0.1054 4 GLY B N 2575 C CA . GLY B 4 ? 0.3538 0.6297 0.6676 0.0389 -0.0216 0.1301 4 GLY B CA 2576 C C . GLY B 4 ? 0.3726 0.6090 0.6688 0.0320 -0.0243 0.1141 4 GLY B C 2577 O O . GLY B 4 ? 0.4092 0.6751 0.7139 0.0264 -0.0232 0.1372 4 GLY B O 2578 N N . ALA B 5 ? 0.3643 0.5409 0.6370 0.0325 -0.0276 0.0786 5 ALA B N 2579 C CA . ALA B 5 ? 0.3702 0.5199 0.6262 0.0339 -0.0292 0.0621 5 ALA B CA 2580 C C . ALA B 5 ? 0.3874 0.5046 0.6439 0.0081 -0.0465 0.0664 5 ALA B C 2581 O O . ALA B 5 ? 0.3998 0.5220 0.6563 0.0005 -0.0518 0.0855 5 ALA B O 2582 C CB . ALA B 5 ? 0.3764 0.4913 0.6102 0.0463 -0.0251 0.0255 5 ALA B CB 2583 N N . ILE B 6 ? 0.4070 0.4850 0.6563 -0.0029 -0.0557 0.0494 6 ILE B N 2584 C CA . ILE B 6 ? 0.4531 0.4855 0.6877 -0.0194 -0.0736 0.0484 6 ILE B CA 2585 C C . ILE B 6 ? 0.4617 0.4949 0.7044 -0.0469 -0.0907 0.0814 6 ILE B C 2586 O O . ILE B 6 ? 0.4433 0.5026 0.7051 -0.0610 -0.0949 0.0976 6 ILE B O 2587 C CB . ILE B 6 ? 0.4868 0.4828 0.7071 -0.0204 -0.0776 0.0251 6 ILE B CB 2588 C CG1 . ILE B 6 ? 0.5046 0.4996 0.7165 -0.0015 -0.0655 -0.0022 6 ILE B CG1 2589 C CG2 . ILE B 6 ? 0.5331 0.4755 0.7279 -0.0339 -0.0989 0.0267 6 ILE B CG2 2590 C CD1 . ILE B 6 ? 0.5478 0.5280 0.7522 -0.0013 -0.0617 -0.0208 6 ILE B CD1 2591 N N . ALA B 7 ? 0.4987 0.5036 0.7254 -0.0564 -0.1026 0.0936 7 ALA B N 2592 C CA . ALA B 7 ? 0.5430 0.5409 0.7734 -0.0919 -0.1233 0.1290 7 ALA B CA 2593 C C . ALA B 7 ? 0.5434 0.6277 0.8171 -0.1004 -0.1122 0.1628 7 ALA B C 2594 O O . ALA B 7 ? 0.6041 0.7106 0.8976 -0.1321 -0.1275 0.1908 7 ALA B O 2595 C CB . ALA B 7 ? 0.5642 0.5078 0.7757 -0.1153 -0.1485 0.1232 7 ALA B CB 2596 N N . GLY B 8 ? 0.5388 0.6746 0.8243 -0.0693 -0.0864 0.1596 8 GLY B N 2597 C CA . GLY B 8 ? 0.5083 0.7319 0.8267 -0.0617 -0.0698 0.1895 8 GLY B CA 2598 C C . GLY B 8 ? 0.5193 0.7694 0.8301 -0.0418 -0.0538 0.2002 8 GLY B C 2599 O O . GLY B 8 ? 0.5647 0.8041 0.8704 -0.0632 -0.0637 0.2250 8 GLY B O 2600 N N . PHE B 9 ? 0.4813 0.7563 0.7830 -0.0011 -0.0316 0.1810 9 PHE B N 2601 C CA . PHE B 9 ? 0.4805 0.7788 0.7673 0.0214 -0.0177 0.1888 9 PHE B CA 2602 C C . PHE B 9 ? 0.4983 0.7302 0.7543 0.0233 -0.0279 0.1619 9 PHE B C 2603 O O . PHE B 9 ? 0.5348 0.7704 0.7759 0.0300 -0.0255 0.1748 9 PHE B O 2604 C CB . PHE B 9 ? 0.4751 0.8179 0.7519 0.0669 0.0061 0.1790 9 PHE B CB 2605 C CG . PHE B 9 ? 0.4662 0.7575 0.7140 0.0897 0.0069 0.1300 9 PHE B CG 2606 C CD1 . PHE B 9 ? 0.4847 0.7422 0.7025 0.1033 0.0052 0.1036 9 PHE B CD1 2607 C CD2 . PHE B 9 ? 0.4593 0.7394 0.7091 0.0956 0.0081 0.1136 9 PHE B CD2 2608 C CE1 . PHE B 9 ? 0.4882 0.7045 0.6829 0.1154 0.0025 0.0630 9 PHE B CE1 2609 C CE2 . PHE B 9 ? 0.4678 0.6976 0.6895 0.1092 0.0071 0.0734 9 PHE B CE2 2610 C CZ . PHE B 9 ? 0.4868 0.6864 0.6830 0.1157 0.0035 0.0487 9 PHE B CZ 2611 N N . ILE B 10 ? 0.4922 0.6697 0.7383 0.0198 -0.0384 0.1275 10 ILE B N 2612 C CA . ILE B 10 ? 0.5226 0.6451 0.7442 0.0202 -0.0506 0.1084 10 ILE B CA 2613 C C . ILE B 10 ? 0.5817 0.6559 0.7983 -0.0110 -0.0721 0.1232 10 ILE B C 2614 O O . ILE B 10 ? 0.6225 0.6691 0.8407 -0.0234 -0.0815 0.1107 10 ILE B O 2615 C CB . ILE B 10 ? 0.4877 0.5884 0.6994 0.0367 -0.0488 0.0661 10 ILE B CB 2616 C CG1 . ILE B 10 ? 0.4781 0.6120 0.6860 0.0613 -0.0336 0.0514 10 ILE B CG1 2617 C CG2 . ILE B 10 ? 0.5123 0.5778 0.7020 0.0454 -0.0586 0.0513 10 ILE B CG2 2618 C CD1 . ILE B 10 ? 0.4754 0.5908 0.6777 0.0661 -0.0340 0.0155 10 ILE B CD1 2619 N N . GLU B 11 ? 0.6720 0.7295 0.8752 -0.0236 -0.0815 0.1508 11 GLU B N 2620 C CA . GLU B 11 ? 0.7502 0.7566 0.9420 -0.0614 -0.1063 0.1751 11 GLU B CA 2621 C C . GLU B 11 ? 0.7342 0.6575 0.8927 -0.0615 -0.1256 0.1460 11 GLU B C 2622 O O . GLU B 11 ? 0.7647 0.6513 0.9174 -0.0906 -0.1454 0.1531 11 GLU B O 2623 C CB . GLU B 11 ? 0.8695 0.8545 1.0389 -0.0710 -0.1138 0.2067 11 GLU B CB 2624 C CG . GLU B 11 ? 0.9489 0.9734 1.1418 -0.1120 -0.1188 0.2603 11 GLU B CG 2625 C CD . GLU B 11 ? 1.0731 1.0284 1.2268 -0.1368 -0.1401 0.2899 11 GLU B CD 2626 O OE1 . GLU B 11 ? 1.0964 1.0205 1.2158 -0.1070 -0.1354 0.2806 11 GLU B OE1 2627 O OE2 . GLU B 11 ? 1.1572 1.0845 1.3106 -0.1875 -0.1645 0.3229 11 GLU B OE2 2628 N N . GLY B 12 ? 0.7068 0.6039 0.8402 -0.0273 -0.1209 0.1153 12 GLY B N 2629 C CA . GLY B 12 ? 0.7225 0.5486 0.8183 -0.0154 -0.1351 0.0884 12 GLY B CA 2630 C C . GLY B 12 ? 0.6833 0.5300 0.7772 0.0243 -0.1205 0.0535 12 GLY B C 2631 O O . GLY B 12 ? 0.6398 0.5419 0.7536 0.0408 -0.1046 0.0491 12 GLY B O 2632 N N . GLY B 13 ? 0.6972 0.5024 0.7650 0.0395 -0.1271 0.0300 13 GLY B N 2633 C CA . GLY B 13 ? 0.6799 0.5180 0.7517 0.0733 -0.1137 0.0013 13 GLY B CA 2634 C C . GLY B 13 ? 0.7157 0.5377 0.7566 0.1079 -0.1178 -0.0022 13 GLY B C 2635 O O . GLY B 13 ? 0.7854 0.5589 0.7955 0.1066 -0.1309 0.0168 13 GLY B O 2636 N N . TRP B 14 ? 0.6897 0.5553 0.7387 0.1381 -0.1075 -0.0240 14 TRP B N 2637 C CA . TRP B 14 ? 0.7217 0.5950 0.7497 0.1766 -0.1097 -0.0280 14 TRP B CA 2638 C C . TRP B 14 ? 0.7867 0.6411 0.7825 0.2154 -0.1115 -0.0451 14 TRP B C 2639 O O . TRP B 14 ? 0.7405 0.6579 0.7639 0.2252 -0.0985 -0.0611 14 TRP B O 2640 C CB . TRP B 14 ? 0.6380 0.6019 0.7085 0.1812 -0.0973 -0.0360 14 TRP B CB 2641 C CG . TRP B 14 ? 0.6068 0.5877 0.6935 0.1597 -0.0949 -0.0204 14 TRP B CG 2642 C CD1 . TRP B 14 ? 0.6401 0.5777 0.7072 0.1468 -0.1016 0.0052 14 TRP B CD1 2643 C CD2 . TRP B 14 ? 0.5567 0.6021 0.6761 0.1512 -0.0854 -0.0279 14 TRP B CD2 2644 N NE1 . TRP B 14 ? 0.6046 0.5860 0.6928 0.1359 -0.0929 0.0152 14 TRP B NE1 2645 C CE2 . TRP B 14 ? 0.5620 0.6021 0.6768 0.1410 -0.0842 -0.0073 14 TRP B CE2 2646 C CE3 . TRP B 14 ? 0.5178 0.6209 0.6648 0.1498 -0.0798 -0.0486 14 TRP B CE3 2647 C CZ2 . TRP B 14 ? 0.5522 0.6368 0.6815 0.1377 -0.0764 -0.0106 14 TRP B CZ2 2648 C CZ3 . TRP B 14 ? 0.5108 0.6471 0.6705 0.1393 -0.0766 -0.0525 14 TRP B CZ3 2649 C CH2 . TRP B 14 ? 0.5251 0.6494 0.6723 0.1375 -0.0744 -0.0355 14 TRP B CH2 2650 N N . GLN B 15 ? 0.9129 0.6793 0.8454 0.2389 -0.1279 -0.0398 15 GLN B N 2651 C CA . GLN B 15 ? 0.9974 0.7413 0.8844 0.2922 -0.1294 -0.0555 15 GLN B CA 2652 C C . GLN B 15 ? 0.9177 0.7621 0.8352 0.3306 -0.1160 -0.0638 15 GLN B C 2653 O O . GLN B 15 ? 0.9209 0.8054 0.8341 0.3691 -0.1070 -0.0772 15 GLN B O 2654 C CB . GLN B 15 ? 1.1486 0.7681 0.9499 0.3169 -0.1528 -0.0471 15 GLN B CB 2655 C CG . GLN B 15 ? 1.2428 0.7505 1.0020 0.2774 -0.1744 -0.0373 15 GLN B CG 2656 C CD . GLN B 15 ? 1.3329 0.7749 1.0370 0.2994 -0.1820 -0.0568 15 GLN B CD 2657 O OE1 . GLN B 15 ? 1.3789 0.8010 1.0913 0.2609 -0.1874 -0.0578 15 GLN B OE1 2658 N NE2 . GLN B 15 ? 1.4092 0.8185 1.0525 0.3661 -0.1828 -0.0719 15 GLN B NE2 2659 N N . GLY B 16 ? 0.8734 0.7621 0.8196 0.3210 -0.1157 -0.0539 16 GLY B N 2660 C CA . GLY B 16 ? 0.8447 0.8301 0.8196 0.3520 -0.1091 -0.0597 16 GLY B CA 2661 C C . GLY B 16 ? 0.7651 0.8639 0.8089 0.3306 -0.0945 -0.0714 16 GLY B C 2662 O O . GLY B 16 ? 0.7482 0.9357 0.8170 0.3555 -0.0913 -0.0763 16 GLY B O 2663 N N . MET B 17 ? 0.6830 0.7808 0.7566 0.2836 -0.0877 -0.0737 17 MET B N 2664 C CA . MET B 17 ? 0.6377 0.8244 0.7666 0.2592 -0.0762 -0.0833 17 MET B CA 2665 C C . MET B 17 ? 0.6394 0.8385 0.7674 0.2696 -0.0654 -0.0904 17 MET B C 2666 O O . MET B 17 ? 0.6654 0.8104 0.7807 0.2499 -0.0628 -0.0912 17 MET B O 2667 C CB . MET B 17 ? 0.6183 0.7961 0.7735 0.2086 -0.0739 -0.0819 17 MET B CB 2668 C CG . MET B 17 ? 0.5870 0.8388 0.7878 0.1815 -0.0662 -0.0913 17 MET B CG 2669 S SD . MET B 17 ? 0.5600 0.7954 0.7761 0.1368 -0.0670 -0.0918 17 MET B SD 2670 C CE . MET B 17 ? 0.6310 0.7832 0.8240 0.1271 -0.0631 -0.0826 17 MET B CE 2671 N N . VAL B 18 ? 0.6405 0.9222 0.7846 0.3006 -0.0587 -0.0937 18 VAL B N 2672 C CA . VAL B 18 ? 0.6667 0.9616 0.7943 0.3317 -0.0470 -0.0974 18 VAL B CA 2673 C C . VAL B 18 ? 0.6229 1.0120 0.8043 0.3030 -0.0314 -0.0972 18 VAL B C 2674 O O . VAL B 18 ? 0.6534 1.0456 0.8229 0.3149 -0.0186 -0.0983 18 VAL B O 2675 C CB . VAL B 18 ? 0.7324 1.0544 0.8296 0.4009 -0.0484 -0.0966 18 VAL B CB 2676 C CG1 . VAL B 18 ? 0.7207 1.1760 0.8583 0.4246 -0.0321 -0.0945 18 VAL B CG1 2677 C CG2 . VAL B 18 ? 0.8310 1.0292 0.8440 0.4426 -0.0560 -0.1003 18 VAL B CG2 2678 N N . ASP B 19 ? 0.6021 1.0623 0.8368 0.2636 -0.0339 -0.0951 19 ASP B N 2679 C CA . ASP B 19 ? 0.5780 1.1350 0.8639 0.2331 -0.0229 -0.0907 19 ASP B CA 2680 C C . ASP B 19 ? 0.5144 1.0359 0.8183 0.1702 -0.0240 -0.0924 19 ASP B C 2681 O O . ASP B 19 ? 0.5433 1.1293 0.8873 0.1314 -0.0224 -0.0882 19 ASP B O 2682 C CB . ASP B 19 ? 0.5838 1.2600 0.9142 0.2366 -0.0294 -0.0853 19 ASP B CB 2683 C CG . ASP B 19 ? 0.6101 1.2641 0.9421 0.2190 -0.0497 -0.0903 19 ASP B CG 2684 O OD1 . ASP B 19 ? 0.5756 1.1275 0.8748 0.2094 -0.0552 -0.0955 19 ASP B OD1 2685 O OD2 . ASP B 19 ? 0.6695 1.4144 1.0349 0.2160 -0.0603 -0.0873 19 ASP B OD2 2686 N N . GLY B 20 ? 0.4950 0.9139 0.7671 0.1596 -0.0280 -0.0967 20 GLY B N 2687 C CA . GLY B 20 ? 0.4847 0.8697 0.7666 0.1119 -0.0259 -0.0973 20 GLY B CA 2688 C C . GLY B 20 ? 0.4886 0.7741 0.7360 0.1103 -0.0290 -0.0982 20 GLY B C 2689 O O . GLY B 20 ? 0.5262 0.7636 0.7427 0.1379 -0.0358 -0.0975 20 GLY B O 2690 N N . TRP B 21 ? 0.4837 0.7376 0.7347 0.0767 -0.0257 -0.0975 21 TRP B N 2691 C CA . TRP B 21 ? 0.4804 0.6551 0.7054 0.0732 -0.0297 -0.0950 21 TRP B CA 2692 C C . TRP B 21 ? 0.4440 0.5946 0.6694 0.0641 -0.0388 -0.0928 21 TRP B C 2693 O O . TRP B 21 ? 0.4581 0.5606 0.6643 0.0701 -0.0449 -0.0857 21 TRP B O 2694 C CB . TRP B 21 ? 0.5125 0.6656 0.7369 0.0497 -0.0223 -0.0931 21 TRP B CB 2695 C CG . TRP B 21 ? 0.5520 0.6868 0.7516 0.0680 -0.0164 -0.0927 21 TRP B CG 2696 C CD1 . TRP B 21 ? 0.5985 0.6926 0.7617 0.0992 -0.0231 -0.0946 21 TRP B CD1 2697 C CD2 . TRP B 21 ? 0.5790 0.7232 0.7778 0.0566 -0.0050 -0.0902 21 TRP B CD2 2698 N NE1 . TRP B 21 ? 0.6261 0.7039 0.7629 0.1110 -0.0170 -0.0964 21 TRP B NE1 2699 C CE2 . TRP B 21 ? 0.6108 0.7251 0.7719 0.0857 -0.0040 -0.0925 21 TRP B CE2 2700 C CE3 . TRP B 21 ? 0.6172 0.7830 0.8362 0.0244 0.0031 -0.0856 21 TRP B CE3 2701 C CZ2 . TRP B 21 ? 0.6597 0.7763 0.8059 0.0863 0.0072 -0.0901 21 TRP B CZ2 2702 C CZ3 . TRP B 21 ? 0.6540 0.8209 0.8613 0.0211 0.0146 -0.0803 21 TRP B CZ3 2703 C CH2 . TRP B 21 ? 0.6877 0.8354 0.8603 0.0533 0.0179 -0.0824 21 TRP B CH2 2704 N N . TYR B 22 ? 0.4060 0.5912 0.6499 0.0488 -0.0409 -0.0974 22 TYR B N 2705 C CA . TYR B 22 ? 0.4090 0.5754 0.6467 0.0451 -0.0474 -0.0966 22 TYR B CA 2706 C C . TYR B 22 ? 0.3901 0.6028 0.6371 0.0479 -0.0554 -0.1037 22 TYR B C 2707 O O . TYR B 22 ? 0.4092 0.6707 0.6758 0.0353 -0.0570 -0.1094 22 TYR B O 2708 C CB . TYR B 22 ? 0.3971 0.5338 0.6312 0.0222 -0.0448 -0.0977 22 TYR B CB 2709 C CG . TYR B 22 ? 0.4069 0.5193 0.6399 0.0100 -0.0373 -0.0942 22 TYR B CG 2710 C CD1 . TYR B 22 ? 0.4324 0.5125 0.6554 0.0181 -0.0363 -0.0848 22 TYR B CD1 2711 C CD2 . TYR B 22 ? 0.4327 0.5515 0.6712 -0.0127 -0.0337 -0.0986 22 TYR B CD2 2712 C CE1 . TYR B 22 ? 0.4467 0.5045 0.6646 0.0085 -0.0316 -0.0819 22 TYR B CE1 2713 C CE2 . TYR B 22 ? 0.4433 0.5385 0.6761 -0.0217 -0.0264 -0.0936 22 TYR B CE2 2714 C CZ . TYR B 22 ? 0.4598 0.5261 0.6821 -0.0087 -0.0253 -0.0864 22 TYR B CZ 2715 O OH . TYR B 22 ? 0.4830 0.5267 0.6961 -0.0158 -0.0204 -0.0819 22 TYR B OH 2716 N N . GLY B 23 ? 0.4002 0.6023 0.6335 0.0614 -0.0615 -0.1011 23 GLY B N 2717 C CA . GLY B 23 ? 0.4147 0.6569 0.6504 0.0648 -0.0724 -0.1089 23 GLY B CA 2718 C C . GLY B 23 ? 0.4471 0.6705 0.6600 0.0833 -0.0764 -0.1030 23 GLY B C 2719 O O . GLY B 23 ? 0.4402 0.6238 0.6393 0.0847 -0.0697 -0.0928 23 GLY B O 2720 N N . TYR B 24 ? 0.4784 0.7394 0.6891 0.0983 -0.0870 -0.1066 24 TYR B N 2721 C CA . TYR B 24 ? 0.4985 0.7505 0.6834 0.1161 -0.0921 -0.1019 24 TYR B CA 2722 C C . TYR B 24 ? 0.4997 0.7642 0.6760 0.1470 -0.0960 -0.0907 24 TYR B C 2723 O O . TYR B 24 ? 0.5162 0.8144 0.7064 0.1590 -0.0996 -0.0932 24 TYR B O 2724 C CB . TYR B 24 ? 0.5387 0.8169 0.7155 0.1070 -0.1071 -0.1186 24 TYR B CB 2725 C CG . TYR B 24 ? 0.5596 0.8217 0.7382 0.0743 -0.1101 -0.1330 24 TYR B CG 2726 C CD1 . TYR B 24 ? 0.5403 0.8341 0.7491 0.0483 -0.1139 -0.1387 24 TYR B CD1 2727 C CD2 . TYR B 24 ? 0.6268 0.8403 0.7717 0.0721 -0.1087 -0.1386 24 TYR B CD2 2728 C CE1 . TYR B 24 ? 0.6056 0.8749 0.8105 0.0141 -0.1186 -0.1488 24 TYR B CE1 2729 C CE2 . TYR B 24 ? 0.6663 0.8480 0.8011 0.0450 -0.1138 -0.1520 24 TYR B CE2 2730 C CZ . TYR B 24 ? 0.6648 0.8704 0.8292 0.0127 -0.1199 -0.1566 24 TYR B CZ 2731 O OH . TYR B 24 ? 0.7273 0.8945 0.8779 -0.0189 -0.1270 -0.1666 24 TYR B OH 2732 N N . HIS B 25 ? 0.5122 0.7512 0.6621 0.1628 -0.0946 -0.0762 25 HIS B N 2733 C CA . HIS B 25 ? 0.5355 0.7796 0.6666 0.1931 -0.1013 -0.0648 25 HIS B CA 2734 C C . HIS B 25 ? 0.5554 0.8140 0.6626 0.2045 -0.1074 -0.0639 25 HIS B C 2735 O O . HIS B 25 ? 0.5470 0.7849 0.6396 0.1979 -0.0994 -0.0572 25 HIS B O 2736 C CB . HIS B 25 ? 0.5474 0.7349 0.6597 0.1999 -0.0954 -0.0410 25 HIS B CB 2737 C CG . HIS B 25 ? 0.5963 0.7713 0.6791 0.2317 -0.1037 -0.0272 25 HIS B CG 2738 N ND1 . HIS B 25 ? 0.6156 0.7735 0.6698 0.2409 -0.1039 -0.0064 25 HIS B ND1 2739 C CD2 . HIS B 25 ? 0.6211 0.7992 0.6939 0.2611 -0.1116 -0.0300 25 HIS B CD2 2740 C CE1 . HIS B 25 ? 0.6727 0.8143 0.6986 0.2712 -0.1132 0.0033 25 HIS B CE1 2741 N NE2 . HIS B 25 ? 0.6667 0.8194 0.7019 0.2868 -0.1183 -0.0118 25 HIS B NE2 2742 N N . HIS B 26 ? 0.5822 0.8803 0.6826 0.2257 -0.1213 -0.0694 26 HIS B N 2743 C CA . HIS B 26 ? 0.6256 0.9375 0.6960 0.2392 -0.1300 -0.0705 26 HIS B CA 2744 C C . HIS B 26 ? 0.6693 0.9761 0.7105 0.2742 -0.1337 -0.0502 26 HIS B C 2745 O O . HIS B 26 ? 0.6703 0.9757 0.7156 0.2921 -0.1365 -0.0432 26 HIS B O 2746 C CB . HIS B 26 ? 0.6118 0.9759 0.6924 0.2285 -0.1496 -0.0963 26 HIS B CB 2747 C CG . HIS B 26 ? 0.6173 1.0413 0.7177 0.2449 -0.1641 -0.0990 26 HIS B CG 2748 N ND1 . HIS B 26 ? 0.6142 1.0737 0.7554 0.2360 -0.1625 -0.1030 26 HIS B ND1 2749 C CD2 . HIS B 26 ? 0.6546 1.1170 0.7388 0.2744 -0.1797 -0.0960 26 HIS B CD2 2750 C CE1 . HIS B 26 ? 0.6055 1.1294 0.7579 0.2612 -0.1755 -0.1018 26 HIS B CE1 2751 N NE2 . HIS B 26 ? 0.6529 1.1786 0.7716 0.2842 -0.1875 -0.0982 26 HIS B NE2 2752 N N . SER B 27 ? 0.7175 1.0175 0.7228 0.2873 -0.1333 -0.0404 27 SER B N 2753 C CA . SER B 27 ? 0.7672 1.0584 0.7358 0.3201 -0.1367 -0.0175 27 SER B CA 2754 C C . SER B 27 ? 0.7854 1.1064 0.7213 0.3358 -0.1471 -0.0258 27 SER B C 2755 O O . SER B 27 ? 0.8010 1.1120 0.7177 0.3289 -0.1382 -0.0269 27 SER B O 2756 C CB . SER B 27 ? 0.7992 1.0375 0.7487 0.3157 -0.1189 0.0169 27 SER B CB 2757 O OG . SER B 27 ? 0.8567 1.0519 0.8050 0.3193 -0.1196 0.0342 27 SER B OG 2758 N N . ASN B 28 ? 0.8195 1.1775 0.7438 0.3610 -0.1665 -0.0315 28 ASN B N 2759 C CA . ASN B 28 ? 0.8440 1.2266 0.7286 0.3790 -0.1803 -0.0387 28 ASN B CA 2760 C C . ASN B 28 ? 0.8994 1.3053 0.7626 0.4178 -0.1952 -0.0259 28 ASN B C 2761 O O . ASN B 28 ? 0.9112 1.3020 0.7844 0.4325 -0.1918 -0.0100 28 ASN B O 2762 C CB . ASN B 28 ? 0.8306 1.2478 0.7278 0.3550 -0.1994 -0.0754 28 ASN B CB 2763 C CG . ASN B 28 ? 0.8002 1.2764 0.7439 0.3447 -0.2196 -0.0917 28 ASN B CG 2764 O OD1 . ASN B 28 ? 0.8364 1.3398 0.7910 0.3707 -0.2234 -0.0789 28 ASN B OD1 2765 N ND2 . ASN B 28 ? 0.7764 1.2742 0.7443 0.3082 -0.2331 -0.1179 28 ASN B ND2 2766 N N . GLU B 29 ? 0.9335 1.3698 0.7603 0.4382 -0.2131 -0.0331 29 GLU B N 2767 C CA . GLU B 29 ? 1.0055 1.4604 0.8043 0.4801 -0.2263 -0.0170 29 GLU B CA 2768 C C . GLU B 29 ? 0.9990 1.5112 0.8394 0.4914 -0.2445 -0.0277 29 GLU B C 2769 O O . GLU B 29 ? 1.0192 1.5374 0.8411 0.5323 -0.2510 -0.0103 29 GLU B O 2770 C CB . GLU B 29 ? 1.0829 1.5634 0.8307 0.5002 -0.2445 -0.0246 29 GLU B CB 2771 C CG . GLU B 29 ? 1.1231 1.5581 0.8194 0.5032 -0.2243 -0.0098 29 GLU B CG 2772 C CD . GLU B 29 ? 1.2077 1.6613 0.8385 0.5357 -0.2409 -0.0119 29 GLU B CD 2773 O OE1 . GLU B 29 ? 1.2199 1.7167 0.8412 0.5595 -0.2686 -0.0179 29 GLU B OE1 2774 O OE2 . GLU B 29 ? 1.2673 1.6959 0.8528 0.5409 -0.2257 -0.0065 29 GLU B OE2 2775 N N . GLN B 30 ? 0.9583 1.5155 0.8513 0.4582 -0.2524 -0.0536 30 GLN B N 2776 C CA . GLN B 30 ? 0.9569 1.5893 0.8960 0.4683 -0.2670 -0.0606 30 GLN B CA 2777 C C . GLN B 30 ? 0.8945 1.4946 0.8566 0.4771 -0.2460 -0.0477 30 GLN B C 2778 O O . GLN B 30 ? 0.8936 1.5482 0.8815 0.5026 -0.2523 -0.0468 30 GLN B O 2779 C CB . GLN B 30 ? 0.9685 1.6714 0.9548 0.4243 -0.2863 -0.0892 30 GLN B CB 2780 C CG . GLN B 30 ? 1.0229 1.7627 0.9829 0.4150 -0.3180 -0.1069 30 GLN B CG 2781 C CD . GLN B 30 ? 1.0395 1.7864 1.0212 0.3557 -0.3319 -0.1347 30 GLN B CD 2782 O OE1 . GLN B 30 ? 1.0140 1.6885 0.9831 0.3302 -0.3136 -0.1411 30 GLN B OE1 2783 N NE2 . GLN B 30 ? 1.0649 1.8989 1.0771 0.3328 -0.3665 -0.1493 30 GLN B NE2 2784 N N . GLY B 31 ? 0.8459 1.3612 0.7959 0.4586 -0.2223 -0.0373 31 GLY B N 2785 C CA . GLY B 31 ? 0.8225 1.2919 0.7836 0.4634 -0.2059 -0.0270 31 GLY B CA 2786 C C . GLY B 31 ? 0.7568 1.1779 0.7389 0.4182 -0.1869 -0.0313 31 GLY B C 2787 O O . GLY B 31 ? 0.7563 1.1519 0.7282 0.3922 -0.1800 -0.0316 31 GLY B O 2788 N N . SER B 32 ? 0.7132 1.1233 0.7206 0.4141 -0.1782 -0.0339 32 SER B N 2789 C CA . SER B 32 ? 0.6644 1.0285 0.6901 0.3745 -0.1617 -0.0365 32 SER B CA 2790 C C . SER B 32 ? 0.6329 1.0219 0.6954 0.3698 -0.1571 -0.0483 32 SER B C 2791 O O . SER B 32 ? 0.6495 1.0813 0.7170 0.4044 -0.1633 -0.0496 32 SER B O 2792 C CB . SER B 32 ? 0.6957 0.9648 0.6828 0.3748 -0.1504 -0.0107 32 SER B CB 2793 O OG . SER B 32 ? 0.7312 0.9552 0.6918 0.4068 -0.1532 0.0006 32 SER B OG 2794 N N . GLY B 33 ? 0.6040 0.9725 0.6907 0.3307 -0.1454 -0.0559 33 GLY B N 2795 C CA . GLY B 33 ? 0.6041 0.9869 0.7183 0.3271 -0.1381 -0.0637 33 GLY B CA 2796 C C . GLY B 33 ? 0.5687 0.9384 0.7109 0.2816 -0.1271 -0.0730 33 GLY B C 2797 O O . GLY B 33 ? 0.5895 0.9376 0.7305 0.2525 -0.1249 -0.0749 33 GLY B O 2798 N N . TYR B 34 ? 0.5816 0.9642 0.7437 0.2812 -0.1194 -0.0778 34 TYR B N 2799 C CA . TYR B 34 ? 0.5404 0.9062 0.7247 0.2424 -0.1084 -0.0845 34 TYR B CA 2800 C C . TYR B 34 ? 0.5200 0.9697 0.7491 0.2186 -0.1104 -0.0969 34 TYR B C 2801 O O . TYR B 34 ? 0.5256 1.0541 0.7751 0.2386 -0.1156 -0.0975 34 TYR B O 2802 C CB . TYR B 34 ? 0.5561 0.8684 0.7234 0.2558 -0.0987 -0.0795 34 TYR B CB 2803 C CG . TYR B 34 ? 0.6047 0.8244 0.7244 0.2708 -0.1014 -0.0644 34 TYR B CG 2804 C CD1 . TYR B 34 ? 0.6011 0.7609 0.7134 0.2391 -0.0979 -0.0554 34 TYR B CD1 2805 C CD2 . TYR B 34 ? 0.6793 0.8718 0.7595 0.3160 -0.1089 -0.0566 34 TYR B CD2 2806 C CE1 . TYR B 34 ? 0.6539 0.7356 0.7265 0.2438 -0.1030 -0.0364 34 TYR B CE1 2807 C CE2 . TYR B 34 ? 0.7292 0.8260 0.7600 0.3227 -0.1151 -0.0397 34 TYR B CE2 2808 C CZ . TYR B 34 ? 0.7371 0.7821 0.7673 0.2824 -0.1127 -0.0285 34 TYR B CZ 2809 O OH . TYR B 34 ? 0.8280 0.7844 0.8130 0.2804 -0.1213 -0.0070 34 TYR B OH 2810 N N . ALA B 35 ? 0.5215 0.9561 0.7646 0.1754 -0.1073 -0.1041 35 ALA B N 2811 C CA . ALA B 35 ? 0.5184 1.0155 0.7995 0.1418 -0.1100 -0.1124 35 ALA B CA 2812 C C . ALA B 35 ? 0.5183 0.9669 0.8027 0.1084 -0.0977 -0.1144 35 ALA B C 2813 O O . ALA B 35 ? 0.5132 0.9001 0.7776 0.0922 -0.0968 -0.1171 35 ALA B O 2814 C CB . ALA B 35 ? 0.5206 1.0515 0.8058 0.1189 -0.1301 -0.1220 35 ALA B CB 2815 N N . ALA B 36 ? 0.5238 1.0057 0.8311 0.1033 -0.0872 -0.1114 36 ALA B N 2816 C CA . ALA B 36 ? 0.5263 0.9721 0.8374 0.0726 -0.0761 -0.1117 36 ALA B CA 2817 C C . ALA B 36 ? 0.5254 0.9728 0.8460 0.0244 -0.0864 -0.1190 36 ALA B C 2818 O O . ALA B 36 ? 0.5485 1.0595 0.8906 0.0057 -0.1006 -0.1214 36 ALA B O 2819 C CB . ALA B 36 ? 0.5369 1.0318 0.8678 0.0819 -0.0624 -0.1050 36 ALA B CB 2820 N N . ASP B 37 ? 0.5319 0.9063 0.8324 0.0053 -0.0817 -0.1217 37 ASP B N 2821 C CA . ASP B 37 ? 0.5559 0.9081 0.8522 -0.0375 -0.0903 -0.1284 37 ASP B CA 2822 C C . ASP B 37 ? 0.5827 0.9619 0.9031 -0.0638 -0.0800 -0.1198 37 ASP B C 2823 O O . ASP B 37 ? 0.5535 0.8943 0.8660 -0.0587 -0.0643 -0.1144 37 ASP B O 2824 C CB . ASP B 37 ? 0.5829 0.8464 0.8417 -0.0354 -0.0870 -0.1328 37 ASP B CB 2825 C CG . ASP B 37 ? 0.6236 0.8440 0.8599 -0.0701 -0.0992 -0.1425 37 ASP B CG 2826 O OD1 . ASP B 37 ? 0.6600 0.8787 0.8784 -0.0786 -0.1187 -0.1539 37 ASP B OD1 2827 O OD2 . ASP B 37 ? 0.6352 0.8154 0.8643 -0.0873 -0.0913 -0.1391 37 ASP B OD2 2828 N N . LYS B 38 ? 0.6528 1.1043 1.0031 -0.0933 -0.0899 -0.1161 38 LYS B N 2829 C CA . LYS B 38 ? 0.6945 1.1975 1.0746 -0.1185 -0.0787 -0.1019 38 LYS B CA 2830 C C . LYS B 38 ? 0.6942 1.1211 1.0518 -0.1540 -0.0750 -0.1003 38 LYS B C 2831 O O . LYS B 38 ? 0.6574 1.0827 1.0187 -0.1519 -0.0562 -0.0896 38 LYS B O 2832 C CB . LYS B 38 ? 0.7652 1.3721 1.1861 -0.1500 -0.0941 -0.0940 38 LYS B CB 2833 C CG . LYS B 38 ? 0.8602 1.5489 1.3206 -0.1770 -0.0809 -0.0724 38 LYS B CG 2834 C CD . LYS B 38 ? 0.9406 1.6091 1.4019 -0.2500 -0.0965 -0.0653 38 LYS B CD 2835 C CE . LYS B 38 ? 0.9589 1.6901 1.4436 -0.2935 -0.1289 -0.0647 38 LYS B CE 2836 N NZ . LYS B 38 ? 0.9529 1.8468 1.5039 -0.2969 -0.1245 -0.0414 38 LYS B NZ 2837 N N . GLU B 39 ? 0.7273 1.0846 1.0532 -0.1807 -0.0936 -0.1117 39 GLU B N 2838 C CA . GLU B 39 ? 0.7637 1.0409 1.0595 -0.2129 -0.0940 -0.1103 39 GLU B CA 2839 C C . GLU B 39 ? 0.6940 0.9092 0.9677 -0.1817 -0.0734 -0.1087 39 GLU B C 2840 O O . GLU B 39 ? 0.6894 0.8877 0.9611 -0.1971 -0.0617 -0.0975 39 GLU B O 2841 C CB . GLU B 39 ? 0.8801 1.0789 1.1297 -0.2360 -0.1203 -0.1266 39 GLU B CB 2842 C CG . GLU B 39 ? 0.9991 1.0859 1.1974 -0.2463 -0.1193 -0.1293 39 GLU B CG 2843 C CD . GLU B 39 ? 1.1422 1.1433 1.2833 -0.2715 -0.1485 -0.1455 39 GLU B CD 2844 O OE1 . GLU B 39 ? 1.2139 1.2203 1.3559 -0.3269 -0.1706 -0.1419 39 GLU B OE1 2845 O OE2 . GLU B 39 ? 1.1857 1.1140 1.2776 -0.2359 -0.1504 -0.1608 39 GLU B OE2 2846 N N . SER B 40 ? 0.6335 0.8177 0.8904 -0.1407 -0.0702 -0.1173 40 SER B N 2847 C CA . SER B 40 ? 0.5841 0.7141 0.8219 -0.1166 -0.0558 -0.1139 40 SER B CA 2848 C C . SER B 40 ? 0.5465 0.7178 0.8077 -0.0992 -0.0389 -0.1031 40 SER B C 2849 O O . SER B 40 ? 0.5151 0.6523 0.7648 -0.0955 -0.0283 -0.0966 40 SER B O 2850 C CB . SER B 40 ? 0.5564 0.6494 0.7716 -0.0840 -0.0581 -0.1209 40 SER B CB 2851 O OG . SER B 40 ? 0.5665 0.7047 0.7998 -0.0581 -0.0572 -0.1199 40 SER B OG 2852 N N . THR B 41 ? 0.4890 0.7305 0.7767 -0.0848 -0.0379 -0.1017 41 THR B N 2853 C CA . THR B 41 ? 0.4672 0.7446 0.7658 -0.0617 -0.0232 -0.0938 41 THR B CA 2854 C C . THR B 41 ? 0.4528 0.7540 0.7611 -0.0877 -0.0120 -0.0823 41 THR B C 2855 O O . THR B 41 ? 0.4245 0.7018 0.7184 -0.0766 0.0002 -0.0770 41 THR B O 2856 C CB . THR B 41 ? 0.4756 0.8280 0.7955 -0.0352 -0.0245 -0.0939 41 THR B CB 2857 O OG1 . THR B 41 ? 0.4912 0.8139 0.7955 -0.0073 -0.0331 -0.1009 41 THR B OG1 2858 C CG2 . THR B 41 ? 0.4887 0.8745 0.8089 -0.0051 -0.0089 -0.0869 41 THR B CG2 2859 N N . GLN B 42 ? 0.4755 0.8237 0.8060 -0.1254 -0.0181 -0.0766 42 GLN B N 2860 C CA . GLN B 42 ? 0.5172 0.9015 0.8609 -0.1553 -0.0066 -0.0594 42 GLN B CA 2861 C C . GLN B 42 ? 0.5185 0.8135 0.8281 -0.1738 -0.0036 -0.0568 42 GLN B C 2862 O O . GLN B 42 ? 0.5253 0.8266 0.8309 -0.1761 0.0120 -0.0436 42 GLN B O 2863 C CB . GLN B 42 ? 0.5536 1.0063 0.9297 -0.2031 -0.0190 -0.0499 42 GLN B CB 2864 C CG . GLN B 42 ? 0.6059 1.1170 1.0035 -0.2378 -0.0055 -0.0247 42 GLN B CG 2865 C CD . GLN B 42 ? 0.6209 1.2224 1.0400 -0.1965 0.0201 -0.0122 42 GLN B CD 2866 O OE1 . GLN B 42 ? 0.6913 1.2766 1.0931 -0.1863 0.0394 -0.0025 42 GLN B OE1 2867 N NE2 . GLN B 42 ? 0.5912 1.2858 1.0417 -0.1680 0.0198 -0.0127 42 GLN B NE2 2868 N N . LYS B 43 ? 0.5364 0.7508 0.8176 -0.1821 -0.0182 -0.0686 43 LYS B N 2869 C CA . LYS B 43 ? 0.6076 0.7332 0.8509 -0.1867 -0.0162 -0.0674 43 LYS B CA 2870 C C . LYS B 43 ? 0.5676 0.6773 0.8009 -0.1501 -0.0016 -0.0649 43 LYS B C 2871 O O . LYS B 43 ? 0.5899 0.6656 0.8039 -0.1561 0.0065 -0.0553 43 LYS B O 2872 C CB . LYS B 43 ? 0.7015 0.7534 0.9130 -0.1811 -0.0320 -0.0825 43 LYS B CB 2873 C CG . LYS B 43 ? 0.8576 0.8221 1.0258 -0.2041 -0.0390 -0.0808 43 LYS B CG 2874 C CD . LYS B 43 ? 0.9620 0.8752 1.0990 -0.2153 -0.0610 -0.0962 43 LYS B CD 2875 C CE . LYS B 43 ? 1.0654 0.8818 1.1489 -0.2425 -0.0721 -0.0946 43 LYS B CE 2876 N NZ . LYS B 43 ? 1.1750 0.9450 1.2240 -0.2607 -0.0983 -0.1110 43 LYS B NZ 2877 N N . ALA B 44 ? 0.4738 0.6018 0.7151 -0.1144 -0.0014 -0.0729 44 ALA B N 2878 C CA . ALA B 44 ? 0.4777 0.5847 0.7051 -0.0847 0.0055 -0.0716 44 ALA B CA 2879 C C . ALA B 44 ? 0.4777 0.6270 0.7084 -0.0787 0.0200 -0.0627 44 ALA B C 2880 O O . ALA B 44 ? 0.5112 0.6304 0.7196 -0.0704 0.0262 -0.0579 44 ALA B O 2881 C CB . ALA B 44 ? 0.4746 0.5819 0.7039 -0.0540 -0.0014 -0.0798 44 ALA B CB 2882 N N . ILE B 45 ? 0.4748 0.7001 0.7315 -0.0791 0.0257 -0.0594 45 ILE B N 2883 C CA . ILE B 45 ? 0.4925 0.7722 0.7510 -0.0654 0.0432 -0.0487 45 ILE B CA 2884 C C . ILE B 45 ? 0.5164 0.7896 0.7677 -0.0973 0.0539 -0.0323 45 ILE B C 2885 O O . ILE B 45 ? 0.5647 0.8331 0.7933 -0.0800 0.0669 -0.0258 45 ILE B O 2886 C CB . ILE B 45 ? 0.5076 0.8889 0.8018 -0.0583 0.0481 -0.0442 45 ILE B CB 2887 C CG1 . ILE B 45 ? 0.4949 0.8740 0.7826 -0.0141 0.0402 -0.0586 45 ILE B CG1 2888 C CG2 . ILE B 45 ? 0.5050 0.9619 0.8057 -0.0491 0.0705 -0.0268 45 ILE B CG2 2889 C CD1 . ILE B 45 ? 0.5291 1.0090 0.8520 -0.0029 0.0418 -0.0546 45 ILE B CD1 2890 N N . ASP B 46 ? 0.5249 0.7894 0.7875 -0.1433 0.0465 -0.0255 46 ASP B N 2891 C CA . ASP B 46 ? 0.5632 0.8033 0.8110 -0.1784 0.0535 -0.0074 46 ASP B CA 2892 C C . ASP B 46 ? 0.5705 0.7203 0.7750 -0.1637 0.0534 -0.0104 46 ASP B C 2893 O O . ASP B 46 ? 0.6177 0.7604 0.8027 -0.1675 0.0661 0.0044 46 ASP B O 2894 C CB . ASP B 46 ? 0.5935 0.8152 0.8484 -0.2324 0.0383 -0.0021 46 ASP B CB 2895 C CG . ASP B 46 ? 0.5921 0.9145 0.8938 -0.2580 0.0351 0.0060 46 ASP B CG 2896 O OD1 . ASP B 46 ? 0.5430 0.9587 0.8737 -0.2290 0.0489 0.0101 46 ASP B OD1 2897 O OD2 . ASP B 46 ? 0.6473 0.9530 0.9523 -0.3053 0.0164 0.0081 46 ASP B OD2 2898 N N . GLY B 47 ? 0.5453 0.6344 0.7355 -0.1458 0.0394 -0.0269 47 GLY B N 2899 C CA . GLY B 47 ? 0.5685 0.5850 0.7239 -0.1319 0.0367 -0.0274 47 GLY B CA 2900 C C . GLY B 47 ? 0.5609 0.5839 0.7008 -0.0998 0.0441 -0.0271 47 GLY B C 2901 O O . GLY B 47 ? 0.5821 0.5788 0.6948 -0.0989 0.0501 -0.0171 47 GLY B O 2902 N N . VAL B 48 ? 0.5587 0.6098 0.7086 -0.0724 0.0416 -0.0384 48 VAL B N 2903 C CA . VAL B 48 ? 0.5498 0.5933 0.6738 -0.0400 0.0430 -0.0422 48 VAL B CA 2904 C C . VAL B 48 ? 0.5677 0.6529 0.6792 -0.0349 0.0628 -0.0306 48 VAL B C 2905 O O . VAL B 48 ? 0.6101 0.6675 0.6851 -0.0197 0.0654 -0.0281 48 VAL B O 2906 C CB . VAL B 48 ? 0.5530 0.6081 0.6833 -0.0135 0.0341 -0.0558 48 VAL B CB 2907 C CG1 . VAL B 48 ? 0.5867 0.6289 0.6789 0.0216 0.0342 -0.0615 48 VAL B CG1 2908 C CG2 . VAL B 48 ? 0.5501 0.5622 0.6864 -0.0173 0.0159 -0.0619 48 VAL B CG2 2909 N N . THR B 49 ? 0.5384 0.6957 0.6801 -0.0491 0.0764 -0.0210 49 THR B N 2910 C CA . THR B 49 ? 0.5587 0.7754 0.6954 -0.0460 0.0991 -0.0036 49 THR B CA 2911 C C . THR B 49 ? 0.6123 0.7953 0.7272 -0.0731 0.1062 0.0143 49 THR B C 2912 O O . THR B 49 ? 0.6522 0.8434 0.7357 -0.0552 0.1208 0.0242 49 THR B O 2913 C CB . THR B 49 ? 0.5394 0.8559 0.7243 -0.0648 0.1099 0.0087 49 THR B CB 2914 O OG1 . THR B 49 ? 0.4924 0.8399 0.6931 -0.0334 0.1031 -0.0073 49 THR B OG1 2915 C CG2 . THR B 49 ? 0.5605 0.9590 0.7457 -0.0591 0.1369 0.0321 49 THR B CG2 2916 N N . ASN B 50 ? 0.6286 0.7673 0.7517 -0.1124 0.0953 0.0188 50 ASN B N 2917 C CA . ASN B 50 ? 0.6686 0.7571 0.7618 -0.1354 0.0989 0.0360 50 ASN B CA 2918 C C . ASN B 50 ? 0.6815 0.7047 0.7310 -0.1040 0.0919 0.0279 50 ASN B C 2919 O O . ASN B 50 ? 0.7229 0.7305 0.7393 -0.1021 0.1015 0.0424 50 ASN B O 2920 C CB . ASN B 50 ? 0.6940 0.7316 0.7924 -0.1774 0.0850 0.0394 50 ASN B CB 2921 C CG . ASN B 50 ? 0.7166 0.8135 0.8499 -0.2224 0.0887 0.0543 50 ASN B CG 2922 O OD1 . ASN B 50 ? 0.7238 0.9076 0.8785 -0.2272 0.1070 0.0715 50 ASN B OD1 2923 N ND2 . ASN B 50 ? 0.7311 0.7846 0.8679 -0.2546 0.0703 0.0487 50 ASN B ND2 2924 N N . LYS B 51 ? 0.6533 0.6434 0.7035 -0.0817 0.0739 0.0070 51 LYS B N 2925 C CA . LYS B 51 ? 0.6617 0.5997 0.6768 -0.0562 0.0614 0.0000 51 LYS B CA 2926 C C . LYS B 51 ? 0.6930 0.6472 0.6736 -0.0272 0.0702 -0.0001 51 LYS B C 2927 O O . LYS B 51 ? 0.7457 0.6693 0.6869 -0.0199 0.0706 0.0075 51 LYS B O 2928 C CB . LYS B 51 ? 0.6186 0.5375 0.6487 -0.0429 0.0410 -0.0177 51 LYS B CB 2929 C CG . LYS B 51 ? 0.6473 0.5244 0.6480 -0.0235 0.0235 -0.0225 51 LYS B CG 2930 C CD . LYS B 51 ? 0.6354 0.5027 0.6561 -0.0183 0.0039 -0.0332 51 LYS B CD 2931 C CE . LYS B 51 ? 0.6281 0.4844 0.6719 -0.0319 -0.0002 -0.0282 51 LYS B CE 2932 N NZ . LYS B 51 ? 0.6388 0.4863 0.6925 -0.0243 -0.0199 -0.0298 51 LYS B NZ 2933 N N . VAL B 52 ? 0.6614 0.6622 0.6503 -0.0064 0.0772 -0.0090 52 VAL B N 2934 C CA . VAL B 52 ? 0.6828 0.6910 0.6272 0.0309 0.0845 -0.0131 52 VAL B CA 2935 C C . VAL B 52 ? 0.7132 0.7533 0.6384 0.0250 0.1095 0.0099 52 VAL B C 2936 O O . VAL B 52 ? 0.7675 0.7754 0.6401 0.0449 0.1096 0.0116 52 VAL B O 2937 C CB . VAL B 52 ? 0.6706 0.7235 0.6228 0.0616 0.0893 -0.0258 52 VAL B CB 2938 C CG1 . VAL B 52 ? 0.7342 0.7797 0.6239 0.1099 0.0953 -0.0331 52 VAL B CG1 2939 C CG2 . VAL B 52 ? 0.6340 0.6491 0.6012 0.0636 0.0643 -0.0444 52 VAL B CG2 2940 N N . ASN B 53 ? 0.6905 0.7917 0.6558 -0.0059 0.1285 0.0299 53 ASN B N 2941 C CA . ASN B 53 ? 0.7375 0.8750 0.6892 -0.0201 0.1532 0.0589 53 ASN B CA 2942 C C . ASN B 53 ? 0.7735 0.8366 0.6910 -0.0392 0.1459 0.0703 53 ASN B C 2943 O O . ASN B 53 ? 0.8156 0.8797 0.6927 -0.0292 0.1602 0.0865 53 ASN B O 2944 C CB . ASN B 53 ? 0.7324 0.9513 0.7389 -0.0609 0.1695 0.0816 53 ASN B CB 2945 C CG . ASN B 53 ? 0.7254 1.0414 0.7626 -0.0349 0.1826 0.0778 53 ASN B CG 2946 O OD1 . ASN B 53 ? 0.7714 1.1033 0.7749 0.0185 0.1906 0.0668 53 ASN B OD1 2947 N ND2 . ASN B 53 ? 0.7115 1.0903 0.8070 -0.0701 0.1831 0.0870 53 ASN B ND2 2948 N N . SER B 54 ? 0.7750 0.7755 0.7048 -0.0609 0.1242 0.0625 54 SER B N 2949 C CA . SER B 54 ? 0.8255 0.7519 0.7195 -0.0681 0.1139 0.0708 54 SER B CA 2950 C C . SER B 54 ? 0.8589 0.7529 0.7042 -0.0286 0.1034 0.0595 54 SER B C 2951 O O . SER B 54 ? 0.8851 0.7519 0.6867 -0.0240 0.1076 0.0744 54 SER B O 2952 C CB . SER B 54 ? 0.8107 0.6817 0.7238 -0.0845 0.0919 0.0611 54 SER B CB 2953 O OG . SER B 54 ? 0.8302 0.6984 0.7636 -0.1254 0.0968 0.0749 54 SER B OG 2954 N N . ILE B 55 ? 0.8482 0.7391 0.6965 -0.0028 0.0868 0.0342 55 ILE B N 2955 C CA . ILE B 55 ? 0.8973 0.7486 0.6956 0.0289 0.0688 0.0210 55 ILE B CA 2956 C C . ILE B 55 ? 0.9759 0.8481 0.7224 0.0568 0.0875 0.0266 55 ILE B C 2957 O O . ILE B 55 ? 1.0478 0.8849 0.7417 0.0703 0.0817 0.0314 55 ILE B O 2958 C CB . ILE B 55 ? 0.9060 0.7436 0.7145 0.0442 0.0452 -0.0046 55 ILE B CB 2959 C CG1 . ILE B 55 ? 0.8641 0.6758 0.7101 0.0231 0.0239 -0.0069 55 ILE B CG1 2960 C CG2 . ILE B 55 ? 0.9780 0.7749 0.7236 0.0759 0.0261 -0.0194 55 ILE B CG2 2961 C CD1 . ILE B 55 ? 0.8483 0.6526 0.7129 0.0288 0.0027 -0.0251 55 ILE B CD1 2962 N N . ILE B 56 ? 0.9802 0.9148 0.7387 0.0697 0.1102 0.0272 56 ILE B N 2963 C CA . ILE B 56 ? 1.0225 0.9904 0.7308 0.1037 0.1333 0.0350 56 ILE B CA 2964 C C . ILE B 56 ? 1.0980 1.0738 0.7884 0.0838 0.1530 0.0669 56 ILE B C 2965 O O . ILE B 56 ? 1.1786 1.1332 0.8041 0.1107 0.1565 0.0710 56 ILE B O 2966 C CB . ILE B 56 ? 1.0126 1.0706 0.7514 0.1180 0.1601 0.0390 56 ILE B CB 2967 C CG1 . ILE B 56 ? 0.9937 1.0351 0.7331 0.1480 0.1412 0.0078 56 ILE B CG1 2968 C CG2 . ILE B 56 ? 1.0658 1.1793 0.7583 0.1528 0.1922 0.0560 56 ILE B CG2 2969 C CD1 . ILE B 56 ? 0.9774 1.1117 0.7581 0.1609 0.1641 0.0123 56 ILE B CD1 2970 N N . ASP B 57 ? 1.0939 1.0927 0.8350 0.0363 0.1638 0.0899 57 ASP B N 2971 C CA . ASP B 57 ? 1.1496 1.1564 0.8754 0.0099 0.1845 0.1261 57 ASP B CA 2972 C C . ASP B 57 ? 1.1783 1.1004 0.8517 0.0137 0.1669 0.1291 57 ASP B C 2973 O O . ASP B 57 ? 1.2079 1.1284 0.8324 0.0225 0.1819 0.1506 57 ASP B O 2974 C CB . ASP B 57 ? 1.1342 1.1645 0.9192 -0.0471 0.1915 0.1471 57 ASP B CB 2975 C CG . ASP B 57 ? 1.2269 1.2561 0.9928 -0.0820 0.2104 0.1882 57 ASP B CG 2976 O OD1 . ASP B 57 ? 1.3022 1.4013 1.0530 -0.0741 0.2401 0.2132 57 ASP B OD1 2977 O OD2 . ASP B 57 ? 1.2510 1.2081 1.0120 -0.1149 0.1962 0.1972 57 ASP B OD2 2978 N N . LYS B 58 ? 1.1501 1.0097 0.8342 0.0096 0.1355 0.1097 58 LYS B N 2979 C CA . LYS B 58 ? 1.1890 0.9789 0.8306 0.0169 0.1153 0.1124 58 LYS B CA 2980 C C . LYS B 58 ? 1.2610 1.0357 0.8362 0.0583 0.1071 0.1025 58 LYS B C 2981 O O . LYS B 58 ? 1.2978 1.0357 0.8244 0.0659 0.1024 0.1162 58 LYS B O 2982 C CB . LYS B 58 ? 1.1635 0.9111 0.8375 0.0097 0.0844 0.0943 58 LYS B CB 2983 C CG . LYS B 58 ? 1.1805 0.8871 0.8674 -0.0181 0.0822 0.1117 58 LYS B CG 2984 C CD . LYS B 58 ? 1.2291 0.9406 0.9042 -0.0477 0.1092 0.1436 58 LYS B CD 2985 C CE . LYS B 58 ? 1.2460 0.9078 0.9353 -0.0798 0.1038 0.1545 58 LYS B CE 2986 N NZ . LYS B 58 ? 1.3128 0.9538 0.9732 -0.1124 0.1227 0.1904 58 LYS B NZ 2987 N N . MET B 59 ? 1.2880 1.0844 0.8534 0.0871 0.1037 0.0785 59 MET B N 2988 C CA . MET B 59 ? 1.3765 1.1472 0.8661 0.1291 0.0925 0.0645 59 MET B CA 2989 C C . MET B 59 ? 1.4632 1.2774 0.9043 0.1529 0.1289 0.0839 59 MET B C 2990 O O . MET B 59 ? 1.5429 1.3325 0.9077 0.1919 0.1229 0.0746 59 MET B O 2991 C CB . MET B 59 ? 1.3806 1.1368 0.8656 0.1524 0.0694 0.0294 59 MET B CB 2992 C CG . MET B 59 ? 1.3256 1.0539 0.8639 0.1276 0.0371 0.0143 59 MET B CG 2993 S SD . MET B 59 ? 1.3597 1.0282 0.8810 0.1175 -0.0055 0.0135 59 MET B SD 2994 C CE . MET B 59 ? 1.4629 1.0878 0.8785 0.1559 -0.0230 0.0025 59 MET B CE 2995 N N . ASN B 60 ? 1.4765 1.3571 0.9598 0.1282 0.1652 0.1126 60 ASN B N 2996 C CA . ASN B 60 ? 1.5302 1.4739 0.9806 0.1433 0.2055 0.1415 60 ASN B CA 2997 C C . ASN B 60 ? 1.5859 1.4887 0.9557 0.1620 0.2064 0.1571 60 ASN B C 2998 O O . ASN B 60 ? 1.6185 1.5307 0.9179 0.2102 0.2161 0.1515 60 ASN B O 2999 C CB . ASN B 60 ? 1.5184 1.5299 1.0361 0.0923 0.2356 0.1784 60 ASN B CB 3000 C CG . ASN B 60 ? 1.6124 1.7095 1.1094 0.1002 0.2796 0.2161 60 ASN B CG 3001 O OD1 . ASN B 60 ? 1.6618 1.7566 1.1447 0.0704 0.2953 0.2543 60 ASN B OD1 3002 N ND2 . ASN B 60 ? 1.6333 1.8080 1.1257 0.1424 0.3006 0.2083 60 ASN B ND2 3003 N N . THR B 61 ? 1.5388 1.9342 1.1767 -0.1773 -0.4230 -0.2307 61 THR B N 3004 C CA . THR B 61 ? 1.4891 1.8084 1.1527 -0.1871 -0.3852 -0.2277 61 THR B CA 3005 C C . THR B 61 ? 1.4349 1.6989 1.0717 -0.1274 -0.3454 -0.2080 61 THR B C 3006 O O . THR B 61 ? 1.5060 1.7298 1.0671 -0.1042 -0.3430 -0.2198 61 THR B O 3007 C CB . THR B 61 ? 1.5955 1.7973 1.2028 -0.2355 -0.3947 -0.2665 61 THR B CB 3008 O OG1 . THR B 61 ? 1.6790 1.9149 1.2798 -0.3029 -0.4434 -0.2889 61 THR B OG1 3009 C CG2 . THR B 61 ? 1.5724 1.7157 1.2184 -0.2534 -0.3651 -0.2533 61 THR B CG2 3010 N N . GLN B 62 ? 1.3171 1.5906 1.0138 -0.1073 -0.3151 -0.1790 62 GLN B N 3011 C CA . GLN B 62 ? 1.2767 1.5067 0.9563 -0.0617 -0.2809 -0.1543 62 GLN B CA 3012 C C . GLN B 62 ? 1.1985 1.4362 0.9492 -0.0529 -0.2547 -0.1323 62 GLN B C 3013 O O . GLN B 62 ? 1.2121 1.5274 1.0281 -0.0626 -0.2659 -0.1284 62 GLN B O 3014 C CB . GLN B 62 ? 1.2905 1.5561 0.9359 -0.0259 -0.2973 -0.1282 62 GLN B CB 3015 C CG . GLN B 62 ? 1.2572 1.4904 0.9017 0.0095 -0.2735 -0.0886 62 GLN B CG 3016 C CD . GLN B 62 ? 1.3035 1.5437 0.8912 0.0346 -0.2970 -0.0557 62 GLN B CD 3017 O OE1 . GLN B 62 ? 1.3515 1.6215 0.8884 0.0281 -0.3233 -0.0641 62 GLN B OE1 3018 N NE2 . GLN B 62 ? 1.2943 1.4963 0.8801 0.0604 -0.2924 -0.0166 62 GLN B NE2 3019 N N . PHE B 63 ? 1.1202 1.2940 0.8571 -0.0342 -0.2204 -0.1205 63 PHE B N 3020 C CA . PHE B 63 ? 1.0547 1.2203 0.8446 -0.0289 -0.1941 -0.1058 63 PHE B CA 3021 C C . PHE B 63 ? 1.0442 1.2758 0.8874 -0.0004 -0.2028 -0.0863 63 PHE B C 3022 O O . PHE B 63 ? 1.1053 1.3463 0.9282 0.0339 -0.2217 -0.0691 63 PHE B O 3023 C CB . PHE B 63 ? 1.0027 1.1021 0.7619 -0.0110 -0.1626 -0.0941 63 PHE B CB 3024 C CG . PHE B 63 ? 0.9463 1.0276 0.7482 -0.0110 -0.1373 -0.0849 63 PHE B CG 3025 C CD1 . PHE B 63 ? 0.9295 0.9788 0.7416 -0.0365 -0.1265 -0.1000 63 PHE B CD1 3026 C CD2 . PHE B 63 ? 0.9236 1.0073 0.7449 0.0144 -0.1295 -0.0611 63 PHE B CD2 3027 C CE1 . PHE B 63 ? 0.8799 0.9181 0.7250 -0.0383 -0.1047 -0.0891 63 PHE B CE1 3028 C CE2 . PHE B 63 ? 0.8629 0.9330 0.7172 0.0144 -0.1075 -0.0572 63 PHE B CE2 3029 C CZ . PHE B 63 ? 0.8434 0.9000 0.7117 -0.0127 -0.0934 -0.0699 63 PHE B CZ 3030 N N . GLU B 64 ? 1.0137 1.2894 0.9176 -0.0123 -0.1916 -0.0902 64 GLU B N 3031 C CA . GLU B 64 ? 1.0038 1.3543 0.9617 0.0250 -0.1959 -0.0833 64 GLU B CA 3032 C C . GLU B 64 ? 0.9634 1.2775 0.9393 0.0340 -0.1628 -0.0779 64 GLU B C 3033 O O . GLU B 64 ? 0.9318 1.2364 0.9201 -0.0064 -0.1415 -0.0831 64 GLU B O 3034 C CB . GLU B 64 ? 1.0007 1.4870 1.0213 0.0000 -0.2125 -0.0983 64 GLU B CB 3035 C CG . GLU B 64 ? 1.0592 1.5951 1.0656 -0.0193 -0.2501 -0.1072 64 GLU B CG 3036 C CD . GLU B 64 ? 1.0888 1.7863 1.1659 -0.0513 -0.2685 -0.1196 64 GLU B CD 3037 O OE1 . GLU B 64 ? 1.0833 1.8666 1.2213 -0.0517 -0.2487 -0.1206 64 GLU B OE1 3038 O OE2 . GLU B 64 ? 1.1005 1.8534 1.1717 -0.0794 -0.3026 -0.1292 64 GLU B OE2 3039 N N . ALA B 65 ? 0.9866 1.2688 0.9543 0.0853 -0.1638 -0.0668 65 ALA B N 3040 C CA . ALA B 65 ? 0.9704 1.2135 0.9466 0.0954 -0.1370 -0.0652 65 ALA B CA 3041 C C . ALA B 65 ? 0.9641 1.3174 1.0048 0.1082 -0.1294 -0.0832 65 ALA B C 3042 O O . ALA B 65 ? 0.9471 1.4015 1.0245 0.1413 -0.1513 -0.0948 65 ALA B O 3043 C CB . ALA B 65 ? 1.0174 1.1672 0.9471 0.1369 -0.1471 -0.0483 65 ALA B CB 3044 N N . VAL B 66 ? 0.9632 1.3106 1.0162 0.0828 -0.0989 -0.0854 66 VAL B N 3045 C CA . VAL B 66 ? 0.9736 1.4335 1.0788 0.0884 -0.0834 -0.1010 66 VAL B CA 3046 C C . VAL B 66 ? 0.9505 1.3514 1.0376 0.1229 -0.0661 -0.1055 66 VAL B C 3047 O O . VAL B 66 ? 0.9594 1.2479 1.0049 0.1045 -0.0550 -0.0913 66 VAL B O 3048 C CB . VAL B 66 ? 0.9870 1.5008 1.1128 0.0104 -0.0648 -0.0959 66 VAL B CB 3049 C CG1 . VAL B 66 ? 0.9866 1.6592 1.1684 0.0072 -0.0486 -0.1086 66 VAL B CG1 3050 C CG2 . VAL B 66 ? 1.0240 1.5507 1.1464 -0.0378 -0.0869 -0.0921 66 VAL B CG2 3051 N N . GLY B 67 ? 0.9358 1.4235 1.0538 0.1742 -0.0651 -0.1293 67 GLY B N 3052 C CA . GLY B 67 ? 0.9378 1.3786 1.0348 0.2077 -0.0508 -0.1428 67 GLY B CA 3053 C C . GLY B 67 ? 0.8808 1.3455 0.9826 0.1500 -0.0149 -0.1364 67 GLY B C 3054 O O . GLY B 67 ? 0.8354 1.4263 0.9770 0.1093 0.0014 -0.1366 67 GLY B O 3055 N N . ARG B 68 ? 0.8622 1.2075 0.9190 0.1408 -0.0062 -0.1266 68 ARG B N 3056 C CA . ARG B 68 ? 0.8346 1.1869 0.8850 0.0949 0.0216 -0.1183 68 ARG B CA 3057 C C . ARG B 68 ? 0.8626 1.1425 0.8756 0.1285 0.0243 -0.1321 68 ARG B C 3058 O O . ARG B 68 ? 0.9385 1.0995 0.9130 0.1452 0.0064 -0.1263 68 ARG B O 3059 C CB . ARG B 68 ? 0.8163 1.0865 0.8445 0.0369 0.0238 -0.0878 68 ARG B CB 3060 C CG . ARG B 68 ? 0.8003 1.1219 0.8496 -0.0139 0.0208 -0.0753 68 ARG B CG 3061 C CD . ARG B 68 ? 0.7805 0.9988 0.7945 -0.0540 0.0174 -0.0544 68 ARG B CD 3062 N NE . ARG B 68 ? 0.7980 1.0237 0.8165 -0.0809 -0.0003 -0.0524 68 ARG B NE 3063 C CZ . ARG B 68 ? 0.8107 1.0025 0.8192 -0.0580 -0.0175 -0.0576 68 ARG B CZ 3064 N NH1 . ARG B 68 ? 0.8029 0.9420 0.7922 -0.0157 -0.0194 -0.0581 68 ARG B NH1 3065 N NH2 . ARG B 68 ? 0.8600 1.0680 0.8696 -0.0856 -0.0357 -0.0602 68 ARG B NH2 3066 N N . GLU B 69 ? 0.8475 1.1992 0.8648 0.1299 0.0454 -0.1486 69 GLU B N 3067 C CA . GLU B 69 ? 0.8657 1.1528 0.8416 0.1651 0.0439 -0.1705 69 GLU B CA 3068 C C . GLU B 69 ? 0.8141 1.0745 0.7655 0.1143 0.0629 -0.1519 69 GLU B C 3069 O O . GLU B 69 ? 0.7547 1.0821 0.7221 0.0637 0.0817 -0.1308 69 GLU B O 3070 C CB . GLU B 69 ? 0.9291 1.3195 0.9175 0.2312 0.0471 -0.2178 69 GLU B CB 3071 C CG . GLU B 69 ? 1.0123 1.3585 0.9954 0.3093 0.0121 -0.2428 69 GLU B CG 3072 C CD . GLU B 69 ? 1.0767 1.5759 1.0948 0.3831 0.0142 -0.2908 69 GLU B CD 3073 O OE1 . GLU B 69 ? 1.0728 1.7239 1.1531 0.3738 0.0223 -0.2864 69 GLU B OE1 3074 O OE2 . GLU B 69 ? 1.1636 1.6375 1.1457 0.4511 0.0058 -0.3359 69 GLU B OE2 3075 N N . PHE B 70 ? 0.8504 1.0048 0.7563 0.1246 0.0521 -0.1573 70 PHE B N 3076 C CA . PHE B 70 ? 0.8331 0.9567 0.7126 0.0825 0.0628 -0.1399 70 PHE B CA 3077 C C . PHE B 70 ? 0.8779 0.9606 0.7118 0.1102 0.0563 -0.1714 70 PHE B C 3078 O O . PHE B 70 ? 0.9325 0.9485 0.7408 0.1566 0.0334 -0.1996 70 PHE B O 3079 C CB . PHE B 70 ? 0.8082 0.8429 0.6794 0.0491 0.0515 -0.1062 70 PHE B CB 3080 C CG . PHE B 70 ? 0.7641 0.8168 0.6665 0.0306 0.0517 -0.0843 70 PHE B CG 3081 C CD1 . PHE B 70 ? 0.7757 0.8056 0.6871 0.0539 0.0356 -0.0875 70 PHE B CD1 3082 C CD2 . PHE B 70 ? 0.7147 0.7942 0.6266 -0.0098 0.0622 -0.0609 70 PHE B CD2 3083 C CE1 . PHE B 70 ? 0.7438 0.7925 0.6776 0.0362 0.0336 -0.0721 70 PHE B CE1 3084 C CE2 . PHE B 70 ? 0.7000 0.7788 0.6292 -0.0267 0.0565 -0.0472 70 PHE B CE2 3085 C CZ . PHE B 70 ? 0.6983 0.7689 0.6405 -0.0041 0.0439 -0.0550 70 PHE B CZ 3086 N N . ASN B 71 ? 0.8790 0.9911 0.6933 0.0817 0.0712 -0.1667 71 ASN B N 3087 C CA . ASN B 71 ? 0.9533 1.0340 0.7172 0.1038 0.0643 -0.2010 71 ASN B CA 3088 C C . ASN B 71 ? 0.9604 0.9197 0.6884 0.0769 0.0400 -0.1862 71 ASN B C 3089 O O . ASN B 71 ? 0.8939 0.8136 0.6409 0.0470 0.0332 -0.1508 71 ASN B O 3090 C CB . ASN B 71 ? 0.9576 1.1473 0.7098 0.0871 0.0914 -0.2065 71 ASN B CB 3091 C CG . ASN B 71 ? 0.9333 1.1146 0.6770 0.0254 0.0964 -0.1593 71 ASN B CG 3092 O OD1 . ASN B 71 ? 0.9317 1.0264 0.6600 0.0073 0.0777 -0.1426 71 ASN B OD1 3093 N ND2 . ASN B 71 ? 0.9388 1.2152 0.6889 -0.0078 0.1188 -0.1362 71 ASN B ND2 3094 N N . ASN B 72 ? 1.0452 0.9589 0.7199 0.0857 0.0267 -0.2161 72 ASN B N 3095 C CA . ASN B 72 ? 1.0985 0.9038 0.7345 0.0542 -0.0020 -0.2069 72 ASN B CA 3096 C C . ASN B 72 ? 1.0263 0.8588 0.6810 -0.0031 0.0036 -0.1619 72 ASN B C 3097 O O . ASN B 72 ? 1.0299 0.8054 0.6741 -0.0361 -0.0169 -0.1444 72 ASN B O 3098 C CB . ASN B 72 ? 1.2229 0.9733 0.7897 0.0741 -0.0215 -0.2550 72 ASN B CB 3099 C CG . ASN B 72 ? 1.3357 0.9536 0.8531 0.0384 -0.0616 -0.2507 72 ASN B CG 3100 O OD1 . ASN B 72 ? 1.3859 0.9311 0.9083 0.0226 -0.0801 -0.2262 72 ASN B OD1 3101 N ND2 . ASN B 72 ? 1.4092 0.9997 0.8733 0.0176 -0.0770 -0.2721 72 ASN B ND2 3102 N N . LEU B 73 ? 0.9615 0.8836 0.6391 -0.0147 0.0280 -0.1430 73 LEU B N 3103 C CA . LEU B 73 ? 0.9150 0.8599 0.6075 -0.0521 0.0282 -0.1026 73 LEU B CA 3104 C C . LEU B 73 ? 0.8544 0.8275 0.5928 -0.0557 0.0414 -0.0701 73 LEU B C 3105 O O . LEU B 73 ? 0.8181 0.8154 0.5620 -0.0723 0.0437 -0.0411 73 LEU B O 3106 C CB . LEU B 73 ? 0.9476 0.9419 0.6074 -0.0650 0.0335 -0.1021 73 LEU B CB 3107 C CG . LEU B 73 ? 1.0190 0.9839 0.6247 -0.0700 0.0143 -0.1331 73 LEU B CG 3108 C CD1 . LEU B 73 ? 1.0373 1.0667 0.6055 -0.0788 0.0232 -0.1336 73 LEU B CD1 3109 C CD2 . LEU B 73 ? 1.0194 0.9423 0.6265 -0.1021 -0.0126 -0.1170 73 LEU B CD2 3110 N N . GLU B 74 ? 0.8392 0.7970 0.6022 -0.0376 0.0439 -0.0767 74 GLU B N 3111 C CA . GLU B 74 ? 0.8039 0.7718 0.6030 -0.0423 0.0496 -0.0524 74 GLU B CA 3112 C C . GLU B 74 ? 0.8124 0.7328 0.6223 -0.0375 0.0369 -0.0496 74 GLU B C 3113 O O . GLU B 74 ? 0.7838 0.7064 0.6160 -0.0280 0.0394 -0.0459 74 GLU B O 3114 C CB . GLU B 74 ? 0.7842 0.8049 0.6022 -0.0327 0.0650 -0.0603 74 GLU B CB 3115 C CG . GLU B 74 ? 0.7729 0.8550 0.5789 -0.0551 0.0798 -0.0492 74 GLU B CG 3116 C CD . GLU B 74 ? 0.7751 0.9370 0.6046 -0.0571 0.0959 -0.0554 74 GLU B CD 3117 O OE1 . GLU B 74 ? 0.7928 0.9826 0.6402 -0.0211 0.0976 -0.0867 74 GLU B OE1 3118 O OE2 . GLU B 74 ? 0.7975 0.9956 0.6247 -0.0963 0.1031 -0.0278 74 GLU B OE2 3119 N N . ARG B 75 ? 0.8395 0.7230 0.6286 -0.0513 0.0218 -0.0491 75 ARG B N 3120 C CA . ARG B 75 ? 0.8464 0.6882 0.6327 -0.0603 0.0085 -0.0404 75 ARG B CA 3121 C C . ARG B 75 ? 0.7975 0.6751 0.6140 -0.0665 0.0157 -0.0174 75 ARG B C 3122 O O . ARG B 75 ? 0.7939 0.6555 0.6123 -0.0663 0.0120 -0.0105 75 ARG B O 3123 C CB . ARG B 75 ? 0.9254 0.7305 0.6782 -0.0927 -0.0113 -0.0389 75 ARG B CB 3124 C CG . ARG B 75 ? 1.0456 0.7806 0.7494 -0.0846 -0.0290 -0.0691 75 ARG B CG 3125 C CD . ARG B 75 ? 1.1381 0.8035 0.8234 -0.0499 -0.0409 -0.0854 75 ARG B CD 3126 N NE . ARG B 75 ? 1.3077 0.9029 0.9417 -0.0211 -0.0601 -0.1255 75 ARG B NE 3127 C CZ . ARG B 75 ? 1.4351 0.9797 1.0504 0.0322 -0.0731 -0.1528 75 ARG B CZ 3128 N NH1 . ARG B 75 ? 1.4284 0.9902 1.0754 0.0547 -0.0690 -0.1392 75 ARG B NH1 3129 N NH2 . ARG B 75 ? 1.5474 1.0266 1.1090 0.0696 -0.0934 -0.1981 75 ARG B NH2 3130 N N . ARG B 76 ? 0.7743 0.6961 0.6063 -0.0675 0.0223 -0.0071 76 ARG B N 3131 C CA . ARG B 76 ? 0.7265 0.6783 0.5792 -0.0604 0.0251 0.0050 76 ARG B CA 3132 C C . ARG B 76 ? 0.7055 0.6410 0.5681 -0.0436 0.0309 0.0012 76 ARG B C 3133 O O . ARG B 76 ? 0.6909 0.6294 0.5574 -0.0402 0.0305 0.0028 76 ARG B O 3134 C CB . ARG B 76 ? 0.7206 0.7066 0.5793 -0.0510 0.0223 0.0127 76 ARG B CB 3135 C CG . ARG B 76 ? 0.7252 0.7568 0.5836 -0.0680 0.0134 0.0178 76 ARG B CG 3136 C CD . ARG B 76 ? 0.7240 0.7827 0.5830 -0.0484 0.0048 0.0248 76 ARG B CD 3137 N NE . ARG B 76 ? 0.7138 0.7295 0.5479 -0.0505 0.0056 0.0265 76 ARG B NE 3138 C CZ . ARG B 76 ? 0.7240 0.7245 0.5427 -0.0354 -0.0031 0.0398 76 ARG B CZ 3139 N NH1 . ARG B 76 ? 0.7305 0.7408 0.5555 -0.0036 -0.0177 0.0465 76 ARG B NH1 3140 N NH2 . ARG B 76 ? 0.7364 0.7115 0.5272 -0.0507 0.0004 0.0463 76 ARG B NH2 3141 N N . ILE B 77 ? 0.7106 0.6386 0.5738 -0.0399 0.0352 -0.0023 77 ILE B N 3142 C CA . ILE B 77 ? 0.7112 0.6338 0.5846 -0.0352 0.0371 -0.0058 77 ILE B CA 3143 C C . ILE B 77 ? 0.7359 0.6567 0.6152 -0.0270 0.0358 -0.0168 77 ILE B C 3144 O O . ILE B 77 ? 0.7442 0.6657 0.6315 -0.0216 0.0322 -0.0182 77 ILE B O 3145 C CB . ILE B 77 ? 0.7242 0.6530 0.5950 -0.0488 0.0402 -0.0007 77 ILE B CB 3146 C CG1 . ILE B 77 ? 0.7585 0.7207 0.6254 -0.0552 0.0502 -0.0075 77 ILE B CG1 3147 C CG2 . ILE B 77 ? 0.7622 0.6620 0.6136 -0.0518 0.0304 0.0148 77 ILE B CG2 3148 C CD1 . ILE B 77 ? 0.7936 0.7870 0.6559 -0.0815 0.0566 0.0030 77 ILE B CD1 3149 N N . GLU B 78 ? 0.7414 0.6505 0.6089 -0.0217 0.0331 -0.0263 78 GLU B N 3150 C CA . GLU B 78 ? 0.7673 0.6521 0.6287 -0.0035 0.0220 -0.0356 78 GLU B CA 3151 C C . GLU B 78 ? 0.7624 0.6196 0.6113 -0.0133 0.0123 -0.0191 78 GLU B C 3152 O O . GLU B 78 ? 0.7376 0.5853 0.5846 -0.0011 0.0029 -0.0179 78 GLU B O 3153 C CB . GLU B 78 ? 0.8516 0.6983 0.6856 0.0099 0.0118 -0.0528 78 GLU B CB 3154 C CG . GLU B 78 ? 0.9541 0.7397 0.7636 0.0343 -0.0116 -0.0595 78 GLU B CG 3155 C CD . GLU B 78 ? 1.1085 0.8356 0.8793 0.0588 -0.0285 -0.0859 78 GLU B CD 3156 O OE1 . GLU B 78 ? 1.1862 0.8737 0.9268 0.0326 -0.0338 -0.0854 78 GLU B OE1 3157 O OE2 . GLU B 78 ? 1.2261 0.9511 0.9951 0.1083 -0.0394 -0.1113 78 GLU B OE2 3158 N N . ASN B 79 ? 0.7470 0.6068 0.5865 -0.0364 0.0139 -0.0057 79 ASN B N 3159 C CA . ASN B 79 ? 0.7654 0.6242 0.5892 -0.0546 0.0083 0.0120 79 ASN B CA 3160 C C . ASN B 79 ? 0.7247 0.6260 0.5650 -0.0431 0.0176 0.0119 79 ASN B C 3161 O O . ASN B 79 ? 0.7280 0.6330 0.5535 -0.0472 0.0135 0.0207 79 ASN B O 3162 C CB . ASN B 79 ? 0.7921 0.6739 0.6079 -0.0864 0.0085 0.0242 79 ASN B CB 3163 C CG . ASN B 79 ? 0.8383 0.7527 0.6396 -0.1161 0.0072 0.0461 79 ASN B CG 3164 O OD1 . ASN B 79 ? 0.9292 0.7912 0.6928 -0.1411 -0.0089 0.0628 79 ASN B OD1 3165 N ND2 . ASN B 79 ? 0.8065 0.8087 0.6312 -0.1129 0.0218 0.0467 79 ASN B ND2 3166 N N . LEU B 80 ? 0.7009 0.6234 0.5616 -0.0298 0.0261 0.0016 80 LEU B N 3167 C CA . LEU B 80 ? 0.7070 0.6432 0.5721 -0.0151 0.0276 -0.0062 80 LEU B CA 3168 C C . LEU B 80 ? 0.7182 0.6391 0.5832 -0.0109 0.0204 -0.0118 80 LEU B C 3169 O O . LEU B 80 ? 0.7337 0.6631 0.5868 -0.0063 0.0163 -0.0140 80 LEU B O 3170 C CB . LEU B 80 ? 0.7151 0.6408 0.5866 -0.0070 0.0276 -0.0121 80 LEU B CB 3171 C CG . LEU B 80 ? 0.7507 0.6636 0.6110 0.0128 0.0206 -0.0239 80 LEU B CG 3172 C CD1 . LEU B 80 ? 0.7826 0.6567 0.6333 0.0174 0.0114 -0.0216 80 LEU B CD1 3173 C CD2 . LEU B 80 ? 0.7919 0.6854 0.6460 0.0089 0.0134 -0.0336 80 LEU B CD2 3174 N N . ASN B 81 ? 0.7089 0.6226 0.5871 -0.0106 0.0184 -0.0162 81 ASN B N 3175 C CA . ASN B 81 ? 0.7108 0.6349 0.5986 -0.0024 0.0092 -0.0231 81 ASN B CA 3176 C C . ASN B 81 ? 0.7372 0.6446 0.6041 0.0070 -0.0042 -0.0155 81 ASN B C 3177 O O . ASN B 81 ? 0.7460 0.6665 0.6113 0.0130 -0.0147 -0.0180 81 ASN B O 3178 C CB . ASN B 81 ? 0.7059 0.6511 0.6123 0.0055 0.0113 -0.0322 81 ASN B CB 3179 C CG . ASN B 81 ? 0.7166 0.7075 0.6455 0.0164 0.0023 -0.0424 81 ASN B CG 3180 O OD1 . ASN B 81 ? 0.7252 0.7423 0.6660 -0.0029 0.0007 -0.0434 81 ASN B OD1 3181 N ND2 . ASN B 81 ? 0.7351 0.7331 0.6662 0.0489 -0.0086 -0.0517 81 ASN B ND2 3182 N N . LYS B 82 ? 0.7650 0.6372 0.6083 0.0027 -0.0082 -0.0035 82 LYS B N 3183 C CA . LYS B 82 ? 0.8529 0.6860 0.6602 0.0030 -0.0276 0.0126 82 LYS B CA 3184 C C . LYS B 82 ? 0.8615 0.7217 0.6492 -0.0155 -0.0229 0.0266 82 LYS B C 3185 O O . LYS B 82 ? 0.8663 0.7245 0.6331 -0.0102 -0.0366 0.0340 82 LYS B O 3186 C CB . LYS B 82 ? 0.9364 0.7062 0.7105 -0.0104 -0.0387 0.0243 82 LYS B CB 3187 C CG . LYS B 82 ? 1.0740 0.7695 0.7913 -0.0186 -0.0684 0.0491 82 LYS B CG 3188 C CD . LYS B 82 ? 1.1968 0.8243 0.8712 -0.0563 -0.0803 0.0659 82 LYS B CD 3189 C CE . LYS B 82 ? 1.3553 0.8692 0.9539 -0.0727 -0.1204 0.0952 82 LYS B CE 3190 N NZ . LYS B 82 ? 1.3853 0.9238 0.9560 -0.0981 -0.1236 0.1289 82 LYS B NZ 3191 N N . LYS B 83 ? 0.8364 0.7338 0.6300 -0.0317 -0.0044 0.0273 83 LYS B N 3192 C CA . LYS B 83 ? 0.8649 0.8136 0.6408 -0.0408 0.0043 0.0324 83 LYS B CA 3193 C C . LYS B 83 ? 0.8192 0.7854 0.5988 -0.0177 0.0026 0.0105 83 LYS B C 3194 O O . LYS B 83 ? 0.8027 0.7924 0.5526 -0.0193 -0.0009 0.0138 83 LYS B O 3195 C CB . LYS B 83 ? 0.8803 0.8865 0.6694 -0.0490 0.0227 0.0301 83 LYS B CB 3196 C CG . LYS B 83 ? 0.9822 1.0212 0.7457 -0.0918 0.0244 0.0598 83 LYS B CG 3197 C CD . LYS B 83 ? 1.0729 1.0316 0.8186 -0.1204 0.0063 0.0796 83 LYS B CD 3198 C CE . LYS B 83 ? 1.2075 1.1134 0.8951 -0.1575 -0.0149 0.1145 83 LYS B CE 3199 N NZ . LYS B 83 ? 1.2504 1.2409 0.9117 -0.2057 -0.0044 0.1426 83 LYS B NZ 3200 N N . MET B 84 ? 0.7864 0.7386 0.5948 -0.0031 0.0024 -0.0101 84 MET B N 3201 C CA . MET B 84 ? 0.8009 0.7528 0.6082 0.0067 -0.0070 -0.0305 84 MET B CA 3202 C C . MET B 84 ? 0.7884 0.7414 0.5860 0.0072 -0.0253 -0.0240 84 MET B C 3203 O O . MET B 84 ? 0.7949 0.7639 0.5648 0.0096 -0.0333 -0.0302 84 MET B O 3204 C CB . MET B 84 ? 0.8005 0.7311 0.6341 0.0043 -0.0086 -0.0435 84 MET B CB 3205 C CG . MET B 84 ? 0.8566 0.7683 0.6747 0.0042 -0.0213 -0.0659 84 MET B CG 3206 S SD . MET B 84 ? 0.9298 0.8411 0.7736 -0.0241 -0.0361 -0.0682 84 MET B SD 3207 C CE . MET B 84 ? 0.9250 0.8899 0.7858 -0.0143 -0.0431 -0.0589 84 MET B CE 3208 N N . GLU B 85 ? 0.8534 1.0451 0.6008 -0.0191 -0.0665 0.0128 85 GLU B N 3209 C CA . GLU B 85 ? 0.8467 1.0163 0.5961 -0.0062 -0.0540 -0.0023 85 GLU B CA 3210 C C . GLU B 85 ? 0.8251 0.9531 0.5823 -0.0155 -0.0639 -0.0143 85 GLU B C 3211 O O . GLU B 85 ? 0.7777 0.8997 0.5660 -0.0094 -0.0545 -0.0130 85 GLU B O 3212 C CB . GLU B 85 ? 0.9217 1.0899 0.6199 0.0168 -0.0479 -0.0224 85 GLU B CB 3213 C CG . GLU B 85 ? 0.9605 1.1890 0.6575 0.0198 -0.0343 -0.0058 85 GLU B CG 3214 C CD . GLU B 85 ? 1.0232 1.3003 0.7007 0.0477 -0.0161 -0.0163 85 GLU B CD 3215 O OE1 . GLU B 85 ? 1.1224 1.3766 0.7474 0.0815 -0.0194 -0.0442 85 GLU B OE1 3216 O OE2 . GLU B 85 ? 0.9987 1.3389 0.7022 0.0354 0.0000 0.0041 85 GLU B OE2 3217 N N . ASP B 86 ? 0.8616 0.9645 0.5864 -0.0381 -0.0842 -0.0236 86 ASP B N 3218 C CA . ASP B 86 ? 0.8768 0.9417 0.5965 -0.0627 -0.0973 -0.0309 86 ASP B CA 3219 C C . ASP B 86 ? 0.7883 0.9008 0.5764 -0.0703 -0.0941 -0.0112 86 ASP B C 3220 O O . ASP B 86 ? 0.7577 0.8447 0.5587 -0.0764 -0.0935 -0.0151 86 ASP B O 3221 C CB . ASP B 86 ? 0.9613 1.0072 0.6256 -0.1050 -0.1232 -0.0381 86 ASP B CB 3222 C CG . ASP B 86 ? 1.0924 1.0268 0.6565 -0.1086 -0.1356 -0.0656 86 ASP B CG 3223 O OD1 . ASP B 86 ? 1.1746 1.0418 0.7182 -0.0959 -0.1330 -0.0767 86 ASP B OD1 3224 O OD2 . ASP B 86 ? 1.1635 1.0685 0.6590 -0.1209 -0.1497 -0.0764 86 ASP B OD2 3225 N N . GLY B 87 ? 0.7435 0.9198 0.5631 -0.0654 -0.0943 0.0089 87 GLY B N 3226 C CA . GLY B 87 ? 0.7000 0.9201 0.5679 -0.0577 -0.0931 0.0267 87 GLY B CA 3227 C C . GLY B 87 ? 0.6752 0.8632 0.5704 -0.0377 -0.0757 0.0301 87 GLY B C 3228 O O . GLY B 87 ? 0.6408 0.8329 0.5645 -0.0388 -0.0753 0.0324 87 GLY B O 3229 N N . PHE B 88 ? 0.6604 0.8264 0.5445 -0.0248 -0.0619 0.0312 88 PHE B N 3230 C CA . PHE B 88 ? 0.6386 0.7850 0.5423 -0.0176 -0.0471 0.0354 88 PHE B CA 3231 C C . PHE B 88 ? 0.6520 0.7759 0.5629 -0.0195 -0.0436 0.0164 88 PHE B C 3232 O O . PHE B 88 ? 0.6405 0.7561 0.5784 -0.0183 -0.0384 0.0193 88 PHE B O 3233 C CB . PHE B 88 ? 0.6540 0.8045 0.5386 -0.0168 -0.0348 0.0445 88 PHE B CB 3234 C CG . PHE B 88 ? 0.6826 0.8227 0.5459 -0.0155 -0.0380 0.0688 88 PHE B CG 3235 C CD1 . PHE B 88 ? 0.6881 0.7929 0.5497 -0.0084 -0.0406 0.0837 88 PHE B CD1 3236 C CD2 . PHE B 88 ? 0.7138 0.8656 0.5437 -0.0169 -0.0398 0.0765 88 PHE B CD2 3237 C CE1 . PHE B 88 ? 0.7287 0.7942 0.5427 0.0014 -0.0470 0.1053 88 PHE B CE1 3238 C CE2 . PHE B 88 ? 0.7558 0.8785 0.5476 -0.0125 -0.0451 0.1002 88 PHE B CE2 3239 C CZ . PHE B 88 ? 0.7795 0.8510 0.5569 -0.0013 -0.0497 0.1144 88 PHE B CZ 3240 N N . LEU B 89 ? 0.7114 0.8132 0.5856 -0.0182 -0.0485 -0.0034 89 LEU B N 3241 C CA . LEU B 89 ? 0.7479 0.8043 0.6051 -0.0127 -0.0502 -0.0217 89 LEU B CA 3242 C C . LEU B 89 ? 0.7069 0.7485 0.5826 -0.0361 -0.0610 -0.0183 89 LEU B C 3243 O O . LEU B 89 ? 0.6669 0.6879 0.5558 -0.0311 -0.0566 -0.0218 89 LEU B O 3244 C CB . LEU B 89 ? 0.8654 0.8661 0.6475 -0.0052 -0.0611 -0.0445 89 LEU B CB 3245 C CG . LEU B 89 ? 0.9659 0.9844 0.7142 0.0267 -0.0516 -0.0537 89 LEU B CG 3246 C CD1 . LEU B 89 ? 1.0791 1.0114 0.7295 0.0389 -0.0680 -0.0798 89 LEU B CD1 3247 C CD2 . LEU B 89 ? 0.9436 1.0147 0.7199 0.0585 -0.0303 -0.0523 89 LEU B CD2 3248 N N . ASP B 90 ? 0.7137 0.7797 0.5883 -0.0626 -0.0755 -0.0107 90 ASP B N 3249 C CA . ASP B 90 ? 0.6952 0.7807 0.5887 -0.0897 -0.0858 -0.0041 90 ASP B CA 3250 C C . ASP B 90 ? 0.6187 0.7431 0.5721 -0.0697 -0.0736 0.0104 90 ASP B C 3251 O O . ASP B 90 ? 0.6165 0.7341 0.5860 -0.0773 -0.0734 0.0099 90 ASP B O 3252 C CB . ASP B 90 ? 0.7298 0.8721 0.6126 -0.1215 -0.1034 0.0037 90 ASP B CB 3253 C CG . ASP B 90 ? 0.8561 0.9391 0.6609 -0.1585 -0.1217 -0.0117 90 ASP B CG 3254 O OD1 . ASP B 90 ? 0.9212 0.9043 0.6710 -0.1547 -0.1229 -0.0296 90 ASP B OD1 3255 O OD2 . ASP B 90 ? 0.9311 1.0633 0.7186 -0.1891 -0.1371 -0.0062 90 ASP B OD2 3256 N N . VAL B 91 ? 0.5985 0.7486 0.5703 -0.0447 -0.0652 0.0232 91 VAL B N 3257 C CA . VAL B 91 ? 0.5715 0.7263 0.5718 -0.0231 -0.0564 0.0356 91 VAL B CA 3258 C C . VAL B 91 ? 0.5747 0.6880 0.5856 -0.0213 -0.0440 0.0285 91 VAL B C 3259 O O . VAL B 91 ? 0.5738 0.6850 0.6065 -0.0176 -0.0418 0.0310 91 VAL B O 3260 C CB . VAL B 91 ? 0.5872 0.7394 0.5710 -0.0010 -0.0535 0.0508 91 VAL B CB 3261 C CG1 . VAL B 91 ? 0.5909 0.7053 0.5730 0.0160 -0.0464 0.0614 91 VAL B CG1 3262 C CG2 . VAL B 91 ? 0.6085 0.8161 0.5843 0.0112 -0.0667 0.0605 91 VAL B CG2 3263 N N . TRP B 92 ? 0.5782 0.6723 0.5727 -0.0204 -0.0361 0.0197 92 TRP B N 3264 C CA . TRP B 92 ? 0.5672 0.6487 0.5722 -0.0151 -0.0248 0.0138 92 TRP B CA 3265 C C . TRP B 92 ? 0.5742 0.6281 0.5727 -0.0147 -0.0294 -0.0021 92 TRP B C 3266 O O . TRP B 92 ? 0.5687 0.6164 0.5843 -0.0097 -0.0237 -0.0038 92 TRP B O 3267 C CB . TRP B 92 ? 0.5738 0.6760 0.5629 -0.0091 -0.0138 0.0121 92 TRP B CB 3268 C CG . TRP B 92 ? 0.5999 0.7131 0.5845 -0.0217 -0.0090 0.0324 92 TRP B CG 3269 C CD1 . TRP B 92 ? 0.6371 0.7589 0.5965 -0.0258 -0.0105 0.0414 92 TRP B CD1 3270 C CD2 . TRP B 92 ? 0.6048 0.7020 0.5920 -0.0358 -0.0051 0.0473 92 TRP B CD2 3271 N NE1 . TRP B 92 ? 0.6618 0.7665 0.6011 -0.0429 -0.0082 0.0623 92 TRP B NE1 3272 C CE2 . TRP B 92 ? 0.6504 0.7331 0.6008 -0.0510 -0.0059 0.0658 92 TRP B CE2 3273 C CE3 . TRP B 92 ? 0.6055 0.6891 0.6110 -0.0397 -0.0026 0.0470 92 TRP B CE3 3274 C CZ2 . TRP B 92 ? 0.7055 0.7430 0.6225 -0.0739 -0.0068 0.0839 92 TRP B CZ2 3275 C CZ3 . TRP B 92 ? 0.6378 0.6884 0.6193 -0.0608 -0.0022 0.0634 92 TRP B CZ3 3276 C CH2 . TRP B 92 ? 0.6923 0.7117 0.6231 -0.0797 -0.0054 0.0817 92 TRP B CH2 3277 N N . THR B 93 ? 0.6386 0.6648 0.6000 -0.0240 -0.0423 -0.0129 93 THR B N 3278 C CA . THR B 93 ? 0.6777 0.6499 0.6084 -0.0309 -0.0513 -0.0252 93 THR B CA 3279 C C . THR B 93 ? 0.6550 0.6490 0.6256 -0.0508 -0.0537 -0.0135 93 THR B C 3280 O O . THR B 93 ? 0.6593 0.6284 0.6341 -0.0468 -0.0512 -0.0171 93 THR B O 3281 C CB . THR B 93 ? 0.7573 0.6733 0.6164 -0.0512 -0.0699 -0.0367 93 THR B CB 3282 O OG1 . THR B 93 ? 0.8216 0.7072 0.6320 -0.0187 -0.0668 -0.0519 93 THR B OG1 3283 C CG2 . THR B 93 ? 0.8271 0.6666 0.6354 -0.0723 -0.0840 -0.0444 93 THR B CG2 3284 N N . TYR B 94 ? 0.6125 0.6622 0.6097 -0.0644 -0.0581 0.0003 94 TYR B N 3285 C CA . TYR B 94 ? 0.5842 0.6785 0.6149 -0.0748 -0.0606 0.0114 94 TYR B CA 3286 C C . TYR B 94 ? 0.5322 0.6230 0.5972 -0.0482 -0.0467 0.0154 94 TYR B C 3287 O O . TYR B 94 ? 0.5075 0.5905 0.5840 -0.0530 -0.0456 0.0141 94 TYR B O 3288 C CB . TYR B 94 ? 0.5869 0.7615 0.6320 -0.0771 -0.0680 0.0249 94 TYR B CB 3289 C CG . TYR B 94 ? 0.5474 0.7908 0.6276 -0.0631 -0.0668 0.0371 94 TYR B CG 3290 C CD1 . TYR B 94 ? 0.5378 0.7748 0.6329 -0.0188 -0.0567 0.0437 94 TYR B CD1 3291 C CD2 . TYR B 94 ? 0.5479 0.8613 0.6336 -0.0951 -0.0773 0.0426 94 TYR B CD2 3292 C CE1 . TYR B 94 ? 0.5296 0.8199 0.6414 0.0068 -0.0565 0.0519 94 TYR B CE1 3293 C CE2 . TYR B 94 ? 0.5248 0.9216 0.6412 -0.0734 -0.0750 0.0531 94 TYR B CE2 3294 C CZ . TYR B 94 ? 0.5188 0.8997 0.6469 -0.0151 -0.0643 0.0560 94 TYR B CZ 3295 O OH . TYR B 94 ? 0.5332 0.9881 0.6770 0.0191 -0.0629 0.0637 94 TYR B OH 3296 N N . ASN B 95 ? 0.5398 0.6280 0.6102 -0.0269 -0.0375 0.0206 95 ASN B N 3297 C CA . ASN B 95 ? 0.5354 0.6060 0.6200 -0.0139 -0.0273 0.0246 95 ASN B CA 3298 C C . ASN B 95 ? 0.5544 0.6035 0.6449 -0.0177 -0.0221 0.0136 95 ASN B C 3299 O O . ASN B 95 ? 0.5930 0.6385 0.7007 -0.0159 -0.0197 0.0151 95 ASN B O 3300 C CB . ASN B 95 ? 0.5390 0.5953 0.6062 -0.0089 -0.0210 0.0328 95 ASN B CB 3301 C CG . ASN B 95 ? 0.5770 0.6323 0.6237 0.0062 -0.0274 0.0465 95 ASN B CG 3302 O OD1 . ASN B 95 ? 0.5833 0.6675 0.6372 0.0217 -0.0347 0.0496 95 ASN B OD1 3303 N ND2 . ASN B 95 ? 0.6427 0.6708 0.6564 0.0035 -0.0253 0.0560 95 ASN B ND2 3304 N N . ALA B 96 ? 0.5665 0.6015 0.6355 -0.0155 -0.0212 0.0019 96 ALA B N 3305 C CA . ALA B 96 ? 0.5691 0.5876 0.6326 -0.0039 -0.0169 -0.0088 96 ALA B CA 3306 C C . ALA B 96 ? 0.5884 0.5712 0.6421 -0.0135 -0.0262 -0.0132 96 ALA B C 3307 O O . ALA B 96 ? 0.5765 0.5554 0.6450 -0.0084 -0.0225 -0.0136 96 ALA B O 3308 C CB . ALA B 96 ? 0.5907 0.6038 0.6171 0.0172 -0.0153 -0.0220 96 ALA B CB 3309 N N . GLU B 97 ? 0.6143 0.5735 0.6373 -0.0350 -0.0397 -0.0146 97 GLU B N 3310 C CA . GLU B 97 ? 0.6713 0.5962 0.6721 -0.0588 -0.0505 -0.0150 97 GLU B CA 3311 C C . GLU B 97 ? 0.6287 0.6084 0.6824 -0.0675 -0.0459 -0.0021 97 GLU B C 3312 O O . GLU B 97 ? 0.6530 0.6145 0.7070 -0.0711 -0.0459 -0.0024 97 GLU B O 3313 C CB . GLU B 97 ? 0.7419 0.6326 0.6850 -0.0972 -0.0692 -0.0164 97 GLU B CB 3314 C CG . GLU B 97 ? 0.8456 0.6474 0.7097 -0.0787 -0.0763 -0.0338 97 GLU B CG 3315 C CD . GLU B 97 ? 0.9496 0.6949 0.7357 -0.1199 -0.0975 -0.0373 97 GLU B CD 3316 O OE1 . GLU B 97 ? 0.9945 0.7902 0.7944 -0.1717 -0.1071 -0.0240 97 GLU B OE1 3317 O OE2 . GLU B 97 ? 1.0633 0.7172 0.7657 -0.0988 -0.1056 -0.0538 97 GLU B OE2 3318 N N . LEU B 98 ? 0.5923 0.6344 0.6814 -0.0628 -0.0424 0.0084 98 LEU B N 3319 C CA . LEU B 98 ? 0.5508 0.6453 0.6739 -0.0583 -0.0398 0.0187 98 LEU B CA 3320 C C . LEU B 98 ? 0.5087 0.5791 0.6501 -0.0350 -0.0286 0.0166 98 LEU B C 3321 O O . LEU B 98 ? 0.4963 0.5772 0.6509 -0.0355 -0.0273 0.0186 98 LEU B O 3322 C CB . LEU B 98 ? 0.5616 0.7184 0.6983 -0.0415 -0.0408 0.0290 98 LEU B CB 3323 C CG . LEU B 98 ? 0.5447 0.7692 0.7026 -0.0232 -0.0403 0.0382 98 LEU B CG 3324 C CD1 . LEU B 98 ? 0.5398 0.8331 0.7006 -0.0635 -0.0497 0.0434 98 LEU B CD1 3325 C CD2 . LEU B 98 ? 0.5566 0.8210 0.7093 0.0179 -0.0412 0.0463 98 LEU B CD2 3326 N N . LEU B 99 ? 0.5064 0.5515 0.6445 -0.0208 -0.0212 0.0135 99 LEU B N 3327 C CA . LEU B 99 ? 0.5142 0.5443 0.6624 -0.0115 -0.0128 0.0132 99 LEU B CA 3328 C C . LEU B 99 ? 0.5199 0.5350 0.6697 -0.0143 -0.0124 0.0050 99 LEU B C 3329 O O . LEU B 99 ? 0.5542 0.5693 0.7175 -0.0120 -0.0098 0.0063 99 LEU B O 3330 C CB . LEU B 99 ? 0.5692 0.5937 0.7071 -0.0113 -0.0066 0.0141 99 LEU B CB 3331 C CG . LEU B 99 ? 0.6062 0.6248 0.7443 -0.0177 -0.0005 0.0171 99 LEU B CG 3332 C CD1 . LEU B 99 ? 0.6343 0.6175 0.7533 -0.0152 -0.0037 0.0263 99 LEU B CD1 3333 C CD2 . LEU B 99 ? 0.6593 0.7010 0.7852 -0.0309 0.0048 0.0197 99 LEU B CD2 3334 N N . VAL B 100 ? 0.5168 0.5085 0.6404 -0.0142 -0.0166 -0.0040 100 VAL B N 3335 C CA . VAL B 100 ? 0.5067 0.4663 0.6113 -0.0066 -0.0188 -0.0118 100 VAL B CA 3336 C C . VAL B 100 ? 0.5073 0.4550 0.6109 -0.0277 -0.0258 -0.0064 100 VAL B C 3337 O O . VAL B 100 ? 0.4874 0.4291 0.5985 -0.0216 -0.0232 -0.0070 100 VAL B O 3338 C CB . VAL B 100 ? 0.5594 0.4722 0.6082 0.0097 -0.0253 -0.0243 100 VAL B CB 3339 C CG1 . VAL B 100 ? 0.6138 0.4593 0.6122 0.0187 -0.0344 -0.0313 100 VAL B CG1 3340 C CG2 . VAL B 100 ? 0.5385 0.4949 0.5959 0.0390 -0.0145 -0.0295 100 VAL B CG2 3341 N N . LEU B 101 ? 0.4937 0.4530 0.5880 -0.0557 -0.0346 0.0000 101 LEU B N 3342 C CA . LEU B 101 ? 0.4935 0.4707 0.5871 -0.0845 -0.0410 0.0086 101 LEU B CA 3343 C C . LEU B 101 ? 0.4725 0.5034 0.6155 -0.0664 -0.0304 0.0144 101 LEU B C 3344 O O . LEU B 101 ? 0.4907 0.5152 0.6352 -0.0701 -0.0296 0.0156 101 LEU B O 3345 C CB . LEU B 101 ? 0.4958 0.5190 0.5796 -0.1211 -0.0513 0.0178 101 LEU B CB 3346 C CG . LEU B 101 ? 0.5887 0.5467 0.6020 -0.1576 -0.0678 0.0140 101 LEU B CG 3347 C CD1 . LEU B 101 ? 0.6006 0.6355 0.6118 -0.2052 -0.0788 0.0266 101 LEU B CD1 3348 C CD2 . LEU B 101 ? 0.6722 0.5284 0.6135 -0.1791 -0.0795 0.0103 101 LEU B CD2 3349 N N . MET B 102 ? 0.4458 0.5166 0.6152 -0.0446 -0.0242 0.0177 102 MET B N 3350 C CA . MET B 102 ? 0.4293 0.5286 0.6199 -0.0207 -0.0178 0.0215 102 MET B CA 3351 C C . MET B 102 ? 0.4447 0.5014 0.6380 -0.0108 -0.0114 0.0154 102 MET B C 3352 O O . MET B 102 ? 0.4470 0.5143 0.6480 -0.0045 -0.0092 0.0165 102 MET B O 3353 C CB . MET B 102 ? 0.4492 0.5599 0.6363 0.0066 -0.0162 0.0251 102 MET B CB 3354 C CG . MET B 102 ? 0.4808 0.6649 0.6698 0.0101 -0.0223 0.0331 102 MET B CG 3355 S SD . MET B 102 ? 0.5528 0.7221 0.7165 0.0566 -0.0224 0.0370 102 MET B SD 3356 C CE . MET B 102 ? 0.5527 0.8513 0.7256 0.0761 -0.0291 0.0467 102 MET B CE 3357 N N . GLU B 103 ? 0.4243 0.4482 0.6110 -0.0096 -0.0085 0.0096 103 GLU B N 3358 C CA . GLU B 103 ? 0.4626 0.4720 0.6530 -0.0050 -0.0033 0.0059 103 GLU B CA 3359 C C . GLU B 103 ? 0.4563 0.4565 0.6447 -0.0064 -0.0051 0.0011 103 GLU B C 3360 O O . GLU B 103 ? 0.4563 0.4578 0.6520 -0.0028 -0.0024 0.0000 103 GLU B O 3361 C CB . GLU B 103 ? 0.4554 0.4646 0.6392 -0.0074 0.0004 0.0045 103 GLU B CB 3362 C CG . GLU B 103 ? 0.5323 0.5257 0.6993 -0.0105 0.0001 0.0119 103 GLU B CG 3363 C CD . GLU B 103 ? 0.5798 0.5394 0.7264 -0.0090 -0.0012 0.0150 103 GLU B CD 3364 O OE1 . GLU B 103 ? 0.6249 0.5858 0.7773 -0.0161 0.0001 0.0117 103 GLU B OE1 3365 O OE2 . GLU B 103 ? 0.6628 0.5866 0.7761 0.0039 -0.0054 0.0201 103 GLU B OE2 3366 N N . ASN B 104 ? 0.4726 0.4503 0.6373 -0.0119 -0.0117 -0.0015 104 ASN B N 3367 C CA . ASN B 104 ? 0.4839 0.4257 0.6217 -0.0122 -0.0174 -0.0043 104 ASN B CA 3368 C C . ASN B 104 ? 0.4987 0.4593 0.6509 -0.0283 -0.0178 0.0036 104 ASN B C 3369 O O . ASN B 104 ? 0.4543 0.4058 0.6058 -0.0218 -0.0167 0.0026 104 ASN B O 3370 C CB . ASN B 104 ? 0.5467 0.4297 0.6268 -0.0229 -0.0296 -0.0070 104 ASN B CB 3371 C CG . ASN B 104 ? 0.5846 0.4391 0.6324 0.0094 -0.0300 -0.0187 104 ASN B CG 3372 O OD1 . ASN B 104 ? 0.5321 0.4300 0.6066 0.0367 -0.0205 -0.0231 104 ASN B OD1 3373 N ND2 . ASN B 104 ? 0.6633 0.4500 0.6454 0.0046 -0.0423 -0.0236 104 ASN B ND2 3374 N N . GLU B 105 ? 0.4970 0.4984 0.6618 -0.0455 -0.0191 0.0118 105 GLU B N 3375 C CA . GLU B 105 ? 0.4808 0.5274 0.6607 -0.0535 -0.0178 0.0196 105 GLU B CA 3376 C C . GLU B 105 ? 0.4317 0.4860 0.6347 -0.0249 -0.0089 0.0155 105 GLU B C 3377 O O . GLU B 105 ? 0.4031 0.4614 0.6078 -0.0248 -0.0075 0.0164 105 GLU B O 3378 C CB . GLU B 105 ? 0.5011 0.6225 0.6938 -0.0624 -0.0192 0.0286 105 GLU B CB 3379 C CG . GLU B 105 ? 0.5714 0.7624 0.7703 -0.0781 -0.0197 0.0387 105 GLU B CG 3380 C CD . GLU B 105 ? 0.6960 0.9818 0.8971 -0.1028 -0.0252 0.0505 105 GLU B CD 3381 O OE1 . GLU B 105 ? 0.7662 1.1115 0.9877 -0.0647 -0.0208 0.0502 105 GLU B OE1 3382 O OE2 . GLU B 105 ? 0.7023 0.9974 0.8737 -0.1618 -0.0361 0.0606 105 GLU B OE2 3383 N N . ARG B 106 ? 0.4430 0.4897 0.6520 -0.0058 -0.0047 0.0117 106 ARG B N 3384 C CA . ARG B 106 ? 0.4676 0.4984 0.6752 0.0104 -0.0005 0.0081 106 ARG B CA 3385 C C . ARG B 106 ? 0.4427 0.4541 0.6519 0.0040 0.0005 0.0030 106 ARG B C 3386 O O . ARG B 106 ? 0.4719 0.4800 0.6795 0.0081 0.0017 0.0013 106 ARG B O 3387 C CB . ARG B 106 ? 0.5238 0.5286 0.7133 0.0208 -0.0003 0.0078 106 ARG B CB 3388 C CG . ARG B 106 ? 0.5776 0.6043 0.7559 0.0442 -0.0023 0.0126 106 ARG B CG 3389 C CD . ARG B 106 ? 0.7179 0.6859 0.8471 0.0690 -0.0051 0.0120 106 ARG B CD 3390 N NE . ARG B 106 ? 0.7916 0.7407 0.8892 0.1004 -0.0062 0.0085 106 ARG B NE 3391 C CZ . ARG B 106 ? 0.8981 0.7572 0.9323 0.1089 -0.0114 0.0045 106 ARG B CZ 3392 N NH1 . ARG B 106 ? 0.9955 0.7861 0.9955 0.0772 -0.0158 0.0065 106 ARG B NH1 3393 N NH2 . ARG B 106 ? 1.0224 0.8568 1.0164 0.1447 -0.0137 -0.0008 106 ARG B NH2 3394 N N . THR B 107 ? 0.4595 0.4637 0.6661 0.0001 -0.0007 0.0000 107 THR B N 3395 C CA . THR B 107 ? 0.3917 0.3982 0.5965 0.0061 -0.0003 -0.0048 107 THR B CA 3396 C C . THR B 107 ? 0.4225 0.4164 0.6194 0.0080 -0.0036 -0.0035 107 THR B C 3397 O O . THR B 107 ? 0.4047 0.4088 0.6064 0.0125 -0.0025 -0.0053 107 THR B O 3398 C CB . THR B 107 ? 0.3951 0.4048 0.5870 0.0186 -0.0015 -0.0096 107 THR B CB 3399 O OG1 . THR B 107 ? 0.3948 0.4296 0.5949 0.0113 0.0025 -0.0089 107 THR B OG1 3400 C CG2 . THR B 107 ? 0.4065 0.4372 0.5908 0.0396 -0.0021 -0.0146 107 THR B CG2 3401 N N . LEU B 108 ? 0.4263 0.3979 0.6041 -0.0027 -0.0091 0.0010 108 LEU B N 3402 C CA . LEU B 108 ? 0.4640 0.4185 0.6228 -0.0115 -0.0136 0.0059 108 LEU B CA 3403 C C . LEU B 108 ? 0.4450 0.4403 0.6305 -0.0133 -0.0078 0.0091 108 LEU B C 3404 O O . LEU B 108 ? 0.4368 0.4278 0.6178 -0.0090 -0.0079 0.0089 108 LEU B O 3405 C CB . LEU B 108 ? 0.4999 0.4229 0.6192 -0.0414 -0.0234 0.0140 108 LEU B CB 3406 C CG . LEU B 108 ? 0.5844 0.4353 0.6491 -0.0350 -0.0331 0.0085 108 LEU B CG 3407 C CD1 . LEU B 108 ? 0.6464 0.4411 0.6467 -0.0789 -0.0477 0.0178 108 LEU B CD1 3408 C CD2 . LEU B 108 ? 0.6231 0.4295 0.6542 0.0052 -0.0360 -0.0002 108 LEU B CD2 3409 N N . ASP B 109 ? 0.4302 0.4622 0.6342 -0.0121 -0.0035 0.0112 109 ASP B N 3410 C CA . ASP B 109 ? 0.4090 0.4711 0.6219 0.0013 0.0012 0.0110 109 ASP B CA 3411 C C . ASP B 109 ? 0.4050 0.4385 0.6146 0.0144 0.0031 0.0021 109 ASP B C 3412 O O . ASP B 109 ? 0.4570 0.4937 0.6611 0.0217 0.0043 0.0000 109 ASP B O 3413 C CB . ASP B 109 ? 0.4245 0.5248 0.6405 0.0163 0.0033 0.0134 109 ASP B CB 3414 C CG . ASP B 109 ? 0.4577 0.6215 0.6787 -0.0055 0.0005 0.0250 109 ASP B CG 3415 O OD1 . ASP B 109 ? 0.4619 0.6423 0.6760 -0.0347 -0.0024 0.0330 109 ASP B OD1 3416 O OD2 . ASP B 109 ? 0.4967 0.6967 0.7215 0.0024 0.0000 0.0276 109 ASP B OD2 3417 N N . PHE B 110 ? 0.3774 0.3899 0.5851 0.0113 0.0024 -0.0021 110 PHE B N 3418 C CA . PHE B 110 ? 0.3723 0.3694 0.5683 0.0059 0.0015 -0.0074 110 PHE B CA 3419 C C . PHE B 110 ? 0.3875 0.4013 0.5905 0.0050 0.0005 -0.0089 110 PHE B C 3420 O O . PHE B 110 ? 0.4178 0.4253 0.6090 0.0027 -0.0007 -0.0120 110 PHE B O 3421 C CB . PHE B 110 ? 0.3591 0.3576 0.5532 -0.0076 0.0009 -0.0075 110 PHE B CB 3422 C CG . PHE B 110 ? 0.3830 0.3884 0.5619 -0.0313 -0.0018 -0.0091 110 PHE B CG 3423 C CD1 . PHE B 110 ? 0.4414 0.3982 0.5786 -0.0463 -0.0069 -0.0104 110 PHE B CD1 3424 C CD2 . PHE B 110 ? 0.3447 0.4075 0.5394 -0.0396 -0.0012 -0.0087 110 PHE B CD2 3425 C CE1 . PHE B 110 ? 0.4705 0.4325 0.5816 -0.0849 -0.0127 -0.0096 110 PHE B CE1 3426 C CE2 . PHE B 110 ? 0.3822 0.4819 0.5645 -0.0720 -0.0046 -0.0072 110 PHE B CE2 3427 C CZ . PHE B 110 ? 0.4355 0.4825 0.5752 -0.1032 -0.0112 -0.0066 110 PHE B CZ 3428 N N . HIS B 111 ? 0.3632 0.3866 0.5723 0.0108 -0.0008 -0.0071 111 HIS B N 3429 C CA . HIS B 111 ? 0.3819 0.4122 0.5853 0.0197 -0.0038 -0.0075 111 HIS B CA 3430 C C . HIS B 111 ? 0.3935 0.4161 0.5920 0.0170 -0.0036 -0.0037 111 HIS B C 3431 O O . HIS B 111 ? 0.3867 0.4198 0.5831 0.0198 -0.0045 -0.0057 111 HIS B O 3432 C CB . HIS B 111 ? 0.4314 0.4398 0.6121 0.0365 -0.0088 -0.0064 111 HIS B CB 3433 C CG . HIS B 111 ? 0.4202 0.4563 0.6012 0.0532 -0.0086 -0.0118 111 HIS B CG 3434 N ND1 . HIS B 111 ? 0.4131 0.5138 0.6070 0.0606 -0.0075 -0.0152 111 HIS B ND1 3435 C CD2 . HIS B 111 ? 0.4289 0.4510 0.5964 0.0632 -0.0096 -0.0139 111 HIS B CD2 3436 C CE1 . HIS B 111 ? 0.4320 0.5709 0.6239 0.0767 -0.0065 -0.0183 111 HIS B CE1 3437 N NE2 . HIS B 111 ? 0.4324 0.5168 0.6071 0.0816 -0.0074 -0.0186 111 HIS B NE2 3438 N N . ASP B 112 ? 0.3682 0.3867 0.5641 0.0092 -0.0026 0.0027 112 ASP B N 3439 C CA . ASP B 112 ? 0.3633 0.3996 0.5553 0.0039 -0.0011 0.0086 112 ASP B CA 3440 C C . ASP B 112 ? 0.3602 0.4086 0.5559 0.0177 0.0027 0.0009 112 ASP B C 3441 O O . ASP B 112 ? 0.3922 0.4473 0.5814 0.0207 0.0028 0.0003 112 ASP B O 3442 C CB . ASP B 112 ? 0.3690 0.4352 0.5622 -0.0104 -0.0001 0.0177 112 ASP B CB 3443 C CG . ASP B 112 ? 0.3929 0.5012 0.5784 -0.0254 0.0006 0.0284 112 ASP B CG 3444 O OD1 . ASP B 112 ? 0.4176 0.5133 0.5925 -0.0245 -0.0001 0.0289 112 ASP B OD1 3445 O OD2 . ASP B 112 ? 0.4021 0.5692 0.5915 -0.0400 0.0019 0.0375 112 ASP B OD2 3446 N N . SER B 113 ? 0.3511 0.3874 0.5432 0.0259 0.0040 -0.0051 113 SER B N 3447 C CA . SER B 113 ? 0.3747 0.3871 0.5398 0.0394 0.0035 -0.0134 113 SER B CA 3448 C C . SER B 113 ? 0.3936 0.3882 0.5487 0.0240 -0.0011 -0.0190 113 SER B C 3449 O O . SER B 113 ? 0.4494 0.4300 0.5801 0.0291 -0.0030 -0.0244 113 SER B O 3450 C CB . SER B 113 ? 0.3981 0.3724 0.5375 0.0483 0.0017 -0.0170 113 SER B CB 3451 O OG . SER B 113 ? 0.4706 0.3806 0.5553 0.0506 -0.0043 -0.0257 113 SER B OG 3452 N N . ASN B 114 ? 0.3753 0.3812 0.5452 0.0067 -0.0035 -0.0179 114 ASN B N 3453 C CA . ASN B 114 ? 0.3889 0.4111 0.5530 -0.0094 -0.0084 -0.0211 114 ASN B CA 3454 C C . ASN B 114 ? 0.3744 0.4182 0.5459 0.0022 -0.0085 -0.0199 114 ASN B C 3455 O O . ASN B 114 ? 0.4024 0.4515 0.5590 -0.0072 -0.0129 -0.0241 114 ASN B O 3456 C CB . ASN B 114 ? 0.3845 0.4502 0.5661 -0.0209 -0.0099 -0.0190 114 ASN B CB 3457 C CG . ASN B 114 ? 0.4132 0.4610 0.5809 -0.0422 -0.0107 -0.0185 114 ASN B CG 3458 O OD1 . ASN B 114 ? 0.4309 0.4210 0.5568 -0.0589 -0.0149 -0.0208 114 ASN B OD1 3459 N ND2 . ASN B 114 ? 0.4245 0.5096 0.6136 -0.0383 -0.0081 -0.0155 114 ASN B ND2 3460 N N . VAL B 115 ? 0.3575 0.4064 0.5413 0.0165 -0.0057 -0.0129 115 VAL B N 3461 C CA . VAL B 115 ? 0.3884 0.4455 0.5662 0.0236 -0.0074 -0.0088 115 VAL B CA 3462 C C . VAL B 115 ? 0.4024 0.4583 0.5689 0.0255 -0.0041 -0.0108 115 VAL B C 3463 O O . VAL B 115 ? 0.4259 0.4886 0.5821 0.0264 -0.0066 -0.0137 115 VAL B O 3464 C CB . VAL B 115 ? 0.4205 0.4597 0.5881 0.0274 -0.0093 0.0017 115 VAL B CB 3465 C CG1 . VAL B 115 ? 0.4583 0.4916 0.6046 0.0279 -0.0122 0.0090 115 VAL B CG1 3466 C CG2 . VAL B 115 ? 0.4447 0.4755 0.6039 0.0426 -0.0146 0.0004 115 VAL B CG2 3467 N N . LYS B 116 ? 0.3967 0.4534 0.5618 0.0317 0.0010 -0.0097 116 LYS B N 3468 C CA . LYS B 116 ? 0.4151 0.4842 0.5626 0.0483 0.0049 -0.0131 116 LYS B CA 3469 C C . LYS B 116 ? 0.4766 0.5036 0.5885 0.0541 0.0000 -0.0270 116 LYS B C 3470 O O . LYS B 116 ? 0.4998 0.5298 0.5906 0.0647 0.0000 -0.0314 116 LYS B O 3471 C CB . LYS B 116 ? 0.4470 0.5399 0.5951 0.0647 0.0102 -0.0107 116 LYS B CB 3472 C CG . LYS B 116 ? 0.4814 0.6014 0.6025 0.1012 0.0147 -0.0161 116 LYS B CG 3473 C CD . LYS B 116 ? 0.5362 0.7151 0.6626 0.0985 0.0190 -0.0088 116 LYS B CD 3474 C CE . LYS B 116 ? 0.5732 0.8337 0.6866 0.1371 0.0268 -0.0081 116 LYS B CE 3475 N NZ . LYS B 116 ? 0.5737 0.9295 0.7213 0.1093 0.0309 0.0114 116 LYS B NZ 3476 N N . ASN B 117 ? 0.4957 0.4801 0.5915 0.0402 -0.0057 -0.0330 117 ASN B N 3477 C CA . ASN B 117 ? 0.5828 0.5079 0.6221 0.0293 -0.0149 -0.0445 117 ASN B CA 3478 C C . ASN B 117 ? 0.5908 0.5401 0.6345 0.0032 -0.0210 -0.0454 117 ASN B C 3479 O O . ASN B 117 ? 0.6710 0.5792 0.6628 -0.0058 -0.0290 -0.0546 117 ASN B O 3480 C CB . ASN B 117 ? 0.6397 0.5099 0.6469 0.0073 -0.0216 -0.0465 117 ASN B CB 3481 C CG . ASN B 117 ? 0.6840 0.5087 0.6593 0.0416 -0.0194 -0.0486 117 ASN B CG 3482 O OD1 . ASN B 117 ? 0.7287 0.5666 0.6956 0.0853 -0.0138 -0.0511 117 ASN B OD1 3483 N ND2 . ASN B 117 ? 0.7060 0.4899 0.6615 0.0240 -0.0238 -0.0465 117 ASN B ND2 3484 N N . LEU B 118 ? 0.5393 0.5507 0.6332 -0.0051 -0.0193 -0.0368 118 LEU B N 3485 C CA . LEU B 118 ? 0.5285 0.5823 0.6277 -0.0186 -0.0254 -0.0366 118 LEU B CA 3486 C C . LEU B 118 ? 0.5291 0.5875 0.6245 0.0027 -0.0224 -0.0358 118 LEU B C 3487 O O . LEU B 118 ? 0.5692 0.6254 0.6383 -0.0055 -0.0283 -0.0419 118 LEU B O 3488 C CB . LEU B 118 ? 0.5065 0.6231 0.6450 -0.0156 -0.0255 -0.0287 118 LEU B CB 3489 C CG . LEU B 118 ? 0.5122 0.6945 0.6574 -0.0144 -0.0320 -0.0270 118 LEU B CG 3490 C CD1 . LEU B 118 ? 0.5778 0.7880 0.7001 -0.0584 -0.0417 -0.0326 118 LEU B CD1 3491 C CD2 . LEU B 118 ? 0.4994 0.7333 0.6680 0.0117 -0.0317 -0.0207 118 LEU B CD2 3492 N N . TYR B 119 ? 0.4853 0.5510 0.5996 0.0235 -0.0142 -0.0274 119 TYR B N 3493 C CA . TYR B 119 ? 0.4707 0.5492 0.5764 0.0368 -0.0104 -0.0238 119 TYR B CA 3494 C C . TYR B 119 ? 0.5473 0.5991 0.6114 0.0486 -0.0103 -0.0369 119 TYR B C 3495 O O . TYR B 119 ? 0.5895 0.6476 0.6341 0.0519 -0.0125 -0.0404 119 TYR B O 3496 C CB . TYR B 119 ? 0.4232 0.5201 0.5444 0.0418 -0.0029 -0.0104 119 TYR B CB 3497 C CG . TYR B 119 ? 0.4441 0.5725 0.5540 0.0457 0.0014 -0.0025 119 TYR B CG 3498 C CD1 . TYR B 119 ? 0.4481 0.5792 0.5494 0.0365 -0.0028 0.0086 119 TYR B CD1 3499 C CD2 . TYR B 119 ? 0.4364 0.5982 0.5370 0.0628 0.0096 -0.0051 119 TYR B CD2 3500 C CE1 . TYR B 119 ? 0.4618 0.6251 0.5477 0.0322 0.0011 0.0187 119 TYR B CE1 3501 C CE2 . TYR B 119 ? 0.4411 0.6558 0.5328 0.0644 0.0150 0.0037 119 TYR B CE2 3502 C CZ . TYR B 119 ? 0.4704 0.6847 0.5562 0.0432 0.0109 0.0164 119 TYR B CZ 3503 O OH . TYR B 119 ? 0.4824 0.7528 0.5548 0.0387 0.0163 0.0271 119 TYR B OH 3504 N N . ASP B 120 ? 0.5639 0.5766 0.6020 0.0611 -0.0092 -0.0451 120 ASP B N 3505 C CA . ASP B 120 ? 0.6393 0.6028 0.6115 0.0867 -0.0119 -0.0599 120 ASP B CA 3506 C C . ASP B 120 ? 0.6821 0.5854 0.6018 0.0587 -0.0261 -0.0717 120 ASP B C 3507 O O . ASP B 120 ? 0.7395 0.6186 0.6118 0.0705 -0.0300 -0.0814 120 ASP B O 3508 C CB . ASP B 120 ? 0.6807 0.5999 0.6162 0.1176 -0.0106 -0.0662 120 ASP B CB 3509 C CG . ASP B 120 ? 0.6410 0.6429 0.6165 0.1486 0.0025 -0.0558 120 ASP B CG 3510 O OD1 . ASP B 120 ? 0.6495 0.7229 0.6441 0.1580 0.0099 -0.0492 120 ASP B OD1 3511 O OD2 . ASP B 120 ? 0.6518 0.6566 0.6378 0.1577 0.0049 -0.0523 120 ASP B OD2 3512 N N . LYS B 121 ? 0.6955 0.5837 0.6197 0.0172 -0.0345 -0.0699 121 LYS B N 3513 C CA . LYS B 121 ? 0.7914 0.6467 0.6670 -0.0277 -0.0502 -0.0770 121 LYS B CA 3514 C C . LYS B 121 ? 0.7788 0.6872 0.6686 -0.0295 -0.0517 -0.0768 121 LYS B C 3515 O O . LYS B 121 ? 0.8763 0.7351 0.6994 -0.0438 -0.0629 -0.0881 121 LYS B O 3516 C CB . LYS B 121 ? 0.7955 0.6931 0.7044 -0.0743 -0.0551 -0.0682 121 LYS B CB 3517 C CG . LYS B 121 ? 0.8967 0.7856 0.7552 -0.1381 -0.0727 -0.0713 121 LYS B CG 3518 C CD . LYS B 121 ? 0.8903 0.8619 0.7950 -0.1767 -0.0738 -0.0597 121 LYS B CD 3519 C CE . LYS B 121 ? 1.0094 0.9966 0.8604 -0.2569 -0.0925 -0.0586 121 LYS B CE 3520 N NZ . LYS B 121 ? 1.0812 1.1267 0.9281 -0.2726 -0.1010 -0.0613 121 LYS B NZ 3521 N N . VAL B 122 ? 0.6768 0.6726 0.6405 -0.0151 -0.0426 -0.0639 122 VAL B N 3522 C CA . VAL B 122 ? 0.6446 0.6892 0.6203 -0.0097 -0.0437 -0.0608 122 VAL B CA 3523 C C . VAL B 122 ? 0.6760 0.6971 0.6210 0.0226 -0.0374 -0.0663 122 VAL B C 3524 O O . VAL B 122 ? 0.7207 0.7355 0.6302 0.0193 -0.0437 -0.0737 122 VAL B O 3525 C CB . VAL B 122 ? 0.5802 0.6957 0.6174 0.0028 -0.0385 -0.0443 122 VAL B CB 3526 C CG1 . VAL B 122 ? 0.5786 0.7261 0.6155 0.0175 -0.0390 -0.0383 122 VAL B CG1 3527 C CG2 . VAL B 122 ? 0.5614 0.7261 0.6202 -0.0189 -0.0464 -0.0415 122 VAL B CG2 3528 N N . ARG B 123 ? 0.6646 0.6869 0.6215 0.0537 -0.0251 -0.0624 123 ARG B N 3529 C CA . ARG B 123 ? 0.6994 0.7282 0.6273 0.0899 -0.0175 -0.0669 123 ARG B CA 3530 C C . ARG B 123 ? 0.8087 0.7557 0.6472 0.1043 -0.0270 -0.0890 123 ARG B C 3531 O O . ARG B 123 ? 0.8453 0.7975 0.6508 0.1203 -0.0275 -0.0957 123 ARG B O 3532 C CB . ARG B 123 ? 0.6939 0.7546 0.6425 0.1183 -0.0047 -0.0599 123 ARG B CB 3533 C CG . ARG B 123 ? 0.7157 0.8331 0.6485 0.1559 0.0057 -0.0592 123 ARG B CG 3534 C CD . ARG B 123 ? 0.7252 0.9052 0.6817 0.1787 0.0173 -0.0501 123 ARG B CD 3535 N NE . ARG B 123 ? 0.7619 0.8798 0.6884 0.2027 0.0136 -0.0625 123 ARG B NE 3536 C CZ . ARG B 123 ? 0.8397 0.8978 0.6869 0.2552 0.0099 -0.0823 123 ARG B CZ 3537 N NH1 . ARG B 123 ? 0.8903 0.9449 0.6805 0.2929 0.0099 -0.0949 123 ARG B NH1 3538 N NH2 . ARG B 123 ? 0.8620 0.8508 0.6731 0.2741 0.0046 -0.0902 123 ARG B NH2 3539 N N . LEU B 124 ? 0.8834 0.7417 0.6686 0.0969 -0.0365 -0.1002 124 LEU B N 3540 C CA . LEU B 124 ? 1.0302 0.7673 0.6950 0.1089 -0.0507 -0.1221 124 LEU B CA 3541 C C . LEU B 124 ? 1.0820 0.7838 0.7004 0.0601 -0.0678 -0.1298 124 LEU B C 3542 O O . LEU B 124 ? 1.2178 0.8149 0.7241 0.0692 -0.0810 -0.1484 124 LEU B O 3543 C CB . LEU B 124 ? 1.1215 0.7491 0.7202 0.1046 -0.0605 -0.1290 124 LEU B CB 3544 C CG . LEU B 124 ? 1.1333 0.7809 0.7519 0.1619 -0.0471 -0.1254 124 LEU B CG 3545 C CD1 . LEU B 124 ? 1.1682 0.7410 0.7617 0.1391 -0.0550 -0.1233 124 LEU B CD1 3546 C CD2 . LEU B 124 ? 1.2317 0.8405 0.7642 0.2449 -0.0447 -0.1416 124 LEU B CD2 3547 N N . GLN B 125 ? 1.0074 0.7939 0.7002 0.0115 -0.0694 -0.1162 125 GLN B N 3548 C CA . GLN B 125 ? 1.0536 0.8463 0.7167 -0.0345 -0.0850 -0.1204 125 GLN B CA 3549 C C . GLN B 125 ? 0.9964 0.8469 0.6792 -0.0032 -0.0777 -0.1198 125 GLN B C 3550 O O . GLN B 125 ? 1.1176 0.9183 0.7254 -0.0068 -0.0885 -0.1339 125 GLN B O 3551 C CB . GLN B 125 ? 1.0065 0.8943 0.7405 -0.0863 -0.0896 -0.1054 125 GLN B CB 3552 C CG . GLN B 125 ? 1.0707 0.9204 0.7804 -0.1355 -0.0996 -0.1042 125 GLN B CG 3553 C CD . GLN B 125 ? 1.0353 1.0096 0.8092 -0.1822 -0.1046 -0.0905 125 GLN B CD 3554 O OE1 . GLN B 125 ? 1.1113 1.1237 0.8560 -0.2327 -0.1204 -0.0917 125 GLN B OE1 3555 N NE2 . GLN B 125 ? 0.9385 0.9858 0.7945 -0.1623 -0.0921 -0.0775 125 GLN B NE2 3556 N N . LEU B 126 ? 0.8632 0.8092 0.6358 0.0227 -0.0611 -0.1026 126 LEU B N 3557 C CA . LEU B 126 ? 0.8610 0.8686 0.6551 0.0445 -0.0541 -0.0960 126 LEU B CA 3558 C C . LEU B 126 ? 0.9453 0.9242 0.6849 0.0920 -0.0463 -0.1078 126 LEU B C 3559 O O . LEU B 126 ? 0.9821 0.9865 0.7042 0.1020 -0.0462 -0.1097 126 LEU B O 3560 C CB . LEU B 126 ? 0.7659 0.8561 0.6444 0.0532 -0.0416 -0.0721 126 LEU B CB 3561 C CG . LEU B 126 ? 0.7019 0.8302 0.6281 0.0261 -0.0485 -0.0609 126 LEU B CG 3562 C CD1 . LEU B 126 ? 0.6492 0.8232 0.6219 0.0425 -0.0406 -0.0395 126 LEU B CD1 3563 C CD2 . LEU B 126 ? 0.7324 0.8868 0.6396 -0.0031 -0.0647 -0.0664 126 LEU B CD2 3564 N N . ARG B 127 ? 1.0334 0.9695 0.7431 0.1276 -0.0398 -0.1158 127 ARG B N 3565 C CA . ARG B 127 ? 1.1307 1.0541 0.7781 0.1890 -0.0325 -0.1292 127 ARG B CA 3566 C C . ARG B 127 ? 1.0723 1.1126 0.7689 0.2041 -0.0179 -0.1141 127 ARG B C 3567 O O . ARG B 127 ? 0.9849 1.1118 0.7605 0.1906 -0.0062 -0.0907 127 ARG B O 3568 C CB . ARG B 127 ? 1.2886 1.0798 0.8064 0.1966 -0.0513 -0.1571 127 ARG B CB 3569 C CG . ARG B 127 ? 1.3886 1.0419 0.8254 0.1861 -0.0666 -0.1706 127 ARG B CG 3570 C CD . ARG B 127 ? 1.5490 1.0555 0.8541 0.1496 -0.0935 -0.1914 127 ARG B CD 3571 N NE . ARG B 127 ? 1.7200 1.1500 0.9073 0.2115 -0.0978 -0.2147 127 ARG B NE 3572 C CZ . ARG B 127 ? 1.9325 1.1967 0.9638 0.1954 -0.1235 -0.2378 127 ARG B CZ 3573 N NH1 . ARG B 127 ? 2.0215 1.1922 1.0015 0.1061 -0.1474 -0.2375 127 ARG B NH1 3574 N NH2 . ARG B 127 ? 2.0616 1.2537 0.9776 0.2651 -0.1269 -0.2609 127 ARG B NH2 3575 N N . ASP B 128 ? 1.1175 1.1521 0.7581 0.2249 -0.0204 -0.1261 128 ASP B N 3576 C CA . ASP B 128 ? 1.0917 1.2382 0.7692 0.2359 -0.0066 -0.1102 128 ASP B CA 3577 C C . ASP B 128 ? 1.0499 1.2190 0.7572 0.1895 -0.0147 -0.0979 128 ASP B C 3578 O O . ASP B 128 ? 1.0464 1.2856 0.7631 0.1945 -0.0072 -0.0860 128 ASP B O 3579 C CB . ASP B 128 ? 1.2039 1.3579 0.8032 0.3018 -0.0005 -0.1290 128 ASP B CB 3580 C CG . ASP B 128 ? 1.3653 1.3901 0.8550 0.3107 -0.0199 -0.1591 128 ASP B CG 3581 O OD1 . ASP B 128 ? 1.3870 1.3488 0.8742 0.2527 -0.0372 -0.1608 128 ASP B OD1 3582 O OD2 . ASP B 128 ? 1.5406 1.5295 0.9371 0.3763 -0.0191 -0.1812 128 ASP B OD2 3583 N N . ASN B 129 ? 1.0144 1.1352 0.7324 0.1467 -0.0303 -0.0994 129 ASN B N 3584 C CA . ASN B 129 ? 0.9678 1.1264 0.7170 0.1127 -0.0388 -0.0863 129 ASN B CA 3585 C C . ASN B 129 ? 0.8823 1.1011 0.7048 0.0992 -0.0321 -0.0567 129 ASN B C 3586 O O . ASN B 129 ? 0.8807 1.1239 0.7187 0.0837 -0.0408 -0.0452 129 ASN B O 3587 C CB . ASN B 129 ? 1.0123 1.1222 0.7373 0.0732 -0.0595 -0.0992 129 ASN B CB 3588 C CG . ASN B 129 ? 1.1375 1.1721 0.7648 0.0704 -0.0734 -0.1255 129 ASN B CG 3589 O OD1 . ASN B 129 ? 1.2355 1.2390 0.8061 0.1126 -0.0669 -0.1387 129 ASN B OD1 3590 N ND2 . ASN B 129 ? 1.1659 1.1747 0.7638 0.0197 -0.0941 -0.1331 129 ASN B ND2 3591 N N . ALA B 130 ? 0.8200 1.0566 0.6738 0.1075 -0.0192 -0.0448 130 ALA B N 3592 C CA . ALA B 130 ? 0.7452 1.0095 0.6424 0.0906 -0.0158 -0.0175 130 ALA B CA 3593 C C . ALA B 130 ? 0.7540 1.0616 0.6623 0.0944 -0.0003 -0.0034 130 ALA B C 3594 O O . ALA B 130 ? 0.7979 1.1159 0.6981 0.1180 0.0077 -0.0171 130 ALA B O 3595 C CB . ALA B 130 ? 0.7137 0.9462 0.6407 0.0774 -0.0232 -0.0181 130 ALA B CB 3596 N N . LYS B 131 ? 0.7519 1.0824 0.6670 0.0701 0.0015 0.0245 131 LYS B N 3597 C CA . LYS B 131 ? 0.7527 1.1383 0.6760 0.0538 0.0133 0.0433 131 LYS B CA 3598 C C . LYS B 131 ? 0.7075 1.0601 0.6580 0.0399 0.0116 0.0473 131 LYS B C 3599 O O . LYS B 131 ? 0.7190 1.0080 0.6698 0.0275 0.0004 0.0534 131 LYS B O 3600 C CB . LYS B 131 ? 0.8302 1.2364 0.7261 0.0160 0.0120 0.0749 131 LYS B CB 3601 C CG . LYS B 131 ? 0.9512 1.4018 0.8183 0.0236 0.0150 0.0766 131 LYS B CG 3602 C CD . LYS B 131 ? 1.0881 1.5092 0.9116 -0.0153 0.0057 0.1078 131 LYS B CD 3603 C CE . LYS B 131 ? 1.1871 1.6935 0.9817 -0.0294 0.0148 0.1226 131 LYS B CE 3604 N NZ . LYS B 131 ? 1.2138 1.8299 1.0135 -0.0622 0.0290 0.1413 131 LYS B NZ 3605 N N . GLU B 132 ? 0.6533 1.0547 0.6214 0.0486 0.0221 0.0435 132 GLU B N 3606 C CA . GLU B 132 ? 0.6098 0.9897 0.6018 0.0332 0.0210 0.0486 132 GLU B CA 3607 C C . GLU B 132 ? 0.6340 1.0405 0.6128 -0.0186 0.0205 0.0807 132 GLU B C 3608 O O . GLU B 132 ? 0.6526 1.1590 0.6299 -0.0351 0.0304 0.0943 132 GLU B O 3609 C CB . GLU B 132 ? 0.6003 1.0222 0.6071 0.0678 0.0306 0.0319 132 GLU B CB 3610 C CG . GLU B 132 ? 0.5801 0.9691 0.6123 0.0596 0.0284 0.0313 132 GLU B CG 3611 C CD . GLU B 132 ? 0.5974 1.0105 0.6313 0.1032 0.0353 0.0133 132 GLU B CD 3612 O OE1 . GLU B 132 ? 0.6799 1.1398 0.6880 0.1470 0.0422 0.0013 132 GLU B OE1 3613 O OE2 . GLU B 132 ? 0.5854 0.9651 0.6371 0.0998 0.0328 0.0109 132 GLU B OE2 3614 N N . LEU B 133 ? 0.6495 0.9672 0.6063 -0.0453 0.0073 0.0936 133 LEU B N 3615 C CA . LEU B 133 ? 0.6927 0.9922 0.6014 -0.1032 0.0004 0.1255 133 LEU B CA 3616 C C . LEU B 133 ? 0.6859 1.0209 0.6005 -0.1431 0.0029 0.1385 133 LEU B C 3617 O O . LEU B 133 ? 0.7351 1.0916 0.6055 -0.2057 -0.0008 0.1670 133 LEU B O 3618 C CB . LEU B 133 ? 0.7618 0.9290 0.6172 -0.1056 -0.0181 0.1332 133 LEU B CB 3619 C CG . LEU B 133 ? 0.7870 0.9283 0.6192 -0.0781 -0.0241 0.1299 133 LEU B CG 3620 C CD1 . LEU B 133 ? 0.8722 0.8863 0.6352 -0.0717 -0.0442 0.1407 133 LEU B CD1 3621 C CD2 . LEU B 133 ? 0.8197 1.0265 0.6258 -0.1067 -0.0181 0.1473 133 LEU B CD2 3622 N N . GLY B 134 ? 0.6261 0.9666 0.5873 -0.1141 0.0074 0.1196 134 GLY B N 3623 C CA . GLY B 134 ? 0.6313 1.0162 0.6040 -0.1459 0.0097 0.1293 134 GLY B CA 3624 C C . GLY B 134 ? 0.6807 0.9519 0.6302 -0.1656 -0.0038 0.1323 134 GLY B C 3625 O O . GLY B 134 ? 0.6905 0.9884 0.6413 -0.1997 -0.0045 0.1415 134 GLY B O 3626 N N . ASN B 135 ? 0.7119 0.8673 0.6371 -0.1399 -0.0149 0.1238 135 ASN B N 3627 C CA . ASN B 135 ? 0.7621 0.7994 0.6428 -0.1491 -0.0299 0.1274 135 ASN B CA 3628 C C . ASN B 135 ? 0.7169 0.7103 0.6297 -0.0902 -0.0313 0.1030 135 ASN B C 3629 O O . ASN B 135 ? 0.7875 0.6864 0.6574 -0.0787 -0.0439 0.1028 135 ASN B O 3630 C CB . ASN B 135 ? 0.8859 0.8121 0.6631 -0.1809 -0.0480 0.1498 135 ASN B CB 3631 C CG . ASN B 135 ? 0.9087 0.8080 0.6729 -0.1380 -0.0512 0.1439 135 ASN B CG 3632 O OD1 . ASN B 135 ? 0.8461 0.8227 0.6790 -0.0975 -0.0394 0.1250 135 ASN B OD1 3633 N ND2 . ASN B 135 ? 1.0312 0.8118 0.6939 -0.1476 -0.0696 0.1606 135 ASN B ND2 3634 N N . GLY B 136 ? 0.6328 0.6942 0.6091 -0.0539 -0.0199 0.0829 136 GLY B N 3635 C CA . GLY B 136 ? 0.5847 0.6263 0.5891 -0.0125 -0.0219 0.0626 136 GLY B CA 3636 C C . GLY B 136 ? 0.5813 0.6307 0.5817 0.0124 -0.0253 0.0557 136 GLY B C 3637 O O . GLY B 136 ? 0.5689 0.6346 0.5966 0.0368 -0.0262 0.0393 136 GLY B O 3638 N N . CYS B 137 ? 0.6326 0.6791 0.5964 -0.0003 -0.0277 0.0696 137 CYS B N 3639 C CA . CYS B 137 ? 0.6702 0.7173 0.6193 0.0229 -0.0337 0.0663 137 CYS B CA 3640 C C . CYS B 137 ? 0.6524 0.7666 0.6229 0.0211 -0.0240 0.0591 137 CYS B C 3641 O O . CYS B 137 ? 0.6521 0.8111 0.6290 0.0022 -0.0136 0.0646 137 CYS B O 3642 C CB . CYS B 137 ? 0.7675 0.7382 0.6378 0.0183 -0.0475 0.0875 137 CYS B CB 3643 S SG . CYS B 137 ? 0.8825 0.7400 0.6886 0.0397 -0.0642 0.0929 137 CYS B SG 3644 N N . PHE B 138 ? 0.6370 0.7661 0.6128 0.0435 -0.0286 0.0467 138 PHE B N 3645 C CA . PHE B 138 ? 0.6238 0.7960 0.6009 0.0467 -0.0237 0.0379 138 PHE B CA 3646 C C . PHE B 138 ? 0.6647 0.8280 0.6071 0.0546 -0.0337 0.0475 138 PHE B C 3647 O O . PHE B 138 ? 0.6850 0.8359 0.6218 0.0741 -0.0450 0.0453 138 PHE B O 3648 C CB . PHE B 138 ? 0.5909 0.7779 0.5908 0.0573 -0.0241 0.0127 138 PHE B CB 3649 C CG . PHE B 138 ? 0.5716 0.7527 0.5912 0.0559 -0.0162 0.0026 138 PHE B CG 3650 C CD1 . PHE B 138 ? 0.5787 0.7809 0.5902 0.0647 -0.0056 -0.0027 138 PHE B CD1 3651 C CD2 . PHE B 138 ? 0.5671 0.7285 0.6079 0.0525 -0.0196 -0.0007 138 PHE B CD2 3652 C CE1 . PHE B 138 ? 0.5917 0.7867 0.6119 0.0736 0.0000 -0.0114 138 PHE B CE1 3653 C CE2 . PHE B 138 ? 0.5672 0.7176 0.6204 0.0521 -0.0135 -0.0084 138 PHE B CE2 3654 C CZ . PHE B 138 ? 0.5907 0.7540 0.6318 0.0642 -0.0042 -0.0134 138 PHE B CZ 3655 N N . GLU B 139 ? 0.6872 0.8688 0.6042 0.0431 -0.0295 0.0587 139 GLU B N 3656 C CA . GLU B 139 ? 0.7461 0.9172 0.6239 0.0506 -0.0389 0.0689 139 GLU B CA 3657 C C . GLU B 139 ? 0.7362 0.9587 0.6254 0.0618 -0.0361 0.0504 139 GLU B C 3658 O O . GLU B 139 ? 0.7393 0.9991 0.6315 0.0570 -0.0246 0.0445 139 GLU B O 3659 C CB . GLU B 139 ? 0.8288 0.9777 0.6560 0.0204 -0.0382 0.0972 139 GLU B CB 3660 C CG . GLU B 139 ? 0.9145 1.0346 0.6839 0.0265 -0.0495 0.1123 139 GLU B CG 3661 C CD . GLU B 139 ? 1.0311 1.1350 0.7427 -0.0193 -0.0482 0.1424 139 GLU B CD 3662 O OE1 . GLU B 139 ? 1.1109 1.1526 0.7821 -0.0523 -0.0534 0.1613 139 GLU B OE1 3663 O OE2 . GLU B 139 ? 1.1037 1.2596 0.8042 -0.0285 -0.0427 0.1478 139 GLU B OE2 3664 N N . PHE B 140 ? 0.7537 0.9834 0.6418 0.0793 -0.0481 0.0409 140 PHE B N 3665 C CA . PHE B 140 ? 0.7672 1.0337 0.6564 0.0816 -0.0501 0.0208 140 PHE B CA 3666 C C . PHE B 140 ? 0.8135 1.0987 0.6688 0.0825 -0.0481 0.0275 140 PHE B C 3667 O O . PHE B 140 ? 0.8499 1.1216 0.6759 0.0827 -0.0514 0.0506 140 PHE B O 3668 C CB . PHE B 140 ? 0.7481 1.0406 0.6446 0.0900 -0.0655 0.0126 140 PHE B CB 3669 C CG . PHE B 140 ? 0.7072 1.0045 0.6361 0.0830 -0.0674 0.0017 140 PHE B CG 3670 C CD1 . PHE B 140 ? 0.7029 0.9902 0.6440 0.0991 -0.0698 0.0129 140 PHE B CD1 3671 C CD2 . PHE B 140 ? 0.7066 1.0079 0.6392 0.0594 -0.0686 -0.0195 140 PHE B CD2 3672 C CE1 . PHE B 140 ? 0.6663 0.9704 0.6379 0.0923 -0.0707 0.0035 140 PHE B CE1 3673 C CE2 . PHE B 140 ? 0.6872 0.9934 0.6424 0.0444 -0.0714 -0.0268 140 PHE B CE2 3674 C CZ . PHE B 140 ? 0.6546 0.9738 0.6370 0.0611 -0.0711 -0.0149 140 PHE B CZ 3675 N N . TYR B 141 ? 0.8399 1.1445 0.6853 0.0837 -0.0448 0.0073 141 TYR B N 3676 C CA . TYR B 141 ? 0.9000 1.2301 0.7108 0.0885 -0.0438 0.0101 141 TYR B CA 3677 C C . TYR B 141 ? 0.9020 1.2456 0.6982 0.0917 -0.0607 0.0078 141 TYR B C 3678 O O . TYR B 141 ? 0.9789 1.3349 0.7494 0.0972 -0.0642 0.0238 141 TYR B O 3679 C CB . TYR B 141 ? 0.9300 1.2691 0.7187 0.0996 -0.0342 -0.0120 141 TYR B CB 3680 C CG . TYR B 141 ? 0.9253 1.2875 0.7249 0.1060 -0.0164 -0.0046 141 TYR B CG 3681 C CD1 . TYR B 141 ? 0.9490 1.3567 0.7472 0.0927 -0.0071 0.0236 141 TYR B CD1 3682 C CD2 . TYR B 141 ? 0.9318 1.2745 0.7369 0.1206 -0.0107 -0.0230 141 TYR B CD2 3683 C CE1 . TYR B 141 ? 0.9555 1.4132 0.7655 0.0896 0.0081 0.0333 141 TYR B CE1 3684 C CE2 . TYR B 141 ? 0.9329 1.3199 0.7505 0.1310 0.0049 -0.0151 141 TYR B CE2 3685 C CZ . TYR B 141 ? 0.9466 1.4037 0.7714 0.1133 0.0148 0.0131 141 TYR B CZ 3686 O OH . TYR B 141 ? 0.9807 1.5111 0.8193 0.1147 0.0296 0.0238 141 TYR B OH 3687 N N . HIS B 142 ? 1.1036 1.4986 0.9449 0.2846 0.0505 -0.1520 142 HIS B N 3688 C CA . HIS B 142 ? 1.1410 1.5249 0.8781 0.3013 0.0025 -0.1719 142 HIS B CA 3689 C C . HIS B 142 ? 1.0792 1.4736 0.8431 0.2795 -0.0229 -0.1348 142 HIS B C 3690 O O . HIS B 142 ? 0.9942 1.3925 0.8518 0.2460 -0.0135 -0.1049 142 HIS B O 3691 C CB . HIS B 142 ? 1.1410 1.5201 0.8866 0.2913 -0.0577 -0.2383 142 HIS B CB 3692 C CG . HIS B 142 ? 1.0269 1.4088 0.8978 0.2446 -0.0796 -0.2425 142 HIS B CG 3693 N ND1 . HIS B 142 ? 0.9606 1.3586 0.8816 0.2120 -0.1210 -0.2383 142 HIS B ND1 3694 C CD2 . HIS B 142 ? 0.9891 1.3542 0.9340 0.2339 -0.0622 -0.2470 142 HIS B CD2 3695 C CE1 . HIS B 142 ? 0.8903 1.2695 0.8946 0.1820 -0.1237 -0.2378 142 HIS B CE1 3696 N NE2 . HIS B 142 ? 0.9092 1.2664 0.9269 0.1964 -0.0942 -0.2434 142 HIS B NE2 3697 N N . LYS B 143 ? 1.1557 1.5524 0.8322 0.3055 -0.0597 -0.1401 143 LYS B N 3698 C CA . LYS B 143 ? 1.1091 1.5210 0.8184 0.2925 -0.0930 -0.1171 143 LYS B CA 3699 C C . LYS B 143 ? 1.0060 1.4493 0.8207 0.2522 -0.1377 -0.1526 143 LYS B C 3700 O O . LYS B 143 ? 1.0071 1.4599 0.8347 0.2441 -0.1637 -0.2040 143 LYS B O 3701 C CB . LYS B 143 ? 1.2215 1.6400 0.8211 0.3411 -0.1279 -0.1171 143 LYS B CB 3702 C CG . LYS B 143 ? 1.3687 1.7321 0.8506 0.3834 -0.0774 -0.0597 143 LYS B CG 3703 C CD . LYS B 143 ? 1.4400 1.8003 0.8649 0.4201 -0.1126 -0.0344 143 LYS B CD 3704 C CE . LYS B 143 ? 1.4996 1.9206 0.8889 0.4565 -0.1969 -0.0890 143 LYS B CE 3705 N NZ . LYS B 143 ? 1.4212 1.9018 0.9112 0.4445 -0.2445 -0.0933 143 LYS B NZ 3706 N N . CYS B 144 ? 0.9126 1.3579 0.7932 0.2281 -0.1408 -0.1245 144 CYS B N 3707 C CA . CYS B 144 ? 0.8287 1.2889 0.7992 0.1920 -0.1642 -0.1443 144 CYS B CA 3708 C C . CYS B 144 ? 0.8196 1.3074 0.8066 0.1973 -0.1842 -0.1278 144 CYS B C 3709 O O . CYS B 144 ? 0.8390 1.2974 0.8354 0.1939 -0.1676 -0.0917 144 CYS B O 3710 C CB . CYS B 144 ? 0.7721 1.1938 0.7994 0.1654 -0.1388 -0.1261 144 CYS B CB 3711 S SG . CYS B 144 ? 0.7257 1.1304 0.8274 0.1304 -0.1537 -0.1465 144 CYS B SG 3712 N N . ASP B 145 ? 0.8357 1.3826 0.8299 0.2091 -0.2231 -0.1589 145 ASP B N 3713 C CA . ASP B 145 ? 0.8045 1.4006 0.8332 0.2230 -0.2416 -0.1478 145 ASP B CA 3714 C C . ASP B 145 ? 0.7208 1.3182 0.8432 0.1840 -0.2242 -0.1429 145 ASP B C 3715 O O . ASP B 145 ? 0.7011 1.2516 0.8465 0.1503 -0.2044 -0.1459 145 ASP B O 3716 C CB . ASP B 145 ? 0.8405 1.5207 0.8761 0.2472 -0.2970 -0.1902 145 ASP B CB 3717 C CG . ASP B 145 ? 0.8330 1.5498 0.9489 0.2031 -0.3246 -0.2501 145 ASP B CG 3718 O OD1 . ASP B 145 ? 0.8051 1.4788 0.9719 0.1569 -0.2948 -0.2520 145 ASP B OD1 3719 O OD2 . ASP B 145 ? 0.8904 1.6710 1.0141 0.2165 -0.3809 -0.2979 145 ASP B OD2 3720 N N . ASN B 146 ? 0.7006 1.3479 0.8691 0.1964 -0.2278 -0.1334 146 ASN B N 3721 C CA . ASN B 146 ? 0.6501 1.2861 0.8831 0.1696 -0.1961 -0.1198 146 ASN B CA 3722 C C . ASN B 146 ? 0.6613 1.3055 0.9746 0.1172 -0.1898 -0.1499 146 ASN B C 3723 O O . ASN B 146 ? 0.6684 1.2441 0.9815 0.0937 -0.1565 -0.1327 146 ASN B O 3724 C CB . ASN B 146 ? 0.6263 1.3266 0.9007 0.2005 -0.1921 -0.1062 146 ASN B CB 3725 C CG . ASN B 146 ? 0.6455 1.2963 0.8259 0.2534 -0.1875 -0.0690 146 ASN B CG 3726 O OD1 . ASN B 146 ? 0.6421 1.1981 0.7426 0.2526 -0.1753 -0.0470 146 ASN B OD1 3727 N ND2 . ASN B 146 ? 0.6711 1.3854 0.8709 0.2995 -0.1975 -0.0633 146 ASN B ND2 3728 N N . GLU B 147 ? 0.7188 1.4330 1.0903 0.1011 -0.2254 -0.1962 147 GLU B N 3729 C CA . GLU B 147 ? 0.7735 1.4757 1.2191 0.0452 -0.2215 -0.2307 147 GLU B CA 3730 C C . GLU B 147 ? 0.7462 1.3399 1.1212 0.0343 -0.2072 -0.2296 147 GLU B C 3731 O O . GLU B 147 ? 0.7426 1.2724 1.1438 0.0005 -0.1785 -0.2259 147 GLU B O 3732 C CB . GLU B 147 ? 0.8508 1.6395 1.3628 0.0306 -0.2779 -0.2932 147 GLU B CB 3733 C CG . GLU B 147 ? 0.9036 1.8259 1.5216 0.0411 -0.3022 -0.3036 147 GLU B CG 3734 C CD . GLU B 147 ? 0.9676 1.9386 1.5038 0.1135 -0.3465 -0.2978 147 GLU B CD 3735 O OE1 . GLU B 147 ? 0.9659 1.8841 1.4092 0.1561 -0.3164 -0.2452 147 GLU B OE1 3736 O OE2 . GLU B 147 ? 1.0488 2.1008 1.6068 0.1294 -0.4149 -0.3474 147 GLU B OE2 3737 N N . CYS B 148 ? 0.7304 1.3032 1.0166 0.0681 -0.2228 -0.2302 148 CYS B N 3738 C CA . CYS B 148 ? 0.7455 1.2366 0.9786 0.0691 -0.2054 -0.2258 148 CYS B CA 3739 C C . CYS B 148 ? 0.6909 1.1204 0.9177 0.0670 -0.1718 -0.1799 148 CYS B C 3740 O O . CYS B 148 ? 0.6969 1.0625 0.9333 0.0499 -0.1568 -0.1793 148 CYS B O 3741 C CB . CYS B 148 ? 0.7850 1.2800 0.9337 0.1094 -0.2128 -0.2239 148 CYS B CB 3742 S SG . CYS B 148 ? 0.8535 1.2807 0.9615 0.1198 -0.1821 -0.2143 148 CYS B SG 3743 N N . MET B 149 ? 0.6365 1.0747 0.8368 0.0894 -0.1649 -0.1439 149 MET B N 3744 C CA . MET B 149 ? 0.6154 0.9901 0.7946 0.0924 -0.1457 -0.1090 149 MET B CA 3745 C C . MET B 149 ? 0.6421 0.9807 0.8506 0.0702 -0.1245 -0.1044 149 MET B C 3746 O O . MET B 149 ? 0.6658 0.9278 0.8457 0.0706 -0.1156 -0.0905 149 MET B O 3747 C CB . MET B 149 ? 0.5995 0.9793 0.7437 0.1184 -0.1437 -0.0797 149 MET B CB 3748 C CG . MET B 149 ? 0.6029 0.9843 0.7048 0.1385 -0.1514 -0.0701 149 MET B CG 3749 S SD . MET B 149 ? 0.6205 0.9526 0.7202 0.1288 -0.1468 -0.0651 149 MET B SD 3750 C CE . MET B 149 ? 0.6458 0.9829 0.7041 0.1474 -0.1351 -0.0427 149 MET B CE 3751 N N . GLU B 150 ? 0.6681 1.0625 0.9362 0.0533 -0.1150 -0.1147 150 GLU B N 3752 C CA . GLU B 150 ? 0.7202 1.0813 1.0247 0.0276 -0.0768 -0.1029 150 GLU B CA 3753 C C . GLU B 150 ? 0.7570 1.0444 1.0673 -0.0012 -0.0702 -0.1178 150 GLU B C 3754 O O . GLU B 150 ? 0.8245 1.0268 1.1086 -0.0069 -0.0352 -0.0917 150 GLU B O 3755 C CB . GLU B 150 ? 0.7413 1.2038 1.1463 0.0094 -0.0650 -0.1149 150 GLU B CB 3756 C CG . GLU B 150 ? 0.8241 1.2687 1.3011 -0.0312 -0.0118 -0.1050 150 GLU B CG 3757 C CD . GLU B 150 ? 0.8981 1.2606 1.3043 -0.0085 0.0452 -0.0531 150 GLU B CD 3758 O OE1 . GLU B 150 ? 0.9294 1.2440 1.2307 0.0372 0.0337 -0.0310 150 GLU B OE1 3759 O OE2 . GLU B 150 ? 0.9831 1.3206 1.4349 -0.0375 0.1045 -0.0350 150 GLU B OE2 3760 N N . SER B 151 ? 0.7412 1.0457 1.0674 -0.0112 -0.1013 -0.1582 151 SER B N 3761 C CA . SER B 151 ? 0.8131 1.0357 1.1387 -0.0318 -0.0964 -0.1778 151 SER B CA 3762 C C . SER B 151 ? 0.8471 0.9789 1.0958 0.0021 -0.0940 -0.1524 151 SER B C 3763 O O . SER B 151 ? 0.9396 0.9750 1.1692 -0.0020 -0.0782 -0.1473 151 SER B O 3764 C CB . SER B 151 ? 0.8280 1.0856 1.1736 -0.0414 -0.1324 -0.2347 151 SER B CB 3765 O OG . SER B 151 ? 0.8038 1.0733 1.0869 0.0000 -0.1521 -0.2373 151 SER B OG 3766 N N . VAL B 152 ? 0.7944 0.9560 1.0055 0.0365 -0.1120 -0.1374 152 VAL B N 3767 C CA . VAL B 152 ? 0.7924 0.8937 0.9566 0.0681 -0.1203 -0.1162 152 VAL B CA 3768 C C . VAL B 152 ? 0.8474 0.8702 0.9629 0.0765 -0.1025 -0.0793 152 VAL B C 3769 O O . VAL B 152 ? 0.8766 0.8111 0.9502 0.0953 -0.1035 -0.0675 152 VAL B O 3770 C CB . VAL B 152 ? 0.7231 0.8794 0.8812 0.0902 -0.1407 -0.1099 152 VAL B CB 3771 C CG1 . VAL B 152 ? 0.7414 0.8564 0.8851 0.1168 -0.1591 -0.0977 152 VAL B CG1 3772 C CG2 . VAL B 152 ? 0.7073 0.9271 0.8872 0.0898 -0.1449 -0.1385 152 VAL B CG2 3773 N N . ARG B 153 ? 0.8514 0.9002 0.9615 0.0710 -0.0840 -0.0608 153 ARG B N 3774 C CA . ARG B 153 ? 0.9488 0.9169 0.9932 0.0851 -0.0549 -0.0247 153 ARG B CA 3775 C C . ARG B 153 ? 1.0578 0.9616 1.1134 0.0583 -0.0067 -0.0142 153 ARG B C 3776 O O . ARG B 153 ? 1.1415 0.9403 1.1149 0.0784 0.0216 0.0201 153 ARG B O 3777 C CB . ARG B 153 ? 0.9334 0.9480 0.9707 0.0926 -0.0373 -0.0094 153 ARG B CB 3778 C CG . ARG B 153 ? 0.8720 0.9298 0.8928 0.1149 -0.0760 -0.0152 153 ARG B CG 3779 C CD . ARG B 153 ? 0.9094 0.9764 0.8979 0.1344 -0.0531 0.0032 153 ARG B CD 3780 N NE . ARG B 153 ? 0.8804 1.0191 0.8949 0.1412 -0.0761 -0.0072 153 ARG B NE 3781 C CZ . ARG B 153 ? 0.8456 1.0794 0.9278 0.1329 -0.0689 -0.0178 153 ARG B CZ 3782 N NH1 . ARG B 153 ? 0.8468 1.1342 1.0046 0.1082 -0.0420 -0.0260 153 ARG B NH1 3783 N NH2 . ARG B 153 ? 0.8521 1.1247 0.9282 0.1504 -0.0912 -0.0206 153 ARG B NH2 3784 N N . ASN B 154 ? 1.0920 1.0528 1.2438 0.0131 0.0027 -0.0441 154 ASN B N 3785 C CA . ASN B 154 ? 1.2197 1.1177 1.4099 -0.0284 0.0471 -0.0429 154 ASN B CA 3786 C C . ASN B 154 ? 1.3068 1.0666 1.4254 -0.0106 0.0463 -0.0342 154 ASN B C 3787 O O . ASN B 154 ? 1.4490 1.0947 1.5280 -0.0187 0.0963 -0.0018 154 ASN B O 3788 C CB . ASN B 154 ? 1.2428 1.2270 1.5515 -0.0793 0.0305 -0.0956 154 ASN B CB 3789 C CG . ASN B 154 ? 1.3133 1.4122 1.7293 -0.1142 0.0520 -0.1013 154 ASN B CG 3790 O OD1 . ASN B 154 ? 1.3093 1.4348 1.7117 -0.0952 0.0844 -0.0651 154 ASN B OD1 3791 N ND2 . ASN B 154 ? 1.4474 1.6170 1.9733 -0.1613 0.0301 -0.1520 154 ASN B ND2 3792 N N . GLY B 155 ? 1.2385 1.0074 1.3413 0.0178 -0.0049 -0.0606 155 GLY B N 3793 C CA . GLY B 155 ? 1.2962 0.9600 1.3642 0.0353 -0.0128 -0.0693 155 GLY B CA 3794 C C . GLY B 155 ? 1.2659 0.9566 1.4080 -0.0028 -0.0217 -0.1236 155 GLY B C 3795 O O . GLY B 155 ? 1.3569 0.9549 1.4776 0.0073 -0.0236 -0.1403 155 GLY B O 3796 N N . THR B 156 ? 1.1564 0.9689 1.3744 -0.0378 -0.0333 -0.1547 156 THR B N 3797 C CA . THR B 156 ? 1.1645 1.0031 1.4501 -0.0809 -0.0469 -0.2125 156 THR B CA 3798 C C . THR B 156 ? 1.0859 1.0037 1.3623 -0.0527 -0.0929 -0.2557 156 THR B C 3799 O O . THR B 156 ? 1.1141 1.0486 1.4188 -0.0750 -0.1150 -0.3108 156 THR B O 3800 C CB . THR B 156 ? 1.1477 1.0735 1.5325 -0.1380 -0.0323 -0.2208 156 THR B CB 3801 O OG1 . THR B 156 ? 1.2296 1.0658 1.6360 -0.1752 0.0273 -0.1859 156 THR B OG1 3802 C CG2 . THR B 156 ? 1.1642 1.1561 1.6258 -0.1772 -0.0725 -0.2929 156 THR B CG2 3803 N N . TYR B 157 ? 1.0188 0.9780 1.2523 -0.0041 -0.1055 -0.2323 157 TYR B N 3804 C CA . TYR B 157 ? 0.9707 1.0090 1.1931 0.0225 -0.1319 -0.2608 157 TYR B CA 3805 C C . TYR B 157 ? 1.0762 1.0681 1.2814 0.0300 -0.1415 -0.3137 157 TYR B C 3806 O O . TYR B 157 ? 1.1222 1.0354 1.2997 0.0604 -0.1321 -0.3128 157 TYR B O 3807 C CB . TYR B 157 ? 0.8919 0.9532 1.0865 0.0679 -0.1335 -0.2269 157 TYR B CB 3808 C CG . TYR B 157 ? 0.8426 0.9740 1.0266 0.0941 -0.1411 -0.2467 157 TYR B CG 3809 C CD1 . TYR B 157 ? 0.7916 1.0043 0.9701 0.0896 -0.1487 -0.2464 157 TYR B CD1 3810 C CD2 . TYR B 157 ? 0.8608 0.9722 1.0343 0.1302 -0.1338 -0.2619 157 TYR B CD2 3811 C CE1 . TYR B 157 ? 0.7744 1.0325 0.9218 0.1178 -0.1442 -0.2555 157 TYR B CE1 3812 C CE2 . TYR B 157 ? 0.8471 1.0186 1.0054 0.1562 -0.1238 -0.2735 157 TYR B CE2 3813 C CZ . TYR B 157 ? 0.7989 1.0365 0.9367 0.1484 -0.1267 -0.2678 157 TYR B CZ 3814 O OH . TYR B 157 ? 0.7995 1.0784 0.9025 0.1782 -0.1060 -0.2705 157 TYR B OH 3815 N N . ASP B 158 ? 1.1396 1.1783 1.3543 0.0103 -0.1650 -0.3631 158 ASP B N 3816 C CA . ASP B 158 ? 1.2815 1.2619 1.4644 0.0159 -0.1798 -0.4255 158 ASP B CA 3817 C C . ASP B 158 ? 1.3077 1.3122 1.4236 0.0787 -0.1748 -0.4327 158 ASP B C 3818 O O . ASP B 158 ? 1.2906 1.3715 1.3711 0.0973 -0.1877 -0.4449 158 ASP B O 3819 C CB . ASP B 158 ? 1.3140 1.3312 1.5290 -0.0278 -0.2187 -0.4847 158 ASP B CB 3820 C CG . ASP B 158 ? 1.4545 1.3686 1.6472 -0.0411 -0.2357 -0.5539 158 ASP B CG 3821 O OD1 . ASP B 158 ? 1.5190 1.3811 1.6293 0.0114 -0.2303 -0.5759 158 ASP B OD1 3822 O OD2 . ASP B 158 ? 1.5236 1.4052 1.7867 -0.1046 -0.2505 -0.5874 158 ASP B OD2 3823 N N . TYR B 159 ? 1.3577 1.2948 1.4570 0.1157 -0.1512 -0.4212 159 TYR B N 3824 C CA . TYR B 159 ? 1.3529 1.3237 1.4191 0.1759 -0.1309 -0.4182 159 TYR B CA 3825 C C . TYR B 159 ? 1.4979 1.4557 1.4891 0.2022 -0.1353 -0.4804 159 TYR B C 3826 O O . TYR B 159 ? 1.5068 1.5353 1.4564 0.2331 -0.1220 -0.4760 159 TYR B O 3827 C CB . TYR B 159 ? 1.3517 1.2639 1.4378 0.2143 -0.1114 -0.3953 159 TYR B CB 3828 C CG . TYR B 159 ? 1.3556 1.2994 1.4313 0.2788 -0.0835 -0.4042 159 TYR B CG 3829 C CD1 . TYR B 159 ? 1.2463 1.2932 1.3725 0.3006 -0.0643 -0.3626 159 TYR B CD1 3830 C CD2 . TYR B 159 ? 1.4761 1.3444 1.4980 0.3174 -0.0715 -0.4561 159 TYR B CD2 3831 C CE1 . TYR B 159 ? 1.2776 1.3685 1.4195 0.3560 -0.0266 -0.3675 159 TYR B CE1 3832 C CE2 . TYR B 159 ? 1.4995 1.4039 1.5168 0.3837 -0.0335 -0.4624 159 TYR B CE2 3833 C CZ . TYR B 159 ? 1.3954 1.4196 1.4821 0.4012 -0.0074 -0.4155 159 TYR B CZ 3834 O OH . TYR B 159 ? 1.4189 1.4929 1.5252 0.4633 0.0418 -0.4189 159 TYR B OH 3835 N N . PRO B 160 ? 1.6555 1.5088 1.6162 0.1917 -0.1521 -0.5389 160 PRO B N 3836 C CA . PRO B 160 ? 1.7960 1.6241 1.6623 0.2203 -0.1664 -0.6088 160 PRO B CA 3837 C C . PRO B 160 ? 1.7767 1.6921 1.6046 0.2072 -0.2023 -0.6271 160 PRO B C 3838 O O . PRO B 160 ? 1.8419 1.7705 1.5666 0.2580 -0.1976 -0.6537 160 PRO B O 3839 C CB . PRO B 160 ? 1.9264 1.6178 1.7863 0.1891 -0.1916 -0.6702 160 PRO B CB 3840 C CG . PRO B 160 ? 1.8963 1.5204 1.8188 0.1810 -0.1638 -0.6214 160 PRO B CG 3841 C CD . PRO B 160 ? 1.7153 1.4485 1.7075 0.1629 -0.1534 -0.5444 160 PRO B CD 3842 N N . GLN B 161 ? 1.6950 1.6676 1.5973 0.1491 -0.2339 -0.6096 161 GLN B N 3843 C CA . GLN B 161 ? 1.6820 1.7460 1.5585 0.1452 -0.2748 -0.6224 161 GLN B CA 3844 C C . GLN B 161 ? 1.6064 1.7401 1.4150 0.2010 -0.2412 -0.5728 161 GLN B C 3845 O O . GLN B 161 ? 1.6785 1.8517 1.4032 0.2292 -0.2673 -0.5909 161 GLN B O 3846 C CB . GLN B 161 ? 1.6080 1.7354 1.6003 0.0810 -0.3008 -0.6005 161 GLN B CB 3847 C CG . GLN B 161 ? 1.6373 1.8557 1.6236 0.0761 -0.3608 -0.6324 161 GLN B CG 3848 C CD . GLN B 161 ? 1.5483 1.8511 1.6626 0.0257 -0.3711 -0.5993 161 GLN B CD 3849 O OE1 . GLN B 161 ? 1.5327 1.8044 1.7483 -0.0292 -0.3517 -0.5883 161 GLN B OE1 3850 N NE2 . GLN B 161 ? 1.5120 1.9140 1.6134 0.0508 -0.3951 -0.5800 161 GLN B NE2 3851 N N . TYR B 162 ? 1.4733 1.6173 1.3189 0.2167 -0.1857 -0.5107 162 TYR B N 3852 C CA . TYR B 162 ? 1.4147 1.6110 1.2146 0.2612 -0.1408 -0.4639 162 TYR B CA 3853 C C . TYR B 162 ? 1.4309 1.5943 1.2169 0.3070 -0.0838 -0.4611 162 TYR B C 3854 O O . TYR B 162 ? 1.4430 1.6311 1.1676 0.3530 -0.0363 -0.4440 162 TYR B O 3855 C CB . TYR B 162 ? 1.2757 1.5332 1.1572 0.2347 -0.1288 -0.3938 162 TYR B CB 3856 C CG . TYR B 162 ? 1.2216 1.5158 1.1408 0.1934 -0.1757 -0.3913 162 TYR B CG 3857 C CD1 . TYR B 162 ? 1.2510 1.5950 1.1117 0.2094 -0.2007 -0.3909 162 TYR B CD1 3858 C CD2 . TYR B 162 ? 1.1564 1.4349 1.1673 0.1457 -0.1897 -0.3851 162 TYR B CD2 3859 C CE1 . TYR B 162 ? 1.1988 1.5928 1.1124 0.1798 -0.2421 -0.3889 162 TYR B CE1 3860 C CE2 . TYR B 162 ? 1.1093 1.4332 1.1698 0.1112 -0.2194 -0.3803 162 TYR B CE2 3861 C CZ . TYR B 162 ? 1.1232 1.5137 1.1461 0.1285 -0.2474 -0.3843 162 TYR B CZ 3862 O OH . TYR B 162 ? 1.0628 1.5135 1.1525 0.1019 -0.2759 -0.3809 162 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG B1154 HAS WRONG CHIRALITY AT ATOM C1' # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 GLN 2 2 2 GLN GLN A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 ILE 5 5 5 ILE ILE A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 TYR 7 7 7 TYR TYR A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 ASN 10 10 10 ASN ASN A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 SER 12 12 12 SER SER A . n A 1 13 THR 13 13 13 THR THR A . n A 1 14 GLU 14 14 14 GLU GLU A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASP 17 17 17 ASP ASP A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 ILE 19 19 19 ILE ILE A . n A 1 20 MET 20 20 20 MET MET A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 LYS 22 22 22 LYS LYS A . n A 1 23 ASN 23 23 23 ASN ASN A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 THR 25 25 25 THR THR A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 HIS 28 28 28 HIS HIS A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 GLN 30 30 30 GLN GLN A . n A 1 31 ASP 31 31 31 ASP ASP A . n A 1 32 ILE 32 32 32 ILE ILE A . n A 1 33 LEU 33 33 33 LEU LEU A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 LYS 35 35 35 LYS LYS A . n A 1 36 THR 36 36 36 THR THR A . n A 1 37 HIS 37 37 37 HIS HIS A . n A 1 38 ASN 38 38 38 ASN ASN A . n A 1 39 GLY 39 39 39 GLY GLY A . n A 1 40 LYS 40 40 40 LYS LYS A . n A 1 41 LEU 41 41 41 LEU LEU A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 ASP 43 43 43 ASP ASP A . n A 1 44 LEU 44 44 44 LEU LEU A . n A 1 45 ASP 45 45 45 ASP ASP A . n A 1 46 GLY 46 46 46 GLY GLY A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 LYS 48 48 48 LYS LYS A . n A 1 49 PRO 49 49 49 PRO PRO A . n A 1 50 LEU 50 50 50 LEU LEU A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 ARG 53 53 53 ARG ARG A . n A 1 54 ASP 54 54 54 ASP ASP A . n A 1 55 CYS 55 55 55 CYS CYS A . n A 1 56 SER 56 56 56 SER SER A . n A 1 57 VAL 57 57 57 VAL VAL A . n A 1 58 ALA 58 58 58 ALA ALA A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 TRP 60 60 60 TRP TRP A . n A 1 61 LEU 61 61 61 LEU LEU A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 GLY 63 63 63 GLY GLY A . n A 1 64 ASN 64 64 64 ASN ASN A . n A 1 65 PRO 65 65 65 PRO PRO A . n A 1 66 MET 66 66 66 MET MET A . n A 1 67 CYS 67 67 67 CYS CYS A . n A 1 68 ASP 68 68 68 ASP ASP A . n A 1 69 GLU 69 69 69 GLU GLU A . n A 1 70 PHE 70 70 70 PHE PHE A . n A 1 71 ILE 71 71 71 ILE ILE A . n A 1 72 ASN 72 72 72 ASN ASN A . n A 1 73 VAL 73 73 73 VAL VAL A . n A 1 74 PRO 74 74 74 PRO PRO A . n A 1 75 GLU 75 75 75 GLU GLU A . n A 1 76 TRP 76 76 76 TRP TRP A . n A 1 77 SER 77 77 77 SER SER A . n A 1 78 TYR 78 78 78 TYR TYR A . n A 1 79 ILE 79 79 79 ILE ILE A . n A 1 80 VAL 80 80 80 VAL VAL A . n A 1 81 GLU 81 81 81 GLU GLU A . n A 1 82 LYS 82 82 82 LYS LYS A . n A 1 83 ALA 83 83 83 ALA ALA A . n A 1 84 ASN 84 84 84 ASN ASN A . n A 1 85 PRO 85 85 85 PRO PRO A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 ASN 87 87 87 ASN ASN A . n A 1 88 ASP 88 88 88 ASP ASP A . n A 1 89 LEU 89 89 89 LEU LEU A . n A 1 90 CYS 90 90 90 CYS CYS A . n A 1 91 TYR 91 91 91 TYR TYR A . n A 1 92 PRO 92 92 92 PRO PRO A . n A 1 93 GLY 93 93 93 GLY GLY A . n A 1 94 ASP 94 94 94 ASP ASP A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 ASP 97 97 97 ASP ASP A . n A 1 98 TYR 98 98 98 TYR TYR A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 GLU 100 100 100 GLU GLU A . n A 1 101 LEU 101 101 101 LEU LEU A . n A 1 102 LYS 102 102 102 LYS LYS A . n A 1 103 HIS 103 103 103 HIS HIS A . n A 1 104 LEU 104 104 104 LEU LEU A . n A 1 105 LEU 105 105 105 LEU LEU A . n A 1 106 SER 106 106 106 SER SER A . n A 1 107 ARG 107 107 107 ARG ARG A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 HIS 110 110 110 HIS HIS A . n A 1 111 PHE 111 111 111 PHE PHE A . n A 1 112 GLU 112 112 112 GLU GLU A . n A 1 113 LYS 113 113 113 LYS LYS A . n A 1 114 ILE 114 114 114 ILE ILE A . n A 1 115 GLN 115 115 115 GLN GLN A . n A 1 116 ILE 116 116 116 ILE ILE A . n A 1 117 ILE 117 117 117 ILE ILE A . n A 1 118 PRO 118 118 118 PRO PRO A . n A 1 119 LYS 119 119 119 LYS LYS A . n A 1 120 SER 120 120 120 SER SER A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 TRP 122 122 122 TRP TRP A . n A 1 123 SER 123 123 123 SER SER A . n A 1 124 SER 124 124 124 SER SER A . n A 1 125 HIS 125 125 125 HIS HIS A . n A 1 126 GLU 126 126 126 GLU GLU A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 LEU 129 129 129 LEU LEU A . n A 1 130 GLY 130 130 130 GLY GLY A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 SER 133 133 133 SER SER A . n A 1 134 ALA 134 134 134 ALA ALA A . n A 1 135 CYS 135 135 135 CYS CYS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 GLN 138 138 138 GLN GLN A . n A 1 139 GLY 139 139 139 GLY GLY A . n A 1 140 LYS 140 140 140 LYS LYS A . n A 1 141 SER 141 141 141 SER SER A . n A 1 142 SER 142 142 142 SER SER A . n A 1 143 PHE 143 143 143 PHE PHE A . n A 1 144 PHE 144 144 144 PHE PHE A . n A 1 145 ARG 145 145 145 ARG ARG A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 VAL 147 147 147 VAL VAL A . n A 1 148 VAL 148 148 148 VAL VAL A . n A 1 149 TRP 149 149 149 TRP TRP A . n A 1 150 LEU 150 150 150 LEU LEU A . n A 1 151 ILE 151 151 151 ILE ILE A . n A 1 152 LYS 152 152 152 LYS LYS A . n A 1 153 LYS 153 153 153 LYS LYS A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 TYR 157 157 157 TYR TYR A . n A 1 158 PRO 158 158 158 PRO PRO A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 LYS 161 161 161 LYS LYS A . n A 1 162 ARG 162 162 162 ARG ARG A . n A 1 163 SER 163 163 163 SER SER A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ASN 165 165 165 ASN ASN A . n A 1 166 ASN 166 166 166 ASN ASN A . n A 1 167 THR 167 167 167 THR THR A . n A 1 168 ASN 168 168 168 ASN ASN A . n A 1 169 GLN 169 169 169 GLN GLN A . n A 1 170 GLU 170 170 170 GLU GLU A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 LEU 172 172 172 LEU LEU A . n A 1 173 LEU 173 173 173 LEU LEU A . n A 1 174 VAL 174 174 174 VAL VAL A . n A 1 175 LEU 175 175 175 LEU LEU A . n A 1 176 TRP 176 176 176 TRP TRP A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ILE 178 178 178 ILE ILE A . n A 1 179 HIS 179 179 179 HIS HIS A . n A 1 180 HIS 180 180 180 HIS HIS A . n A 1 181 PRO 181 181 181 PRO PRO A . n A 1 182 ASN 182 182 182 ASN ASN A . n A 1 183 ASP 183 183 183 ASP ASP A . n A 1 184 ALA 184 184 184 ALA ALA A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 GLU 186 186 186 GLU GLU A . n A 1 187 GLN 187 187 187 GLN GLN A . n A 1 188 THR 188 188 188 THR THR A . n A 1 189 LYS 189 189 189 LYS LYS A . n A 1 190 LEU 190 190 190 LEU LEU A . n A 1 191 TYR 191 191 191 TYR TYR A . n A 1 192 GLN 192 192 192 GLN GLN A . n A 1 193 ASN 193 193 193 ASN ASN A . n A 1 194 PRO 194 194 194 PRO PRO A . n A 1 195 THR 195 195 195 THR THR A . n A 1 196 THR 196 196 196 THR THR A . n A 1 197 TYR 197 197 197 TYR TYR A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 SER 199 199 199 SER SER A . n A 1 200 VAL 200 200 200 VAL VAL A . n A 1 201 GLY 201 201 201 GLY GLY A . n A 1 202 THR 202 202 202 THR THR A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 THR 204 204 204 THR THR A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 ASN 206 206 206 ASN ASN A . n A 1 207 GLN 207 207 207 GLN GLN A . n A 1 208 ARG 208 208 208 ARG ARG A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 VAL 210 210 210 VAL VAL A . n A 1 211 PRO 211 211 211 PRO PRO A . n A 1 212 ARG 212 212 212 ARG ARG A . n A 1 213 ILE 213 213 213 ILE ILE A . n A 1 214 ALA 214 214 214 ALA ALA A . n A 1 215 THR 215 215 215 THR THR A . n A 1 216 ARG 216 216 216 ARG ARG A . n A 1 217 SER 217 217 217 SER SER A . n A 1 218 LYS 218 218 218 LYS LYS A . n A 1 219 VAL 219 219 219 VAL VAL A . n A 1 220 ASN 220 220 220 ASN ASN A . n A 1 221 GLY 221 221 221 GLY GLY A . n A 1 222 GLN 222 222 222 GLN GLN A . n A 1 223 SER 223 223 223 SER SER A . n A 1 224 GLY 224 224 224 GLY GLY A . n A 1 225 ARG 225 225 225 ARG ARG A . n A 1 226 MET 226 226 226 MET MET A . n A 1 227 GLU 227 227 227 GLU GLU A . n A 1 228 PHE 228 228 228 PHE PHE A . n A 1 229 PHE 229 229 229 PHE PHE A . n A 1 230 TRP 230 230 230 TRP TRP A . n A 1 231 THR 231 231 231 THR THR A . n A 1 232 ILE 232 232 232 ILE ILE A . n A 1 233 LEU 233 233 233 LEU LEU A . n A 1 234 LYS 234 234 234 LYS LYS A . n A 1 235 PRO 235 235 235 PRO PRO A . n A 1 236 ASN 236 236 236 ASN ASN A . n A 1 237 ASP 237 237 237 ASP ASP A . n A 1 238 ALA 238 238 238 ALA ALA A . n A 1 239 ILE 239 239 239 ILE ILE A . n A 1 240 ASN 240 240 240 ASN ASN A . n A 1 241 PHE 241 241 241 PHE PHE A . n A 1 242 GLU 242 242 242 GLU GLU A . n A 1 243 SER 243 243 243 SER SER A . n A 1 244 ASN 244 244 244 ASN ASN A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 ASN 246 246 246 ASN ASN A . n A 1 247 PHE 247 247 247 PHE PHE A . n A 1 248 ILE 248 248 248 ILE ILE A . n A 1 249 ALA 249 249 249 ALA ALA A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 GLU 251 251 251 GLU GLU A . n A 1 252 TYR 252 252 252 TYR TYR A . n A 1 253 ALA 253 253 253 ALA ALA A . n A 1 254 TYR 254 254 254 TYR TYR A . n A 1 255 LYS 255 255 255 LYS LYS A . n A 1 256 ILE 256 256 256 ILE ILE A . n A 1 257 VAL 257 257 257 VAL VAL A . n A 1 258 LYS 258 258 258 LYS LYS A . n A 1 259 LYS 259 259 259 LYS LYS A . n A 1 260 GLY 260 260 260 GLY GLY A . n A 1 261 ASP 261 261 261 ASP ASP A . n A 1 262 SER 262 262 262 SER SER A . n A 1 263 THR 263 263 263 THR THR A . n A 1 264 ILE 264 264 264 ILE ILE A . n A 1 265 MET 265 265 265 MET MET A . n A 1 266 LYS 266 266 266 LYS LYS A . n A 1 267 SER 267 267 267 SER SER A . n A 1 268 GLU 268 268 268 GLU GLU A . n A 1 269 LEU 269 269 269 LEU LEU A . n A 1 270 GLU 270 270 270 GLU GLU A . n A 1 271 TYR 271 271 271 TYR TYR A . n A 1 272 GLY 272 272 272 GLY GLY A . n A 1 273 ASN 273 273 273 ASN ASN A . n A 1 274 CYS 274 274 274 CYS CYS A . n A 1 275 ASN 275 275 275 ASN ASN A . n A 1 276 THR 276 276 276 THR THR A . n A 1 277 LYS 277 277 277 LYS LYS A . n A 1 278 CYS 278 278 278 CYS CYS A . n A 1 279 GLN 279 279 279 GLN GLN A . n A 1 280 THR 280 280 280 THR THR A . n A 1 281 PRO 281 281 281 PRO PRO A . n A 1 282 MET 282 282 282 MET MET A . n A 1 283 GLY 283 283 283 GLY GLY A . n A 1 284 ALA 284 284 284 ALA ALA A . n A 1 285 ILE 285 285 285 ILE ILE A . n A 1 286 ASN 286 286 286 ASN ASN A . n A 1 287 SER 287 287 287 SER SER A . n A 1 288 SER 288 288 288 SER SER A . n A 1 289 MET 289 289 289 MET MET A . n A 1 290 PRO 290 290 290 PRO PRO A . n A 1 291 PHE 291 291 291 PHE PHE A . n A 1 292 HIS 292 292 292 HIS HIS A . n A 1 293 ASN 293 293 293 ASN ASN A . n A 1 294 ILE 294 294 294 ILE ILE A . n A 1 295 HIS 295 295 295 HIS HIS A . n A 1 296 PRO 296 296 296 PRO PRO A . n A 1 297 LEU 297 297 297 LEU LEU A . n A 1 298 THR 298 298 298 THR THR A . n A 1 299 ILE 299 299 299 ILE ILE A . n A 1 300 GLY 300 300 300 GLY GLY A . n A 1 301 GLU 301 301 301 GLU GLU A . n A 1 302 CYS 302 302 302 CYS CYS A . n A 1 303 PRO 303 303 303 PRO PRO A . n A 1 304 LYS 304 304 304 LYS LYS A . n A 1 305 TYR 305 305 305 TYR TYR A . n A 1 306 VAL 306 306 306 VAL VAL A . n A 1 307 LYS 307 307 307 LYS LYS A . n A 1 308 SER 308 308 308 SER SER A . n A 1 309 ASN 309 309 309 ASN ASN A . n A 1 310 ARG 310 310 310 ARG ARG A . n A 1 311 LEU 311 311 311 LEU LEU A . n A 1 312 VAL 312 312 312 VAL VAL A . n A 1 313 LEU 313 313 313 LEU LEU A . n A 1 314 ALA 314 314 314 ALA ALA A . n A 1 315 THR 315 315 315 THR THR A . n A 1 316 GLY 316 316 316 GLY GLY A . n A 1 317 LEU 317 317 317 LEU LEU A . n A 1 318 ARG 318 318 318 ARG ARG A . n A 1 319 ASN 319 319 319 ASN ASN A . n A 1 320 SER 320 320 320 SER SER A . n A 1 321 PRO 321 321 321 PRO PRO A . n A 1 322 GLN 322 322 ? ? ? A . n A 1 323 ARG 323 323 ? ? ? A . n A 1 324 GLU 324 324 ? ? ? A . n A 1 325 THR 325 325 ? ? ? A . n A 1 326 ARG 326 326 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 LEU 2 2 2 LEU LEU B . n B 2 3 PHE 3 3 3 PHE PHE B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 ALA 5 5 5 ALA ALA B . n B 2 6 ILE 6 6 6 ILE ILE B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 PHE 9 9 9 PHE PHE B . n B 2 10 ILE 10 10 10 ILE ILE B . n B 2 11 GLU 11 11 11 GLU GLU B . n B 2 12 GLY 12 12 12 GLY GLY B . n B 2 13 GLY 13 13 13 GLY GLY B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 VAL 18 18 18 VAL VAL B . n B 2 19 ASP 19 19 19 ASP ASP B . n B 2 20 GLY 20 20 20 GLY GLY B . n B 2 21 TRP 21 21 21 TRP TRP B . n B 2 22 TYR 22 22 22 TYR TYR B . n B 2 23 GLY 23 23 23 GLY GLY B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 HIS 25 25 25 HIS HIS B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 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 LYS 143 143 143 LYS LYS B . n B 2 144 CYS 144 144 144 CYS CYS B . n B 2 145 ASP 145 145 145 ASP ASP B . n B 2 146 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 156 156 156 THR THR B . n B 2 157 TYR 157 157 157 TYR TYR B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 TYR 159 159 159 TYR TYR B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 GLN 161 161 161 GLN GLN B . n B 2 162 TYR 162 162 162 TYR TYR 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 # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 1023 1023 NAG NAG A . D 3 NAG 1 1165 1165 NAG NAG A . E 4 SIA 1 1322 1322 SIA SIA A . F 5 GAL 2 1323 1323 GAL GAL A . G 3 NAG 1 1154 1154 NAG NAG B . H 6 EPE 1 1163 1163 EPE EPE B . I 7 HOH 1 2001 2001 HOH HOH A . I 7 HOH 2 2002 2002 HOH HOH A . I 7 HOH 3 2003 2003 HOH HOH A . I 7 HOH 4 2004 2004 HOH HOH A . I 7 HOH 5 2005 2005 HOH HOH A . I 7 HOH 6 2006 2006 HOH HOH A . I 7 HOH 7 2007 2007 HOH HOH A . I 7 HOH 8 2008 2008 HOH HOH A . I 7 HOH 9 2009 2009 HOH HOH A . I 7 HOH 10 2010 2010 HOH HOH A . I 7 HOH 11 2011 2011 HOH HOH A . I 7 HOH 12 2012 2012 HOH HOH A . I 7 HOH 13 2013 2013 HOH HOH A . I 7 HOH 14 2014 2014 HOH HOH A . I 7 HOH 15 2015 2015 HOH HOH A . I 7 HOH 16 2016 2016 HOH HOH A . I 7 HOH 17 2017 2017 HOH HOH A . I 7 HOH 18 2018 2018 HOH HOH A . I 7 HOH 19 2019 2019 HOH HOH A . I 7 HOH 20 2020 2020 HOH HOH A . I 7 HOH 21 2021 2021 HOH HOH A . I 7 HOH 22 2022 2022 HOH HOH A . I 7 HOH 23 2023 2023 HOH HOH A . I 7 HOH 24 2024 2024 HOH HOH A . I 7 HOH 25 2025 2025 HOH HOH A . I 7 HOH 26 2026 2026 HOH HOH A . I 7 HOH 27 2027 2027 HOH HOH A . I 7 HOH 28 2028 2028 HOH HOH A . I 7 HOH 29 2029 2029 HOH HOH A . I 7 HOH 30 2030 2030 HOH HOH A . I 7 HOH 31 2031 2031 HOH HOH A . I 7 HOH 32 2032 2032 HOH HOH A . I 7 HOH 33 2033 2033 HOH HOH A . I 7 HOH 34 2034 2034 HOH HOH A . I 7 HOH 35 2035 2035 HOH HOH A . I 7 HOH 36 2036 2036 HOH HOH A . I 7 HOH 37 2037 2037 HOH HOH A . I 7 HOH 38 2038 2038 HOH HOH A . I 7 HOH 39 2039 2039 HOH HOH A . I 7 HOH 40 2040 2040 HOH HOH A . I 7 HOH 41 2041 2041 HOH HOH A . I 7 HOH 42 2042 2042 HOH HOH A . I 7 HOH 43 2043 2043 HOH HOH A . I 7 HOH 44 2044 2044 HOH HOH A . I 7 HOH 45 2045 2045 HOH HOH A . I 7 HOH 46 2046 2046 HOH HOH A . I 7 HOH 47 2047 2047 HOH HOH A . I 7 HOH 48 2048 2048 HOH HOH A . I 7 HOH 49 2049 2049 HOH HOH A . I 7 HOH 50 2050 2050 HOH HOH A . I 7 HOH 51 2051 2051 HOH HOH A . I 7 HOH 52 2052 2052 HOH HOH A . I 7 HOH 53 2053 2053 HOH HOH A . I 7 HOH 54 2054 2054 HOH HOH A . I 7 HOH 55 2055 2055 HOH HOH A . I 7 HOH 56 2056 2056 HOH HOH A . I 7 HOH 57 2057 2057 HOH HOH A . I 7 HOH 58 2058 2058 HOH HOH A . I 7 HOH 59 2059 2059 HOH HOH A . I 7 HOH 60 2060 2060 HOH HOH A . I 7 HOH 61 2061 2061 HOH HOH A . I 7 HOH 62 2062 2062 HOH HOH A . I 7 HOH 63 2063 2063 HOH HOH A . I 7 HOH 64 2064 2064 HOH HOH A . I 7 HOH 65 2065 2065 HOH HOH A . I 7 HOH 66 2066 2066 HOH HOH A . I 7 HOH 67 2067 2067 HOH HOH A . I 7 HOH 68 2068 2068 HOH HOH A . I 7 HOH 69 2069 2069 HOH HOH A . I 7 HOH 70 2070 2070 HOH HOH A . I 7 HOH 71 2071 2071 HOH HOH A . I 7 HOH 72 2072 2072 HOH HOH A . I 7 HOH 73 2073 2073 HOH HOH A . I 7 HOH 74 2074 2074 HOH HOH A . I 7 HOH 75 2075 2075 HOH HOH A . I 7 HOH 76 2076 2076 HOH HOH A . I 7 HOH 77 2077 2077 HOH HOH A . I 7 HOH 78 2078 2078 HOH HOH A . I 7 HOH 79 2079 2079 HOH HOH A . I 7 HOH 80 2080 2080 HOH HOH A . I 7 HOH 81 2081 2081 HOH HOH A . I 7 HOH 82 2082 2082 HOH HOH A . I 7 HOH 83 2083 2083 HOH HOH A . I 7 HOH 84 2084 2084 HOH HOH A . I 7 HOH 85 2085 2085 HOH HOH A . I 7 HOH 86 2086 2086 HOH HOH A . I 7 HOH 87 2087 2087 HOH HOH A . I 7 HOH 88 2088 2088 HOH HOH A . I 7 HOH 89 2089 2089 HOH HOH A . I 7 HOH 90 2090 2090 HOH HOH A . I 7 HOH 91 2091 2091 HOH HOH A . I 7 HOH 92 2092 2092 HOH HOH A . I 7 HOH 93 2093 2093 HOH HOH A . I 7 HOH 94 2094 2094 HOH HOH A . I 7 HOH 95 2095 2095 HOH HOH A . I 7 HOH 96 2096 2096 HOH HOH A . I 7 HOH 97 2097 2097 HOH HOH A . I 7 HOH 98 2098 2098 HOH HOH A . I 7 HOH 99 2099 2099 HOH HOH A . I 7 HOH 100 2100 2100 HOH HOH A . I 7 HOH 101 2101 2101 HOH HOH A . I 7 HOH 102 2102 2102 HOH HOH A . I 7 HOH 103 2103 2103 HOH HOH A . I 7 HOH 104 2104 2104 HOH HOH A . I 7 HOH 105 2105 2105 HOH HOH A . I 7 HOH 106 2106 2106 HOH HOH A . I 7 HOH 107 2107 2107 HOH HOH A . I 7 HOH 108 2108 2108 HOH HOH A . I 7 HOH 109 2109 2109 HOH HOH A . I 7 HOH 110 2110 2110 HOH HOH A . I 7 HOH 111 2111 2111 HOH HOH A . I 7 HOH 112 2112 2112 HOH HOH A . I 7 HOH 113 2113 2113 HOH HOH A . I 7 HOH 114 2114 2114 HOH HOH A . I 7 HOH 115 2115 2115 HOH HOH A . I 7 HOH 116 2116 2116 HOH HOH A . I 7 HOH 117 2117 2117 HOH HOH A . I 7 HOH 118 2118 2118 HOH HOH A . I 7 HOH 119 2119 2119 HOH HOH A . I 7 HOH 120 2120 2120 HOH HOH A . I 7 HOH 121 2121 2121 HOH HOH A . I 7 HOH 122 2122 2122 HOH HOH A . J 7 HOH 1 2001 2001 HOH HOH B . J 7 HOH 2 2002 2002 HOH HOH B . J 7 HOH 3 2003 2003 HOH HOH B . J 7 HOH 4 2004 2004 HOH HOH B . J 7 HOH 5 2005 2005 HOH HOH B . J 7 HOH 6 2006 2006 HOH HOH B . J 7 HOH 7 2007 2007 HOH HOH B . J 7 HOH 8 2008 2008 HOH HOH B . J 7 HOH 9 2009 2009 HOH HOH B . J 7 HOH 10 2010 2010 HOH HOH B . J 7 HOH 11 2011 2011 HOH HOH B . J 7 HOH 12 2012 2012 HOH HOH B . J 7 HOH 13 2013 2013 HOH HOH B . J 7 HOH 14 2014 2014 HOH HOH B . J 7 HOH 15 2015 2015 HOH HOH B . J 7 HOH 16 2016 2016 HOH HOH B . J 7 HOH 17 2017 2017 HOH HOH B . J 7 HOH 18 2018 2018 HOH HOH B . J 7 HOH 19 2019 2019 HOH HOH B . J 7 HOH 20 2020 2020 HOH HOH B . J 7 HOH 21 2021 2021 HOH HOH B . J 7 HOH 22 2022 2022 HOH HOH B . J 7 HOH 23 2023 2023 HOH HOH B . J 7 HOH 24 2024 2024 HOH HOH B . J 7 HOH 25 2025 2025 HOH HOH B . J 7 HOH 26 2026 2026 HOH HOH B . J 7 HOH 27 2027 2027 HOH HOH B . J 7 HOH 28 2028 2028 HOH HOH B . J 7 HOH 29 2029 2029 HOH HOH B . J 7 HOH 30 2030 2030 HOH HOH B . J 7 HOH 31 2031 2031 HOH HOH B . J 7 HOH 32 2032 2032 HOH HOH B . J 7 HOH 33 2033 2033 HOH HOH B . J 7 HOH 34 2034 2034 HOH HOH B . J 7 HOH 35 2035 2035 HOH HOH B . J 7 HOH 36 2036 2036 HOH HOH B . J 7 HOH 37 2037 2037 HOH HOH B . J 7 HOH 38 2038 2038 HOH HOH B . J 7 HOH 39 2039 2039 HOH HOH B . J 7 HOH 40 2040 2040 HOH HOH B . J 7 HOH 41 2041 2041 HOH HOH B . J 7 HOH 42 2042 2042 HOH HOH B . J 7 HOH 43 2043 2043 HOH HOH B . J 7 HOH 44 2044 2044 HOH HOH B . J 7 HOH 45 2045 2045 HOH HOH B . J 7 HOH 46 2046 2046 HOH HOH B . J 7 HOH 47 2047 2047 HOH HOH B . J 7 HOH 48 2048 2048 HOH HOH B . J 7 HOH 49 2049 2049 HOH HOH B . J 7 HOH 50 2050 2050 HOH HOH B . J 7 HOH 51 2051 2051 HOH HOH B . J 7 HOH 52 2052 2052 HOH HOH B . J 7 HOH 53 2053 2053 HOH HOH B . J 7 HOH 54 2054 2054 HOH HOH B . J 7 HOH 55 2055 2055 HOH HOH B . J 7 HOH 56 2056 2056 HOH HOH B . J 7 HOH 57 2057 2057 HOH HOH B . J 7 HOH 58 2058 2058 HOH HOH B . J 7 HOH 59 2059 2059 HOH HOH B . J 7 HOH 60 2060 2060 HOH HOH B . J 7 HOH 61 2061 2061 HOH HOH B . J 7 HOH 62 2062 2062 HOH HOH B . J 7 HOH 63 2063 2063 HOH HOH B . J 7 HOH 64 2064 2064 HOH HOH B . J 7 HOH 65 2065 2065 HOH HOH B . J 7 HOH 66 2066 2066 HOH HOH B . J 7 HOH 67 2067 2067 HOH HOH B . J 7 HOH 68 2068 2068 HOH HOH B . J 7 HOH 69 2069 2069 HOH HOH B . J 7 HOH 70 2070 2070 HOH HOH B . J 7 HOH 71 2071 2071 HOH HOH B . J 7 HOH 72 2072 2072 HOH HOH B . J 7 HOH 73 2073 2073 HOH HOH B . J 7 HOH 74 2074 2074 HOH HOH B . J 7 HOH 75 2075 2075 HOH HOH B . J 7 HOH 76 2076 2076 HOH HOH B . J 7 HOH 77 2077 2077 HOH HOH B . J 7 HOH 78 2078 2078 HOH HOH B . J 7 HOH 79 2079 2079 HOH HOH B . J 7 HOH 80 2080 2080 HOH HOH B . J 7 HOH 81 2081 2081 HOH HOH B . J 7 HOH 82 2082 2082 HOH HOH B . J 7 HOH 83 2083 2083 HOH HOH B . J 7 HOH 84 2084 2084 HOH HOH B . J 7 HOH 85 2085 2085 HOH HOH B . J 7 HOH 86 2086 2086 HOH HOH B . J 7 HOH 87 2087 2087 HOH HOH B . J 7 HOH 88 2088 2088 HOH HOH B . J 7 HOH 89 2089 2089 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 23 A ASN 23 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 165 A ASN 165 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 154 B ASN 154 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 33330 ? 1 MORE -90.1 ? 1 'SSA (A^2)' 59180 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_545 -y,x-y-1,z -0.5000000000 -0.8660254038 0.0000000000 50.6690000000 0.8660254038 -0.5000000000 0.0000000000 -87.7612823687 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038 0.0000000000 101.3380000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 B HOH 2023 ? J HOH . 2 1 B HOH 2025 ? J HOH . 3 1 B HOH 2058 ? J HOH . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 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 34.3807 -14.0801 -18.8127 0.4095 0.4680 0.3302 0.1056 0.0305 -0.1242 0.4270 0.2167 4.7855 -0.0457 -0.3819 0.1270 0.0415 -0.2430 0.1068 0.1644 -0.0769 0.1442 -0.5871 -0.8134 0.0354 'X-RAY DIFFRACTION' 2 ? refined 32.2627 -21.5677 16.4463 0.7568 0.9080 0.2363 0.0261 0.1209 -0.1321 2.3353 3.2549 1.8207 0.1802 -0.0773 -0.9585 -0.0307 -0.4148 0.0690 0.8272 -0.1521 0.1352 -0.0569 -0.5459 0.1827 'X-RAY DIFFRACTION' 3 ? refined 35.5691 -14.7490 -26.9442 0.3651 0.3160 0.3722 0.1280 0.0746 -0.0753 1.2749 0.5821 12.5829 -0.1683 -1.5059 2.5396 0.1380 -0.3911 0.2266 0.0479 -0.1247 0.1445 -0.2014 -0.4945 -0.0132 'X-RAY DIFFRACTION' 4 ? refined 36.1940 -21.0566 -58.6731 0.0596 0.1732 0.2880 0.0201 -0.0274 -0.0906 3.1492 3.5950 9.6241 -1.6816 1.8064 -2.3312 -0.0347 0.0732 -0.0840 0.1610 -0.0937 0.2815 -0.1650 -1.0637 0.1283 'X-RAY DIFFRACTION' 5 ? refined 48.1596 -22.7221 -10.4025 0.3178 0.2620 0.2238 0.0163 0.0106 -0.0371 8.2666 4.4148 16.9038 0.7345 5.1243 0.6979 -0.1000 -0.1482 0.2744 -0.1467 -0.2171 0.4856 -0.5952 -0.9255 0.3171 'X-RAY DIFFRACTION' 6 ? refined 44.5280 -23.9884 -56.7188 0.0118 0.0416 0.2172 0.0149 0.0027 -0.0009 2.1630 1.2053 18.2112 -0.2045 2.3047 -0.9123 0.0160 0.2402 -0.0161 -0.0856 -0.1222 -0.0199 0.1323 0.4247 0.1061 'X-RAY DIFFRACTION' 7 ? refined 31.5088 -26.1711 -80.5988 0.3515 0.7010 0.5519 0.0608 -0.1784 -0.2448 8.2369 16.1201 11.9895 -5.5888 -1.1529 1.2281 0.2445 1.4227 -1.4591 -0.6736 -0.4286 0.8139 1.0068 -0.9082 0.1841 # 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 105 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 106 ? ? A 262 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 263 ? ? A 321 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 B 1 ? ? B 60 ? ? ? ? 'X-RAY DIFFRACTION' 5 5 B 61 ? ? B 84 ? ? ? ? 'X-RAY DIFFRACTION' 6 6 B 85 ? ? B 141 ? ? ? ? 'X-RAY DIFFRACTION' 7 7 B 142 ? ? B 163 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.7.0032 ? 1 MOSFLM 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4BGX _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 O A HOH 2033 ? ? O A HOH 2061 ? ? 1.96 2 1 O B HOH 2027 ? ? O B HOH 2028 ? ? 2.03 3 1 O B HOH 2004 ? ? O B HOH 2005 ? ? 2.05 4 1 OD1 A ASN 166 ? ? ND2 A ASN 168 ? ? 2.11 # 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 ARG A 53 ? ? 59.69 -111.16 2 1 ASP A 88 ? ? -104.80 -123.88 3 1 CYS A 135 ? ? -115.83 71.21 4 1 PHE A 144 ? ? -38.50 116.06 5 1 ASP A 171 ? ? -38.75 142.53 6 1 GLN A 192 ? ? 66.63 -67.54 7 1 ASN A 273 ? ? 57.58 82.11 8 1 CYS A 274 ? ? -170.97 148.69 9 1 ARG B 127 ? ? 47.30 -121.83 10 1 ASP B 145 ? ? -68.75 -177.88 # _pdbx_validate_peptide_omega.id 1 _pdbx_validate_peptide_omega.PDB_model_num 1 _pdbx_validate_peptide_omega.auth_comp_id_1 ASN _pdbx_validate_peptide_omega.auth_asym_id_1 A _pdbx_validate_peptide_omega.auth_seq_id_1 273 _pdbx_validate_peptide_omega.PDB_ins_code_1 ? _pdbx_validate_peptide_omega.label_alt_id_1 ? _pdbx_validate_peptide_omega.auth_comp_id_2 CYS _pdbx_validate_peptide_omega.auth_asym_id_2 A _pdbx_validate_peptide_omega.auth_seq_id_2 274 _pdbx_validate_peptide_omega.PDB_ins_code_2 ? _pdbx_validate_peptide_omega.label_alt_id_2 ? _pdbx_validate_peptide_omega.omega -139.21 # _pdbx_validate_chiral.id 1 _pdbx_validate_chiral.PDB_model_num 1 _pdbx_validate_chiral.auth_atom_id C1 _pdbx_validate_chiral.label_alt_id ? _pdbx_validate_chiral.auth_asym_id B _pdbx_validate_chiral.auth_comp_id NAG _pdbx_validate_chiral.auth_seq_id 1154 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # _pdbx_distant_solvent_atoms.id 1 _pdbx_distant_solvent_atoms.PDB_model_num 1 _pdbx_distant_solvent_atoms.auth_atom_id O _pdbx_distant_solvent_atoms.label_alt_id ? _pdbx_distant_solvent_atoms.auth_asym_id B _pdbx_distant_solvent_atoms.auth_comp_id HOH _pdbx_distant_solvent_atoms.auth_seq_id 2089 _pdbx_distant_solvent_atoms.PDB_ins_code ? _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 7.30 _pdbx_distant_solvent_atoms.neighbor_ligand_distance . # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLN 322 ? A GLN 322 2 1 Y 1 A ARG 323 ? A ARG 323 3 1 Y 1 A GLU 324 ? A GLU 324 4 1 Y 1 A THR 325 ? A THR 325 5 1 Y 1 A ARG 326 ? A ARG 326 6 1 Y 1 B SER 163 ? B SER 163 7 1 Y 1 B GLU 164 ? B GLU 164 8 1 Y 1 B GLU 165 ? B GLU 165 9 1 Y 1 B ALA 166 ? B 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 '4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID' EPE 7 water HOH #