data_4BGY # _entry.id 4BGY # _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 4BGY PDBE EBI-56329 WWPDB D_1290056329 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4BGW unspecified 'STRUCTURE OF H5 (VN1194) INFLUENZA HAEMAGGLUTININ' PDB 4BGX unspecified ;H5 (VN1194) INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'-SLN ; PDB 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 4BGY _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 4BGY _cell.length_a 101.403 _cell.length_b 101.403 _cell.length_c 449.997 _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 4BGY _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 7 ? ? ? ? 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 18.015 133 ? ? ? ? # 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 4BGY A 1 ? 326 ? Q6DQ34 17 ? 342 ? 1 326 2 2 4BGY B 1 ? 166 ? Q6DQ34 347 ? 512 ? 1 166 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 4BGY _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 4BGY _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.97 _exptl_crystal.density_percent_sol 69.03 _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 4BGY _reflns.observed_criterion_sigma_I 3.1 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40.90 _reflns.d_resolution_high 2.68 _reflns.number_obs 25658 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.10 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 15.30 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 9.0 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.68 _reflns_shell.d_res_low 2.82 _reflns_shell.percent_possible_all 99.8 _reflns_shell.Rmerge_I_obs 0.62 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.10 _reflns_shell.pdbx_redundancy 8.0 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4BGY _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 24350 _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 40.94 _refine.ls_d_res_high 2.68 _refine.ls_percent_reflns_obs 99.90 _refine.ls_R_factor_obs 0.20433 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.20207 _refine.ls_R_factor_R_free 0.24806 _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 1307 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.946 _refine.correlation_coeff_Fo_to_Fc_free 0.920 _refine.B_iso_mean 75.629 _refine.aniso_B[1][1] 2.32 _refine.aniso_B[2][2] 2.32 _refine.aniso_B[3][3] -7.53 _refine.aniso_B[1][2] 2.32 _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. STRONG ELECTRON DENSITY FEATURE FOR THE NAG MOIETY OF AVIAN RECEPTOR IS OBSERVED BUT NOT VERY WELL DEFINED AND SO THERE MAY BE OTHER CONFORMATIONS PRESENT AS WELL AS THE ONE WE HAVE BUILT. ; _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.401 _refine.pdbx_overall_ESU_R_Free 0.279 _refine.overall_SU_ML 0.215 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 20.203 _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 145 _refine_hist.number_atoms_solvent 133 _refine_hist.number_atoms_total 4137 _refine_hist.d_res_high 2.68 _refine_hist.d_res_low 40.94 # 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 0.007 0.019 ? 4107 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3765 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.143 1.979 ? 5579 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.716 3.003 ? 8652 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.653 5.000 ? 481 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 39.407 25.174 ? 201 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 17.655 15.000 ? 677 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 14.030 15.000 ? 17 'X-RAY DIFFRACTION' ? r_chiral_restr 0.064 0.200 ? 612 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.004 0.020 ? 4616 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 945 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.991 3.212 ? 1930 'X-RAY DIFFRACTION' ? r_mcbond_other 0.990 3.212 ? 1929 'X-RAY DIFFRACTION' ? r_mcangle_it 1.670 4.817 ? 2409 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 1.836 3.792 ? 2176 '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 2.680 _refine_ls_shell.d_res_low 2.750 _refine_ls_shell.number_reflns_R_work 1760 _refine_ls_shell.R_factor_R_work 0.285 _refine_ls_shell.percent_reflns_obs 99.73 _refine_ls_shell.R_factor_R_free 0.302 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 93 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4BGY _struct.title ;H5 (VN1194) Influenza Virus Haemagglutinin in Complex with Avian Receptor Analogue 3'-SLN ; _struct.pdbx_descriptor HEMAGGLUTININ _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4BGY _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 3 ? F N N 3 ? G N N 4 ? H N N 5 ? I N N 3 ? J N N 3 ? K N N 3 ? L N N 6 ? M N N 7 ? N 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 ? THR B 61 ? ASP B 37 THR B 61 1 ? 25 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 ? GLY B 155 ? ASP B 145 GLY B 155 1 ? 11 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 4 SG ? ? ? 1_555 B CYS 137 SG ? ? A CYS 4 B CYS 137 1_555 ? ? ? ? ? ? ? 2.072 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 274 SG ? ? A CYS 42 A CYS 274 1_555 ? ? ? ? ? ? ? 2.008 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 55 A CYS 67 1_555 ? ? ? ? ? ? ? 2.034 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 135 SG ? ? A CYS 90 A CYS 135 1_555 ? ? ? ? ? ? ? 2.034 ? disulf5 disulf ? ? A CYS 278 SG ? ? ? 1_555 A CYS 302 SG ? ? A CYS 278 A CYS 302 1_555 ? ? ? ? ? ? ? 2.047 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.024 ? covale1 covale ? ? A ASN 23 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 23 A NAG 1322 1_555 ? ? ? ? ? ? ? 1.444 ? covale2 covale ? ? A ASN 165 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 165 A NAG 1324 1_555 ? ? ? ? ? ? ? 1.442 ? covale3 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 1322 A NAG 1323 1_555 ? ? ? ? ? ? ? 1.440 ? covale4 covale ? ? E NAG . O4 ? ? ? 1_555 F NAG . C1 ? ? A NAG 1324 A NAG 1325 1_555 ? ? ? ? ? ? ? 1.433 ? covale5 covale ? ? H GAL . O3 ? ? ? 1_555 G SIA . C2 ? ? A GAL 1327 A SIA 1326 1_555 ? ? ? ? ? ? ? 1.416 ? covale6 covale ? ? H GAL . C1 ? ? ? 1_555 I NAG . O4 ? ? A GAL 1327 A NAG 1328 1_555 ? ? ? ? ? ? ? 1.418 ? covale7 covale ? ? B ASN 154 ND2 ? ? ? 1_555 J NAG . C1 ? ? B ASN 154 B NAG 1163 1_555 ? ? ? ? ? ? ? 1.436 ? covale8 covale ? ? J NAG . O4 ? ? ? 1_555 K NAG . C1 ? ? B NAG 1163 B NAG 1164 1_555 ? ? ? ? ? ? ? 1.441 ? # 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 ? ARG A 53 ? LEU A 50 ARG A 53 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 N LEU A 52 ? N LEU A 52 O VAL A 80 ? O 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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE EPE B 1165' AC2 Software ? ? ? ? 1 'Binding site for Poly-Saccharide residues NAG A1322 through NAG A1323 bound to ASN A 23' AC3 Software ? ? ? ? 2 'Binding site for Poly-Saccharide residues NAG A1324 through NAG A1325 bound to ASN A 165' AC4 Software ? ? ? ? 3 'Binding site for Poly-Saccharide residues NAG B1163 through NAG B1164 bound to ASN B 154' AC5 Software ? ? ? ? 11 'Binding site for Poly-Saccharide residues SIA A1326 through NAG A1328' # 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 4 TRP B 14 ? TRP B 14 . ? 1_555 ? 2 AC1 4 HIS B 25 ? HIS B 25 . ? 1_555 ? 3 AC1 4 TYR B 34 ? TYR B 34 . ? 1_555 ? 4 AC1 4 ASN B 135 ? ASN B 135 . ? 1_555 ? 5 AC2 1 ASN A 23 ? ASN A 23 . ? 1_555 ? 6 AC3 2 ASN A 165 ? ASN A 165 . ? 1_555 ? 7 AC3 2 ASN A 236 ? ASN A 236 . ? 1_555 ? 8 AC4 3 GLU B 147 ? GLU B 147 . ? 1_555 ? 9 AC4 3 GLU B 150 ? GLU B 150 . ? 1_555 ? 10 AC4 3 ASN B 154 ? ASN B 154 . ? 1_555 ? 11 AC5 11 TYR A 91 ? TYR A 91 . ? 1_555 ? 12 AC5 11 LEU A 129 ? LEU A 129 . ? 1_555 ? 13 AC5 11 VAL A 131 ? VAL A 131 . ? 1_555 ? 14 AC5 11 SER A 132 ? SER A 132 . ? 1_555 ? 15 AC5 11 SER A 133 ? SER A 133 . ? 1_555 ? 16 AC5 11 HIS A 179 ? HIS A 179 . ? 1_555 ? 17 AC5 11 ASN A 182 ? ASN A 182 . ? 1_555 ? 18 AC5 11 GLU A 186 ? GLU A 186 . ? 1_555 ? 19 AC5 11 LEU A 190 ? LEU A 190 . ? 1_555 ? 20 AC5 11 GLN A 222 ? GLN A 222 . ? 1_555 ? 21 AC5 11 HOH M . ? HOH A 2035 . ? 1_555 ? # _database_PDB_matrix.entry_id 4BGY _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 4BGY _atom_sites.fract_transf_matrix[1][1] 0.009862 _atom_sites.fract_transf_matrix[1][2] 0.005694 _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] 0.011387 _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] 0.002222 _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 ? -31.981 34.482 -8.430 1.00 58.56 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? -32.129 35.478 -7.328 1.00 59.79 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? -33.200 35.063 -6.343 1.00 57.76 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? -34.284 34.663 -6.746 1.00 55.37 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? -32.527 36.852 -7.869 1.00 60.49 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? -31.489 37.450 -8.766 1.00 61.11 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? -30.572 36.727 -9.206 1.00 60.59 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? -31.617 38.660 -9.034 1.00 63.91 ? 1 ASP A OD2 1 ATOM 9 N N . GLN A 1 2 ? -32.902 35.215 -5.054 1.00 59.51 ? 2 GLN A N 1 ATOM 10 C CA . GLN A 1 2 ? -33.852 34.871 -4.004 1.00 57.55 ? 2 GLN A CA 1 ATOM 11 C C . GLN A 1 2 ? -33.712 35.674 -2.729 1.00 56.04 ? 2 GLN A C 1 ATOM 12 O O . GLN A 1 2 ? -32.643 36.220 -2.434 1.00 57.17 ? 2 GLN A O 1 ATOM 13 C CB . GLN A 1 2 ? -33.733 33.396 -3.663 1.00 58.91 ? 2 GLN A CB 1 ATOM 14 C CG . GLN A 1 2 ? -32.411 32.939 -3.090 1.00 61.33 ? 2 GLN A CG 1 ATOM 15 C CD . GLN A 1 2 ? -32.481 31.476 -2.688 1.00 62.51 ? 2 GLN A CD 1 ATOM 16 O OE1 . GLN A 1 2 ? -32.224 31.138 -1.543 1.00 65.68 ? 2 GLN A OE1 1 ATOM 17 N NE2 . GLN A 1 2 ? -32.859 30.604 -3.628 1.00 62.05 ? 2 GLN A NE2 1 ATOM 18 N N . ILE A 1 3 ? -34.817 35.754 -1.992 1.00 52.87 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? -34.820 36.339 -0.664 1.00 52.05 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? -35.371 35.328 0.321 1.00 50.45 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? -36.323 34.623 0.013 1.00 49.81 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? -35.620 37.648 -0.603 1.00 51.89 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? -35.287 38.397 0.692 1.00 53.19 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? -37.115 37.394 -0.689 1.00 50.20 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? -35.569 39.882 0.636 1.00 53.75 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? -34.752 35.240 1.494 1.00 50.51 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? -35.146 34.258 2.491 1.00 49.31 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? -35.505 34.937 3.782 1.00 48.58 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? -34.970 35.996 4.103 1.00 50.19 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? -34.018 33.269 2.765 1.00 50.08 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? -33.366 32.511 1.270 1.00 52.44 ? 4 CYS A SG 1 ATOM 32 N N . ILE A 1 5 ? -36.414 34.321 4.524 1.00 46.40 ? 5 ILE A N 1 ATOM 33 C CA . ILE A 1 5 ? -36.699 34.756 5.869 1.00 45.92 ? 5 ILE A CA 1 ATOM 34 C C . ILE A 1 5 ? -36.047 33.770 6.808 1.00 45.88 ? 5 ILE A C 1 ATOM 35 O O . ILE A 1 5 ? -36.160 32.545 6.624 1.00 43.81 ? 5 ILE A O 1 ATOM 36 C CB . ILE A 1 5 ? -38.204 34.794 6.145 1.00 44.76 ? 5 ILE A CB 1 ATOM 37 C CG1 . ILE A 1 5 ? -38.901 35.681 5.122 1.00 46.14 ? 5 ILE A CG1 1 ATOM 38 C CG2 . ILE A 1 5 ? -38.488 35.276 7.552 1.00 44.04 ? 5 ILE A CG2 1 ATOM 39 C CD1 . ILE A 1 5 ? -38.354 37.082 5.061 1.00 48.70 ? 5 ILE A CD1 1 ATOM 40 N N . GLY A 1 6 ? -35.362 34.317 7.811 1.00 45.96 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? -34.723 33.509 8.831 1.00 46.48 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? -34.623 34.218 10.159 1.00 46.78 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? -35.129 35.332 10.328 1.00 48.84 ? 6 GLY A O 1 ATOM 44 N N . TYR A 1 7 ? -33.938 33.571 11.088 1.00 46.36 ? 7 TYR A N 1 ATOM 45 C CA . TYR A 1 7 ? -33.835 34.047 12.444 1.00 46.79 ? 7 TYR A CA 1 ATOM 46 C C . TYR A 1 7 ? -32.416 33.897 13.005 1.00 48.77 ? 7 TYR A C 1 ATOM 47 O O . TYR A 1 7 ? -31.583 33.146 12.478 1.00 47.11 ? 7 TYR A O 1 ATOM 48 C CB . TYR A 1 7 ? -34.832 33.286 13.323 1.00 45.48 ? 7 TYR A CB 1 ATOM 49 C CG . TYR A 1 7 ? -34.685 31.781 13.266 1.00 44.81 ? 7 TYR A CG 1 ATOM 50 C CD1 . TYR A 1 7 ? -35.289 31.042 12.266 1.00 44.25 ? 7 TYR A CD1 1 ATOM 51 C CD2 . TYR A 1 7 ? -33.953 31.105 14.208 1.00 45.12 ? 7 TYR A CD2 1 ATOM 52 C CE1 . TYR A 1 7 ? -35.163 29.667 12.214 1.00 43.75 ? 7 TYR A CE1 1 ATOM 53 C CE2 . TYR A 1 7 ? -33.818 29.734 14.160 1.00 45.92 ? 7 TYR A CE2 1 ATOM 54 C CZ . TYR A 1 7 ? -34.420 29.020 13.166 1.00 44.82 ? 7 TYR A CZ 1 ATOM 55 O OH . TYR A 1 7 ? -34.244 27.654 13.131 1.00 45.82 ? 7 TYR A OH 1 ATOM 56 N N . HIS A 1 8 ? -32.182 34.608 14.104 1.00 50.33 ? 8 HIS A N 1 ATOM 57 C CA . HIS A 1 8 ? -30.862 34.717 14.734 1.00 53.29 ? 8 HIS A CA 1 ATOM 58 C C . HIS A 1 8 ? -30.355 33.418 15.332 1.00 52.59 ? 8 HIS A C 1 ATOM 59 O O . HIS A 1 8 ? -31.108 32.659 15.890 1.00 52.19 ? 8 HIS A O 1 ATOM 60 C CB . HIS A 1 8 ? -30.917 35.773 15.840 1.00 53.42 ? 8 HIS A CB 1 ATOM 61 C CG . HIS A 1 8 ? -29.620 35.980 16.556 1.00 56.45 ? 8 HIS A CG 1 ATOM 62 N ND1 . HIS A 1 8 ? -28.468 36.391 15.916 1.00 58.48 ? 8 HIS A ND1 1 ATOM 63 C CD2 . HIS A 1 8 ? -29.299 35.863 17.866 1.00 56.92 ? 8 HIS A CD2 1 ATOM 64 C CE1 . HIS A 1 8 ? -27.492 36.506 16.801 1.00 59.42 ? 8 HIS A CE1 1 ATOM 65 N NE2 . HIS A 1 8 ? -27.971 36.195 17.992 1.00 58.16 ? 8 HIS A NE2 1 ATOM 66 N N . ALA A 1 9 ? -29.063 33.177 15.209 1.00 54.61 ? 9 ALA A N 1 ATOM 67 C CA . ALA A 1 9 ? -28.409 32.106 15.953 1.00 55.46 ? 9 ALA A CA 1 ATOM 68 C C . ALA A 1 9 ? -27.100 32.656 16.494 1.00 57.59 ? 9 ALA A C 1 ATOM 69 O O . ALA A 1 9 ? -26.636 33.701 16.060 1.00 60.57 ? 9 ALA A O 1 ATOM 70 C CB . ALA A 1 9 ? -28.165 30.899 15.066 1.00 55.43 ? 9 ALA A CB 1 ATOM 71 N N . ASN A 1 10 ? -26.514 31.962 17.455 1.00 57.96 ? 10 ASN A N 1 ATOM 72 C CA . ASN A 1 10 ? -25.287 32.421 18.075 1.00 60.21 ? 10 ASN A CA 1 ATOM 73 C C . ASN A 1 10 ? -24.608 31.264 18.788 1.00 62.53 ? 10 ASN A C 1 ATOM 74 O O . ASN A 1 10 ? -25.102 30.145 18.745 1.00 61.33 ? 10 ASN A O 1 ATOM 75 C CB . ASN A 1 10 ? -25.581 33.565 19.045 1.00 60.38 ? 10 ASN A CB 1 ATOM 76 C CG . ASN A 1 10 ? -26.210 33.091 20.339 1.00 59.86 ? 10 ASN A CG 1 ATOM 77 O OD1 . ASN A 1 10 ? -26.447 31.901 20.544 1.00 60.59 ? 10 ASN A OD1 1 ATOM 78 N ND2 . ASN A 1 10 ? -26.482 34.022 21.220 1.00 60.55 ? 10 ASN A ND2 1 ATOM 79 N N . ASN A 1 11 ? -23.494 31.533 19.462 1.00 67.13 ? 11 ASN A N 1 ATOM 80 C CA . ASN A 1 11 ? -22.700 30.467 20.077 1.00 70.91 ? 11 ASN A CA 1 ATOM 81 C C . ASN A 1 11 ? -23.082 30.187 21.546 1.00 69.71 ? 11 ASN A C 1 ATOM 82 O O . ASN A 1 11 ? -22.374 29.474 22.255 1.00 71.68 ? 11 ASN A O 1 ATOM 83 C CB . ASN A 1 11 ? -21.197 30.780 19.936 1.00 75.42 ? 11 ASN A CB 1 ATOM 84 C CG . ASN A 1 11 ? -20.772 31.998 20.740 1.00 79.44 ? 11 ASN A CG 1 ATOM 85 O OD1 . ASN A 1 11 ? -21.484 32.425 21.656 1.00 81.86 ? 11 ASN A OD1 1 ATOM 86 N ND2 . ASN A 1 11 ? -19.611 32.575 20.397 1.00 82.53 ? 11 ASN A ND2 1 ATOM 87 N N . SER A 1 12 ? -24.207 30.740 21.989 1.00 67.68 ? 12 SER A N 1 ATOM 88 C CA . SER A 1 12 ? -24.674 30.572 23.372 1.00 66.60 ? 12 SER A CA 1 ATOM 89 C C . SER A 1 12 ? -24.984 29.121 23.718 1.00 67.89 ? 12 SER A C 1 ATOM 90 O O . SER A 1 12 ? -25.561 28.407 22.905 1.00 67.27 ? 12 SER A O 1 ATOM 91 C CB . SER A 1 12 ? -25.942 31.399 23.622 1.00 62.15 ? 12 SER A CB 1 ATOM 92 O OG . SER A 1 12 ? -26.528 31.040 24.857 1.00 58.11 ? 12 SER A OG 1 ATOM 93 N N . THR A 1 13 ? -24.620 28.708 24.934 1.00 69.36 ? 13 THR A N 1 ATOM 94 C CA . THR A 1 13 ? -24.934 27.378 25.435 1.00 69.38 ? 13 THR A CA 1 ATOM 95 C C . THR A 1 13 ? -26.036 27.408 26.477 1.00 68.29 ? 13 THR A C 1 ATOM 96 O O . THR A 1 13 ? -26.413 26.356 26.991 1.00 68.58 ? 13 THR A O 1 ATOM 97 C CB . THR A 1 13 ? -23.725 26.745 26.125 1.00 72.95 ? 13 THR A CB 1 ATOM 98 O OG1 . THR A 1 13 ? -23.137 27.710 27.008 1.00 76.27 ? 13 THR A OG1 1 ATOM 99 C CG2 . THR A 1 13 ? -22.701 26.275 25.106 1.00 74.71 ? 13 THR A CG2 1 ATOM 100 N N . GLU A 1 14 ? -26.551 28.591 26.803 1.00 67.05 ? 14 GLU A N 1 ATOM 101 C CA . GLU A 1 14 ? -27.539 28.698 27.872 1.00 66.60 ? 14 GLU A CA 1 ATOM 102 C C . GLU A 1 14 ? -28.794 27.883 27.575 1.00 62.22 ? 14 GLU A C 1 ATOM 103 O O . GLU A 1 14 ? -29.281 27.869 26.447 1.00 61.29 ? 14 GLU A O 1 ATOM 104 C CB . GLU A 1 14 ? -27.936 30.149 28.115 1.00 69.98 ? 14 GLU A CB 1 ATOM 105 C CG . GLU A 1 14 ? -26.824 31.008 28.669 1.00 75.75 ? 14 GLU A CG 1 ATOM 106 C CD . GLU A 1 14 ? -27.226 31.731 29.942 1.00 81.26 ? 14 GLU A CD 1 ATOM 107 O OE1 . GLU A 1 14 ? -27.313 31.072 31.005 1.00 81.53 ? 14 GLU A OE1 1 ATOM 108 O OE2 . GLU A 1 14 ? -27.472 32.958 29.875 1.00 88.54 ? 14 GLU A OE2 1 ATOM 109 N N . GLN A 1 15 ? -29.314 27.219 28.603 1.00 59.37 ? 15 GLN A N 1 ATOM 110 C CA . GLN A 1 15 ? -30.441 26.313 28.458 1.00 56.19 ? 15 GLN A CA 1 ATOM 111 C C . GLN A 1 15 ? -31.557 26.727 29.390 1.00 53.03 ? 15 GLN A C 1 ATOM 112 O O . GLN A 1 15 ? -31.307 27.227 30.473 1.00 53.64 ? 15 GLN A O 1 ATOM 113 C CB . GLN A 1 15 ? -30.014 24.890 28.792 1.00 58.03 ? 15 GLN A CB 1 ATOM 114 C CG . GLN A 1 15 ? -28.984 24.317 27.836 1.00 61.01 ? 15 GLN A CG 1 ATOM 115 C CD . GLN A 1 15 ? -28.441 22.975 28.274 1.00 62.98 ? 15 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 15 ? -28.026 22.162 27.450 1.00 64.70 ? 15 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 15 ? -28.434 22.739 29.573 1.00 64.29 ? 15 GLN A NE2 1 ATOM 118 N N . VAL A 1 16 ? -32.790 26.519 28.960 1.00 49.76 ? 16 VAL A N 1 ATOM 119 C CA . VAL A 1 16 ? -33.954 26.798 29.787 1.00 47.23 ? 16 VAL A CA 1 ATOM 120 C C . VAL A 1 16 ? -34.842 25.597 29.730 1.00 45.98 ? 16 VAL A C 1 ATOM 121 O O . VAL A 1 16 ? -34.785 24.845 28.766 1.00 45.62 ? 16 VAL A O 1 ATOM 122 C CB . VAL A 1 16 ? -34.742 28.022 29.296 1.00 45.58 ? 16 VAL A CB 1 ATOM 123 C CG1 . VAL A 1 16 ? -33.810 29.209 29.201 1.00 46.97 ? 16 VAL A CG1 1 ATOM 124 C CG2 . VAL A 1 16 ? -35.408 27.760 27.948 1.00 44.80 ? 16 VAL A CG2 1 ATOM 125 N N . ASP A 1 17 ? -35.654 25.419 30.764 1.00 45.88 ? 17 ASP A N 1 ATOM 126 C CA . ASP A 1 17 ? -36.652 24.366 30.773 1.00 46.37 ? 17 ASP A CA 1 ATOM 127 C C . ASP A 1 17 ? -38.026 24.903 30.420 1.00 44.24 ? 17 ASP A C 1 ATOM 128 O O . ASP A 1 17 ? -38.362 26.026 30.742 1.00 42.95 ? 17 ASP A O 1 ATOM 129 C CB . ASP A 1 17 ? -36.748 23.744 32.152 1.00 48.21 ? 17 ASP A CB 1 ATOM 130 C CG . ASP A 1 17 ? -35.525 22.967 32.525 1.00 50.45 ? 17 ASP A CG 1 ATOM 131 O OD1 . ASP A 1 17 ? -34.963 22.272 31.646 1.00 52.22 ? 17 ASP A OD1 1 ATOM 132 O OD2 . ASP A 1 17 ? -35.153 23.031 33.718 1.00 52.13 ? 17 ASP A OD2 1 ATOM 133 N N . THR A 1 18 ? -38.808 24.058 29.767 1.00 45.06 ? 18 THR A N 1 ATOM 134 C CA . THR A 1 18 ? -40.230 24.273 29.532 1.00 43.74 ? 18 THR A CA 1 ATOM 135 C C . THR A 1 18 ? -40.961 23.035 30.039 1.00 45.47 ? 18 THR A C 1 ATOM 136 O O . THR A 1 18 ? -40.351 22.107 30.558 1.00 47.51 ? 18 THR A O 1 ATOM 137 C CB . THR A 1 18 ? -40.525 24.412 28.026 1.00 42.06 ? 18 THR A CB 1 ATOM 138 O OG1 . THR A 1 18 ? -40.368 23.139 27.398 1.00 42.36 ? 18 THR A OG1 1 ATOM 139 C CG2 . THR A 1 18 ? -39.589 25.383 27.388 1.00 41.89 ? 18 THR A CG2 1 ATOM 140 N N . ILE A 1 19 ? -42.267 23.001 29.839 1.00 47.31 ? 19 ILE A N 1 ATOM 141 C CA . ILE A 1 19 ? -43.113 21.922 30.336 1.00 48.24 ? 19 ILE A CA 1 ATOM 142 C C . ILE A 1 19 ? -42.910 20.627 29.554 1.00 48.88 ? 19 ILE A C 1 ATOM 143 O O . ILE A 1 19 ? -42.935 19.538 30.122 1.00 48.38 ? 19 ILE A O 1 ATOM 144 C CB . ILE A 1 19 ? -44.593 22.340 30.211 1.00 49.32 ? 19 ILE A CB 1 ATOM 145 C CG1 . ILE A 1 19 ? -44.878 23.553 31.086 1.00 50.23 ? 19 ILE A CG1 1 ATOM 146 C CG2 . ILE A 1 19 ? -45.536 21.200 30.571 1.00 50.03 ? 19 ILE A CG2 1 ATOM 147 C CD1 . ILE A 1 19 ? -44.982 23.222 32.561 1.00 51.74 ? 19 ILE A CD1 1 ATOM 148 N N . MET A 1 20 ? -42.751 20.751 28.242 1.00 49.35 ? 20 MET A N 1 ATOM 149 C CA . MET A 1 20 ? -42.626 19.583 27.380 1.00 50.76 ? 20 MET A CA 1 ATOM 150 C C . MET A 1 20 ? -41.186 19.187 27.093 1.00 52.31 ? 20 MET A C 1 ATOM 151 O O . MET A 1 20 ? -40.931 18.078 26.604 1.00 51.68 ? 20 MET A O 1 ATOM 152 C CB . MET A 1 20 ? -43.297 19.847 26.050 1.00 50.95 ? 20 MET A CB 1 ATOM 153 C CG . MET A 1 20 ? -44.788 19.987 26.146 1.00 51.54 ? 20 MET A CG 1 ATOM 154 S SD . MET A 1 20 ? -45.462 20.107 24.501 1.00 53.47 ? 20 MET A SD 1 ATOM 155 C CE . MET A 1 20 ? -47.052 20.823 24.930 1.00 55.83 ? 20 MET A CE 1 ATOM 156 N N . GLU A 1 21 ? -40.252 20.092 27.358 1.00 52.21 ? 21 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? -38.874 19.845 27.005 1.00 54.56 ? 21 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? -37.922 20.535 27.961 1.00 56.05 ? 21 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? -38.114 21.717 28.324 1.00 53.08 ? 21 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? -38.613 20.313 25.583 1.00 54.93 ? 21 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? -37.313 19.791 25.010 1.00 57.79 ? 21 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? -37.113 20.200 23.563 1.00 59.37 ? 21 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? -37.984 20.928 23.024 1.00 58.80 ? 21 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? -36.080 19.800 22.974 1.00 59.06 ? 21 GLU A OE2 1 ATOM 165 N N . LYS A 1 22 ? -36.890 19.787 28.351 1.00 56.07 ? 22 LYS A N 1 ATOM 166 C CA . LYS A 1 22 ? -35.913 20.264 29.304 1.00 57.61 ? 22 LYS A CA 1 ATOM 167 C C . LYS A 1 22 ? -34.591 20.545 28.624 1.00 56.90 ? 22 LYS A C 1 ATOM 168 O O . LYS A 1 22 ? -34.300 20.003 27.569 1.00 56.67 ? 22 LYS A O 1 ATOM 169 C CB . LYS A 1 22 ? -35.753 19.233 30.411 1.00 61.31 ? 22 LYS A CB 1 ATOM 170 C CG . LYS A 1 22 ? -36.967 19.159 31.325 1.00 63.55 ? 22 LYS A CG 1 ATOM 171 C CD . LYS A 1 22 ? -36.803 18.075 32.386 1.00 67.64 ? 22 LYS A CD 1 ATOM 172 C CE . LYS A 1 22 ? -37.082 18.621 33.785 1.00 69.32 ? 22 LYS A CE 1 ATOM 173 N NZ . LYS A 1 22 ? -36.851 17.642 34.885 1.00 69.78 ? 22 LYS A NZ 1 ATOM 174 N N . ASN A 1 23 ? -33.795 21.413 29.223 1.00 58.79 ? 23 ASN A N 1 ATOM 175 C CA . ASN A 1 23 ? -32.460 21.700 28.708 1.00 62.37 ? 23 ASN A CA 1 ATOM 176 C C . ASN A 1 23 ? -32.448 22.178 27.255 1.00 58.53 ? 23 ASN A C 1 ATOM 177 O O . ASN A 1 23 ? -31.598 21.770 26.477 1.00 59.06 ? 23 ASN A O 1 ATOM 178 C CB . ASN A 1 23 ? -31.552 20.459 28.860 1.00 68.42 ? 23 ASN A CB 1 ATOM 179 C CG . ASN A 1 23 ? -31.245 20.131 30.303 1.00 74.79 ? 23 ASN A CG 1 ATOM 180 O OD1 . ASN A 1 23 ? -31.426 20.967 31.187 1.00 73.91 ? 23 ASN A OD1 1 ATOM 181 N ND2 . ASN A 1 23 ? -30.764 18.914 30.554 1.00 85.23 ? 23 ASN A ND2 1 ATOM 182 N N . VAL A 1 24 ? -33.386 23.050 26.900 1.00 55.82 ? 24 VAL A N 1 ATOM 183 C CA . VAL A 1 24 ? -33.423 23.673 25.563 1.00 53.48 ? 24 VAL A CA 1 ATOM 184 C C . VAL A 1 24 ? -32.415 24.822 25.450 1.00 52.66 ? 24 VAL A C 1 ATOM 185 O O . VAL A 1 24 ? -32.445 25.749 26.242 1.00 53.47 ? 24 VAL A O 1 ATOM 186 C CB . VAL A 1 24 ? -34.824 24.232 25.248 1.00 51.09 ? 24 VAL A CB 1 ATOM 187 C CG1 . VAL A 1 24 ? -34.832 24.951 23.907 1.00 50.42 ? 24 VAL A CG1 1 ATOM 188 C CG2 . VAL A 1 24 ? -35.844 23.106 25.253 1.00 50.80 ? 24 VAL A CG2 1 ATOM 189 N N . THR A 1 25 ? -31.537 24.768 24.456 1.00 51.94 ? 25 THR A N 1 ATOM 190 C CA . THR A 1 25 ? -30.513 25.793 24.287 1.00 52.27 ? 25 THR A CA 1 ATOM 191 C C . THR A 1 25 ? -31.078 27.015 23.589 1.00 50.91 ? 25 THR A C 1 ATOM 192 O O . THR A 1 25 ? -31.674 26.887 22.524 1.00 51.58 ? 25 THR A O 1 ATOM 193 C CB . THR A 1 25 ? -29.344 25.279 23.437 1.00 53.87 ? 25 THR A CB 1 ATOM 194 O OG1 . THR A 1 25 ? -28.921 24.008 23.933 1.00 56.37 ? 25 THR A OG1 1 ATOM 195 C CG2 . THR A 1 25 ? -28.182 26.246 23.498 1.00 55.28 ? 25 THR A CG2 1 ATOM 196 N N . VAL A 1 26 ? -30.865 28.195 24.163 1.00 50.51 ? 26 VAL A N 1 ATOM 197 C CA . VAL A 1 26 ? -31.438 29.427 23.627 1.00 49.28 ? 26 VAL A CA 1 ATOM 198 C C . VAL A 1 26 ? -30.356 30.443 23.375 1.00 50.82 ? 26 VAL A C 1 ATOM 199 O O . VAL A 1 26 ? -29.304 30.376 23.976 1.00 53.01 ? 26 VAL A O 1 ATOM 200 C CB . VAL A 1 26 ? -32.477 30.042 24.574 1.00 47.76 ? 26 VAL A CB 1 ATOM 201 C CG1 . VAL A 1 26 ? -33.695 29.145 24.650 1.00 46.92 ? 26 VAL A CG1 1 ATOM 202 C CG2 . VAL A 1 26 ? -31.897 30.266 25.955 1.00 48.70 ? 26 VAL A CG2 1 ATOM 203 N N . THR A 1 27 ? -30.632 31.391 22.492 1.00 50.92 ? 27 THR A N 1 ATOM 204 C CA . THR A 1 27 ? -29.660 32.410 22.126 1.00 52.10 ? 27 THR A CA 1 ATOM 205 C C . THR A 1 27 ? -29.416 33.365 23.277 1.00 52.96 ? 27 THR A C 1 ATOM 206 O O . THR A 1 27 ? -28.279 33.780 23.507 1.00 55.80 ? 27 THR A O 1 ATOM 207 C CB . THR A 1 27 ? -30.130 33.215 20.914 1.00 51.95 ? 27 THR A CB 1 ATOM 208 O OG1 . THR A 1 27 ? -31.376 33.853 21.214 1.00 50.46 ? 27 THR A OG1 1 ATOM 209 C CG2 . THR A 1 27 ? -30.315 32.304 19.716 1.00 51.79 ? 27 THR A CG2 1 ATOM 210 N N . HIS A 1 28 ? -30.482 33.714 23.991 1.00 51.77 ? 28 HIS A N 1 ATOM 211 C CA . HIS A 1 28 ? -30.398 34.613 25.141 1.00 52.74 ? 28 HIS A CA 1 ATOM 212 C C . HIS A 1 28 ? -31.314 34.173 26.259 1.00 52.60 ? 28 HIS A C 1 ATOM 213 O O . HIS A 1 28 ? -32.363 33.585 26.020 1.00 52.39 ? 28 HIS A O 1 ATOM 214 C CB . HIS A 1 28 ? -30.771 36.032 24.737 1.00 52.61 ? 28 HIS A CB 1 ATOM 215 C CG . HIS A 1 28 ? -30.008 36.532 23.559 1.00 54.25 ? 28 HIS A CG 1 ATOM 216 N ND1 . HIS A 1 28 ? -30.290 36.127 22.273 1.00 53.66 ? 28 HIS A ND1 1 ATOM 217 C CD2 . HIS A 1 28 ? -28.954 37.375 23.470 1.00 56.10 ? 28 HIS A CD2 1 ATOM 218 C CE1 . HIS A 1 28 ? -29.448 36.708 21.441 1.00 54.98 ? 28 HIS A CE1 1 ATOM 219 N NE2 . HIS A 1 28 ? -28.627 37.469 22.142 1.00 56.73 ? 28 HIS A NE2 1 ATOM 220 N N . ALA A 1 29 ? -30.926 34.483 27.485 1.00 54.64 ? 29 ALA A N 1 ATOM 221 C CA . ALA A 1 29 ? -31.696 34.082 28.658 1.00 55.01 ? 29 ALA A CA 1 ATOM 222 C C . ALA A 1 29 ? -31.373 35.005 29.807 1.00 56.06 ? 29 ALA A C 1 ATOM 223 O O . ALA A 1 29 ? -30.464 35.837 29.714 1.00 58.70 ? 29 ALA A O 1 ATOM 224 C CB . ALA A 1 29 ? -31.384 32.642 29.042 1.00 55.55 ? 29 ALA A CB 1 ATOM 225 N N . GLN A 1 30 ? -32.121 34.868 30.888 1.00 54.80 ? 30 GLN A N 1 ATOM 226 C CA . GLN A 1 30 ? -31.910 35.716 32.040 1.00 56.69 ? 30 GLN A CA 1 ATOM 227 C C . GLN A 1 30 ? -32.090 34.942 33.330 1.00 56.31 ? 30 GLN A C 1 ATOM 228 O O . GLN A 1 30 ? -33.187 34.475 33.652 1.00 54.51 ? 30 GLN A O 1 ATOM 229 C CB . GLN A 1 30 ? -32.852 36.912 32.013 1.00 57.31 ? 30 GLN A CB 1 ATOM 230 C CG . GLN A 1 30 ? -32.402 38.000 32.964 1.00 59.46 ? 30 GLN A CG 1 ATOM 231 C CD . GLN A 1 30 ? -33.318 39.202 32.964 1.00 60.15 ? 30 GLN A CD 1 ATOM 232 O OE1 . GLN A 1 30 ? -33.703 39.710 31.912 1.00 61.49 ? 30 GLN A OE1 1 ATOM 233 N NE2 . GLN A 1 30 ? -33.657 39.678 34.151 1.00 60.53 ? 30 GLN A NE2 1 ATOM 234 N N . ASP A 1 31 ? -30.996 34.808 34.065 1.00 57.31 ? 31 ASP A N 1 ATOM 235 C CA . ASP A 1 31 ? -31.028 34.197 35.375 1.00 57.46 ? 31 ASP A CA 1 ATOM 236 C C . ASP A 1 31 ? -31.633 35.206 36.368 1.00 56.74 ? 31 ASP A C 1 ATOM 237 O O . ASP A 1 31 ? -31.270 36.382 36.369 1.00 58.15 ? 31 ASP A O 1 ATOM 238 C CB . ASP A 1 31 ? -29.612 33.796 35.774 1.00 59.20 ? 31 ASP A CB 1 ATOM 239 C CG . ASP A 1 31 ? -29.572 32.997 37.045 1.00 60.02 ? 31 ASP A CG 1 ATOM 240 O OD1 . ASP A 1 31 ? -30.649 32.699 37.589 1.00 60.00 ? 31 ASP A OD1 1 ATOM 241 O OD2 . ASP A 1 31 ? -28.463 32.657 37.504 1.00 62.45 ? 31 ASP A OD2 1 ATOM 242 N N . ILE A 1 32 ? -32.577 34.753 37.185 1.00 54.23 ? 32 ILE A N 1 ATOM 243 C CA . ILE A 1 32 ? -33.258 35.637 38.134 1.00 54.01 ? 32 ILE A CA 1 ATOM 244 C C . ILE A 1 32 ? -33.138 35.161 39.586 1.00 54.12 ? 32 ILE A C 1 ATOM 245 O O . ILE A 1 32 ? -33.777 35.708 40.480 1.00 53.78 ? 32 ILE A O 1 ATOM 246 C CB . ILE A 1 32 ? -34.749 35.790 37.772 1.00 52.93 ? 32 ILE A CB 1 ATOM 247 C CG1 . ILE A 1 32 ? -35.405 34.420 37.584 1.00 52.13 ? 32 ILE A CG1 1 ATOM 248 C CG2 . ILE A 1 32 ? -34.897 36.617 36.513 1.00 52.72 ? 32 ILE A CG2 1 ATOM 249 C CD1 . ILE A 1 32 ? -36.908 34.464 37.692 1.00 51.67 ? 32 ILE A CD1 1 ATOM 250 N N . LEU A 1 33 ? -32.314 34.146 39.813 1.00 54.17 ? 33 LEU A N 1 ATOM 251 C CA . LEU A 1 33 ? -32.115 33.577 41.129 1.00 54.24 ? 33 LEU A CA 1 ATOM 252 C C . LEU A 1 33 ? -30.699 33.860 41.609 1.00 57.20 ? 33 LEU A C 1 ATOM 253 O O . LEU A 1 33 ? -29.715 33.524 40.938 1.00 58.72 ? 33 LEU A O 1 ATOM 254 C CB . LEU A 1 33 ? -32.336 32.068 41.077 1.00 53.12 ? 33 LEU A CB 1 ATOM 255 C CG . LEU A 1 33 ? -32.232 31.296 42.392 1.00 52.73 ? 33 LEU A CG 1 ATOM 256 C CD1 . LEU A 1 33 ? -33.348 31.725 43.337 1.00 51.39 ? 33 LEU A CD1 1 ATOM 257 C CD2 . LEU A 1 33 ? -32.277 29.792 42.147 1.00 52.49 ? 33 LEU A CD2 1 ATOM 258 N N . GLU A 1 34 ? -30.596 34.459 42.787 1.00 58.30 ? 34 GLU A N 1 ATOM 259 C CA . GLU A 1 34 ? -29.303 34.731 43.378 1.00 60.63 ? 34 GLU A CA 1 ATOM 260 C C . GLU A 1 34 ? -28.838 33.521 44.181 1.00 60.85 ? 34 GLU A C 1 ATOM 261 O O . GLU A 1 34 ? -29.457 33.157 45.174 1.00 60.60 ? 34 GLU A O 1 ATOM 262 C CB . GLU A 1 34 ? -29.381 35.970 44.264 1.00 61.41 ? 34 GLU A CB 1 ATOM 263 C CG . GLU A 1 34 ? -28.059 36.339 44.904 1.00 63.90 ? 34 GLU A CG 1 ATOM 264 C CD . GLU A 1 34 ? -26.966 36.485 43.879 1.00 65.83 ? 34 GLU A CD 1 ATOM 265 O OE1 . GLU A 1 34 ? -26.922 37.536 43.204 1.00 67.88 ? 34 GLU A OE1 1 ATOM 266 O OE2 . GLU A 1 34 ? -26.183 35.526 43.720 1.00 66.03 ? 34 GLU A OE2 1 ATOM 267 N N . LYS A 1 35 ? -27.742 32.909 43.750 1.00 62.08 ? 35 LYS A N 1 ATOM 268 C CA . LYS A 1 35 ? -27.239 31.691 44.379 1.00 63.01 ? 35 LYS A CA 1 ATOM 269 C C . LYS A 1 35 ? -26.055 31.915 45.328 1.00 65.85 ? 35 LYS A C 1 ATOM 270 O O . LYS A 1 35 ? -25.636 30.969 45.991 1.00 66.97 ? 35 LYS A O 1 ATOM 271 C CB . LYS A 1 35 ? -26.863 30.655 43.306 1.00 62.59 ? 35 LYS A CB 1 ATOM 272 C CG . LYS A 1 35 ? -28.038 29.831 42.787 1.00 60.19 ? 35 LYS A CG 1 ATOM 273 C CD . LYS A 1 35 ? -27.644 28.949 41.605 1.00 60.38 ? 35 LYS A CD 1 ATOM 274 C CE . LYS A 1 35 ? -28.128 29.497 40.263 1.00 59.70 ? 35 LYS A CE 1 ATOM 275 N NZ . LYS A 1 35 ? -27.811 30.933 39.997 1.00 59.39 ? 35 LYS A NZ 1 ATOM 276 N N . THR A 1 36 ? -25.529 33.141 45.417 1.00 67.10 ? 36 THR A N 1 ATOM 277 C CA . THR A 1 36 ? -24.332 33.377 46.235 1.00 70.98 ? 36 THR A CA 1 ATOM 278 C C . THR A 1 36 ? -24.503 34.410 47.339 1.00 72.03 ? 36 THR A C 1 ATOM 279 O O . THR A 1 36 ? -25.313 35.326 47.234 1.00 69.65 ? 36 THR A O 1 ATOM 280 C CB . THR A 1 36 ? -23.118 33.820 45.389 1.00 73.22 ? 36 THR A CB 1 ATOM 281 O OG1 . THR A 1 36 ? -23.412 35.062 44.740 1.00 72.88 ? 36 THR A OG1 1 ATOM 282 C CG2 . THR A 1 36 ? -22.767 32.773 44.357 1.00 73.40 ? 36 THR A CG2 1 ATOM 283 N N . HIS A 1 37 ? -23.686 34.243 48.380 1.00 74.65 ? 37 HIS A N 1 ATOM 284 C CA . HIS A 1 37 ? -23.616 35.153 49.520 1.00 76.09 ? 37 HIS A CA 1 ATOM 285 C C . HIS A 1 37 ? -22.151 35.285 49.928 1.00 80.88 ? 37 HIS A C 1 ATOM 286 O O . HIS A 1 37 ? -21.330 34.431 49.583 1.00 82.51 ? 37 HIS A O 1 ATOM 287 C CB . HIS A 1 37 ? -24.441 34.605 50.688 1.00 74.21 ? 37 HIS A CB 1 ATOM 288 C CG . HIS A 1 37 ? -23.977 33.269 51.184 1.00 74.47 ? 37 HIS A CG 1 ATOM 289 N ND1 . HIS A 1 37 ? -23.215 33.123 52.321 1.00 75.78 ? 37 HIS A ND1 1 ATOM 290 C CD2 . HIS A 1 37 ? -24.165 32.019 50.695 1.00 73.77 ? 37 HIS A CD2 1 ATOM 291 C CE1 . HIS A 1 37 ? -22.957 31.842 52.518 1.00 76.29 ? 37 HIS A CE1 1 ATOM 292 N NE2 . HIS A 1 37 ? -23.521 31.151 51.544 1.00 74.95 ? 37 HIS A NE2 1 ATOM 293 N N . ASN A 1 38 ? -21.814 36.340 50.663 1.00 83.32 ? 38 ASN A N 1 ATOM 294 C CA . ASN A 1 38 ? -20.413 36.565 51.048 1.00 86.70 ? 38 ASN A CA 1 ATOM 295 C C . ASN A 1 38 ? -19.917 35.631 52.167 1.00 87.75 ? 38 ASN A C 1 ATOM 296 O O . ASN A 1 38 ? -18.716 35.441 52.329 1.00 91.64 ? 38 ASN A O 1 ATOM 297 C CB . ASN A 1 38 ? -20.163 38.036 51.421 1.00 87.40 ? 38 ASN A CB 1 ATOM 298 C CG . ASN A 1 38 ? -20.713 38.399 52.777 1.00 85.81 ? 38 ASN A CG 1 ATOM 299 O OD1 . ASN A 1 38 ? -20.921 37.539 53.629 1.00 86.58 ? 38 ASN A OD1 1 ATOM 300 N ND2 . ASN A 1 38 ? -20.931 39.683 52.990 1.00 85.17 ? 38 ASN A ND2 1 ATOM 301 N N . GLY A 1 39 ? -20.840 35.076 52.946 1.00 85.83 ? 39 GLY A N 1 ATOM 302 C CA . GLY A 1 39 ? -20.503 34.096 53.990 1.00 84.66 ? 39 GLY A CA 1 ATOM 303 C C . GLY A 1 39 ? -20.264 34.704 55.360 1.00 84.85 ? 39 GLY A C 1 ATOM 304 O O . GLY A 1 39 ? -19.754 34.026 56.261 1.00 83.85 ? 39 GLY A O 1 ATOM 305 N N . LYS A 1 40 ? -20.645 35.974 55.517 1.00 84.55 ? 40 LYS A N 1 ATOM 306 C CA . LYS A 1 40 ? -20.316 36.760 56.695 1.00 86.46 ? 40 LYS A CA 1 ATOM 307 C C . LYS A 1 40 ? -21.497 37.533 57.247 1.00 85.85 ? 40 LYS A C 1 ATOM 308 O O . LYS A 1 40 ? -22.332 38.030 56.494 1.00 86.13 ? 40 LYS A O 1 ATOM 309 C CB . LYS A 1 40 ? -19.229 37.762 56.341 1.00 89.40 ? 40 LYS A CB 1 ATOM 310 C CG . LYS A 1 40 ? -17.889 37.122 56.038 1.00 92.48 ? 40 LYS A CG 1 ATOM 311 C CD . LYS A 1 40 ? -17.032 37.999 55.148 1.00 94.74 ? 40 LYS A CD 1 ATOM 312 C CE . LYS A 1 40 ? -15.711 37.311 54.855 1.00 97.83 ? 40 LYS A CE 1 ATOM 313 N NZ . LYS A 1 40 ? -14.919 38.058 53.846 1.00 100.47 ? 40 LYS A NZ 1 ATOM 314 N N . LEU A 1 41 ? -21.548 37.641 58.571 1.00 87.26 ? 41 LEU A N 1 ATOM 315 C CA . LEU A 1 41 ? -22.432 38.589 59.232 1.00 86.32 ? 41 LEU A CA 1 ATOM 316 C C . LEU A 1 41 ? -21.842 39.981 59.013 1.00 86.42 ? 41 LEU A C 1 ATOM 317 O O . LEU A 1 41 ? -20.631 40.161 59.106 1.00 88.25 ? 41 LEU A O 1 ATOM 318 C CB . LEU A 1 41 ? -22.540 38.272 60.718 1.00 88.59 ? 41 LEU A CB 1 ATOM 319 C CG . LEU A 1 41 ? -23.035 36.858 61.050 1.00 88.77 ? 41 LEU A CG 1 ATOM 320 C CD1 . LEU A 1 41 ? -22.835 36.569 62.529 1.00 90.62 ? 41 LEU A CD1 1 ATOM 321 C CD2 . LEU A 1 41 ? -24.493 36.659 60.666 1.00 85.70 ? 41 LEU A CD2 1 ATOM 322 N N . CYS A 1 42 ? -22.706 40.948 58.728 1.00 83.94 ? 42 CYS A N 1 ATOM 323 C CA . CYS A 1 42 ? -22.300 42.242 58.205 1.00 85.12 ? 42 CYS A CA 1 ATOM 324 C C . CYS A 1 42 ? -23.109 43.350 58.835 1.00 83.13 ? 42 CYS A C 1 ATOM 325 O O . CYS A 1 42 ? -24.206 43.110 59.310 1.00 80.69 ? 42 CYS A O 1 ATOM 326 C CB . CYS A 1 42 ? -22.550 42.261 56.691 1.00 85.64 ? 42 CYS A CB 1 ATOM 327 S SG . CYS A 1 42 ? -21.348 41.309 55.755 1.00 87.24 ? 42 CYS A SG 1 ATOM 328 N N . ASP A 1 43 ? -22.584 44.574 58.807 1.00 84.93 ? 43 ASP A N 1 ATOM 329 C CA . ASP A 1 43 ? -23.371 45.752 59.187 1.00 84.52 ? 43 ASP A CA 1 ATOM 330 C C . ASP A 1 43 ? -24.545 45.880 58.231 1.00 81.65 ? 43 ASP A C 1 ATOM 331 O O . ASP A 1 43 ? -24.428 45.513 57.067 1.00 81.04 ? 43 ASP A O 1 ATOM 332 C CB . ASP A 1 43 ? -22.523 47.033 59.140 1.00 87.67 ? 43 ASP A CB 1 ATOM 333 C CG . ASP A 1 43 ? -21.404 47.046 60.181 1.00 89.93 ? 43 ASP A CG 1 ATOM 334 O OD1 . ASP A 1 43 ? -21.426 46.208 61.099 1.00 88.92 ? 43 ASP A OD1 1 ATOM 335 O OD2 . ASP A 1 43 ? -20.496 47.899 60.084 1.00 92.06 ? 43 ASP A OD2 1 ATOM 336 N N . LEU A 1 44 ? -25.668 46.401 58.710 1.00 81.35 ? 44 LEU A N 1 ATOM 337 C CA . LEU A 1 44 ? -26.866 46.525 57.875 1.00 81.09 ? 44 LEU A CA 1 ATOM 338 C C . LEU A 1 44 ? -27.250 47.972 57.633 1.00 83.90 ? 44 LEU A C 1 ATOM 339 O O . LEU A 1 44 ? -27.797 48.638 58.512 1.00 82.83 ? 44 LEU A O 1 ATOM 340 C CB . LEU A 1 44 ? -28.054 45.796 58.502 1.00 78.88 ? 44 LEU A CB 1 ATOM 341 C CG . LEU A 1 44 ? -29.332 45.800 57.647 1.00 77.52 ? 44 LEU A CG 1 ATOM 342 C CD1 . LEU A 1 44 ? -29.182 44.898 56.423 1.00 76.44 ? 44 LEU A CD1 1 ATOM 343 C CD2 . LEU A 1 44 ? -30.545 45.392 58.470 1.00 75.45 ? 44 LEU A CD2 1 ATOM 344 N N . ASP A 1 45 ? -27.014 48.438 56.411 1.00 88.35 ? 45 ASP A N 1 ATOM 345 C CA . ASP A 1 45 ? -27.184 49.850 56.087 1.00 92.22 ? 45 ASP A CA 1 ATOM 346 C C . ASP A 1 45 ? -26.161 50.663 56.878 1.00 93.11 ? 45 ASP A C 1 ATOM 347 O O . ASP A 1 45 ? -26.458 51.767 57.341 1.00 93.31 ? 45 ASP A O 1 ATOM 348 C CB . ASP A 1 45 ? -28.610 50.314 56.428 1.00 93.78 ? 45 ASP A CB 1 ATOM 349 C CG . ASP A 1 45 ? -29.090 51.425 55.526 1.00 96.68 ? 45 ASP A CG 1 ATOM 350 O OD1 . ASP A 1 45 ? -29.121 51.188 54.303 1.00 98.48 ? 45 ASP A OD1 1 ATOM 351 O OD2 . ASP A 1 45 ? -29.438 52.519 56.031 1.00 98.64 ? 45 ASP A OD2 1 ATOM 352 N N . GLY A 1 46 ? -24.970 50.087 57.059 1.00 93.13 ? 46 GLY A N 1 ATOM 353 C CA . GLY A 1 46 ? -23.896 50.713 57.848 1.00 95.02 ? 46 GLY A CA 1 ATOM 354 C C . GLY A 1 46 ? -24.016 50.554 59.356 1.00 94.12 ? 46 GLY A C 1 ATOM 355 O O . GLY A 1 46 ? -23.077 50.881 60.086 1.00 94.64 ? 46 GLY A O 1 ATOM 356 N N . VAL A 1 47 ? -25.163 50.049 59.824 1.00 91.05 ? 47 VAL A N 1 ATOM 357 C CA . VAL A 1 47 ? -25.466 49.948 61.258 1.00 89.67 ? 47 VAL A CA 1 ATOM 358 C C . VAL A 1 47 ? -25.122 48.559 61.792 1.00 88.44 ? 47 VAL A C 1 ATOM 359 O O . VAL A 1 47 ? -25.661 47.558 61.328 1.00 87.34 ? 47 VAL A O 1 ATOM 360 C CB . VAL A 1 47 ? -26.955 50.209 61.530 1.00 86.47 ? 47 VAL A CB 1 ATOM 361 C CG1 . VAL A 1 47 ? -27.258 50.038 63.012 1.00 86.33 ? 47 VAL A CG1 1 ATOM 362 C CG2 . VAL A 1 47 ? -27.354 51.594 61.042 1.00 87.27 ? 47 VAL A CG2 1 ATOM 363 N N . LYS A 1 48 ? -24.246 48.507 62.786 1.00 90.11 ? 48 LYS A N 1 ATOM 364 C CA . LYS A 1 48 ? -23.710 47.238 63.263 1.00 90.09 ? 48 LYS A CA 1 ATOM 365 C C . LYS A 1 48 ? -24.794 46.403 63.934 1.00 87.24 ? 48 LYS A C 1 ATOM 366 O O . LYS A 1 48 ? -25.634 46.944 64.660 1.00 85.92 ? 48 LYS A O 1 ATOM 367 C CB . LYS A 1 48 ? -22.556 47.461 64.255 1.00 93.79 ? 48 LYS A CB 1 ATOM 368 C CG . LYS A 1 48 ? -21.396 46.486 64.091 1.00 95.88 ? 48 LYS A CG 1 ATOM 369 C CD . LYS A 1 48 ? -20.644 46.227 65.385 1.00 97.68 ? 48 LYS A CD 1 ATOM 370 C CE . LYS A 1 48 ? -19.640 45.099 65.198 1.00 99.01 ? 48 LYS A CE 1 ATOM 371 N NZ . LYS A 1 48 ? -18.914 44.806 66.463 1.00 101.84 ? 48 LYS A NZ 1 ATOM 372 N N . PRO A 1 49 ? -24.781 45.079 63.690 1.00 86.02 ? 49 PRO A N 1 ATOM 373 C CA . PRO A 1 49 ? -25.631 44.193 64.466 1.00 83.19 ? 49 PRO A CA 1 ATOM 374 C C . PRO A 1 49 ? -25.112 44.085 65.883 1.00 83.34 ? 49 PRO A C 1 ATOM 375 O O . PRO A 1 49 ? -23.907 44.181 66.104 1.00 84.97 ? 49 PRO A O 1 ATOM 376 C CB . PRO A 1 49 ? -25.451 42.843 63.774 1.00 81.39 ? 49 PRO A CB 1 ATOM 377 C CG . PRO A 1 49 ? -24.070 42.896 63.243 1.00 83.98 ? 49 PRO A CG 1 ATOM 378 C CD . PRO A 1 49 ? -23.935 44.313 62.754 1.00 85.99 ? 49 PRO A CD 1 ATOM 379 N N . LEU A 1 50 ? -26.014 43.876 66.827 1.00 80.99 ? 50 LEU A N 1 ATOM 380 C CA . LEU A 1 50 ? -25.617 43.511 68.168 1.00 81.22 ? 50 LEU A CA 1 ATOM 381 C C . LEU A 1 50 ? -25.267 42.037 68.167 1.00 80.10 ? 50 LEU A C 1 ATOM 382 O O . LEU A 1 50 ? -26.145 41.202 68.034 1.00 78.76 ? 50 LEU A O 1 ATOM 383 C CB . LEU A 1 50 ? -26.754 43.776 69.148 1.00 80.05 ? 50 LEU A CB 1 ATOM 384 C CG . LEU A 1 50 ? -26.674 43.034 70.482 1.00 80.03 ? 50 LEU A CG 1 ATOM 385 C CD1 . LEU A 1 50 ? -25.257 43.029 71.049 1.00 82.65 ? 50 LEU A CD1 1 ATOM 386 C CD2 . LEU A 1 50 ? -27.662 43.642 71.468 1.00 79.53 ? 50 LEU A CD2 1 ATOM 387 N N . ILE A 1 51 ? -23.993 41.707 68.314 1.00 82.17 ? 51 ILE A N 1 ATOM 388 C CA . ILE A 1 51 ? -23.589 40.303 68.332 1.00 83.17 ? 51 ILE A CA 1 ATOM 389 C C . ILE A 1 51 ? -23.298 39.847 69.757 1.00 84.48 ? 51 ILE A C 1 ATOM 390 O O . ILE A 1 51 ? -22.322 40.278 70.372 1.00 88.68 ? 51 ILE A O 1 ATOM 391 C CB . ILE A 1 51 ? -22.386 40.052 67.399 1.00 85.26 ? 51 ILE A CB 1 ATOM 392 C CG1 . ILE A 1 51 ? -22.776 40.474 65.976 1.00 85.19 ? 51 ILE A CG1 1 ATOM 393 C CG2 . ILE A 1 51 ? -21.940 38.593 67.457 1.00 85.29 ? 51 ILE A CG2 1 ATOM 394 C CD1 . ILE A 1 51 ? -21.972 39.829 64.870 1.00 86.49 ? 51 ILE A CD1 1 ATOM 395 N N . LEU A 1 52 ? -24.142 38.958 70.266 1.00 82.45 ? 52 LEU A N 1 ATOM 396 C CA . LEU A 1 52 ? -24.001 38.474 71.632 1.00 83.01 ? 52 LEU A CA 1 ATOM 397 C C . LEU A 1 52 ? -22.827 37.521 71.784 1.00 85.93 ? 52 LEU A C 1 ATOM 398 O O . LEU A 1 52 ? -22.297 37.386 72.870 1.00 87.50 ? 52 LEU A O 1 ATOM 399 C CB . LEU A 1 52 ? -25.296 37.810 72.101 1.00 79.85 ? 52 LEU A CB 1 ATOM 400 C CG . LEU A 1 52 ? -26.498 38.759 72.027 1.00 77.99 ? 52 LEU A CG 1 ATOM 401 C CD1 . LEU A 1 52 ? -27.761 38.111 72.568 1.00 75.68 ? 52 LEU A CD1 1 ATOM 402 C CD2 . LEU A 1 52 ? -26.195 40.043 72.780 1.00 79.63 ? 52 LEU A CD2 1 ATOM 403 N N . ARG A 1 53 ? -22.406 36.878 70.701 1.00 87.48 ? 53 ARG A N 1 ATOM 404 C CA . ARG A 1 53 ? -21.311 35.935 70.778 1.00 90.85 ? 53 ARG A CA 1 ATOM 405 C C . ARG A 1 53 ? -21.762 34.793 71.703 1.00 91.06 ? 53 ARG A C 1 ATOM 406 O O . ARG A 1 53 ? -22.853 34.257 71.512 1.00 91.62 ? 53 ARG A O 1 ATOM 407 C CB . ARG A 1 53 ? -20.047 36.652 71.268 1.00 95.56 ? 53 ARG A CB 1 ATOM 408 C CG . ARG A 1 53 ? -18.756 36.163 70.621 1.00 99.69 ? 53 ARG A CG 1 ATOM 409 C CD . ARG A 1 53 ? -17.545 36.373 71.522 1.00 104.04 ? 53 ARG A CD 1 ATOM 410 N NE . ARG A 1 53 ? -16.432 37.009 70.815 1.00 107.40 ? 53 ARG A NE 1 ATOM 411 C CZ . ARG A 1 53 ? -16.286 38.326 70.641 1.00 108.62 ? 53 ARG A CZ 1 ATOM 412 N NH1 . ARG A 1 53 ? -17.182 39.193 71.112 1.00 107.30 ? 53 ARG A NH1 1 ATOM 413 N NH2 . ARG A 1 53 ? -15.229 38.784 69.982 1.00 111.30 ? 53 ARG A NH2 1 ATOM 414 N N . ASP A 1 54 ? -20.960 34.425 72.699 1.00 93.25 ? 54 ASP A N 1 ATOM 415 C CA . ASP A 1 54 ? -21.328 33.346 73.616 1.00 92.67 ? 54 ASP A CA 1 ATOM 416 C C . ASP A 1 54 ? -22.468 33.691 74.580 1.00 90.49 ? 54 ASP A C 1 ATOM 417 O O . ASP A 1 54 ? -23.116 32.795 75.091 1.00 91.38 ? 54 ASP A O 1 ATOM 418 C CB . ASP A 1 54 ? -20.110 32.889 74.413 1.00 96.56 ? 54 ASP A CB 1 ATOM 419 C CG . ASP A 1 54 ? -19.071 32.199 73.545 1.00 99.48 ? 54 ASP A CG 1 ATOM 420 O OD1 . ASP A 1 54 ? -19.461 31.507 72.579 1.00 97.38 ? 54 ASP A OD1 1 ATOM 421 O OD2 . ASP A 1 54 ? -17.862 32.337 73.841 1.00 102.61 ? 54 ASP A OD2 1 ATOM 422 N N . CYS A 1 55 ? -22.717 34.972 74.834 1.00 88.80 ? 55 CYS A N 1 ATOM 423 C CA . CYS A 1 55 ? -23.845 35.372 75.692 1.00 87.34 ? 55 CYS A CA 1 ATOM 424 C C . CYS A 1 55 ? -25.232 35.212 75.020 1.00 82.18 ? 55 CYS A C 1 ATOM 425 O O . CYS A 1 55 ? -25.343 35.096 73.799 1.00 81.12 ? 55 CYS A O 1 ATOM 426 C CB . CYS A 1 55 ? -23.648 36.812 76.178 1.00 89.30 ? 55 CYS A CB 1 ATOM 427 S SG . CYS A 1 55 ? -22.287 36.965 77.355 1.00 95.20 ? 55 CYS A SG 1 ATOM 428 N N . SER A 1 56 ? -26.278 35.209 75.844 1.00 78.49 ? 56 SER A N 1 ATOM 429 C CA . SER A 1 56 ? -27.664 35.066 75.389 1.00 74.57 ? 56 SER A CA 1 ATOM 430 C C . SER A 1 56 ? -28.527 36.242 75.840 1.00 72.41 ? 56 SER A C 1 ATOM 431 O O . SER A 1 56 ? -28.198 36.949 76.781 1.00 73.13 ? 56 SER A O 1 ATOM 432 C CB . SER A 1 56 ? -28.268 33.775 75.952 1.00 73.83 ? 56 SER A CB 1 ATOM 433 O OG . SER A 1 56 ? -28.749 33.969 77.276 1.00 72.83 ? 56 SER A OG 1 ATOM 434 N N . VAL A 1 57 ? -29.670 36.418 75.197 1.00 70.37 ? 57 VAL A N 1 ATOM 435 C CA . VAL A 1 57 ? -30.524 37.564 75.498 1.00 69.31 ? 57 VAL A CA 1 ATOM 436 C C . VAL A 1 57 ? -30.706 37.673 77.015 1.00 70.14 ? 57 VAL A C 1 ATOM 437 O O . VAL A 1 57 ? -30.658 38.772 77.582 1.00 69.92 ? 57 VAL A O 1 ATOM 438 C CB . VAL A 1 57 ? -31.886 37.472 74.781 1.00 66.64 ? 57 VAL A CB 1 ATOM 439 C CG1 . VAL A 1 57 ? -32.786 38.632 75.185 1.00 66.52 ? 57 VAL A CG1 1 ATOM 440 C CG2 . VAL A 1 57 ? -31.688 37.463 73.271 1.00 66.16 ? 57 VAL A CG2 1 ATOM 441 N N . ALA A 1 58 ? -30.883 36.525 77.669 1.00 69.93 ? 58 ALA A N 1 ATOM 442 C CA . ALA A 1 58 ? -30.984 36.482 79.124 1.00 70.54 ? 58 ALA A CA 1 ATOM 443 C C . ALA A 1 58 ? -29.678 36.927 79.810 1.00 72.77 ? 58 ALA A C 1 ATOM 444 O O . ALA A 1 58 ? -29.687 37.854 80.635 1.00 72.54 ? 58 ALA A O 1 ATOM 445 C CB . ALA A 1 58 ? -31.392 35.092 79.587 1.00 69.47 ? 58 ALA A CB 1 ATOM 446 N N . GLY A 1 59 ? -28.569 36.271 79.466 1.00 73.86 ? 59 GLY A N 1 ATOM 447 C CA . GLY A 1 59 ? -27.256 36.649 79.979 1.00 75.56 ? 59 GLY A CA 1 ATOM 448 C C . GLY A 1 59 ? -27.047 38.152 79.892 1.00 76.99 ? 59 GLY A C 1 ATOM 449 O O . GLY A 1 59 ? -26.670 38.795 80.869 1.00 80.05 ? 59 GLY A O 1 ATOM 450 N N . TRP A 1 60 ? -27.321 38.711 78.719 1.00 75.83 ? 60 TRP A N 1 ATOM 451 C CA . TRP A 1 60 ? -27.172 40.138 78.467 1.00 76.12 ? 60 TRP A CA 1 ATOM 452 C C . TRP A 1 60 ? -28.086 40.974 79.363 1.00 76.66 ? 60 TRP A C 1 ATOM 453 O O . TRP A 1 60 ? -27.615 41.860 80.081 1.00 79.77 ? 60 TRP A O 1 ATOM 454 C CB . TRP A 1 60 ? -27.436 40.425 76.977 1.00 74.81 ? 60 TRP A CB 1 ATOM 455 C CG . TRP A 1 60 ? -27.700 41.861 76.626 1.00 74.99 ? 60 TRP A CG 1 ATOM 456 C CD1 . TRP A 1 60 ? -27.119 42.965 77.179 1.00 76.89 ? 60 TRP A CD1 1 ATOM 457 C CD2 . TRP A 1 60 ? -28.592 42.344 75.615 1.00 73.07 ? 60 TRP A CD2 1 ATOM 458 N NE1 . TRP A 1 60 ? -27.609 44.102 76.589 1.00 76.81 ? 60 TRP A NE1 1 ATOM 459 C CE2 . TRP A 1 60 ? -28.513 43.749 75.625 1.00 74.21 ? 60 TRP A CE2 1 ATOM 460 C CE3 . TRP A 1 60 ? -29.462 41.723 74.713 1.00 71.29 ? 60 TRP A CE3 1 ATOM 461 C CZ2 . TRP A 1 60 ? -29.267 44.544 74.770 1.00 74.11 ? 60 TRP A CZ2 1 ATOM 462 C CZ3 . TRP A 1 60 ? -30.213 42.516 73.854 1.00 70.39 ? 60 TRP A CZ3 1 ATOM 463 C CH2 . TRP A 1 60 ? -30.111 43.908 73.889 1.00 72.13 ? 60 TRP A CH2 1 ATOM 464 N N . LEU A 1 61 ? -29.384 40.685 79.344 1.00 75.13 ? 61 LEU A N 1 ATOM 465 C CA . LEU A 1 61 ? -30.364 41.562 79.996 1.00 74.47 ? 61 LEU A CA 1 ATOM 466 C C . LEU A 1 61 ? -30.362 41.519 81.525 1.00 75.06 ? 61 LEU A C 1 ATOM 467 O O . LEU A 1 61 ? -30.577 42.548 82.171 1.00 76.52 ? 61 LEU A O 1 ATOM 468 C CB . LEU A 1 61 ? -31.768 41.289 79.463 1.00 72.57 ? 61 LEU A CB 1 ATOM 469 C CG . LEU A 1 61 ? -32.010 41.658 77.997 1.00 71.61 ? 61 LEU A CG 1 ATOM 470 C CD1 . LEU A 1 61 ? -33.503 41.592 77.718 1.00 69.99 ? 61 LEU A CD1 1 ATOM 471 C CD2 . LEU A 1 61 ? -31.470 43.036 77.643 1.00 72.92 ? 61 LEU A CD2 1 ATOM 472 N N . LEU A 1 62 ? -30.129 40.347 82.106 1.00 74.41 ? 62 LEU A N 1 ATOM 473 C CA . LEU A 1 62 ? -29.932 40.252 83.558 1.00 74.76 ? 62 LEU A CA 1 ATOM 474 C C . LEU A 1 62 ? -28.558 40.800 83.960 1.00 77.76 ? 62 LEU A C 1 ATOM 475 O O . LEU A 1 62 ? -28.351 41.210 85.101 1.00 78.07 ? 62 LEU A O 1 ATOM 476 C CB . LEU A 1 62 ? -30.074 38.806 84.028 1.00 73.24 ? 62 LEU A CB 1 ATOM 477 C CG . LEU A 1 62 ? -31.467 38.217 83.827 1.00 70.56 ? 62 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 62 ? -31.413 36.703 83.872 1.00 69.94 ? 62 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 62 ? -32.439 38.752 84.865 1.00 70.38 ? 62 LEU A CD2 1 ATOM 480 N N . GLY A 1 63 ? -27.624 40.810 83.012 1.00 79.25 ? 63 GLY A N 1 ATOM 481 C CA . GLY A 1 63 ? -26.271 41.263 83.280 1.00 82.21 ? 63 GLY A CA 1 ATOM 482 C C . GLY A 1 63 ? -25.432 40.164 83.902 1.00 83.33 ? 63 GLY A C 1 ATOM 483 O O . GLY A 1 63 ? -24.842 40.354 84.953 1.00 84.90 ? 63 GLY A O 1 ATOM 484 N N . ASN A 1 64 ? -25.384 39.006 83.252 1.00 83.06 ? 64 ASN A N 1 ATOM 485 C CA . ASN A 1 64 ? -24.445 37.960 83.622 1.00 84.06 ? 64 ASN A CA 1 ATOM 486 C C . ASN A 1 64 ? -23.055 38.592 83.684 1.00 88.21 ? 64 ASN A C 1 ATOM 487 O O . ASN A 1 64 ? -22.710 39.398 82.816 1.00 88.62 ? 64 ASN A O 1 ATOM 488 C CB . ASN A 1 64 ? -24.508 36.821 82.594 1.00 81.89 ? 64 ASN A CB 1 ATOM 489 C CG . ASN A 1 64 ? -23.501 35.711 82.860 1.00 82.43 ? 64 ASN A CG 1 ATOM 490 O OD1 . ASN A 1 64 ? -22.302 35.960 82.973 1.00 84.51 ? 64 ASN A OD1 1 ATOM 491 N ND2 . ASN A 1 64 ? -23.978 34.473 82.909 1.00 80.58 ? 64 ASN A ND2 1 ATOM 492 N N . PRO A 1 65 ? -22.263 38.252 84.718 1.00 92.65 ? 65 PRO A N 1 ATOM 493 C CA . PRO A 1 65 ? -20.928 38.848 84.888 1.00 96.85 ? 65 PRO A CA 1 ATOM 494 C C . PRO A 1 65 ? -19.973 38.612 83.714 1.00 99.41 ? 65 PRO A C 1 ATOM 495 O O . PRO A 1 65 ? -19.106 39.442 83.457 1.00 102.21 ? 65 PRO A O 1 ATOM 496 C CB . PRO A 1 65 ? -20.387 38.161 86.149 1.00 98.24 ? 65 PRO A CB 1 ATOM 497 C CG . PRO A 1 65 ? -21.207 36.931 86.311 1.00 95.93 ? 65 PRO A CG 1 ATOM 498 C CD . PRO A 1 65 ? -22.562 37.282 85.788 1.00 92.83 ? 65 PRO A CD 1 ATOM 499 N N . MET A 1 66 ? -20.130 37.492 83.011 1.00 99.88 ? 66 MET A N 1 ATOM 500 C CA . MET A 1 66 ? -19.283 37.189 81.851 1.00 101.46 ? 66 MET A CA 1 ATOM 501 C C . MET A 1 66 ? -19.836 37.773 80.546 1.00 98.32 ? 66 MET A C 1 ATOM 502 O O . MET A 1 66 ? -19.310 37.513 79.466 1.00 97.25 ? 66 MET A O 1 ATOM 503 C CB . MET A 1 66 ? -19.069 35.682 81.737 1.00 102.51 ? 66 MET A CB 1 ATOM 504 C CG . MET A 1 66 ? -18.196 35.137 82.851 1.00 105.96 ? 66 MET A CG 1 ATOM 505 S SD . MET A 1 66 ? -17.387 33.610 82.362 1.00 111.20 ? 66 MET A SD 1 ATOM 506 C CE . MET A 1 66 ? -15.971 33.590 83.463 1.00 113.81 ? 66 MET A CE 1 ATOM 507 N N . CYS A 1 67 ? -20.891 38.572 80.663 1.00 96.83 ? 67 CYS A N 1 ATOM 508 C CA . CYS A 1 67 ? -21.459 39.305 79.535 1.00 95.92 ? 67 CYS A CA 1 ATOM 509 C C . CYS A 1 67 ? -21.219 40.791 79.733 1.00 96.33 ? 67 CYS A C 1 ATOM 510 O O . CYS A 1 67 ? -22.067 41.624 79.407 1.00 92.60 ? 67 CYS A O 1 ATOM 511 C CB . CYS A 1 67 ? -22.950 39.009 79.436 1.00 94.15 ? 67 CYS A CB 1 ATOM 512 S SG . CYS A 1 67 ? -23.242 37.258 79.127 1.00 94.44 ? 67 CYS A SG 1 ATOM 513 N N . ASP A 1 68 ? -20.044 41.107 80.272 1.00 98.71 ? 68 ASP A N 1 ATOM 514 C CA . ASP A 1 68 ? -19.665 42.486 80.568 1.00 99.74 ? 68 ASP A CA 1 ATOM 515 C C . ASP A 1 68 ? -19.478 43.315 79.308 1.00 99.21 ? 68 ASP A C 1 ATOM 516 O O . ASP A 1 68 ? -19.687 44.534 79.331 1.00 99.47 ? 68 ASP A O 1 ATOM 517 C CB . ASP A 1 68 ? -18.385 42.523 81.406 1.00 102.77 ? 68 ASP A CB 1 ATOM 518 C CG . ASP A 1 68 ? -18.655 42.350 82.877 1.00 102.54 ? 68 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 68 ? -19.739 41.845 83.231 1.00 100.25 ? 68 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 68 ? -17.789 42.728 83.687 1.00 105.76 ? 68 ASP A OD2 1 ATOM 521 N N . GLU A 1 69 ? -19.092 42.653 78.217 1.00 97.51 ? 69 GLU A N 1 ATOM 522 C CA . GLU A 1 69 ? -19.007 43.303 76.912 1.00 96.54 ? 69 GLU A CA 1 ATOM 523 C C . GLU A 1 69 ? -20.279 44.083 76.588 1.00 94.15 ? 69 GLU A C 1 ATOM 524 O O . GLU A 1 69 ? -20.220 45.134 75.945 1.00 93.87 ? 69 GLU A O 1 ATOM 525 C CB . GLU A 1 69 ? -18.747 42.275 75.800 1.00 95.10 ? 69 GLU A CB 1 ATOM 526 C CG . GLU A 1 69 ? -18.852 42.866 74.395 1.00 94.35 ? 69 GLU A CG 1 ATOM 527 C CD . GLU A 1 69 ? -18.456 41.907 73.284 1.00 93.33 ? 69 GLU A CD 1 ATOM 528 O OE1 . GLU A 1 69 ? -18.149 40.726 73.569 1.00 92.62 ? 69 GLU A OE1 1 ATOM 529 O OE2 . GLU A 1 69 ? -18.456 42.351 72.113 1.00 92.30 ? 69 GLU A OE2 1 ATOM 530 N N . PHE A 1 70 ? -21.419 43.568 77.046 1.00 91.94 ? 70 PHE A N 1 ATOM 531 C CA . PHE A 1 70 ? -22.721 44.050 76.598 1.00 90.10 ? 70 PHE A CA 1 ATOM 532 C C . PHE A 1 70 ? -23.452 44.984 77.571 1.00 91.40 ? 70 PHE A C 1 ATOM 533 O O . PHE A 1 70 ? -24.664 45.171 77.456 1.00 88.41 ? 70 PHE A O 1 ATOM 534 C CB . PHE A 1 70 ? -23.591 42.847 76.215 1.00 86.83 ? 70 PHE A CB 1 ATOM 535 C CG . PHE A 1 70 ? -22.910 41.909 75.257 1.00 85.78 ? 70 PHE A CG 1 ATOM 536 C CD1 . PHE A 1 70 ? -22.640 42.314 73.961 1.00 85.58 ? 70 PHE A CD1 1 ATOM 537 C CD2 . PHE A 1 70 ? -22.497 40.647 75.659 1.00 85.17 ? 70 PHE A CD2 1 ATOM 538 C CE1 . PHE A 1 70 ? -22.005 41.471 73.073 1.00 85.37 ? 70 PHE A CE1 1 ATOM 539 C CE2 . PHE A 1 70 ? -21.852 39.800 74.776 1.00 85.08 ? 70 PHE A CE2 1 ATOM 540 C CZ . PHE A 1 70 ? -21.605 40.214 73.479 1.00 85.16 ? 70 PHE A CZ 1 ATOM 541 N N . ILE A 1 71 ? -22.727 45.595 78.507 1.00 95.76 ? 71 ILE A N 1 ATOM 542 C CA . ILE A 1 71 ? -23.292 46.723 79.250 1.00 98.13 ? 71 ILE A CA 1 ATOM 543 C C . ILE A 1 71 ? -23.403 47.901 78.284 1.00 100.88 ? 71 ILE A C 1 ATOM 544 O O . ILE A 1 71 ? -22.556 48.064 77.401 1.00 103.52 ? 71 ILE A O 1 ATOM 545 C CB . ILE A 1 71 ? -22.422 47.148 80.439 1.00 102.49 ? 71 ILE A CB 1 ATOM 546 C CG1 . ILE A 1 71 ? -22.271 45.992 81.435 1.00 102.21 ? 71 ILE A CG1 1 ATOM 547 C CG2 . ILE A 1 71 ? -23.021 48.383 81.109 1.00 104.24 ? 71 ILE A CG2 1 ATOM 548 C CD1 . ILE A 1 71 ? -21.452 46.330 82.666 1.00 103.53 ? 71 ILE A CD1 1 ATOM 549 N N . ASN A 1 72 ? -24.455 48.704 78.440 1.00 101.12 ? 72 ASN A N 1 ATOM 550 C CA . ASN A 1 72 ? -24.700 49.888 77.593 1.00 102.01 ? 72 ASN A CA 1 ATOM 551 C C . ASN A 1 72 ? -24.397 49.746 76.094 1.00 100.40 ? 72 ASN A C 1 ATOM 552 O O . ASN A 1 72 ? -23.842 50.659 75.484 1.00 102.14 ? 72 ASN A O 1 ATOM 553 C CB . ASN A 1 72 ? -23.932 51.079 78.163 1.00 106.44 ? 72 ASN A CB 1 ATOM 554 C CG . ASN A 1 72 ? -24.417 51.463 79.538 1.00 109.38 ? 72 ASN A CG 1 ATOM 555 O OD1 . ASN A 1 72 ? -25.570 51.205 79.886 1.00 109.86 ? 72 ASN A OD1 1 ATOM 556 N ND2 . ASN A 1 72 ? -23.546 52.074 80.332 1.00 113.26 ? 72 ASN A ND2 1 ATOM 557 N N . VAL A 1 73 ? -24.774 48.612 75.504 1.00 96.60 ? 73 VAL A N 1 ATOM 558 C CA . VAL A 1 73 ? -24.574 48.392 74.063 1.00 95.22 ? 73 VAL A CA 1 ATOM 559 C C . VAL A 1 73 ? -25.280 49.462 73.231 1.00 94.42 ? 73 VAL A C 1 ATOM 560 O O . VAL A 1 73 ? -26.414 49.839 73.540 1.00 93.44 ? 73 VAL A O 1 ATOM 561 C CB . VAL A 1 73 ? -25.096 47.015 73.588 1.00 92.14 ? 73 VAL A CB 1 ATOM 562 C CG1 . VAL A 1 73 ? -24.286 45.889 74.207 1.00 92.40 ? 73 VAL A CG1 1 ATOM 563 C CG2 . VAL A 1 73 ? -26.588 46.851 73.881 1.00 89.42 ? 73 VAL A CG2 1 ATOM 564 N N . PRO A 1 74 ? -24.623 49.940 72.157 1.00 94.52 ? 74 PRO A N 1 ATOM 565 C CA . PRO A 1 74 ? -25.259 50.965 71.334 1.00 94.09 ? 74 PRO A CA 1 ATOM 566 C C . PRO A 1 74 ? -26.393 50.405 70.481 1.00 91.05 ? 74 PRO A C 1 ATOM 567 O O . PRO A 1 74 ? -26.598 49.186 70.430 1.00 87.84 ? 74 PRO A O 1 ATOM 568 C CB . PRO A 1 74 ? -24.117 51.451 70.436 1.00 95.95 ? 74 PRO A CB 1 ATOM 569 C CG . PRO A 1 74 ? -23.224 50.267 70.298 1.00 95.83 ? 74 PRO A CG 1 ATOM 570 C CD . PRO A 1 74 ? -23.350 49.474 71.575 1.00 95.42 ? 74 PRO A CD 1 ATOM 571 N N . GLU A 1 75 ? -27.114 51.313 69.825 1.00 90.70 ? 75 GLU A N 1 ATOM 572 C CA . GLU A 1 75 ? -28.120 50.983 68.820 1.00 87.13 ? 75 GLU A CA 1 ATOM 573 C C . GLU A 1 75 ? -27.650 49.866 67.879 1.00 85.95 ? 75 GLU A C 1 ATOM 574 O O . GLU A 1 75 ? -26.487 49.837 67.465 1.00 85.58 ? 75 GLU A O 1 ATOM 575 C CB . GLU A 1 75 ? -28.464 52.247 68.027 1.00 88.33 ? 75 GLU A CB 1 ATOM 576 C CG . GLU A 1 75 ? -29.395 52.045 66.842 1.00 86.87 ? 75 GLU A CG 1 ATOM 577 C CD . GLU A 1 75 ? -30.092 53.326 66.409 1.00 88.16 ? 75 GLU A CD 1 ATOM 578 O OE1 . GLU A 1 75 ? -29.643 54.424 66.810 1.00 91.27 ? 75 GLU A OE1 1 ATOM 579 O OE2 . GLU A 1 75 ? -31.098 53.235 65.670 1.00 86.13 ? 75 GLU A OE2 1 ATOM 580 N N . TRP A 1 76 ? -28.562 48.942 67.568 1.00 84.39 ? 76 TRP A N 1 ATOM 581 C CA . TRP A 1 76 ? -28.262 47.812 66.692 1.00 83.88 ? 76 TRP A CA 1 ATOM 582 C C . TRP A 1 76 ? -29.254 47.745 65.538 1.00 82.17 ? 76 TRP A C 1 ATOM 583 O O . TRP A 1 76 ? -30.348 48.310 65.603 1.00 83.27 ? 76 TRP A O 1 ATOM 584 C CB . TRP A 1 76 ? -28.262 46.499 67.472 1.00 82.93 ? 76 TRP A CB 1 ATOM 585 C CG . TRP A 1 76 ? -29.595 46.134 68.060 1.00 83.23 ? 76 TRP A CG 1 ATOM 586 C CD1 . TRP A 1 76 ? -30.606 45.437 67.447 1.00 81.55 ? 76 TRP A CD1 1 ATOM 587 C CD2 . TRP A 1 76 ? -30.063 46.436 69.382 1.00 84.39 ? 76 TRP A CD2 1 ATOM 588 N NE1 . TRP A 1 76 ? -31.674 45.298 68.306 1.00 80.19 ? 76 TRP A NE1 1 ATOM 589 C CE2 . TRP A 1 76 ? -31.368 45.900 69.497 1.00 82.10 ? 76 TRP A CE2 1 ATOM 590 C CE3 . TRP A 1 76 ? -29.510 47.113 70.479 1.00 86.35 ? 76 TRP A CE3 1 ATOM 591 C CZ2 . TRP A 1 76 ? -32.124 46.018 70.668 1.00 82.24 ? 76 TRP A CZ2 1 ATOM 592 C CZ3 . TRP A 1 76 ? -30.265 47.233 71.642 1.00 86.05 ? 76 TRP A CZ3 1 ATOM 593 C CH2 . TRP A 1 76 ? -31.556 46.686 71.727 1.00 84.04 ? 76 TRP A CH2 1 ATOM 594 N N . SER A 1 77 ? -28.848 47.072 64.471 1.00 80.36 ? 77 SER A N 1 ATOM 595 C CA . SER A 1 77 ? -29.697 46.886 63.304 1.00 78.69 ? 77 SER A CA 1 ATOM 596 C C . SER A 1 77 ? -30.479 45.601 63.491 1.00 76.39 ? 77 SER A C 1 ATOM 597 O O . SER A 1 77 ? -31.688 45.557 63.287 1.00 75.33 ? 77 SER A O 1 ATOM 598 C CB . SER A 1 77 ? -28.842 46.789 62.045 1.00 78.92 ? 77 SER A CB 1 ATOM 599 O OG . SER A 1 77 ? -27.679 46.019 62.292 1.00 79.29 ? 77 SER A OG 1 ATOM 600 N N . TYR A 1 78 ? -29.753 44.555 63.874 1.00 74.85 ? 78 TYR A N 1 ATOM 601 C CA . TYR A 1 78 ? -30.335 43.281 64.230 1.00 71.12 ? 78 TYR A CA 1 ATOM 602 C C . TYR A 1 78 ? -29.452 42.629 65.296 1.00 71.24 ? 78 TYR A C 1 ATOM 603 O O . TYR A 1 78 ? -28.324 43.061 65.510 1.00 72.52 ? 78 TYR A O 1 ATOM 604 C CB . TYR A 1 78 ? -30.462 42.393 62.982 1.00 68.92 ? 78 TYR A CB 1 ATOM 605 C CG . TYR A 1 78 ? -29.157 42.060 62.277 1.00 68.24 ? 78 TYR A CG 1 ATOM 606 C CD1 . TYR A 1 78 ? -28.563 42.954 61.387 1.00 68.34 ? 78 TYR A CD1 1 ATOM 607 C CD2 . TYR A 1 78 ? -28.531 40.831 62.485 1.00 67.66 ? 78 TYR A CD2 1 ATOM 608 C CE1 . TYR A 1 78 ? -27.371 42.638 60.737 1.00 69.15 ? 78 TYR A CE1 1 ATOM 609 C CE2 . TYR A 1 78 ? -27.344 40.510 61.847 1.00 68.42 ? 78 TYR A CE2 1 ATOM 610 C CZ . TYR A 1 78 ? -26.764 41.413 60.975 1.00 69.13 ? 78 TYR A CZ 1 ATOM 611 O OH . TYR A 1 78 ? -25.582 41.062 60.358 1.00 69.25 ? 78 TYR A OH 1 ATOM 612 N N . ILE A 1 79 ? -29.972 41.601 65.961 1.00 68.80 ? 79 ILE A N 1 ATOM 613 C CA . ILE A 1 79 ? -29.238 40.893 67.006 1.00 69.07 ? 79 ILE A CA 1 ATOM 614 C C . ILE A 1 79 ? -28.881 39.496 66.528 1.00 68.15 ? 79 ILE A C 1 ATOM 615 O O . ILE A 1 79 ? -29.656 38.870 65.814 1.00 65.64 ? 79 ILE A O 1 ATOM 616 C CB . ILE A 1 79 ? -30.090 40.745 68.279 1.00 68.96 ? 79 ILE A CB 1 ATOM 617 C CG1 . ILE A 1 79 ? -30.459 42.119 68.843 1.00 70.13 ? 79 ILE A CG1 1 ATOM 618 C CG2 . ILE A 1 79 ? -29.366 39.906 69.327 1.00 69.41 ? 79 ILE A CG2 1 ATOM 619 C CD1 . ILE A 1 79 ? -31.513 42.065 69.929 1.00 69.58 ? 79 ILE A CD1 1 ATOM 620 N N . VAL A 1 80 ? -27.723 38.998 66.955 1.00 70.13 ? 80 VAL A N 1 ATOM 621 C CA . VAL A 1 80 ? -27.258 37.663 66.574 1.00 70.28 ? 80 VAL A CA 1 ATOM 622 C C . VAL A 1 80 ? -26.947 36.846 67.822 1.00 70.90 ? 80 VAL A C 1 ATOM 623 O O . VAL A 1 80 ? -26.117 37.237 68.634 1.00 73.12 ? 80 VAL A O 1 ATOM 624 C CB . VAL A 1 80 ? -26.004 37.734 65.676 1.00 71.64 ? 80 VAL A CB 1 ATOM 625 C CG1 . VAL A 1 80 ? -25.513 36.336 65.304 1.00 71.68 ? 80 VAL A CG1 1 ATOM 626 C CG2 . VAL A 1 80 ? -26.310 38.539 64.426 1.00 71.11 ? 80 VAL A CG2 1 ATOM 627 N N . GLU A 1 81 ? -27.613 35.705 67.945 1.00 69.80 ? 81 GLU A N 1 ATOM 628 C CA . GLU A 1 81 ? -27.490 34.837 69.100 1.00 70.48 ? 81 GLU A CA 1 ATOM 629 C C . GLU A 1 81 ? -27.202 33.444 68.585 1.00 71.14 ? 81 GLU A C 1 ATOM 630 O O . GLU A 1 81 ? -27.812 33.011 67.612 1.00 70.40 ? 81 GLU A O 1 ATOM 631 C CB . GLU A 1 81 ? -28.805 34.838 69.887 1.00 68.82 ? 81 GLU A CB 1 ATOM 632 C CG . GLU A 1 81 ? -28.766 34.093 71.212 1.00 69.21 ? 81 GLU A CG 1 ATOM 633 C CD . GLU A 1 81 ? -30.144 33.898 71.833 1.00 67.86 ? 81 GLU A CD 1 ATOM 634 O OE1 . GLU A 1 81 ? -31.044 33.378 71.138 1.00 64.87 ? 81 GLU A OE1 1 ATOM 635 O OE2 . GLU A 1 81 ? -30.323 34.258 73.024 1.00 68.61 ? 81 GLU A OE2 1 ATOM 636 N N . LYS A 1 82 ? -26.276 32.749 69.233 1.00 74.09 ? 82 LYS A N 1 ATOM 637 C CA . LYS A 1 82 ? -25.987 31.355 68.905 1.00 75.97 ? 82 LYS A CA 1 ATOM 638 C C . LYS A 1 82 ? -27.148 30.410 69.257 1.00 75.29 ? 82 LYS A C 1 ATOM 639 O O . LYS A 1 82 ? -28.114 30.794 69.923 1.00 72.54 ? 82 LYS A O 1 ATOM 640 C CB . LYS A 1 82 ? -24.711 30.896 69.622 1.00 79.79 ? 82 LYS A CB 1 ATOM 641 C CG . LYS A 1 82 ? -23.423 31.422 69.005 1.00 82.62 ? 82 LYS A CG 1 ATOM 642 C CD . LYS A 1 82 ? -22.213 30.961 69.802 1.00 86.03 ? 82 LYS A CD 1 ATOM 643 C CE . LYS A 1 82 ? -20.984 30.762 68.927 1.00 88.86 ? 82 LYS A CE 1 ATOM 644 N NZ . LYS A 1 82 ? -20.479 32.037 68.357 1.00 90.16 ? 82 LYS A NZ 1 ATOM 645 N N . ALA A 1 83 ? -27.039 29.168 68.792 1.00 77.70 ? 83 ALA A N 1 ATOM 646 C CA . ALA A 1 83 ? -28.033 28.133 69.088 1.00 78.68 ? 83 ALA A CA 1 ATOM 647 C C . ALA A 1 83 ? -27.975 27.664 70.555 1.00 81.02 ? 83 ALA A C 1 ATOM 648 O O . ALA A 1 83 ? -29.014 27.456 71.179 1.00 80.56 ? 83 ALA A O 1 ATOM 649 C CB . ALA A 1 83 ? -27.870 26.954 68.134 1.00 78.11 ? 83 ALA A CB 1 ATOM 650 N N . ASN A 1 84 ? -26.768 27.511 71.101 1.00 85.39 ? 84 ASN A N 1 ATOM 651 C CA . ASN A 1 84 ? -26.586 27.076 72.493 1.00 88.13 ? 84 ASN A CA 1 ATOM 652 C C . ASN A 1 84 ? -25.523 27.906 73.207 1.00 89.75 ? 84 ASN A C 1 ATOM 653 O O . ASN A 1 84 ? -24.461 27.394 73.563 1.00 91.64 ? 84 ASN A O 1 ATOM 654 C CB . ASN A 1 84 ? -26.230 25.585 72.545 1.00 90.88 ? 84 ASN A CB 1 ATOM 655 C CG . ASN A 1 84 ? -27.392 24.697 72.126 1.00 91.84 ? 84 ASN A CG 1 ATOM 656 O OD1 . ASN A 1 84 ? -28.408 24.626 72.822 1.00 92.18 ? 84 ASN A OD1 1 ATOM 657 N ND2 . ASN A 1 84 ? -27.256 24.023 70.981 1.00 92.23 ? 84 ASN A ND2 1 ATOM 658 N N . PRO A 1 85 ? -25.810 29.201 73.422 1.00 89.61 ? 85 PRO A N 1 ATOM 659 C CA . PRO A 1 85 ? -24.818 30.079 74.047 1.00 91.55 ? 85 PRO A CA 1 ATOM 660 C C . PRO A 1 85 ? -24.452 29.588 75.447 1.00 93.72 ? 85 PRO A C 1 ATOM 661 O O . PRO A 1 85 ? -25.348 29.274 76.225 1.00 94.23 ? 85 PRO A O 1 ATOM 662 C CB . PRO A 1 85 ? -25.529 31.441 74.111 1.00 90.23 ? 85 PRO A CB 1 ATOM 663 C CG . PRO A 1 85 ? -26.740 31.331 73.245 1.00 87.24 ? 85 PRO A CG 1 ATOM 664 C CD . PRO A 1 85 ? -27.098 29.883 73.194 1.00 86.89 ? 85 PRO A CD 1 ATOM 665 N N . VAL A 1 86 ? -23.157 29.509 75.759 1.00 95.24 ? 86 VAL A N 1 ATOM 666 C CA . VAL A 1 86 ? -22.728 28.968 77.058 1.00 95.93 ? 86 VAL A CA 1 ATOM 667 C C . VAL A 1 86 ? -23.094 29.884 78.235 1.00 93.63 ? 86 VAL A C 1 ATOM 668 O O . VAL A 1 86 ? -23.559 29.404 79.268 1.00 93.11 ? 86 VAL A O 1 ATOM 669 C CB . VAL A 1 86 ? -21.210 28.624 77.104 1.00 99.98 ? 86 VAL A CB 1 ATOM 670 C CG1 . VAL A 1 86 ? -20.832 27.689 75.958 1.00 100.53 ? 86 VAL A CG1 1 ATOM 671 C CG2 . VAL A 1 86 ? -20.338 29.878 77.101 1.00 101.49 ? 86 VAL A CG2 1 ATOM 672 N N . ASN A 1 87 ? -22.888 31.191 78.069 1.00 91.11 ? 87 ASN A N 1 ATOM 673 C CA . ASN A 1 87 ? -23.131 32.167 79.131 1.00 89.41 ? 87 ASN A CA 1 ATOM 674 C C . ASN A 1 87 ? -24.579 32.626 79.125 1.00 85.88 ? 87 ASN A C 1 ATOM 675 O O . ASN A 1 87 ? -24.897 33.718 78.652 1.00 84.73 ? 87 ASN A O 1 ATOM 676 C CB . ASN A 1 87 ? -22.207 33.380 78.986 1.00 91.06 ? 87 ASN A CB 1 ATOM 677 C CG . ASN A 1 87 ? -20.758 33.042 79.252 1.00 94.05 ? 87 ASN A CG 1 ATOM 678 O OD1 . ASN A 1 87 ? -20.372 32.778 80.392 1.00 97.71 ? 87 ASN A OD1 1 ATOM 679 N ND2 . ASN A 1 87 ? -19.942 33.062 78.206 1.00 95.07 ? 87 ASN A ND2 1 ATOM 680 N N . ASP A 1 88 ? -25.450 31.778 79.661 1.00 84.25 ? 88 ASP A N 1 ATOM 681 C CA . ASP A 1 88 ? -26.871 32.072 79.776 1.00 81.34 ? 88 ASP A CA 1 ATOM 682 C C . ASP A 1 88 ? -27.175 32.413 81.246 1.00 81.68 ? 88 ASP A C 1 ATOM 683 O O . ASP A 1 88 ? -26.503 33.265 81.831 1.00 81.96 ? 88 ASP A O 1 ATOM 684 C CB . ASP A 1 88 ? -27.680 30.868 79.262 1.00 79.36 ? 88 ASP A CB 1 ATOM 685 C CG . ASP A 1 88 ? -29.157 31.184 79.054 1.00 77.10 ? 88 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 88 ? -29.530 32.374 79.034 1.00 76.46 ? 88 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 88 ? -29.951 30.232 78.923 1.00 76.67 ? 88 ASP A OD2 1 ATOM 688 N N . LEU A 1 89 ? -28.193 31.769 81.821 1.00 80.55 ? 89 LEU A N 1 ATOM 689 C CA . LEU A 1 89 ? -28.464 31.802 83.257 1.00 80.34 ? 89 LEU A CA 1 ATOM 690 C C . LEU A 1 89 ? -27.375 31.048 84.019 1.00 82.25 ? 89 LEU A C 1 ATOM 691 O O . LEU A 1 89 ? -27.449 29.827 84.178 1.00 82.10 ? 89 LEU A O 1 ATOM 692 C CB . LEU A 1 89 ? -29.825 31.145 83.547 1.00 77.92 ? 89 LEU A CB 1 ATOM 693 C CG . LEU A 1 89 ? -31.119 31.965 83.590 1.00 74.90 ? 89 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 89 ? -31.026 33.308 82.881 1.00 73.65 ? 89 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 89 ? -32.248 31.115 83.028 1.00 73.18 ? 89 LEU A CD2 1 ATOM 696 N N . CYS A 1 90 ? -26.376 31.785 84.493 1.00 84.80 ? 90 CYS A N 1 ATOM 697 C CA . CYS A 1 90 ? -25.250 31.195 85.219 1.00 87.72 ? 90 CYS A CA 1 ATOM 698 C C . CYS A 1 90 ? -25.722 30.530 86.518 1.00 87.09 ? 90 CYS A C 1 ATOM 699 O O . CYS A 1 90 ? -25.392 29.376 86.776 1.00 88.20 ? 90 CYS A O 1 ATOM 700 C CB . CYS A 1 90 ? -24.171 32.249 85.468 1.00 90.39 ? 90 CYS A CB 1 ATOM 701 S SG . CYS A 1 90 ? -24.830 33.808 86.081 1.00 90.51 ? 90 CYS A SG 1 ATOM 702 N N . TYR A 1 91 ? -26.528 31.239 87.303 1.00 85.83 ? 91 TYR A N 1 ATOM 703 C CA . TYR A 1 91 ? -27.239 30.631 88.421 1.00 86.12 ? 91 TYR A CA 1 ATOM 704 C C . TYR A 1 91 ? -28.518 30.010 87.880 1.00 83.75 ? 91 TYR A C 1 ATOM 705 O O . TYR A 1 91 ? -29.375 30.725 87.367 1.00 82.78 ? 91 TYR A O 1 ATOM 706 C CB . TYR A 1 91 ? -27.594 31.679 89.467 1.00 87.49 ? 91 TYR A CB 1 ATOM 707 C CG . TYR A 1 91 ? -27.937 31.107 90.823 1.00 89.72 ? 91 TYR A CG 1 ATOM 708 C CD1 . TYR A 1 91 ? -29.213 30.632 91.098 1.00 89.39 ? 91 TYR A CD1 1 ATOM 709 C CD2 . TYR A 1 91 ? -26.982 31.051 91.836 1.00 91.79 ? 91 TYR A CD2 1 ATOM 710 C CE1 . TYR A 1 91 ? -29.528 30.118 92.348 1.00 90.54 ? 91 TYR A CE1 1 ATOM 711 C CE2 . TYR A 1 91 ? -27.288 30.537 93.084 1.00 92.90 ? 91 TYR A CE2 1 ATOM 712 C CZ . TYR A 1 91 ? -28.563 30.072 93.333 1.00 91.78 ? 91 TYR A CZ 1 ATOM 713 O OH . TYR A 1 91 ? -28.875 29.561 94.569 1.00 93.80 ? 91 TYR A OH 1 ATOM 714 N N . PRO A 1 92 ? -28.669 28.685 88.006 1.00 83.37 ? 92 PRO A N 1 ATOM 715 C CA . PRO A 1 92 ? -29.764 28.005 87.312 1.00 81.52 ? 92 PRO A CA 1 ATOM 716 C C . PRO A 1 92 ? -31.140 28.545 87.672 1.00 80.37 ? 92 PRO A C 1 ATOM 717 O O . PRO A 1 92 ? -31.335 29.079 88.761 1.00 81.43 ? 92 PRO A O 1 ATOM 718 C CB . PRO A 1 92 ? -29.632 26.556 87.779 1.00 82.36 ? 92 PRO A CB 1 ATOM 719 C CG . PRO A 1 92 ? -28.973 26.650 89.108 1.00 84.40 ? 92 PRO A CG 1 ATOM 720 C CD . PRO A 1 92 ? -28.035 27.821 89.016 1.00 85.25 ? 92 PRO A CD 1 ATOM 721 N N . GLY A 1 93 ? -32.084 28.405 86.751 1.00 80.10 ? 93 GLY A N 1 ATOM 722 C CA . GLY A 1 93 ? -33.449 28.842 86.995 1.00 79.23 ? 93 GLY A CA 1 ATOM 723 C C . GLY A 1 93 ? -34.325 28.825 85.758 1.00 77.86 ? 93 GLY A C 1 ATOM 724 O O . GLY A 1 93 ? -34.215 27.929 84.914 1.00 76.56 ? 93 GLY A O 1 ATOM 725 N N . ASP A 1 94 ? -35.219 29.809 85.686 1.00 77.45 ? 94 ASP A N 1 ATOM 726 C CA . ASP A 1 94 ? -36.078 30.031 84.529 1.00 76.04 ? 94 ASP A CA 1 ATOM 727 C C . ASP A 1 94 ? -36.176 31.521 84.311 1.00 75.49 ? 94 ASP A C 1 ATOM 728 O O . ASP A 1 94 ? -35.935 32.311 85.229 1.00 76.56 ? 94 ASP A O 1 ATOM 729 C CB . ASP A 1 94 ? -37.482 29.487 84.763 1.00 75.63 ? 94 ASP A CB 1 ATOM 730 C CG . ASP A 1 94 ? -37.498 27.996 85.003 1.00 77.59 ? 94 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 94 ? -37.145 27.238 84.077 1.00 78.64 ? 94 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 94 ? -37.868 27.577 86.122 1.00 80.73 ? 94 ASP A OD2 1 ATOM 733 N N . PHE A 1 95 ? -36.519 31.896 83.086 1.00 73.70 ? 95 PHE A N 1 ATOM 734 C CA . PHE A 1 95 ? -36.792 33.278 82.747 1.00 71.64 ? 95 PHE A CA 1 ATOM 735 C C . PHE A 1 95 ? -38.226 33.277 82.262 1.00 70.27 ? 95 PHE A C 1 ATOM 736 O O . PHE A 1 95 ? -38.528 32.751 81.190 1.00 69.65 ? 95 PHE A O 1 ATOM 737 C CB . PHE A 1 95 ? -35.837 33.752 81.662 1.00 71.34 ? 95 PHE A CB 1 ATOM 738 C CG . PHE A 1 95 ? -35.727 35.242 81.555 1.00 71.52 ? 95 PHE A CG 1 ATOM 739 C CD1 . PHE A 1 95 ? -36.843 36.022 81.301 1.00 70.80 ? 95 PHE A CD1 1 ATOM 740 C CD2 . PHE A 1 95 ? -34.496 35.865 81.687 1.00 72.60 ? 95 PHE A CD2 1 ATOM 741 C CE1 . PHE A 1 95 ? -36.734 37.394 81.191 1.00 71.39 ? 95 PHE A CE1 1 ATOM 742 C CE2 . PHE A 1 95 ? -34.382 37.235 81.579 1.00 73.03 ? 95 PHE A CE2 1 ATOM 743 C CZ . PHE A 1 95 ? -35.503 38.002 81.335 1.00 72.81 ? 95 PHE A CZ 1 ATOM 744 N N . ASN A 1 96 ? -39.110 33.842 83.074 1.00 69.85 ? 96 ASN A N 1 ATOM 745 C CA . ASN A 1 96 ? -40.539 33.796 82.812 1.00 68.37 ? 96 ASN A CA 1 ATOM 746 C C . ASN A 1 96 ? -40.917 34.591 81.559 1.00 66.74 ? 96 ASN A C 1 ATOM 747 O O . ASN A 1 96 ? -40.424 35.705 81.345 1.00 65.95 ? 96 ASN A O 1 ATOM 748 C CB . ASN A 1 96 ? -41.294 34.326 84.032 1.00 69.54 ? 96 ASN A CB 1 ATOM 749 C CG . ASN A 1 96 ? -42.770 33.987 83.998 1.00 69.76 ? 96 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 96 ? -43.156 32.812 84.045 1.00 68.82 ? 96 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 96 ? -43.608 35.019 83.932 1.00 70.46 ? 96 ASN A ND2 1 ATOM 752 N N . ASP A 1 97 ? -41.793 34.006 80.742 1.00 65.33 ? 97 ASP A N 1 ATOM 753 C CA . ASP A 1 97 ? -42.238 34.604 79.476 1.00 64.62 ? 97 ASP A CA 1 ATOM 754 C C . ASP A 1 97 ? -41.067 35.095 78.619 1.00 63.22 ? 97 ASP A C 1 ATOM 755 O O . ASP A 1 97 ? -41.105 36.185 78.047 1.00 62.59 ? 97 ASP A O 1 ATOM 756 C CB . ASP A 1 97 ? -43.255 35.729 79.743 1.00 66.64 ? 97 ASP A CB 1 ATOM 757 C CG . ASP A 1 97 ? -44.667 35.201 79.980 1.00 67.42 ? 97 ASP A CG 1 ATOM 758 O OD1 . ASP A 1 97 ? -45.028 34.181 79.357 1.00 68.46 ? 97 ASP A OD1 1 ATOM 759 O OD2 . ASP A 1 97 ? -45.418 35.810 80.773 1.00 68.72 ? 97 ASP A OD2 1 ATOM 760 N N . TYR A 1 98 ? -40.033 34.264 78.532 1.00 62.51 ? 98 TYR A N 1 ATOM 761 C CA . TYR A 1 98 ? -38.787 34.614 77.854 1.00 62.88 ? 98 TYR A CA 1 ATOM 762 C C . TYR A 1 98 ? -39.004 34.853 76.355 1.00 61.45 ? 98 TYR A C 1 ATOM 763 O O . TYR A 1 98 ? -38.455 35.787 75.770 1.00 61.77 ? 98 TYR A O 1 ATOM 764 C CB . TYR A 1 98 ? -37.768 33.481 78.082 1.00 63.87 ? 98 TYR A CB 1 ATOM 765 C CG . TYR A 1 98 ? -36.335 33.738 77.617 1.00 65.18 ? 98 TYR A CG 1 ATOM 766 C CD1 . TYR A 1 98 ? -35.720 34.982 77.797 1.00 65.72 ? 98 TYR A CD1 1 ATOM 767 C CD2 . TYR A 1 98 ? -35.579 32.711 77.032 1.00 64.74 ? 98 TYR A CD2 1 ATOM 768 C CE1 . TYR A 1 98 ? -34.414 35.201 77.380 1.00 66.54 ? 98 TYR A CE1 1 ATOM 769 C CE2 . TYR A 1 98 ? -34.273 32.922 76.619 1.00 65.81 ? 98 TYR A CE2 1 ATOM 770 C CZ . TYR A 1 98 ? -33.692 34.167 76.796 1.00 67.00 ? 98 TYR A CZ 1 ATOM 771 O OH . TYR A 1 98 ? -32.389 34.385 76.389 1.00 68.83 ? 98 TYR A OH 1 ATOM 772 N N . GLU A 1 99 ? -39.824 34.008 75.746 1.00 60.51 ? 99 GLU A N 1 ATOM 773 C CA . GLU A 1 99 ? -40.036 34.044 74.311 1.00 59.75 ? 99 GLU A CA 1 ATOM 774 C C . GLU A 1 99 ? -40.879 35.243 73.929 1.00 59.68 ? 99 GLU A C 1 ATOM 775 O O . GLU A 1 99 ? -40.667 35.847 72.880 1.00 59.89 ? 99 GLU A O 1 ATOM 776 C CB . GLU A 1 99 ? -40.703 32.758 73.830 1.00 59.49 ? 99 GLU A CB 1 ATOM 777 C CG . GLU A 1 99 ? -39.807 31.523 73.898 1.00 60.21 ? 99 GLU A CG 1 ATOM 778 C CD . GLU A 1 99 ? -39.551 31.035 75.316 1.00 61.26 ? 99 GLU A CD 1 ATOM 779 O OE1 . GLU A 1 99 ? -40.463 31.130 76.167 1.00 62.06 ? 99 GLU A OE1 1 ATOM 780 O OE2 . GLU A 1 99 ? -38.434 30.551 75.576 1.00 61.02 ? 99 GLU A OE2 1 ATOM 781 N N . GLU A 1 100 ? -41.835 35.591 74.784 1.00 59.81 ? 100 GLU A N 1 ATOM 782 C CA . GLU A 1 100 ? -42.640 36.786 74.569 1.00 59.50 ? 100 GLU A CA 1 ATOM 783 C C . GLU A 1 100 ? -41.769 38.035 74.683 1.00 59.75 ? 100 GLU A C 1 ATOM 784 O O . GLU A 1 100 ? -42.019 39.047 74.027 1.00 59.93 ? 100 GLU A O 1 ATOM 785 C CB . GLU A 1 100 ? -43.821 36.831 75.547 1.00 59.63 ? 100 GLU A CB 1 ATOM 786 C CG . GLU A 1 100 ? -44.978 35.917 75.150 1.00 59.45 ? 100 GLU A CG 1 ATOM 787 C CD . GLU A 1 100 ? -45.730 36.407 73.922 1.00 59.62 ? 100 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 100 ? -46.109 37.597 73.886 1.00 60.62 ? 100 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 100 ? -45.954 35.609 72.984 1.00 59.61 ? 100 GLU A OE2 1 ATOM 790 N N . LEU A 1 101 ? -40.736 37.955 75.512 1.00 60.08 ? 101 LEU A N 1 ATOM 791 C CA . LEU A 1 101 ? -39.821 39.069 75.679 1.00 60.59 ? 101 LEU A CA 1 ATOM 792 C C . LEU A 1 101 ? -38.909 39.168 74.468 1.00 59.71 ? 101 LEU A C 1 ATOM 793 O O . LEU A 1 101 ? -38.731 40.256 73.917 1.00 58.60 ? 101 LEU A O 1 ATOM 794 C CB . LEU A 1 101 ? -38.991 38.914 76.953 1.00 61.32 ? 101 LEU A CB 1 ATOM 795 C CG . LEU A 1 101 ? -37.980 40.036 77.221 1.00 62.78 ? 101 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 101 ? -38.640 41.408 77.283 1.00 62.42 ? 101 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 101 ? -37.232 39.732 78.513 1.00 64.43 ? 101 LEU A CD2 1 ATOM 798 N N . LYS A 1 102 ? -38.327 38.038 74.072 1.00 58.53 ? 102 LYS A N 1 ATOM 799 C CA . LYS A 1 102 ? -37.505 37.993 72.865 1.00 59.05 ? 102 LYS A CA 1 ATOM 800 C C . LYS A 1 102 ? -38.270 38.536 71.661 1.00 58.61 ? 102 LYS A C 1 ATOM 801 O O . LYS A 1 102 ? -37.720 39.260 70.832 1.00 58.45 ? 102 LYS A O 1 ATOM 802 C CB . LYS A 1 102 ? -37.039 36.571 72.578 1.00 59.00 ? 102 LYS A CB 1 ATOM 803 C CG . LYS A 1 102 ? -35.936 36.106 73.504 1.00 61.19 ? 102 LYS A CG 1 ATOM 804 C CD . LYS A 1 102 ? -35.598 34.640 73.281 1.00 61.72 ? 102 LYS A CD 1 ATOM 805 C CE . LYS A 1 102 ? -34.343 34.464 72.443 1.00 62.70 ? 102 LYS A CE 1 ATOM 806 N NZ . LYS A 1 102 ? -34.029 33.022 72.257 1.00 63.00 ? 102 LYS A NZ 1 ATOM 807 N N . HIS A 1 103 ? -39.547 38.193 71.577 1.00 58.64 ? 103 HIS A N 1 ATOM 808 C CA . HIS A 1 103 ? -40.393 38.716 70.520 1.00 59.19 ? 103 HIS A CA 1 ATOM 809 C C . HIS A 1 103 ? -40.513 40.238 70.600 1.00 60.48 ? 103 HIS A C 1 ATOM 810 O O . HIS A 1 103 ? -40.563 40.911 69.584 1.00 62.12 ? 103 HIS A O 1 ATOM 811 C CB . HIS A 1 103 ? -41.783 38.068 70.558 1.00 58.80 ? 103 HIS A CB 1 ATOM 812 C CG . HIS A 1 103 ? -42.723 38.612 69.526 1.00 58.31 ? 103 HIS A CG 1 ATOM 813 N ND1 . HIS A 1 103 ? -42.792 38.109 68.245 1.00 57.59 ? 103 HIS A ND1 1 ATOM 814 C CD2 . HIS A 1 103 ? -43.602 39.639 69.577 1.00 57.95 ? 103 HIS A CD2 1 ATOM 815 C CE1 . HIS A 1 103 ? -43.682 38.797 67.554 1.00 56.92 ? 103 HIS A CE1 1 ATOM 816 N NE2 . HIS A 1 103 ? -44.189 39.729 68.340 1.00 57.14 ? 103 HIS A NE2 1 ATOM 817 N N . LEU A 1 104 ? -40.563 40.772 71.806 1.00 61.96 ? 104 LEU A N 1 ATOM 818 C CA . LEU A 1 104 ? -40.641 42.210 72.000 1.00 64.58 ? 104 LEU A CA 1 ATOM 819 C C . LEU A 1 104 ? -39.409 42.911 71.422 1.00 67.00 ? 104 LEU A C 1 ATOM 820 O O . LEU A 1 104 ? -39.508 44.017 70.897 1.00 67.92 ? 104 LEU A O 1 ATOM 821 C CB . LEU A 1 104 ? -40.760 42.520 73.497 1.00 66.22 ? 104 LEU A CB 1 ATOM 822 C CG . LEU A 1 104 ? -41.751 43.587 73.957 1.00 67.00 ? 104 LEU A CG 1 ATOM 823 C CD1 . LEU A 1 104 ? -43.176 43.224 73.561 1.00 66.16 ? 104 LEU A CD1 1 ATOM 824 C CD2 . LEU A 1 104 ? -41.641 43.728 75.466 1.00 67.65 ? 104 LEU A CD2 1 ATOM 825 N N . LEU A 1 105 ? -38.256 42.251 71.533 1.00 69.16 ? 105 LEU A N 1 ATOM 826 C CA . LEU A 1 105 ? -36.971 42.774 71.050 1.00 70.27 ? 105 LEU A CA 1 ATOM 827 C C . LEU A 1 105 ? -36.880 42.890 69.552 1.00 70.27 ? 105 LEU A C 1 ATOM 828 O O . LEU A 1 105 ? -36.073 43.663 69.047 1.00 73.07 ? 105 LEU A O 1 ATOM 829 C CB . LEU A 1 105 ? -35.821 41.860 71.457 1.00 70.18 ? 105 LEU A CB 1 ATOM 830 C CG . LEU A 1 105 ? -35.201 42.001 72.828 1.00 70.88 ? 105 LEU A CG 1 ATOM 831 C CD1 . LEU A 1 105 ? -33.991 41.084 72.894 1.00 71.60 ? 105 LEU A CD1 1 ATOM 832 C CD2 . LEU A 1 105 ? -34.797 43.441 73.087 1.00 73.47 ? 105 LEU A CD2 1 ATOM 833 N N . SER A 1 106 ? -37.655 42.091 68.836 1.00 77.51 ? 106 SER A N 1 ATOM 834 C CA . SER A 1 106 ? -37.701 42.218 67.388 1.00 79.79 ? 106 SER A CA 1 ATOM 835 C C . SER A 1 106 ? -38.263 43.586 66.959 1.00 81.27 ? 106 SER A C 1 ATOM 836 O O . SER A 1 106 ? -38.094 43.994 65.815 1.00 82.24 ? 106 SER A O 1 ATOM 837 C CB . SER A 1 106 ? -38.524 41.080 66.783 1.00 79.57 ? 106 SER A CB 1 ATOM 838 O OG . SER A 1 106 ? -39.895 41.215 67.108 1.00 79.94 ? 106 SER A OG 1 ATOM 839 N N . ARG A 1 107 ? -38.934 44.275 67.881 1.00 83.14 ? 107 ARG A N 1 ATOM 840 C CA . ARG A 1 107 ? -39.442 45.636 67.662 1.00 86.92 ? 107 ARG A CA 1 ATOM 841 C C . ARG A 1 107 ? -38.525 46.728 68.245 1.00 85.36 ? 107 ARG A C 1 ATOM 842 O O . ARG A 1 107 ? -38.886 47.903 68.217 1.00 85.34 ? 107 ARG A O 1 ATOM 843 C CB . ARG A 1 107 ? -40.837 45.788 68.298 1.00 90.03 ? 107 ARG A CB 1 ATOM 844 C CG . ARG A 1 107 ? -41.990 45.202 67.497 1.00 93.57 ? 107 ARG A CG 1 ATOM 845 C CD . ARG A 1 107 ? -42.775 46.252 66.704 1.00 99.46 ? 107 ARG A CD 1 ATOM 846 N NE . ARG A 1 107 ? -44.206 45.918 66.605 1.00 103.43 ? 107 ARG A NE 1 ATOM 847 C CZ . ARG A 1 107 ? -45.075 46.459 65.742 1.00 107.50 ? 107 ARG A CZ 1 ATOM 848 N NH1 . ARG A 1 107 ? -44.693 47.382 64.857 1.00 109.66 ? 107 ARG A NH1 1 ATOM 849 N NH2 . ARG A 1 107 ? -46.348 46.066 65.762 1.00 108.53 ? 107 ARG A NH2 1 ATOM 850 N N . ILE A 1 108 ? -37.354 46.349 68.763 1.00 82.82 ? 108 ILE A N 1 ATOM 851 C CA . ILE A 1 108 ? -36.478 47.291 69.464 1.00 82.57 ? 108 ILE A CA 1 ATOM 852 C C . ILE A 1 108 ? -35.074 47.358 68.859 1.00 82.73 ? 108 ILE A C 1 ATOM 853 O O . ILE A 1 108 ? -34.454 46.330 68.588 1.00 81.66 ? 108 ILE A O 1 ATOM 854 C CB . ILE A 1 108 ? -36.341 46.933 70.961 1.00 81.11 ? 108 ILE A CB 1 ATOM 855 C CG1 . ILE A 1 108 ? -37.714 46.884 71.633 1.00 79.74 ? 108 ILE A CG1 1 ATOM 856 C CG2 . ILE A 1 108 ? -35.456 47.956 71.667 1.00 82.00 ? 108 ILE A CG2 1 ATOM 857 C CD1 . ILE A 1 108 ? -37.677 46.452 73.086 1.00 78.18 ? 108 ILE A CD1 1 ATOM 858 N N . ASN A 1 109 ? -34.573 48.581 68.683 1.00 83.73 ? 109 ASN A N 1 ATOM 859 C CA . ASN A 1 109 ? -33.231 48.810 68.156 1.00 84.62 ? 109 ASN A CA 1 ATOM 860 C C . ASN A 1 109 ? -32.235 49.355 69.170 1.00 84.35 ? 109 ASN A C 1 ATOM 861 O O . ASN A 1 109 ? -31.032 49.250 68.945 1.00 84.63 ? 109 ASN A O 1 ATOM 862 C CB . ASN A 1 109 ? -33.294 49.771 66.978 1.00 87.23 ? 109 ASN A CB 1 ATOM 863 C CG . ASN A 1 109 ? -34.047 49.191 65.807 1.00 87.52 ? 109 ASN A CG 1 ATOM 864 O OD1 . ASN A 1 109 ? -33.567 48.274 65.141 1.00 87.62 ? 109 ASN A OD1 1 ATOM 865 N ND2 . ASN A 1 109 ? -35.234 49.720 65.549 1.00 88.21 ? 109 ASN A ND2 1 ATOM 866 N N . HIS A 1 110 ? -32.714 49.951 70.263 1.00 83.12 ? 110 HIS A N 1 ATOM 867 C CA . HIS A 1 110 ? -31.808 50.510 71.268 1.00 83.52 ? 110 HIS A CA 1 ATOM 868 C C . HIS A 1 110 ? -32.407 50.595 72.672 1.00 81.89 ? 110 HIS A C 1 ATOM 869 O O . HIS A 1 110 ? -33.527 51.077 72.876 1.00 80.16 ? 110 HIS A O 1 ATOM 870 C CB . HIS A 1 110 ? -31.323 51.897 70.820 1.00 86.51 ? 110 HIS A CB 1 ATOM 871 C CG . HIS A 1 110 ? -30.140 52.411 71.587 1.00 87.54 ? 110 HIS A CG 1 ATOM 872 N ND1 . HIS A 1 110 ? -29.887 53.757 71.746 1.00 89.58 ? 110 HIS A ND1 1 ATOM 873 C CD2 . HIS A 1 110 ? -29.144 51.760 72.234 1.00 86.75 ? 110 HIS A CD2 1 ATOM 874 C CE1 . HIS A 1 110 ? -28.783 53.911 72.454 1.00 90.62 ? 110 HIS A CE1 1 ATOM 875 N NE2 . HIS A 1 110 ? -28.314 52.715 72.764 1.00 88.47 ? 110 HIS A NE2 1 ATOM 876 N N . PHE A 1 111 ? -31.633 50.109 73.634 1.00 82.09 ? 111 PHE A N 1 ATOM 877 C CA . PHE A 1 111 ? -31.937 50.268 75.046 1.00 82.53 ? 111 PHE A CA 1 ATOM 878 C C . PHE A 1 111 ? -30.981 51.301 75.620 1.00 85.14 ? 111 PHE A C 1 ATOM 879 O O . PHE A 1 111 ? -29.832 51.371 75.197 1.00 86.69 ? 111 PHE A O 1 ATOM 880 C CB . PHE A 1 111 ? -31.707 48.962 75.809 1.00 80.75 ? 111 PHE A CB 1 ATOM 881 C CG . PHE A 1 111 ? -32.808 47.947 75.670 1.00 78.04 ? 111 PHE A CG 1 ATOM 882 C CD1 . PHE A 1 111 ? -34.140 48.291 75.873 1.00 77.52 ? 111 PHE A CD1 1 ATOM 883 C CD2 . PHE A 1 111 ? -32.499 46.625 75.404 1.00 76.39 ? 111 PHE A CD2 1 ATOM 884 C CE1 . PHE A 1 111 ? -35.137 47.337 75.778 1.00 75.04 ? 111 PHE A CE1 1 ATOM 885 C CE2 . PHE A 1 111 ? -33.491 45.673 75.309 1.00 74.49 ? 111 PHE A CE2 1 ATOM 886 C CZ . PHE A 1 111 ? -34.812 46.028 75.497 1.00 73.89 ? 111 PHE A CZ 1 ATOM 887 N N . GLU A 1 112 ? -31.448 52.081 76.590 1.00 86.45 ? 112 GLU A N 1 ATOM 888 C CA . GLU A 1 112 ? -30.574 52.953 77.375 1.00 89.52 ? 112 GLU A CA 1 ATOM 889 C C . GLU A 1 112 ? -30.745 52.548 78.845 1.00 87.97 ? 112 GLU A C 1 ATOM 890 O O . GLU A 1 112 ? -31.801 52.755 79.434 1.00 86.42 ? 112 GLU A O 1 ATOM 891 C CB . GLU A 1 112 ? -30.929 54.431 77.130 1.00 92.85 ? 112 GLU A CB 1 ATOM 892 C CG . GLU A 1 112 ? -29.757 55.412 77.148 1.00 96.27 ? 112 GLU A CG 1 ATOM 893 C CD . GLU A 1 112 ? -29.507 56.018 78.518 1.00 99.47 ? 112 GLU A CD 1 ATOM 894 O OE1 . GLU A 1 112 ? -29.330 55.256 79.492 1.00 100.12 ? 112 GLU A OE1 1 ATOM 895 O OE2 . GLU A 1 112 ? -29.494 57.264 78.632 1.00 103.01 ? 112 GLU A OE2 1 ATOM 896 N N . LYS A 1 113 ? -29.711 51.940 79.420 1.00 87.68 ? 113 LYS A N 1 ATOM 897 C CA . LYS A 1 113 ? -29.775 51.416 80.789 1.00 86.95 ? 113 LYS A CA 1 ATOM 898 C C . LYS A 1 113 ? -29.763 52.534 81.829 1.00 88.48 ? 113 LYS A C 1 ATOM 899 O O . LYS A 1 113 ? -28.910 53.410 81.766 1.00 90.94 ? 113 LYS A O 1 ATOM 900 C CB . LYS A 1 113 ? -28.592 50.482 81.024 1.00 86.60 ? 113 LYS A CB 1 ATOM 901 C CG . LYS A 1 113 ? -28.468 49.931 82.433 1.00 86.39 ? 113 LYS A CG 1 ATOM 902 C CD . LYS A 1 113 ? -28.072 48.459 82.423 1.00 85.38 ? 113 LYS A CD 1 ATOM 903 C CE . LYS A 1 113 ? -26.754 48.175 81.711 1.00 86.13 ? 113 LYS A CE 1 ATOM 904 N NZ . LYS A 1 113 ? -26.609 46.710 81.464 1.00 84.83 ? 113 LYS A NZ 1 ATOM 905 N N . ILE A 1 114 ? -30.707 52.515 82.771 1.00 87.93 ? 114 ILE A N 1 ATOM 906 C CA . ILE A 1 114 ? -30.659 53.448 83.903 1.00 91.40 ? 114 ILE A CA 1 ATOM 907 C C . ILE A 1 114 ? -30.973 52.803 85.249 1.00 91.17 ? 114 ILE A C 1 ATOM 908 O O . ILE A 1 114 ? -31.722 51.827 85.332 1.00 89.45 ? 114 ILE A O 1 ATOM 909 C CB . ILE A 1 114 ? -31.578 54.681 83.729 1.00 93.14 ? 114 ILE A CB 1 ATOM 910 C CG1 . ILE A 1 114 ? -33.039 54.269 83.511 1.00 91.85 ? 114 ILE A CG1 1 ATOM 911 C CG2 . ILE A 1 114 ? -31.070 55.581 82.604 1.00 94.89 ? 114 ILE A CG2 1 ATOM 912 C CD1 . ILE A 1 114 ? -34.016 55.372 83.874 1.00 93.23 ? 114 ILE A CD1 1 ATOM 913 N N . GLN A 1 115 ? -30.400 53.386 86.298 1.00 92.43 ? 115 GLN A N 1 ATOM 914 C CA . GLN A 1 115 ? -30.521 52.869 87.651 1.00 92.35 ? 115 GLN A CA 1 ATOM 915 C C . GLN A 1 115 ? -31.795 53.389 88.303 1.00 92.16 ? 115 GLN A C 1 ATOM 916 O O . GLN A 1 115 ? -31.966 54.596 88.454 1.00 92.61 ? 115 GLN A O 1 ATOM 917 C CB . GLN A 1 115 ? -29.307 53.305 88.465 1.00 95.04 ? 115 GLN A CB 1 ATOM 918 C CG . GLN A 1 115 ? -29.206 52.676 89.843 1.00 95.37 ? 115 GLN A CG 1 ATOM 919 C CD . GLN A 1 115 ? -28.110 53.306 90.675 1.00 97.65 ? 115 GLN A CD 1 ATOM 920 O OE1 . GLN A 1 115 ? -27.110 52.665 90.988 1.00 98.14 ? 115 GLN A OE1 1 ATOM 921 N NE2 . GLN A 1 115 ? -28.290 54.574 91.030 1.00 99.16 ? 115 GLN A NE2 1 ATOM 922 N N . ILE A 1 116 ? -32.685 52.480 88.692 1.00 91.08 ? 116 ILE A N 1 ATOM 923 C CA . ILE A 1 116 ? -33.949 52.875 89.338 1.00 91.82 ? 116 ILE A CA 1 ATOM 924 C C . ILE A 1 116 ? -33.900 52.714 90.859 1.00 93.73 ? 116 ILE A C 1 ATOM 925 O O . ILE A 1 116 ? -34.483 53.519 91.594 1.00 95.23 ? 116 ILE A O 1 ATOM 926 C CB . ILE A 1 116 ? -35.185 52.126 88.775 1.00 88.44 ? 116 ILE A CB 1 ATOM 927 C CG1 . ILE A 1 116 ? -34.845 50.665 88.461 1.00 86.16 ? 116 ILE A CG1 1 ATOM 928 C CG2 . ILE A 1 116 ? -35.741 52.858 87.554 1.00 87.70 ? 116 ILE A CG2 1 ATOM 929 C CD1 . ILE A 1 116 ? -36.047 49.754 88.497 1.00 84.33 ? 116 ILE A CD1 1 ATOM 930 N N . ILE A 1 117 ? -33.215 51.677 91.330 1.00 93.84 ? 117 ILE A N 1 ATOM 931 C CA . ILE A 1 117 ? -32.993 51.507 92.760 1.00 95.48 ? 117 ILE A CA 1 ATOM 932 C C . ILE A 1 117 ? -31.504 51.314 93.019 1.00 97.00 ? 117 ILE A C 1 ATOM 933 O O . ILE A 1 117 ? -30.936 50.298 92.612 1.00 96.44 ? 117 ILE A O 1 ATOM 934 C CB . ILE A 1 117 ? -33.775 50.317 93.325 1.00 93.96 ? 117 ILE A CB 1 ATOM 935 C CG1 . ILE A 1 117 ? -35.262 50.443 92.961 1.00 92.12 ? 117 ILE A CG1 1 ATOM 936 C CG2 . ILE A 1 117 ? -33.578 50.247 94.835 1.00 95.83 ? 117 ILE A CG2 1 ATOM 937 C CD1 . ILE A 1 117 ? -36.126 49.303 93.460 1.00 90.49 ? 117 ILE A CD1 1 ATOM 938 N N . PRO A 1 118 ? -30.865 52.302 93.674 1.00 99.52 ? 118 PRO A N 1 ATOM 939 C CA . PRO A 1 118 ? -29.441 52.204 94.001 1.00 101.56 ? 118 PRO A CA 1 ATOM 940 C C . PRO A 1 118 ? -29.111 51.092 94.997 1.00 102.16 ? 118 PRO A C 1 ATOM 941 O O . PRO A 1 118 ? -29.865 50.850 95.945 1.00 102.62 ? 118 PRO A O 1 ATOM 942 C CB . PRO A 1 118 ? -29.119 53.580 94.600 1.00 104.44 ? 118 PRO A CB 1 ATOM 943 C CG . PRO A 1 118 ? -30.148 54.499 94.030 1.00 103.24 ? 118 PRO A CG 1 ATOM 944 C CD . PRO A 1 118 ? -31.386 53.667 93.893 1.00 100.93 ? 118 PRO A CD 1 ATOM 945 N N . LYS A 1 119 ? -27.984 50.428 94.771 1.00 102.42 ? 119 LYS A N 1 ATOM 946 C CA . LYS A 1 119 ? -27.546 49.338 95.628 1.00 103.22 ? 119 LYS A CA 1 ATOM 947 C C . LYS A 1 119 ? -27.268 49.886 97.027 1.00 107.23 ? 119 LYS A C 1 ATOM 948 O O . LYS A 1 119 ? -27.535 49.225 98.033 1.00 109.45 ? 119 LYS A O 1 ATOM 949 C CB . LYS A 1 119 ? -26.291 48.689 95.042 1.00 103.37 ? 119 LYS A CB 1 ATOM 950 C CG . LYS A 1 119 ? -26.125 47.218 95.365 1.00 102.66 ? 119 LYS A CG 1 ATOM 951 C CD . LYS A 1 119 ? -24.902 46.650 94.665 1.00 103.16 ? 119 LYS A CD 1 ATOM 952 C CE . LYS A 1 119 ? -24.439 45.360 95.324 1.00 103.77 ? 119 LYS A CE 1 ATOM 953 N NZ . LYS A 1 119 ? -23.270 44.760 94.623 1.00 104.16 ? 119 LYS A NZ 1 ATOM 954 N N . SER A 1 120 ? -26.738 51.106 97.081 1.00 109.11 ? 120 SER A N 1 ATOM 955 C CA . SER A 1 120 ? -26.469 51.782 98.347 1.00 111.10 ? 120 SER A CA 1 ATOM 956 C C . SER A 1 120 ? -27.727 51.883 99.192 1.00 111.29 ? 120 SER A C 1 ATOM 957 O O . SER A 1 120 ? -27.671 51.747 100.404 1.00 114.05 ? 120 SER A O 1 ATOM 958 C CB . SER A 1 120 ? -25.938 53.195 98.105 1.00 112.20 ? 120 SER A CB 1 ATOM 959 O OG . SER A 1 120 ? -26.992 54.067 97.733 1.00 110.46 ? 120 SER A OG 1 ATOM 960 N N . SER A 1 121 ? -28.861 52.117 98.542 1.00 109.98 ? 121 SER A N 1 ATOM 961 C CA . SER A 1 121 ? -30.104 52.426 99.251 1.00 110.42 ? 121 SER A CA 1 ATOM 962 C C . SER A 1 121 ? -30.625 51.345 100.207 1.00 109.14 ? 121 SER A C 1 ATOM 963 O O . SER A 1 121 ? -31.458 51.650 101.056 1.00 109.18 ? 121 SER A O 1 ATOM 964 C CB . SER A 1 121 ? -31.224 52.782 98.265 1.00 109.28 ? 121 SER A CB 1 ATOM 965 O OG . SER A 1 121 ? -31.115 54.104 97.784 1.00 111.98 ? 121 SER A OG 1 ATOM 966 N N . TRP A 1 122 ? -30.166 50.100 100.081 1.00 107.59 ? 122 TRP A N 1 ATOM 967 C CA . TRP A 1 122 ? -30.681 49.020 100.934 1.00 107.33 ? 122 TRP A CA 1 ATOM 968 C C . TRP A 1 122 ? -30.017 49.035 102.302 1.00 110.70 ? 122 TRP A C 1 ATOM 969 O O . TRP A 1 122 ? -29.219 48.158 102.632 1.00 112.31 ? 122 TRP A O 1 ATOM 970 C CB . TRP A 1 122 ? -30.503 47.662 100.262 1.00 105.00 ? 122 TRP A CB 1 ATOM 971 C CG . TRP A 1 122 ? -31.293 47.542 99.011 1.00 102.18 ? 122 TRP A CG 1 ATOM 972 C CD1 . TRP A 1 122 ? -30.805 47.419 97.747 1.00 100.92 ? 122 TRP A CD1 1 ATOM 973 C CD2 . TRP A 1 122 ? -32.718 47.560 98.894 1.00 100.65 ? 122 TRP A CD2 1 ATOM 974 N NE1 . TRP A 1 122 ? -31.838 47.340 96.846 1.00 99.49 ? 122 TRP A NE1 1 ATOM 975 C CE2 . TRP A 1 122 ? -33.024 47.429 97.523 1.00 99.00 ? 122 TRP A CE2 1 ATOM 976 C CE3 . TRP A 1 122 ? -33.766 47.661 99.814 1.00 101.03 ? 122 TRP A CE3 1 ATOM 977 C CZ2 . TRP A 1 122 ? -34.335 47.400 97.045 1.00 96.66 ? 122 TRP A CZ2 1 ATOM 978 C CZ3 . TRP A 1 122 ? -35.075 47.640 99.338 1.00 99.72 ? 122 TRP A CZ3 1 ATOM 979 C CH2 . TRP A 1 122 ? -35.344 47.507 97.963 1.00 97.67 ? 122 TRP A CH2 1 ATOM 980 N N . SER A 1 123 ? -30.368 50.038 103.099 1.00 112.63 ? 123 SER A N 1 ATOM 981 C CA . SER A 1 123 ? -29.701 50.290 104.372 1.00 115.71 ? 123 SER A CA 1 ATOM 982 C C . SER A 1 123 ? -30.035 49.231 105.422 1.00 116.71 ? 123 SER A C 1 ATOM 983 O O . SER A 1 123 ? -29.171 48.846 106.203 1.00 119.34 ? 123 SER A O 1 ATOM 984 C CB . SER A 1 123 ? -30.069 51.680 104.894 1.00 117.37 ? 123 SER A CB 1 ATOM 985 O OG . SER A 1 123 ? -31.473 51.821 105.002 1.00 115.81 ? 123 SER A OG 1 ATOM 986 N N . SER A 1 124 ? -31.278 48.753 105.424 1.00 114.53 ? 124 SER A N 1 ATOM 987 C CA . SER A 1 124 ? -31.751 47.802 106.441 1.00 114.24 ? 124 SER A CA 1 ATOM 988 C C . SER A 1 124 ? -31.521 46.332 106.075 1.00 111.82 ? 124 SER A C 1 ATOM 989 O O . SER A 1 124 ? -31.861 45.434 106.849 1.00 111.20 ? 124 SER A O 1 ATOM 990 C CB . SER A 1 124 ? -33.239 48.029 106.695 1.00 113.57 ? 124 SER A CB 1 ATOM 991 O OG . SER A 1 124 ? -33.536 49.411 106.688 1.00 114.94 ? 124 SER A OG 1 ATOM 992 N N . HIS A 1 125 ? -30.965 46.089 104.892 1.00 109.75 ? 125 HIS A N 1 ATOM 993 C CA . HIS A 1 125 ? -30.643 44.737 104.451 1.00 108.18 ? 125 HIS A CA 1 ATOM 994 C C . HIS A 1 125 ? -29.214 44.701 103.932 1.00 109.24 ? 125 HIS A C 1 ATOM 995 O O . HIS A 1 125 ? -28.653 45.733 103.562 1.00 109.91 ? 125 HIS A O 1 ATOM 996 C CB . HIS A 1 125 ? -31.604 44.287 103.348 1.00 104.13 ? 125 HIS A CB 1 ATOM 997 C CG . HIS A 1 125 ? -33.048 44.331 103.743 1.00 103.12 ? 125 HIS A CG 1 ATOM 998 N ND1 . HIS A 1 125 ? -33.794 45.490 103.702 1.00 103.00 ? 125 HIS A ND1 1 ATOM 999 C CD2 . HIS A 1 125 ? -33.886 43.358 104.175 1.00 102.40 ? 125 HIS A CD2 1 ATOM 1000 C CE1 . HIS A 1 125 ? -35.028 45.230 104.097 1.00 102.78 ? 125 HIS A CE1 1 ATOM 1001 N NE2 . HIS A 1 125 ? -35.110 43.944 104.393 1.00 102.44 ? 125 HIS A NE2 1 ATOM 1002 N N . GLU A 1 126 ? -28.623 43.511 103.919 1.00 109.48 ? 126 GLU A N 1 ATOM 1003 C CA . GLU A 1 126 ? -27.303 43.326 103.333 1.00 110.07 ? 126 GLU A CA 1 ATOM 1004 C C . GLU A 1 126 ? -27.473 43.162 101.828 1.00 106.26 ? 126 GLU A C 1 ATOM 1005 O O . GLU A 1 126 ? -28.236 42.311 101.377 1.00 104.53 ? 126 GLU A O 1 ATOM 1006 C CB . GLU A 1 126 ? -26.635 42.092 103.920 1.00 112.36 ? 126 GLU A CB 1 ATOM 1007 C CG . GLU A 1 126 ? -25.287 41.782 103.320 1.00 113.80 ? 126 GLU A CG 1 ATOM 1008 C CD . GLU A 1 126 ? -24.209 42.782 103.703 1.00 118.13 ? 126 GLU A CD 1 ATOM 1009 O OE1 . GLU A 1 126 ? -24.206 43.262 104.865 1.00 119.88 ? 126 GLU A OE1 1 ATOM 1010 O OE2 . GLU A 1 126 ? -23.349 43.072 102.839 1.00 118.86 ? 126 GLU A OE2 1 ATOM 1011 N N . ALA A 1 127 ? -26.765 43.974 101.051 1.00 105.01 ? 127 ALA A N 1 ATOM 1012 C CA . ALA A 1 127 ? -26.920 43.972 99.598 1.00 101.06 ? 127 ALA A CA 1 ATOM 1013 C C . ALA A 1 127 ? -25.666 43.534 98.844 1.00 101.02 ? 127 ALA A C 1 ATOM 1014 O O . ALA A 1 127 ? -25.693 43.440 97.616 1.00 100.25 ? 127 ALA A O 1 ATOM 1015 C CB . ALA A 1 127 ? -27.353 45.353 99.127 1.00 100.41 ? 127 ALA A CB 1 ATOM 1016 N N . SER A 1 128 ? -24.579 43.251 99.559 1.00 103.06 ? 128 SER A N 1 ATOM 1017 C CA . SER A 1 128 ? -23.286 43.007 98.916 1.00 103.17 ? 128 SER A CA 1 ATOM 1018 C C . SER A 1 128 ? -22.723 41.609 99.148 1.00 103.14 ? 128 SER A C 1 ATOM 1019 O O . SER A 1 128 ? -21.604 41.316 98.730 1.00 103.47 ? 128 SER A O 1 ATOM 1020 C CB . SER A 1 128 ? -22.281 44.072 99.359 1.00 106.24 ? 128 SER A CB 1 ATOM 1021 O OG . SER A 1 128 ? -22.448 45.242 98.580 1.00 105.54 ? 128 SER A OG 1 ATOM 1022 N N . LEU A 1 129 ? -23.503 40.746 99.790 1.00 102.79 ? 129 LEU A N 1 ATOM 1023 C CA . LEU A 1 129 ? -23.110 39.358 99.972 1.00 103.79 ? 129 LEU A CA 1 ATOM 1024 C C . LEU A 1 129 ? -23.981 38.452 99.110 1.00 101.34 ? 129 LEU A C 1 ATOM 1025 O O . LEU A 1 129 ? -23.920 37.232 99.236 1.00 101.88 ? 129 LEU A O 1 ATOM 1026 C CB . LEU A 1 129 ? -23.227 38.946 101.440 1.00 107.13 ? 129 LEU A CB 1 ATOM 1027 C CG . LEU A 1 129 ? -22.977 40.025 102.497 1.00 110.07 ? 129 LEU A CG 1 ATOM 1028 C CD1 . LEU A 1 129 ? -23.413 39.550 103.877 1.00 112.10 ? 129 LEU A CD1 1 ATOM 1029 C CD2 . LEU A 1 129 ? -21.537 40.496 102.556 1.00 112.19 ? 129 LEU A CD2 1 ATOM 1030 N N . GLY A 1 130 ? -24.779 39.052 98.226 1.00 99.78 ? 130 GLY A N 1 ATOM 1031 C CA . GLY A 1 130 ? -25.686 38.313 97.351 1.00 96.58 ? 130 GLY A CA 1 ATOM 1032 C C . GLY A 1 130 ? -25.023 37.777 96.094 1.00 96.03 ? 130 GLY A C 1 ATOM 1033 O O . GLY A 1 130 ? -25.257 38.284 94.986 1.00 92.99 ? 130 GLY A O 1 ATOM 1034 N N . VAL A 1 131 ? -24.206 36.739 96.264 1.00 97.89 ? 131 VAL A N 1 ATOM 1035 C CA . VAL A 1 131 ? -23.452 36.155 95.157 1.00 97.57 ? 131 VAL A CA 1 ATOM 1036 C C . VAL A 1 131 ? -23.406 34.632 95.241 1.00 97.43 ? 131 VAL A C 1 ATOM 1037 O O . VAL A 1 131 ? -23.769 34.042 96.258 1.00 98.52 ? 131 VAL A O 1 ATOM 1038 C CB . VAL A 1 131 ? -22.010 36.709 95.123 1.00 100.26 ? 131 VAL A CB 1 ATOM 1039 C CG1 . VAL A 1 131 ? -22.021 38.227 95.258 1.00 101.27 ? 131 VAL A CG1 1 ATOM 1040 C CG2 . VAL A 1 131 ? -21.156 36.089 96.223 1.00 102.43 ? 131 VAL A CG2 1 ATOM 1041 N N . SER A 1 132 ? -22.945 34.006 94.163 1.00 96.84 ? 132 SER A N 1 ATOM 1042 C CA . SER A 1 132 ? -22.852 32.552 94.086 1.00 96.38 ? 132 SER A CA 1 ATOM 1043 C C . SER A 1 132 ? -21.640 32.117 93.284 1.00 97.43 ? 132 SER A C 1 ATOM 1044 O O . SER A 1 132 ? -21.127 32.866 92.457 1.00 96.74 ? 132 SER A O 1 ATOM 1045 C CB . SER A 1 132 ? -24.104 31.970 93.437 1.00 93.42 ? 132 SER A CB 1 ATOM 1046 O OG . SER A 1 132 ? -23.885 30.620 93.051 1.00 92.55 ? 132 SER A OG 1 ATOM 1047 N N . SER A 1 133 ? -21.199 30.889 93.526 1.00 98.57 ? 133 SER A N 1 ATOM 1048 C CA . SER A 1 133 ? -20.056 30.331 92.821 1.00 98.95 ? 133 SER A CA 1 ATOM 1049 C C . SER A 1 133 ? -20.427 30.003 91.374 1.00 97.07 ? 133 SER A C 1 ATOM 1050 O O . SER A 1 133 ? -19.549 29.896 90.524 1.00 97.24 ? 133 SER A O 1 ATOM 1051 C CB . SER A 1 133 ? -19.556 29.068 93.523 1.00 100.53 ? 133 SER A CB 1 ATOM 1052 O OG . SER A 1 133 ? -20.413 27.971 93.253 1.00 99.09 ? 133 SER A OG 1 ATOM 1053 N N . ALA A 1 134 ? -21.720 29.833 91.100 1.00 95.33 ? 134 ALA A N 1 ATOM 1054 C CA . ALA A 1 134 ? -22.195 29.520 89.742 1.00 94.67 ? 134 ALA A CA 1 ATOM 1055 C C . ALA A 1 134 ? -21.988 30.662 88.731 1.00 93.68 ? 134 ALA A C 1 ATOM 1056 O O . ALA A 1 134 ? -21.624 30.413 87.582 1.00 93.08 ? 134 ALA A O 1 ATOM 1057 C CB . ALA A 1 134 ? -23.660 29.107 89.774 1.00 93.08 ? 134 ALA A CB 1 ATOM 1058 N N . CYS A 1 135 ? -22.225 31.902 89.153 1.00 93.25 ? 135 CYS A N 1 ATOM 1059 C CA . CYS A 1 135 ? -21.895 33.075 88.348 1.00 92.93 ? 135 CYS A CA 1 ATOM 1060 C C . CYS A 1 135 ? -20.584 33.687 88.865 1.00 94.28 ? 135 CYS A C 1 ATOM 1061 O O . CYS A 1 135 ? -20.615 34.519 89.766 1.00 94.11 ? 135 CYS A O 1 ATOM 1062 C CB . CYS A 1 135 ? -23.013 34.112 88.455 1.00 92.74 ? 135 CYS A CB 1 ATOM 1063 S SG . CYS A 1 135 ? -24.680 33.520 88.089 1.00 94.43 ? 135 CYS A SG 1 ATOM 1064 N N . PRO A 1 136 ? -19.427 33.250 88.326 1.00 94.50 ? 136 PRO A N 1 ATOM 1065 C CA . PRO A 1 136 ? -18.107 33.732 88.731 1.00 97.86 ? 136 PRO A CA 1 ATOM 1066 C C . PRO A 1 136 ? -17.479 34.795 87.827 1.00 99.20 ? 136 PRO A C 1 ATOM 1067 O O . PRO A 1 136 ? -17.460 34.635 86.605 1.00 98.06 ? 136 PRO A O 1 ATOM 1068 C CB . PRO A 1 136 ? -17.261 32.465 88.669 1.00 98.93 ? 136 PRO A CB 1 ATOM 1069 C CG . PRO A 1 136 ? -17.854 31.701 87.544 1.00 96.05 ? 136 PRO A CG 1 ATOM 1070 C CD . PRO A 1 136 ? -19.325 31.954 87.634 1.00 93.78 ? 136 PRO A CD 1 ATOM 1071 N N . TYR A 1 137 ? -16.950 35.853 88.443 1.00 101.98 ? 137 TYR A N 1 ATOM 1072 C CA . TYR A 1 137 ? -16.259 36.914 87.720 1.00 103.92 ? 137 TYR A CA 1 ATOM 1073 C C . TYR A 1 137 ? -14.855 37.084 88.254 1.00 106.68 ? 137 TYR A C 1 ATOM 1074 O O . TYR A 1 137 ? -14.674 37.314 89.446 1.00 109.15 ? 137 TYR A O 1 ATOM 1075 C CB . TYR A 1 137 ? -17.000 38.243 87.867 1.00 104.06 ? 137 TYR A CB 1 ATOM 1076 C CG . TYR A 1 137 ? -16.264 39.405 87.233 1.00 105.68 ? 137 TYR A CG 1 ATOM 1077 C CD1 . TYR A 1 137 ? -16.253 39.580 85.847 1.00 104.74 ? 137 TYR A CD1 1 ATOM 1078 C CD2 . TYR A 1 137 ? -15.573 40.327 88.015 1.00 107.49 ? 137 TYR A CD2 1 ATOM 1079 C CE1 . TYR A 1 137 ? -15.579 40.642 85.265 1.00 105.76 ? 137 TYR A CE1 1 ATOM 1080 C CE2 . TYR A 1 137 ? -14.898 41.389 87.440 1.00 108.86 ? 137 TYR A CE2 1 ATOM 1081 C CZ . TYR A 1 137 ? -14.906 41.542 86.067 1.00 107.83 ? 137 TYR A CZ 1 ATOM 1082 O OH . TYR A 1 137 ? -14.238 42.596 85.499 1.00 109.49 ? 137 TYR A OH 1 ATOM 1083 N N . GLN A 1 138 ? -13.869 36.996 87.365 1.00 108.22 ? 138 GLN A N 1 ATOM 1084 C CA . GLN A 1 138 ? -12.458 37.196 87.725 1.00 112.07 ? 138 GLN A CA 1 ATOM 1085 C C . GLN A 1 138 ? -12.003 36.322 88.901 1.00 113.44 ? 138 GLN A C 1 ATOM 1086 O O . GLN A 1 138 ? -11.252 36.764 89.773 1.00 115.68 ? 138 GLN A O 1 ATOM 1087 C CB . GLN A 1 138 ? -12.179 38.681 88.003 1.00 114.55 ? 138 GLN A CB 1 ATOM 1088 C CG . GLN A 1 138 ? -11.751 39.455 86.765 1.00 115.81 ? 138 GLN A CG 1 ATOM 1089 C CD . GLN A 1 138 ? -11.550 40.939 87.025 1.00 118.00 ? 138 GLN A CD 1 ATOM 1090 O OE1 . GLN A 1 138 ? -11.452 41.379 88.171 1.00 119.45 ? 138 GLN A OE1 1 ATOM 1091 N NE2 . GLN A 1 138 ? -11.485 41.719 85.952 1.00 118.36 ? 138 GLN A NE2 1 ATOM 1092 N N . GLY A 1 139 ? -12.470 35.075 88.910 1.00 111.66 ? 139 GLY A N 1 ATOM 1093 C CA . GLY A 1 139 ? -12.064 34.097 89.917 1.00 112.12 ? 139 GLY A CA 1 ATOM 1094 C C . GLY A 1 139 ? -12.823 34.217 91.220 1.00 110.39 ? 139 GLY A C 1 ATOM 1095 O O . GLY A 1 139 ? -12.639 33.399 92.116 1.00 111.22 ? 139 GLY A O 1 ATOM 1096 N N . LYS A 1 140 ? -13.680 35.229 91.321 1.00 107.86 ? 140 LYS A N 1 ATOM 1097 C CA . LYS A 1 140 ? -14.406 35.523 92.551 1.00 108.30 ? 140 LYS A CA 1 ATOM 1098 C C . LYS A 1 140 ? -15.894 35.379 92.301 1.00 105.62 ? 140 LYS A C 1 ATOM 1099 O O . LYS A 1 140 ? -16.393 35.780 91.249 1.00 104.79 ? 140 LYS A O 1 ATOM 1100 C CB . LYS A 1 140 ? -14.107 36.950 93.024 1.00 109.54 ? 140 LYS A CB 1 ATOM 1101 C CG . LYS A 1 140 ? -12.734 37.126 93.655 1.00 113.03 ? 140 LYS A CG 1 ATOM 1102 C CD . LYS A 1 140 ? -12.149 38.504 93.362 1.00 114.40 ? 140 LYS A CD 1 ATOM 1103 C CE . LYS A 1 140 ? -10.631 38.542 93.523 1.00 117.40 ? 140 LYS A CE 1 ATOM 1104 N NZ . LYS A 1 140 ? -10.193 38.585 94.947 1.00 119.98 ? 140 LYS A NZ 1 ATOM 1105 N N . SER A 1 141 ? -16.604 34.812 93.272 1.00 105.65 ? 141 SER A N 1 ATOM 1106 C CA . SER A 1 141 ? -18.052 34.660 93.172 1.00 102.50 ? 141 SER A CA 1 ATOM 1107 C C . SER A 1 141 ? -18.716 36.024 92.979 1.00 100.78 ? 141 SER A C 1 ATOM 1108 O O . SER A 1 141 ? -18.499 36.941 93.762 1.00 103.33 ? 141 SER A O 1 ATOM 1109 C CB . SER A 1 141 ? -18.607 33.980 94.425 1.00 103.23 ? 141 SER A CB 1 ATOM 1110 O OG . SER A 1 141 ? -18.003 32.714 94.633 1.00 104.78 ? 141 SER A OG 1 ATOM 1111 N N . SER A 1 142 ? -19.505 36.147 91.916 1.00 97.59 ? 142 SER A N 1 ATOM 1112 C CA . SER A 1 142 ? -20.222 37.377 91.581 1.00 95.35 ? 142 SER A CA 1 ATOM 1113 C C . SER A 1 142 ? -21.693 37.009 91.340 1.00 91.95 ? 142 SER A C 1 ATOM 1114 O O . SER A 1 142 ? -22.144 35.961 91.805 1.00 90.88 ? 142 SER A O 1 ATOM 1115 C CB . SER A 1 142 ? -19.578 38.027 90.347 1.00 95.11 ? 142 SER A CB 1 ATOM 1116 O OG . SER A 1 142 ? -20.253 39.210 89.957 1.00 93.76 ? 142 SER A OG 1 ATOM 1117 N N . PHE A 1 143 ? -22.435 37.858 90.628 1.00 89.72 ? 143 PHE A N 1 ATOM 1118 C CA . PHE A 1 143 ? -23.855 37.604 90.338 1.00 86.58 ? 143 PHE A CA 1 ATOM 1119 C C . PHE A 1 143 ? -24.357 38.485 89.188 1.00 84.98 ? 143 PHE A C 1 ATOM 1120 O O . PHE A 1 143 ? -23.714 39.468 88.829 1.00 86.20 ? 143 PHE A O 1 ATOM 1121 C CB . PHE A 1 143 ? -24.693 37.858 91.595 1.00 86.29 ? 143 PHE A CB 1 ATOM 1122 C CG . PHE A 1 143 ? -26.083 37.278 91.538 1.00 83.68 ? 143 PHE A CG 1 ATOM 1123 C CD1 . PHE A 1 143 ? -26.283 35.902 91.596 1.00 82.74 ? 143 PHE A CD1 1 ATOM 1124 C CD2 . PHE A 1 143 ? -27.195 38.108 91.453 1.00 82.24 ? 143 PHE A CD2 1 ATOM 1125 C CE1 . PHE A 1 143 ? -27.563 35.367 91.564 1.00 80.81 ? 143 PHE A CE1 1 ATOM 1126 C CE2 . PHE A 1 143 ? -28.476 37.576 91.421 1.00 80.65 ? 143 PHE A CE2 1 ATOM 1127 C CZ . PHE A 1 143 ? -28.661 36.203 91.475 1.00 79.75 ? 143 PHE A CZ 1 ATOM 1128 N N . PHE A 1 144 ? -25.499 38.121 88.606 1.00 82.04 ? 144 PHE A N 1 ATOM 1129 C CA . PHE A 1 144 ? -26.185 38.984 87.641 1.00 80.42 ? 144 PHE A CA 1 ATOM 1130 C C . PHE A 1 144 ? -26.083 40.452 88.084 1.00 81.13 ? 144 PHE A C 1 ATOM 1131 O O . PHE A 1 144 ? -26.640 40.828 89.109 1.00 82.13 ? 144 PHE A O 1 ATOM 1132 C CB . PHE A 1 144 ? -27.672 38.605 87.508 1.00 78.34 ? 144 PHE A CB 1 ATOM 1133 C CG . PHE A 1 144 ? -27.921 37.180 87.063 1.00 77.02 ? 144 PHE A CG 1 ATOM 1134 C CD1 . PHE A 1 144 ? -27.627 36.773 85.762 1.00 76.27 ? 144 PHE A CD1 1 ATOM 1135 C CD2 . PHE A 1 144 ? -28.477 36.251 87.943 1.00 76.23 ? 144 PHE A CD2 1 ATOM 1136 C CE1 . PHE A 1 144 ? -27.869 35.463 85.358 1.00 75.37 ? 144 PHE A CE1 1 ATOM 1137 C CE2 . PHE A 1 144 ? -28.720 34.945 87.542 1.00 75.25 ? 144 PHE A CE2 1 ATOM 1138 C CZ . PHE A 1 144 ? -28.416 34.549 86.250 1.00 74.71 ? 144 PHE A CZ 1 ATOM 1139 N N . ARG A 1 145 ? -25.378 41.269 87.308 1.00 81.36 ? 145 ARG A N 1 ATOM 1140 C CA . ARG A 1 145 ? -25.077 42.651 87.685 1.00 82.95 ? 145 ARG A CA 1 ATOM 1141 C C . ARG A 1 145 ? -26.267 43.605 87.790 1.00 83.39 ? 145 ARG A C 1 ATOM 1142 O O . ARG A 1 145 ? -26.185 44.605 88.492 1.00 86.17 ? 145 ARG A O 1 ATOM 1143 C CB . ARG A 1 145 ? -24.082 43.264 86.700 1.00 83.42 ? 145 ARG A CB 1 ATOM 1144 C CG . ARG A 1 145 ? -22.729 42.585 86.654 1.00 84.57 ? 145 ARG A CG 1 ATOM 1145 C CD . ARG A 1 145 ? -21.684 43.557 86.143 1.00 86.66 ? 145 ARG A CD 1 ATOM 1146 N NE . ARG A 1 145 ? -20.420 42.894 85.837 1.00 88.47 ? 145 ARG A NE 1 ATOM 1147 C CZ . ARG A 1 145 ? -19.513 42.532 86.741 1.00 90.23 ? 145 ARG A CZ 1 ATOM 1148 N NH1 . ARG A 1 145 ? -19.727 42.744 88.033 1.00 91.38 ? 145 ARG A NH1 1 ATOM 1149 N NH2 . ARG A 1 145 ? -18.390 41.936 86.352 1.00 91.54 ? 145 ARG A NH2 1 ATOM 1150 N N . ASN A 1 146 ? -27.356 43.337 87.083 1.00 83.17 ? 146 ASN A N 1 ATOM 1151 C CA . ASN A 1 146 ? -28.450 44.317 87.006 1.00 83.33 ? 146 ASN A CA 1 ATOM 1152 C C . ASN A 1 146 ? -29.474 44.195 88.132 1.00 82.45 ? 146 ASN A C 1 ATOM 1153 O O . ASN A 1 146 ? -30.320 45.080 88.301 1.00 81.68 ? 146 ASN A O 1 ATOM 1154 C CB . ASN A 1 146 ? -29.145 44.250 85.640 1.00 82.12 ? 146 ASN A CB 1 ATOM 1155 C CG . ASN A 1 146 ? -28.270 44.768 84.516 1.00 84.07 ? 146 ASN A CG 1 ATOM 1156 O OD1 . ASN A 1 146 ? -27.626 45.809 84.653 1.00 87.75 ? 146 ASN A OD1 1 ATOM 1157 N ND2 . ASN A 1 146 ? -28.249 44.052 83.392 1.00 84.06 ? 146 ASN A ND2 1 ATOM 1158 N N . VAL A 1 147 ? -29.383 43.116 88.907 1.00 81.87 ? 147 VAL A N 1 ATOM 1159 C CA . VAL A 1 147 ? -30.312 42.874 90.008 1.00 81.88 ? 147 VAL A CA 1 ATOM 1160 C C . VAL A 1 147 ? -29.564 42.533 91.296 1.00 82.87 ? 147 VAL A C 1 ATOM 1161 O O . VAL A 1 147 ? -28.552 41.837 91.264 1.00 83.42 ? 147 VAL A O 1 ATOM 1162 C CB . VAL A 1 147 ? -31.316 41.751 89.662 1.00 80.51 ? 147 VAL A CB 1 ATOM 1163 C CG1 . VAL A 1 147 ? -32.231 42.193 88.529 1.00 79.11 ? 147 VAL A CG1 1 ATOM 1164 C CG2 . VAL A 1 147 ? -30.600 40.452 89.293 1.00 80.18 ? 147 VAL A CG2 1 ATOM 1165 N N . VAL A 1 148 ? -30.070 43.021 92.423 1.00 83.81 ? 148 VAL A N 1 ATOM 1166 C CA . VAL A 1 148 ? -29.414 42.831 93.725 1.00 85.85 ? 148 VAL A CA 1 ATOM 1167 C C . VAL A 1 148 ? -30.058 41.673 94.498 1.00 85.36 ? 148 VAL A C 1 ATOM 1168 O O . VAL A 1 148 ? -31.272 41.679 94.735 1.00 84.28 ? 148 VAL A O 1 ATOM 1169 C CB . VAL A 1 148 ? -29.495 44.110 94.589 1.00 87.73 ? 148 VAL A CB 1 ATOM 1170 C CG1 . VAL A 1 148 ? -28.593 43.987 95.809 1.00 90.69 ? 148 VAL A CG1 1 ATOM 1171 C CG2 . VAL A 1 148 ? -29.113 45.345 93.781 1.00 88.08 ? 148 VAL A CG2 1 ATOM 1172 N N . TRP A 1 149 ? -29.246 40.687 94.884 1.00 86.00 ? 149 TRP A N 1 ATOM 1173 C CA . TRP A 1 149 ? -29.716 39.556 95.697 1.00 86.56 ? 149 TRP A CA 1 ATOM 1174 C C . TRP A 1 149 ? -29.647 39.917 97.192 1.00 89.68 ? 149 TRP A C 1 ATOM 1175 O O . TRP A 1 149 ? -28.628 39.701 97.849 1.00 91.12 ? 149 TRP A O 1 ATOM 1176 C CB . TRP A 1 149 ? -28.886 38.299 95.392 1.00 86.19 ? 149 TRP A CB 1 ATOM 1177 C CG . TRP A 1 149 ? -29.334 37.032 96.103 1.00 86.12 ? 149 TRP A CG 1 ATOM 1178 C CD1 . TRP A 1 149 ? -30.332 36.908 97.032 1.00 86.67 ? 149 TRP A CD1 1 ATOM 1179 C CD2 . TRP A 1 149 ? -28.768 35.723 95.954 1.00 85.62 ? 149 TRP A CD2 1 ATOM 1180 N NE1 . TRP A 1 149 ? -30.431 35.604 97.453 1.00 86.78 ? 149 TRP A NE1 1 ATOM 1181 C CE2 . TRP A 1 149 ? -29.483 34.856 96.808 1.00 86.12 ? 149 TRP A CE2 1 ATOM 1182 C CE3 . TRP A 1 149 ? -27.736 35.198 95.173 1.00 85.29 ? 149 TRP A CE3 1 ATOM 1183 C CZ2 . TRP A 1 149 ? -29.198 33.495 96.904 1.00 86.15 ? 149 TRP A CZ2 1 ATOM 1184 C CZ3 . TRP A 1 149 ? -27.446 33.848 95.275 1.00 85.97 ? 149 TRP A CZ3 1 ATOM 1185 C CH2 . TRP A 1 149 ? -28.178 33.010 96.132 1.00 86.44 ? 149 TRP A CH2 1 ATOM 1186 N N . LEU A 1 150 ? -30.747 40.450 97.723 1.00 90.91 ? 150 LEU A N 1 ATOM 1187 C CA . LEU A 1 150 ? -30.786 40.947 99.101 1.00 93.90 ? 150 LEU A CA 1 ATOM 1188 C C . LEU A 1 150 ? -30.892 39.810 100.106 1.00 95.39 ? 150 LEU A C 1 ATOM 1189 O O . LEU A 1 150 ? -31.688 38.888 99.913 1.00 93.77 ? 150 LEU A O 1 ATOM 1190 C CB . LEU A 1 150 ? -31.971 41.902 99.298 1.00 93.94 ? 150 LEU A CB 1 ATOM 1191 C CG . LEU A 1 150 ? -31.958 43.196 98.477 1.00 93.64 ? 150 LEU A CG 1 ATOM 1192 C CD1 . LEU A 1 150 ? -33.282 43.929 98.607 1.00 93.44 ? 150 LEU A CD1 1 ATOM 1193 C CD2 . LEU A 1 150 ? -30.807 44.106 98.885 1.00 95.99 ? 150 LEU A CD2 1 ATOM 1194 N N . ILE A 1 151 ? -30.084 39.895 101.170 1.00 99.07 ? 151 ILE A N 1 ATOM 1195 C CA . ILE A 1 151 ? -30.131 38.961 102.313 1.00 100.67 ? 151 ILE A CA 1 ATOM 1196 C C . ILE A 1 151 ? -30.288 39.708 103.650 1.00 103.31 ? 151 ILE A C 1 ATOM 1197 O O . ILE A 1 151 ? -30.171 40.938 103.714 1.00 103.72 ? 151 ILE A O 1 ATOM 1198 C CB . ILE A 1 151 ? -28.888 38.033 102.359 1.00 101.22 ? 151 ILE A CB 1 ATOM 1199 C CG1 . ILE A 1 151 ? -27.632 38.798 102.784 1.00 103.67 ? 151 ILE A CG1 1 ATOM 1200 C CG2 . ILE A 1 151 ? -28.665 37.369 101.007 1.00 98.52 ? 151 ILE A CG2 1 ATOM 1201 C CD1 . ILE A 1 151 ? -26.389 37.936 102.870 1.00 105.15 ? 151 ILE A CD1 1 ATOM 1202 N N . LYS A 1 152 ? -30.551 38.950 104.711 1.00 105.61 ? 152 LYS A N 1 ATOM 1203 C CA . LYS A 1 152 ? -30.805 39.511 106.048 1.00 108.92 ? 152 LYS A CA 1 ATOM 1204 C C . LYS A 1 152 ? -29.578 40.208 106.663 1.00 112.52 ? 152 LYS A C 1 ATOM 1205 O O . LYS A 1 152 ? -28.435 39.844 106.374 1.00 112.26 ? 152 LYS A O 1 ATOM 1206 C CB . LYS A 1 152 ? -31.292 38.404 106.997 1.00 109.96 ? 152 LYS A CB 1 ATOM 1207 C CG . LYS A 1 152 ? -30.205 37.412 107.396 1.00 111.73 ? 152 LYS A CG 1 ATOM 1208 C CD . LYS A 1 152 ? -30.742 36.218 108.165 1.00 112.75 ? 152 LYS A CD 1 ATOM 1209 C CE . LYS A 1 152 ? -29.592 35.439 108.784 1.00 115.23 ? 152 LYS A CE 1 ATOM 1210 N NZ . LYS A 1 152 ? -30.065 34.240 109.523 1.00 116.71 ? 152 LYS A NZ 1 ATOM 1211 N N . LYS A 1 153 ? -29.831 41.195 107.524 1.00 116.20 ? 153 LYS A N 1 ATOM 1212 C CA . LYS A 1 153 ? -28.772 41.908 108.254 1.00 120.81 ? 153 LYS A CA 1 ATOM 1213 C C . LYS A 1 153 ? -29.008 41.840 109.772 1.00 123.65 ? 153 LYS A C 1 ATOM 1214 O O . LYS A 1 153 ? -30.082 42.210 110.255 1.00 123.68 ? 153 LYS A O 1 ATOM 1215 C CB . LYS A 1 153 ? -28.697 43.367 107.791 1.00 121.57 ? 153 LYS A CB 1 ATOM 1216 C CG . LYS A 1 153 ? -27.316 43.997 107.938 1.00 124.73 ? 153 LYS A CG 1 ATOM 1217 C CD . LYS A 1 153 ? -27.291 45.429 107.429 1.00 124.85 ? 153 LYS A CD 1 ATOM 1218 C CE . LYS A 1 153 ? -28.056 46.362 108.354 1.00 126.64 ? 153 LYS A CE 1 ATOM 1219 N NZ . LYS A 1 153 ? -27.899 47.788 107.960 1.00 127.18 ? 153 LYS A NZ 1 ATOM 1220 N N . ASN A 1 154 ? -27.992 41.381 110.509 1.00 126.12 ? 154 ASN A N 1 ATOM 1221 C CA . ASN A 1 154 ? -28.099 41.082 111.946 1.00 129.44 ? 154 ASN A CA 1 ATOM 1222 C C . ASN A 1 154 ? -29.286 40.145 112.237 1.00 128.01 ? 154 ASN A C 1 ATOM 1223 O O . ASN A 1 154 ? -30.073 40.364 113.160 1.00 128.27 ? 154 ASN A O 1 ATOM 1224 C CB . ASN A 1 154 ? -28.155 42.374 112.785 1.00 131.93 ? 154 ASN A CB 1 ATOM 1225 C CG . ASN A 1 154 ? -27.375 42.264 114.093 1.00 137.32 ? 154 ASN A CG 1 ATOM 1226 O OD1 . ASN A 1 154 ? -26.294 41.676 114.134 1.00 139.81 ? 154 ASN A OD1 1 ATOM 1227 N ND2 . ASN A 1 154 ? -27.912 42.845 115.166 1.00 139.69 ? 154 ASN A ND2 1 ATOM 1228 N N . SER A 1 155 ? -29.393 39.099 111.419 1.00 125.55 ? 155 SER A N 1 ATOM 1229 C CA . SER A 1 155 ? -30.399 38.050 111.587 1.00 124.45 ? 155 SER A CA 1 ATOM 1230 C C . SER A 1 155 ? -31.836 38.516 111.347 1.00 122.57 ? 155 SER A C 1 ATOM 1231 O O . SER A 1 155 ? -32.754 37.861 111.789 1.00 124.95 ? 155 SER A O 1 ATOM 1232 C CB . SER A 1 155 ? -30.252 37.389 112.977 1.00 127.51 ? 155 SER A CB 1 ATOM 1233 O OG . SER A 1 155 ? -29.456 36.227 112.899 1.00 127.28 ? 155 SER A OG 1 ATOM 1234 N N . THR A 1 156 ? -32.060 39.621 110.647 1.00 119.62 ? 156 THR A N 1 ATOM 1235 C CA . THR A 1 156 ? -33.429 40.118 110.452 1.00 116.79 ? 156 THR A CA 1 ATOM 1236 C C . THR A 1 156 ? -33.641 40.637 109.038 1.00 113.47 ? 156 THR A C 1 ATOM 1237 O O . THR A 1 156 ? -32.822 41.396 108.525 1.00 114.91 ? 156 THR A O 1 ATOM 1238 C CB . THR A 1 156 ? -33.768 41.271 111.424 1.00 119.04 ? 156 THR A CB 1 ATOM 1239 O OG1 . THR A 1 156 ? -32.971 41.175 112.612 1.00 122.12 ? 156 THR A OG1 1 ATOM 1240 C CG2 . THR A 1 156 ? -35.253 41.263 111.789 1.00 118.35 ? 156 THR A CG2 1 ATOM 1241 N N . TYR A 1 157 ? -34.745 40.218 108.418 1.00 109.82 ? 157 TYR A N 1 ATOM 1242 C CA . TYR A 1 157 ? -35.162 40.714 107.110 1.00 104.83 ? 157 TYR A CA 1 ATOM 1243 C C . TYR A 1 157 ? -36.464 41.477 107.313 1.00 103.81 ? 157 TYR A C 1 ATOM 1244 O O . TYR A 1 157 ? -37.543 40.878 107.359 1.00 102.31 ? 157 TYR A O 1 ATOM 1245 C CB . TYR A 1 157 ? -35.372 39.550 106.141 1.00 102.27 ? 157 TYR A CB 1 ATOM 1246 C CG . TYR A 1 157 ? -35.377 39.918 104.666 1.00 98.53 ? 157 TYR A CG 1 ATOM 1247 C CD1 . TYR A 1 157 ? -36.403 40.679 104.107 1.00 96.65 ? 157 TYR A CD1 1 ATOM 1248 C CD2 . TYR A 1 157 ? -34.358 39.486 103.829 1.00 97.11 ? 157 TYR A CD2 1 ATOM 1249 C CE1 . TYR A 1 157 ? -36.402 40.997 102.755 1.00 94.25 ? 157 TYR A CE1 1 ATOM 1250 C CE2 . TYR A 1 157 ? -34.351 39.798 102.484 1.00 94.74 ? 157 TYR A CE2 1 ATOM 1251 C CZ . TYR A 1 157 ? -35.370 40.551 101.948 1.00 92.97 ? 157 TYR A CZ 1 ATOM 1252 O OH . TYR A 1 157 ? -35.332 40.845 100.605 1.00 89.79 ? 157 TYR A OH 1 ATOM 1253 N N . PRO A 1 158 ? -36.366 42.804 107.481 1.00 104.46 ? 158 PRO A N 1 ATOM 1254 C CA . PRO A 1 158 ? -37.583 43.602 107.604 1.00 103.98 ? 158 PRO A CA 1 ATOM 1255 C C . PRO A 1 158 ? -38.278 43.765 106.260 1.00 100.13 ? 158 PRO A C 1 ATOM 1256 O O . PRO A 1 158 ? -37.625 43.741 105.211 1.00 98.18 ? 158 PRO A O 1 ATOM 1257 C CB . PRO A 1 158 ? -37.080 44.950 108.139 1.00 106.19 ? 158 PRO A CB 1 ATOM 1258 C CG . PRO A 1 158 ? -35.634 45.001 107.784 1.00 106.70 ? 158 PRO A CG 1 ATOM 1259 C CD . PRO A 1 158 ? -35.153 43.580 107.796 1.00 106.43 ? 158 PRO A CD 1 ATOM 1260 N N . THR A 1 159 ? -39.597 43.917 106.295 1.00 99.29 ? 159 THR A N 1 ATOM 1261 C CA . THR A 1 159 ? -40.360 44.049 105.067 1.00 96.23 ? 159 THR A CA 1 ATOM 1262 C C . THR A 1 159 ? -39.773 45.188 104.235 1.00 96.05 ? 159 THR A C 1 ATOM 1263 O O . THR A 1 159 ? -39.496 46.280 104.747 1.00 96.71 ? 159 THR A O 1 ATOM 1264 C CB . THR A 1 159 ? -41.865 44.282 105.324 1.00 95.91 ? 159 THR A CB 1 ATOM 1265 O OG1 . THR A 1 159 ? -42.389 43.215 106.118 1.00 96.51 ? 159 THR A OG1 1 ATOM 1266 C CG2 . THR A 1 159 ? -42.643 44.329 104.016 1.00 93.34 ? 159 THR A CG2 1 ATOM 1267 N N . ILE A 1 160 ? -39.538 44.877 102.962 1.00 94.69 ? 160 ILE A N 1 ATOM 1268 C CA . ILE A 1 160 ? -39.136 45.842 101.948 1.00 93.84 ? 160 ILE A CA 1 ATOM 1269 C C . ILE A 1 160 ? -40.401 46.442 101.350 1.00 93.62 ? 160 ILE A C 1 ATOM 1270 O O . ILE A 1 160 ? -41.315 45.706 100.982 1.00 92.24 ? 160 ILE A O 1 ATOM 1271 C CB . ILE A 1 160 ? -38.320 45.148 100.832 1.00 91.35 ? 160 ILE A CB 1 ATOM 1272 C CG1 . ILE A 1 160 ? -36.937 44.756 101.367 1.00 92.67 ? 160 ILE A CG1 1 ATOM 1273 C CG2 . ILE A 1 160 ? -38.197 46.047 99.608 1.00 90.18 ? 160 ILE A CG2 1 ATOM 1274 C CD1 . ILE A 1 160 ? -36.139 43.852 100.451 1.00 90.97 ? 160 ILE A CD1 1 ATOM 1275 N N . LYS A 1 161 ? -40.459 47.770 101.273 1.00 95.46 ? 161 LYS A N 1 ATOM 1276 C CA . LYS A 1 161 ? -41.559 48.474 100.602 1.00 95.13 ? 161 LYS A CA 1 ATOM 1277 C C . LYS A 1 161 ? -40.980 49.564 99.716 1.00 95.36 ? 161 LYS A C 1 ATOM 1278 O O . LYS A 1 161 ? -40.634 50.644 100.188 1.00 97.27 ? 161 LYS A O 1 ATOM 1279 C CB . LYS A 1 161 ? -42.541 49.079 101.614 1.00 97.58 ? 161 LYS A CB 1 ATOM 1280 C CG . LYS A 1 161 ? -43.616 48.112 102.085 1.00 97.92 ? 161 LYS A CG 1 ATOM 1281 C CD . LYS A 1 161 ? -44.532 48.726 103.137 1.00 99.99 ? 161 LYS A CD 1 ATOM 1282 C CE . LYS A 1 161 ? -45.208 47.640 103.966 1.00 100.97 ? 161 LYS A CE 1 ATOM 1283 N NZ . LYS A 1 161 ? -46.110 48.161 105.030 1.00 103.48 ? 161 LYS A NZ 1 ATOM 1284 N N . ARG A 1 162 ? -40.872 49.273 98.426 1.00 93.95 ? 162 ARG A N 1 ATOM 1285 C CA . ARG A 1 162 ? -40.212 50.179 97.506 1.00 94.51 ? 162 ARG A CA 1 ATOM 1286 C C . ARG A 1 162 ? -41.046 50.443 96.267 1.00 93.23 ? 162 ARG A C 1 ATOM 1287 O O . ARG A 1 162 ? -41.834 49.603 95.834 1.00 92.18 ? 162 ARG A O 1 ATOM 1288 C CB . ARG A 1 162 ? -38.840 49.630 97.129 1.00 94.35 ? 162 ARG A CB 1 ATOM 1289 C CG . ARG A 1 162 ? -37.918 49.468 98.323 1.00 97.13 ? 162 ARG A CG 1 ATOM 1290 C CD . ARG A 1 162 ? -37.532 50.797 98.951 1.00 99.95 ? 162 ARG A CD 1 ATOM 1291 N NE . ARG A 1 162 ? -36.323 51.339 98.334 1.00 100.40 ? 162 ARG A NE 1 ATOM 1292 C CZ . ARG A 1 162 ? -35.082 51.128 98.771 1.00 101.79 ? 162 ARG A CZ 1 ATOM 1293 N NH1 . ARG A 1 162 ? -34.845 50.384 99.850 1.00 103.38 ? 162 ARG A NH1 1 ATOM 1294 N NH2 . ARG A 1 162 ? -34.060 51.675 98.127 1.00 101.89 ? 162 ARG A NH2 1 ATOM 1295 N N . SER A 1 163 ? -40.843 51.626 95.701 1.00 93.92 ? 163 SER A N 1 ATOM 1296 C CA . SER A 1 163 ? -41.684 52.129 94.644 1.00 92.65 ? 163 SER A CA 1 ATOM 1297 C C . SER A 1 163 ? -40.862 52.993 93.684 1.00 92.86 ? 163 SER A C 1 ATOM 1298 O O . SER A 1 163 ? -40.167 53.909 94.121 1.00 93.71 ? 163 SER A O 1 ATOM 1299 C CB . SER A 1 163 ? -42.817 52.945 95.265 1.00 93.82 ? 163 SER A CB 1 ATOM 1300 O OG . SER A 1 163 ? -43.654 53.503 94.271 1.00 94.94 ? 163 SER A OG 1 ATOM 1301 N N . TYR A 1 164 ? -40.919 52.683 92.387 1.00 91.62 ? 164 TYR A N 1 ATOM 1302 C CA . TYR A 1 164 ? -40.312 53.543 91.373 1.00 92.01 ? 164 TYR A CA 1 ATOM 1303 C C . TYR A 1 164 ? -41.352 54.100 90.403 1.00 92.61 ? 164 TYR A C 1 ATOM 1304 O O . TYR A 1 164 ? -42.154 53.353 89.841 1.00 91.55 ? 164 TYR A O 1 ATOM 1305 C CB . TYR A 1 164 ? -39.222 52.830 90.578 1.00 89.85 ? 164 TYR A CB 1 ATOM 1306 C CG . TYR A 1 164 ? -38.727 53.713 89.460 1.00 90.68 ? 164 TYR A CG 1 ATOM 1307 C CD1 . TYR A 1 164 ? -37.826 54.745 89.708 1.00 92.97 ? 164 TYR A CD1 1 ATOM 1308 C CD2 . TYR A 1 164 ? -39.211 53.563 88.164 1.00 90.05 ? 164 TYR A CD2 1 ATOM 1309 C CE1 . TYR A 1 164 ? -37.393 55.578 88.689 1.00 94.19 ? 164 TYR A CE1 1 ATOM 1310 C CE2 . TYR A 1 164 ? -38.785 54.388 87.137 1.00 90.79 ? 164 TYR A CE2 1 ATOM 1311 C CZ . TYR A 1 164 ? -37.876 55.392 87.399 1.00 93.30 ? 164 TYR A CZ 1 ATOM 1312 O OH . TYR A 1 164 ? -37.458 56.206 86.370 1.00 94.31 ? 164 TYR A OH 1 ATOM 1313 N N . ASN A 1 165 ? -41.299 55.413 90.200 1.00 95.34 ? 165 ASN A N 1 ATOM 1314 C CA . ASN A 1 165 ? -42.177 56.113 89.276 1.00 97.70 ? 165 ASN A CA 1 ATOM 1315 C C . ASN A 1 165 ? -41.433 56.419 87.972 1.00 95.79 ? 165 ASN A C 1 ATOM 1316 O O . ASN A 1 165 ? -40.378 57.051 87.986 1.00 97.54 ? 165 ASN A O 1 ATOM 1317 C CB . ASN A 1 165 ? -42.664 57.396 89.948 1.00 102.96 ? 165 ASN A CB 1 ATOM 1318 C CG . ASN A 1 165 ? -43.663 58.176 89.113 1.00 108.17 ? 165 ASN A CG 1 ATOM 1319 O OD1 . ASN A 1 165 ? -43.549 58.272 87.897 1.00 106.66 ? 165 ASN A OD1 1 ATOM 1320 N ND2 . ASN A 1 165 ? -44.649 58.751 89.780 1.00 117.28 ? 165 ASN A ND2 1 ATOM 1321 N N . ASN A 1 166 ? -41.979 55.961 86.849 1.00 92.68 ? 166 ASN A N 1 ATOM 1322 C CA . ASN A 1 166 ? -41.365 56.215 85.547 1.00 91.64 ? 166 ASN A CA 1 ATOM 1323 C C . ASN A 1 166 ? -41.645 57.628 85.054 1.00 92.42 ? 166 ASN A C 1 ATOM 1324 O O . ASN A 1 166 ? -42.653 57.876 84.390 1.00 91.15 ? 166 ASN A O 1 ATOM 1325 C CB . ASN A 1 166 ? -41.836 55.201 84.502 1.00 89.81 ? 166 ASN A CB 1 ATOM 1326 C CG . ASN A 1 166 ? -41.056 55.307 83.206 1.00 90.76 ? 166 ASN A CG 1 ATOM 1327 O OD1 . ASN A 1 166 ? -39.955 55.865 83.182 1.00 92.34 ? 166 ASN A OD1 1 ATOM 1328 N ND2 . ASN A 1 166 ? -41.617 54.774 82.119 1.00 89.47 ? 166 ASN A ND2 1 ATOM 1329 N N . THR A 1 167 ? -40.741 58.548 85.381 1.00 93.42 ? 167 THR A N 1 ATOM 1330 C CA . THR A 1 167 ? -40.863 59.941 84.947 1.00 95.31 ? 167 THR A CA 1 ATOM 1331 C C . THR A 1 167 ? -40.296 60.171 83.541 1.00 95.12 ? 167 THR A C 1 ATOM 1332 O O . THR A 1 167 ? -40.515 61.232 82.953 1.00 97.97 ? 167 THR A O 1 ATOM 1333 C CB . THR A 1 167 ? -40.164 60.906 85.926 1.00 97.22 ? 167 THR A CB 1 ATOM 1334 O OG1 . THR A 1 167 ? -38.773 60.574 86.022 1.00 97.24 ? 167 THR A OG1 1 ATOM 1335 C CG2 . THR A 1 167 ? -40.807 60.824 87.299 1.00 97.06 ? 167 THR A CG2 1 ATOM 1336 N N . ASN A 1 168 ? -39.573 59.186 83.009 1.00 92.07 ? 168 ASN A N 1 ATOM 1337 C CA . ASN A 1 168 ? -39.079 59.245 81.632 1.00 91.17 ? 168 ASN A CA 1 ATOM 1338 C C . ASN A 1 168 ? -40.237 59.240 80.643 1.00 89.96 ? 168 ASN A C 1 ATOM 1339 O O . ASN A 1 168 ? -41.325 58.769 80.966 1.00 89.26 ? 168 ASN A O 1 ATOM 1340 C CB . ASN A 1 168 ? -38.187 58.044 81.327 1.00 89.07 ? 168 ASN A CB 1 ATOM 1341 C CG . ASN A 1 168 ? -37.176 57.781 82.413 1.00 89.02 ? 168 ASN A CG 1 ATOM 1342 O OD1 . ASN A 1 168 ? -36.139 58.440 82.477 1.00 90.99 ? 168 ASN A OD1 1 ATOM 1343 N ND2 . ASN A 1 168 ? -37.469 56.809 83.277 1.00 87.27 ? 168 ASN A ND2 1 ATOM 1344 N N . GLN A 1 169 ? -40.004 59.760 79.442 1.00 89.98 ? 169 GLN A N 1 ATOM 1345 C CA . GLN A 1 169 ? -41.018 59.715 78.385 1.00 89.56 ? 169 GLN A CA 1 ATOM 1346 C C . GLN A 1 169 ? -41.222 58.292 77.818 1.00 86.51 ? 169 GLN A C 1 ATOM 1347 O O . GLN A 1 169 ? -42.242 58.013 77.195 1.00 85.49 ? 169 GLN A O 1 ATOM 1348 C CB . GLN A 1 169 ? -40.650 60.654 77.238 1.00 91.37 ? 169 GLN A CB 1 ATOM 1349 C CG . GLN A 1 169 ? -41.278 62.033 77.289 1.00 93.91 ? 169 GLN A CG 1 ATOM 1350 C CD . GLN A 1 169 ? -41.439 62.621 75.886 1.00 95.71 ? 169 GLN A CD 1 ATOM 1351 O OE1 . GLN A 1 169 ? -40.634 63.443 75.446 1.00 96.66 ? 169 GLN A OE1 1 ATOM 1352 N NE2 . GLN A 1 169 ? -42.461 62.164 75.163 1.00 94.81 ? 169 GLN A NE2 1 ATOM 1353 N N . GLU A 1 170 ? -40.253 57.409 78.052 1.00 84.71 ? 170 GLU A N 1 ATOM 1354 C CA . GLU A 1 170 ? -40.212 56.077 77.446 1.00 82.20 ? 170 GLU A CA 1 ATOM 1355 C C . GLU A 1 170 ? -40.937 54.970 78.238 1.00 80.38 ? 170 GLU A C 1 ATOM 1356 O O . GLU A 1 170 ? -41.328 55.153 79.389 1.00 81.00 ? 170 GLU A O 1 ATOM 1357 C CB . GLU A 1 170 ? -38.749 55.666 77.231 1.00 81.03 ? 170 GLU A CB 1 ATOM 1358 C CG . GLU A 1 170 ? -38.012 56.518 76.201 1.00 82.61 ? 170 GLU A CG 1 ATOM 1359 C CD . GLU A 1 170 ? -37.379 57.787 76.758 1.00 84.93 ? 170 GLU A CD 1 ATOM 1360 O OE1 . GLU A 1 170 ? -37.672 58.185 77.905 1.00 85.17 ? 170 GLU A OE1 1 ATOM 1361 O OE2 . GLU A 1 170 ? -36.582 58.402 76.026 1.00 84.16 ? 170 GLU A OE2 1 ATOM 1362 N N . ASP A 1 171 ? -41.136 53.832 77.578 1.00 79.02 ? 171 ASP A N 1 ATOM 1363 C CA . ASP A 1 171 ? -41.505 52.598 78.249 1.00 77.35 ? 171 ASP A CA 1 ATOM 1364 C C . ASP A 1 171 ? -40.220 52.118 78.909 1.00 77.74 ? 171 ASP A C 1 ATOM 1365 O O . ASP A 1 171 ? -39.129 52.284 78.353 1.00 77.81 ? 171 ASP A O 1 ATOM 1366 C CB . ASP A 1 171 ? -41.991 51.511 77.263 1.00 75.72 ? 171 ASP A CB 1 ATOM 1367 C CG . ASP A 1 171 ? -43.311 51.854 76.564 1.00 76.03 ? 171 ASP A CG 1 ATOM 1368 O OD1 . ASP A 1 171 ? -44.174 52.554 77.137 1.00 76.93 ? 171 ASP A OD1 1 ATOM 1369 O OD2 . ASP A 1 171 ? -43.493 51.385 75.420 1.00 75.50 ? 171 ASP A OD2 1 ATOM 1370 N N . LEU A 1 172 ? -40.353 51.521 80.088 1.00 78.44 ? 172 LEU A N 1 ATOM 1371 C CA . LEU A 1 172 ? -39.216 50.984 80.807 1.00 79.68 ? 172 LEU A CA 1 ATOM 1372 C C . LEU A 1 172 ? -39.374 49.478 80.981 1.00 77.63 ? 172 LEU A C 1 ATOM 1373 O O . LEU A 1 172 ? -40.425 48.999 81.402 1.00 76.19 ? 172 LEU A O 1 ATOM 1374 C CB . LEU A 1 172 ? -39.100 51.655 82.171 1.00 82.68 ? 172 LEU A CB 1 ATOM 1375 C CG . LEU A 1 172 ? -37.680 51.682 82.746 1.00 85.36 ? 172 LEU A CG 1 ATOM 1376 C CD1 . LEU A 1 172 ? -36.904 52.862 82.176 1.00 88.16 ? 172 LEU A CD1 1 ATOM 1377 C CD2 . LEU A 1 172 ? -37.700 51.769 84.263 1.00 86.46 ? 172 LEU A CD2 1 ATOM 1378 N N . LEU A 1 173 ? -38.326 48.743 80.631 1.00 76.80 ? 173 LEU A N 1 ATOM 1379 C CA . LEU A 1 173 ? -38.266 47.321 80.878 1.00 75.54 ? 173 LEU A CA 1 ATOM 1380 C C . LEU A 1 173 ? -37.654 47.110 82.245 1.00 76.66 ? 173 LEU A C 1 ATOM 1381 O O . LEU A 1 173 ? -36.464 47.350 82.440 1.00 79.89 ? 173 LEU A O 1 ATOM 1382 C CB . LEU A 1 173 ? -37.399 46.629 79.836 1.00 75.59 ? 173 LEU A CB 1 ATOM 1383 C CG . LEU A 1 173 ? -37.076 45.162 80.139 1.00 74.85 ? 173 LEU A CG 1 ATOM 1384 C CD1 . LEU A 1 173 ? -38.343 44.325 80.197 1.00 73.68 ? 173 LEU A CD1 1 ATOM 1385 C CD2 . LEU A 1 173 ? -36.128 44.608 79.092 1.00 75.08 ? 173 LEU A CD2 1 ATOM 1386 N N . VAL A 1 174 ? -38.469 46.653 83.186 1.00 75.53 ? 174 VAL A N 1 ATOM 1387 C CA . VAL A 1 174 ? -38.024 46.372 84.536 1.00 74.66 ? 174 VAL A CA 1 ATOM 1388 C C . VAL A 1 174 ? -37.864 44.861 84.678 1.00 72.77 ? 174 VAL A C 1 ATOM 1389 O O . VAL A 1 174 ? -38.709 44.101 84.221 1.00 70.71 ? 174 VAL A O 1 ATOM 1390 C CB . VAL A 1 174 ? -39.050 46.883 85.569 1.00 75.59 ? 174 VAL A CB 1 ATOM 1391 C CG1 . VAL A 1 174 ? -38.501 46.754 86.982 1.00 77.12 ? 174 VAL A CG1 1 ATOM 1392 C CG2 . VAL A 1 174 ? -39.426 48.327 85.278 1.00 76.41 ? 174 VAL A CG2 1 ATOM 1393 N N . LEU A 1 175 ? -36.774 44.443 85.314 1.00 72.93 ? 175 LEU A N 1 ATOM 1394 C CA . LEU A 1 175 ? -36.503 43.038 85.591 1.00 71.90 ? 175 LEU A CA 1 ATOM 1395 C C . LEU A 1 175 ? -36.347 42.807 87.092 1.00 72.66 ? 175 LEU A C 1 ATOM 1396 O O . LEU A 1 175 ? -35.781 43.640 87.790 1.00 73.76 ? 175 LEU A O 1 ATOM 1397 C CB . LEU A 1 175 ? -35.210 42.613 84.904 1.00 71.72 ? 175 LEU A CB 1 ATOM 1398 C CG . LEU A 1 175 ? -35.175 42.636 83.380 1.00 70.95 ? 175 LEU A CG 1 ATOM 1399 C CD1 . LEU A 1 175 ? -33.751 42.435 82.898 1.00 71.54 ? 175 LEU A CD1 1 ATOM 1400 C CD2 . LEU A 1 175 ? -36.070 41.554 82.810 1.00 69.77 ? 175 LEU A CD2 1 ATOM 1401 N N . TRP A 1 176 ? -36.846 41.670 87.576 1.00 72.16 ? 176 TRP A N 1 ATOM 1402 C CA . TRP A 1 176 ? -36.611 41.232 88.956 1.00 72.93 ? 176 TRP A CA 1 ATOM 1403 C C . TRP A 1 176 ? -36.700 39.709 89.072 1.00 72.29 ? 176 TRP A C 1 ATOM 1404 O O . TRP A 1 176 ? -36.953 39.016 88.084 1.00 71.20 ? 176 TRP A O 1 ATOM 1405 C CB . TRP A 1 176 ? -37.592 41.913 89.917 1.00 73.81 ? 176 TRP A CB 1 ATOM 1406 C CG . TRP A 1 176 ? -39.025 41.493 89.760 1.00 72.94 ? 176 TRP A CG 1 ATOM 1407 C CD1 . TRP A 1 176 ? -39.697 40.582 90.519 1.00 72.62 ? 176 TRP A CD1 1 ATOM 1408 C CD2 . TRP A 1 176 ? -39.965 41.983 88.797 1.00 72.17 ? 176 TRP A CD2 1 ATOM 1409 N NE1 . TRP A 1 176 ? -40.995 40.469 90.088 1.00 71.64 ? 176 TRP A NE1 1 ATOM 1410 C CE2 . TRP A 1 176 ? -41.186 41.318 89.030 1.00 71.76 ? 176 TRP A CE2 1 ATOM 1411 C CE3 . TRP A 1 176 ? -39.893 42.918 87.758 1.00 72.34 ? 176 TRP A CE3 1 ATOM 1412 C CZ2 . TRP A 1 176 ? -42.328 41.556 88.259 1.00 71.67 ? 176 TRP A CZ2 1 ATOM 1413 C CZ3 . TRP A 1 176 ? -41.030 43.156 86.988 1.00 71.97 ? 176 TRP A CZ3 1 ATOM 1414 C CH2 . TRP A 1 176 ? -42.229 42.478 87.242 1.00 71.49 ? 176 TRP A CH2 1 ATOM 1415 N N . GLY A 1 177 ? -36.481 39.191 90.278 1.00 73.86 ? 177 GLY A N 1 ATOM 1416 C CA . GLY A 1 177 ? -36.533 37.746 90.512 1.00 73.72 ? 177 GLY A CA 1 ATOM 1417 C C . GLY A 1 177 ? -36.877 37.309 91.927 1.00 74.74 ? 177 GLY A C 1 ATOM 1418 O O . GLY A 1 177 ? -36.883 38.108 92.863 1.00 75.14 ? 177 GLY A O 1 ATOM 1419 N N . ILE A 1 178 ? -37.166 36.016 92.054 1.00 75.20 ? 178 ILE A N 1 ATOM 1420 C CA . ILE A 1 178 ? -37.439 35.352 93.333 1.00 76.70 ? 178 ILE A CA 1 ATOM 1421 C C . ILE A 1 178 ? -36.414 34.238 93.455 1.00 77.46 ? 178 ILE A C 1 ATOM 1422 O O . ILE A 1 178 ? -36.027 33.638 92.455 1.00 76.36 ? 178 ILE A O 1 ATOM 1423 C CB . ILE A 1 178 ? -38.877 34.756 93.387 1.00 76.48 ? 178 ILE A CB 1 ATOM 1424 C CG1 . ILE A 1 178 ? -39.142 33.972 94.684 1.00 78.28 ? 178 ILE A CG1 1 ATOM 1425 C CG2 . ILE A 1 178 ? -39.157 33.829 92.210 1.00 74.82 ? 178 ILE A CG2 1 ATOM 1426 C CD1 . ILE A 1 178 ? -40.105 34.644 95.637 1.00 79.69 ? 178 ILE A CD1 1 ATOM 1427 N N . HIS A 1 179 ? -35.962 33.964 94.668 1.00 79.90 ? 179 HIS A N 1 ATOM 1428 C CA . HIS A 1 179 ? -35.056 32.851 94.883 1.00 81.86 ? 179 HIS A CA 1 ATOM 1429 C C . HIS A 1 179 ? -35.755 31.692 95.572 1.00 82.80 ? 179 HIS A C 1 ATOM 1430 O O . HIS A 1 179 ? -36.415 31.869 96.596 1.00 84.16 ? 179 HIS A O 1 ATOM 1431 C CB . HIS A 1 179 ? -33.855 33.281 95.709 1.00 84.16 ? 179 HIS A CB 1 ATOM 1432 C CG . HIS A 1 179 ? -32.994 32.139 96.149 1.00 85.48 ? 179 HIS A CG 1 ATOM 1433 N ND1 . HIS A 1 179 ? -32.789 31.833 97.476 1.00 87.85 ? 179 HIS A ND1 1 ATOM 1434 C CD2 . HIS A 1 179 ? -32.306 31.216 95.439 1.00 85.26 ? 179 HIS A CD2 1 ATOM 1435 C CE1 . HIS A 1 179 ? -31.994 30.783 97.565 1.00 89.05 ? 179 HIS A CE1 1 ATOM 1436 N NE2 . HIS A 1 179 ? -31.689 30.387 96.344 1.00 87.62 ? 179 HIS A NE2 1 ATOM 1437 N N . HIS A 1 180 ? -35.585 30.505 95.005 1.00 82.73 ? 180 HIS A N 1 ATOM 1438 C CA . HIS A 1 180 ? -36.122 29.293 95.585 1.00 84.73 ? 180 HIS A CA 1 ATOM 1439 C C . HIS A 1 180 ? -34.998 28.560 96.317 1.00 86.85 ? 180 HIS A C 1 ATOM 1440 O O . HIS A 1 180 ? -34.034 28.120 95.688 1.00 87.22 ? 180 HIS A O 1 ATOM 1441 C CB . HIS A 1 180 ? -36.715 28.420 94.488 1.00 84.04 ? 180 HIS A CB 1 ATOM 1442 C CG . HIS A 1 180 ? -37.751 29.120 93.664 1.00 83.01 ? 180 HIS A CG 1 ATOM 1443 N ND1 . HIS A 1 180 ? -39.048 29.289 94.091 1.00 83.68 ? 180 HIS A ND1 1 ATOM 1444 C CD2 . HIS A 1 180 ? -37.677 29.709 92.447 1.00 81.88 ? 180 HIS A CD2 1 ATOM 1445 C CE1 . HIS A 1 180 ? -39.736 29.941 93.170 1.00 82.02 ? 180 HIS A CE1 1 ATOM 1446 N NE2 . HIS A 1 180 ? -38.927 30.207 92.161 1.00 81.02 ? 180 HIS A NE2 1 ATOM 1447 N N . PRO A 1 181 ? -35.111 28.437 97.652 1.00 88.25 ? 181 PRO A N 1 ATOM 1448 C CA . PRO A 1 181 ? -34.082 27.799 98.458 1.00 90.48 ? 181 PRO A CA 1 ATOM 1449 C C . PRO A 1 181 ? -34.192 26.281 98.433 1.00 90.54 ? 181 PRO A C 1 ATOM 1450 O O . PRO A 1 181 ? -35.258 25.737 98.131 1.00 89.56 ? 181 PRO A O 1 ATOM 1451 C CB . PRO A 1 181 ? -34.370 28.329 99.865 1.00 92.99 ? 181 PRO A CB 1 ATOM 1452 C CG . PRO A 1 181 ? -35.852 28.513 99.886 1.00 92.14 ? 181 PRO A CG 1 ATOM 1453 C CD . PRO A 1 181 ? -36.273 28.830 98.469 1.00 89.37 ? 181 PRO A CD 1 ATOM 1454 N N . ASN A 1 182 ? -33.093 25.609 98.756 1.00 91.79 ? 182 ASN A N 1 ATOM 1455 C CA . ASN A 1 182 ? -33.054 24.145 98.765 1.00 92.53 ? 182 ASN A CA 1 ATOM 1456 C C . ASN A 1 182 ? -33.937 23.503 99.837 1.00 93.88 ? 182 ASN A C 1 ATOM 1457 O O . ASN A 1 182 ? -34.627 22.516 99.564 1.00 92.59 ? 182 ASN A O 1 ATOM 1458 C CB . ASN A 1 182 ? -31.610 23.662 98.921 1.00 94.26 ? 182 ASN A CB 1 ATOM 1459 C CG . ASN A 1 182 ? -30.770 23.971 97.701 1.00 92.84 ? 182 ASN A CG 1 ATOM 1460 O OD1 . ASN A 1 182 ? -30.996 23.412 96.638 1.00 91.21 ? 182 ASN A OD1 1 ATOM 1461 N ND2 . ASN A 1 182 ? -29.807 24.870 97.845 1.00 93.42 ? 182 ASN A ND2 1 ATOM 1462 N N . ASP A 1 183 ? -33.912 24.076 101.043 1.00 95.96 ? 183 ASP A N 1 ATOM 1463 C CA . ASP A 1 183 ? -34.599 23.510 102.211 1.00 98.51 ? 183 ASP A CA 1 ATOM 1464 C C . ASP A 1 183 ? -34.991 24.589 103.231 1.00 98.90 ? 183 ASP A C 1 ATOM 1465 O O . ASP A 1 183 ? -34.549 25.736 103.142 1.00 98.14 ? 183 ASP A O 1 ATOM 1466 C CB . ASP A 1 183 ? -33.701 22.467 102.889 1.00 101.53 ? 183 ASP A CB 1 ATOM 1467 C CG . ASP A 1 183 ? -32.429 23.076 103.465 1.00 103.48 ? 183 ASP A CG 1 ATOM 1468 O OD1 . ASP A 1 183 ? -32.474 24.235 103.929 1.00 104.46 ? 183 ASP A OD1 1 ATOM 1469 O OD2 . ASP A 1 183 ? -31.382 22.392 103.455 1.00 104.49 ? 183 ASP A OD2 1 ATOM 1470 N N . ALA A 1 184 ? -35.796 24.197 104.216 1.00 100.26 ? 184 ALA A N 1 ATOM 1471 C CA . ALA A 1 184 ? -36.286 25.124 105.247 1.00 101.27 ? 184 ALA A CA 1 ATOM 1472 C C . ALA A 1 184 ? -35.149 25.813 106.002 1.00 102.61 ? 184 ALA A C 1 ATOM 1473 O O . ALA A 1 184 ? -35.223 27.005 106.289 1.00 102.10 ? 184 ALA A O 1 ATOM 1474 C CB . ALA A 1 184 ? -37.204 24.401 106.226 1.00 102.70 ? 184 ALA A CB 1 ATOM 1475 N N . ALA A 1 185 ? -34.101 25.057 106.307 1.00 104.40 ? 185 ALA A N 1 ATOM 1476 C CA . ALA A 1 185 ? -32.937 25.602 106.998 1.00 106.48 ? 185 ALA A CA 1 ATOM 1477 C C . ALA A 1 185 ? -32.271 26.682 106.151 1.00 103.72 ? 185 ALA A C 1 ATOM 1478 O O . ALA A 1 185 ? -31.863 27.724 106.664 1.00 103.70 ? 185 ALA A O 1 ATOM 1479 C CB . ALA A 1 185 ? -31.948 24.492 107.328 1.00 109.03 ? 185 ALA A CB 1 ATOM 1480 N N . GLU A 1 186 ? -32.180 26.426 104.851 1.00 101.42 ? 186 GLU A N 1 ATOM 1481 C CA . GLU A 1 186 ? -31.597 27.382 103.913 1.00 99.92 ? 186 GLU A CA 1 ATOM 1482 C C . GLU A 1 186 ? -32.416 28.674 103.840 1.00 98.03 ? 186 GLU A C 1 ATOM 1483 O O . GLU A 1 186 ? -31.859 29.770 103.771 1.00 97.41 ? 186 GLU A O 1 ATOM 1484 C CB . GLU A 1 186 ? -31.469 26.760 102.519 1.00 98.16 ? 186 GLU A CB 1 ATOM 1485 C CG . GLU A 1 186 ? -30.802 27.680 101.505 1.00 97.10 ? 186 GLU A CG 1 ATOM 1486 C CD . GLU A 1 186 ? -30.018 26.926 100.438 1.00 96.76 ? 186 GLU A CD 1 ATOM 1487 O OE1 . GLU A 1 186 ? -30.638 26.429 99.466 1.00 95.44 ? 186 GLU A OE1 1 ATOM 1488 O OE2 . GLU A 1 186 ? -28.775 26.843 100.567 1.00 98.06 ? 186 GLU A OE2 1 ATOM 1489 N N . GLN A 1 187 ? -33.736 28.537 103.857 1.00 97.10 ? 187 GLN A N 1 ATOM 1490 C CA . GLN A 1 187 ? -34.627 29.696 103.848 1.00 96.66 ? 187 GLN A CA 1 ATOM 1491 C C . GLN A 1 187 ? -34.421 30.598 105.069 1.00 99.39 ? 187 GLN A C 1 ATOM 1492 O O . GLN A 1 187 ? -34.273 31.819 104.947 1.00 98.75 ? 187 GLN A O 1 ATOM 1493 C CB . GLN A 1 187 ? -36.092 29.239 103.773 1.00 95.64 ? 187 GLN A CB 1 ATOM 1494 C CG . GLN A 1 187 ? -37.120 30.303 104.146 1.00 95.00 ? 187 GLN A CG 1 ATOM 1495 C CD . GLN A 1 187 ? -37.199 31.456 103.150 1.00 92.19 ? 187 GLN A CD 1 ATOM 1496 O OE1 . GLN A 1 187 ? -37.365 31.245 101.947 1.00 89.25 ? 187 GLN A OE1 1 ATOM 1497 N NE2 . GLN A 1 187 ? -37.109 32.682 103.654 1.00 92.82 ? 187 GLN A NE2 1 ATOM 1498 N N . THR A 1 188 ? -34.427 29.985 106.245 1.00 103.35 ? 188 THR A N 1 ATOM 1499 C CA . THR A 1 188 ? -34.274 30.732 107.498 1.00 106.32 ? 188 THR A CA 1 ATOM 1500 C C . THR A 1 188 ? -32.885 31.358 107.541 1.00 107.15 ? 188 THR A C 1 ATOM 1501 O O . THR A 1 188 ? -32.728 32.527 107.890 1.00 107.61 ? 188 THR A O 1 ATOM 1502 C CB . THR A 1 188 ? -34.461 29.869 108.775 1.00 109.73 ? 188 THR A CB 1 ATOM 1503 O OG1 . THR A 1 188 ? -33.256 29.876 109.553 1.00 112.72 ? 188 THR A OG1 1 ATOM 1504 C CG2 . THR A 1 188 ? -34.850 28.434 108.460 1.00 109.80 ? 188 THR A CG2 1 ATOM 1505 N N . LYS A 1 189 ? -31.884 30.561 107.182 1.00 107.48 ? 189 LYS A N 1 ATOM 1506 C CA . LYS A 1 189 ? -30.499 31.015 107.157 1.00 108.85 ? 189 LYS A CA 1 ATOM 1507 C C . LYS A 1 189 ? -30.312 32.276 106.316 1.00 107.53 ? 189 LYS A C 1 ATOM 1508 O O . LYS A 1 189 ? -29.653 33.221 106.737 1.00 108.75 ? 189 LYS A O 1 ATOM 1509 C CB . LYS A 1 189 ? -29.595 29.904 106.617 1.00 108.55 ? 189 LYS A CB 1 ATOM 1510 C CG . LYS A 1 189 ? -28.184 30.360 106.302 1.00 109.45 ? 189 LYS A CG 1 ATOM 1511 C CD . LYS A 1 189 ? -27.320 29.197 105.848 1.00 110.14 ? 189 LYS A CD 1 ATOM 1512 C CE . LYS A 1 189 ? -25.961 29.681 105.369 1.00 110.60 ? 189 LYS A CE 1 ATOM 1513 N NZ . LYS A 1 189 ? -25.242 28.632 104.599 1.00 110.23 ? 189 LYS A NZ 1 ATOM 1514 N N . LEU A 1 190 ? -30.892 32.283 105.124 1.00 105.19 ? 190 LEU A N 1 ATOM 1515 C CA . LEU A 1 190 ? -30.682 33.391 104.197 1.00 104.18 ? 190 LEU A CA 1 ATOM 1516 C C . LEU A 1 190 ? -31.530 34.610 104.521 1.00 103.72 ? 190 LEU A C 1 ATOM 1517 O O . LEU A 1 190 ? -31.076 35.747 104.379 1.00 102.72 ? 190 LEU A O 1 ATOM 1518 C CB . LEU A 1 190 ? -30.984 32.946 102.770 1.00 102.17 ? 190 LEU A CB 1 ATOM 1519 C CG . LEU A 1 190 ? -29.925 32.056 102.126 1.00 103.41 ? 190 LEU A CG 1 ATOM 1520 C CD1 . LEU A 1 190 ? -30.526 31.255 100.981 1.00 101.22 ? 190 LEU A CD1 1 ATOM 1521 C CD2 . LEU A 1 190 ? -28.743 32.889 101.652 1.00 103.88 ? 190 LEU A CD2 1 ATOM 1522 N N . TYR A 1 191 ? -32.767 34.370 104.938 1.00 104.02 ? 191 TYR A N 1 ATOM 1523 C CA . TYR A 1 191 ? -33.754 35.440 105.033 1.00 103.79 ? 191 TYR A CA 1 ATOM 1524 C C . TYR A 1 191 ? -34.427 35.551 106.400 1.00 107.75 ? 191 TYR A C 1 ATOM 1525 O O . TYR A 1 191 ? -35.278 36.421 106.592 1.00 108.68 ? 191 TYR A O 1 ATOM 1526 C CB . TYR A 1 191 ? -34.822 35.226 103.958 1.00 100.97 ? 191 TYR A CB 1 ATOM 1527 C CG . TYR A 1 191 ? -34.259 34.964 102.571 1.00 97.99 ? 191 TYR A CG 1 ATOM 1528 C CD1 . TYR A 1 191 ? -33.641 35.985 101.846 1.00 97.19 ? 191 TYR A CD1 1 ATOM 1529 C CD2 . TYR A 1 191 ? -34.327 33.698 101.991 1.00 96.18 ? 191 TYR A CD2 1 ATOM 1530 C CE1 . TYR A 1 191 ? -33.120 35.759 100.580 1.00 94.67 ? 191 TYR A CE1 1 ATOM 1531 C CE2 . TYR A 1 191 ? -33.806 33.463 100.726 1.00 94.36 ? 191 TYR A CE2 1 ATOM 1532 C CZ . TYR A 1 191 ? -33.201 34.499 100.028 1.00 93.31 ? 191 TYR A CZ 1 ATOM 1533 O OH . TYR A 1 191 ? -32.674 34.285 98.777 1.00 91.45 ? 191 TYR A OH 1 ATOM 1534 N N . GLN A 1 192 ? -34.040 34.683 107.338 1.00 110.81 ? 192 GLN A N 1 ATOM 1535 C CA . GLN A 1 192 ? -34.666 34.568 108.663 1.00 112.83 ? 192 GLN A CA 1 ATOM 1536 C C . GLN A 1 192 ? -36.117 34.053 108.622 1.00 110.86 ? 192 GLN A C 1 ATOM 1537 O O . GLN A 1 192 ? -36.394 32.967 109.126 1.00 112.02 ? 192 GLN A O 1 ATOM 1538 C CB . GLN A 1 192 ? -34.560 35.882 109.454 1.00 115.71 ? 192 GLN A CB 1 ATOM 1539 C CG . GLN A 1 192 ? -34.594 35.690 110.973 1.00 120.06 ? 192 GLN A CG 1 ATOM 1540 C CD . GLN A 1 192 ? -33.323 36.125 111.689 1.00 124.07 ? 192 GLN A CD 1 ATOM 1541 O OE1 . GLN A 1 192 ? -32.282 35.449 111.647 1.00 125.01 ? 192 GLN A OE1 1 ATOM 1542 N NE2 . GLN A 1 192 ? -33.426 37.252 112.403 1.00 127.04 ? 192 GLN A NE2 1 ATOM 1543 N N . ASN A 1 193 ? -37.023 34.807 108.005 1.00 108.35 ? 193 ASN A N 1 ATOM 1544 C CA . ASN A 1 193 ? -38.452 34.468 108.001 1.00 107.74 ? 193 ASN A CA 1 ATOM 1545 C C . ASN A 1 193 ? -38.679 33.173 107.222 1.00 105.36 ? 193 ASN A C 1 ATOM 1546 O O . ASN A 1 193 ? -38.042 32.961 106.194 1.00 103.95 ? 193 ASN A O 1 ATOM 1547 C CB . ASN A 1 193 ? -39.314 35.577 107.370 1.00 106.62 ? 193 ASN A CB 1 ATOM 1548 C CG . ASN A 1 193 ? -38.861 36.982 107.744 1.00 108.54 ? 193 ASN A CG 1 ATOM 1549 O OD1 . ASN A 1 193 ? -39.609 37.755 108.343 1.00 109.93 ? 193 ASN A OD1 1 ATOM 1550 N ND2 . ASN A 1 193 ? -37.641 37.326 107.365 1.00 108.94 ? 193 ASN A ND2 1 ATOM 1551 N N . PRO A 1 194 ? -39.587 32.305 107.700 1.00 105.49 ? 194 PRO A N 1 ATOM 1552 C CA . PRO A 1 194 ? -39.830 31.044 107.010 1.00 103.67 ? 194 PRO A CA 1 ATOM 1553 C C . PRO A 1 194 ? -40.866 31.156 105.887 1.00 100.14 ? 194 PRO A C 1 ATOM 1554 O O . PRO A 1 194 ? -40.712 30.505 104.857 1.00 98.23 ? 194 PRO A O 1 ATOM 1555 C CB . PRO A 1 194 ? -40.345 30.139 108.128 1.00 106.61 ? 194 PRO A CB 1 ATOM 1556 C CG . PRO A 1 194 ? -41.066 31.065 109.045 1.00 108.28 ? 194 PRO A CG 1 ATOM 1557 C CD . PRO A 1 194 ? -40.402 32.415 108.925 1.00 108.12 ? 194 PRO A CD 1 ATOM 1558 N N . THR A 1 195 ? -41.908 31.961 106.084 1.00 99.29 ? 195 THR A N 1 ATOM 1559 C CA . THR A 1 195 ? -42.951 32.133 105.075 1.00 96.28 ? 195 THR A CA 1 ATOM 1560 C C . THR A 1 195 ? -42.801 33.515 104.452 1.00 94.00 ? 195 THR A C 1 ATOM 1561 O O . THR A 1 195 ? -42.988 34.523 105.132 1.00 94.58 ? 195 THR A O 1 ATOM 1562 C CB . THR A 1 195 ? -44.354 31.976 105.694 1.00 97.26 ? 195 THR A CB 1 ATOM 1563 O OG1 . THR A 1 195 ? -44.417 30.748 106.429 1.00 98.88 ? 195 THR A OG1 1 ATOM 1564 C CG2 . THR A 1 195 ? -45.428 31.962 104.618 1.00 95.08 ? 195 THR A CG2 1 ATOM 1565 N N . THR A 1 196 ? -42.457 33.557 103.164 1.00 91.14 ? 196 THR A N 1 ATOM 1566 C CA . THR A 1 196 ? -42.172 34.823 102.484 1.00 89.60 ? 196 THR A CA 1 ATOM 1567 C C . THR A 1 196 ? -42.963 35.014 101.191 1.00 87.03 ? 196 THR A C 1 ATOM 1568 O O . THR A 1 196 ? -43.676 34.118 100.746 1.00 85.79 ? 196 THR A O 1 ATOM 1569 C CB . THR A 1 196 ? -40.663 34.985 102.191 1.00 89.50 ? 196 THR A CB 1 ATOM 1570 O OG1 . THR A 1 196 ? -40.198 33.889 101.392 1.00 87.86 ? 196 THR A OG1 1 ATOM 1571 C CG2 . THR A 1 196 ? -39.883 35.038 103.496 1.00 92.51 ? 196 THR A CG2 1 ATOM 1572 N N . TYR A 1 197 ? -42.836 36.205 100.610 1.00 86.16 ? 197 TYR A N 1 ATOM 1573 C CA . TYR A 1 197 ? -43.583 36.583 99.419 1.00 83.93 ? 197 TYR A CA 1 ATOM 1574 C C . TYR A 1 197 ? -42.966 37.820 98.776 1.00 83.67 ? 197 TYR A C 1 ATOM 1575 O O . TYR A 1 197 ? -42.243 38.564 99.436 1.00 85.11 ? 197 TYR A O 1 ATOM 1576 C CB . TYR A 1 197 ? -45.030 36.909 99.790 1.00 84.04 ? 197 TYR A CB 1 ATOM 1577 C CG . TYR A 1 197 ? -45.178 38.205 100.566 1.00 84.86 ? 197 TYR A CG 1 ATOM 1578 C CD1 . TYR A 1 197 ? -44.922 38.255 101.935 1.00 87.22 ? 197 TYR A CD1 1 ATOM 1579 C CD2 . TYR A 1 197 ? -45.569 39.381 99.928 1.00 83.51 ? 197 TYR A CD2 1 ATOM 1580 C CE1 . TYR A 1 197 ? -45.051 39.439 102.646 1.00 88.57 ? 197 TYR A CE1 1 ATOM 1581 C CE2 . TYR A 1 197 ? -45.705 40.566 100.628 1.00 85.13 ? 197 TYR A CE2 1 ATOM 1582 C CZ . TYR A 1 197 ? -45.442 40.594 101.988 1.00 87.61 ? 197 TYR A CZ 1 ATOM 1583 O OH . TYR A 1 197 ? -45.571 41.777 102.683 1.00 88.91 ? 197 TYR A OH 1 ATOM 1584 N N . ILE A 1 198 ? -43.262 38.033 97.495 1.00 81.78 ? 198 ILE A N 1 ATOM 1585 C CA . ILE A 1 198 ? -42.935 39.287 96.822 1.00 81.28 ? 198 ILE A CA 1 ATOM 1586 C C . ILE A 1 198 ? -44.160 39.787 96.071 1.00 80.23 ? 198 ILE A C 1 ATOM 1587 O O . ILE A 1 198 ? -44.546 39.200 95.059 1.00 79.79 ? 198 ILE A O 1 ATOM 1588 C CB . ILE A 1 198 ? -41.800 39.129 95.794 1.00 80.48 ? 198 ILE A CB 1 ATOM 1589 C CG1 . ILE A 1 198 ? -40.565 38.480 96.414 1.00 81.85 ? 198 ILE A CG1 1 ATOM 1590 C CG2 . ILE A 1 198 ? -41.424 40.487 95.219 1.00 80.65 ? 198 ILE A CG2 1 ATOM 1591 C CD1 . ILE A 1 198 ? -39.636 37.890 95.375 1.00 81.08 ? 198 ILE A CD1 1 ATOM 1592 N N . SER A 1 199 ? -44.763 40.870 96.551 1.00 80.53 ? 199 SER A N 1 ATOM 1593 C CA . SER A 1 199 ? -45.863 41.504 95.830 1.00 79.73 ? 199 SER A CA 1 ATOM 1594 C C . SER A 1 199 ? -45.332 42.617 94.930 1.00 79.45 ? 199 SER A C 1 ATOM 1595 O O . SER A 1 199 ? -44.664 43.534 95.391 1.00 80.14 ? 199 SER A O 1 ATOM 1596 C CB . SER A 1 199 ? -46.939 42.034 96.790 1.00 80.83 ? 199 SER A CB 1 ATOM 1597 O OG . SER A 1 199 ? -46.376 42.630 97.939 1.00 82.03 ? 199 SER A OG 1 ATOM 1598 N N . VAL A 1 200 ? -45.619 42.505 93.638 1.00 79.43 ? 200 VAL A N 1 ATOM 1599 C CA . VAL A 1 200 ? -45.265 43.524 92.659 1.00 79.50 ? 200 VAL A CA 1 ATOM 1600 C C . VAL A 1 200 ? -46.558 44.077 92.083 1.00 80.61 ? 200 VAL A C 1 ATOM 1601 O O . VAL A 1 200 ? -47.500 43.322 91.840 1.00 81.19 ? 200 VAL A O 1 ATOM 1602 C CB . VAL A 1 200 ? -44.434 42.936 91.507 1.00 78.06 ? 200 VAL A CB 1 ATOM 1603 C CG1 . VAL A 1 200 ? -43.750 44.051 90.731 1.00 78.70 ? 200 VAL A CG1 1 ATOM 1604 C CG2 . VAL A 1 200 ? -43.415 41.938 92.031 1.00 78.26 ? 200 VAL A CG2 1 ATOM 1605 N N . GLY A 1 201 ? -46.609 45.387 91.857 1.00 81.65 ? 201 GLY A N 1 ATOM 1606 C CA . GLY A 1 201 ? -47.821 46.019 91.342 1.00 81.76 ? 201 GLY A CA 1 ATOM 1607 C C . GLY A 1 201 ? -47.520 47.229 90.483 1.00 81.91 ? 201 GLY A C 1 ATOM 1608 O O . GLY A 1 201 ? -46.656 48.027 90.822 1.00 84.00 ? 201 GLY A O 1 ATOM 1609 N N . THR A 1 202 ? -48.218 47.338 89.357 1.00 80.69 ? 202 THR A N 1 ATOM 1610 C CA . THR A 1 202 ? -48.225 48.547 88.541 1.00 80.89 ? 202 THR A CA 1 ATOM 1611 C C . THR A 1 202 ? -49.689 48.883 88.308 1.00 81.97 ? 202 THR A C 1 ATOM 1612 O O . THR A 1 202 ? -50.552 48.437 89.068 1.00 83.20 ? 202 THR A O 1 ATOM 1613 C CB . THR A 1 202 ? -47.495 48.351 87.192 1.00 79.34 ? 202 THR A CB 1 ATOM 1614 O OG1 . THR A 1 202 ? -48.232 47.443 86.360 1.00 77.46 ? 202 THR A OG1 1 ATOM 1615 C CG2 . THR A 1 202 ? -46.085 47.829 87.411 1.00 78.42 ? 202 THR A CG2 1 ATOM 1616 N N . SER A 1 203 ? -49.984 49.657 87.268 1.00 82.07 ? 203 SER A N 1 ATOM 1617 C CA . SER A 1 203 ? -51.372 49.924 86.909 1.00 82.36 ? 203 SER A CA 1 ATOM 1618 C C . SER A 1 203 ? -52.048 48.672 86.362 1.00 80.95 ? 203 SER A C 1 ATOM 1619 O O . SER A 1 203 ? -53.261 48.525 86.475 1.00 82.40 ? 203 SER A O 1 ATOM 1620 C CB . SER A 1 203 ? -51.456 51.030 85.866 1.00 83.22 ? 203 SER A CB 1 ATOM 1621 O OG . SER A 1 203 ? -51.002 50.569 84.612 1.00 81.51 ? 203 SER A OG 1 ATOM 1622 N N . THR A 1 204 ? -51.263 47.784 85.761 1.00 78.79 ? 204 THR A N 1 ATOM 1623 C CA . THR A 1 204 ? -51.794 46.559 85.176 1.00 77.13 ? 204 THR A CA 1 ATOM 1624 C C . THR A 1 204 ? -51.382 45.357 86.008 1.00 76.00 ? 204 THR A C 1 ATOM 1625 O O . THR A 1 204 ? -52.209 44.507 86.331 1.00 77.58 ? 204 THR A O 1 ATOM 1626 C CB . THR A 1 204 ? -51.289 46.357 83.733 1.00 75.49 ? 204 THR A CB 1 ATOM 1627 O OG1 . THR A 1 204 ? -49.929 45.907 83.757 1.00 75.19 ? 204 THR A OG1 1 ATOM 1628 C CG2 . THR A 1 204 ? -51.379 47.648 82.937 1.00 75.29 ? 204 THR A CG2 1 ATOM 1629 N N . LEU A 1 205 ? -50.101 45.293 86.356 1.00 74.61 ? 205 LEU A N 1 ATOM 1630 C CA . LEU A 1 205 ? -49.545 44.138 87.054 1.00 73.04 ? 205 LEU A CA 1 ATOM 1631 C C . LEU A 1 205 ? -50.141 43.954 88.457 1.00 73.25 ? 205 LEU A C 1 ATOM 1632 O O . LEU A 1 205 ? -50.322 44.922 89.202 1.00 73.25 ? 205 LEU A O 1 ATOM 1633 C CB . LEU A 1 205 ? -48.019 44.260 87.132 1.00 72.99 ? 205 LEU A CB 1 ATOM 1634 C CG . LEU A 1 205 ? -47.209 43.017 87.519 1.00 73.28 ? 205 LEU A CG 1 ATOM 1635 C CD1 . LEU A 1 205 ? -47.450 41.864 86.554 1.00 71.95 ? 205 LEU A CD1 1 ATOM 1636 C CD2 . LEU A 1 205 ? -45.724 43.353 87.586 1.00 73.57 ? 205 LEU A CD2 1 ATOM 1637 N N . ASN A 1 206 ? -50.460 42.700 88.784 1.00 72.81 ? 206 ASN A N 1 ATOM 1638 C CA . ASN A 1 206 ? -50.920 42.304 90.114 1.00 73.65 ? 206 ASN A CA 1 ATOM 1639 C C . ASN A 1 206 ? -50.288 40.979 90.552 1.00 73.62 ? 206 ASN A C 1 ATOM 1640 O O . ASN A 1 206 ? -50.965 39.973 90.724 1.00 73.58 ? 206 ASN A O 1 ATOM 1641 C CB . ASN A 1 206 ? -52.442 42.191 90.146 1.00 74.21 ? 206 ASN A CB 1 ATOM 1642 C CG . ASN A 1 206 ? -52.984 42.071 91.555 1.00 75.98 ? 206 ASN A CG 1 ATOM 1643 O OD1 . ASN A 1 206 ? -52.408 42.616 92.497 1.00 77.74 ? 206 ASN A OD1 1 ATOM 1644 N ND2 . ASN A 1 206 ? -54.093 41.357 91.711 1.00 76.51 ? 206 ASN A ND2 1 ATOM 1645 N N . GLN A 1 207 ? -48.980 40.999 90.755 1.00 74.32 ? 207 GLN A N 1 ATOM 1646 C CA . GLN A 1 207 ? -48.224 39.796 91.064 1.00 74.99 ? 207 GLN A CA 1 ATOM 1647 C C . GLN A 1 207 ? -48.030 39.578 92.569 1.00 77.43 ? 207 GLN A C 1 ATOM 1648 O O . GLN A 1 207 ? -47.986 40.526 93.353 1.00 78.09 ? 207 GLN A O 1 ATOM 1649 C CB . GLN A 1 207 ? -46.870 39.895 90.372 1.00 74.59 ? 207 GLN A CB 1 ATOM 1650 C CG . GLN A 1 207 ? -45.919 38.740 90.604 1.00 74.95 ? 207 GLN A CG 1 ATOM 1651 C CD . GLN A 1 207 ? -44.661 38.885 89.767 1.00 75.36 ? 207 GLN A CD 1 ATOM 1652 O OE1 . GLN A 1 207 ? -43.578 39.159 90.292 1.00 77.37 ? 207 GLN A OE1 1 ATOM 1653 N NE2 . GLN A 1 207 ? -44.801 38.729 88.453 1.00 73.52 ? 207 GLN A NE2 1 ATOM 1654 N N . ARG A 1 208 ? -47.930 38.313 92.960 1.00 78.74 ? 208 ARG A N 1 ATOM 1655 C CA . ARG A 1 208 ? -47.462 37.946 94.293 1.00 81.45 ? 208 ARG A CA 1 ATOM 1656 C C . ARG A 1 208 ? -46.809 36.569 94.234 1.00 82.09 ? 208 ARG A C 1 ATOM 1657 O O . ARG A 1 208 ? -47.498 35.552 94.140 1.00 83.01 ? 208 ARG A O 1 ATOM 1658 C CB . ARG A 1 208 ? -48.599 37.943 95.314 1.00 83.43 ? 208 ARG A CB 1 ATOM 1659 C CG . ARG A 1 208 ? -48.105 37.884 96.753 1.00 85.68 ? 208 ARG A CG 1 ATOM 1660 C CD . ARG A 1 208 ? -49.159 37.329 97.696 1.00 87.86 ? 208 ARG A CD 1 ATOM 1661 N NE . ARG A 1 208 ? -48.809 37.549 99.097 1.00 89.63 ? 208 ARG A NE 1 ATOM 1662 C CZ . ARG A 1 208 ? -48.942 38.708 99.741 1.00 91.27 ? 208 ARG A CZ 1 ATOM 1663 N NH1 . ARG A 1 208 ? -49.421 39.784 99.119 1.00 90.49 ? 208 ARG A NH1 1 ATOM 1664 N NH2 . ARG A 1 208 ? -48.594 38.796 101.022 1.00 94.19 ? 208 ARG A NH2 1 ATOM 1665 N N . LEU A 1 209 ? -45.480 36.543 94.289 1.00 82.20 ? 209 LEU A N 1 ATOM 1666 C CA . LEU A 1 209 ? -44.728 35.301 94.167 1.00 81.24 ? 209 LEU A CA 1 ATOM 1667 C C . LEU A 1 209 ? -44.455 34.742 95.556 1.00 82.43 ? 209 LEU A C 1 ATOM 1668 O O . LEU A 1 209 ? -44.328 35.498 96.511 1.00 83.43 ? 209 LEU A O 1 ATOM 1669 C CB . LEU A 1 209 ? -43.408 35.552 93.440 1.00 80.42 ? 209 LEU A CB 1 ATOM 1670 C CG . LEU A 1 209 ? -43.469 36.353 92.129 1.00 79.90 ? 209 LEU A CG 1 ATOM 1671 C CD1 . LEU A 1 209 ? -42.085 36.880 91.763 1.00 79.54 ? 209 LEU A CD1 1 ATOM 1672 C CD2 . LEU A 1 209 ? -44.064 35.534 90.985 1.00 78.44 ? 209 LEU A CD2 1 ATOM 1673 N N . VAL A 1 210 ? -44.400 33.418 95.662 1.00 82.67 ? 210 VAL A N 1 ATOM 1674 C CA . VAL A 1 210 ? -43.898 32.746 96.859 1.00 84.70 ? 210 VAL A CA 1 ATOM 1675 C C . VAL A 1 210 ? -42.829 31.739 96.437 1.00 84.09 ? 210 VAL A C 1 ATOM 1676 O O . VAL A 1 210 ? -42.906 31.180 95.342 1.00 81.69 ? 210 VAL A O 1 ATOM 1677 C CB . VAL A 1 210 ? -45.009 32.027 97.670 1.00 86.27 ? 210 VAL A CB 1 ATOM 1678 C CG1 . VAL A 1 210 ? -45.966 33.040 98.274 1.00 86.87 ? 210 VAL A CG1 1 ATOM 1679 C CG2 . VAL A 1 210 ? -45.769 31.018 96.816 1.00 85.69 ? 210 VAL A CG2 1 ATOM 1680 N N . PRO A 1 211 ? -41.821 31.510 97.296 1.00 86.15 ? 211 PRO A N 1 ATOM 1681 C CA . PRO A 1 211 ? -40.795 30.531 96.934 1.00 86.47 ? 211 PRO A CA 1 ATOM 1682 C C . PRO A 1 211 ? -41.297 29.092 97.038 1.00 87.06 ? 211 PRO A C 1 ATOM 1683 O O . PRO A 1 211 ? -41.866 28.703 98.056 1.00 88.71 ? 211 PRO A O 1 ATOM 1684 C CB . PRO A 1 211 ? -39.672 30.782 97.959 1.00 88.05 ? 211 PRO A CB 1 ATOM 1685 C CG . PRO A 1 211 ? -40.026 32.050 98.662 1.00 88.57 ? 211 PRO A CG 1 ATOM 1686 C CD . PRO A 1 211 ? -41.512 32.183 98.570 1.00 87.90 ? 211 PRO A CD 1 ATOM 1687 N N . ARG A 1 212 ? -41.136 28.342 95.956 1.00 85.83 ? 212 ARG A N 1 ATOM 1688 C CA . ARG A 1 212 ? -41.312 26.900 95.952 1.00 87.00 ? 212 ARG A CA 1 ATOM 1689 C C . ARG A 1 212 ? -40.041 26.161 96.379 1.00 87.41 ? 212 ARG A C 1 ATOM 1690 O O . ARG A 1 212 ? -39.010 26.230 95.712 1.00 85.73 ? 212 ARG A O 1 ATOM 1691 C CB . ARG A 1 212 ? -41.743 26.438 94.558 1.00 86.57 ? 212 ARG A CB 1 ATOM 1692 C CG . ARG A 1 212 ? -43.177 26.805 94.224 1.00 86.70 ? 212 ARG A CG 1 ATOM 1693 C CD . ARG A 1 212 ? -43.523 26.498 92.776 1.00 85.89 ? 212 ARG A CD 1 ATOM 1694 N NE . ARG A 1 212 ? -43.171 27.615 91.903 1.00 85.59 ? 212 ARG A NE 1 ATOM 1695 C CZ . ARG A 1 212 ? -42.180 27.624 91.012 1.00 86.51 ? 212 ARG A CZ 1 ATOM 1696 N NH1 . ARG A 1 212 ? -41.404 26.564 90.829 1.00 88.64 ? 212 ARG A NH1 1 ATOM 1697 N NH2 . ARG A 1 212 ? -41.965 28.712 90.280 1.00 85.12 ? 212 ARG A NH2 1 ATOM 1698 N N . ILE A 1 213 ? -40.132 25.444 97.495 1.00 89.50 ? 213 ILE A N 1 ATOM 1699 C CA . ILE A 1 213 ? -39.028 24.619 97.974 1.00 90.20 ? 213 ILE A CA 1 ATOM 1700 C C . ILE A 1 213 ? -39.137 23.210 97.393 1.00 89.47 ? 213 ILE A C 1 ATOM 1701 O O . ILE A 1 213 ? -40.215 22.611 97.382 1.00 88.67 ? 213 ILE A O 1 ATOM 1702 C CB . ILE A 1 213 ? -38.993 24.565 99.515 1.00 92.49 ? 213 ILE A CB 1 ATOM 1703 C CG1 . ILE A 1 213 ? -38.597 25.937 100.073 1.00 92.55 ? 213 ILE A CG1 1 ATOM 1704 C CG2 . ILE A 1 213 ? -38.006 23.508 100.004 1.00 94.30 ? 213 ILE A CG2 1 ATOM 1705 C CD1 . ILE A 1 213 ? -39.057 26.174 101.494 1.00 94.55 ? 213 ILE A CD1 1 ATOM 1706 N N . ALA A 1 214 ? -38.009 22.703 96.901 1.00 89.15 ? 214 ALA A N 1 ATOM 1707 C CA . ALA A 1 214 ? -37.903 21.323 96.424 1.00 89.91 ? 214 ALA A CA 1 ATOM 1708 C C . ALA A 1 214 ? -36.439 20.907 96.328 1.00 90.49 ? 214 ALA A C 1 ATOM 1709 O O . ALA A 1 214 ? -35.541 21.754 96.296 1.00 89.89 ? 214 ALA A O 1 ATOM 1710 C CB . ALA A 1 214 ? -38.580 21.171 95.070 1.00 88.22 ? 214 ALA A CB 1 ATOM 1711 N N . THR A 1 215 ? -36.203 19.601 96.285 1.00 91.88 ? 215 THR A N 1 ATOM 1712 C CA . THR A 1 215 ? -34.846 19.074 96.177 1.00 92.42 ? 215 THR A CA 1 ATOM 1713 C C . THR A 1 215 ? -34.538 18.896 94.706 1.00 90.10 ? 215 THR A C 1 ATOM 1714 O O . THR A 1 215 ? -35.243 18.178 94.002 1.00 89.54 ? 215 THR A O 1 ATOM 1715 C CB . THR A 1 215 ? -34.687 17.728 96.914 1.00 95.33 ? 215 THR A CB 1 ATOM 1716 O OG1 . THR A 1 215 ? -35.540 17.704 98.067 1.00 95.74 ? 215 THR A OG1 1 ATOM 1717 C CG2 . THR A 1 215 ? -33.225 17.512 97.343 1.00 96.88 ? 215 THR A CG2 1 ATOM 1718 N N . ARG A 1 216 ? -33.487 19.560 94.244 1.00 89.30 ? 216 ARG A N 1 ATOM 1719 C CA . ARG A 1 216 ? -33.201 19.633 92.823 1.00 87.35 ? 216 ARG A CA 1 ATOM 1720 C C . ARG A 1 216 ? -31.770 19.214 92.536 1.00 88.59 ? 216 ARG A C 1 ATOM 1721 O O . ARG A 1 216 ? -30.870 19.431 93.351 1.00 89.03 ? 216 ARG A O 1 ATOM 1722 C CB . ARG A 1 216 ? -33.407 21.063 92.337 1.00 84.90 ? 216 ARG A CB 1 ATOM 1723 C CG . ARG A 1 216 ? -34.662 21.732 92.869 1.00 84.26 ? 216 ARG A CG 1 ATOM 1724 C CD . ARG A 1 216 ? -34.665 23.221 92.574 1.00 82.70 ? 216 ARG A CD 1 ATOM 1725 N NE . ARG A 1 216 ? -34.384 24.037 93.761 1.00 84.35 ? 216 ARG A NE 1 ATOM 1726 C CZ . ARG A 1 216 ? -35.304 24.555 94.578 1.00 84.36 ? 216 ARG A CZ 1 ATOM 1727 N NH1 . ARG A 1 216 ? -36.600 24.356 94.364 1.00 83.56 ? 216 ARG A NH1 1 ATOM 1728 N NH2 . ARG A 1 216 ? -34.927 25.285 95.623 1.00 85.76 ? 216 ARG A NH2 1 ATOM 1729 N N . SER A 1 217 ? -31.570 18.620 91.364 1.00 88.14 ? 217 SER A N 1 ATOM 1730 C CA . SER A 1 217 ? -30.239 18.284 90.901 1.00 89.90 ? 217 SER A CA 1 ATOM 1731 C C . SER A 1 217 ? -29.427 19.560 90.801 1.00 89.62 ? 217 SER A C 1 ATOM 1732 O O . SER A 1 217 ? -29.934 20.573 90.348 1.00 88.36 ? 217 SER A O 1 ATOM 1733 C CB . SER A 1 217 ? -30.315 17.616 89.532 1.00 89.12 ? 217 SER A CB 1 ATOM 1734 O OG . SER A 1 217 ? -31.324 16.622 89.523 1.00 89.81 ? 217 SER A OG 1 ATOM 1735 N N . LYS A 1 218 ? -28.175 19.521 91.239 1.00 92.38 ? 218 LYS A N 1 ATOM 1736 C CA . LYS A 1 218 ? -27.294 20.671 91.066 1.00 92.39 ? 218 LYS A CA 1 ATOM 1737 C C . LYS A 1 218 ? -27.161 20.987 89.589 1.00 90.05 ? 218 LYS A C 1 ATOM 1738 O O . LYS A 1 218 ? -26.997 20.089 88.770 1.00 90.19 ? 218 LYS A O 1 ATOM 1739 C CB . LYS A 1 218 ? -25.899 20.411 91.646 1.00 95.57 ? 218 LYS A CB 1 ATOM 1740 C CG . LYS A 1 218 ? -25.799 20.626 93.147 1.00 98.18 ? 218 LYS A CG 1 ATOM 1741 C CD . LYS A 1 218 ? -24.511 20.042 93.715 1.00 101.31 ? 218 LYS A CD 1 ATOM 1742 C CE . LYS A 1 218 ? -24.580 18.528 93.886 1.00 103.10 ? 218 LYS A CE 1 ATOM 1743 N NZ . LYS A 1 218 ? -25.214 18.119 95.170 1.00 104.39 ? 218 LYS A NZ 1 ATOM 1744 N N . VAL A 1 219 ? -27.264 22.265 89.254 1.00 88.10 ? 219 VAL A N 1 ATOM 1745 C CA . VAL A 1 219 ? -26.911 22.748 87.933 1.00 86.08 ? 219 VAL A CA 1 ATOM 1746 C C . VAL A 1 219 ? -25.924 23.886 88.127 1.00 86.17 ? 219 VAL A C 1 ATOM 1747 O O . VAL A 1 219 ? -26.218 24.841 88.830 1.00 84.89 ? 219 VAL A O 1 ATOM 1748 C CB . VAL A 1 219 ? -28.150 23.248 87.164 1.00 84.48 ? 219 VAL A CB 1 ATOM 1749 C CG1 . VAL A 1 219 ? -27.762 24.280 86.112 1.00 83.51 ? 219 VAL A CG1 1 ATOM 1750 C CG2 . VAL A 1 219 ? -28.874 22.080 86.507 1.00 84.01 ? 219 VAL A CG2 1 ATOM 1751 N N . ASN A 1 220 ? -24.759 23.791 87.494 1.00 87.38 ? 220 ASN A N 1 ATOM 1752 C CA . ASN A 1 220 ? -23.698 24.780 87.682 1.00 88.36 ? 220 ASN A CA 1 ATOM 1753 C C . ASN A 1 220 ? -23.288 24.844 89.152 1.00 88.95 ? 220 ASN A C 1 ATOM 1754 O O . ASN A 1 220 ? -22.965 25.912 89.666 1.00 89.97 ? 220 ASN A O 1 ATOM 1755 C CB . ASN A 1 220 ? -24.142 26.176 87.201 1.00 87.81 ? 220 ASN A CB 1 ATOM 1756 C CG . ASN A 1 220 ? -23.822 26.435 85.741 1.00 87.52 ? 220 ASN A CG 1 ATOM 1757 O OD1 . ASN A 1 220 ? -23.991 25.568 84.880 1.00 87.05 ? 220 ASN A OD1 1 ATOM 1758 N ND2 . ASN A 1 220 ? -23.379 27.657 85.453 1.00 87.91 ? 220 ASN A ND2 1 ATOM 1759 N N . GLY A 1 221 ? -23.332 23.700 89.830 1.00 88.99 ? 221 GLY A N 1 ATOM 1760 C CA . GLY A 1 221 ? -22.914 23.611 91.224 1.00 90.60 ? 221 GLY A CA 1 ATOM 1761 C C . GLY A 1 221 ? -23.925 24.066 92.267 1.00 89.99 ? 221 GLY A C 1 ATOM 1762 O O . GLY A 1 221 ? -23.603 24.130 93.450 1.00 90.94 ? 221 GLY A O 1 ATOM 1763 N N . GLN A 1 222 ? -25.148 24.377 91.854 1.00 87.68 ? 222 GLN A N 1 ATOM 1764 C CA . GLN A 1 222 ? -26.164 24.812 92.805 1.00 87.43 ? 222 GLN A CA 1 ATOM 1765 C C . GLN A 1 222 ? -27.489 24.115 92.568 1.00 86.24 ? 222 GLN A C 1 ATOM 1766 O O . GLN A 1 222 ? -27.884 23.899 91.427 1.00 85.31 ? 222 GLN A O 1 ATOM 1767 C CB . GLN A 1 222 ? -26.344 26.328 92.720 1.00 86.46 ? 222 GLN A CB 1 ATOM 1768 C CG . GLN A 1 222 ? -25.079 27.121 93.028 1.00 88.13 ? 222 GLN A CG 1 ATOM 1769 C CD . GLN A 1 222 ? -24.599 26.934 94.454 1.00 90.60 ? 222 GLN A CD 1 ATOM 1770 O OE1 . GLN A 1 222 ? -25.358 26.498 95.321 1.00 90.87 ? 222 GLN A OE1 1 ATOM 1771 N NE2 . GLN A 1 222 ? -23.335 27.259 94.702 1.00 92.39 ? 222 GLN A NE2 1 ATOM 1772 N N . SER A 1 223 ? -28.164 23.751 93.655 1.00 87.69 ? 223 SER A N 1 ATOM 1773 C CA . SER A 1 223 ? -29.486 23.132 93.579 1.00 86.94 ? 223 SER A CA 1 ATOM 1774 C C . SER A 1 223 ? -30.590 24.172 93.767 1.00 85.58 ? 223 SER A C 1 ATOM 1775 O O . SER A 1 223 ? -31.761 23.882 93.534 1.00 83.66 ? 223 SER A O 1 ATOM 1776 C CB . SER A 1 223 ? -29.617 22.007 94.611 1.00 89.56 ? 223 SER A CB 1 ATOM 1777 O OG . SER A 1 223 ? -29.013 20.817 94.145 1.00 90.98 ? 223 SER A OG 1 ATOM 1778 N N . GLY A 1 224 ? -30.215 25.379 94.186 1.00 86.63 ? 224 GLY A N 1 ATOM 1779 C CA . GLY A 1 224 ? -31.164 26.483 94.331 1.00 86.33 ? 224 GLY A CA 1 ATOM 1780 C C . GLY A 1 224 ? -31.506 27.086 92.984 1.00 84.55 ? 224 GLY A C 1 ATOM 1781 O O . GLY A 1 224 ? -30.729 26.965 92.035 1.00 85.36 ? 224 GLY A O 1 ATOM 1782 N N . ARG A 1 225 ? -32.666 27.738 92.897 1.00 83.83 ? 225 ARG A N 1 ATOM 1783 C CA . ARG A 1 225 ? -33.171 28.267 91.619 1.00 81.68 ? 225 ARG A CA 1 ATOM 1784 C C . ARG A 1 225 ? -33.567 29.737 91.695 1.00 81.14 ? 225 ARG A C 1 ATOM 1785 O O . ARG A 1 225 ? -34.005 30.219 92.735 1.00 82.06 ? 225 ARG A O 1 ATOM 1786 C CB . ARG A 1 225 ? -34.375 27.453 91.143 1.00 80.27 ? 225 ARG A CB 1 ATOM 1787 C CG . ARG A 1 225 ? -34.067 26.001 90.813 1.00 80.96 ? 225 ARG A CG 1 ATOM 1788 C CD . ARG A 1 225 ? -33.383 25.849 89.465 1.00 80.35 ? 225 ARG A CD 1 ATOM 1789 N NE . ARG A 1 225 ? -33.114 24.445 89.169 1.00 81.22 ? 225 ARG A NE 1 ATOM 1790 C CZ . ARG A 1 225 ? -32.083 23.748 89.645 1.00 82.81 ? 225 ARG A CZ 1 ATOM 1791 N NH1 . ARG A 1 225 ? -31.188 24.307 90.459 1.00 83.54 ? 225 ARG A NH1 1 ATOM 1792 N NH2 . ARG A 1 225 ? -31.946 22.475 89.302 1.00 83.77 ? 225 ARG A NH2 1 ATOM 1793 N N . MET A 1 226 ? -33.410 30.435 90.574 1.00 80.77 ? 226 MET A N 1 ATOM 1794 C CA . MET A 1 226 ? -33.814 31.829 90.448 1.00 80.26 ? 226 MET A CA 1 ATOM 1795 C C . MET A 1 226 ? -34.787 31.953 89.287 1.00 77.94 ? 226 MET A C 1 ATOM 1796 O O . MET A 1 226 ? -34.439 31.653 88.151 1.00 78.36 ? 226 MET A O 1 ATOM 1797 C CB . MET A 1 226 ? -32.601 32.715 90.177 1.00 81.50 ? 226 MET A CB 1 ATOM 1798 C CG . MET A 1 226 ? -31.656 32.874 91.354 1.00 84.08 ? 226 MET A CG 1 ATOM 1799 S SD . MET A 1 226 ? -32.232 34.055 92.589 1.00 86.14 ? 226 MET A SD 1 ATOM 1800 C CE . MET A 1 226 ? -30.721 34.275 93.526 1.00 89.13 ? 226 MET A CE 1 ATOM 1801 N N . GLU A 1 227 ? -36.007 32.392 89.579 1.00 76.24 ? 227 GLU A N 1 ATOM 1802 C CA . GLU A 1 227 ? -37.023 32.607 88.559 1.00 73.71 ? 227 GLU A CA 1 ATOM 1803 C C . GLU A 1 227 ? -37.145 34.104 88.313 1.00 72.10 ? 227 GLU A C 1 ATOM 1804 O O . GLU A 1 227 ? -37.390 34.869 89.245 1.00 72.07 ? 227 GLU A O 1 ATOM 1805 C CB . GLU A 1 227 ? -38.354 32.028 89.026 1.00 74.27 ? 227 GLU A CB 1 ATOM 1806 C CG . GLU A 1 227 ? -39.419 31.929 87.948 1.00 73.76 ? 227 GLU A CG 1 ATOM 1807 C CD . GLU A 1 227 ? -40.652 31.184 88.423 1.00 74.65 ? 227 GLU A CD 1 ATOM 1808 O OE1 . GLU A 1 227 ? -40.771 30.926 89.641 1.00 75.66 ? 227 GLU A OE1 1 ATOM 1809 O OE2 . GLU A 1 227 ? -41.506 30.849 87.576 1.00 75.18 ? 227 GLU A OE2 1 ATOM 1810 N N . PHE A 1 228 ? -36.967 34.523 87.063 1.00 69.85 ? 228 PHE A N 1 ATOM 1811 C CA . PHE A 1 228 ? -36.917 35.943 86.740 1.00 68.60 ? 228 PHE A CA 1 ATOM 1812 C C . PHE A 1 228 ? -38.166 36.385 86.003 1.00 67.20 ? 228 PHE A C 1 ATOM 1813 O O . PHE A 1 228 ? -38.645 35.694 85.108 1.00 66.25 ? 228 PHE A O 1 ATOM 1814 C CB . PHE A 1 228 ? -35.672 36.253 85.916 1.00 68.49 ? 228 PHE A CB 1 ATOM 1815 C CG . PHE A 1 228 ? -34.398 36.086 86.681 1.00 69.19 ? 228 PHE A CG 1 ATOM 1816 C CD1 . PHE A 1 228 ? -33.910 37.115 87.464 1.00 70.42 ? 228 PHE A CD1 1 ATOM 1817 C CD2 . PHE A 1 228 ? -33.700 34.888 86.641 1.00 69.71 ? 228 PHE A CD2 1 ATOM 1818 C CE1 . PHE A 1 228 ? -32.738 36.961 88.185 1.00 71.67 ? 228 PHE A CE1 1 ATOM 1819 C CE2 . PHE A 1 228 ? -32.526 34.724 87.360 1.00 70.83 ? 228 PHE A CE2 1 ATOM 1820 C CZ . PHE A 1 228 ? -32.046 35.762 88.134 1.00 71.77 ? 228 PHE A CZ 1 ATOM 1821 N N . PHE A 1 229 ? -38.684 37.543 86.400 1.00 67.38 ? 229 PHE A N 1 ATOM 1822 C CA . PHE A 1 229 ? -39.891 38.118 85.813 1.00 66.78 ? 229 PHE A CA 1 ATOM 1823 C C . PHE A 1 229 ? -39.611 39.503 85.270 1.00 67.12 ? 229 PHE A C 1 ATOM 1824 O O . PHE A 1 229 ? -38.627 40.147 85.645 1.00 68.05 ? 229 PHE A O 1 ATOM 1825 C CB . PHE A 1 229 ? -40.997 38.207 86.857 1.00 66.94 ? 229 PHE A CB 1 ATOM 1826 C CG . PHE A 1 229 ? -41.455 36.877 87.345 1.00 67.50 ? 229 PHE A CG 1 ATOM 1827 C CD1 . PHE A 1 229 ? -40.742 36.207 88.322 1.00 68.09 ? 229 PHE A CD1 1 ATOM 1828 C CD2 . PHE A 1 229 ? -42.589 36.274 86.805 1.00 67.62 ? 229 PHE A CD2 1 ATOM 1829 C CE1 . PHE A 1 229 ? -41.155 34.966 88.772 1.00 68.59 ? 229 PHE A CE1 1 ATOM 1830 C CE2 . PHE A 1 229 ? -43.007 35.031 87.250 1.00 67.70 ? 229 PHE A CE2 1 ATOM 1831 C CZ . PHE A 1 229 ? -42.288 34.376 88.238 1.00 68.36 ? 229 PHE A CZ 1 ATOM 1832 N N . TRP A 1 230 ? -40.491 39.967 84.394 1.00 66.46 ? 230 TRP A N 1 ATOM 1833 C CA . TRP A 1 230 ? -40.333 41.281 83.812 1.00 66.67 ? 230 TRP A CA 1 ATOM 1834 C C . TRP A 1 230 ? -41.667 41.961 83.586 1.00 66.25 ? 230 TRP A C 1 ATOM 1835 O O . TRP A 1 230 ? -42.706 41.320 83.616 1.00 65.92 ? 230 TRP A O 1 ATOM 1836 C CB . TRP A 1 230 ? -39.575 41.164 82.496 1.00 66.50 ? 230 TRP A CB 1 ATOM 1837 C CG . TRP A 1 230 ? -40.234 40.311 81.476 1.00 65.89 ? 230 TRP A CG 1 ATOM 1838 C CD1 . TRP A 1 230 ? -40.086 38.970 81.316 1.00 66.04 ? 230 TRP A CD1 1 ATOM 1839 C CD2 . TRP A 1 230 ? -41.130 40.743 80.453 1.00 65.90 ? 230 TRP A CD2 1 ATOM 1840 N NE1 . TRP A 1 230 ? -40.842 38.530 80.259 1.00 65.77 ? 230 TRP A NE1 1 ATOM 1841 C CE2 . TRP A 1 230 ? -41.493 39.603 79.710 1.00 66.00 ? 230 TRP A CE2 1 ATOM 1842 C CE3 . TRP A 1 230 ? -41.666 41.984 80.094 1.00 66.85 ? 230 TRP A CE3 1 ATOM 1843 C CZ2 . TRP A 1 230 ? -42.366 39.665 78.622 1.00 66.47 ? 230 TRP A CZ2 1 ATOM 1844 C CZ3 . TRP A 1 230 ? -42.540 42.046 79.013 1.00 67.07 ? 230 TRP A CZ3 1 ATOM 1845 C CH2 . TRP A 1 230 ? -42.882 40.894 78.293 1.00 66.64 ? 230 TRP A CH2 1 ATOM 1846 N N . THR A 1 231 ? -41.623 43.268 83.372 1.00 66.55 ? 231 THR A N 1 ATOM 1847 C CA . THR A 1 231 ? -42.780 44.000 82.881 1.00 66.66 ? 231 THR A CA 1 ATOM 1848 C C . THR A 1 231 ? -42.326 45.208 82.071 1.00 68.10 ? 231 THR A C 1 ATOM 1849 O O . THR A 1 231 ? -41.160 45.592 82.120 1.00 69.58 ? 231 THR A O 1 ATOM 1850 C CB . THR A 1 231 ? -43.689 44.459 84.035 1.00 66.55 ? 231 THR A CB 1 ATOM 1851 O OG1 . THR A 1 231 ? -44.927 44.941 83.509 1.00 65.80 ? 231 THR A OG1 1 ATOM 1852 C CG2 . THR A 1 231 ? -43.035 45.554 84.854 1.00 67.60 ? 231 THR A CG2 1 ATOM 1853 N N . ILE A 1 232 ? -43.240 45.785 81.305 1.00 68.63 ? 232 ILE A N 1 ATOM 1854 C CA . ILE A 1 232 ? -43.013 47.090 80.708 1.00 69.83 ? 232 ILE A CA 1 ATOM 1855 C C . ILE A 1 232 ? -43.755 48.090 81.572 1.00 70.97 ? 232 ILE A C 1 ATOM 1856 O O . ILE A 1 232 ? -44.974 48.048 81.688 1.00 70.54 ? 232 ILE A O 1 ATOM 1857 C CB . ILE A 1 232 ? -43.472 47.163 79.234 1.00 69.77 ? 232 ILE A CB 1 ATOM 1858 C CG1 . ILE A 1 232 ? -42.323 46.809 78.288 1.00 69.15 ? 232 ILE A CG1 1 ATOM 1859 C CG2 . ILE A 1 232 ? -43.916 48.573 78.863 1.00 71.54 ? 232 ILE A CG2 1 ATOM 1860 C CD1 . ILE A 1 232 ? -41.536 45.587 78.681 1.00 68.42 ? 232 ILE A CD1 1 ATOM 1861 N N . LEU A 1 233 ? -43.002 48.976 82.203 1.00 73.54 ? 233 LEU A N 1 ATOM 1862 C CA . LEU A 1 233 ? -43.592 50.046 82.985 1.00 75.40 ? 233 LEU A CA 1 ATOM 1863 C C . LEU A 1 233 ? -43.829 51.210 82.045 1.00 76.72 ? 233 LEU A C 1 ATOM 1864 O O . LEU A 1 233 ? -42.896 51.706 81.421 1.00 76.67 ? 233 LEU A O 1 ATOM 1865 C CB . LEU A 1 233 ? -42.661 50.449 84.130 1.00 76.40 ? 233 LEU A CB 1 ATOM 1866 C CG . LEU A 1 233 ? -43.221 51.402 85.185 1.00 77.94 ? 233 LEU A CG 1 ATOM 1867 C CD1 . LEU A 1 233 ? -44.445 50.807 85.873 1.00 77.36 ? 233 LEU A CD1 1 ATOM 1868 C CD2 . LEU A 1 233 ? -42.132 51.753 86.190 1.00 79.05 ? 233 LEU A CD2 1 ATOM 1869 N N . LYS A 1 234 ? -45.080 51.637 81.941 1.00 78.74 ? 234 LYS A N 1 ATOM 1870 C CA . LYS A 1 234 ? -45.430 52.728 81.040 1.00 82.68 ? 234 LYS A CA 1 ATOM 1871 C C . LYS A 1 234 ? -44.937 54.044 81.623 1.00 84.81 ? 234 LYS A C 1 ATOM 1872 O O . LYS A 1 234 ? -44.607 54.104 82.808 1.00 85.14 ? 234 LYS A O 1 ATOM 1873 C CB . LYS A 1 234 ? -46.946 52.770 80.804 1.00 85.29 ? 234 LYS A CB 1 ATOM 1874 C CG . LYS A 1 234 ? -47.558 51.416 80.435 1.00 85.48 ? 234 LYS A CG 1 ATOM 1875 C CD . LYS A 1 234 ? -48.365 51.460 79.148 1.00 86.95 ? 234 LYS A CD 1 ATOM 1876 C CE . LYS A 1 234 ? -47.447 51.435 77.933 1.00 88.81 ? 234 LYS A CE 1 ATOM 1877 N NZ . LYS A 1 234 ? -48.192 51.541 76.643 1.00 90.76 ? 234 LYS A NZ 1 ATOM 1878 N N . PRO A 1 235 ? -44.864 55.105 80.796 1.00 87.75 ? 235 PRO A N 1 ATOM 1879 C CA . PRO A 1 235 ? -44.475 56.404 81.354 1.00 89.49 ? 235 PRO A CA 1 ATOM 1880 C C . PRO A 1 235 ? -45.524 56.911 82.334 1.00 90.88 ? 235 PRO A C 1 ATOM 1881 O O . PRO A 1 235 ? -46.714 56.632 82.158 1.00 90.15 ? 235 PRO A O 1 ATOM 1882 C CB . PRO A 1 235 ? -44.385 57.307 80.120 1.00 90.71 ? 235 PRO A CB 1 ATOM 1883 C CG . PRO A 1 235 ? -45.244 56.648 79.095 1.00 89.74 ? 235 PRO A CG 1 ATOM 1884 C CD . PRO A 1 235 ? -45.080 55.181 79.339 1.00 87.47 ? 235 PRO A CD 1 ATOM 1885 N N . ASN A 1 236 ? -45.076 57.611 83.373 1.00 93.10 ? 236 ASN A N 1 ATOM 1886 C CA . ASN A 1 236 ? -45.953 58.104 84.433 1.00 95.76 ? 236 ASN A CA 1 ATOM 1887 C C . ASN A 1 236 ? -46.696 57.034 85.224 1.00 95.20 ? 236 ASN A C 1 ATOM 1888 O O . ASN A 1 236 ? -47.609 57.353 85.985 1.00 97.33 ? 236 ASN A O 1 ATOM 1889 C CB . ASN A 1 236 ? -46.953 59.130 83.879 1.00 98.24 ? 236 ASN A CB 1 ATOM 1890 C CG . ASN A 1 236 ? -46.481 60.551 84.063 1.00 103.39 ? 236 ASN A CG 1 ATOM 1891 O OD1 . ASN A 1 236 ? -45.489 60.809 84.753 1.00 104.93 ? 236 ASN A OD1 1 ATOM 1892 N ND2 . ASN A 1 236 ? -47.193 61.491 83.452 1.00 106.47 ? 236 ASN A ND2 1 ATOM 1893 N N . ASP A 1 237 ? -46.314 55.772 85.054 1.00 93.08 ? 237 ASP A N 1 ATOM 1894 C CA . ASP A 1 237 ? -46.802 54.713 85.925 1.00 92.26 ? 237 ASP A CA 1 ATOM 1895 C C . ASP A 1 237 ? -45.700 54.407 86.938 1.00 91.22 ? 237 ASP A C 1 ATOM 1896 O O . ASP A 1 237 ? -44.519 54.690 86.704 1.00 90.94 ? 237 ASP A O 1 ATOM 1897 C CB . ASP A 1 237 ? -47.177 53.459 85.117 1.00 91.13 ? 237 ASP A CB 1 ATOM 1898 C CG . ASP A 1 237 ? -48.062 52.474 85.902 1.00 90.64 ? 237 ASP A CG 1 ATOM 1899 O OD1 . ASP A 1 237 ? -48.656 52.863 86.933 1.00 91.06 ? 237 ASP A OD1 1 ATOM 1900 O OD2 . ASP A 1 237 ? -48.171 51.300 85.473 1.00 89.37 ? 237 ASP A OD2 1 ATOM 1901 N N . ALA A 1 238 ? -46.099 53.845 88.072 1.00 89.98 ? 238 ALA A N 1 ATOM 1902 C CA . ALA A 1 238 ? -45.164 53.468 89.114 1.00 89.26 ? 238 ALA A CA 1 ATOM 1903 C C . ALA A 1 238 ? -45.245 51.968 89.343 1.00 86.28 ? 238 ALA A C 1 ATOM 1904 O O . ALA A 1 238 ? -46.319 51.377 89.225 1.00 84.97 ? 238 ALA A O 1 ATOM 1905 C CB . ALA A 1 238 ? -45.478 54.222 90.399 1.00 90.71 ? 238 ALA A CB 1 ATOM 1906 N N . ILE A 1 239 ? -44.103 51.358 89.650 1.00 84.89 ? 239 ILE A N 1 ATOM 1907 C CA . ILE A 1 239 ? -44.058 49.954 90.069 1.00 82.86 ? 239 ILE A CA 1 ATOM 1908 C C . ILE A 1 239 ? -43.828 49.873 91.591 1.00 84.11 ? 239 ILE A C 1 ATOM 1909 O O . ILE A 1 239 ? -43.078 50.671 92.151 1.00 85.59 ? 239 ILE A O 1 ATOM 1910 C CB . ILE A 1 239 ? -42.995 49.152 89.279 1.00 80.52 ? 239 ILE A CB 1 ATOM 1911 C CG1 . ILE A 1 239 ? -43.148 47.657 89.557 1.00 79.29 ? 239 ILE A CG1 1 ATOM 1912 C CG2 . ILE A 1 239 ? -41.579 49.604 89.610 1.00 81.61 ? 239 ILE A CG2 1 ATOM 1913 C CD1 . ILE A 1 239 ? -42.376 46.781 88.598 1.00 77.90 ? 239 ILE A CD1 1 ATOM 1914 N N . ASN A 1 240 ? -44.489 48.924 92.251 1.00 83.72 ? 240 ASN A N 1 ATOM 1915 C CA . ASN A 1 240 ? -44.443 48.806 93.714 1.00 85.60 ? 240 ASN A CA 1 ATOM 1916 C C . ASN A 1 240 ? -44.034 47.417 94.180 1.00 85.21 ? 240 ASN A C 1 ATOM 1917 O O . ASN A 1 240 ? -44.785 46.455 94.013 1.00 84.08 ? 240 ASN A O 1 ATOM 1918 C CB . ASN A 1 240 ? -45.806 49.119 94.310 1.00 86.47 ? 240 ASN A CB 1 ATOM 1919 C CG . ASN A 1 240 ? -46.205 50.563 94.121 1.00 88.21 ? 240 ASN A CG 1 ATOM 1920 O OD1 . ASN A 1 240 ? -45.435 51.472 94.421 1.00 88.78 ? 240 ASN A OD1 1 ATOM 1921 N ND2 . ASN A 1 240 ? -47.421 50.785 93.626 1.00 88.40 ? 240 ASN A ND2 1 ATOM 1922 N N . PHE A 1 241 ? -42.850 47.324 94.778 1.00 85.92 ? 241 PHE A N 1 ATOM 1923 C CA . PHE A 1 241 ? -42.370 46.073 95.342 1.00 85.84 ? 241 PHE A CA 1 ATOM 1924 C C . PHE A 1 241 ? -42.641 46.010 96.837 1.00 87.68 ? 241 PHE A C 1 ATOM 1925 O O . PHE A 1 241 ? -42.590 47.024 97.529 1.00 90.52 ? 241 PHE A O 1 ATOM 1926 C CB . PHE A 1 241 ? -40.876 45.912 95.083 1.00 85.70 ? 241 PHE A CB 1 ATOM 1927 C CG . PHE A 1 241 ? -40.545 45.660 93.648 1.00 84.43 ? 241 PHE A CG 1 ATOM 1928 C CD1 . PHE A 1 241 ? -40.832 44.431 93.068 1.00 83.54 ? 241 PHE A CD1 1 ATOM 1929 C CD2 . PHE A 1 241 ? -39.968 46.648 92.867 1.00 85.01 ? 241 PHE A CD2 1 ATOM 1930 C CE1 . PHE A 1 241 ? -40.539 44.189 91.737 1.00 82.56 ? 241 PHE A CE1 1 ATOM 1931 C CE2 . PHE A 1 241 ? -39.669 46.414 91.533 1.00 83.91 ? 241 PHE A CE2 1 ATOM 1932 C CZ . PHE A 1 241 ? -39.956 45.183 90.967 1.00 82.63 ? 241 PHE A CZ 1 ATOM 1933 N N . GLU A 1 242 ? -42.950 44.814 97.324 1.00 87.17 ? 242 GLU A N 1 ATOM 1934 C CA . GLU A 1 242 ? -43.006 44.554 98.755 1.00 89.21 ? 242 GLU A CA 1 ATOM 1935 C C . GLU A 1 242 ? -42.648 43.093 99.019 1.00 88.70 ? 242 GLU A C 1 ATOM 1936 O O . GLU A 1 242 ? -43.264 42.187 98.448 1.00 87.82 ? 242 GLU A O 1 ATOM 1937 C CB . GLU A 1 242 ? -44.390 44.893 99.327 1.00 90.79 ? 242 GLU A CB 1 ATOM 1938 C CG . GLU A 1 242 ? -44.559 44.540 100.809 1.00 93.38 ? 242 GLU A CG 1 ATOM 1939 C CD . GLU A 1 242 ? -45.964 44.788 101.337 1.00 94.11 ? 242 GLU A CD 1 ATOM 1940 O OE1 . GLU A 1 242 ? -46.615 45.753 100.889 1.00 94.56 ? 242 GLU A OE1 1 ATOM 1941 O OE2 . GLU A 1 242 ? -46.414 44.022 102.213 1.00 94.61 ? 242 GLU A OE2 1 ATOM 1942 N N . SER A 1 243 ? -41.656 42.862 99.874 1.00 89.33 ? 243 SER A N 1 ATOM 1943 C CA . SER A 1 243 ? -41.250 41.496 100.197 1.00 89.42 ? 243 SER A CA 1 ATOM 1944 C C . SER A 1 243 ? -40.626 41.373 101.578 1.00 91.68 ? 243 SER A C 1 ATOM 1945 O O . SER A 1 243 ? -40.048 42.330 102.087 1.00 94.36 ? 243 SER A O 1 ATOM 1946 C CB . SER A 1 243 ? -40.267 40.976 99.150 1.00 87.80 ? 243 SER A CB 1 ATOM 1947 O OG . SER A 1 243 ? -39.902 39.632 99.419 1.00 87.46 ? 243 SER A OG 1 ATOM 1948 N N . ASN A 1 244 ? -40.738 40.179 102.160 1.00 91.69 ? 244 ASN A N 1 ATOM 1949 C CA . ASN A 1 244 ? -40.133 39.852 103.462 1.00 93.94 ? 244 ASN A CA 1 ATOM 1950 C C . ASN A 1 244 ? -39.100 38.718 103.351 1.00 93.60 ? 244 ASN A C 1 ATOM 1951 O O . ASN A 1 244 ? -38.863 37.994 104.315 1.00 95.40 ? 244 ASN A O 1 ATOM 1952 C CB . ASN A 1 244 ? -41.226 39.448 104.452 1.00 94.72 ? 244 ASN A CB 1 ATOM 1953 C CG . ASN A 1 244 ? -41.971 38.204 104.011 1.00 93.23 ? 244 ASN A CG 1 ATOM 1954 O OD1 . ASN A 1 244 ? -41.980 37.865 102.827 1.00 90.70 ? 244 ASN A OD1 1 ATOM 1955 N ND2 . ASN A 1 244 ? -42.595 37.518 104.954 1.00 94.60 ? 244 ASN A ND2 1 ATOM 1956 N N . GLY A 1 245 ? -38.498 38.579 102.171 1.00 92.13 ? 245 GLY A N 1 ATOM 1957 C CA . GLY A 1 245 ? -37.507 37.537 101.900 1.00 92.06 ? 245 GLY A CA 1 ATOM 1958 C C . GLY A 1 245 ? -37.558 37.022 100.467 1.00 89.50 ? 245 GLY A C 1 ATOM 1959 O O . GLY A 1 245 ? -38.585 37.130 99.789 1.00 87.49 ? 245 GLY A O 1 ATOM 1960 N N . ASN A 1 246 ? -36.433 36.463 100.021 1.00 89.33 ? 246 ASN A N 1 ATOM 1961 C CA . ASN A 1 246 ? -36.298 35.823 98.705 1.00 87.12 ? 246 ASN A CA 1 ATOM 1962 C C . ASN A 1 246 ? -36.431 36.790 97.525 1.00 85.31 ? 246 ASN A C 1 ATOM 1963 O O . ASN A 1 246 ? -36.656 36.363 96.393 1.00 83.54 ? 246 ASN A O 1 ATOM 1964 C CB . ASN A 1 246 ? -37.291 34.654 98.543 1.00 86.41 ? 246 ASN A CB 1 ATOM 1965 C CG . ASN A 1 246 ? -37.180 33.622 99.657 1.00 88.57 ? 246 ASN A CG 1 ATOM 1966 O OD1 . ASN A 1 246 ? -37.677 33.832 100.765 1.00 89.81 ? 246 ASN A OD1 1 ATOM 1967 N ND2 . ASN A 1 246 ? -36.545 32.490 99.358 1.00 88.50 ? 246 ASN A ND2 1 ATOM 1968 N N . PHE A 1 247 ? -36.253 38.085 97.780 1.00 86.20 ? 247 PHE A N 1 ATOM 1969 C CA . PHE A 1 247 ? -36.449 39.112 96.754 1.00 83.55 ? 247 PHE A CA 1 ATOM 1970 C C . PHE A 1 247 ? -35.138 39.467 96.070 1.00 83.01 ? 247 PHE A C 1 ATOM 1971 O O . PHE A 1 247 ? -34.161 39.834 96.723 1.00 85.04 ? 247 PHE A O 1 ATOM 1972 C CB . PHE A 1 247 ? -37.075 40.359 97.385 1.00 84.60 ? 247 PHE A CB 1 ATOM 1973 C CG . PHE A 1 247 ? -37.334 41.486 96.418 1.00 83.12 ? 247 PHE A CG 1 ATOM 1974 C CD1 . PHE A 1 247 ? -37.942 41.254 95.196 1.00 80.81 ? 247 PHE A CD1 1 ATOM 1975 C CD2 . PHE A 1 247 ? -37.004 42.789 96.757 1.00 84.03 ? 247 PHE A CD2 1 ATOM 1976 C CE1 . PHE A 1 247 ? -38.188 42.293 94.318 1.00 79.93 ? 247 PHE A CE1 1 ATOM 1977 C CE2 . PHE A 1 247 ? -37.256 43.830 95.888 1.00 83.24 ? 247 PHE A CE2 1 ATOM 1978 C CZ . PHE A 1 247 ? -37.847 43.582 94.665 1.00 81.27 ? 247 PHE A CZ 1 ATOM 1979 N N . ILE A 1 248 ? -35.125 39.325 94.749 1.00 81.66 ? 248 ILE A N 1 ATOM 1980 C CA . ILE A 1 248 ? -34.012 39.763 93.919 1.00 81.31 ? 248 ILE A CA 1 ATOM 1981 C C . ILE A 1 248 ? -34.467 41.072 93.299 1.00 80.49 ? 248 ILE A C 1 ATOM 1982 O O . ILE A 1 248 ? -35.334 41.084 92.430 1.00 77.82 ? 248 ILE A O 1 ATOM 1983 C CB . ILE A 1 248 ? -33.674 38.731 92.822 1.00 79.77 ? 248 ILE A CB 1 ATOM 1984 C CG1 . ILE A 1 248 ? -33.633 37.313 93.400 1.00 80.51 ? 248 ILE A CG1 1 ATOM 1985 C CG2 . ILE A 1 248 ? -32.349 39.067 92.161 1.00 80.33 ? 248 ILE A CG2 1 ATOM 1986 C CD1 . ILE A 1 248 ? -32.855 37.179 94.696 1.00 83.29 ? 248 ILE A CD1 1 ATOM 1987 N N . ALA A 1 249 ? -33.901 42.176 93.770 1.00 82.22 ? 249 ALA A N 1 ATOM 1988 C CA . ALA A 1 249 ? -34.417 43.496 93.428 1.00 82.88 ? 249 ALA A CA 1 ATOM 1989 C C . ALA A 1 249 ? -33.788 44.067 92.162 1.00 82.79 ? 249 ALA A C 1 ATOM 1990 O O . ALA A 1 249 ? -32.644 43.747 91.839 1.00 82.75 ? 249 ALA A O 1 ATOM 1991 C CB . ALA A 1 249 ? -34.199 44.452 94.584 1.00 85.25 ? 249 ALA A CB 1 ATOM 1992 N N . PRO A 1 250 ? -34.539 44.920 91.441 1.00 82.76 ? 250 PRO A N 1 ATOM 1993 C CA . PRO A 1 250 ? -33.930 45.653 90.338 1.00 83.13 ? 250 PRO A CA 1 ATOM 1994 C C . PRO A 1 250 ? -32.887 46.648 90.836 1.00 86.02 ? 250 PRO A C 1 ATOM 1995 O O . PRO A 1 250 ? -33.101 47.301 91.852 1.00 88.03 ? 250 PRO A O 1 ATOM 1996 C CB . PRO A 1 250 ? -35.114 46.397 89.699 1.00 81.71 ? 250 PRO A CB 1 ATOM 1997 C CG . PRO A 1 250 ? -36.189 46.403 90.719 1.00 81.55 ? 250 PRO A CG 1 ATOM 1998 C CD . PRO A 1 250 ? -35.991 45.163 91.531 1.00 81.74 ? 250 PRO A CD 1 ATOM 1999 N N . GLU A 1 251 ? -31.761 46.730 90.132 1.00 87.45 ? 251 GLU A N 1 ATOM 2000 C CA . GLU A 1 251 ? -30.776 47.793 90.336 1.00 90.14 ? 251 GLU A CA 1 ATOM 2001 C C . GLU A 1 251 ? -30.954 48.740 89.149 1.00 89.36 ? 251 GLU A C 1 ATOM 2002 O O . GLU A 1 251 ? -31.349 49.903 89.310 1.00 89.08 ? 251 GLU A O 1 ATOM 2003 C CB . GLU A 1 251 ? -29.351 47.206 90.380 1.00 91.55 ? 251 GLU A CB 1 ATOM 2004 C CG . GLU A 1 251 ? -28.499 47.616 91.573 1.00 94.63 ? 251 GLU A CG 1 ATOM 2005 C CD . GLU A 1 251 ? -27.530 48.747 91.280 1.00 96.98 ? 251 GLU A CD 1 ATOM 2006 O OE1 . GLU A 1 251 ? -27.922 49.928 91.402 1.00 97.49 ? 251 GLU A OE1 1 ATOM 2007 O OE2 . GLU A 1 251 ? -26.357 48.445 90.967 1.00 97.98 ? 251 GLU A OE2 1 ATOM 2008 N N . TYR A 1 252 ? -30.698 48.200 87.955 1.00 87.91 ? 252 TYR A N 1 ATOM 2009 C CA . TYR A 1 252 ? -30.840 48.921 86.700 1.00 88.05 ? 252 TYR A CA 1 ATOM 2010 C C . TYR A 1 252 ? -32.014 48.351 85.914 1.00 85.97 ? 252 TYR A C 1 ATOM 2011 O O . TYR A 1 252 ? -32.281 47.156 85.967 1.00 84.60 ? 252 TYR A O 1 ATOM 2012 C CB . TYR A 1 252 ? -29.573 48.778 85.854 1.00 89.25 ? 252 TYR A CB 1 ATOM 2013 C CG . TYR A 1 252 ? -28.297 49.226 86.532 1.00 92.86 ? 252 TYR A CG 1 ATOM 2014 C CD1 . TYR A 1 252 ? -27.911 50.564 86.517 1.00 95.40 ? 252 TYR A CD1 1 ATOM 2015 C CD2 . TYR A 1 252 ? -27.469 48.310 87.181 1.00 93.30 ? 252 TYR A CD2 1 ATOM 2016 C CE1 . TYR A 1 252 ? -26.742 50.980 87.135 1.00 97.70 ? 252 TYR A CE1 1 ATOM 2017 C CE2 . TYR A 1 252 ? -26.298 48.716 87.798 1.00 95.62 ? 252 TYR A CE2 1 ATOM 2018 C CZ . TYR A 1 252 ? -25.936 50.054 87.772 1.00 97.82 ? 252 TYR A CZ 1 ATOM 2019 O OH . TYR A 1 252 ? -24.773 50.472 88.385 1.00 99.51 ? 252 TYR A OH 1 ATOM 2020 N N . ALA A 1 253 ? -32.708 49.221 85.188 1.00 85.75 ? 253 ALA A N 1 ATOM 2021 C CA . ALA A 1 253 ? -33.756 48.816 84.259 1.00 83.47 ? 253 ALA A CA 1 ATOM 2022 C C . ALA A 1 253 ? -33.552 49.550 82.930 1.00 83.37 ? 253 ALA A C 1 ATOM 2023 O O . ALA A 1 253 ? -33.068 50.690 82.908 1.00 84.27 ? 253 ALA A O 1 ATOM 2024 C CB . ALA A 1 253 ? -35.124 49.127 84.847 1.00 83.70 ? 253 ALA A CB 1 ATOM 2025 N N . TYR A 1 254 ? -33.932 48.894 81.836 1.00 80.91 ? 254 TYR A N 1 ATOM 2026 C CA . TYR A 1 254 ? -33.608 49.370 80.496 1.00 80.40 ? 254 TYR A CA 1 ATOM 2027 C C . TYR A 1 254 ? -34.667 50.309 79.938 1.00 81.47 ? 254 TYR A C 1 ATOM 2028 O O . TYR A 1 254 ? -35.854 50.009 79.971 1.00 81.27 ? 254 TYR A O 1 ATOM 2029 C CB . TYR A 1 254 ? -33.446 48.190 79.548 1.00 77.87 ? 254 TYR A CB 1 ATOM 2030 C CG . TYR A 1 254 ? -32.231 47.327 79.808 1.00 76.92 ? 254 TYR A CG 1 ATOM 2031 C CD1 . TYR A 1 254 ? -31.012 47.605 79.196 1.00 77.83 ? 254 TYR A CD1 1 ATOM 2032 C CD2 . TYR A 1 254 ? -32.307 46.216 80.631 1.00 75.46 ? 254 TYR A CD2 1 ATOM 2033 C CE1 . TYR A 1 254 ? -29.899 46.813 79.408 1.00 77.86 ? 254 TYR A CE1 1 ATOM 2034 C CE2 . TYR A 1 254 ? -31.202 45.413 80.849 1.00 75.89 ? 254 TYR A CE2 1 ATOM 2035 C CZ . TYR A 1 254 ? -29.997 45.715 80.232 1.00 77.38 ? 254 TYR A CZ 1 ATOM 2036 O OH . TYR A 1 254 ? -28.883 44.927 80.445 1.00 78.60 ? 254 TYR A OH 1 ATOM 2037 N N . LYS A 1 255 ? -34.223 51.440 79.407 1.00 83.73 ? 255 LYS A N 1 ATOM 2038 C CA . LYS A 1 255 ? -35.114 52.403 78.776 1.00 84.82 ? 255 LYS A CA 1 ATOM 2039 C C . LYS A 1 255 ? -35.196 52.054 77.290 1.00 84.54 ? 255 LYS A C 1 ATOM 2040 O O . LYS A 1 255 ? -34.183 51.730 76.671 1.00 84.29 ? 255 LYS A O 1 ATOM 2041 C CB . LYS A 1 255 ? -34.556 53.811 78.980 1.00 87.91 ? 255 LYS A CB 1 ATOM 2042 C CG . LYS A 1 255 ? -35.577 54.901 79.276 1.00 89.45 ? 255 LYS A CG 1 ATOM 2043 C CD . LYS A 1 255 ? -34.935 56.105 79.976 1.00 91.06 ? 255 LYS A CD 1 ATOM 2044 C CE . LYS A 1 255 ? -33.696 56.606 79.247 1.00 92.43 ? 255 LYS A CE 1 ATOM 2045 N NZ . LYS A 1 255 ? -33.458 58.053 79.488 1.00 95.53 ? 255 LYS A NZ 1 ATOM 2046 N N . ILE A 1 256 ? -36.400 52.100 76.726 1.00 83.98 ? 256 ILE A N 1 ATOM 2047 C CA . ILE A 1 256 ? -36.608 51.748 75.324 1.00 83.44 ? 256 ILE A CA 1 ATOM 2048 C C . ILE A 1 256 ? -36.640 53.010 74.477 1.00 85.83 ? 256 ILE A C 1 ATOM 2049 O O . ILE A 1 256 ? -37.684 53.649 74.341 1.00 85.69 ? 256 ILE A O 1 ATOM 2050 C CB . ILE A 1 256 ? -37.922 50.975 75.128 1.00 81.94 ? 256 ILE A CB 1 ATOM 2051 C CG1 . ILE A 1 256 ? -37.928 49.708 75.983 1.00 80.17 ? 256 ILE A CG1 1 ATOM 2052 C CG2 . ILE A 1 256 ? -38.097 50.599 73.662 1.00 81.83 ? 256 ILE A CG2 1 ATOM 2053 C CD1 . ILE A 1 256 ? -39.260 48.984 76.008 1.00 78.83 ? 256 ILE A CD1 1 ATOM 2054 N N . VAL A 1 257 ? -35.501 53.365 73.895 1.00 88.59 ? 257 VAL A N 1 ATOM 2055 C CA . VAL A 1 257 ? -35.391 54.660 73.218 1.00 92.30 ? 257 VAL A CA 1 ATOM 2056 C C . VAL A 1 257 ? -35.820 54.587 71.751 1.00 93.24 ? 257 VAL A C 1 ATOM 2057 O O . VAL A 1 257 ? -36.615 55.424 71.304 1.00 94.61 ? 257 VAL A O 1 ATOM 2058 C CB . VAL A 1 257 ? -33.988 55.313 73.391 1.00 94.45 ? 257 VAL A CB 1 ATOM 2059 C CG1 . VAL A 1 257 ? -33.631 55.384 74.867 1.00 94.45 ? 257 VAL A CG1 1 ATOM 2060 C CG2 . VAL A 1 257 ? -32.893 54.580 72.624 1.00 94.39 ? 257 VAL A CG2 1 ATOM 2061 N N . LYS A 1 258 ? -35.311 53.595 71.015 1.00 92.96 ? 258 LYS A N 1 ATOM 2062 C CA . LYS A 1 258 ? -35.687 53.399 69.604 1.00 94.31 ? 258 LYS A CA 1 ATOM 2063 C C . LYS A 1 258 ? -36.469 52.111 69.430 1.00 91.22 ? 258 LYS A C 1 ATOM 2064 O O . LYS A 1 258 ? -35.998 51.038 69.810 1.00 89.36 ? 258 LYS A O 1 ATOM 2065 C CB . LYS A 1 258 ? -34.459 53.370 68.682 1.00 96.08 ? 258 LYS A CB 1 ATOM 2066 C CG . LYS A 1 258 ? -33.998 54.741 68.214 1.00 100.63 ? 258 LYS A CG 1 ATOM 2067 C CD . LYS A 1 258 ? -34.892 55.313 67.122 1.00 102.94 ? 258 LYS A CD 1 ATOM 2068 C CE . LYS A 1 258 ? -34.586 54.712 65.755 1.00 103.95 ? 258 LYS A CE 1 ATOM 2069 N NZ . LYS A 1 258 ? -33.306 55.207 65.174 1.00 105.78 ? 258 LYS A NZ 1 ATOM 2070 N N . LYS A 1 259 ? -37.668 52.233 68.868 1.00 90.98 ? 259 LYS A N 1 ATOM 2071 C CA . LYS A 1 259 ? -38.438 51.084 68.407 1.00 89.60 ? 259 LYS A CA 1 ATOM 2072 C C . LYS A 1 259 ? -38.395 51.049 66.888 1.00 91.05 ? 259 LYS A C 1 ATOM 2073 O O . LYS A 1 259 ? -38.360 52.092 66.236 1.00 94.38 ? 259 LYS A O 1 ATOM 2074 C CB . LYS A 1 259 ? -39.893 51.181 68.861 1.00 88.94 ? 259 LYS A CB 1 ATOM 2075 C CG . LYS A 1 259 ? -40.089 51.066 70.357 1.00 88.00 ? 259 LYS A CG 1 ATOM 2076 C CD . LYS A 1 259 ? -41.557 51.159 70.733 1.00 87.95 ? 259 LYS A CD 1 ATOM 2077 C CE . LYS A 1 259 ? -41.710 51.274 72.241 1.00 87.87 ? 259 LYS A CE 1 ATOM 2078 N NZ . LYS A 1 259 ? -43.128 51.287 72.693 1.00 87.99 ? 259 LYS A NZ 1 ATOM 2079 N N . GLY A 1 260 ? -38.409 49.848 66.322 1.00 89.95 ? 260 GLY A N 1 ATOM 2080 C CA . GLY A 1 260 ? -38.436 49.695 64.871 1.00 90.06 ? 260 GLY A CA 1 ATOM 2081 C C . GLY A 1 260 ? -38.063 48.303 64.414 1.00 87.54 ? 260 GLY A C 1 ATOM 2082 O O . GLY A 1 260 ? -37.985 47.376 65.217 1.00 84.37 ? 260 GLY A O 1 ATOM 2083 N N . ASP A 1 261 ? -37.824 48.173 63.114 1.00 88.12 ? 261 ASP A N 1 ATOM 2084 C CA . ASP A 1 261 ? -37.519 46.888 62.515 1.00 87.36 ? 261 ASP A CA 1 ATOM 2085 C C . ASP A 1 261 ? -36.215 46.318 63.043 1.00 85.78 ? 261 ASP A C 1 ATOM 2086 O O . ASP A 1 261 ? -35.172 46.974 62.988 1.00 87.73 ? 261 ASP A O 1 ATOM 2087 C CB . ASP A 1 261 ? -37.441 47.008 60.991 1.00 90.45 ? 261 ASP A CB 1 ATOM 2088 C CG . ASP A 1 261 ? -38.809 47.052 60.338 1.00 91.89 ? 261 ASP A CG 1 ATOM 2089 O OD1 . ASP A 1 261 ? -39.741 46.414 60.882 1.00 90.67 ? 261 ASP A OD1 1 ATOM 2090 O OD2 . ASP A 1 261 ? -38.944 47.714 59.278 1.00 94.19 ? 261 ASP A OD2 1 ATOM 2091 N N . SER A 1 262 ? -36.294 45.094 63.555 1.00 81.83 ? 262 SER A N 1 ATOM 2092 C CA . SER A 1 262 ? -35.125 44.344 63.978 1.00 80.78 ? 262 SER A CA 1 ATOM 2093 C C . SER A 1 262 ? -35.486 42.853 63.990 1.00 79.39 ? 262 SER A C 1 ATOM 2094 O O . SER A 1 262 ? -36.607 42.478 63.644 1.00 79.50 ? 262 SER A O 1 ATOM 2095 C CB . SER A 1 262 ? -34.658 44.824 65.356 1.00 79.89 ? 262 SER A CB 1 ATOM 2096 O OG . SER A 1 262 ? -33.678 43.964 65.916 1.00 79.10 ? 262 SER A OG 1 ATOM 2097 N N . THR A 1 263 ? -34.534 42.007 64.373 1.00 74.27 ? 263 THR A N 1 ATOM 2098 C CA . THR A 1 263 ? -34.745 40.567 64.377 1.00 70.79 ? 263 THR A CA 1 ATOM 2099 C C . THR A 1 263 ? -33.684 39.905 65.232 1.00 69.61 ? 263 THR A C 1 ATOM 2100 O O . THR A 1 263 ? -32.563 40.415 65.341 1.00 70.72 ? 263 THR A O 1 ATOM 2101 C CB . THR A 1 263 ? -34.677 39.981 62.948 1.00 68.55 ? 263 THR A CB 1 ATOM 2102 O OG1 . THR A 1 263 ? -35.148 38.635 62.951 1.00 66.69 ? 263 THR A OG1 1 ATOM 2103 C CG2 . THR A 1 263 ? -33.260 39.983 62.411 1.00 68.15 ? 263 THR A CG2 1 ATOM 2104 N N . ILE A 1 264 ? -34.046 38.784 65.853 1.00 67.91 ? 264 ILE A N 1 ATOM 2105 C CA . ILE A 1 264 ? -33.066 37.923 66.502 1.00 66.16 ? 264 ILE A CA 1 ATOM 2106 C C . ILE A 1 264 ? -32.710 36.821 65.520 1.00 64.69 ? 264 ILE A C 1 ATOM 2107 O O . ILE A 1 264 ? -33.441 35.849 65.347 1.00 62.95 ? 264 ILE A O 1 ATOM 2108 C CB . ILE A 1 264 ? -33.559 37.331 67.832 1.00 65.53 ? 264 ILE A CB 1 ATOM 2109 C CG1 . ILE A 1 264 ? -34.040 38.458 68.743 1.00 67.22 ? 264 ILE A CG1 1 ATOM 2110 C CG2 . ILE A 1 264 ? -32.436 36.551 68.501 1.00 64.78 ? 264 ILE A CG2 1 ATOM 2111 C CD1 . ILE A 1 264 ? -34.445 38.008 70.126 1.00 68.19 ? 264 ILE A CD1 1 ATOM 2112 N N . MET A 1 265 ? -31.570 37.015 64.874 1.00 65.79 ? 265 MET A N 1 ATOM 2113 C CA . MET A 1 265 ? -31.000 36.059 63.943 1.00 65.89 ? 265 MET A CA 1 ATOM 2114 C C . MET A 1 265 ? -30.252 34.981 64.725 1.00 66.31 ? 265 MET A C 1 ATOM 2115 O O . MET A 1 265 ? -29.631 35.271 65.740 1.00 67.12 ? 265 MET A O 1 ATOM 2116 C CB . MET A 1 265 ? -30.043 36.809 63.028 1.00 66.52 ? 265 MET A CB 1 ATOM 2117 C CG . MET A 1 265 ? -29.623 36.069 61.784 1.00 66.41 ? 265 MET A CG 1 ATOM 2118 S SD . MET A 1 265 ? -28.835 37.233 60.661 1.00 68.54 ? 265 MET A SD 1 ATOM 2119 C CE . MET A 1 265 ? -30.250 38.219 60.154 1.00 66.99 ? 265 MET A CE 1 ATOM 2120 N N . LYS A 1 266 ? -30.327 33.741 64.259 1.00 67.02 ? 266 LYS A N 1 ATOM 2121 C CA . LYS A 1 266 ? -29.676 32.633 64.931 1.00 70.24 ? 266 LYS A CA 1 ATOM 2122 C C . LYS A 1 266 ? -28.578 32.043 64.062 1.00 70.97 ? 266 LYS A C 1 ATOM 2123 O O . LYS A 1 266 ? -28.849 31.385 63.055 1.00 70.16 ? 266 LYS A O 1 ATOM 2124 C CB . LYS A 1 266 ? -30.697 31.569 65.325 1.00 73.09 ? 266 LYS A CB 1 ATOM 2125 C CG . LYS A 1 266 ? -31.550 31.984 66.523 1.00 76.31 ? 266 LYS A CG 1 ATOM 2126 C CD . LYS A 1 266 ? -31.746 30.847 67.519 1.00 79.75 ? 266 LYS A CD 1 ATOM 2127 C CE . LYS A 1 266 ? -31.483 31.314 68.944 1.00 83.64 ? 266 LYS A CE 1 ATOM 2128 N NZ . LYS A 1 266 ? -31.032 30.211 69.855 1.00 87.41 ? 266 LYS A NZ 1 ATOM 2129 N N . SER A 1 267 ? -27.335 32.285 64.475 1.00 72.91 ? 267 SER A N 1 ATOM 2130 C CA . SER A 1 267 ? -26.157 31.908 63.704 1.00 74.27 ? 267 SER A CA 1 ATOM 2131 C C . SER A 1 267 ? -24.980 31.620 64.623 1.00 76.10 ? 267 SER A C 1 ATOM 2132 O O . SER A 1 267 ? -24.855 32.220 65.687 1.00 76.57 ? 267 SER A O 1 ATOM 2133 C CB . SER A 1 267 ? -25.784 33.053 62.763 1.00 75.04 ? 267 SER A CB 1 ATOM 2134 O OG . SER A 1 267 ? -24.689 32.699 61.935 1.00 78.15 ? 267 SER A OG 1 ATOM 2135 N N . GLU A 1 268 ? -24.113 30.706 64.206 1.00 77.76 ? 268 GLU A N 1 ATOM 2136 C CA . GLU A 1 268 ? -22.865 30.466 64.920 1.00 80.61 ? 268 GLU A CA 1 ATOM 2137 C C . GLU A 1 268 ? -21.811 31.459 64.466 1.00 82.61 ? 268 GLU A C 1 ATOM 2138 O O . GLU A 1 268 ? -20.788 31.608 65.121 1.00 85.76 ? 268 GLU A O 1 ATOM 2139 C CB . GLU A 1 268 ? -22.350 29.050 64.669 1.00 82.67 ? 268 GLU A CB 1 ATOM 2140 C CG . GLU A 1 268 ? -23.332 27.947 65.015 1.00 82.42 ? 268 GLU A CG 1 ATOM 2141 C CD . GLU A 1 268 ? -23.809 28.013 66.453 1.00 83.09 ? 268 GLU A CD 1 ATOM 2142 O OE1 . GLU A 1 268 ? -22.969 27.850 67.371 1.00 84.85 ? 268 GLU A OE1 1 ATOM 2143 O OE2 . GLU A 1 268 ? -25.031 28.221 66.654 1.00 81.28 ? 268 GLU A OE2 1 ATOM 2144 N N . LEU A 1 269 ? -22.061 32.139 63.349 1.00 81.92 ? 269 LEU A N 1 ATOM 2145 C CA . LEU A 1 269 ? -21.051 32.988 62.728 1.00 84.70 ? 269 LEU A CA 1 ATOM 2146 C C . LEU A 1 269 ? -20.706 34.203 63.572 1.00 86.25 ? 269 LEU A C 1 ATOM 2147 O O . LEU A 1 269 ? -21.479 34.639 64.423 1.00 83.67 ? 269 LEU A O 1 ATOM 2148 C CB . LEU A 1 269 ? -21.488 33.445 61.327 1.00 83.41 ? 269 LEU A CB 1 ATOM 2149 C CG . LEU A 1 269 ? -21.673 32.386 60.227 1.00 82.89 ? 269 LEU A CG 1 ATOM 2150 C CD1 . LEU A 1 269 ? -21.936 33.061 58.889 1.00 82.30 ? 269 LEU A CD1 1 ATOM 2151 C CD2 . LEU A 1 269 ? -20.477 31.452 60.104 1.00 85.89 ? 269 LEU A CD2 1 ATOM 2152 N N . GLU A 1 270 ? -19.521 34.737 63.311 1.00 90.87 ? 270 GLU A N 1 ATOM 2153 C CA . GLU A 1 270 ? -19.027 35.931 63.991 1.00 94.53 ? 270 GLU A CA 1 ATOM 2154 C C . GLU A 1 270 ? -19.080 37.121 63.021 1.00 93.82 ? 270 GLU A C 1 ATOM 2155 O O . GLU A 1 270 ? -19.516 36.979 61.877 1.00 93.58 ? 270 GLU A O 1 ATOM 2156 C CB . GLU A 1 270 ? -17.611 35.693 64.576 1.00 99.53 ? 270 GLU A CB 1 ATOM 2157 C CG . GLU A 1 270 ? -16.728 34.713 63.799 1.00 102.61 ? 270 GLU A CG 1 ATOM 2158 C CD . GLU A 1 270 ? -15.311 34.591 64.352 1.00 108.26 ? 270 GLU A CD 1 ATOM 2159 O OE1 . GLU A 1 270 ? -15.094 34.840 65.562 1.00 109.52 ? 270 GLU A OE1 1 ATOM 2160 O OE2 . GLU A 1 270 ? -14.407 34.238 63.562 1.00 111.38 ? 270 GLU A OE2 1 ATOM 2161 N N . TYR A 1 271 ? -18.672 38.292 63.498 1.00 94.64 ? 271 TYR A N 1 ATOM 2162 C CA . TYR A 1 271 ? -18.652 39.513 62.698 1.00 95.25 ? 271 TYR A CA 1 ATOM 2163 C C . TYR A 1 271 ? -17.659 39.416 61.539 1.00 97.91 ? 271 TYR A C 1 ATOM 2164 O O . TYR A 1 271 ? -16.551 38.907 61.705 1.00 99.28 ? 271 TYR A O 1 ATOM 2165 C CB . TYR A 1 271 ? -18.271 40.684 63.599 1.00 98.40 ? 271 TYR A CB 1 ATOM 2166 C CG . TYR A 1 271 ? -18.473 42.057 63.008 1.00 99.38 ? 271 TYR A CG 1 ATOM 2167 C CD1 . TYR A 1 271 ? -19.748 42.603 62.889 1.00 96.30 ? 271 TYR A CD1 1 ATOM 2168 C CD2 . TYR A 1 271 ? -17.387 42.829 62.606 1.00 103.42 ? 271 TYR A CD2 1 ATOM 2169 C CE1 . TYR A 1 271 ? -19.942 43.867 62.368 1.00 98.28 ? 271 TYR A CE1 1 ATOM 2170 C CE2 . TYR A 1 271 ? -17.570 44.102 62.091 1.00 105.42 ? 271 TYR A CE2 1 ATOM 2171 C CZ . TYR A 1 271 ? -18.848 44.619 61.968 1.00 102.84 ? 271 TYR A CZ 1 ATOM 2172 O OH . TYR A 1 271 ? -19.030 45.885 61.457 1.00 104.06 ? 271 TYR A OH 1 ATOM 2173 N N . GLY A 1 272 ? -18.060 39.915 60.370 1.00 97.98 ? 272 GLY A N 1 ATOM 2174 C CA . GLY A 1 272 ? -17.222 39.850 59.168 1.00 100.74 ? 272 GLY A CA 1 ATOM 2175 C C . GLY A 1 272 ? -16.473 41.128 58.807 1.00 105.39 ? 272 GLY A C 1 ATOM 2176 O O . GLY A 1 272 ? -15.678 41.132 57.861 1.00 107.69 ? 272 GLY A O 1 ATOM 2177 N N . ASN A 1 273 ? -16.732 42.215 59.535 1.00 106.43 ? 273 ASN A N 1 ATOM 2178 C CA . ASN A 1 273 ? -16.134 43.514 59.219 1.00 110.37 ? 273 ASN A CA 1 ATOM 2179 C C . ASN A 1 273 ? -16.460 43.928 57.781 1.00 108.54 ? 273 ASN A C 1 ATOM 2180 O O . ASN A 1 273 ? -15.589 44.260 56.981 1.00 112.13 ? 273 ASN A O 1 ATOM 2181 C CB . ASN A 1 273 ? -14.626 43.508 59.500 1.00 115.59 ? 273 ASN A CB 1 ATOM 2182 C CG . ASN A 1 273 ? -14.283 44.128 60.843 1.00 119.44 ? 273 ASN A CG 1 ATOM 2183 O OD1 . ASN A 1 273 ? -13.992 43.425 61.814 1.00 119.95 ? 273 ASN A OD1 1 ATOM 2184 N ND2 . ASN A 1 273 ? -14.326 45.458 60.908 1.00 122.18 ? 273 ASN A ND2 1 ATOM 2185 N N . CYS A 1 274 ? -17.756 43.908 57.497 1.00 103.02 ? 274 CYS A N 1 ATOM 2186 C CA . CYS A 1 274 ? -18.320 44.181 56.176 1.00 101.73 ? 274 CYS A CA 1 ATOM 2187 C C . CYS A 1 274 ? -19.629 44.915 56.376 1.00 98.19 ? 274 CYS A C 1 ATOM 2188 O O . CYS A 1 274 ? -20.117 45.037 57.500 1.00 97.32 ? 274 CYS A O 1 ATOM 2189 C CB . CYS A 1 274 ? -18.666 42.866 55.478 1.00 98.77 ? 274 CYS A CB 1 ATOM 2190 S SG . CYS A 1 274 ? -19.635 41.881 56.632 1.00 96.24 ? 274 CYS A SG 1 ATOM 2191 N N . ASN A 1 275 ? -20.219 45.348 55.265 1.00 96.23 ? 275 ASN A N 1 ATOM 2192 C CA . ASN A 1 275 ? -21.505 46.053 55.248 1.00 93.49 ? 275 ASN A CA 1 ATOM 2193 C C . ASN A 1 275 ? -22.413 45.503 54.138 1.00 89.98 ? 275 ASN A C 1 ATOM 2194 O O . ASN A 1 275 ? -21.927 45.033 53.108 1.00 89.97 ? 275 ASN A O 1 ATOM 2195 C CB . ASN A 1 275 ? -21.257 47.548 55.037 1.00 96.37 ? 275 ASN A CB 1 ATOM 2196 C CG . ASN A 1 275 ? -22.526 48.372 55.113 1.00 94.71 ? 275 ASN A CG 1 ATOM 2197 O OD1 . ASN A 1 275 ? -23.070 48.584 56.180 1.00 94.87 ? 275 ASN A OD1 1 ATOM 2198 N ND2 . ASN A 1 275 ? -22.994 48.845 53.977 1.00 94.85 ? 275 ASN A ND2 1 ATOM 2199 N N . THR A 1 276 ? -23.726 45.564 54.339 1.00 87.52 ? 276 THR A N 1 ATOM 2200 C CA . THR A 1 276 ? -24.672 45.053 53.344 1.00 84.46 ? 276 THR A CA 1 ATOM 2201 C C . THR A 1 276 ? -26.020 45.768 53.418 1.00 84.46 ? 276 THR A C 1 ATOM 2202 O O . THR A 1 276 ? -26.266 46.545 54.339 1.00 86.71 ? 276 THR A O 1 ATOM 2203 C CB . THR A 1 276 ? -24.863 43.527 53.521 1.00 81.01 ? 276 THR A CB 1 ATOM 2204 O OG1 . THR A 1 276 ? -25.380 42.951 52.318 1.00 78.35 ? 276 THR A OG1 1 ATOM 2205 C CG2 . THR A 1 276 ? -25.786 43.197 54.708 1.00 79.62 ? 276 THR A CG2 1 ATOM 2206 N N . LYS A 1 277 ? -26.874 45.507 52.431 1.00 83.44 ? 277 LYS A N 1 ATOM 2207 C CA . LYS A 1 277 ? -28.260 45.994 52.427 1.00 84.91 ? 277 LYS A CA 1 ATOM 2208 C C . LYS A 1 277 ? -29.250 44.867 52.698 1.00 80.15 ? 277 LYS A C 1 ATOM 2209 O O . LYS A 1 277 ? -30.455 45.091 52.771 1.00 80.33 ? 277 LYS A O 1 ATOM 2210 C CB . LYS A 1 277 ? -28.600 46.642 51.081 1.00 88.31 ? 277 LYS A CB 1 ATOM 2211 C CG . LYS A 1 277 ? -28.048 48.049 50.916 1.00 95.79 ? 277 LYS A CG 1 ATOM 2212 C CD . LYS A 1 277 ? -28.684 48.772 49.728 1.00 99.25 ? 277 LYS A CD 1 ATOM 2213 C CE . LYS A 1 277 ? -30.088 49.292 50.031 1.00 100.64 ? 277 LYS A CE 1 ATOM 2214 N NZ . LYS A 1 277 ? -30.104 50.323 51.113 1.00 105.90 ? 277 LYS A NZ 1 ATOM 2215 N N . CYS A 1 278 ? -28.739 43.654 52.831 1.00 76.89 ? 278 CYS A N 1 ATOM 2216 C CA . CYS A 1 278 ? -29.576 42.496 53.012 1.00 74.30 ? 278 CYS A CA 1 ATOM 2217 C C . CYS A 1 278 ? -28.759 41.410 53.673 1.00 72.06 ? 278 CYS A C 1 ATOM 2218 O O . CYS A 1 278 ? -27.729 40.998 53.135 1.00 71.74 ? 278 CYS A O 1 ATOM 2219 C CB . CYS A 1 278 ? -30.061 42.010 51.654 1.00 74.26 ? 278 CYS A CB 1 ATOM 2220 S SG . CYS A 1 278 ? -30.879 40.398 51.686 1.00 73.88 ? 278 CYS A SG 1 ATOM 2221 N N . GLN A 1 279 ? -29.215 40.940 54.830 1.00 70.47 ? 279 GLN A N 1 ATOM 2222 C CA . GLN A 1 279 ? -28.443 39.984 55.612 1.00 69.64 ? 279 GLN A CA 1 ATOM 2223 C C . GLN A 1 279 ? -29.203 38.694 55.846 1.00 66.17 ? 279 GLN A C 1 ATOM 2224 O O . GLN A 1 279 ? -30.410 38.717 56.068 1.00 64.62 ? 279 GLN A O 1 ATOM 2225 C CB . GLN A 1 279 ? -28.059 40.594 56.956 1.00 71.63 ? 279 GLN A CB 1 ATOM 2226 C CG . GLN A 1 279 ? -27.150 39.699 57.781 1.00 72.35 ? 279 GLN A CG 1 ATOM 2227 C CD . GLN A 1 279 ? -25.737 39.673 57.248 1.00 74.62 ? 279 GLN A CD 1 ATOM 2228 O OE1 . GLN A 1 279 ? -25.088 40.713 57.159 1.00 78.20 ? 279 GLN A OE1 1 ATOM 2229 N NE2 . GLN A 1 279 ? -25.249 38.490 56.894 1.00 74.03 ? 279 GLN A NE2 1 ATOM 2230 N N . THR A 1 280 ? -28.478 37.580 55.791 1.00 65.62 ? 280 THR A N 1 ATOM 2231 C CA . THR A 1 280 ? -28.998 36.282 56.196 1.00 65.47 ? 280 THR A CA 1 ATOM 2232 C C . THR A 1 280 ? -28.083 35.657 57.247 1.00 68.19 ? 280 THR A C 1 ATOM 2233 O O . THR A 1 280 ? -26.899 36.009 57.332 1.00 68.82 ? 280 THR A O 1 ATOM 2234 C CB . THR A 1 280 ? -29.099 35.286 55.017 1.00 64.02 ? 280 THR A CB 1 ATOM 2235 O OG1 . THR A 1 280 ? -27.855 34.586 54.843 1.00 65.78 ? 280 THR A OG1 1 ATOM 2236 C CG2 . THR A 1 280 ? -29.470 35.992 53.740 1.00 63.25 ? 280 THR A CG2 1 ATOM 2237 N N . PRO A 1 281 ? -28.617 34.694 58.023 1.00 69.17 ? 281 PRO A N 1 ATOM 2238 C CA . PRO A 1 281 ? -27.839 33.933 59.016 1.00 71.27 ? 281 PRO A CA 1 ATOM 2239 C C . PRO A 1 281 ? -26.628 33.159 58.466 1.00 73.52 ? 281 PRO A C 1 ATOM 2240 O O . PRO A 1 281 ? -25.815 32.673 59.265 1.00 74.58 ? 281 PRO A O 1 ATOM 2241 C CB . PRO A 1 281 ? -28.851 32.937 59.593 1.00 70.77 ? 281 PRO A CB 1 ATOM 2242 C CG . PRO A 1 281 ? -30.198 33.427 59.202 1.00 69.75 ? 281 PRO A CG 1 ATOM 2243 C CD . PRO A 1 281 ? -30.060 34.397 58.078 1.00 68.25 ? 281 PRO A CD 1 ATOM 2244 N N . MET A 1 282 ? -26.519 33.029 57.138 1.00 73.93 ? 282 MET A N 1 ATOM 2245 C CA . MET A 1 282 ? -25.365 32.370 56.499 1.00 75.88 ? 282 MET A CA 1 ATOM 2246 C C . MET A 1 282 ? -24.371 33.334 55.860 1.00 75.01 ? 282 MET A C 1 ATOM 2247 O O . MET A 1 282 ? -23.266 32.939 55.508 1.00 74.25 ? 282 MET A O 1 ATOM 2248 C CB . MET A 1 282 ? -25.840 31.416 55.415 1.00 77.95 ? 282 MET A CB 1 ATOM 2249 C CG . MET A 1 282 ? -26.991 30.527 55.842 1.00 80.24 ? 282 MET A CG 1 ATOM 2250 S SD . MET A 1 282 ? -26.970 28.921 55.029 1.00 86.29 ? 282 MET A SD 1 ATOM 2251 C CE . MET A 1 282 ? -26.480 29.371 53.360 1.00 84.23 ? 282 MET A CE 1 ATOM 2252 N N . GLY A 1 283 ? -24.774 34.589 55.691 1.00 74.07 ? 283 GLY A N 1 ATOM 2253 C CA . GLY A 1 283 ? -23.956 35.571 54.986 1.00 75.09 ? 283 GLY A CA 1 ATOM 2254 C C . GLY A 1 283 ? -24.836 36.640 54.375 1.00 74.03 ? 283 GLY A C 1 ATOM 2255 O O . GLY A 1 283 ? -26.066 36.491 54.345 1.00 70.13 ? 283 GLY A O 1 ATOM 2256 N N . ALA A 1 284 ? -24.210 37.717 53.892 1.00 75.53 ? 284 ALA A N 1 ATOM 2257 C CA . ALA A 1 284 ? -24.951 38.832 53.291 1.00 74.47 ? 284 ALA A CA 1 ATOM 2258 C C . ALA A 1 284 ? -25.152 38.657 51.784 1.00 72.89 ? 284 ALA A C 1 ATOM 2259 O O . ALA A 1 284 ? -24.477 37.852 51.127 1.00 72.00 ? 284 ALA A O 1 ATOM 2260 C CB . ALA A 1 284 ? -24.256 40.151 53.576 1.00 77.47 ? 284 ALA A CB 1 ATOM 2261 N N . ILE A 1 285 ? -26.080 39.447 51.252 1.00 72.12 ? 285 ILE A N 1 ATOM 2262 C CA . ILE A 1 285 ? -26.517 39.346 49.861 1.00 70.87 ? 285 ILE A CA 1 ATOM 2263 C C . ILE A 1 285 ? -26.385 40.694 49.159 1.00 73.03 ? 285 ILE A C 1 ATOM 2264 O O . ILE A 1 285 ? -26.799 41.734 49.679 1.00 72.90 ? 285 ILE A O 1 ATOM 2265 C CB . ILE A 1 285 ? -27.987 38.863 49.779 1.00 68.25 ? 285 ILE A CB 1 ATOM 2266 C CG1 . ILE A 1 285 ? -28.033 37.337 49.816 1.00 67.00 ? 285 ILE A CG1 1 ATOM 2267 C CG2 . ILE A 1 285 ? -28.686 39.375 48.521 1.00 67.52 ? 285 ILE A CG2 1 ATOM 2268 C CD1 . ILE A 1 285 ? -29.407 36.765 50.088 1.00 65.07 ? 285 ILE A CD1 1 ATOM 2269 N N . ASN A 1 286 ? -25.816 40.655 47.963 1.00 74.55 ? 286 ASN A N 1 ATOM 2270 C CA . ASN A 1 286 ? -25.741 41.826 47.120 1.00 77.80 ? 286 ASN A CA 1 ATOM 2271 C C . ASN A 1 286 ? -26.081 41.422 45.699 1.00 76.56 ? 286 ASN A C 1 ATOM 2272 O O . ASN A 1 286 ? -25.244 40.848 44.994 1.00 76.72 ? 286 ASN A O 1 ATOM 2273 C CB . ASN A 1 286 ? -24.336 42.434 47.182 1.00 81.92 ? 286 ASN A CB 1 ATOM 2274 C CG . ASN A 1 286 ? -24.258 43.783 46.505 1.00 85.20 ? 286 ASN A CG 1 ATOM 2275 O OD1 . ASN A 1 286 ? -25.239 44.530 46.465 1.00 84.74 ? 286 ASN A OD1 1 ATOM 2276 N ND2 . ASN A 1 286 ? -23.086 44.108 45.970 1.00 89.33 ? 286 ASN A ND2 1 ATOM 2277 N N . SER A 1 287 ? -27.317 41.688 45.286 1.00 74.72 ? 287 SER A N 1 ATOM 2278 C CA . SER A 1 287 ? -27.707 41.450 43.899 1.00 73.00 ? 287 SER A CA 1 ATOM 2279 C C . SER A 1 287 ? -28.935 42.226 43.482 1.00 72.73 ? 287 SER A C 1 ATOM 2280 O O . SER A 1 287 ? -29.678 42.748 44.309 1.00 71.70 ? 287 SER A O 1 ATOM 2281 C CB . SER A 1 287 ? -27.938 39.963 43.651 1.00 70.40 ? 287 SER A CB 1 ATOM 2282 O OG . SER A 1 287 ? -28.900 39.449 44.538 1.00 68.11 ? 287 SER A OG 1 ATOM 2283 N N . SER A 1 288 ? -29.126 42.289 42.172 1.00 74.48 ? 288 SER A N 1 ATOM 2284 C CA . SER A 1 288 ? -30.311 42.893 41.585 1.00 76.17 ? 288 SER A CA 1 ATOM 2285 C C . SER A 1 288 ? -31.386 41.840 41.273 1.00 72.63 ? 288 SER A C 1 ATOM 2286 O O . SER A 1 288 ? -32.480 42.185 40.824 1.00 72.87 ? 288 SER A O 1 ATOM 2287 C CB . SER A 1 288 ? -29.921 43.664 40.319 1.00 80.18 ? 288 SER A CB 1 ATOM 2288 O OG . SER A 1 288 ? -28.870 43.009 39.617 1.00 81.14 ? 288 SER A OG 1 ATOM 2289 N N . MET A 1 289 ? -31.094 40.568 41.543 1.00 69.23 ? 289 MET A N 1 ATOM 2290 C CA . MET A 1 289 ? -32.021 39.486 41.209 1.00 67.11 ? 289 MET A CA 1 ATOM 2291 C C . MET A 1 289 ? -33.312 39.608 42.012 1.00 66.03 ? 289 MET A C 1 ATOM 2292 O O . MET A 1 289 ? -33.290 40.049 43.152 1.00 68.92 ? 289 MET A O 1 ATOM 2293 C CB . MET A 1 289 ? -31.410 38.126 41.513 1.00 67.49 ? 289 MET A CB 1 ATOM 2294 C CG . MET A 1 289 ? -30.052 37.860 40.894 1.00 69.40 ? 289 MET A CG 1 ATOM 2295 S SD . MET A 1 289 ? -30.159 37.494 39.146 1.00 69.49 ? 289 MET A SD 1 ATOM 2296 C CE . MET A 1 289 ? -28.979 36.134 39.097 1.00 69.09 ? 289 MET A CE 1 ATOM 2297 N N . PRO A 1 290 ? -34.447 39.216 41.422 1.00 63.32 ? 290 PRO A N 1 ATOM 2298 C CA . PRO A 1 290 ? -35.705 39.244 42.170 1.00 62.41 ? 290 PRO A CA 1 ATOM 2299 C C . PRO A 1 290 ? -35.846 38.113 43.175 1.00 61.17 ? 290 PRO A C 1 ATOM 2300 O O . PRO A 1 290 ? -36.695 38.195 44.057 1.00 63.11 ? 290 PRO A O 1 ATOM 2301 C CB . PRO A 1 290 ? -36.755 39.094 41.078 1.00 61.58 ? 290 PRO A CB 1 ATOM 2302 C CG . PRO A 1 290 ? -36.051 38.345 40.008 1.00 60.49 ? 290 PRO A CG 1 ATOM 2303 C CD . PRO A 1 290 ? -34.656 38.864 40.010 1.00 60.91 ? 290 PRO A CD 1 ATOM 2304 N N . PHE A 1 291 ? -35.045 37.062 43.026 1.00 59.90 ? 291 PHE A N 1 ATOM 2305 C CA . PHE A 1 291 ? -35.110 35.900 43.906 1.00 60.08 ? 291 PHE A CA 1 ATOM 2306 C C . PHE A 1 291 ? -33.739 35.493 44.381 1.00 58.26 ? 291 PHE A C 1 ATOM 2307 O O . PHE A 1 291 ? -32.747 35.765 43.713 1.00 57.90 ? 291 PHE A O 1 ATOM 2308 C CB . PHE A 1 291 ? -35.622 34.684 43.155 1.00 61.30 ? 291 PHE A CB 1 ATOM 2309 C CG . PHE A 1 291 ? -37.037 34.772 42.732 1.00 62.32 ? 291 PHE A CG 1 ATOM 2310 C CD1 . PHE A 1 291 ? -38.040 34.349 43.577 1.00 64.03 ? 291 PHE A CD1 1 ATOM 2311 C CD2 . PHE A 1 291 ? -37.366 35.227 41.468 1.00 63.75 ? 291 PHE A CD2 1 ATOM 2312 C CE1 . PHE A 1 291 ? -39.361 34.402 43.183 1.00 64.48 ? 291 PHE A CE1 1 ATOM 2313 C CE2 . PHE A 1 291 ? -38.688 35.287 41.065 1.00 64.85 ? 291 PHE A CE2 1 ATOM 2314 C CZ . PHE A 1 291 ? -39.682 34.869 41.925 1.00 64.53 ? 291 PHE A CZ 1 ATOM 2315 N N . HIS A 1 292 ? -33.709 34.778 45.503 1.00 56.97 ? 292 HIS A N 1 ATOM 2316 C CA . HIS A 1 292 ? -32.504 34.083 45.973 1.00 55.86 ? 292 HIS A CA 1 ATOM 2317 C C . HIS A 1 292 ? -32.910 32.794 46.679 1.00 55.49 ? 292 HIS A C 1 ATOM 2318 O O . HIS A 1 292 ? -34.092 32.587 46.960 1.00 56.43 ? 292 HIS A O 1 ATOM 2319 C CB . HIS A 1 292 ? -31.738 34.965 46.946 1.00 56.06 ? 292 HIS A CB 1 ATOM 2320 C CG . HIS A 1 292 ? -32.404 35.105 48.275 1.00 56.32 ? 292 HIS A CG 1 ATOM 2321 N ND1 . HIS A 1 292 ? -32.041 34.357 49.367 1.00 55.89 ? 292 HIS A ND1 1 ATOM 2322 C CD2 . HIS A 1 292 ? -33.428 35.891 48.682 1.00 57.38 ? 292 HIS A CD2 1 ATOM 2323 C CE1 . HIS A 1 292 ? -32.805 34.680 50.394 1.00 57.16 ? 292 HIS A CE1 1 ATOM 2324 N NE2 . HIS A 1 292 ? -33.656 35.609 50.006 1.00 56.95 ? 292 HIS A NE2 1 ATOM 2325 N N . ASN A 1 293 ? -31.934 31.948 46.994 1.00 55.19 ? 293 ASN A N 1 ATOM 2326 C CA . ASN A 1 293 ? -32.202 30.688 47.688 1.00 55.11 ? 293 ASN A CA 1 ATOM 2327 C C . ASN A 1 293 ? -31.232 30.417 48.826 1.00 56.66 ? 293 ASN A C 1 ATOM 2328 O O . ASN A 1 293 ? -30.894 29.266 49.108 1.00 58.79 ? 293 ASN A O 1 ATOM 2329 C CB . ASN A 1 293 ? -32.134 29.544 46.688 1.00 55.69 ? 293 ASN A CB 1 ATOM 2330 C CG . ASN A 1 293 ? -30.741 29.325 46.150 1.00 55.55 ? 293 ASN A CG 1 ATOM 2331 O OD1 . ASN A 1 293 ? -29.867 30.153 46.327 1.00 57.58 ? 293 ASN A OD1 1 ATOM 2332 N ND2 . ASN A 1 293 ? -30.532 28.207 45.498 1.00 56.62 ? 293 ASN A ND2 1 ATOM 2333 N N . ILE A 1 294 ? -30.790 31.475 49.486 1.00 57.23 ? 294 ILE A N 1 ATOM 2334 C CA . ILE A 1 294 ? -29.741 31.373 50.498 1.00 59.80 ? 294 ILE A CA 1 ATOM 2335 C C . ILE A 1 294 ? -30.293 30.855 51.816 1.00 60.50 ? 294 ILE A C 1 ATOM 2336 O O . ILE A 1 294 ? -29.780 29.879 52.357 1.00 61.42 ? 294 ILE A O 1 ATOM 2337 C CB . ILE A 1 294 ? -29.040 32.732 50.729 1.00 60.20 ? 294 ILE A CB 1 ATOM 2338 C CG1 . ILE A 1 294 ? -28.453 33.274 49.418 1.00 60.63 ? 294 ILE A CG1 1 ATOM 2339 C CG2 . ILE A 1 294 ? -27.938 32.599 51.760 1.00 62.58 ? 294 ILE A CG2 1 ATOM 2340 C CD1 . ILE A 1 294 ? -27.608 32.278 48.648 1.00 62.10 ? 294 ILE A CD1 1 ATOM 2341 N N . HIS A 1 295 ? -31.342 31.510 52.312 1.00 60.48 ? 295 HIS A N 1 ATOM 2342 C CA . HIS A 1 295 ? -31.933 31.201 53.611 1.00 61.79 ? 295 HIS A CA 1 ATOM 2343 C C . HIS A 1 295 ? -33.208 32.039 53.784 1.00 61.36 ? 295 HIS A C 1 ATOM 2344 O O . HIS A 1 295 ? -33.209 33.217 53.446 1.00 61.18 ? 295 HIS A O 1 ATOM 2345 C CB . HIS A 1 295 ? -30.926 31.539 54.711 1.00 64.34 ? 295 HIS A CB 1 ATOM 2346 C CG . HIS A 1 295 ? -31.314 31.056 56.072 1.00 66.16 ? 295 HIS A CG 1 ATOM 2347 N ND1 . HIS A 1 295 ? -32.376 31.585 56.770 1.00 67.00 ? 295 HIS A ND1 1 ATOM 2348 C CD2 . HIS A 1 295 ? -30.759 30.124 56.882 1.00 67.24 ? 295 HIS A CD2 1 ATOM 2349 C CE1 . HIS A 1 295 ? -32.471 30.988 57.945 1.00 68.76 ? 295 HIS A CE1 1 ATOM 2350 N NE2 . HIS A 1 295 ? -31.500 30.097 58.038 1.00 68.63 ? 295 HIS A NE2 1 ATOM 2351 N N . PRO A 1 296 ? -34.294 31.442 54.315 1.00 61.29 ? 296 PRO A N 1 ATOM 2352 C CA . PRO A 1 296 ? -35.570 32.163 54.367 1.00 60.66 ? 296 PRO A CA 1 ATOM 2353 C C . PRO A 1 296 ? -35.585 33.381 55.283 1.00 60.95 ? 296 PRO A C 1 ATOM 2354 O O . PRO A 1 296 ? -36.131 34.414 54.923 1.00 60.95 ? 296 PRO A O 1 ATOM 2355 C CB . PRO A 1 296 ? -36.556 31.102 54.891 1.00 61.45 ? 296 PRO A CB 1 ATOM 2356 C CG . PRO A 1 296 ? -35.715 30.100 55.591 1.00 62.16 ? 296 PRO A CG 1 ATOM 2357 C CD . PRO A 1 296 ? -34.432 30.059 54.813 1.00 62.13 ? 296 PRO A CD 1 ATOM 2358 N N . LEU A 1 297 ? -35.023 33.245 56.475 1.00 61.92 ? 297 LEU A N 1 ATOM 2359 C CA . LEU A 1 297 ? -34.998 34.340 57.436 1.00 62.83 ? 297 LEU A CA 1 ATOM 2360 C C . LEU A 1 297 ? -33.961 35.390 57.049 1.00 62.79 ? 297 LEU A C 1 ATOM 2361 O O . LEU A 1 297 ? -32.762 35.194 57.231 1.00 64.77 ? 297 LEU A O 1 ATOM 2362 C CB . LEU A 1 297 ? -34.716 33.808 58.843 1.00 63.45 ? 297 LEU A CB 1 ATOM 2363 C CG . LEU A 1 297 ? -35.651 32.705 59.336 1.00 64.59 ? 297 LEU A CG 1 ATOM 2364 C CD1 . LEU A 1 297 ? -35.140 32.153 60.662 1.00 66.20 ? 297 LEU A CD1 1 ATOM 2365 C CD2 . LEU A 1 297 ? -37.083 33.212 59.465 1.00 65.86 ? 297 LEU A CD2 1 ATOM 2366 N N . THR A 1 298 ? -34.422 36.505 56.503 1.00 62.75 ? 298 THR A N 1 ATOM 2367 C CA . THR A 1 298 ? -33.521 37.608 56.187 1.00 62.47 ? 298 THR A CA 1 ATOM 2368 C C . THR A 1 298 ? -34.035 38.903 56.789 1.00 64.27 ? 298 THR A C 1 ATOM 2369 O O . THR A 1 298 ? -35.181 38.989 57.239 1.00 63.19 ? 298 THR A O 1 ATOM 2370 C CB . THR A 1 298 ? -33.356 37.793 54.670 1.00 60.56 ? 298 THR A CB 1 ATOM 2371 O OG1 . THR A 1 298 ? -34.486 38.493 54.142 1.00 59.81 ? 298 THR A OG1 1 ATOM 2372 C CG2 . THR A 1 298 ? -33.232 36.455 53.987 1.00 59.40 ? 298 THR A CG2 1 ATOM 2373 N N . ILE A 1 299 ? -33.166 39.904 56.784 1.00 65.77 ? 299 ILE A N 1 ATOM 2374 C CA . ILE A 1 299 ? -33.501 41.229 57.265 1.00 69.30 ? 299 ILE A CA 1 ATOM 2375 C C . ILE A 1 299 ? -32.939 42.176 56.226 1.00 72.11 ? 299 ILE A C 1 ATOM 2376 O O . ILE A 1 299 ? -31.855 41.922 55.683 1.00 71.19 ? 299 ILE A O 1 ATOM 2377 C CB . ILE A 1 299 ? -32.895 41.491 58.672 1.00 71.49 ? 299 ILE A CB 1 ATOM 2378 C CG1 . ILE A 1 299 ? -33.074 42.952 59.132 1.00 74.13 ? 299 ILE A CG1 1 ATOM 2379 C CG2 . ILE A 1 299 ? -31.415 41.128 58.710 1.00 71.31 ? 299 ILE A CG2 1 ATOM 2380 C CD1 . ILE A 1 299 ? -34.483 43.323 59.544 1.00 75.77 ? 299 ILE A CD1 1 ATOM 2381 N N . GLY A 1 300 ? -33.689 43.243 55.941 1.00 76.03 ? 300 GLY A N 1 ATOM 2382 C CA . GLY A 1 300 ? -33.272 44.284 55.003 1.00 79.92 ? 300 GLY A CA 1 ATOM 2383 C C . GLY A 1 300 ? -34.043 44.246 53.692 1.00 82.30 ? 300 GLY A C 1 ATOM 2384 O O . GLY A 1 300 ? -35.055 43.544 53.567 1.00 80.07 ? 300 GLY A O 1 ATOM 2385 N N . GLU A 1 301 ? -33.559 45.012 52.715 1.00 86.14 ? 301 GLU A N 1 ATOM 2386 C CA . GLU A 1 301 ? -34.146 45.044 51.375 1.00 87.33 ? 301 GLU A CA 1 ATOM 2387 C C . GLU A 1 301 ? -33.585 43.885 50.570 1.00 81.45 ? 301 GLU A C 1 ATOM 2388 O O . GLU A 1 301 ? -32.485 43.979 50.023 1.00 80.59 ? 301 GLU A O 1 ATOM 2389 C CB . GLU A 1 301 ? -33.843 46.374 50.674 1.00 94.12 ? 301 GLU A CB 1 ATOM 2390 C CG . GLU A 1 301 ? -34.952 46.840 49.741 1.00 98.79 ? 301 GLU A CG 1 ATOM 2391 C CD . GLU A 1 301 ? -36.204 47.257 50.500 1.00 103.33 ? 301 GLU A CD 1 ATOM 2392 O OE1 . GLU A 1 301 ? -36.203 48.346 51.124 1.00 107.18 ? 301 GLU A OE1 1 ATOM 2393 O OE2 . GLU A 1 301 ? -37.183 46.480 50.490 1.00 104.81 ? 301 GLU A OE2 1 ATOM 2394 N N . CYS A 1 302 ? -34.351 42.798 50.506 1.00 77.21 ? 302 CYS A N 1 ATOM 2395 C CA . CYS A 1 302 ? -33.885 41.543 49.925 1.00 72.86 ? 302 CYS A CA 1 ATOM 2396 C C . CYS A 1 302 ? -34.761 41.016 48.795 1.00 69.85 ? 302 CYS A C 1 ATOM 2397 O O . CYS A 1 302 ? -35.957 41.307 48.733 1.00 68.81 ? 302 CYS A O 1 ATOM 2398 C CB . CYS A 1 302 ? -33.840 40.462 51.002 1.00 71.79 ? 302 CYS A CB 1 ATOM 2399 S SG . CYS A 1 302 ? -32.752 40.833 52.387 1.00 74.64 ? 302 CYS A SG 1 ATOM 2400 N N . PRO A 1 303 ? -34.166 40.205 47.907 1.00 66.97 ? 303 PRO A N 1 ATOM 2401 C CA . PRO A 1 303 ? -34.981 39.406 47.007 1.00 65.03 ? 303 PRO A CA 1 ATOM 2402 C C . PRO A 1 303 ? -35.827 38.384 47.770 1.00 64.64 ? 303 PRO A C 1 ATOM 2403 O O . PRO A 1 303 ? -35.575 38.122 48.953 1.00 64.13 ? 303 PRO A O 1 ATOM 2404 C CB . PRO A 1 303 ? -33.953 38.693 46.120 1.00 64.19 ? 303 PRO A CB 1 ATOM 2405 C CG . PRO A 1 303 ? -32.627 38.869 46.786 1.00 64.88 ? 303 PRO A CG 1 ATOM 2406 C CD . PRO A 1 303 ? -32.728 40.111 47.602 1.00 67.15 ? 303 PRO A CD 1 ATOM 2407 N N . LYS A 1 304 ? -36.817 37.810 47.091 1.00 63.84 ? 304 LYS A N 1 ATOM 2408 C CA . LYS A 1 304 ? -37.712 36.844 47.709 1.00 63.57 ? 304 LYS A CA 1 ATOM 2409 C C . LYS A 1 304 ? -37.091 35.452 47.735 1.00 60.07 ? 304 LYS A C 1 ATOM 2410 O O . LYS A 1 304 ? -36.511 34.982 46.753 1.00 58.56 ? 304 LYS A O 1 ATOM 2411 C CB . LYS A 1 304 ? -39.043 36.823 46.976 1.00 67.33 ? 304 LYS A CB 1 ATOM 2412 C CG . LYS A 1 304 ? -39.716 38.192 46.917 1.00 72.75 ? 304 LYS A CG 1 ATOM 2413 C CD . LYS A 1 304 ? -40.326 38.586 48.257 1.00 76.57 ? 304 LYS A CD 1 ATOM 2414 C CE . LYS A 1 304 ? -40.256 40.084 48.513 1.00 80.42 ? 304 LYS A CE 1 ATOM 2415 N NZ . LYS A 1 304 ? -41.367 40.529 49.412 1.00 85.17 ? 304 LYS A NZ 1 ATOM 2416 N N . TYR A 1 305 ? -37.197 34.799 48.881 1.00 58.26 ? 305 TYR A N 1 ATOM 2417 C CA . TYR A 1 305 ? -36.599 33.493 49.043 1.00 56.86 ? 305 TYR A CA 1 ATOM 2418 C C . TYR A 1 305 ? -37.427 32.432 48.333 1.00 56.81 ? 305 TYR A C 1 ATOM 2419 O O . TYR A 1 305 ? -38.665 32.408 48.448 1.00 57.94 ? 305 TYR A O 1 ATOM 2420 C CB . TYR A 1 305 ? -36.478 33.138 50.514 1.00 56.83 ? 305 TYR A CB 1 ATOM 2421 C CG . TYR A 1 305 ? -35.978 31.742 50.729 1.00 56.33 ? 305 TYR A CG 1 ATOM 2422 C CD1 . TYR A 1 305 ? -34.635 31.432 50.563 1.00 55.71 ? 305 TYR A CD1 1 ATOM 2423 C CD2 . TYR A 1 305 ? -36.842 30.730 51.092 1.00 56.61 ? 305 TYR A CD2 1 ATOM 2424 C CE1 . TYR A 1 305 ? -34.171 30.144 50.759 1.00 56.34 ? 305 TYR A CE1 1 ATOM 2425 C CE2 . TYR A 1 305 ? -36.387 29.441 51.293 1.00 57.74 ? 305 TYR A CE2 1 ATOM 2426 C CZ . TYR A 1 305 ? -35.051 29.152 51.125 1.00 56.92 ? 305 TYR A CZ 1 ATOM 2427 O OH . TYR A 1 305 ? -34.595 27.869 51.323 1.00 56.97 ? 305 TYR A OH 1 ATOM 2428 N N . VAL A 1 306 ? -36.740 31.576 47.578 1.00 54.91 ? 306 VAL A N 1 ATOM 2429 C CA . VAL A 1 306 ? -37.348 30.368 47.040 1.00 55.52 ? 306 VAL A CA 1 ATOM 2430 C C . VAL A 1 306 ? -36.418 29.187 47.242 1.00 56.09 ? 306 VAL A C 1 ATOM 2431 O O . VAL A 1 306 ? -35.205 29.351 47.281 1.00 56.76 ? 306 VAL A O 1 ATOM 2432 C CB . VAL A 1 306 ? -37.717 30.500 45.544 1.00 55.62 ? 306 VAL A CB 1 ATOM 2433 C CG1 . VAL A 1 306 ? -38.907 31.443 45.364 1.00 55.81 ? 306 VAL A CG1 1 ATOM 2434 C CG2 . VAL A 1 306 ? -36.519 30.947 44.712 1.00 53.93 ? 306 VAL A CG2 1 ATOM 2435 N N . LYS A 1 307 ? -36.999 28.000 47.361 1.00 58.15 ? 307 LYS A N 1 ATOM 2436 C CA . LYS A 1 307 ? -36.235 26.754 47.478 1.00 60.92 ? 307 LYS A CA 1 ATOM 2437 C C . LYS A 1 307 ? -35.649 26.253 46.143 1.00 61.62 ? 307 LYS A C 1 ATOM 2438 O O . LYS A 1 307 ? -35.061 25.177 46.079 1.00 64.93 ? 307 LYS A O 1 ATOM 2439 C CB . LYS A 1 307 ? -37.115 25.656 48.092 1.00 63.26 ? 307 LYS A CB 1 ATOM 2440 C CG . LYS A 1 307 ? -37.177 25.669 49.607 1.00 64.33 ? 307 LYS A CG 1 ATOM 2441 C CD . LYS A 1 307 ? -38.150 24.609 50.094 1.00 68.40 ? 307 LYS A CD 1 ATOM 2442 C CE . LYS A 1 307 ? -37.807 24.102 51.486 1.00 71.45 ? 307 LYS A CE 1 ATOM 2443 N NZ . LYS A 1 307 ? -38.572 22.865 51.833 1.00 75.20 ? 307 LYS A NZ 1 ATOM 2444 N N . SER A 1 308 ? -35.803 27.022 45.075 1.00 61.39 ? 308 SER A N 1 ATOM 2445 C CA . SER A 1 308 ? -35.307 26.607 43.770 1.00 61.35 ? 308 SER A CA 1 ATOM 2446 C C . SER A 1 308 ? -33.787 26.520 43.723 1.00 62.16 ? 308 SER A C 1 ATOM 2447 O O . SER A 1 308 ? -33.086 27.325 44.333 1.00 60.66 ? 308 SER A O 1 ATOM 2448 C CB . SER A 1 308 ? -35.785 27.585 42.707 1.00 58.95 ? 308 SER A CB 1 ATOM 2449 O OG . SER A 1 308 ? -37.183 27.515 42.587 1.00 60.33 ? 308 SER A OG 1 ATOM 2450 N N . ASN A 1 309 ? -33.279 25.541 42.986 1.00 64.22 ? 309 ASN A N 1 ATOM 2451 C CA . ASN A 1 309 ? -31.857 25.514 42.646 1.00 66.31 ? 309 ASN A CA 1 ATOM 2452 C C . ASN A 1 309 ? -31.552 26.333 41.406 1.00 64.42 ? 309 ASN A C 1 ATOM 2453 O O . ASN A 1 309 ? -30.476 26.919 41.297 1.00 63.30 ? 309 ASN A O 1 ATOM 2454 C CB . ASN A 1 309 ? -31.367 24.077 42.479 1.00 69.97 ? 309 ASN A CB 1 ATOM 2455 C CG . ASN A 1 309 ? -31.141 23.396 43.816 1.00 72.80 ? 309 ASN A CG 1 ATOM 2456 O OD1 . ASN A 1 309 ? -30.534 23.976 44.719 1.00 71.11 ? 309 ASN A OD1 1 ATOM 2457 N ND2 . ASN A 1 309 ? -31.643 22.169 43.958 1.00 76.57 ? 309 ASN A ND2 1 ATOM 2458 N N . ARG A 1 310 ? -32.516 26.394 40.490 1.00 63.31 ? 310 ARG A N 1 ATOM 2459 C CA . ARG A 1 310 ? -32.347 27.085 39.217 1.00 62.55 ? 310 ARG A CA 1 ATOM 2460 C C . ARG A 1 310 ? -33.629 27.831 38.786 1.00 59.19 ? 310 ARG A C 1 ATOM 2461 O O . ARG A 1 310 ? -34.716 27.246 38.737 1.00 59.06 ? 310 ARG A O 1 ATOM 2462 C CB . ARG A 1 310 ? -31.962 26.045 38.166 1.00 66.53 ? 310 ARG A CB 1 ATOM 2463 C CG . ARG A 1 310 ? -31.414 26.616 36.874 1.00 69.04 ? 310 ARG A CG 1 ATOM 2464 C CD . ARG A 1 310 ? -31.188 25.533 35.826 1.00 71.91 ? 310 ARG A CD 1 ATOM 2465 N NE . ARG A 1 310 ? -31.207 26.082 34.464 1.00 72.87 ? 310 ARG A NE 1 ATOM 2466 C CZ . ARG A 1 310 ? -30.174 26.675 33.861 1.00 73.24 ? 310 ARG A CZ 1 ATOM 2467 N NH1 . ARG A 1 310 ? -29.004 26.817 34.479 1.00 75.75 ? 310 ARG A NH1 1 ATOM 2468 N NH2 . ARG A 1 310 ? -30.306 27.128 32.622 1.00 72.92 ? 310 ARG A NH2 1 ATOM 2469 N N . LEU A 1 311 ? -33.508 29.124 38.491 1.00 56.12 ? 311 LEU A N 1 ATOM 2470 C CA . LEU A 1 311 ? -34.595 29.872 37.826 1.00 54.79 ? 311 LEU A CA 1 ATOM 2471 C C . LEU A 1 311 ? -34.017 30.676 36.667 1.00 53.55 ? 311 LEU A C 1 ATOM 2472 O O . LEU A 1 311 ? -33.306 31.656 36.881 1.00 55.65 ? 311 LEU A O 1 ATOM 2473 C CB . LEU A 1 311 ? -35.323 30.816 38.791 1.00 54.40 ? 311 LEU A CB 1 ATOM 2474 C CG . LEU A 1 311 ? -36.244 30.234 39.872 1.00 54.94 ? 311 LEU A CG 1 ATOM 2475 C CD1 . LEU A 1 311 ? -36.853 31.337 40.715 1.00 54.60 ? 311 LEU A CD1 1 ATOM 2476 C CD2 . LEU A 1 311 ? -37.363 29.397 39.282 1.00 56.34 ? 311 LEU A CD2 1 ATOM 2477 N N . VAL A 1 312 ? -34.298 30.252 35.443 1.00 51.88 ? 312 VAL A N 1 ATOM 2478 C CA . VAL A 1 312 ? -33.740 30.913 34.271 1.00 51.05 ? 312 VAL A CA 1 ATOM 2479 C C . VAL A 1 312 ? -34.832 31.116 33.249 1.00 49.98 ? 312 VAL A C 1 ATOM 2480 O O . VAL A 1 312 ? -35.476 30.157 32.846 1.00 50.77 ? 312 VAL A O 1 ATOM 2481 C CB . VAL A 1 312 ? -32.621 30.079 33.624 1.00 51.83 ? 312 VAL A CB 1 ATOM 2482 C CG1 . VAL A 1 312 ? -32.085 30.777 32.380 1.00 51.40 ? 312 VAL A CG1 1 ATOM 2483 C CG2 . VAL A 1 312 ? -31.504 29.820 34.629 1.00 52.84 ? 312 VAL A CG2 1 ATOM 2484 N N . LEU A 1 313 ? -35.022 32.367 32.840 1.00 48.87 ? 313 LEU A N 1 ATOM 2485 C CA . LEU A 1 313 ? -36.034 32.743 31.871 1.00 48.81 ? 313 LEU A CA 1 ATOM 2486 C C . LEU A 1 313 ? -35.445 32.831 30.481 1.00 49.07 ? 313 LEU A C 1 ATOM 2487 O O . LEU A 1 313 ? -34.426 33.492 30.289 1.00 49.82 ? 313 LEU A O 1 ATOM 2488 C CB . LEU A 1 313 ? -36.588 34.125 32.189 1.00 48.38 ? 313 LEU A CB 1 ATOM 2489 C CG . LEU A 1 313 ? -37.674 34.228 33.242 1.00 49.84 ? 313 LEU A CG 1 ATOM 2490 C CD1 . LEU A 1 313 ? -37.952 35.695 33.528 1.00 50.42 ? 313 LEU A CD1 1 ATOM 2491 C CD2 . LEU A 1 313 ? -38.956 33.517 32.808 1.00 50.71 ? 313 LEU A CD2 1 ATOM 2492 N N . ALA A 1 314 ? -36.102 32.203 29.506 1.00 48.80 ? 314 ALA A N 1 ATOM 2493 C CA . ALA A 1 314 ? -35.770 32.447 28.101 1.00 48.03 ? 314 ALA A CA 1 ATOM 2494 C C . ALA A 1 314 ? -36.155 33.871 27.723 1.00 47.50 ? 314 ALA A C 1 ATOM 2495 O O . ALA A 1 314 ? -37.241 34.329 28.050 1.00 49.06 ? 314 ALA A O 1 ATOM 2496 C CB . ALA A 1 314 ? -36.479 31.455 27.193 1.00 47.56 ? 314 ALA A CB 1 ATOM 2497 N N . THR A 1 315 ? -35.244 34.572 27.066 1.00 47.83 ? 315 THR A N 1 ATOM 2498 C CA . THR A 1 315 ? -35.545 35.842 26.407 1.00 49.06 ? 315 THR A CA 1 ATOM 2499 C C . THR A 1 315 ? -35.400 35.659 24.906 1.00 48.60 ? 315 THR A C 1 ATOM 2500 O O . THR A 1 315 ? -36.272 36.039 24.151 1.00 48.62 ? 315 THR A O 1 ATOM 2501 C CB . THR A 1 315 ? -34.574 36.954 26.828 1.00 50.24 ? 315 THR A CB 1 ATOM 2502 O OG1 . THR A 1 315 ? -33.231 36.456 26.777 1.00 51.51 ? 315 THR A OG1 1 ATOM 2503 C CG2 . THR A 1 315 ? -34.872 37.412 28.223 1.00 51.11 ? 315 THR A CG2 1 ATOM 2504 N N . GLY A 1 316 ? -34.289 35.070 24.485 1.00 48.08 ? 316 GLY A N 1 ATOM 2505 C CA . GLY A 1 316 ? -34.060 34.797 23.084 1.00 48.94 ? 316 GLY A CA 1 ATOM 2506 C C . GLY A 1 316 ? -34.816 33.582 22.586 1.00 48.82 ? 316 GLY A C 1 ATOM 2507 O O . GLY A 1 316 ? -35.714 33.068 23.251 1.00 48.70 ? 316 GLY A O 1 ATOM 2508 N N . LEU A 1 317 ? -34.440 33.123 21.402 1.00 49.36 ? 317 LEU A N 1 ATOM 2509 C CA . LEU A 1 317 ? -35.110 31.995 20.769 1.00 50.30 ? 317 LEU A CA 1 ATOM 2510 C C . LEU A 1 317 ? -34.240 30.768 20.825 1.00 50.10 ? 317 LEU A C 1 ATOM 2511 O O . LEU A 1 317 ? -33.096 30.810 21.269 1.00 49.92 ? 317 LEU A O 1 ATOM 2512 C CB . LEU A 1 317 ? -35.493 32.300 19.308 1.00 51.30 ? 317 LEU A CB 1 ATOM 2513 C CG . LEU A 1 317 ? -34.474 33.070 18.467 1.00 52.51 ? 317 LEU A CG 1 ATOM 2514 C CD1 . LEU A 1 317 ? -34.236 32.419 17.128 1.00 53.61 ? 317 LEU A CD1 1 ATOM 2515 C CD2 . LEU A 1 317 ? -34.981 34.481 18.252 1.00 53.69 ? 317 LEU A CD2 1 ATOM 2516 N N . ARG A 1 318 ? -34.825 29.671 20.370 1.00 50.56 ? 318 ARG A N 1 ATOM 2517 C CA . ARG A 1 318 ? -34.185 28.384 20.337 1.00 52.65 ? 318 ARG A CA 1 ATOM 2518 C C . ARG A 1 318 ? -32.978 28.456 19.432 1.00 54.09 ? 318 ARG A C 1 ATOM 2519 O O . ARG A 1 318 ? -33.111 28.676 18.229 1.00 54.01 ? 318 ARG A O 1 ATOM 2520 C CB . ARG A 1 318 ? -35.184 27.356 19.822 1.00 53.93 ? 318 ARG A CB 1 ATOM 2521 C CG . ARG A 1 318 ? -34.651 25.946 19.720 1.00 57.56 ? 318 ARG A CG 1 ATOM 2522 C CD . ARG A 1 318 ? -35.727 25.031 19.165 1.00 59.92 ? 318 ARG A CD 1 ATOM 2523 N NE . ARG A 1 318 ? -36.709 24.655 20.177 1.00 60.36 ? 318 ARG A NE 1 ATOM 2524 C CZ . ARG A 1 318 ? -36.672 23.521 20.871 1.00 63.76 ? 318 ARG A CZ 1 ATOM 2525 N NH1 . ARG A 1 318 ? -35.694 22.637 20.677 1.00 65.79 ? 318 ARG A NH1 1 ATOM 2526 N NH2 . ARG A 1 318 ? -37.618 23.266 21.772 1.00 64.45 ? 318 ARG A NH2 1 ATOM 2527 N N . ASN A 1 319 ? -31.807 28.267 20.028 1.00 56.29 ? 319 ASN A N 1 ATOM 2528 C CA . ASN A 1 319 ? -30.536 28.363 19.333 1.00 59.68 ? 319 ASN A CA 1 ATOM 2529 C C . ASN A 1 319 ? -30.174 27.076 18.604 1.00 65.56 ? 319 ASN A C 1 ATOM 2530 O O . ASN A 1 319 ? -30.386 25.977 19.109 1.00 68.36 ? 319 ASN A O 1 ATOM 2531 C CB . ASN A 1 319 ? -29.442 28.710 20.330 1.00 59.72 ? 319 ASN A CB 1 ATOM 2532 C CG . ASN A 1 319 ? -28.125 29.007 19.669 1.00 60.72 ? 319 ASN A CG 1 ATOM 2533 O OD1 . ASN A 1 319 ? -28.073 29.358 18.502 1.00 60.40 ? 319 ASN A OD1 1 ATOM 2534 N ND2 . ASN A 1 319 ? -27.049 28.871 20.419 1.00 62.68 ? 319 ASN A ND2 1 ATOM 2535 N N . SER A 1 320 ? -29.596 27.232 17.421 1.00 71.81 ? 320 SER A N 1 ATOM 2536 C CA . SER A 1 320 ? -29.350 26.118 16.503 1.00 77.93 ? 320 SER A CA 1 ATOM 2537 C C . SER A 1 320 ? -27.962 25.469 16.698 1.00 83.46 ? 320 SER A C 1 ATOM 2538 O O . SER A 1 320 ? -27.015 26.149 17.106 1.00 82.24 ? 320 SER A O 1 ATOM 2539 C CB . SER A 1 320 ? -29.493 26.623 15.065 1.00 77.15 ? 320 SER A CB 1 ATOM 2540 O OG . SER A 1 320 ? -30.615 27.489 14.973 1.00 74.93 ? 320 SER A OG 1 ATOM 2541 N N . PRO A 1 321 ? -27.849 24.149 16.416 1.00 89.23 ? 321 PRO A N 1 ATOM 2542 C CA . PRO A 1 321 ? -26.577 23.412 16.433 1.00 94.22 ? 321 PRO A CA 1 ATOM 2543 C C . PRO A 1 321 ? -25.444 24.070 15.637 1.00 96.46 ? 321 PRO A C 1 ATOM 2544 O O . PRO A 1 321 ? -25.614 24.384 14.459 1.00 95.35 ? 321 PRO A O 1 ATOM 2545 C CB . PRO A 1 321 ? -26.955 22.069 15.801 1.00 96.72 ? 321 PRO A CB 1 ATOM 2546 C CG . PRO A 1 321 ? -28.379 21.863 16.195 1.00 94.13 ? 321 PRO A CG 1 ATOM 2547 C CD . PRO A 1 321 ? -29.002 23.228 16.309 1.00 89.61 ? 321 PRO A CD 1 ATOM 2548 N N . GLY B 2 1 ? -41.710 23.662 17.119 1.00 47.61 ? 1 GLY B N 1 ATOM 2549 C CA . GLY B 2 1 ? -42.553 24.665 17.839 1.00 45.26 ? 1 GLY B CA 1 ATOM 2550 C C . GLY B 2 1 ? -43.962 24.754 17.285 1.00 44.22 ? 1 GLY B C 1 ATOM 2551 O O . GLY B 2 1 ? -44.260 24.202 16.218 1.00 45.30 ? 1 GLY B O 1 ATOM 2552 N N . LEU B 2 2 ? -44.819 25.489 17.993 1.00 41.27 ? 2 LEU B N 1 ATOM 2553 C CA . LEU B 2 2 ? -46.228 25.542 17.648 1.00 40.32 ? 2 LEU B CA 1 ATOM 2554 C C . LEU B 2 2 ? -46.508 26.089 16.249 1.00 40.84 ? 2 LEU B C 1 ATOM 2555 O O . LEU B 2 2 ? -47.461 25.657 15.593 1.00 42.21 ? 2 LEU B O 1 ATOM 2556 C CB . LEU B 2 2 ? -46.988 26.356 18.679 1.00 38.58 ? 2 LEU B CB 1 ATOM 2557 C CG . LEU B 2 2 ? -47.268 25.633 19.988 1.00 38.14 ? 2 LEU B CG 1 ATOM 2558 C CD1 . LEU B 2 2 ? -48.008 26.533 20.947 1.00 36.68 ? 2 LEU B CD1 1 ATOM 2559 C CD2 . LEU B 2 2 ? -48.062 24.375 19.748 1.00 40.35 ? 2 LEU B CD2 1 ATOM 2560 N N . PHE B 2 3 ? -45.660 26.997 15.782 1.00 39.05 ? 3 PHE B N 1 ATOM 2561 C CA . PHE B 2 3 ? -45.947 27.738 14.567 1.00 39.62 ? 3 PHE B CA 1 ATOM 2562 C C . PHE B 2 3 ? -45.236 27.208 13.343 1.00 40.87 ? 3 PHE B C 1 ATOM 2563 O O . PHE B 2 3 ? -45.493 27.663 12.240 1.00 42.52 ? 3 PHE B O 1 ATOM 2564 C CB . PHE B 2 3 ? -45.703 29.228 14.825 1.00 38.14 ? 3 PHE B CB 1 ATOM 2565 C CG . PHE B 2 3 ? -46.685 29.778 15.803 1.00 37.54 ? 3 PHE B CG 1 ATOM 2566 C CD1 . PHE B 2 3 ? -47.926 30.195 15.378 1.00 37.98 ? 3 PHE B CD1 1 ATOM 2567 C CD2 . PHE B 2 3 ? -46.425 29.732 17.166 1.00 36.69 ? 3 PHE B CD2 1 ATOM 2568 C CE1 . PHE B 2 3 ? -48.866 30.630 16.287 1.00 38.23 ? 3 PHE B CE1 1 ATOM 2569 C CE2 . PHE B 2 3 ? -47.366 30.160 18.080 1.00 35.85 ? 3 PHE B CE2 1 ATOM 2570 C CZ . PHE B 2 3 ? -48.587 30.612 17.636 1.00 36.76 ? 3 PHE B CZ 1 ATOM 2571 N N . GLY B 2 4 ? -44.364 26.231 13.544 1.00 41.57 ? 4 GLY B N 1 ATOM 2572 C CA . GLY B 2 4 ? -43.753 25.497 12.449 1.00 43.13 ? 4 GLY B CA 1 ATOM 2573 C C . GLY B 2 4 ? -42.604 26.160 11.715 1.00 42.71 ? 4 GLY B C 1 ATOM 2574 O O . GLY B 2 4 ? -42.095 25.596 10.740 1.00 44.31 ? 4 GLY B O 1 ATOM 2575 N N . ALA B 2 5 ? -42.190 27.350 12.142 1.00 41.11 ? 5 ALA B N 1 ATOM 2576 C CA . ALA B 2 5 ? -41.172 28.090 11.387 1.00 40.96 ? 5 ALA B CA 1 ATOM 2577 C C . ALA B 2 5 ? -39.793 27.746 11.909 1.00 41.07 ? 5 ALA B C 1 ATOM 2578 O O . ALA B 2 5 ? -39.008 27.130 11.204 1.00 41.67 ? 5 ALA B O 1 ATOM 2579 C CB . ALA B 2 5 ? -41.417 29.587 11.456 1.00 39.76 ? 5 ALA B CB 1 ATOM 2580 N N . ILE B 2 6 ? -39.531 28.120 13.157 1.00 40.86 ? 6 ILE B N 1 ATOM 2581 C CA . ILE B 2 6 ? -38.234 27.897 13.787 1.00 42.55 ? 6 ILE B CA 1 ATOM 2582 C C . ILE B 2 6 ? -37.959 26.407 13.959 1.00 44.32 ? 6 ILE B C 1 ATOM 2583 O O . ILE B 2 6 ? -38.779 25.679 14.529 1.00 43.77 ? 6 ILE B O 1 ATOM 2584 C CB . ILE B 2 6 ? -38.135 28.595 15.160 1.00 41.79 ? 6 ILE B CB 1 ATOM 2585 C CG1 . ILE B 2 6 ? -37.926 30.090 14.961 1.00 41.62 ? 6 ILE B CG1 1 ATOM 2586 C CG2 . ILE B 2 6 ? -36.968 28.039 15.958 1.00 43.66 ? 6 ILE B CG2 1 ATOM 2587 C CD1 . ILE B 2 6 ? -38.165 30.939 16.191 1.00 41.37 ? 6 ILE B CD1 1 ATOM 2588 N N . ALA B 2 7 ? -36.795 25.973 13.469 1.00 46.15 ? 7 ALA B N 1 ATOM 2589 C CA . ALA B 2 7 ? -36.439 24.558 13.457 1.00 49.57 ? 7 ALA B CA 1 ATOM 2590 C C . ALA B 2 7 ? -37.583 23.753 12.859 1.00 50.57 ? 7 ALA B C 1 ATOM 2591 O O . ALA B 2 7 ? -37.915 22.683 13.339 1.00 52.39 ? 7 ALA B O 1 ATOM 2592 C CB . ALA B 2 7 ? -36.135 24.078 14.869 1.00 50.60 ? 7 ALA B CB 1 ATOM 2593 N N . GLY B 2 8 ? -38.188 24.303 11.817 1.00 50.54 ? 8 GLY B N 1 ATOM 2594 C CA . GLY B 2 8 ? -39.348 23.711 11.179 1.00 52.50 ? 8 GLY B CA 1 ATOM 2595 C C . GLY B 2 8 ? -39.119 23.711 9.685 1.00 55.10 ? 8 GLY B C 1 ATOM 2596 O O . GLY B 2 8 ? -38.219 23.031 9.213 1.00 60.29 ? 8 GLY B O 1 ATOM 2597 N N . PHE B 2 9 ? -39.916 24.468 8.933 1.00 53.91 ? 9 PHE B N 1 ATOM 2598 C CA . PHE B 2 9 ? -39.657 24.606 7.512 1.00 54.39 ? 9 PHE B CA 1 ATOM 2599 C C . PHE B 2 9 ? -38.420 25.479 7.324 1.00 54.59 ? 9 PHE B C 1 ATOM 2600 O O . PHE B 2 9 ? -37.697 25.313 6.353 1.00 58.09 ? 9 PHE B O 1 ATOM 2601 C CB . PHE B 2 9 ? -40.891 25.085 6.720 1.00 54.25 ? 9 PHE B CB 1 ATOM 2602 C CG . PHE B 2 9 ? -41.304 26.502 6.997 1.00 51.96 ? 9 PHE B CG 1 ATOM 2603 C CD1 . PHE B 2 9 ? -40.759 27.556 6.269 1.00 51.84 ? 9 PHE B CD1 1 ATOM 2604 C CD2 . PHE B 2 9 ? -42.267 26.780 7.942 1.00 50.59 ? 9 PHE B CD2 1 ATOM 2605 C CE1 . PHE B 2 9 ? -41.137 28.862 6.511 1.00 50.33 ? 9 PHE B CE1 1 ATOM 2606 C CE2 . PHE B 2 9 ? -42.653 28.091 8.188 1.00 49.88 ? 9 PHE B CE2 1 ATOM 2607 C CZ . PHE B 2 9 ? -42.081 29.132 7.475 1.00 49.01 ? 9 PHE B CZ 1 ATOM 2608 N N . ILE B 2 10 ? -38.160 26.399 8.245 1.00 52.95 ? 10 ILE B N 1 ATOM 2609 C CA . ILE B 2 10 ? -36.855 27.064 8.283 1.00 53.58 ? 10 ILE B CA 1 ATOM 2610 C C . ILE B 2 10 ? -35.992 26.265 9.230 1.00 55.57 ? 10 ILE B C 1 ATOM 2611 O O . ILE B 2 10 ? -36.177 26.312 10.446 1.00 53.87 ? 10 ILE B O 1 ATOM 2612 C CB . ILE B 2 10 ? -36.922 28.509 8.777 1.00 50.96 ? 10 ILE B CB 1 ATOM 2613 C CG1 . ILE B 2 10 ? -37.895 29.312 7.916 1.00 50.98 ? 10 ILE B CG1 1 ATOM 2614 C CG2 . ILE B 2 10 ? -35.537 29.125 8.735 1.00 50.74 ? 10 ILE B CG2 1 ATOM 2615 C CD1 . ILE B 2 10 ? -38.291 30.629 8.541 1.00 49.65 ? 10 ILE B CD1 1 ATOM 2616 N N . GLU B 2 11 ? -35.037 25.542 8.664 1.00 59.70 ? 11 GLU B N 1 ATOM 2617 C CA . GLU B 2 11 ? -34.343 24.490 9.397 1.00 62.46 ? 11 GLU B CA 1 ATOM 2618 C C . GLU B 2 11 ? -33.455 24.968 10.531 1.00 61.00 ? 11 GLU B C 1 ATOM 2619 O O . GLU B 2 11 ? -33.323 24.266 11.538 1.00 61.52 ? 11 GLU B O 1 ATOM 2620 C CB . GLU B 2 11 ? -33.488 23.682 8.446 1.00 68.26 ? 11 GLU B CB 1 ATOM 2621 C CG . GLU B 2 11 ? -34.250 22.660 7.633 1.00 72.76 ? 11 GLU B CG 1 ATOM 2622 C CD . GLU B 2 11 ? -33.295 21.686 6.972 1.00 79.44 ? 11 GLU B CD 1 ATOM 2623 O OE1 . GLU B 2 11 ? -32.313 22.165 6.334 1.00 80.08 ? 11 GLU B OE1 1 ATOM 2624 O OE2 . GLU B 2 11 ? -33.518 20.458 7.120 1.00 81.68 ? 11 GLU B OE2 1 ATOM 2625 N N . GLY B 2 12 ? -32.825 26.130 10.358 1.00 58.28 ? 12 GLY B N 1 ATOM 2626 C CA . GLY B 2 12 ? -31.862 26.631 11.335 1.00 58.11 ? 12 GLY B CA 1 ATOM 2627 C C . GLY B 2 12 ? -31.661 28.138 11.335 1.00 56.41 ? 12 GLY B C 1 ATOM 2628 O O . GLY B 2 12 ? -31.975 28.836 10.364 1.00 55.03 ? 12 GLY B O 1 ATOM 2629 N N . GLY B 2 13 ? -31.134 28.640 12.443 1.00 55.80 ? 13 GLY B N 1 ATOM 2630 C CA . GLY B 2 13 ? -30.836 30.054 12.573 1.00 55.39 ? 13 GLY B CA 1 ATOM 2631 C C . GLY B 2 13 ? -29.580 30.457 11.813 1.00 57.42 ? 13 GLY B C 1 ATOM 2632 O O . GLY B 2 13 ? -28.888 29.619 11.238 1.00 59.55 ? 13 GLY B O 1 ATOM 2633 N N . TRP B 2 14 ? -29.301 31.754 11.815 1.00 56.63 ? 14 TRP B N 1 ATOM 2634 C CA . TRP B 2 14 ? -28.205 32.324 11.060 1.00 57.69 ? 14 TRP B CA 1 ATOM 2635 C C . TRP B 2 14 ? -27.190 32.947 11.994 1.00 61.23 ? 14 TRP B C 1 ATOM 2636 O O . TRP B 2 14 ? -27.465 33.962 12.616 1.00 60.67 ? 14 TRP B O 1 ATOM 2637 C CB . TRP B 2 14 ? -28.734 33.405 10.123 1.00 54.93 ? 14 TRP B CB 1 ATOM 2638 C CG . TRP B 2 14 ? -29.539 32.877 8.967 1.00 53.27 ? 14 TRP B CG 1 ATOM 2639 C CD1 . TRP B 2 14 ? -29.439 31.646 8.383 1.00 53.29 ? 14 TRP B CD1 1 ATOM 2640 C CD2 . TRP B 2 14 ? -30.534 33.591 8.222 1.00 51.07 ? 14 TRP B CD2 1 ATOM 2641 N NE1 . TRP B 2 14 ? -30.316 31.549 7.331 1.00 52.31 ? 14 TRP B NE1 1 ATOM 2642 C CE2 . TRP B 2 14 ? -31.001 32.729 7.213 1.00 51.02 ? 14 TRP B CE2 1 ATOM 2643 C CE3 . TRP B 2 14 ? -31.074 34.875 8.315 1.00 49.88 ? 14 TRP B CE3 1 ATOM 2644 C CZ2 . TRP B 2 14 ? -31.996 33.105 6.311 1.00 50.43 ? 14 TRP B CZ2 1 ATOM 2645 C CZ3 . TRP B 2 14 ? -32.052 35.249 7.416 1.00 49.09 ? 14 TRP B CZ3 1 ATOM 2646 C CH2 . TRP B 2 14 ? -32.505 34.367 6.428 1.00 49.40 ? 14 TRP B CH2 1 ATOM 2647 N N . GLN B 2 15 ? -26.008 32.353 12.084 1.00 66.84 ? 15 GLN B N 1 ATOM 2648 C CA . GLN B 2 15 ? -24.901 32.981 12.816 1.00 71.85 ? 15 GLN B CA 1 ATOM 2649 C C . GLN B 2 15 ? -24.562 34.344 12.195 1.00 72.79 ? 15 GLN B C 1 ATOM 2650 O O . GLN B 2 15 ? -24.102 35.243 12.889 1.00 75.81 ? 15 GLN B O 1 ATOM 2651 C CB . GLN B 2 15 ? -23.642 32.102 12.795 1.00 76.63 ? 15 GLN B CB 1 ATOM 2652 C CG . GLN B 2 15 ? -23.786 30.717 13.418 1.00 78.69 ? 15 GLN B CG 1 ATOM 2653 C CD . GLN B 2 15 ? -23.711 30.723 14.938 1.00 80.86 ? 15 GLN B CD 1 ATOM 2654 O OE1 . GLN B 2 15 ? -24.732 30.539 15.616 1.00 81.19 ? 15 GLN B OE1 1 ATOM 2655 N NE2 . GLN B 2 15 ? -22.506 30.924 15.483 1.00 82.51 ? 15 GLN B NE2 1 ATOM 2656 N N . GLY B 2 16 ? -24.789 34.483 10.888 1.00 71.64 ? 16 GLY B N 1 ATOM 2657 C CA . GLY B 2 16 ? -24.468 35.709 10.159 1.00 72.03 ? 16 GLY B CA 1 ATOM 2658 C C . GLY B 2 16 ? -25.381 36.911 10.366 1.00 70.07 ? 16 GLY B C 1 ATOM 2659 O O . GLY B 2 16 ? -25.067 38.003 9.892 1.00 72.32 ? 16 GLY B O 1 ATOM 2660 N N . MET B 2 17 ? -26.504 36.742 11.059 1.00 66.12 ? 17 MET B N 1 ATOM 2661 C CA . MET B 2 17 ? -27.384 37.879 11.338 1.00 64.69 ? 17 MET B CA 1 ATOM 2662 C C . MET B 2 17 ? -27.299 38.334 12.791 1.00 64.95 ? 17 MET B C 1 ATOM 2663 O O . MET B 2 17 ? -27.958 37.782 13.660 1.00 64.14 ? 17 MET B O 1 ATOM 2664 C CB . MET B 2 17 ? -28.826 37.544 10.999 1.00 61.93 ? 17 MET B CB 1 ATOM 2665 C CG . MET B 2 17 ? -29.725 38.755 11.115 1.00 62.02 ? 17 MET B CG 1 ATOM 2666 S SD . MET B 2 17 ? -31.374 38.436 10.502 1.00 59.21 ? 17 MET B SD 1 ATOM 2667 C CE . MET B 2 17 ? -31.791 37.046 11.542 1.00 59.03 ? 17 MET B CE 1 ATOM 2668 N N . VAL B 2 18 ? -26.510 39.373 13.038 1.00 67.97 ? 18 VAL B N 1 ATOM 2669 C CA . VAL B 2 18 ? -26.218 39.831 14.398 1.00 69.12 ? 18 VAL B CA 1 ATOM 2670 C C . VAL B 2 18 ? -26.978 41.097 14.796 1.00 68.82 ? 18 VAL B C 1 ATOM 2671 O O . VAL B 2 18 ? -27.086 41.418 15.970 1.00 69.44 ? 18 VAL B O 1 ATOM 2672 C CB . VAL B 2 18 ? -24.705 40.042 14.576 1.00 73.37 ? 18 VAL B CB 1 ATOM 2673 C CG1 . VAL B 2 18 ? -23.961 38.803 14.100 1.00 74.37 ? 18 VAL B CG1 1 ATOM 2674 C CG2 . VAL B 2 18 ? -24.209 41.274 13.822 1.00 75.97 ? 18 VAL B CG2 1 ATOM 2675 N N . ASP B 2 19 ? -27.522 41.800 13.815 1.00 69.09 ? 19 ASP B N 1 ATOM 2676 C CA . ASP B 2 19 ? -28.216 43.055 14.067 1.00 70.88 ? 19 ASP B CA 1 ATOM 2677 C C . ASP B 2 19 ? -29.688 42.866 14.522 1.00 66.76 ? 19 ASP B C 1 ATOM 2678 O O . ASP B 2 19 ? -30.380 43.847 14.782 1.00 67.31 ? 19 ASP B O 1 ATOM 2679 C CB . ASP B 2 19 ? -28.093 44.004 12.837 1.00 74.37 ? 19 ASP B CB 1 ATOM 2680 C CG . ASP B 2 19 ? -28.294 43.290 11.475 1.00 74.46 ? 19 ASP B CG 1 ATOM 2681 O OD1 . ASP B 2 19 ? -28.528 42.064 11.436 1.00 72.68 ? 19 ASP B OD1 1 ATOM 2682 O OD2 . ASP B 2 19 ? -28.214 43.963 10.422 1.00 78.44 ? 19 ASP B OD2 1 ATOM 2683 N N . GLY B 2 20 ? -30.169 41.629 14.638 1.00 62.43 ? 20 GLY B N 1 ATOM 2684 C CA . GLY B 2 20 ? -31.558 41.408 15.072 1.00 59.47 ? 20 GLY B CA 1 ATOM 2685 C C . GLY B 2 20 ? -31.946 39.956 15.307 1.00 56.54 ? 20 GLY B C 1 ATOM 2686 O O . GLY B 2 20 ? -31.142 39.053 15.106 1.00 56.76 ? 20 GLY B O 1 ATOM 2687 N N . TRP B 2 21 ? -33.185 39.728 15.734 1.00 54.12 ? 21 TRP B N 1 ATOM 2688 C CA . TRP B 2 21 ? -33.663 38.361 15.960 1.00 51.92 ? 21 TRP B CA 1 ATOM 2689 C C . TRP B 2 21 ? -34.226 37.734 14.697 1.00 49.38 ? 21 TRP B C 1 ATOM 2690 O O . TRP B 2 21 ? -34.065 36.524 14.482 1.00 48.27 ? 21 TRP B O 1 ATOM 2691 C CB . TRP B 2 21 ? -34.709 38.294 17.077 1.00 51.02 ? 21 TRP B CB 1 ATOM 2692 C CG . TRP B 2 21 ? -34.144 38.068 18.461 1.00 52.73 ? 21 TRP B CG 1 ATOM 2693 C CD1 . TRP B 2 21 ? -33.059 37.309 18.811 1.00 54.19 ? 21 TRP B CD1 1 ATOM 2694 C CD2 . TRP B 2 21 ? -34.666 38.591 19.675 1.00 53.79 ? 21 TRP B CD2 1 ATOM 2695 N NE1 . TRP B 2 21 ? -32.865 37.347 20.169 1.00 55.26 ? 21 TRP B NE1 1 ATOM 2696 C CE2 . TRP B 2 21 ? -33.844 38.126 20.722 1.00 55.09 ? 21 TRP B CE2 1 ATOM 2697 C CE3 . TRP B 2 21 ? -35.752 39.413 19.980 1.00 54.50 ? 21 TRP B CE3 1 ATOM 2698 C CZ2 . TRP B 2 21 ? -34.079 38.451 22.045 1.00 57.52 ? 21 TRP B CZ2 1 ATOM 2699 C CZ3 . TRP B 2 21 ? -35.989 39.733 21.296 1.00 56.00 ? 21 TRP B CZ3 1 ATOM 2700 C CH2 . TRP B 2 21 ? -35.157 39.255 22.316 1.00 57.63 ? 21 TRP B CH2 1 ATOM 2701 N N . TYR B 2 22 ? -34.880 38.551 13.875 1.00 47.57 ? 22 TYR B N 1 ATOM 2702 C CA . TYR B 2 22 ? -35.492 38.078 12.643 1.00 46.44 ? 22 TYR B CA 1 ATOM 2703 C C . TYR B 2 22 ? -35.104 39.002 11.517 1.00 47.39 ? 22 TYR B C 1 ATOM 2704 O O . TYR B 2 22 ? -34.993 40.215 11.707 1.00 48.45 ? 22 TYR B O 1 ATOM 2705 C CB . TYR B 2 22 ? -37.029 38.082 12.744 1.00 45.93 ? 22 TYR B CB 1 ATOM 2706 C CG . TYR B 2 22 ? -37.581 37.812 14.118 1.00 45.31 ? 22 TYR B CG 1 ATOM 2707 C CD1 . TYR B 2 22 ? -37.427 36.574 14.708 1.00 44.44 ? 22 TYR B CD1 1 ATOM 2708 C CD2 . TYR B 2 22 ? -38.254 38.801 14.829 1.00 46.31 ? 22 TYR B CD2 1 ATOM 2709 C CE1 . TYR B 2 22 ? -37.927 36.323 15.967 1.00 44.53 ? 22 TYR B CE1 1 ATOM 2710 C CE2 . TYR B 2 22 ? -38.757 38.559 16.089 1.00 45.50 ? 22 TYR B CE2 1 ATOM 2711 C CZ . TYR B 2 22 ? -38.593 37.316 16.648 1.00 45.01 ? 22 TYR B CZ 1 ATOM 2712 O OH . TYR B 2 22 ? -39.083 37.034 17.898 1.00 45.72 ? 22 TYR B OH 1 ATOM 2713 N N . GLY B 2 23 ? -34.948 38.446 10.326 1.00 47.15 ? 23 GLY B N 1 ATOM 2714 C CA . GLY B 2 23 ? -34.662 39.284 9.183 1.00 49.08 ? 23 GLY B CA 1 ATOM 2715 C C . GLY B 2 23 ? -34.625 38.519 7.895 1.00 49.83 ? 23 GLY B C 1 ATOM 2716 O O . GLY B 2 23 ? -35.149 37.402 7.818 1.00 48.15 ? 23 GLY B O 1 ATOM 2717 N N . TYR B 2 24 ? -33.991 39.137 6.895 1.00 52.28 ? 24 TYR B N 1 ATOM 2718 C CA . TYR B 2 24 ? -33.940 38.622 5.529 1.00 54.06 ? 24 TYR B CA 1 ATOM 2719 C C . TYR B 2 24 ? -32.514 38.319 5.100 1.00 54.93 ? 24 TYR B C 1 ATOM 2720 O O . TYR B 2 24 ? -31.588 39.019 5.490 1.00 55.03 ? 24 TYR B O 1 ATOM 2721 C CB . TYR B 2 24 ? -34.501 39.659 4.560 1.00 56.85 ? 24 TYR B CB 1 ATOM 2722 C CG . TYR B 2 24 ? -35.746 40.335 5.055 1.00 58.25 ? 24 TYR B CG 1 ATOM 2723 C CD1 . TYR B 2 24 ? -35.670 41.410 5.922 1.00 60.00 ? 24 TYR B CD1 1 ATOM 2724 C CD2 . TYR B 2 24 ? -37.002 39.902 4.659 1.00 59.36 ? 24 TYR B CD2 1 ATOM 2725 C CE1 . TYR B 2 24 ? -36.807 42.048 6.378 1.00 61.39 ? 24 TYR B CE1 1 ATOM 2726 C CE2 . TYR B 2 24 ? -38.153 40.527 5.116 1.00 60.42 ? 24 TYR B CE2 1 ATOM 2727 C CZ . TYR B 2 24 ? -38.049 41.601 5.977 1.00 61.41 ? 24 TYR B CZ 1 ATOM 2728 O OH . TYR B 2 24 ? -39.176 42.238 6.441 1.00 62.34 ? 24 TYR B OH 1 ATOM 2729 N N . HIS B 2 25 ? -32.342 37.273 4.296 1.00 55.26 ? 25 HIS B N 1 ATOM 2730 C CA . HIS B 2 25 ? -31.084 37.066 3.586 1.00 56.64 ? 25 HIS B CA 1 ATOM 2731 C C . HIS B 2 25 ? -31.340 37.052 2.111 1.00 58.06 ? 25 HIS B C 1 ATOM 2732 O O . HIS B 2 25 ? -32.114 36.234 1.631 1.00 59.05 ? 25 HIS B O 1 ATOM 2733 C CB . HIS B 2 25 ? -30.432 35.754 3.948 1.00 56.25 ? 25 HIS B CB 1 ATOM 2734 C CG . HIS B 2 25 ? -29.137 35.527 3.239 1.00 59.11 ? 25 HIS B CG 1 ATOM 2735 N ND1 . HIS B 2 25 ? -29.050 34.826 2.054 1.00 60.43 ? 25 HIS B ND1 1 ATOM 2736 C CD2 . HIS B 2 25 ? -27.876 35.930 3.533 1.00 60.73 ? 25 HIS B CD2 1 ATOM 2737 C CE1 . HIS B 2 25 ? -27.789 34.788 1.662 1.00 62.53 ? 25 HIS B CE1 1 ATOM 2738 N NE2 . HIS B 2 25 ? -27.057 35.450 2.542 1.00 62.93 ? 25 HIS B NE2 1 ATOM 2739 N N . HIS B 2 26 ? -30.677 37.947 1.392 1.00 59.96 ? 26 HIS B N 1 ATOM 2740 C CA . HIS B 2 26 ? -30.858 38.067 -0.046 1.00 61.48 ? 26 HIS B CA 1 ATOM 2741 C C . HIS B 2 26 ? -29.643 37.518 -0.779 1.00 62.95 ? 26 HIS B C 1 ATOM 2742 O O . HIS B 2 26 ? -28.556 37.470 -0.216 1.00 63.04 ? 26 HIS B O 1 ATOM 2743 C CB . HIS B 2 26 ? -31.089 39.536 -0.415 1.00 63.19 ? 26 HIS B CB 1 ATOM 2744 C CG . HIS B 2 26 ? -29.850 40.371 -0.405 1.00 65.22 ? 26 HIS B CG 1 ATOM 2745 N ND1 . HIS B 2 26 ? -29.376 40.984 0.733 1.00 65.63 ? 26 HIS B ND1 1 ATOM 2746 C CD2 . HIS B 2 26 ? -28.990 40.703 -1.396 1.00 67.93 ? 26 HIS B CD2 1 ATOM 2747 C CE1 . HIS B 2 26 ? -28.274 41.654 0.445 1.00 67.40 ? 26 HIS B CE1 1 ATOM 2748 N NE2 . HIS B 2 26 ? -28.019 41.501 -0.841 1.00 68.96 ? 26 HIS B NE2 1 ATOM 2749 N N . SER B 2 27 ? -29.831 37.090 -2.024 1.00 64.16 ? 27 SER B N 1 ATOM 2750 C CA . SER B 2 27 ? -28.697 36.753 -2.885 1.00 66.53 ? 27 SER B CA 1 ATOM 2751 C C . SER B 2 27 ? -29.038 36.930 -4.374 1.00 68.50 ? 27 SER B C 1 ATOM 2752 O O . SER B 2 27 ? -30.012 36.361 -4.883 1.00 68.60 ? 27 SER B O 1 ATOM 2753 C CB . SER B 2 27 ? -28.164 35.346 -2.574 1.00 66.44 ? 27 SER B CB 1 ATOM 2754 O OG . SER B 2 27 ? -28.630 34.382 -3.483 1.00 68.23 ? 27 SER B OG 1 ATOM 2755 N N . ASN B 2 28 ? -28.230 37.740 -5.054 1.00 70.52 ? 28 ASN B N 1 ATOM 2756 C CA . ASN B 2 28 ? -28.461 38.095 -6.450 1.00 73.28 ? 28 ASN B CA 1 ATOM 2757 C C . ASN B 2 28 ? -27.136 38.297 -7.184 1.00 76.80 ? 28 ASN B C 1 ATOM 2758 O O . ASN B 2 28 ? -26.083 37.955 -6.658 1.00 76.86 ? 28 ASN B O 1 ATOM 2759 C CB . ASN B 2 28 ? -29.370 39.332 -6.539 1.00 73.12 ? 28 ASN B CB 1 ATOM 2760 C CG . ASN B 2 28 ? -28.751 40.577 -5.940 1.00 72.96 ? 28 ASN B CG 1 ATOM 2761 O OD1 . ASN B 2 28 ? -27.534 40.694 -5.825 1.00 73.90 ? 28 ASN B OD1 1 ATOM 2762 N ND2 . ASN B 2 28 ? -29.596 41.522 -5.559 1.00 72.24 ? 28 ASN B ND2 1 ATOM 2763 N N . GLU B 2 29 ? -27.174 38.839 -8.395 1.00 80.81 ? 29 GLU B N 1 ATOM 2764 C CA . GLU B 2 29 ? -25.948 38.978 -9.176 1.00 85.11 ? 29 GLU B CA 1 ATOM 2765 C C . GLU B 2 29 ? -24.901 39.866 -8.516 1.00 86.19 ? 29 GLU B C 1 ATOM 2766 O O . GLU B 2 29 ? -23.713 39.693 -8.755 1.00 88.38 ? 29 GLU B O 1 ATOM 2767 C CB . GLU B 2 29 ? -26.241 39.533 -10.565 1.00 89.09 ? 29 GLU B CB 1 ATOM 2768 C CG . GLU B 2 29 ? -26.675 38.498 -11.587 1.00 91.03 ? 29 GLU B CG 1 ATOM 2769 C CD . GLU B 2 29 ? -26.483 39.022 -12.993 1.00 95.78 ? 29 GLU B CD 1 ATOM 2770 O OE1 . GLU B 2 29 ? -27.213 39.960 -13.370 1.00 98.00 ? 29 GLU B OE1 1 ATOM 2771 O OE2 . GLU B 2 29 ? -25.580 38.530 -13.704 1.00 98.05 ? 29 GLU B OE2 1 ATOM 2772 N N . GLN B 2 30 ? -25.343 40.817 -7.699 1.00 85.96 ? 30 GLN B N 1 ATOM 2773 C CA . GLN B 2 30 ? -24.456 41.841 -7.146 1.00 87.46 ? 30 GLN B CA 1 ATOM 2774 C C . GLN B 2 30 ? -23.971 41.518 -5.734 1.00 84.40 ? 30 GLN B C 1 ATOM 2775 O O . GLN B 2 30 ? -23.366 42.364 -5.081 1.00 85.04 ? 30 GLN B O 1 ATOM 2776 C CB . GLN B 2 30 ? -25.160 43.203 -7.141 1.00 90.22 ? 30 GLN B CB 1 ATOM 2777 C CG . GLN B 2 30 ? -25.889 43.563 -8.438 1.00 94.53 ? 30 GLN B CG 1 ATOM 2778 C CD . GLN B 2 30 ? -27.398 43.641 -8.255 1.00 95.00 ? 30 GLN B CD 1 ATOM 2779 O OE1 . GLN B 2 30 ? -28.169 42.987 -8.971 1.00 97.81 ? 30 GLN B OE1 1 ATOM 2780 N NE2 . GLN B 2 30 ? -27.827 44.438 -7.279 1.00 93.64 ? 30 GLN B NE2 1 ATOM 2781 N N . GLY B 2 31 ? -24.235 40.300 -5.265 1.00 81.42 ? 31 GLY B N 1 ATOM 2782 C CA . GLY B 2 31 ? -23.856 39.887 -3.915 1.00 78.91 ? 31 GLY B CA 1 ATOM 2783 C C . GLY B 2 31 ? -25.022 39.458 -3.044 1.00 75.04 ? 31 GLY B C 1 ATOM 2784 O O . GLY B 2 31 ? -26.182 39.497 -3.466 1.00 72.91 ? 31 GLY B O 1 ATOM 2785 N N . SER B 2 32 ? -24.698 39.070 -1.814 1.00 72.54 ? 32 SER B N 1 ATOM 2786 C CA . SER B 2 32 ? -25.673 38.539 -0.884 1.00 69.04 ? 32 SER B CA 1 ATOM 2787 C C . SER B 2 32 ? -25.419 39.095 0.501 1.00 67.82 ? 32 SER B C 1 ATOM 2788 O O . SER B 2 32 ? -24.321 39.535 0.785 1.00 69.75 ? 32 SER B O 1 ATOM 2789 C CB . SER B 2 32 ? -25.532 37.025 -0.832 1.00 68.74 ? 32 SER B CB 1 ATOM 2790 O OG . SER B 2 32 ? -24.360 36.672 -0.131 1.00 69.66 ? 32 SER B OG 1 ATOM 2791 N N . GLY B 2 33 ? -26.421 39.045 1.376 1.00 65.49 ? 33 GLY B N 1 ATOM 2792 C CA . GLY B 2 33 ? -26.248 39.525 2.747 1.00 65.08 ? 33 GLY B CA 1 ATOM 2793 C C . GLY B 2 33 ? -27.431 39.402 3.688 1.00 62.22 ? 33 GLY B C 1 ATOM 2794 O O . GLY B 2 33 ? -28.533 39.052 3.286 1.00 60.73 ? 33 GLY B O 1 ATOM 2795 N N . TYR B 2 34 ? -27.182 39.703 4.957 1.00 62.49 ? 34 TYR B N 1 ATOM 2796 C CA . TYR B 2 34 ? -28.200 39.626 5.994 1.00 60.50 ? 34 TYR B CA 1 ATOM 2797 C C . TYR B 2 34 ? -28.711 41.023 6.312 1.00 61.00 ? 34 TYR B C 1 ATOM 2798 O O . TYR B 2 34 ? -27.959 41.978 6.298 1.00 63.87 ? 34 TYR B O 1 ATOM 2799 C CB . TYR B 2 34 ? -27.628 38.964 7.243 1.00 60.32 ? 34 TYR B CB 1 ATOM 2800 C CG . TYR B 2 34 ? -27.157 37.538 7.014 1.00 61.52 ? 34 TYR B CG 1 ATOM 2801 C CD1 . TYR B 2 34 ? -28.042 36.466 7.094 1.00 59.99 ? 34 TYR B CD1 1 ATOM 2802 C CD2 . TYR B 2 34 ? -25.822 37.259 6.719 1.00 64.95 ? 34 TYR B CD2 1 ATOM 2803 C CE1 . TYR B 2 34 ? -27.613 35.161 6.888 1.00 61.12 ? 34 TYR B CE1 1 ATOM 2804 C CE2 . TYR B 2 34 ? -25.383 35.957 6.509 1.00 65.66 ? 34 TYR B CE2 1 ATOM 2805 C CZ . TYR B 2 34 ? -26.279 34.914 6.594 1.00 64.32 ? 34 TYR B CZ 1 ATOM 2806 O OH . TYR B 2 34 ? -25.836 33.626 6.387 1.00 66.10 ? 34 TYR B OH 1 ATOM 2807 N N . ALA B 2 35 ? -30.004 41.135 6.570 1.00 59.90 ? 35 ALA B N 1 ATOM 2808 C CA . ALA B 2 35 ? -30.609 42.385 6.991 1.00 61.33 ? 35 ALA B CA 1 ATOM 2809 C C . ALA B 2 35 ? -31.697 42.092 8.015 1.00 60.57 ? 35 ALA B C 1 ATOM 2810 O O . ALA B 2 35 ? -32.657 41.403 7.717 1.00 60.43 ? 35 ALA B O 1 ATOM 2811 C CB . ALA B 2 35 ? -31.203 43.096 5.806 1.00 62.45 ? 35 ALA B CB 1 ATOM 2812 N N . ALA B 2 36 ? -31.540 42.608 9.223 1.00 62.45 ? 36 ALA B N 1 ATOM 2813 C CA . ALA B 2 36 ? -32.527 42.417 10.263 1.00 61.31 ? 36 ALA B CA 1 ATOM 2814 C C . ALA B 2 36 ? -33.771 43.247 9.967 1.00 62.42 ? 36 ALA B C 1 ATOM 2815 O O . ALA B 2 36 ? -33.672 44.366 9.483 1.00 64.96 ? 36 ALA B O 1 ATOM 2816 C CB . ALA B 2 36 ? -31.947 42.813 11.608 1.00 62.91 ? 36 ALA B CB 1 ATOM 2817 N N . ASP B 2 37 ? -34.933 42.669 10.255 1.00 61.97 ? 37 ASP B N 1 ATOM 2818 C CA . ASP B 2 37 ? -36.211 43.369 10.247 1.00 63.76 ? 37 ASP B CA 1 ATOM 2819 C C . ASP B 2 37 ? -36.397 44.025 11.622 1.00 66.28 ? 37 ASP B C 1 ATOM 2820 O O . ASP B 2 37 ? -36.625 43.341 12.632 1.00 61.89 ? 37 ASP B O 1 ATOM 2821 C CB . ASP B 2 37 ? -37.322 42.355 9.982 1.00 63.18 ? 37 ASP B CB 1 ATOM 2822 C CG . ASP B 2 37 ? -38.672 42.992 9.830 1.00 64.87 ? 37 ASP B CG 1 ATOM 2823 O OD1 . ASP B 2 37 ? -39.016 43.381 8.696 1.00 66.98 ? 37 ASP B OD1 1 ATOM 2824 O OD2 . ASP B 2 37 ? -39.400 43.076 10.842 1.00 64.90 ? 37 ASP B OD2 1 ATOM 2825 N N . LYS B 2 38 ? -36.274 45.350 11.664 1.00 72.65 ? 38 LYS B N 1 ATOM 2826 C CA . LYS B 2 38 ? -36.306 46.094 12.930 1.00 75.25 ? 38 LYS B CA 1 ATOM 2827 C C . LYS B 2 38 ? -37.663 46.043 13.621 1.00 75.14 ? 38 LYS B C 1 ATOM 2828 O O . LYS B 2 38 ? -37.730 45.868 14.833 1.00 75.06 ? 38 LYS B O 1 ATOM 2829 C CB . LYS B 2 38 ? -35.909 47.547 12.706 1.00 80.21 ? 38 LYS B CB 1 ATOM 2830 C CG . LYS B 2 38 ? -34.438 47.727 12.381 1.00 84.23 ? 38 LYS B CG 1 ATOM 2831 C CD . LYS B 2 38 ? -34.089 49.196 12.198 1.00 90.84 ? 38 LYS B CD 1 ATOM 2832 C CE . LYS B 2 38 ? -32.699 49.369 11.607 1.00 94.04 ? 38 LYS B CE 1 ATOM 2833 N NZ . LYS B 2 38 ? -32.250 50.790 11.658 1.00 100.33 ? 38 LYS B NZ 1 ATOM 2834 N N . GLU B 2 39 ? -38.731 46.181 12.837 1.00 76.18 ? 39 GLU B N 1 ATOM 2835 C CA . GLU B 2 39 ? -40.104 46.226 13.342 1.00 75.82 ? 39 GLU B CA 1 ATOM 2836 C C . GLU B 2 39 ? -40.460 44.981 14.140 1.00 69.28 ? 39 GLU B C 1 ATOM 2837 O O . GLU B 2 39 ? -40.848 45.077 15.302 1.00 69.08 ? 39 GLU B O 1 ATOM 2838 C CB . GLU B 2 39 ? -41.075 46.383 12.168 1.00 81.32 ? 39 GLU B CB 1 ATOM 2839 C CG . GLU B 2 39 ? -42.539 46.596 12.537 1.00 85.82 ? 39 GLU B CG 1 ATOM 2840 C CD . GLU B 2 39 ? -43.453 46.506 11.325 1.00 88.95 ? 39 GLU B CD 1 ATOM 2841 O OE1 . GLU B 2 39 ? -43.308 47.342 10.405 1.00 92.80 ? 39 GLU B OE1 1 ATOM 2842 O OE2 . GLU B 2 39 ? -44.312 45.598 11.290 1.00 87.01 ? 39 GLU B OE2 1 ATOM 2843 N N . SER B 2 40 ? -40.331 43.816 13.523 1.00 63.48 ? 40 SER B N 1 ATOM 2844 C CA . SER B 2 40 ? -40.639 42.583 14.222 1.00 59.79 ? 40 SER B CA 1 ATOM 2845 C C . SER B 2 40 ? -39.699 42.398 15.402 1.00 58.85 ? 40 SER B C 1 ATOM 2846 O O . SER B 2 40 ? -40.138 42.003 16.477 1.00 58.68 ? 40 SER B O 1 ATOM 2847 C CB . SER B 2 40 ? -40.579 41.368 13.296 1.00 57.05 ? 40 SER B CB 1 ATOM 2848 O OG . SER B 2 40 ? -39.352 41.310 12.607 1.00 57.49 ? 40 SER B OG 1 ATOM 2849 N N . THR B 2 41 ? -38.416 42.698 15.212 1.00 58.58 ? 41 THR B N 1 ATOM 2850 C CA . THR B 2 41 ? -37.430 42.524 16.280 1.00 57.42 ? 41 THR B CA 1 ATOM 2851 C C . THR B 2 41 ? -37.786 43.367 17.499 1.00 57.80 ? 41 THR B C 1 ATOM 2852 O O . THR B 2 41 ? -37.834 42.856 18.614 1.00 54.98 ? 41 THR B O 1 ATOM 2853 C CB . THR B 2 41 ? -36.013 42.902 15.808 1.00 59.33 ? 41 THR B CB 1 ATOM 2854 O OG1 . THR B 2 41 ? -35.659 42.093 14.686 1.00 59.65 ? 41 THR B OG1 1 ATOM 2855 C CG2 . THR B 2 41 ? -34.987 42.685 16.909 1.00 59.51 ? 41 THR B CG2 1 ATOM 2856 N N . GLN B 2 42 ? -38.045 44.653 17.279 1.00 60.13 ? 42 GLN B N 1 ATOM 2857 C CA . GLN B 2 42 ? -38.363 45.564 18.376 1.00 62.74 ? 42 GLN B CA 1 ATOM 2858 C C . GLN B 2 42 ? -39.629 45.138 19.093 1.00 61.15 ? 42 GLN B C 1 ATOM 2859 O O . GLN B 2 42 ? -39.706 45.210 20.316 1.00 60.39 ? 42 GLN B O 1 ATOM 2860 C CB . GLN B 2 42 ? -38.530 46.998 17.875 1.00 67.28 ? 42 GLN B CB 1 ATOM 2861 C CG . GLN B 2 42 ? -38.636 48.020 18.992 1.00 71.19 ? 42 GLN B CG 1 ATOM 2862 C CD . GLN B 2 42 ? -37.414 48.012 19.895 1.00 74.26 ? 42 GLN B CD 1 ATOM 2863 O OE1 . GLN B 2 42 ? -37.503 47.681 21.081 1.00 74.74 ? 42 GLN B OE1 1 ATOM 2864 N NE2 . GLN B 2 42 ? -36.259 48.360 19.332 1.00 75.99 ? 42 GLN B NE2 1 ATOM 2865 N N . LYS B 2 43 ? -40.621 44.708 18.322 1.00 60.81 ? 43 LYS B N 1 ATOM 2866 C CA . LYS B 2 43 ? -41.846 44.138 18.887 1.00 61.35 ? 43 LYS B CA 1 ATOM 2867 C C . LYS B 2 43 ? -41.528 43.010 19.855 1.00 55.75 ? 43 LYS B C 1 ATOM 2868 O O . LYS B 2 43 ? -42.115 42.936 20.929 1.00 55.32 ? 43 LYS B O 1 ATOM 2869 C CB . LYS B 2 43 ? -42.776 43.621 17.781 1.00 64.41 ? 43 LYS B CB 1 ATOM 2870 C CG . LYS B 2 43 ? -44.217 44.100 17.886 1.00 71.07 ? 43 LYS B CG 1 ATOM 2871 C CD . LYS B 2 43 ? -44.951 43.896 16.560 1.00 77.23 ? 43 LYS B CD 1 ATOM 2872 C CE . LYS B 2 43 ? -46.453 44.151 16.657 1.00 80.21 ? 43 LYS B CE 1 ATOM 2873 N NZ . LYS B 2 43 ? -46.733 45.606 16.536 1.00 85.76 ? 43 LYS B NZ 1 ATOM 2874 N N . ALA B 2 44 ? -40.587 42.149 19.474 1.00 52.28 ? 44 ALA B N 1 ATOM 2875 C CA . ALA B 2 44 ? -40.185 41.019 20.307 1.00 49.90 ? 44 ALA B CA 1 ATOM 2876 C C . ALA B 2 44 ? -39.453 41.473 21.545 1.00 51.25 ? 44 ALA B C 1 ATOM 2877 O O . ALA B 2 44 ? -39.689 40.955 22.626 1.00 51.26 ? 44 ALA B O 1 ATOM 2878 C CB . ALA B 2 44 ? -39.314 40.050 19.521 1.00 48.81 ? 44 ALA B CB 1 ATOM 2879 N N . ILE B 2 45 ? -38.557 42.438 21.398 1.00 53.95 ? 45 ILE B N 1 ATOM 2880 C CA . ILE B 2 45 ? -37.814 42.931 22.548 1.00 57.05 ? 45 ILE B CA 1 ATOM 2881 C C . ILE B 2 45 ? -38.768 43.541 23.571 1.00 58.80 ? 45 ILE B C 1 ATOM 2882 O O . ILE B 2 45 ? -38.580 43.370 24.775 1.00 61.19 ? 45 ILE B O 1 ATOM 2883 C CB . ILE B 2 45 ? -36.724 43.946 22.143 1.00 59.60 ? 45 ILE B CB 1 ATOM 2884 C CG1 . ILE B 2 45 ? -35.609 43.238 21.372 1.00 58.92 ? 45 ILE B CG1 1 ATOM 2885 C CG2 . ILE B 2 45 ? -36.129 44.629 23.364 1.00 61.94 ? 45 ILE B CG2 1 ATOM 2886 C CD1 . ILE B 2 45 ? -34.834 44.155 20.450 1.00 61.37 ? 45 ILE B CD1 1 ATOM 2887 N N . ASP B 2 46 ? -39.791 44.241 23.093 1.00 59.29 ? 46 ASP B N 1 ATOM 2888 C CA . ASP B 2 46 ? -40.788 44.831 23.984 1.00 60.43 ? 46 ASP B CA 1 ATOM 2889 C C . ASP B 2 46 ? -41.619 43.757 24.665 1.00 56.46 ? 46 ASP B C 1 ATOM 2890 O O . ASP B 2 46 ? -41.810 43.784 25.878 1.00 57.11 ? 46 ASP B O 1 ATOM 2891 C CB . ASP B 2 46 ? -41.677 45.797 23.212 1.00 62.99 ? 46 ASP B CB 1 ATOM 2892 C CG . ASP B 2 46 ? -40.894 46.944 22.641 1.00 68.04 ? 46 ASP B CG 1 ATOM 2893 O OD1 . ASP B 2 46 ? -39.669 46.968 22.869 1.00 70.10 ? 46 ASP B OD1 1 ATOM 2894 O OD2 . ASP B 2 46 ? -41.480 47.817 21.972 1.00 72.92 ? 46 ASP B OD2 1 ATOM 2895 N N . GLY B 2 47 ? -42.090 42.795 23.890 1.00 52.17 ? 47 GLY B N 1 ATOM 2896 C CA . GLY B 2 47 ? -42.869 41.705 24.453 1.00 50.69 ? 47 GLY B CA 1 ATOM 2897 C C . GLY B 2 47 ? -42.162 41.006 25.602 1.00 50.38 ? 47 GLY B C 1 ATOM 2898 O O . GLY B 2 47 ? -42.733 40.813 26.679 1.00 51.15 ? 47 GLY B O 1 ATOM 2899 N N . VAL B 2 48 ? -40.901 40.650 25.376 1.00 49.38 ? 48 VAL B N 1 ATOM 2900 C CA . VAL B 2 48 ? -40.149 39.852 26.328 1.00 48.27 ? 48 VAL B CA 1 ATOM 2901 C C . VAL B 2 48 ? -39.724 40.678 27.543 1.00 50.69 ? 48 VAL B C 1 ATOM 2902 O O . VAL B 2 48 ? -39.744 40.179 28.673 1.00 50.95 ? 48 VAL B O 1 ATOM 2903 C CB . VAL B 2 48 ? -38.951 39.214 25.624 1.00 48.25 ? 48 VAL B CB 1 ATOM 2904 C CG1 . VAL B 2 48 ? -37.895 38.750 26.617 1.00 50.19 ? 48 VAL B CG1 1 ATOM 2905 C CG2 . VAL B 2 48 ? -39.439 38.077 24.731 1.00 45.83 ? 48 VAL B CG2 1 ATOM 2906 N N . THR B 2 49 ? -39.358 41.935 27.320 1.00 51.55 ? 49 THR B N 1 ATOM 2907 C CA . THR B 2 49 ? -39.017 42.807 28.424 1.00 55.70 ? 49 THR B CA 1 ATOM 2908 C C . THR B 2 49 ? -40.206 42.894 29.375 1.00 57.26 ? 49 THR B C 1 ATOM 2909 O O . THR B 2 49 ? -40.076 42.601 30.568 1.00 59.38 ? 49 THR B O 1 ATOM 2910 C CB . THR B 2 49 ? -38.611 44.221 27.955 1.00 57.71 ? 49 THR B CB 1 ATOM 2911 O OG1 . THR B 2 49 ? -37.471 44.135 27.096 1.00 57.08 ? 49 THR B OG1 1 ATOM 2912 C CG2 . THR B 2 49 ? -38.268 45.085 29.121 1.00 60.84 ? 49 THR B CG2 1 ATOM 2913 N N . ASN B 2 50 ? -41.365 43.278 28.839 1.00 57.37 ? 50 ASN B N 1 ATOM 2914 C CA . ASN B 2 50 ? -42.579 43.411 29.651 1.00 57.97 ? 50 ASN B CA 1 ATOM 2915 C C . ASN B 2 50 ? -42.865 42.142 30.438 1.00 55.38 ? 50 ASN B C 1 ATOM 2916 O O . ASN B 2 50 ? -43.189 42.190 31.616 1.00 56.30 ? 50 ASN B O 1 ATOM 2917 C CB . ASN B 2 50 ? -43.778 43.768 28.775 1.00 57.43 ? 50 ASN B CB 1 ATOM 2918 C CG . ASN B 2 50 ? -43.762 45.224 28.326 1.00 60.92 ? 50 ASN B CG 1 ATOM 2919 O OD1 . ASN B 2 50 ? -43.508 46.122 29.112 1.00 64.17 ? 50 ASN B OD1 1 ATOM 2920 N ND2 . ASN B 2 50 ? -44.039 45.456 27.056 1.00 61.20 ? 50 ASN B ND2 1 ATOM 2921 N N . LYS B 2 51 ? -42.717 41.014 29.766 1.00 52.95 ? 51 LYS B N 1 ATOM 2922 C CA . LYS B 2 51 ? -42.871 39.691 30.372 1.00 51.73 ? 51 LYS B CA 1 ATOM 2923 C C . LYS B 2 51 ? -41.984 39.508 31.606 1.00 53.40 ? 51 LYS B C 1 ATOM 2924 O O . LYS B 2 51 ? -42.460 39.173 32.689 1.00 53.51 ? 51 LYS B O 1 ATOM 2925 C CB . LYS B 2 51 ? -42.502 38.658 29.322 1.00 49.82 ? 51 LYS B CB 1 ATOM 2926 C CG . LYS B 2 51 ? -42.855 37.228 29.647 1.00 49.72 ? 51 LYS B CG 1 ATOM 2927 C CD . LYS B 2 51 ? -42.327 36.331 28.535 1.00 49.41 ? 51 LYS B CD 1 ATOM 2928 C CE . LYS B 2 51 ? -43.044 35.011 28.469 1.00 48.52 ? 51 LYS B CE 1 ATOM 2929 N NZ . LYS B 2 51 ? -43.817 34.821 27.222 1.00 48.54 ? 51 LYS B NZ 1 ATOM 2930 N N . VAL B 2 52 ? -40.690 39.745 31.430 1.00 54.19 ? 52 VAL B N 1 ATOM 2931 C CA . VAL B 2 52 ? -39.732 39.609 32.506 1.00 56.26 ? 52 VAL B CA 1 ATOM 2932 C C . VAL B 2 52 ? -40.116 40.537 33.661 1.00 59.48 ? 52 VAL B C 1 ATOM 2933 O O . VAL B 2 52 ? -40.157 40.107 34.817 1.00 60.80 ? 52 VAL B O 1 ATOM 2934 C CB . VAL B 2 52 ? -38.303 39.891 31.992 1.00 58.12 ? 52 VAL B CB 1 ATOM 2935 C CG1 . VAL B 2 52 ? -37.307 40.052 33.134 1.00 61.63 ? 52 VAL B CG1 1 ATOM 2936 C CG2 . VAL B 2 52 ? -37.859 38.775 31.058 1.00 55.95 ? 52 VAL B CG2 1 ATOM 2937 N N . ASN B 2 53 ? -40.425 41.795 33.351 1.00 61.36 ? 53 ASN B N 1 ATOM 2938 C CA . ASN B 2 53 ? -40.877 42.741 34.381 1.00 64.87 ? 53 ASN B CA 1 ATOM 2939 C C . ASN B 2 53 ? -42.202 42.316 35.015 1.00 63.08 ? 53 ASN B C 1 ATOM 2940 O O . ASN B 2 53 ? -42.361 42.397 36.224 1.00 65.19 ? 53 ASN B O 1 ATOM 2941 C CB . ASN B 2 53 ? -41.003 44.157 33.815 1.00 67.55 ? 53 ASN B CB 1 ATOM 2942 C CG . ASN B 2 53 ? -39.672 44.729 33.353 1.00 70.69 ? 53 ASN B CG 1 ATOM 2943 O OD1 . ASN B 2 53 ? -38.628 44.441 33.925 1.00 73.51 ? 53 ASN B OD1 1 ATOM 2944 N ND2 . ASN B 2 53 ? -39.709 45.558 32.321 1.00 72.01 ? 53 ASN B ND2 1 ATOM 2945 N N . SER B 2 54 ? -43.144 41.857 34.200 1.00 60.34 ? 54 SER B N 1 ATOM 2946 C CA . SER B 2 54 ? -44.433 41.374 34.711 1.00 60.74 ? 54 SER B CA 1 ATOM 2947 C C . SER B 2 54 ? -44.246 40.239 35.702 1.00 60.94 ? 54 SER B C 1 ATOM 2948 O O . SER B 2 54 ? -44.888 40.215 36.746 1.00 61.63 ? 54 SER B O 1 ATOM 2949 C CB . SER B 2 54 ? -45.360 40.909 33.575 1.00 57.94 ? 54 SER B CB 1 ATOM 2950 O OG . SER B 2 54 ? -46.031 42.016 32.996 1.00 59.63 ? 54 SER B OG 1 ATOM 2951 N N . ILE B 2 55 ? -43.357 39.311 35.358 1.00 61.17 ? 55 ILE B N 1 ATOM 2952 C CA . ILE B 2 55 ? -43.006 38.186 36.225 1.00 62.30 ? 55 ILE B CA 1 ATOM 2953 C C . ILE B 2 55 ? -42.342 38.648 37.519 1.00 66.82 ? 55 ILE B C 1 ATOM 2954 O O . ILE B 2 55 ? -42.726 38.225 38.611 1.00 68.34 ? 55 ILE B O 1 ATOM 2955 C CB . ILE B 2 55 ? -42.068 37.212 35.496 1.00 61.25 ? 55 ILE B CB 1 ATOM 2956 C CG1 . ILE B 2 55 ? -42.857 36.443 34.445 1.00 58.23 ? 55 ILE B CG1 1 ATOM 2957 C CG2 . ILE B 2 55 ? -41.429 36.229 36.469 1.00 63.80 ? 55 ILE B CG2 1 ATOM 2958 C CD1 . ILE B 2 55 ? -41.991 35.729 33.441 1.00 57.34 ? 55 ILE B CD1 1 ATOM 2959 N N . ILE B 2 56 ? -41.343 39.509 37.395 1.00 69.38 ? 56 ILE B N 1 ATOM 2960 C CA . ILE B 2 56 ? -40.668 40.044 38.567 1.00 73.82 ? 56 ILE B CA 1 ATOM 2961 C C . ILE B 2 56 ? -41.665 40.737 39.506 1.00 76.88 ? 56 ILE B C 1 ATOM 2962 O O . ILE B 2 56 ? -41.612 40.531 40.718 1.00 79.79 ? 56 ILE B O 1 ATOM 2963 C CB . ILE B 2 56 ? -39.518 40.988 38.153 1.00 76.53 ? 56 ILE B CB 1 ATOM 2964 C CG1 . ILE B 2 56 ? -38.375 40.165 37.555 1.00 75.67 ? 56 ILE B CG1 1 ATOM 2965 C CG2 . ILE B 2 56 ? -39.004 41.796 39.337 1.00 81.68 ? 56 ILE B CG2 1 ATOM 2966 C CD1 . ILE B 2 56 ? -37.294 40.986 36.895 1.00 77.83 ? 56 ILE B CD1 1 ATOM 2967 N N . ASP B 2 57 ? -42.589 41.528 38.960 1.00 77.78 ? 57 ASP B N 1 ATOM 2968 C CA . ASP B 2 57 ? -43.506 42.312 39.808 1.00 81.64 ? 57 ASP B CA 1 ATOM 2969 C C . ASP B 2 57 ? -44.584 41.467 40.488 1.00 80.53 ? 57 ASP B C 1 ATOM 2970 O O . ASP B 2 57 ? -44.874 41.662 41.660 1.00 81.95 ? 57 ASP B O 1 ATOM 2971 C CB . ASP B 2 57 ? -44.120 43.479 39.025 1.00 82.15 ? 57 ASP B CB 1 ATOM 2972 C CG . ASP B 2 57 ? -43.130 44.629 38.838 1.00 87.69 ? 57 ASP B CG 1 ATOM 2973 O OD1 . ASP B 2 57 ? -42.643 45.156 39.869 1.00 93.00 ? 57 ASP B OD1 1 ATOM 2974 O OD2 . ASP B 2 57 ? -42.827 45.000 37.674 1.00 86.60 ? 57 ASP B OD2 1 ATOM 2975 N N . LYS B 2 58 ? -45.156 40.507 39.773 1.00 77.77 ? 58 LYS B N 1 ATOM 2976 C CA . LYS B 2 58 ? -46.152 39.619 40.384 1.00 77.98 ? 58 LYS B CA 1 ATOM 2977 C C . LYS B 2 58 ? -45.598 38.868 41.592 1.00 80.92 ? 58 LYS B C 1 ATOM 2978 O O . LYS B 2 58 ? -46.308 38.662 42.578 1.00 83.16 ? 58 LYS B O 1 ATOM 2979 C CB . LYS B 2 58 ? -46.753 38.658 39.339 1.00 74.10 ? 58 LYS B CB 1 ATOM 2980 C CG . LYS B 2 58 ? -48.140 39.055 38.828 1.00 73.94 ? 58 LYS B CG 1 ATOM 2981 C CD . LYS B 2 58 ? -48.529 40.481 39.226 1.00 78.14 ? 58 LYS B CD 1 ATOM 2982 C CE . LYS B 2 58 ? -49.620 41.065 38.350 1.00 77.96 ? 58 LYS B CE 1 ATOM 2983 N NZ . LYS B 2 58 ? -50.015 42.419 38.821 1.00 80.70 ? 58 LYS B NZ 1 ATOM 2984 N N . MET B 2 59 ? -44.321 38.507 41.527 1.00 82.45 ? 59 MET B N 1 ATOM 2985 C CA . MET B 2 59 ? -43.645 37.815 42.624 1.00 85.55 ? 59 MET B CA 1 ATOM 2986 C C . MET B 2 59 ? -43.224 38.770 43.752 1.00 90.86 ? 59 MET B C 1 ATOM 2987 O O . MET B 2 59 ? -42.989 38.325 44.878 1.00 92.69 ? 59 MET B O 1 ATOM 2988 C CB . MET B 2 59 ? -42.421 37.073 42.092 1.00 84.66 ? 59 MET B CB 1 ATOM 2989 C CG . MET B 2 59 ? -42.724 36.096 40.964 1.00 80.53 ? 59 MET B CG 1 ATOM 2990 S SD . MET B 2 59 ? -43.701 34.646 41.405 1.00 79.88 ? 59 MET B SD 1 ATOM 2991 C CE . MET B 2 59 ? -43.155 34.236 43.055 1.00 83.75 ? 59 MET B CE 1 ATOM 2992 N N . ASN B 2 60 ? -43.124 40.064 43.434 1.00 93.71 ? 60 ASN B N 1 ATOM 2993 C CA . ASN B 2 60 ? -42.821 41.142 44.404 1.00 99.60 ? 60 ASN B CA 1 ATOM 2994 C C . ASN B 2 60 ? -43.413 40.959 45.806 1.00 101.47 ? 60 ASN B C 1 ATOM 2995 O O . ASN B 2 60 ? -42.677 40.921 46.792 1.00 103.60 ? 60 ASN B O 1 ATOM 2996 C CB . ASN B 2 60 ? -43.292 42.487 43.832 1.00 101.12 ? 60 ASN B CB 1 ATOM 2997 C CG . ASN B 2 60 ? -43.014 43.655 44.753 1.00 107.85 ? 60 ASN B CG 1 ATOM 2998 O OD1 . ASN B 2 60 ? -43.776 43.926 45.683 1.00 110.26 ? 60 ASN B OD1 1 ATOM 2999 N ND2 . ASN B 2 60 ? -41.937 44.379 44.478 1.00 111.48 ? 60 ASN B ND2 1 ATOM 3000 N N . THR B 2 61 ? -44.739 40.882 45.893 1.00 102.24 ? 61 THR B N 1 ATOM 3001 C CA . THR B 2 61 ? -45.410 40.657 47.171 1.00 99.05 ? 61 THR B CA 1 ATOM 3002 C C . THR B 2 61 ? -45.564 39.157 47.353 1.00 93.41 ? 61 THR B C 1 ATOM 3003 O O . THR B 2 61 ? -46.351 38.515 46.660 1.00 94.04 ? 61 THR B O 1 ATOM 3004 C CB . THR B 2 61 ? -46.797 41.333 47.254 1.00 101.82 ? 61 THR B CB 1 ATOM 3005 O OG1 . THR B 2 61 ? -46.745 42.648 46.682 1.00 107.60 ? 61 THR B OG1 1 ATOM 3006 C CG2 . THR B 2 61 ? -47.252 41.431 48.710 1.00 100.73 ? 61 THR B CG2 1 ATOM 3007 N N . GLN B 2 62 ? -44.795 38.610 48.284 1.00 90.09 ? 62 GLN B N 1 ATOM 3008 C CA . GLN B 2 62 ? -44.742 37.172 48.516 1.00 86.23 ? 62 GLN B CA 1 ATOM 3009 C C . GLN B 2 62 ? -44.360 36.922 49.978 1.00 84.65 ? 62 GLN B C 1 ATOM 3010 O O . GLN B 2 62 ? -43.763 37.790 50.626 1.00 90.69 ? 62 GLN B O 1 ATOM 3011 C CB . GLN B 2 62 ? -43.741 36.529 47.544 1.00 86.92 ? 62 GLN B CB 1 ATOM 3012 C CG . GLN B 2 62 ? -42.969 35.331 48.087 1.00 84.48 ? 62 GLN B CG 1 ATOM 3013 C CD . GLN B 2 62 ? -42.041 34.704 47.063 1.00 87.13 ? 62 GLN B CD 1 ATOM 3014 O OE1 . GLN B 2 62 ? -42.062 35.057 45.880 1.00 88.88 ? 62 GLN B OE1 1 ATOM 3015 N NE2 . GLN B 2 62 ? -41.216 33.763 47.517 1.00 87.35 ? 62 GLN B NE2 1 ATOM 3016 N N . PHE B 2 63 ? -44.698 35.743 50.491 1.00 78.82 ? 63 PHE B N 1 ATOM 3017 C CA . PHE B 2 63 ? -44.498 35.428 51.906 1.00 75.63 ? 63 PHE B CA 1 ATOM 3018 C C . PHE B 2 63 ? -43.061 35.674 52.403 1.00 77.78 ? 63 PHE B C 1 ATOM 3019 O O . PHE B 2 63 ? -42.087 35.442 51.677 1.00 81.21 ? 63 PHE B O 1 ATOM 3020 C CB . PHE B 2 63 ? -44.912 33.982 52.209 1.00 70.76 ? 63 PHE B CB 1 ATOM 3021 C CG . PHE B 2 63 ? -44.872 33.649 53.672 1.00 67.56 ? 63 PHE B CG 1 ATOM 3022 C CD1 . PHE B 2 63 ? -45.866 34.114 54.531 1.00 64.98 ? 63 PHE B CD1 1 ATOM 3023 C CD2 . PHE B 2 63 ? -43.825 32.899 54.202 1.00 66.78 ? 63 PHE B CD2 1 ATOM 3024 C CE1 . PHE B 2 63 ? -45.823 33.828 55.882 1.00 62.31 ? 63 PHE B CE1 1 ATOM 3025 C CE2 . PHE B 2 63 ? -43.782 32.604 55.557 1.00 64.09 ? 63 PHE B CE2 1 ATOM 3026 C CZ . PHE B 2 63 ? -44.776 33.076 56.394 1.00 61.94 ? 63 PHE B CZ 1 ATOM 3027 N N . GLU B 2 64 ? -42.962 36.166 53.641 1.00 76.95 ? 64 GLU B N 1 ATOM 3028 C CA . GLU B 2 64 ? -41.689 36.455 54.307 1.00 78.20 ? 64 GLU B CA 1 ATOM 3029 C C . GLU B 2 64 ? -41.734 35.829 55.697 1.00 75.08 ? 64 GLU B C 1 ATOM 3030 O O . GLU B 2 64 ? -42.685 36.053 56.464 1.00 71.48 ? 64 GLU B O 1 ATOM 3031 C CB . GLU B 2 64 ? -41.457 37.967 54.430 1.00 82.00 ? 64 GLU B CB 1 ATOM 3032 C CG . GLU B 2 64 ? -41.528 38.719 53.106 1.00 85.82 ? 64 GLU B CG 1 ATOM 3033 C CD . GLU B 2 64 ? -41.244 40.212 53.243 1.00 91.81 ? 64 GLU B CD 1 ATOM 3034 O OE1 . GLU B 2 64 ? -40.793 40.648 54.324 1.00 93.82 ? 64 GLU B OE1 1 ATOM 3035 O OE2 . GLU B 2 64 ? -41.476 40.956 52.264 1.00 93.06 ? 64 GLU B OE2 1 ATOM 3036 N N . ALA B 2 65 ? -40.715 35.040 56.019 1.00 74.79 ? 65 ALA B N 1 ATOM 3037 C CA . ALA B 2 65 ? -40.665 34.361 57.310 1.00 72.86 ? 65 ALA B CA 1 ATOM 3038 C C . ALA B 2 65 ? -40.050 35.268 58.377 1.00 75.86 ? 65 ALA B C 1 ATOM 3039 O O . ALA B 2 65 ? -39.199 36.111 58.074 1.00 79.51 ? 65 ALA B O 1 ATOM 3040 C CB . ALA B 2 65 ? -39.897 33.048 57.200 1.00 72.82 ? 65 ALA B CB 1 ATOM 3041 N N . VAL B 2 66 ? -40.518 35.095 59.614 1.00 73.77 ? 66 VAL B N 1 ATOM 3042 C CA . VAL B 2 66 ? -40.006 35.814 60.778 1.00 77.25 ? 66 VAL B CA 1 ATOM 3043 C C . VAL B 2 66 ? -39.567 34.788 61.810 1.00 76.68 ? 66 VAL B C 1 ATOM 3044 O O . VAL B 2 66 ? -40.129 33.694 61.877 1.00 73.53 ? 66 VAL B O 1 ATOM 3045 C CB . VAL B 2 66 ? -41.085 36.714 61.415 1.00 76.60 ? 66 VAL B CB 1 ATOM 3046 C CG1 . VAL B 2 66 ? -40.513 37.522 62.579 1.00 82.10 ? 66 VAL B CG1 1 ATOM 3047 C CG2 . VAL B 2 66 ? -41.700 37.627 60.365 1.00 78.35 ? 66 VAL B CG2 1 ATOM 3048 N N . GLY B 2 67 ? -38.567 35.148 62.611 1.00 81.41 ? 67 GLY B N 1 ATOM 3049 C CA . GLY B 2 67 ? -38.125 34.314 63.723 1.00 80.25 ? 67 GLY B CA 1 ATOM 3050 C C . GLY B 2 67 ? -39.091 34.404 64.891 1.00 75.77 ? 67 GLY B C 1 ATOM 3051 O O . GLY B 2 67 ? -39.406 35.495 65.373 1.00 77.33 ? 67 GLY B O 1 ATOM 3052 N N . ARG B 2 68 ? -39.583 33.252 65.325 1.00 70.33 ? 68 ARG B N 1 ATOM 3053 C CA . ARG B 2 68 ? -40.474 33.177 66.473 1.00 67.63 ? 68 ARG B CA 1 ATOM 3054 C C . ARG B 2 68 ? -40.018 31.990 67.293 1.00 66.14 ? 68 ARG B C 1 ATOM 3055 O O . ARG B 2 68 ? -39.650 30.956 66.749 1.00 64.59 ? 68 ARG B O 1 ATOM 3056 C CB . ARG B 2 68 ? -41.941 33.050 66.031 1.00 63.65 ? 68 ARG B CB 1 ATOM 3057 C CG . ARG B 2 68 ? -42.548 34.369 65.541 1.00 65.97 ? 68 ARG B CG 1 ATOM 3058 C CD . ARG B 2 68 ? -44.041 34.284 65.226 1.00 62.96 ? 68 ARG B CD 1 ATOM 3059 N NE . ARG B 2 68 ? -44.296 33.387 64.106 1.00 60.13 ? 68 ARG B NE 1 ATOM 3060 C CZ . ARG B 2 68 ? -44.145 33.697 62.820 1.00 60.46 ? 68 ARG B CZ 1 ATOM 3061 N NH1 . ARG B 2 68 ? -43.768 34.901 62.443 1.00 64.41 ? 68 ARG B NH1 1 ATOM 3062 N NH2 . ARG B 2 68 ? -44.369 32.781 61.891 1.00 59.83 ? 68 ARG B NH2 1 ATOM 3063 N N . GLU B 2 69 ? -40.000 32.150 68.607 1.00 68.20 ? 69 GLU B N 1 ATOM 3064 C CA . GLU B 2 69 ? -39.379 31.161 69.474 1.00 68.73 ? 69 GLU B CA 1 ATOM 3065 C C . GLU B 2 69 ? -40.382 30.620 70.455 1.00 63.96 ? 69 GLU B C 1 ATOM 3066 O O . GLU B 2 69 ? -41.272 31.338 70.896 1.00 63.64 ? 69 GLU B O 1 ATOM 3067 C CB . GLU B 2 69 ? -38.207 31.781 70.220 1.00 76.05 ? 69 GLU B CB 1 ATOM 3068 C CG . GLU B 2 69 ? -37.014 32.087 69.332 1.00 81.75 ? 69 GLU B CG 1 ATOM 3069 C CD . GLU B 2 69 ? -35.735 31.538 69.910 1.00 88.99 ? 69 GLU B CD 1 ATOM 3070 O OE1 . GLU B 2 69 ? -35.786 30.425 70.483 1.00 89.40 ? 69 GLU B OE1 1 ATOM 3071 O OE2 . GLU B 2 69 ? -34.688 32.212 69.800 1.00 95.96 ? 69 GLU B OE2 1 ATOM 3072 N N . PHE B 2 70 ? -40.217 29.355 70.805 1.00 62.14 ? 70 PHE B N 1 ATOM 3073 C CA . PHE B 2 70 ? -41.181 28.645 71.626 1.00 59.65 ? 70 PHE B CA 1 ATOM 3074 C C . PHE B 2 70 ? -40.483 27.765 72.646 1.00 60.55 ? 70 PHE B C 1 ATOM 3075 O O . PHE B 2 70 ? -39.531 27.081 72.311 1.00 60.91 ? 70 PHE B O 1 ATOM 3076 C CB . PHE B 2 70 ? -42.059 27.788 70.722 1.00 57.09 ? 70 PHE B CB 1 ATOM 3077 C CG . PHE B 2 70 ? -42.709 28.561 69.609 1.00 56.37 ? 70 PHE B CG 1 ATOM 3078 C CD1 . PHE B 2 70 ? -43.930 29.204 69.810 1.00 54.96 ? 70 PHE B CD1 1 ATOM 3079 C CD2 . PHE B 2 70 ? -42.096 28.660 68.363 1.00 57.23 ? 70 PHE B CD2 1 ATOM 3080 C CE1 . PHE B 2 70 ? -44.529 29.925 68.789 1.00 54.34 ? 70 PHE B CE1 1 ATOM 3081 C CE2 . PHE B 2 70 ? -42.693 29.378 67.337 1.00 56.17 ? 70 PHE B CE2 1 ATOM 3082 C CZ . PHE B 2 70 ? -43.909 30.016 67.554 1.00 55.02 ? 70 PHE B CZ 1 ATOM 3083 N N . ASN B 2 71 ? -40.965 27.767 73.887 1.00 61.11 ? 71 ASN B N 1 ATOM 3084 C CA . ASN B 2 71 ? -40.319 26.979 74.950 1.00 64.38 ? 71 ASN B CA 1 ATOM 3085 C C . ASN B 2 71 ? -40.593 25.475 74.804 1.00 62.25 ? 71 ASN B C 1 ATOM 3086 O O . ASN B 2 71 ? -41.188 25.044 73.820 1.00 60.86 ? 71 ASN B O 1 ATOM 3087 C CB . ASN B 2 71 ? -40.675 27.519 76.360 1.00 65.82 ? 71 ASN B CB 1 ATOM 3088 C CG . ASN B 2 71 ? -42.078 27.144 76.819 1.00 62.72 ? 71 ASN B CG 1 ATOM 3089 O OD1 . ASN B 2 71 ? -42.549 26.032 76.597 1.00 61.16 ? 71 ASN B OD1 1 ATOM 3090 N ND2 . ASN B 2 71 ? -42.746 28.078 77.483 1.00 64.00 ? 71 ASN B ND2 1 ATOM 3091 N N . ASN B 2 72 ? -40.181 24.687 75.793 1.00 65.04 ? 72 ASN B N 1 ATOM 3092 C CA . ASN B 2 72 ? -40.252 23.230 75.689 1.00 65.80 ? 72 ASN B CA 1 ATOM 3093 C C . ASN B 2 72 ? -41.656 22.611 75.777 1.00 61.40 ? 72 ASN B C 1 ATOM 3094 O O . ASN B 2 72 ? -41.842 21.462 75.385 1.00 60.53 ? 72 ASN B O 1 ATOM 3095 C CB . ASN B 2 72 ? -39.348 22.583 76.739 1.00 71.72 ? 72 ASN B CB 1 ATOM 3096 C CG . ASN B 2 72 ? -38.949 21.165 76.364 1.00 76.36 ? 72 ASN B CG 1 ATOM 3097 O OD1 . ASN B 2 72 ? -38.518 20.907 75.235 1.00 78.43 ? 72 ASN B OD1 1 ATOM 3098 N ND2 . ASN B 2 72 ? -39.095 20.234 77.307 1.00 79.07 ? 72 ASN B ND2 1 ATOM 3099 N N . LEU B 2 73 ? -42.627 23.358 76.301 1.00 59.06 ? 73 LEU B N 1 ATOM 3100 C CA . LEU B 2 73 ? -44.009 22.889 76.385 1.00 56.72 ? 73 LEU B CA 1 ATOM 3101 C C . LEU B 2 73 ? -44.920 23.728 75.502 1.00 53.70 ? 73 LEU B C 1 ATOM 3102 O O . LEU B 2 73 ? -46.078 23.981 75.839 1.00 51.59 ? 73 LEU B O 1 ATOM 3103 C CB . LEU B 2 73 ? -44.485 22.923 77.829 1.00 58.71 ? 73 LEU B CB 1 ATOM 3104 C CG . LEU B 2 73 ? -43.792 21.909 78.747 1.00 62.15 ? 73 LEU B CG 1 ATOM 3105 C CD1 . LEU B 2 73 ? -44.115 22.212 80.202 1.00 63.50 ? 73 LEU B CD1 1 ATOM 3106 C CD2 . LEU B 2 73 ? -44.197 20.485 78.390 1.00 62.05 ? 73 LEU B CD2 1 ATOM 3107 N N . GLU B 2 74 ? -44.373 24.157 74.365 1.00 52.76 ? 74 GLU B N 1 ATOM 3108 C CA . GLU B 2 74 ? -45.151 24.777 73.298 1.00 50.33 ? 74 GLU B CA 1 ATOM 3109 C C . GLU B 2 74 ? -44.785 24.122 71.956 1.00 49.83 ? 74 GLU B C 1 ATOM 3110 O O . GLU B 2 74 ? -44.598 24.816 70.942 1.00 47.75 ? 74 GLU B O 1 ATOM 3111 C CB . GLU B 2 74 ? -44.865 26.271 73.249 1.00 49.71 ? 74 GLU B CB 1 ATOM 3112 C CG . GLU B 2 74 ? -45.179 27.014 74.528 1.00 49.51 ? 74 GLU B CG 1 ATOM 3113 C CD . GLU B 2 74 ? -44.832 28.479 74.411 1.00 51.51 ? 74 GLU B CD 1 ATOM 3114 O OE1 . GLU B 2 74 ? -43.727 28.784 73.922 1.00 52.42 ? 74 GLU B OE1 1 ATOM 3115 O OE2 . GLU B 2 74 ? -45.665 29.331 74.785 1.00 52.54 ? 74 GLU B OE2 1 ATOM 3116 N N . ARG B 2 75 ? -44.682 22.789 71.964 1.00 48.48 ? 75 ARG B N 1 ATOM 3117 C CA . ARG B 2 75 ? -44.246 22.050 70.789 1.00 50.70 ? 75 ARG B CA 1 ATOM 3118 C C . ARG B 2 75 ? -45.296 22.056 69.697 1.00 48.78 ? 75 ARG B C 1 ATOM 3119 O O . ARG B 2 75 ? -44.962 22.063 68.509 1.00 50.57 ? 75 ARG B O 1 ATOM 3120 C CB . ARG B 2 75 ? -43.874 20.596 71.134 1.00 55.15 ? 75 ARG B CB 1 ATOM 3121 C CG . ARG B 2 75 ? -42.612 20.420 71.968 1.00 59.27 ? 75 ARG B CG 1 ATOM 3122 C CD . ARG B 2 75 ? -41.436 21.200 71.405 1.00 62.62 ? 75 ARG B CD 1 ATOM 3123 N NE . ARG B 2 75 ? -40.171 20.874 72.063 1.00 71.21 ? 75 ARG B NE 1 ATOM 3124 C CZ . ARG B 2 75 ? -39.005 21.467 71.792 1.00 76.58 ? 75 ARG B CZ 1 ATOM 3125 N NH1 . ARG B 2 75 ? -38.933 22.421 70.859 1.00 76.62 ? 75 ARG B NH1 1 ATOM 3126 N NH2 . ARG B 2 75 ? -37.906 21.110 72.454 1.00 81.23 ? 75 ARG B NH2 1 ATOM 3127 N N . ARG B 2 76 ? -46.564 22.026 70.086 1.00 46.92 ? 76 ARG B N 1 ATOM 3128 C CA . ARG B 2 76 ? -47.633 22.067 69.102 1.00 46.31 ? 76 ARG B CA 1 ATOM 3129 C C . ARG B 2 76 ? -47.557 23.354 68.277 1.00 44.91 ? 76 ARG B C 1 ATOM 3130 O O . ARG B 2 76 ? -47.557 23.298 67.051 1.00 46.33 ? 76 ARG B O 1 ATOM 3131 C CB . ARG B 2 76 ? -49.001 21.946 69.771 1.00 45.55 ? 76 ARG B CB 1 ATOM 3132 C CG . ARG B 2 76 ? -49.294 20.578 70.344 1.00 47.06 ? 76 ARG B CG 1 ATOM 3133 C CD . ARG B 2 76 ? -50.562 20.635 71.165 1.00 47.36 ? 76 ARG B CD 1 ATOM 3134 N NE . ARG B 2 76 ? -50.385 21.479 72.348 1.00 45.14 ? 76 ARG B NE 1 ATOM 3135 C CZ . ARG B 2 76 ? -51.349 22.157 72.970 1.00 44.48 ? 76 ARG B CZ 1 ATOM 3136 N NH1 . ARG B 2 76 ? -52.605 22.119 72.542 1.00 47.81 ? 76 ARG B NH1 1 ATOM 3137 N NH2 . ARG B 2 76 ? -51.052 22.886 74.033 1.00 42.35 ? 76 ARG B NH2 1 ATOM 3138 N N . ILE B 2 77 ? -47.486 24.507 68.935 1.00 44.13 ? 77 ILE B N 1 ATOM 3139 C CA . ILE B 2 77 ? -47.461 25.760 68.185 1.00 44.36 ? 77 ILE B CA 1 ATOM 3140 C C . ILE B 2 77 ? -46.126 25.961 67.469 1.00 45.35 ? 77 ILE B C 1 ATOM 3141 O O . ILE B 2 77 ? -46.099 26.487 66.355 1.00 45.42 ? 77 ILE B O 1 ATOM 3142 C CB . ILE B 2 77 ? -47.907 26.991 68.998 1.00 43.79 ? 77 ILE B CB 1 ATOM 3143 C CG1 . ILE B 2 77 ? -46.973 27.281 70.154 1.00 45.88 ? 77 ILE B CG1 1 ATOM 3144 C CG2 . ILE B 2 77 ? -49.310 26.777 69.532 1.00 45.42 ? 77 ILE B CG2 1 ATOM 3145 C CD1 . ILE B 2 77 ? -47.343 28.551 70.906 1.00 47.92 ? 77 ILE B CD1 1 ATOM 3146 N N . GLU B 2 78 ? -45.030 25.506 68.064 1.00 47.43 ? 78 GLU B N 1 ATOM 3147 C CA . GLU B 2 78 ? -43.749 25.538 67.359 1.00 49.04 ? 78 GLU B CA 1 ATOM 3148 C C . GLU B 2 78 ? -43.921 24.800 66.043 1.00 47.40 ? 78 GLU B C 1 ATOM 3149 O O . GLU B 2 78 ? -43.524 25.286 64.989 1.00 46.91 ? 78 GLU B O 1 ATOM 3150 C CB . GLU B 2 78 ? -42.626 24.910 68.188 1.00 53.98 ? 78 GLU B CB 1 ATOM 3151 C CG . GLU B 2 78 ? -41.268 24.914 67.503 1.00 60.78 ? 78 GLU B CG 1 ATOM 3152 C CD . GLU B 2 78 ? -40.124 24.652 68.474 1.00 70.21 ? 78 GLU B CD 1 ATOM 3153 O OE1 . GLU B 2 78 ? -40.061 23.529 69.036 1.00 73.77 ? 78 GLU B OE1 1 ATOM 3154 O OE2 . GLU B 2 78 ? -39.283 25.569 68.677 1.00 74.46 ? 78 GLU B OE2 1 ATOM 3155 N N . ASN B 2 79 ? -44.539 23.632 66.110 1.00 47.29 ? 79 ASN B N 1 ATOM 3156 C CA . ASN B 2 79 ? -44.717 22.810 64.933 1.00 50.19 ? 79 ASN B CA 1 ATOM 3157 C C . ASN B 2 79 ? -45.650 23.486 63.936 1.00 49.13 ? 79 ASN B C 1 ATOM 3158 O O . ASN B 2 79 ? -45.417 23.465 62.725 1.00 50.82 ? 79 ASN B O 1 ATOM 3159 C CB . ASN B 2 79 ? -45.273 21.449 65.336 1.00 52.78 ? 79 ASN B CB 1 ATOM 3160 C CG . ASN B 2 79 ? -45.506 20.547 64.148 1.00 56.39 ? 79 ASN B CG 1 ATOM 3161 O OD1 . ASN B 2 79 ? -44.719 19.659 63.873 1.00 60.41 ? 79 ASN B OD1 1 ATOM 3162 N ND2 . ASN B 2 79 ? -46.572 20.797 63.419 1.00 57.51 ? 79 ASN B ND2 1 ATOM 3163 N N . LEU B 2 80 ? -46.714 24.071 64.461 1.00 47.04 ? 80 LEU B N 1 ATOM 3164 C CA . LEU B 2 80 ? -47.693 24.761 63.652 1.00 47.55 ? 80 LEU B CA 1 ATOM 3165 C C . LEU B 2 80 ? -47.016 25.887 62.920 1.00 46.70 ? 80 LEU B C 1 ATOM 3166 O O . LEU B 2 80 ? -47.220 26.077 61.731 1.00 49.23 ? 80 LEU B O 1 ATOM 3167 C CB . LEU B 2 80 ? -48.804 25.315 64.544 1.00 47.61 ? 80 LEU B CB 1 ATOM 3168 C CG . LEU B 2 80 ? -49.978 26.016 63.874 1.00 49.49 ? 80 LEU B CG 1 ATOM 3169 C CD1 . LEU B 2 80 ? -51.076 26.292 64.896 1.00 50.80 ? 80 LEU B CD1 1 ATOM 3170 C CD2 . LEU B 2 80 ? -49.541 27.317 63.224 1.00 50.18 ? 80 LEU B CD2 1 ATOM 3171 N N . ASN B 2 81 ? -46.215 26.643 63.649 1.00 45.05 ? 81 ASN B N 1 ATOM 3172 C CA . ASN B 2 81 ? -45.489 27.755 63.080 1.00 45.24 ? 81 ASN B CA 1 ATOM 3173 C C . ASN B 2 81 ? -44.537 27.333 61.962 1.00 47.67 ? 81 ASN B C 1 ATOM 3174 O O . ASN B 2 81 ? -44.413 28.035 60.969 1.00 47.52 ? 81 ASN B O 1 ATOM 3175 C CB . ASN B 2 81 ? -44.693 28.442 64.174 1.00 46.17 ? 81 ASN B CB 1 ATOM 3176 C CG . ASN B 2 81 ? -43.837 29.547 63.637 1.00 49.01 ? 81 ASN B CG 1 ATOM 3177 O OD1 . ASN B 2 81 ? -44.336 30.608 63.283 1.00 50.27 ? 81 ASN B OD1 1 ATOM 3178 N ND2 . ASN B 2 81 ? -42.541 29.308 63.570 1.00 50.91 ? 81 ASN B ND2 1 ATOM 3179 N N . LYS B 2 82 ? -43.858 26.201 62.150 1.00 49.38 ? 82 LYS B N 1 ATOM 3180 C CA . LYS B 2 82 ? -42.915 25.664 61.182 1.00 53.01 ? 82 LYS B CA 1 ATOM 3181 C C . LYS B 2 82 ? -43.645 25.249 59.916 1.00 54.08 ? 82 LYS B C 1 ATOM 3182 O O . LYS B 2 82 ? -43.202 25.546 58.814 1.00 53.91 ? 82 LYS B O 1 ATOM 3183 C CB . LYS B 2 82 ? -42.196 24.441 61.774 1.00 57.65 ? 82 LYS B CB 1 ATOM 3184 C CG . LYS B 2 82 ? -40.946 23.971 61.024 1.00 63.64 ? 82 LYS B CG 1 ATOM 3185 C CD . LYS B 2 82 ? -40.936 22.453 60.866 1.00 69.74 ? 82 LYS B CD 1 ATOM 3186 C CE . LYS B 2 82 ? -39.539 21.848 60.681 1.00 77.63 ? 82 LYS B CE 1 ATOM 3187 N NZ . LYS B 2 82 ? -38.968 22.007 59.307 1.00 81.28 ? 82 LYS B NZ 1 ATOM 3188 N N . LYS B 2 83 ? -44.770 24.559 60.086 1.00 54.98 ? 83 LYS B N 1 ATOM 3189 C CA . LYS B 2 83 ? -45.567 24.089 58.950 1.00 57.53 ? 83 LYS B CA 1 ATOM 3190 C C . LYS B 2 83 ? -46.114 25.235 58.141 1.00 55.10 ? 83 LYS B C 1 ATOM 3191 O O . LYS B 2 83 ? -46.143 25.201 56.917 1.00 56.20 ? 83 LYS B O 1 ATOM 3192 C CB . LYS B 2 83 ? -46.727 23.219 59.432 1.00 60.52 ? 83 LYS B CB 1 ATOM 3193 C CG . LYS B 2 83 ? -46.569 21.745 59.120 1.00 67.49 ? 83 LYS B CG 1 ATOM 3194 C CD . LYS B 2 83 ? -45.207 21.173 59.491 1.00 72.05 ? 83 LYS B CD 1 ATOM 3195 C CE . LYS B 2 83 ? -44.886 19.979 58.597 1.00 79.76 ? 83 LYS B CE 1 ATOM 3196 N NZ . LYS B 2 83 ? -43.598 19.331 58.964 1.00 84.64 ? 83 LYS B NZ 1 ATOM 3197 N N . MET B 2 84 ? -46.562 26.256 58.845 1.00 53.99 ? 84 MET B N 1 ATOM 3198 C CA . MET B 2 84 ? -47.064 27.451 58.209 1.00 52.81 ? 84 MET B CA 1 ATOM 3199 C C . MET B 2 84 ? -45.978 28.083 57.336 1.00 51.62 ? 84 MET B C 1 ATOM 3200 O O . MET B 2 84 ? -46.229 28.403 56.171 1.00 52.44 ? 84 MET B O 1 ATOM 3201 C CB . MET B 2 84 ? -47.553 28.434 59.268 1.00 51.39 ? 84 MET B CB 1 ATOM 3202 C CG . MET B 2 84 ? -48.500 29.476 58.730 1.00 53.57 ? 84 MET B CG 1 ATOM 3203 S SD . MET B 2 84 ? -48.003 31.115 59.234 1.00 57.71 ? 84 MET B SD 1 ATOM 3204 C CE . MET B 2 84 ? -46.507 31.296 58.269 1.00 57.65 ? 84 MET B CE 1 ATOM 3205 N N . GLU B 2 85 ? -44.772 28.228 57.884 1.00 63.99 ? 85 GLU B N 1 ATOM 3206 C CA . GLU B 2 85 ? -43.684 28.886 57.158 1.00 62.64 ? 85 GLU B CA 1 ATOM 3207 C C . GLU B 2 85 ? -43.232 28.029 55.992 1.00 60.46 ? 85 GLU B C 1 ATOM 3208 O O . GLU B 2 85 ? -43.074 28.516 54.889 1.00 59.13 ? 85 GLU B O 1 ATOM 3209 C CB . GLU B 2 85 ? -42.502 29.173 58.075 1.00 65.94 ? 85 GLU B CB 1 ATOM 3210 C CG . GLU B 2 85 ? -42.863 29.996 59.302 1.00 68.98 ? 85 GLU B CG 1 ATOM 3211 C CD . GLU B 2 85 ? -42.205 31.361 59.365 1.00 71.27 ? 85 GLU B CD 1 ATOM 3212 O OE1 . GLU B 2 85 ? -41.096 31.460 59.936 1.00 75.26 ? 85 GLU B OE1 1 ATOM 3213 O OE2 . GLU B 2 85 ? -42.815 32.340 58.900 1.00 70.78 ? 85 GLU B OE2 1 ATOM 3214 N N . ASP B 2 86 ? -43.025 26.749 56.249 1.00 61.84 ? 86 ASP B N 1 ATOM 3215 C CA . ASP B 2 86 ? -42.689 25.790 55.206 1.00 61.23 ? 86 ASP B CA 1 ATOM 3216 C C . ASP B 2 86 ? -43.741 25.724 54.126 1.00 57.94 ? 86 ASP B C 1 ATOM 3217 O O . ASP B 2 86 ? -43.418 25.629 52.946 1.00 56.19 ? 86 ASP B O 1 ATOM 3218 C CB . ASP B 2 86 ? -42.511 24.386 55.803 1.00 65.29 ? 86 ASP B CB 1 ATOM 3219 C CG . ASP B 2 86 ? -41.082 24.099 56.174 1.00 69.75 ? 86 ASP B CG 1 ATOM 3220 O OD1 . ASP B 2 86 ? -40.208 24.674 55.489 1.00 71.80 ? 86 ASP B OD1 1 ATOM 3221 O OD2 . ASP B 2 86 ? -40.822 23.304 57.113 1.00 73.74 ? 86 ASP B OD2 1 ATOM 3222 N N . GLY B 2 87 ? -45.001 25.752 54.538 1.00 57.18 ? 87 GLY B N 1 ATOM 3223 C CA . GLY B 2 87 ? -46.108 25.679 53.604 1.00 55.74 ? 87 GLY B CA 1 ATOM 3224 C C . GLY B 2 87 ? -46.082 26.800 52.588 1.00 52.92 ? 87 GLY B C 1 ATOM 3225 O O . GLY B 2 87 ? -46.240 26.565 51.392 1.00 52.36 ? 87 GLY B O 1 ATOM 3226 N N . PHE B 2 88 ? -45.876 28.022 53.058 1.00 52.39 ? 88 PHE B N 1 ATOM 3227 C CA . PHE B 2 88 ? -45.853 29.161 52.161 1.00 51.08 ? 88 PHE B CA 1 ATOM 3228 C C . PHE B 2 88 ? -44.628 29.131 51.246 1.00 51.74 ? 88 PHE B C 1 ATOM 3229 O O . PHE B 2 88 ? -44.740 29.440 50.064 1.00 50.19 ? 88 PHE B O 1 ATOM 3230 C CB . PHE B 2 88 ? -45.905 30.468 52.939 1.00 52.36 ? 88 PHE B CB 1 ATOM 3231 C CG . PHE B 2 88 ? -47.269 30.808 53.472 1.00 53.10 ? 88 PHE B CG 1 ATOM 3232 C CD1 . PHE B 2 88 ? -48.355 30.921 52.625 1.00 52.34 ? 88 PHE B CD1 1 ATOM 3233 C CD2 . PHE B 2 88 ? -47.459 31.039 54.817 1.00 55.75 ? 88 PHE B CD2 1 ATOM 3234 C CE1 . PHE B 2 88 ? -49.605 31.245 53.110 1.00 53.29 ? 88 PHE B CE1 1 ATOM 3235 C CE2 . PHE B 2 88 ? -48.707 31.363 55.314 1.00 56.75 ? 88 PHE B CE2 1 ATOM 3236 C CZ . PHE B 2 88 ? -49.783 31.462 54.454 1.00 55.70 ? 88 PHE B CZ 1 ATOM 3237 N N . LEU B 2 89 ? -43.468 28.736 51.764 1.00 54.50 ? 89 LEU B N 1 ATOM 3238 C CA . LEU B 2 89 ? -42.285 28.632 50.913 1.00 56.25 ? 89 LEU B CA 1 ATOM 3239 C C . LEU B 2 89 ? -42.531 27.665 49.760 1.00 53.96 ? 89 LEU B C 1 ATOM 3240 O O . LEU B 2 89 ? -42.272 27.984 48.613 1.00 50.69 ? 89 LEU B O 1 ATOM 3241 C CB . LEU B 2 89 ? -41.071 28.194 51.722 1.00 61.97 ? 89 LEU B CB 1 ATOM 3242 C CG . LEU B 2 89 ? -40.649 29.214 52.795 1.00 67.21 ? 89 LEU B CG 1 ATOM 3243 C CD1 . LEU B 2 89 ? -39.571 28.627 53.704 1.00 71.89 ? 89 LEU B CD1 1 ATOM 3244 C CD2 . LEU B 2 89 ? -40.207 30.551 52.194 1.00 67.13 ? 89 LEU B CD2 1 ATOM 3245 N N . ASP B 2 90 ? -43.061 26.491 50.081 1.00 55.12 ? 90 ASP B N 1 ATOM 3246 C CA . ASP B 2 90 ? -43.430 25.515 49.067 1.00 54.93 ? 90 ASP B CA 1 ATOM 3247 C C . ASP B 2 90 ? -44.396 26.082 48.024 1.00 52.24 ? 90 ASP B C 1 ATOM 3248 O O . ASP B 2 90 ? -44.202 25.883 46.834 1.00 50.64 ? 90 ASP B O 1 ATOM 3249 C CB . ASP B 2 90 ? -44.052 24.280 49.713 1.00 57.01 ? 90 ASP B CB 1 ATOM 3250 C CG . ASP B 2 90 ? -43.044 23.427 50.430 1.00 60.81 ? 90 ASP B CG 1 ATOM 3251 O OD1 . ASP B 2 90 ? -41.824 23.660 50.243 1.00 61.69 ? 90 ASP B OD1 1 ATOM 3252 O OD2 . ASP B 2 90 ? -43.482 22.519 51.183 1.00 63.69 ? 90 ASP B OD2 1 ATOM 3253 N N . VAL B 2 91 ? -45.434 26.776 48.477 1.00 51.96 ? 91 VAL B N 1 ATOM 3254 C CA . VAL B 2 91 ? -46.397 27.411 47.567 1.00 49.89 ? 91 VAL B CA 1 ATOM 3255 C C . VAL B 2 91 ? -45.720 28.435 46.657 1.00 48.10 ? 91 VAL B C 1 ATOM 3256 O O . VAL B 2 91 ? -45.961 28.453 45.463 1.00 48.95 ? 91 VAL B O 1 ATOM 3257 C CB . VAL B 2 91 ? -47.546 28.112 48.332 1.00 49.89 ? 91 VAL B CB 1 ATOM 3258 C CG1 . VAL B 2 91 ? -48.414 28.931 47.382 1.00 48.95 ? 91 VAL B CG1 1 ATOM 3259 C CG2 . VAL B 2 91 ? -48.401 27.092 49.070 1.00 51.86 ? 91 VAL B CG2 1 ATOM 3260 N N . TRP B 2 92 ? -44.886 29.295 47.212 1.00 48.03 ? 92 TRP B N 1 ATOM 3261 C CA . TRP B 2 92 ? -44.232 30.300 46.392 1.00 47.53 ? 92 TRP B CA 1 ATOM 3262 C C . TRP B 2 92 ? -43.104 29.741 45.533 1.00 47.85 ? 92 TRP B C 1 ATOM 3263 O O . TRP B 2 92 ? -42.798 30.304 44.484 1.00 48.05 ? 92 TRP B O 1 ATOM 3264 C CB . TRP B 2 92 ? -43.731 31.439 47.258 1.00 49.00 ? 92 TRP B CB 1 ATOM 3265 C CG . TRP B 2 92 ? -44.844 32.337 47.681 1.00 50.16 ? 92 TRP B CG 1 ATOM 3266 C CD1 . TRP B 2 92 ? -45.342 32.484 48.933 1.00 51.72 ? 92 TRP B CD1 1 ATOM 3267 C CD2 . TRP B 2 92 ? -45.614 33.197 46.838 1.00 50.02 ? 92 TRP B CD2 1 ATOM 3268 N NE1 . TRP B 2 92 ? -46.363 33.397 48.934 1.00 52.68 ? 92 TRP B NE1 1 ATOM 3269 C CE2 . TRP B 2 92 ? -46.554 33.851 47.660 1.00 51.99 ? 92 TRP B CE2 1 ATOM 3270 C CE3 . TRP B 2 92 ? -45.602 33.474 45.471 1.00 49.32 ? 92 TRP B CE3 1 ATOM 3271 C CZ2 . TRP B 2 92 ? -47.475 34.776 47.163 1.00 54.27 ? 92 TRP B CZ2 1 ATOM 3272 C CZ3 . TRP B 2 92 ? -46.512 34.400 44.972 1.00 52.00 ? 92 TRP B CZ3 1 ATOM 3273 C CH2 . TRP B 2 92 ? -47.433 35.049 45.821 1.00 53.65 ? 92 TRP B CH2 1 ATOM 3274 N N . THR B 2 93 ? -42.488 28.645 45.963 1.00 48.63 ? 93 THR B N 1 ATOM 3275 C CA . THR B 2 93 ? -41.465 28.012 45.160 1.00 48.90 ? 93 THR B CA 1 ATOM 3276 C C . THR B 2 93 ? -42.141 27.449 43.920 1.00 47.39 ? 93 THR B C 1 ATOM 3277 O O . THR B 2 93 ? -41.640 27.612 42.799 1.00 46.66 ? 93 THR B O 1 ATOM 3278 C CB . THR B 2 93 ? -40.718 26.901 45.929 1.00 52.12 ? 93 THR B CB 1 ATOM 3279 O OG1 . THR B 2 93 ? -39.927 27.481 46.969 1.00 54.17 ? 93 THR B OG1 1 ATOM 3280 C CG2 . THR B 2 93 ? -39.788 26.137 45.015 1.00 53.76 ? 93 THR B CG2 1 ATOM 3281 N N . TYR B 2 94 ? -43.286 26.804 44.137 1.00 47.39 ? 94 TYR B N 1 ATOM 3282 C CA . TYR B 2 94 ? -44.075 26.192 43.066 1.00 46.81 ? 94 TYR B CA 1 ATOM 3283 C C . TYR B 2 94 ? -44.542 27.253 42.087 1.00 44.50 ? 94 TYR B C 1 ATOM 3284 O O . TYR B 2 94 ? -44.346 27.125 40.890 1.00 43.46 ? 94 TYR B O 1 ATOM 3285 C CB . TYR B 2 94 ? -45.269 25.425 43.652 1.00 48.23 ? 94 TYR B CB 1 ATOM 3286 C CG . TYR B 2 94 ? -46.339 25.014 42.651 1.00 48.37 ? 94 TYR B CG 1 ATOM 3287 C CD1 . TYR B 2 94 ? -47.312 25.923 42.222 1.00 46.79 ? 94 TYR B CD1 1 ATOM 3288 C CD2 . TYR B 2 94 ? -46.376 23.732 42.131 1.00 49.53 ? 94 TYR B CD2 1 ATOM 3289 C CE1 . TYR B 2 94 ? -48.278 25.563 41.313 1.00 46.13 ? 94 TYR B CE1 1 ATOM 3290 C CE2 . TYR B 2 94 ? -47.349 23.361 41.222 1.00 50.27 ? 94 TYR B CE2 1 ATOM 3291 C CZ . TYR B 2 94 ? -48.299 24.284 40.817 1.00 48.41 ? 94 TYR B CZ 1 ATOM 3292 O OH . TYR B 2 94 ? -49.280 23.931 39.917 1.00 48.92 ? 94 TYR B OH 1 ATOM 3293 N N . ASN B 2 95 ? -45.141 28.311 42.606 1.00 45.47 ? 95 ASN B N 1 ATOM 3294 C CA . ASN B 2 95 ? -45.529 29.451 41.774 1.00 45.04 ? 95 ASN B CA 1 ATOM 3295 C C . ASN B 2 95 ? -44.395 29.925 40.871 1.00 45.08 ? 95 ASN B C 1 ATOM 3296 O O . ASN B 2 95 ? -44.597 30.119 39.668 1.00 44.78 ? 95 ASN B O 1 ATOM 3297 C CB . ASN B 2 95 ? -46.051 30.609 42.632 1.00 44.70 ? 95 ASN B CB 1 ATOM 3298 C CG . ASN B 2 95 ? -47.425 30.322 43.233 1.00 46.29 ? 95 ASN B CG 1 ATOM 3299 O OD1 . ASN B 2 95 ? -48.012 29.269 43.002 1.00 46.77 ? 95 ASN B OD1 1 ATOM 3300 N ND2 . ASN B 2 95 ? -47.933 31.259 44.023 1.00 48.02 ? 95 ASN B ND2 1 ATOM 3301 N N . ALA B 2 96 ? -43.203 30.087 41.437 1.00 46.65 ? 96 ALA B N 1 ATOM 3302 C CA . ALA B 2 96 ? -42.055 30.585 40.661 1.00 46.73 ? 96 ALA B CA 1 ATOM 3303 C C . ALA B 2 96 ? -41.606 29.608 39.566 1.00 46.13 ? 96 ALA B C 1 ATOM 3304 O O . ALA B 2 96 ? -41.377 30.009 38.430 1.00 46.29 ? 96 ALA B O 1 ATOM 3305 C CB . ALA B 2 96 ? -40.892 30.895 41.580 1.00 48.56 ? 96 ALA B CB 1 ATOM 3306 N N . GLU B 2 97 ? -41.477 28.334 39.901 1.00 46.18 ? 97 GLU B N 1 ATOM 3307 C CA . GLU B 2 97 ? -40.955 27.375 38.937 1.00 47.18 ? 97 GLU B CA 1 ATOM 3308 C C . GLU B 2 97 ? -41.962 27.110 37.823 1.00 46.34 ? 97 GLU B C 1 ATOM 3309 O O . GLU B 2 97 ? -41.589 26.939 36.663 1.00 48.01 ? 97 GLU B O 1 ATOM 3310 C CB . GLU B 2 97 ? -40.547 26.081 39.633 1.00 49.44 ? 97 GLU B CB 1 ATOM 3311 C CG . GLU B 2 97 ? -39.384 26.293 40.583 1.00 52.09 ? 97 GLU B CG 1 ATOM 3312 C CD . GLU B 2 97 ? -38.999 25.061 41.359 1.00 55.42 ? 97 GLU B CD 1 ATOM 3313 O OE1 . GLU B 2 97 ? -39.689 24.026 41.255 1.00 57.26 ? 97 GLU B OE1 1 ATOM 3314 O OE2 . GLU B 2 97 ? -37.995 25.132 42.090 1.00 59.04 ? 97 GLU B OE2 1 ATOM 3315 N N . LEU B 2 98 ? -43.241 27.086 38.164 1.00 45.83 ? 98 LEU B N 1 ATOM 3316 C CA . LEU B 2 98 ? -44.272 26.884 37.160 1.00 44.44 ? 98 LEU B CA 1 ATOM 3317 C C . LEU B 2 98 ? -44.310 28.073 36.222 1.00 42.65 ? 98 LEU B C 1 ATOM 3318 O O . LEU B 2 98 ? -44.328 27.912 35.016 1.00 41.97 ? 98 LEU B O 1 ATOM 3319 C CB . LEU B 2 98 ? -45.631 26.714 37.805 1.00 44.46 ? 98 LEU B CB 1 ATOM 3320 C CG . LEU B 2 98 ? -46.702 26.096 36.909 1.00 45.46 ? 98 LEU B CG 1 ATOM 3321 C CD1 . LEU B 2 98 ? -46.308 24.686 36.473 1.00 47.70 ? 98 LEU B CD1 1 ATOM 3322 C CD2 . LEU B 2 98 ? -48.022 26.079 37.670 1.00 46.37 ? 98 LEU B CD2 1 ATOM 3323 N N . LEU B 2 99 ? -44.290 29.274 36.779 1.00 42.27 ? 99 LEU B N 1 ATOM 3324 C CA . LEU B 2 99 ? -44.407 30.456 35.958 1.00 41.62 ? 99 LEU B CA 1 ATOM 3325 C C . LEU B 2 99 ? -43.281 30.466 34.936 1.00 41.35 ? 99 LEU B C 1 ATOM 3326 O O . LEU B 2 99 ? -43.509 30.661 33.739 1.00 40.13 ? 99 LEU B O 1 ATOM 3327 C CB . LEU B 2 99 ? -44.389 31.717 36.819 1.00 42.79 ? 99 LEU B CB 1 ATOM 3328 C CG . LEU B 2 99 ? -44.574 33.069 36.103 1.00 45.48 ? 99 LEU B CG 1 ATOM 3329 C CD1 . LEU B 2 99 ? -45.685 33.059 35.066 1.00 46.49 ? 99 LEU B CD1 1 ATOM 3330 C CD2 . LEU B 2 99 ? -44.846 34.186 37.099 1.00 47.54 ? 99 LEU B CD2 1 ATOM 3331 N N . VAL B 2 100 ? -42.067 30.215 35.414 1.00 42.67 ? 100 VAL B N 1 ATOM 3332 C CA . VAL B 2 100 ? -40.900 30.198 34.559 1.00 42.03 ? 100 VAL B CA 1 ATOM 3333 C C . VAL B 2 100 ? -41.056 29.140 33.461 1.00 42.71 ? 100 VAL B C 1 ATOM 3334 O O . VAL B 2 100 ? -40.916 29.469 32.278 1.00 42.53 ? 100 VAL B O 1 ATOM 3335 C CB . VAL B 2 100 ? -39.616 30.033 35.398 1.00 44.84 ? 100 VAL B CB 1 ATOM 3336 C CG1 . VAL B 2 100 ? -38.447 29.495 34.566 1.00 46.35 ? 100 VAL B CG1 1 ATOM 3337 C CG2 . VAL B 2 100 ? -39.259 31.376 36.021 1.00 44.88 ? 100 VAL B CG2 1 ATOM 3338 N N . LEU B 2 101 ? -41.372 27.900 33.850 1.00 42.36 ? 101 LEU B N 1 ATOM 3339 C CA . LEU B 2 101 ? -41.664 26.824 32.895 1.00 42.82 ? 101 LEU B CA 1 ATOM 3340 C C . LEU B 2 101 ? -42.704 27.213 31.837 1.00 43.59 ? 101 LEU B C 1 ATOM 3341 O O . LEU B 2 101 ? -42.446 27.079 30.631 1.00 45.97 ? 101 LEU B O 1 ATOM 3342 C CB . LEU B 2 101 ? -42.167 25.571 33.625 1.00 44.05 ? 101 LEU B CB 1 ATOM 3343 C CG . LEU B 2 101 ? -41.202 24.406 33.848 1.00 47.42 ? 101 LEU B CG 1 ATOM 3344 C CD1 . LEU B 2 101 ? -39.741 24.822 33.970 1.00 49.23 ? 101 LEU B CD1 1 ATOM 3345 C CD2 . LEU B 2 101 ? -41.626 23.634 35.076 1.00 49.24 ? 101 LEU B CD2 1 ATOM 3346 N N . MET B 2 102 ? -43.874 27.669 32.289 1.00 42.05 ? 102 MET B N 1 ATOM 3347 C CA . MET B 2 102 ? -44.980 27.996 31.391 1.00 42.07 ? 102 MET B CA 1 ATOM 3348 C C . MET B 2 102 ? -44.593 29.143 30.465 1.00 41.52 ? 102 MET B C 1 ATOM 3349 O O . MET B 2 102 ? -44.810 29.075 29.249 1.00 43.10 ? 102 MET B O 1 ATOM 3350 C CB . MET B 2 102 ? -46.259 28.358 32.166 1.00 42.65 ? 102 MET B CB 1 ATOM 3351 C CG . MET B 2 102 ? -46.871 27.215 32.957 1.00 46.19 ? 102 MET B CG 1 ATOM 3352 S SD . MET B 2 102 ? -48.593 27.484 33.479 1.00 50.63 ? 102 MET B SD 1 ATOM 3353 C CE . MET B 2 102 ? -48.365 28.900 34.557 1.00 52.20 ? 102 MET B CE 1 ATOM 3354 N N . GLU B 2 103 ? -44.008 30.194 31.022 1.00 40.36 ? 103 GLU B N 1 ATOM 3355 C CA . GLU B 2 103 ? -43.732 31.371 30.211 1.00 40.80 ? 103 GLU B CA 1 ATOM 3356 C C . GLU B 2 103 ? -42.541 31.147 29.294 1.00 41.40 ? 103 GLU B C 1 ATOM 3357 O O . GLU B 2 103 ? -42.548 31.621 28.171 1.00 41.09 ? 103 GLU B O 1 ATOM 3358 C CB . GLU B 2 103 ? -43.547 32.607 31.082 1.00 42.74 ? 103 GLU B CB 1 ATOM 3359 C CG . GLU B 2 103 ? -44.856 33.118 31.696 1.00 44.73 ? 103 GLU B CG 1 ATOM 3360 C CD . GLU B 2 103 ? -45.849 33.643 30.679 1.00 46.06 ? 103 GLU B CD 1 ATOM 3361 O OE1 . GLU B 2 103 ? -45.421 34.089 29.602 1.00 45.13 ? 103 GLU B OE1 1 ATOM 3362 O OE2 . GLU B 2 103 ? -47.075 33.612 30.952 1.00 53.88 ? 103 GLU B OE2 1 ATOM 3363 N N . ASN B 2 104 ? -41.525 30.423 29.761 1.00 42.28 ? 104 ASN B N 1 ATOM 3364 C CA . ASN B 2 104 ? -40.451 30.008 28.882 1.00 41.99 ? 104 ASN B CA 1 ATOM 3365 C C . ASN B 2 104 ? -40.996 29.354 27.620 1.00 42.35 ? 104 ASN B C 1 ATOM 3366 O O . ASN B 2 104 ? -40.546 29.669 26.520 1.00 41.29 ? 104 ASN B O 1 ATOM 3367 C CB . ASN B 2 104 ? -39.536 29.006 29.571 1.00 43.96 ? 104 ASN B CB 1 ATOM 3368 C CG . ASN B 2 104 ? -38.505 29.659 30.459 1.00 44.91 ? 104 ASN B CG 1 ATOM 3369 O OD1 . ASN B 2 104 ? -38.264 30.870 30.383 1.00 43.85 ? 104 ASN B OD1 1 ATOM 3370 N ND2 . ASN B 2 104 ? -37.877 28.850 31.313 1.00 45.81 ? 104 ASN B ND2 1 ATOM 3371 N N . GLU B 2 105 ? -41.946 28.434 27.785 1.00 42.55 ? 105 GLU B N 1 ATOM 3372 C CA . GLU B 2 105 ? -42.574 27.774 26.642 1.00 43.26 ? 105 GLU B CA 1 ATOM 3373 C C . GLU B 2 105 ? -43.316 28.775 25.792 1.00 39.60 ? 105 GLU B C 1 ATOM 3374 O O . GLU B 2 105 ? -43.251 28.740 24.580 1.00 37.68 ? 105 GLU B O 1 ATOM 3375 C CB . GLU B 2 105 ? -43.548 26.682 27.078 1.00 47.73 ? 105 GLU B CB 1 ATOM 3376 C CG . GLU B 2 105 ? -43.881 25.717 25.958 1.00 53.25 ? 105 GLU B CG 1 ATOM 3377 C CD . GLU B 2 105 ? -44.572 24.468 26.453 1.00 62.18 ? 105 GLU B CD 1 ATOM 3378 O OE1 . GLU B 2 105 ? -45.711 24.604 26.955 1.00 70.21 ? 105 GLU B OE1 1 ATOM 3379 O OE2 . GLU B 2 105 ? -43.983 23.357 26.344 1.00 65.34 ? 105 GLU B OE2 1 ATOM 3380 N N . ARG B 2 106 ? -44.017 29.691 26.423 1.00 40.27 ? 106 ARG B N 1 ATOM 3381 C CA . ARG B 2 106 ? -44.692 30.731 25.651 1.00 41.87 ? 106 ARG B CA 1 ATOM 3382 C C . ARG B 2 106 ? -43.710 31.636 24.899 1.00 39.45 ? 106 ARG B C 1 ATOM 3383 O O . ARG B 2 106 ? -43.997 32.076 23.789 1.00 40.14 ? 106 ARG B O 1 ATOM 3384 C CB . ARG B 2 106 ? -45.603 31.558 26.537 1.00 44.79 ? 106 ARG B CB 1 ATOM 3385 C CG . ARG B 2 106 ? -46.690 30.750 27.231 1.00 49.28 ? 106 ARG B CG 1 ATOM 3386 C CD . ARG B 2 106 ? -47.970 31.566 27.313 1.00 54.45 ? 106 ARG B CD 1 ATOM 3387 N NE . ARG B 2 106 ? -48.765 31.369 26.101 1.00 58.85 ? 106 ARG B NE 1 ATOM 3388 C CZ . ARG B 2 106 ? -49.552 32.281 25.532 1.00 64.02 ? 106 ARG B CZ 1 ATOM 3389 N NH1 . ARG B 2 106 ? -49.691 33.510 26.034 1.00 63.68 ? 106 ARG B NH1 1 ATOM 3390 N NH2 . ARG B 2 106 ? -50.224 31.951 24.435 1.00 70.32 ? 106 ARG B NH2 1 ATOM 3391 N N . THR B 2 107 ? -42.545 31.890 25.481 1.00 37.76 ? 107 THR B N 1 ATOM 3392 C CA . THR B 2 107 ? -41.563 32.777 24.854 1.00 36.81 ? 107 THR B CA 1 ATOM 3393 C C . THR B 2 107 ? -41.001 32.162 23.585 1.00 36.62 ? 107 THR B C 1 ATOM 3394 O O . THR B 2 107 ? -40.903 32.824 22.568 1.00 36.77 ? 107 THR B O 1 ATOM 3395 C CB . THR B 2 107 ? -40.416 33.138 25.812 1.00 37.02 ? 107 THR B CB 1 ATOM 3396 O OG1 . THR B 2 107 ? -40.942 33.873 26.916 1.00 36.95 ? 107 THR B OG1 1 ATOM 3397 C CG2 . THR B 2 107 ? -39.385 33.994 25.115 1.00 38.64 ? 107 THR B CG2 1 ATOM 3398 N N . LEU B 2 108 ? -40.646 30.890 23.636 1.00 37.03 ? 108 LEU B N 1 ATOM 3399 C CA . LEU B 2 108 ? -40.111 30.240 22.457 1.00 37.75 ? 108 LEU B CA 1 ATOM 3400 C C . LEU B 2 108 ? -41.147 30.251 21.325 1.00 36.42 ? 108 LEU B C 1 ATOM 3401 O O . LEU B 2 108 ? -40.863 30.715 20.222 1.00 34.36 ? 108 LEU B O 1 ATOM 3402 C CB . LEU B 2 108 ? -39.659 28.818 22.793 1.00 39.90 ? 108 LEU B CB 1 ATOM 3403 C CG . LEU B 2 108 ? -38.606 28.696 23.903 1.00 41.06 ? 108 LEU B CG 1 ATOM 3404 C CD1 . LEU B 2 108 ? -38.264 27.234 24.123 1.00 44.21 ? 108 LEU B CD1 1 ATOM 3405 C CD2 . LEU B 2 108 ? -37.341 29.469 23.602 1.00 42.17 ? 108 LEU B CD2 1 ATOM 3406 N N . ASP B 2 109 ? -42.358 29.774 21.606 1.00 36.47 ? 109 ASP B N 1 ATOM 3407 C CA . ASP B 2 109 ? -43.438 29.844 20.617 1.00 36.71 ? 109 ASP B CA 1 ATOM 3408 C C . ASP B 2 109 ? -43.704 31.282 20.105 1.00 35.88 ? 109 ASP B C 1 ATOM 3409 O O . ASP B 2 109 ? -44.026 31.478 18.949 1.00 37.58 ? 109 ASP B O 1 ATOM 3410 C CB . ASP B 2 109 ? -44.734 29.284 21.184 1.00 37.83 ? 109 ASP B CB 1 ATOM 3411 C CG . ASP B 2 109 ? -44.634 27.819 21.603 1.00 39.60 ? 109 ASP B CG 1 ATOM 3412 O OD1 . ASP B 2 109 ? -43.972 26.998 20.912 1.00 39.05 ? 109 ASP B OD1 1 ATOM 3413 O OD2 . ASP B 2 109 ? -45.279 27.500 22.640 1.00 41.08 ? 109 ASP B OD2 1 ATOM 3414 N N . PHE B 2 110 ? -43.585 32.283 20.964 1.00 34.81 ? 110 PHE B N 1 ATOM 3415 C CA . PHE B 2 110 ? -43.744 33.683 20.553 1.00 34.64 ? 110 PHE B CA 1 ATOM 3416 C C . PHE B 2 110 ? -42.755 34.050 19.438 1.00 35.63 ? 110 PHE B C 1 ATOM 3417 O O . PHE B 2 110 ? -43.141 34.620 18.416 1.00 37.83 ? 110 PHE B O 1 ATOM 3418 C CB . PHE B 2 110 ? -43.559 34.575 21.784 1.00 34.55 ? 110 PHE B CB 1 ATOM 3419 C CG . PHE B 2 110 ? -43.576 36.047 21.498 1.00 36.10 ? 110 PHE B CG 1 ATOM 3420 C CD1 . PHE B 2 110 ? -44.671 36.640 20.912 1.00 38.28 ? 110 PHE B CD1 1 ATOM 3421 C CD2 . PHE B 2 110 ? -42.519 36.846 21.871 1.00 36.73 ? 110 PHE B CD2 1 ATOM 3422 C CE1 . PHE B 2 110 ? -44.693 38.002 20.669 1.00 40.29 ? 110 PHE B CE1 1 ATOM 3423 C CE2 . PHE B 2 110 ? -42.529 38.207 21.632 1.00 39.58 ? 110 PHE B CE2 1 ATOM 3424 C CZ . PHE B 2 110 ? -43.621 38.792 21.033 1.00 41.02 ? 110 PHE B CZ 1 ATOM 3425 N N . HIS B 2 111 ? -41.484 33.706 19.629 1.00 35.16 ? 111 HIS B N 1 ATOM 3426 C CA . HIS B 2 111 ? -40.462 33.913 18.607 1.00 35.99 ? 111 HIS B CA 1 ATOM 3427 C C . HIS B 2 111 ? -40.776 33.174 17.308 1.00 36.96 ? 111 HIS B C 1 ATOM 3428 O O . HIS B 2 111 ? -40.567 33.713 16.219 1.00 38.75 ? 111 HIS B O 1 ATOM 3429 C CB . HIS B 2 111 ? -39.098 33.439 19.108 1.00 36.71 ? 111 HIS B CB 1 ATOM 3430 C CG . HIS B 2 111 ? -38.484 34.333 20.139 1.00 37.76 ? 111 HIS B CG 1 ATOM 3431 N ND1 . HIS B 2 111 ? -38.136 35.643 19.879 1.00 39.03 ? 111 HIS B ND1 1 ATOM 3432 C CD2 . HIS B 2 111 ? -38.123 34.093 21.420 1.00 37.93 ? 111 HIS B CD2 1 ATOM 3433 C CE1 . HIS B 2 111 ? -37.604 36.174 20.964 1.00 40.47 ? 111 HIS B CE1 1 ATOM 3434 N NE2 . HIS B 2 111 ? -37.578 35.251 21.911 1.00 39.61 ? 111 HIS B NE2 1 ATOM 3435 N N . ASP B 2 112 ? -41.262 31.940 17.440 1.00 35.49 ? 112 ASP B N 1 ATOM 3436 C CA . ASP B 2 112 ? -41.661 31.114 16.313 1.00 34.82 ? 112 ASP B CA 1 ATOM 3437 C C . ASP B 2 112 ? -42.794 31.796 15.530 1.00 36.28 ? 112 ASP B C 1 ATOM 3438 O O . ASP B 2 112 ? -42.729 31.943 14.310 1.00 37.56 ? 112 ASP B O 1 ATOM 3439 C CB . ASP B 2 112 ? -42.101 29.764 16.868 1.00 35.23 ? 112 ASP B CB 1 ATOM 3440 C CG . ASP B 2 112 ? -42.240 28.701 15.818 1.00 36.64 ? 112 ASP B CG 1 ATOM 3441 O OD1 . ASP B 2 112 ? -41.894 28.910 14.636 1.00 35.91 ? 112 ASP B OD1 1 ATOM 3442 O OD2 . ASP B 2 112 ? -42.720 27.617 16.202 1.00 38.85 ? 112 ASP B OD2 1 ATOM 3443 N N . SER B 2 113 ? -43.825 32.225 16.251 1.00 36.63 ? 113 SER B N 1 ATOM 3444 C CA . SER B 2 113 ? -44.915 33.002 15.691 1.00 37.26 ? 113 SER B CA 1 ATOM 3445 C C . SER B 2 113 ? -44.430 34.257 14.940 1.00 38.54 ? 113 SER B C 1 ATOM 3446 O O . SER B 2 113 ? -44.915 34.543 13.841 1.00 40.17 ? 113 SER B O 1 ATOM 3447 C CB . SER B 2 113 ? -45.868 33.413 16.813 1.00 37.88 ? 113 SER B CB 1 ATOM 3448 O OG . SER B 2 113 ? -46.826 34.363 16.353 1.00 40.61 ? 113 SER B OG 1 ATOM 3449 N N . ASN B 2 114 ? -43.488 35.007 15.517 1.00 37.37 ? 114 ASN B N 1 ATOM 3450 C CA . ASN B 2 114 ? -42.989 36.210 14.848 1.00 38.15 ? 114 ASN B CA 1 ATOM 3451 C C . ASN B 2 114 ? -42.251 35.876 13.553 1.00 38.00 ? 114 ASN B C 1 ATOM 3452 O O . ASN B 2 114 ? -42.353 36.633 12.580 1.00 37.68 ? 114 ASN B O 1 ATOM 3453 C CB . ASN B 2 114 ? -42.071 37.040 15.747 1.00 38.99 ? 114 ASN B CB 1 ATOM 3454 C CG . ASN B 2 114 ? -42.754 37.523 17.012 1.00 40.27 ? 114 ASN B CG 1 ATOM 3455 O OD1 . ASN B 2 114 ? -43.890 38.001 17.004 1.00 41.95 ? 114 ASN B OD1 1 ATOM 3456 N ND2 . ASN B 2 114 ? -42.041 37.427 18.109 1.00 41.16 ? 114 ASN B ND2 1 ATOM 3457 N N . VAL B 2 115 ? -41.511 34.761 13.533 1.00 36.61 ? 115 VAL B N 1 ATOM 3458 C CA . VAL B 2 115 ? -40.795 34.372 12.315 1.00 37.65 ? 115 VAL B CA 1 ATOM 3459 C C . VAL B 2 115 ? -41.806 34.019 11.235 1.00 38.99 ? 115 VAL B C 1 ATOM 3460 O O . VAL B 2 115 ? -41.666 34.456 10.088 1.00 39.97 ? 115 VAL B O 1 ATOM 3461 C CB . VAL B 2 115 ? -39.847 33.167 12.519 1.00 38.10 ? 115 VAL B CB 1 ATOM 3462 C CG1 . VAL B 2 115 ? -39.327 32.638 11.191 1.00 39.23 ? 115 VAL B CG1 1 ATOM 3463 C CG2 . VAL B 2 115 ? -38.672 33.547 13.382 1.00 38.81 ? 115 VAL B CG2 1 ATOM 3464 N N . LYS B 2 116 ? -42.812 33.226 11.599 1.00 39.07 ? 116 LYS B N 1 ATOM 3465 C CA . LYS B 2 116 ? -43.825 32.810 10.637 1.00 41.83 ? 116 LYS B CA 1 ATOM 3466 C C . LYS B 2 116 ? -44.607 33.988 10.076 1.00 43.00 ? 116 LYS B C 1 ATOM 3467 O O . LYS B 2 116 ? -44.908 34.047 8.893 1.00 43.50 ? 116 LYS B O 1 ATOM 3468 C CB . LYS B 2 116 ? -44.815 31.851 11.263 1.00 43.48 ? 116 LYS B CB 1 ATOM 3469 C CG . LYS B 2 116 ? -45.533 31.044 10.218 1.00 48.43 ? 116 LYS B CG 1 ATOM 3470 C CD . LYS B 2 116 ? -46.887 30.566 10.707 1.00 54.44 ? 116 LYS B CD 1 ATOM 3471 C CE . LYS B 2 116 ? -47.577 29.745 9.624 1.00 58.63 ? 116 LYS B CE 1 ATOM 3472 N NZ . LYS B 2 116 ? -46.672 28.662 9.135 1.00 58.80 ? 116 LYS B NZ 1 ATOM 3473 N N . ASN B 2 117 ? -44.956 34.918 10.945 1.00 43.53 ? 117 ASN B N 1 ATOM 3474 C CA . ASN B 2 117 ? -45.743 36.050 10.535 1.00 45.57 ? 117 ASN B CA 1 ATOM 3475 C C . ASN B 2 117 ? -44.974 36.922 9.561 1.00 47.38 ? 117 ASN B C 1 ATOM 3476 O O . ASN B 2 117 ? -45.549 37.447 8.592 1.00 50.30 ? 117 ASN B O 1 ATOM 3477 C CB . ASN B 2 117 ? -46.183 36.829 11.763 1.00 45.81 ? 117 ASN B CB 1 ATOM 3478 C CG . ASN B 2 117 ? -47.271 36.118 12.518 1.00 46.29 ? 117 ASN B CG 1 ATOM 3479 O OD1 . ASN B 2 117 ? -48.002 35.323 11.950 1.00 46.89 ? 117 ASN B OD1 1 ATOM 3480 N ND2 . ASN B 2 117 ? -47.397 36.409 13.796 1.00 47.36 ? 117 ASN B ND2 1 ATOM 3481 N N . LEU B 2 118 ? -43.674 37.048 9.808 1.00 45.27 ? 118 LEU B N 1 ATOM 3482 C CA . LEU B 2 118 ? -42.790 37.775 8.914 1.00 45.74 ? 118 LEU B CA 1 ATOM 3483 C C . LEU B 2 118 ? -42.717 37.052 7.578 1.00 45.58 ? 118 LEU B C 1 ATOM 3484 O O . LEU B 2 118 ? -42.758 37.684 6.514 1.00 47.99 ? 118 LEU B O 1 ATOM 3485 C CB . LEU B 2 118 ? -41.394 37.885 9.540 1.00 44.86 ? 118 LEU B CB 1 ATOM 3486 C CG . LEU B 2 118 ? -40.282 38.565 8.770 1.00 45.65 ? 118 LEU B CG 1 ATOM 3487 C CD1 . LEU B 2 118 ? -40.696 39.945 8.305 1.00 48.40 ? 118 LEU B CD1 1 ATOM 3488 C CD2 . LEU B 2 118 ? -39.064 38.649 9.663 1.00 45.88 ? 118 LEU B CD2 1 ATOM 3489 N N . TYR B 2 119 ? -42.625 35.728 7.628 1.00 42.68 ? 119 TYR B N 1 ATOM 3490 C CA . TYR B 2 119 ? -42.572 34.945 6.408 1.00 42.34 ? 119 TYR B CA 1 ATOM 3491 C C . TYR B 2 119 ? -43.855 35.127 5.627 1.00 44.31 ? 119 TYR B C 1 ATOM 3492 O O . TYR B 2 119 ? -43.820 35.380 4.426 1.00 46.40 ? 119 TYR B O 1 ATOM 3493 C CB . TYR B 2 119 ? -42.347 33.473 6.731 1.00 41.57 ? 119 TYR B CB 1 ATOM 3494 C CG . TYR B 2 119 ? -42.334 32.568 5.528 1.00 42.98 ? 119 TYR B CG 1 ATOM 3495 C CD1 . TYR B 2 119 ? -41.222 32.493 4.707 1.00 43.53 ? 119 TYR B CD1 1 ATOM 3496 C CD2 . TYR B 2 119 ? -43.431 31.769 5.218 1.00 43.89 ? 119 TYR B CD2 1 ATOM 3497 C CE1 . TYR B 2 119 ? -41.203 31.643 3.611 1.00 45.74 ? 119 TYR B CE1 1 ATOM 3498 C CE2 . TYR B 2 119 ? -43.422 30.926 4.120 1.00 45.36 ? 119 TYR B CE2 1 ATOM 3499 C CZ . TYR B 2 119 ? -42.307 30.862 3.326 1.00 46.02 ? 119 TYR B CZ 1 ATOM 3500 O OH . TYR B 2 119 ? -42.281 30.035 2.237 1.00 47.62 ? 119 TYR B OH 1 ATOM 3501 N N . ASP B 2 120 ? -44.993 35.020 6.301 1.00 45.15 ? 120 ASP B N 1 ATOM 3502 C CA . ASP B 2 120 ? -46.261 35.178 5.610 1.00 48.61 ? 120 ASP B CA 1 ATOM 3503 C C . ASP B 2 120 ? -46.371 36.578 5.024 1.00 49.72 ? 120 ASP B C 1 ATOM 3504 O O . ASP B 2 120 ? -46.767 36.748 3.878 1.00 51.80 ? 120 ASP B O 1 ATOM 3505 C CB . ASP B 2 120 ? -47.437 34.858 6.533 1.00 50.68 ? 120 ASP B CB 1 ATOM 3506 C CG . ASP B 2 120 ? -47.546 33.370 6.846 1.00 51.10 ? 120 ASP B CG 1 ATOM 3507 O OD1 . ASP B 2 120 ? -47.268 32.532 5.951 1.00 52.42 ? 120 ASP B OD1 1 ATOM 3508 O OD2 . ASP B 2 120 ? -47.924 33.033 7.989 1.00 51.51 ? 120 ASP B OD2 1 ATOM 3509 N N . LYS B 2 121 ? -45.981 37.575 5.800 1.00 49.92 ? 121 LYS B N 1 ATOM 3510 C CA . LYS B 2 121 ? -45.963 38.960 5.322 1.00 53.64 ? 121 LYS B CA 1 ATOM 3511 C C . LYS B 2 121 ? -45.248 39.093 3.983 1.00 54.03 ? 121 LYS B C 1 ATOM 3512 O O . LYS B 2 121 ? -45.741 39.766 3.087 1.00 57.19 ? 121 LYS B O 1 ATOM 3513 C CB . LYS B 2 121 ? -45.287 39.844 6.358 1.00 54.39 ? 121 LYS B CB 1 ATOM 3514 C CG . LYS B 2 121 ? -45.294 41.329 6.075 1.00 59.78 ? 121 LYS B CG 1 ATOM 3515 C CD . LYS B 2 121 ? -44.624 42.044 7.243 1.00 62.13 ? 121 LYS B CD 1 ATOM 3516 C CE . LYS B 2 121 ? -44.772 43.553 7.181 1.00 68.11 ? 121 LYS B CE 1 ATOM 3517 N NZ . LYS B 2 121 ? -43.887 44.141 6.139 1.00 71.93 ? 121 LYS B NZ 1 ATOM 3518 N N . VAL B 2 122 ? -44.090 38.449 3.847 1.00 51.23 ? 122 VAL B N 1 ATOM 3519 C CA . VAL B 2 122 ? -43.343 38.500 2.596 1.00 51.54 ? 122 VAL B CA 1 ATOM 3520 C C . VAL B 2 122 ? -44.040 37.693 1.522 1.00 53.13 ? 122 VAL B C 1 ATOM 3521 O O . VAL B 2 122 ? -44.208 38.161 0.396 1.00 55.19 ? 122 VAL B O 1 ATOM 3522 C CB . VAL B 2 122 ? -41.892 38.007 2.767 1.00 49.86 ? 122 VAL B CB 1 ATOM 3523 C CG1 . VAL B 2 122 ? -41.221 37.799 1.411 1.00 51.06 ? 122 VAL B CG1 1 ATOM 3524 C CG2 . VAL B 2 122 ? -41.107 39.012 3.595 1.00 50.00 ? 122 VAL B CG2 1 ATOM 3525 N N . ARG B 2 123 ? -44.441 36.477 1.870 1.00 52.95 ? 123 ARG B N 1 ATOM 3526 C CA . ARG B 2 123 ? -45.160 35.619 0.943 1.00 55.13 ? 123 ARG B CA 1 ATOM 3527 C C . ARG B 2 123 ? -46.339 36.346 0.313 1.00 58.91 ? 123 ARG B C 1 ATOM 3528 O O . ARG B 2 123 ? -46.534 36.273 -0.896 1.00 62.27 ? 123 ARG B O 1 ATOM 3529 C CB . ARG B 2 123 ? -45.671 34.389 1.675 1.00 55.72 ? 123 ARG B CB 1 ATOM 3530 C CG . ARG B 2 123 ? -46.284 33.332 0.776 1.00 58.55 ? 123 ARG B CG 1 ATOM 3531 C CD . ARG B 2 123 ? -46.770 32.156 1.604 1.00 59.46 ? 123 ARG B CD 1 ATOM 3532 N NE . ARG B 2 123 ? -47.733 32.564 2.625 1.00 60.62 ? 123 ARG B NE 1 ATOM 3533 C CZ . ARG B 2 123 ? -49.007 32.873 2.376 1.00 64.91 ? 123 ARG B CZ 1 ATOM 3534 N NH1 . ARG B 2 123 ? -49.504 32.837 1.133 1.00 67.09 ? 123 ARG B NH1 1 ATOM 3535 N NH2 . ARG B 2 123 ? -49.797 33.230 3.380 1.00 65.22 ? 123 ARG B NH2 1 ATOM 3536 N N . LEU B 2 124 ? -47.119 37.050 1.133 1.00 60.75 ? 124 LEU B N 1 ATOM 3537 C CA . LEU B 2 124 ? -48.326 37.742 0.648 1.00 66.49 ? 124 LEU B CA 1 ATOM 3538 C C . LEU B 2 124 ? -48.040 38.914 -0.298 1.00 68.69 ? 124 LEU B C 1 ATOM 3539 O O . LEU B 2 124 ? -48.916 39.332 -1.042 1.00 73.12 ? 124 LEU B O 1 ATOM 3540 C CB . LEU B 2 124 ? -49.189 38.221 1.821 1.00 67.71 ? 124 LEU B CB 1 ATOM 3541 C CG . LEU B 2 124 ? -49.816 37.086 2.640 1.00 67.57 ? 124 LEU B CG 1 ATOM 3542 C CD1 . LEU B 2 124 ? -50.149 37.520 4.068 1.00 68.15 ? 124 LEU B CD1 1 ATOM 3543 C CD2 . LEU B 2 124 ? -51.048 36.532 1.942 1.00 71.76 ? 124 LEU B CD2 1 ATOM 3544 N N . GLN B 2 125 ? -46.823 39.445 -0.263 1.00 66.91 ? 125 GLN B N 1 ATOM 3545 C CA . GLN B 2 125 ? -46.426 40.496 -1.185 1.00 68.97 ? 125 GLN B CA 1 ATOM 3546 C C . GLN B 2 125 ? -46.037 39.917 -2.511 1.00 68.56 ? 125 GLN B C 1 ATOM 3547 O O . GLN B 2 125 ? -46.497 40.368 -3.552 1.00 73.21 ? 125 GLN B O 1 ATOM 3548 C CB . GLN B 2 125 ? -45.231 41.254 -0.650 1.00 68.24 ? 125 GLN B CB 1 ATOM 3549 C CG . GLN B 2 125 ? -45.500 41.940 0.660 1.00 69.54 ? 125 GLN B CG 1 ATOM 3550 C CD . GLN B 2 125 ? -44.384 42.880 1.019 1.00 70.04 ? 125 GLN B CD 1 ATOM 3551 O OE1 . GLN B 2 125 ? -44.225 43.927 0.395 1.00 72.94 ? 125 GLN B OE1 1 ATOM 3552 N NE2 . GLN B 2 125 ? -43.594 42.511 2.022 1.00 68.50 ? 125 GLN B NE2 1 ATOM 3553 N N . LEU B 2 126 ? -45.157 38.931 -2.472 1.00 64.74 ? 126 LEU B N 1 ATOM 3554 C CA . LEU B 2 126 ? -44.636 38.358 -3.692 1.00 65.32 ? 126 LEU B CA 1 ATOM 3555 C C . LEU B 2 126 ? -45.745 37.678 -4.471 1.00 69.59 ? 126 LEU B C 1 ATOM 3556 O O . LEU B 2 126 ? -45.841 37.857 -5.676 1.00 74.20 ? 126 LEU B O 1 ATOM 3557 C CB . LEU B 2 126 ? -43.481 37.399 -3.394 1.00 61.86 ? 126 LEU B CB 1 ATOM 3558 C CG . LEU B 2 126 ? -42.321 38.046 -2.615 1.00 59.57 ? 126 LEU B CG 1 ATOM 3559 C CD1 . LEU B 2 126 ? -41.148 37.099 -2.483 1.00 56.99 ? 126 LEU B CD1 1 ATOM 3560 C CD2 . LEU B 2 126 ? -41.861 39.332 -3.280 1.00 62.47 ? 126 LEU B CD2 1 ATOM 3561 N N . ARG B 2 127 ? -46.613 36.936 -3.791 1.00 71.72 ? 127 ARG B N 1 ATOM 3562 C CA . ARG B 2 127 ? -47.714 36.236 -4.471 1.00 76.96 ? 127 ARG B CA 1 ATOM 3563 C C . ARG B 2 127 ? -47.156 35.299 -5.553 1.00 76.98 ? 127 ARG B C 1 ATOM 3564 O O . ARG B 2 127 ? -46.200 34.569 -5.298 1.00 74.11 ? 127 ARG B O 1 ATOM 3565 C CB . ARG B 2 127 ? -48.745 37.235 -5.041 1.00 82.16 ? 127 ARG B CB 1 ATOM 3566 C CG . ARG B 2 127 ? -49.473 38.040 -3.974 1.00 84.04 ? 127 ARG B CG 1 ATOM 3567 C CD . ARG B 2 127 ? -50.061 39.333 -4.517 1.00 89.27 ? 127 ARG B CD 1 ATOM 3568 N NE . ARG B 2 127 ? -51.081 39.107 -5.540 1.00 95.43 ? 127 ARG B NE 1 ATOM 3569 C CZ . ARG B 2 127 ? -51.787 40.078 -6.122 1.00 102.29 ? 127 ARG B CZ 1 ATOM 3570 N NH1 . ARG B 2 127 ? -51.583 41.349 -5.784 1.00 104.00 ? 127 ARG B NH1 1 ATOM 3571 N NH2 . ARG B 2 127 ? -52.706 39.784 -7.043 1.00 107.28 ? 127 ARG B NH2 1 ATOM 3572 N N . ASP B 2 128 ? -47.714 35.322 -6.758 1.00 80.93 ? 128 ASP B N 1 ATOM 3573 C CA . ASP B 2 128 ? -47.241 34.417 -7.800 1.00 82.45 ? 128 ASP B CA 1 ATOM 3574 C C . ASP B 2 128 ? -46.018 34.955 -8.572 1.00 79.60 ? 128 ASP B C 1 ATOM 3575 O O . ASP B 2 128 ? -45.630 34.371 -9.575 1.00 80.77 ? 128 ASP B O 1 ATOM 3576 C CB . ASP B 2 128 ? -48.389 34.048 -8.756 1.00 88.76 ? 128 ASP B CB 1 ATOM 3577 C CG . ASP B 2 128 ? -48.876 35.230 -9.581 1.00 94.01 ? 128 ASP B CG 1 ATOM 3578 O OD1 . ASP B 2 128 ? -48.729 36.382 -9.115 1.00 93.79 ? 128 ASP B OD1 1 ATOM 3579 O OD2 . ASP B 2 128 ? -49.403 35.006 -10.698 1.00 100.09 ? 128 ASP B OD2 1 ATOM 3580 N N . ASN B 2 129 ? -45.404 36.043 -8.103 1.00 77.38 ? 129 ASN B N 1 ATOM 3581 C CA . ASN B 2 129 ? -44.185 36.593 -8.735 1.00 76.34 ? 129 ASN B CA 1 ATOM 3582 C C . ASN B 2 129 ? -42.855 35.940 -8.313 1.00 72.89 ? 129 ASN B C 1 ATOM 3583 O O . ASN B 2 129 ? -41.786 36.359 -8.785 1.00 72.41 ? 129 ASN B O 1 ATOM 3584 C CB . ASN B 2 129 ? -44.096 38.106 -8.497 1.00 78.01 ? 129 ASN B CB 1 ATOM 3585 C CG . ASN B 2 129 ? -45.079 38.894 -9.351 1.00 84.27 ? 129 ASN B CG 1 ATOM 3586 O OD1 . ASN B 2 129 ? -46.191 38.438 -9.633 1.00 88.23 ? 129 ASN B OD1 1 ATOM 3587 N ND2 . ASN B 2 129 ? -44.669 40.083 -9.770 1.00 86.13 ? 129 ASN B ND2 1 ATOM 3588 N N . ALA B 2 130 ? -42.927 34.916 -7.454 1.00 69.93 ? 130 ALA B N 1 ATOM 3589 C CA . ALA B 2 130 ? -41.756 34.186 -6.965 1.00 65.99 ? 130 ALA B CA 1 ATOM 3590 C C . ALA B 2 130 ? -42.135 32.749 -6.606 1.00 66.13 ? 130 ALA B C 1 ATOM 3591 O O . ALA B 2 130 ? -43.281 32.500 -6.242 1.00 68.06 ? 130 ALA B O 1 ATOM 3592 C CB . ALA B 2 130 ? -41.200 34.888 -5.741 1.00 63.27 ? 130 ALA B CB 1 ATOM 3593 N N . LYS B 2 131 ? -41.180 31.817 -6.685 1.00 64.88 ? 131 LYS B N 1 ATOM 3594 C CA . LYS B 2 131 ? -41.406 30.423 -6.267 1.00 65.37 ? 131 LYS B CA 1 ATOM 3595 C C . LYS B 2 131 ? -41.171 30.235 -4.766 1.00 62.04 ? 131 LYS B C 1 ATOM 3596 O O . LYS B 2 131 ? -40.123 30.602 -4.247 1.00 58.96 ? 131 LYS B O 1 ATOM 3597 C CB . LYS B 2 131 ? -40.479 29.464 -7.013 1.00 68.84 ? 131 LYS B CB 1 ATOM 3598 C CG . LYS B 2 131 ? -40.553 29.572 -8.524 1.00 74.46 ? 131 LYS B CG 1 ATOM 3599 C CD . LYS B 2 131 ? -39.519 28.691 -9.223 1.00 79.11 ? 131 LYS B CD 1 ATOM 3600 C CE . LYS B 2 131 ? -38.640 29.483 -10.187 1.00 80.86 ? 131 LYS B CE 1 ATOM 3601 N NZ . LYS B 2 131 ? -38.222 28.683 -11.375 1.00 86.32 ? 131 LYS B NZ 1 ATOM 3602 N N . GLU B 2 132 ? -42.132 29.635 -4.072 1.00 61.55 ? 132 GLU B N 1 ATOM 3603 C CA . GLU B 2 132 ? -41.947 29.300 -2.670 1.00 58.72 ? 132 GLU B CA 1 ATOM 3604 C C . GLU B 2 132 ? -41.134 28.006 -2.586 1.00 60.97 ? 132 GLU B C 1 ATOM 3605 O O . GLU B 2 132 ? -41.619 26.930 -2.941 1.00 64.18 ? 132 GLU B O 1 ATOM 3606 C CB . GLU B 2 132 ? -43.297 29.148 -2.005 1.00 59.25 ? 132 GLU B CB 1 ATOM 3607 C CG . GLU B 2 132 ? -43.249 29.094 -0.489 1.00 57.16 ? 132 GLU B CG 1 ATOM 3608 C CD . GLU B 2 132 ? -44.635 29.131 0.142 1.00 57.88 ? 132 GLU B CD 1 ATOM 3609 O OE1 . GLU B 2 132 ? -45.631 29.108 -0.621 1.00 60.12 ? 132 GLU B OE1 1 ATOM 3610 O OE2 . GLU B 2 132 ? -44.725 29.189 1.395 1.00 55.67 ? 132 GLU B OE2 1 ATOM 3611 N N . LEU B 2 133 ? -39.889 28.112 -2.133 1.00 59.71 ? 133 LEU B N 1 ATOM 3612 C CA . LEU B 2 133 ? -38.964 26.976 -2.177 1.00 61.38 ? 133 LEU B CA 1 ATOM 3613 C C . LEU B 2 133 ? -39.227 25.884 -1.138 1.00 62.13 ? 133 LEU B C 1 ATOM 3614 O O . LEU B 2 133 ? -38.844 24.730 -1.355 1.00 64.62 ? 133 LEU B O 1 ATOM 3615 C CB . LEU B 2 133 ? -37.515 27.467 -2.075 1.00 61.54 ? 133 LEU B CB 1 ATOM 3616 C CG . LEU B 2 133 ? -36.800 27.728 -3.408 1.00 63.56 ? 133 LEU B CG 1 ATOM 3617 C CD1 . LEU B 2 133 ? -37.749 28.198 -4.498 1.00 64.15 ? 133 LEU B CD1 1 ATOM 3618 C CD2 . LEU B 2 133 ? -35.675 28.736 -3.229 1.00 62.82 ? 133 LEU B CD2 1 ATOM 3619 N N . GLY B 2 134 ? -39.868 26.242 -0.025 1.00 59.03 ? 134 GLY B N 1 ATOM 3620 C CA . GLY B 2 134 ? -40.189 25.282 1.026 1.00 60.13 ? 134 GLY B CA 1 ATOM 3621 C C . GLY B 2 134 ? -39.291 25.351 2.250 1.00 59.16 ? 134 GLY B C 1 ATOM 3622 O O . GLY B 2 134 ? -39.443 24.543 3.186 1.00 62.05 ? 134 GLY B O 1 ATOM 3623 N N . ASN B 2 135 ? -38.378 26.321 2.251 1.00 56.59 ? 135 ASN B N 1 ATOM 3624 C CA . ASN B 2 135 ? -37.323 26.429 3.262 1.00 56.16 ? 135 ASN B CA 1 ATOM 3625 C C . ASN B 2 135 ? -37.148 27.837 3.834 1.00 53.19 ? 135 ASN B C 1 ATOM 3626 O O . ASN B 2 135 ? -36.198 28.099 4.576 1.00 53.67 ? 135 ASN B O 1 ATOM 3627 C CB . ASN B 2 135 ? -35.999 26.006 2.642 1.00 59.34 ? 135 ASN B CB 1 ATOM 3628 C CG . ASN B 2 135 ? -35.595 26.902 1.498 1.00 59.69 ? 135 ASN B CG 1 ATOM 3629 O OD1 . ASN B 2 135 ? -36.324 27.821 1.127 1.00 58.34 ? 135 ASN B OD1 1 ATOM 3630 N ND2 . ASN B 2 135 ? -34.443 26.628 0.914 1.00 63.73 ? 135 ASN B ND2 1 ATOM 3631 N N . GLY B 2 136 ? -38.051 28.744 3.484 1.00 50.29 ? 136 GLY B N 1 ATOM 3632 C CA . GLY B 2 136 ? -37.983 30.097 3.970 1.00 47.48 ? 136 GLY B CA 1 ATOM 3633 C C . GLY B 2 136 ? -37.571 31.046 2.880 1.00 47.33 ? 136 GLY B C 1 ATOM 3634 O O . GLY B 2 136 ? -37.600 32.263 3.082 1.00 45.26 ? 136 GLY B O 1 ATOM 3635 N N . CYS B 2 137 ? -37.220 30.488 1.723 1.00 49.31 ? 137 CYS B N 1 ATOM 3636 C CA . CYS B 2 137 ? -36.740 31.272 0.608 1.00 50.81 ? 137 CYS B CA 1 ATOM 3637 C C . CYS B 2 137 ? -37.764 31.397 -0.509 1.00 51.70 ? 137 CYS B C 1 ATOM 3638 O O . CYS B 2 137 ? -38.575 30.500 -0.738 1.00 52.92 ? 137 CYS B O 1 ATOM 3639 C CB . CYS B 2 137 ? -35.472 30.654 0.048 1.00 53.60 ? 137 CYS B CB 1 ATOM 3640 S SG . CYS B 2 137 ? -34.123 30.583 1.235 1.00 55.63 ? 137 CYS B SG 1 ATOM 3641 N N . PHE B 2 138 ? -37.702 32.523 -1.205 1.00 51.36 ? 138 PHE B N 1 ATOM 3642 C CA . PHE B 2 138 ? -38.478 32.732 -2.396 1.00 53.45 ? 138 PHE B CA 1 ATOM 3643 C C . PHE B 2 138 ? -37.518 32.997 -3.529 1.00 55.90 ? 138 PHE B C 1 ATOM 3644 O O . PHE B 2 138 ? -36.703 33.892 -3.428 1.00 58.01 ? 138 PHE B O 1 ATOM 3645 C CB . PHE B 2 138 ? -39.400 33.931 -2.223 1.00 53.35 ? 138 PHE B CB 1 ATOM 3646 C CG . PHE B 2 138 ? -40.406 33.751 -1.129 1.00 52.82 ? 138 PHE B CG 1 ATOM 3647 C CD1 . PHE B 2 138 ? -41.626 33.140 -1.385 1.00 53.55 ? 138 PHE B CD1 1 ATOM 3648 C CD2 . PHE B 2 138 ? -40.126 34.179 0.159 1.00 51.21 ? 138 PHE B CD2 1 ATOM 3649 C CE1 . PHE B 2 138 ? -42.550 32.960 -0.376 1.00 53.70 ? 138 PHE B CE1 1 ATOM 3650 C CE2 . PHE B 2 138 ? -41.048 34.007 1.172 1.00 50.78 ? 138 PHE B CE2 1 ATOM 3651 C CZ . PHE B 2 138 ? -42.259 33.393 0.907 1.00 52.32 ? 138 PHE B CZ 1 ATOM 3652 N N . GLU B 2 139 ? -37.627 32.223 -4.601 1.00 57.88 ? 139 GLU B N 1 ATOM 3653 C CA . GLU B 2 139 ? -36.809 32.397 -5.776 1.00 60.30 ? 139 GLU B CA 1 ATOM 3654 C C . GLU B 2 139 ? -37.613 33.180 -6.801 1.00 62.17 ? 139 GLU B C 1 ATOM 3655 O O . GLU B 2 139 ? -38.689 32.745 -7.219 1.00 62.52 ? 139 GLU B O 1 ATOM 3656 C CB . GLU B 2 139 ? -36.418 31.034 -6.330 1.00 63.15 ? 139 GLU B CB 1 ATOM 3657 C CG . GLU B 2 139 ? -35.491 31.079 -7.530 1.00 66.10 ? 139 GLU B CG 1 ATOM 3658 C CD . GLU B 2 139 ? -35.205 29.693 -8.067 1.00 70.18 ? 139 GLU B CD 1 ATOM 3659 O OE1 . GLU B 2 139 ? -34.929 28.778 -7.258 1.00 70.96 ? 139 GLU B OE1 1 ATOM 3660 O OE2 . GLU B 2 139 ? -35.261 29.512 -9.303 1.00 74.19 ? 139 GLU B OE2 1 ATOM 3661 N N . PHE B 2 140 ? -37.082 34.334 -7.203 1.00 63.69 ? 140 PHE B N 1 ATOM 3662 C CA . PHE B 2 140 ? -37.817 35.281 -8.047 1.00 65.59 ? 140 PHE B CA 1 ATOM 3663 C C . PHE B 2 140 ? -37.871 34.837 -9.497 1.00 68.56 ? 140 PHE B C 1 ATOM 3664 O O . PHE B 2 140 ? -36.933 34.222 -10.001 1.00 69.22 ? 140 PHE B O 1 ATOM 3665 C CB . PHE B 2 140 ? -37.184 36.670 -7.986 1.00 64.97 ? 140 PHE B CB 1 ATOM 3666 C CG . PHE B 2 140 ? -37.334 37.349 -6.663 1.00 63.85 ? 140 PHE B CG 1 ATOM 3667 C CD1 . PHE B 2 140 ? -36.404 37.146 -5.652 1.00 63.93 ? 140 PHE B CD1 1 ATOM 3668 C CD2 . PHE B 2 140 ? -38.391 38.213 -6.430 1.00 64.56 ? 140 PHE B CD2 1 ATOM 3669 C CE1 . PHE B 2 140 ? -36.530 37.791 -4.430 1.00 63.02 ? 140 PHE B CE1 1 ATOM 3670 C CE2 . PHE B 2 140 ? -38.530 38.858 -5.210 1.00 63.78 ? 140 PHE B CE2 1 ATOM 3671 C CZ . PHE B 2 140 ? -37.599 38.647 -4.208 1.00 62.91 ? 140 PHE B CZ 1 ATOM 3672 N N . TYR B 2 141 ? -38.970 35.165 -10.172 1.00 71.46 ? 141 TYR B N 1 ATOM 3673 C CA . TYR B 2 141 ? -39.065 34.923 -11.615 1.00 75.42 ? 141 TYR B CA 1 ATOM 3674 C C . TYR B 2 141 ? -38.365 36.012 -12.410 1.00 76.17 ? 141 TYR B C 1 ATOM 3675 O O . TYR B 2 141 ? -38.045 35.814 -13.578 1.00 81.40 ? 141 TYR B O 1 ATOM 3676 C CB . TYR B 2 141 ? -40.519 34.821 -12.074 1.00 77.46 ? 141 TYR B CB 1 ATOM 3677 C CG . TYR B 2 141 ? -41.228 33.606 -11.550 1.00 77.89 ? 141 TYR B CG 1 ATOM 3678 C CD1 . TYR B 2 141 ? -40.767 32.330 -11.848 1.00 79.86 ? 141 TYR B CD1 1 ATOM 3679 C CD2 . TYR B 2 141 ? -42.350 33.728 -10.747 1.00 78.21 ? 141 TYR B CD2 1 ATOM 3680 C CE1 . TYR B 2 141 ? -41.412 31.207 -11.367 1.00 81.10 ? 141 TYR B CE1 1 ATOM 3681 C CE2 . TYR B 2 141 ? -43.003 32.614 -10.259 1.00 79.50 ? 141 TYR B CE2 1 ATOM 3682 C CZ . TYR B 2 141 ? -42.530 31.355 -10.573 1.00 81.64 ? 141 TYR B CZ 1 ATOM 3683 O OH . TYR B 2 141 ? -43.180 30.239 -10.094 1.00 84.52 ? 141 TYR B OH 1 ATOM 3684 N N . HIS B 2 142 ? -38.134 37.157 -11.780 1.00 108.70 ? 142 HIS B N 1 ATOM 3685 C CA . HIS B 2 142 ? -37.492 38.281 -12.438 1.00 107.66 ? 142 HIS B CA 1 ATOM 3686 C C . HIS B 2 142 ? -36.204 38.594 -11.713 1.00 102.71 ? 142 HIS B C 1 ATOM 3687 O O . HIS B 2 142 ? -36.053 38.275 -10.537 1.00 100.19 ? 142 HIS B O 1 ATOM 3688 C CB . HIS B 2 142 ? -38.414 39.499 -12.418 1.00 108.54 ? 142 HIS B CB 1 ATOM 3689 C CG . HIS B 2 142 ? -38.896 39.869 -11.050 1.00 105.12 ? 142 HIS B CG 1 ATOM 3690 N ND1 . HIS B 2 142 ? -38.207 40.729 -10.222 1.00 102.36 ? 142 HIS B ND1 1 ATOM 3691 C CD2 . HIS B 2 142 ? -39.993 39.479 -10.358 1.00 104.92 ? 142 HIS B CD2 1 ATOM 3692 C CE1 . HIS B 2 142 ? -38.863 40.858 -9.081 1.00 100.61 ? 142 HIS B CE1 1 ATOM 3693 N NE2 . HIS B 2 142 ? -39.949 40.110 -9.139 1.00 101.86 ? 142 HIS B NE2 1 ATOM 3694 N N . LYS B 2 143 ? -35.268 39.217 -12.412 1.00 102.54 ? 143 LYS B N 1 ATOM 3695 C CA . LYS B 2 143 ? -34.048 39.677 -11.768 1.00 99.85 ? 143 LYS B CA 1 ATOM 3696 C C . LYS B 2 143 ? -34.482 40.637 -10.661 1.00 96.31 ? 143 LYS B C 1 ATOM 3697 O O . LYS B 2 143 ? -35.432 41.401 -10.839 1.00 98.44 ? 143 LYS B O 1 ATOM 3698 C CB . LYS B 2 143 ? -33.128 40.379 -12.772 1.00 103.33 ? 143 LYS B CB 1 ATOM 3699 C CG . LYS B 2 143 ? -31.649 40.093 -12.582 1.00 103.23 ? 143 LYS B CG 1 ATOM 3700 C CD . LYS B 2 143 ? -30.790 41.029 -13.426 1.00 106.67 ? 143 LYS B CD 1 ATOM 3701 C CE . LYS B 2 143 ? -30.540 42.359 -12.729 1.00 106.27 ? 143 LYS B CE 1 ATOM 3702 N NZ . LYS B 2 143 ? -29.468 42.247 -11.695 1.00 104.12 ? 143 LYS B NZ 1 ATOM 3703 N N . CYS B 2 144 ? -33.820 40.567 -9.513 1.00 91.37 ? 144 CYS B N 1 ATOM 3704 C CA . CYS B 2 144 ? -34.206 41.361 -8.352 1.00 88.58 ? 144 CYS B CA 1 ATOM 3705 C C . CYS B 2 144 ? -32.933 41.906 -7.741 1.00 86.67 ? 144 CYS B C 1 ATOM 3706 O O . CYS B 2 144 ? -32.271 41.229 -6.965 1.00 83.86 ? 144 CYS B O 1 ATOM 3707 C CB . CYS B 2 144 ? -35.001 40.496 -7.349 1.00 86.91 ? 144 CYS B CB 1 ATOM 3708 S SG . CYS B 2 144 ? -35.729 41.360 -5.926 1.00 85.62 ? 144 CYS B SG 1 ATOM 3709 N N . ASP B 2 145 ? -32.579 43.125 -8.140 1.00 89.29 ? 145 ASP B N 1 ATOM 3710 C CA . ASP B 2 145 ? -31.365 43.794 -7.668 1.00 89.72 ? 145 ASP B CA 1 ATOM 3711 C C . ASP B 2 145 ? -31.556 44.265 -6.213 1.00 89.23 ? 145 ASP B C 1 ATOM 3712 O O . ASP B 2 145 ? -32.556 43.940 -5.588 1.00 88.07 ? 145 ASP B O 1 ATOM 3713 C CB . ASP B 2 145 ? -31.003 44.961 -8.609 1.00 94.02 ? 145 ASP B CB 1 ATOM 3714 C CG . ASP B 2 145 ? -32.116 45.996 -8.735 1.00 96.89 ? 145 ASP B CG 1 ATOM 3715 O OD1 . ASP B 2 145 ? -33.081 45.942 -7.951 1.00 96.10 ? 145 ASP B OD1 1 ATOM 3716 O OD2 . ASP B 2 145 ? -32.032 46.862 -9.629 1.00 101.11 ? 145 ASP B OD2 1 ATOM 3717 N N . ASN B 2 146 ? -30.616 45.042 -5.685 1.00 91.33 ? 146 ASN B N 1 ATOM 3718 C CA . ASN B 2 146 ? -30.694 45.510 -4.306 1.00 92.06 ? 146 ASN B CA 1 ATOM 3719 C C . ASN B 2 146 ? -31.877 46.440 -4.071 1.00 94.64 ? 146 ASN B C 1 ATOM 3720 O O . ASN B 2 146 ? -32.495 46.402 -3.016 1.00 94.89 ? 146 ASN B O 1 ATOM 3721 C CB . ASN B 2 146 ? -29.394 46.202 -3.908 1.00 94.72 ? 146 ASN B CB 1 ATOM 3722 C CG . ASN B 2 146 ? -28.196 45.272 -3.967 1.00 92.80 ? 146 ASN B CG 1 ATOM 3723 O OD1 . ASN B 2 146 ? -28.331 44.044 -4.006 1.00 88.98 ? 146 ASN B OD1 1 ATOM 3724 N ND2 . ASN B 2 146 ? -27.009 45.858 -3.977 1.00 96.00 ? 146 ASN B ND2 1 ATOM 3725 N N . GLU B 2 147 ? -32.195 47.265 -5.060 1.00 98.45 ? 147 GLU B N 1 ATOM 3726 C CA . GLU B 2 147 ? -33.412 48.081 -5.023 1.00 101.80 ? 147 GLU B CA 1 ATOM 3727 C C . GLU B 2 147 ? -34.661 47.212 -4.858 1.00 97.43 ? 147 GLU B C 1 ATOM 3728 O O . GLU B 2 147 ? -35.549 47.512 -4.057 1.00 98.29 ? 147 GLU B O 1 ATOM 3729 C CB . GLU B 2 147 ? -33.543 48.888 -6.316 1.00 107.16 ? 147 GLU B CB 1 ATOM 3730 C CG . GLU B 2 147 ? -32.504 49.982 -6.468 1.00 113.91 ? 147 GLU B CG 1 ATOM 3731 C CD . GLU B 2 147 ? -32.848 51.194 -5.638 1.00 120.51 ? 147 GLU B CD 1 ATOM 3732 O OE1 . GLU B 2 147 ? -33.621 52.049 -6.128 1.00 126.10 ? 147 GLU B OE1 1 ATOM 3733 O OE2 . GLU B 2 147 ? -32.349 51.281 -4.494 1.00 122.17 ? 147 GLU B OE2 1 ATOM 3734 N N . CYS B 2 148 ? -34.717 46.142 -5.645 1.00 93.19 ? 148 CYS B N 1 ATOM 3735 C CA . CYS B 2 148 ? -35.832 45.224 -5.640 1.00 90.04 ? 148 CYS B CA 1 ATOM 3736 C C . CYS B 2 148 ? -35.911 44.477 -4.306 1.00 87.43 ? 148 CYS B C 1 ATOM 3737 O O . CYS B 2 148 ? -36.992 44.312 -3.734 1.00 87.04 ? 148 CYS B O 1 ATOM 3738 C CB . CYS B 2 148 ? -35.674 44.240 -6.797 1.00 89.27 ? 148 CYS B CB 1 ATOM 3739 S SG . CYS B 2 148 ? -36.819 42.849 -6.758 1.00 87.32 ? 148 CYS B SG 1 ATOM 3740 N N . MET B 2 149 ? -34.762 44.029 -3.813 1.00 85.50 ? 149 MET B N 1 ATOM 3741 C CA . MET B 2 149 ? -34.711 43.342 -2.540 1.00 83.92 ? 149 MET B CA 1 ATOM 3742 C C . MET B 2 149 ? -35.151 44.302 -1.449 1.00 86.79 ? 149 MET B C 1 ATOM 3743 O O . MET B 2 149 ? -35.902 43.935 -0.550 1.00 86.93 ? 149 MET B O 1 ATOM 3744 C CB . MET B 2 149 ? -33.297 42.843 -2.240 1.00 83.11 ? 149 MET B CB 1 ATOM 3745 C CG . MET B 2 149 ? -32.744 41.804 -3.208 1.00 80.96 ? 149 MET B CG 1 ATOM 3746 S SD . MET B 2 149 ? -33.689 40.282 -3.276 1.00 78.69 ? 149 MET B SD 1 ATOM 3747 C CE . MET B 2 149 ? -32.530 39.156 -4.045 1.00 78.76 ? 149 MET B CE 1 ATOM 3748 N N . GLU B 2 150 ? -34.683 45.537 -1.536 1.00 90.55 ? 150 GLU B N 1 ATOM 3749 C CA . GLU B 2 150 ? -35.032 46.541 -0.551 1.00 95.25 ? 150 GLU B CA 1 ATOM 3750 C C . GLU B 2 150 ? -36.538 46.768 -0.473 1.00 95.75 ? 150 GLU B C 1 ATOM 3751 O O . GLU B 2 150 ? -37.073 46.990 0.613 1.00 98.19 ? 150 GLU B O 1 ATOM 3752 C CB . GLU B 2 150 ? -34.304 47.856 -0.863 1.00 100.67 ? 150 GLU B CB 1 ATOM 3753 C CG . GLU B 2 150 ? -34.581 49.002 0.100 1.00 106.62 ? 150 GLU B CG 1 ATOM 3754 C CD . GLU B 2 150 ? -34.323 48.645 1.551 1.00 107.49 ? 150 GLU B CD 1 ATOM 3755 O OE1 . GLU B 2 150 ? -33.685 47.611 1.821 1.00 104.64 ? 150 GLU B OE1 1 ATOM 3756 O OE2 . GLU B 2 150 ? -34.759 49.413 2.430 1.00 112.73 ? 150 GLU B OE2 1 ATOM 3757 N N . SER B 2 151 ? -37.215 46.708 -1.617 1.00 94.59 ? 151 SER B N 1 ATOM 3758 C CA . SER B 2 151 ? -38.650 46.964 -1.664 1.00 95.78 ? 151 SER B CA 1 ATOM 3759 C C . SER B 2 151 ? -39.432 45.838 -0.990 1.00 93.64 ? 151 SER B C 1 ATOM 3760 O O . SER B 2 151 ? -40.521 46.057 -0.457 1.00 95.91 ? 151 SER B O 1 ATOM 3761 C CB . SER B 2 151 ? -39.127 47.149 -3.106 1.00 96.53 ? 151 SER B CB 1 ATOM 3762 O OG . SER B 2 151 ? -39.149 45.923 -3.808 1.00 93.28 ? 151 SER B OG 1 ATOM 3763 N N . VAL B 2 152 ? -38.878 44.628 -1.021 1.00 90.50 ? 152 VAL B N 1 ATOM 3764 C CA . VAL B 2 152 ? -39.480 43.499 -0.328 1.00 88.20 ? 152 VAL B CA 1 ATOM 3765 C C . VAL B 2 152 ? -39.377 43.710 1.180 1.00 90.23 ? 152 VAL B C 1 ATOM 3766 O O . VAL B 2 152 ? -40.355 43.533 1.894 1.00 90.83 ? 152 VAL B O 1 ATOM 3767 C CB . VAL B 2 152 ? -38.839 42.167 -0.752 1.00 85.54 ? 152 VAL B CB 1 ATOM 3768 C CG1 . VAL B 2 152 ? -39.375 41.018 0.089 1.00 85.58 ? 152 VAL B CG1 1 ATOM 3769 C CG2 . VAL B 2 152 ? -39.117 41.905 -2.225 1.00 85.13 ? 152 VAL B CG2 1 ATOM 3770 N N . ARG B 2 153 ? -38.210 44.120 1.662 1.00 92.49 ? 153 ARG B N 1 ATOM 3771 C CA . ARG B 2 153 ? -38.051 44.424 3.084 1.00 96.81 ? 153 ARG B CA 1 ATOM 3772 C C . ARG B 2 153 ? -38.843 45.670 3.469 1.00 103.43 ? 153 ARG B C 1 ATOM 3773 O O . ARG B 2 153 ? -39.330 45.770 4.593 1.00 105.90 ? 153 ARG B O 1 ATOM 3774 C CB . ARG B 2 153 ? -36.587 44.633 3.450 1.00 97.33 ? 153 ARG B CB 1 ATOM 3775 C CG . ARG B 2 153 ? -35.674 43.478 3.099 1.00 93.54 ? 153 ARG B CG 1 ATOM 3776 C CD . ARG B 2 153 ? -34.280 43.701 3.658 1.00 95.25 ? 153 ARG B CD 1 ATOM 3777 N NE . ARG B 2 153 ? -33.262 43.433 2.649 1.00 92.61 ? 153 ARG B NE 1 ATOM 3778 C CZ . ARG B 2 153 ? -32.711 44.351 1.857 1.00 93.39 ? 153 ARG B CZ 1 ATOM 3779 N NH1 . ARG B 2 153 ? -33.045 45.631 1.950 1.00 96.31 ? 153 ARG B NH1 1 ATOM 3780 N NH2 . ARG B 2 153 ? -31.802 43.983 0.965 1.00 92.06 ? 153 ARG B NH2 1 ATOM 3781 N N . ASN B 2 154 ? -38.944 46.619 2.537 1.00 109.38 ? 154 ASN B N 1 ATOM 3782 C CA . ASN B 2 154 ? -39.764 47.830 2.704 1.00 117.41 ? 154 ASN B CA 1 ATOM 3783 C C . ASN B 2 154 ? -41.219 47.564 3.051 1.00 115.75 ? 154 ASN B C 1 ATOM 3784 O O . ASN B 2 154 ? -41.808 48.295 3.848 1.00 121.10 ? 154 ASN B O 1 ATOM 3785 C CB . ASN B 2 154 ? -39.788 48.648 1.407 1.00 123.60 ? 154 ASN B CB 1 ATOM 3786 C CG . ASN B 2 154 ? -38.800 49.787 1.400 1.00 137.55 ? 154 ASN B CG 1 ATOM 3787 O OD1 . ASN B 2 154 ? -38.216 50.133 2.423 1.00 144.05 ? 154 ASN B OD1 1 ATOM 3788 N ND2 . ASN B 2 154 ? -38.619 50.391 0.235 1.00 149.95 ? 154 ASN B ND2 1 ATOM 3789 N N . GLY B 2 155 ? -41.789 46.529 2.430 1.00 108.77 ? 155 GLY B N 1 ATOM 3790 C CA . GLY B 2 155 ? -43.234 46.338 2.366 1.00 106.45 ? 155 GLY B CA 1 ATOM 3791 C C . GLY B 2 155 ? -43.782 46.893 1.062 1.00 105.05 ? 155 GLY B C 1 ATOM 3792 O O . GLY B 2 155 ? -44.990 46.921 0.854 1.00 105.51 ? 155 GLY B O 1 ATOM 3793 N N . THR B 2 156 ? -42.876 47.280 0.167 1.00 104.02 ? 156 THR B N 1 ATOM 3794 C CA . THR B 2 156 ? -43.174 48.142 -0.980 1.00 105.47 ? 156 THR B CA 1 ATOM 3795 C C . THR B 2 156 ? -43.075 47.404 -2.306 1.00 102.40 ? 156 THR B C 1 ATOM 3796 O O . THR B 2 156 ? -43.227 48.013 -3.359 1.00 105.19 ? 156 THR B O 1 ATOM 3797 C CB . THR B 2 156 ? -42.177 49.321 -1.002 1.00 108.94 ? 156 THR B CB 1 ATOM 3798 O OG1 . THR B 2 156 ? -42.407 50.151 0.139 1.00 112.80 ? 156 THR B OG1 1 ATOM 3799 C CG2 . THR B 2 156 ? -42.307 50.178 -2.252 1.00 113.35 ? 156 THR B CG2 1 ATOM 3800 N N . TYR B 2 157 ? -42.826 46.099 -2.264 1.00 98.12 ? 157 TYR B N 1 ATOM 3801 C CA . TYR B 2 157 ? -42.577 45.336 -3.484 1.00 96.81 ? 157 TYR B CA 1 ATOM 3802 C C . TYR B 2 157 ? -43.712 45.533 -4.475 1.00 100.23 ? 157 TYR B C 1 ATOM 3803 O O . TYR B 2 157 ? -44.833 45.101 -4.232 1.00 99.86 ? 157 TYR B O 1 ATOM 3804 C CB . TYR B 2 157 ? -42.408 43.846 -3.174 1.00 93.27 ? 157 TYR B CB 1 ATOM 3805 C CG . TYR B 2 157 ? -42.294 42.978 -4.409 1.00 91.96 ? 157 TYR B CG 1 ATOM 3806 C CD1 . TYR B 2 157 ? -41.134 42.974 -5.180 1.00 91.41 ? 157 TYR B CD1 1 ATOM 3807 C CD2 . TYR B 2 157 ? -43.341 42.167 -4.807 1.00 92.11 ? 157 TYR B CD2 1 ATOM 3808 C CE1 . TYR B 2 157 ? -41.024 42.181 -6.311 1.00 91.16 ? 157 TYR B CE1 1 ATOM 3809 C CE2 . TYR B 2 157 ? -43.241 41.374 -5.937 1.00 92.85 ? 157 TYR B CE2 1 ATOM 3810 C CZ . TYR B 2 157 ? -42.083 41.383 -6.684 1.00 92.23 ? 157 TYR B CZ 1 ATOM 3811 O OH . TYR B 2 157 ? -41.994 40.589 -7.807 1.00 93.54 ? 157 TYR B OH 1 ATOM 3812 N N . ASP B 2 158 ? -43.420 46.198 -5.586 1.00 105.49 ? 158 ASP B N 1 ATOM 3813 C CA . ASP B 2 158 ? -44.461 46.538 -6.545 1.00 112.02 ? 158 ASP B CA 1 ATOM 3814 C C . ASP B 2 158 ? -44.766 45.332 -7.427 1.00 113.19 ? 158 ASP B C 1 ATOM 3815 O O . ASP B 2 158 ? -44.050 45.040 -8.390 1.00 114.54 ? 158 ASP B O 1 ATOM 3816 C CB . ASP B 2 158 ? -44.084 47.759 -7.390 1.00 117.03 ? 158 ASP B CB 1 ATOM 3817 C CG . ASP B 2 158 ? -45.282 48.367 -8.090 1.00 122.65 ? 158 ASP B CG 1 ATOM 3818 O OD1 . ASP B 2 158 ? -46.404 48.262 -7.553 1.00 122.83 ? 158 ASP B OD1 1 ATOM 3819 O OD2 . ASP B 2 158 ? -45.110 48.949 -9.178 1.00 128.58 ? 158 ASP B OD2 1 ATOM 3820 N N . TYR B 2 159 ? -45.840 44.638 -7.067 1.00 114.24 ? 159 TYR B N 1 ATOM 3821 C CA . TYR B 2 159 ? -46.239 43.405 -7.724 1.00 115.06 ? 159 TYR B CA 1 ATOM 3822 C C . TYR B 2 159 ? -46.668 43.629 -9.183 1.00 121.74 ? 159 TYR B C 1 ATOM 3823 O O . TYR B 2 159 ? -46.214 42.897 -10.066 1.00 123.57 ? 159 TYR B O 1 ATOM 3824 C CB . TYR B 2 159 ? -47.329 42.717 -6.890 1.00 114.05 ? 159 TYR B CB 1 ATOM 3825 C CG . TYR B 2 159 ? -48.092 41.628 -7.596 1.00 115.87 ? 159 TYR B CG 1 ATOM 3826 C CD1 . TYR B 2 159 ? -49.187 41.928 -8.406 1.00 120.20 ? 159 TYR B CD1 1 ATOM 3827 C CD2 . TYR B 2 159 ? -47.740 40.296 -7.434 1.00 114.15 ? 159 TYR B CD2 1 ATOM 3828 C CE1 . TYR B 2 159 ? -49.898 40.928 -9.046 1.00 123.01 ? 159 TYR B CE1 1 ATOM 3829 C CE2 . TYR B 2 159 ? -48.448 39.292 -8.068 1.00 117.32 ? 159 TYR B CE2 1 ATOM 3830 C CZ . TYR B 2 159 ? -49.522 39.613 -8.872 1.00 121.37 ? 159 TYR B CZ 1 ATOM 3831 O OH . TYR B 2 159 ? -50.221 38.617 -9.501 1.00 125.31 ? 159 TYR B OH 1 ATOM 3832 N N . PRO B 2 160 ? -47.529 44.641 -9.449 1.00 127.74 ? 160 PRO B N 1 ATOM 3833 C CA . PRO B 2 160 ? -47.893 44.918 -10.858 1.00 134.24 ? 160 PRO B CA 1 ATOM 3834 C C . PRO B 2 160 ? -46.720 45.302 -11.781 1.00 135.69 ? 160 PRO B C 1 ATOM 3835 O O . PRO B 2 160 ? -46.837 45.150 -13.000 1.00 140.46 ? 160 PRO B O 1 ATOM 3836 C CB . PRO B 2 160 ? -48.898 46.079 -10.753 1.00 138.29 ? 160 PRO B CB 1 ATOM 3837 C CG . PRO B 2 160 ? -49.446 45.989 -9.371 1.00 134.96 ? 160 PRO B CG 1 ATOM 3838 C CD . PRO B 2 160 ? -48.330 45.455 -8.512 1.00 128.48 ? 160 PRO B CD 1 ATOM 3839 N N . GLN B 2 161 ? -45.619 45.801 -11.215 1.00 132.26 ? 161 GLN B N 1 ATOM 3840 C CA . GLN B 2 161 ? -44.429 46.126 -12.006 1.00 133.18 ? 161 GLN B CA 1 ATOM 3841 C C . GLN B 2 161 ? -43.797 44.861 -12.577 1.00 129.57 ? 161 GLN B C 1 ATOM 3842 O O . GLN B 2 161 ? -43.477 44.807 -13.766 1.00 133.26 ? 161 GLN B O 1 ATOM 3843 C CB . GLN B 2 161 ? -43.395 46.879 -11.167 1.00 131.69 ? 161 GLN B CB 1 ATOM 3844 C CG . GLN B 2 161 ? -42.167 47.338 -11.947 1.00 134.68 ? 161 GLN B CG 1 ATOM 3845 C CD . GLN B 2 161 ? -41.112 47.990 -11.065 1.00 133.58 ? 161 GLN B CD 1 ATOM 3846 O OE1 . GLN B 2 161 ? -41.305 48.162 -9.859 1.00 131.37 ? 161 GLN B OE1 1 ATOM 3847 N NE2 . GLN B 2 161 ? -39.987 48.360 -11.669 1.00 135.91 ? 161 GLN B NE2 1 ATOM 3848 N N . TYR B 2 162 ? -43.609 43.855 -11.727 1.00 121.76 ? 162 TYR B N 1 ATOM 3849 C CA . TYR B 2 162 ? -43.024 42.598 -12.163 1.00 119.10 ? 162 TYR B CA 1 ATOM 3850 C C . TYR B 2 162 ? -44.119 41.561 -12.388 1.00 119.92 ? 162 TYR B C 1 ATOM 3851 O O . TYR B 2 162 ? -44.107 40.837 -13.379 1.00 121.72 ? 162 TYR B O 1 ATOM 3852 C CB . TYR B 2 162 ? -42.020 42.093 -11.133 1.00 114.06 ? 162 TYR B CB 1 ATOM 3853 C CG . TYR B 2 162 ? -40.969 43.102 -10.684 1.00 112.79 ? 162 TYR B CG 1 ATOM 3854 C CD1 . TYR B 2 162 ? -39.890 43.443 -11.503 1.00 114.20 ? 162 TYR B CD1 1 ATOM 3855 C CD2 . TYR B 2 162 ? -41.040 43.693 -9.421 1.00 110.26 ? 162 TYR B CD2 1 ATOM 3856 C CE1 . TYR B 2 162 ? -38.927 44.352 -11.079 1.00 113.36 ? 162 TYR B CE1 1 ATOM 3857 C CE2 . TYR B 2 162 ? -40.084 44.602 -8.992 1.00 109.65 ? 162 TYR B CE2 1 ATOM 3858 C CZ . TYR B 2 162 ? -39.031 44.928 -9.817 1.00 111.12 ? 162 TYR B CZ 1 ATOM 3859 O OH . TYR B 2 162 ? -38.091 45.830 -9.371 1.00 110.85 ? 162 TYR B OH 1 HETATM 3860 C C1 . NAG C 3 . ? -30.422 18.544 31.907 1.00 75.75 ? 1322 NAG A C1 1 HETATM 3861 C C2 . NAG C 3 . ? -30.540 17.059 32.239 1.00 86.64 ? 1322 NAG A C2 1 HETATM 3862 C C3 . NAG C 3 . ? -29.933 16.685 33.595 1.00 91.06 ? 1322 NAG A C3 1 HETATM 3863 C C4 . NAG C 3 . ? -28.663 17.461 33.917 1.00 93.24 ? 1322 NAG A C4 1 HETATM 3864 C C5 . NAG C 3 . ? -28.867 18.943 33.644 1.00 86.63 ? 1322 NAG A C5 1 HETATM 3865 C C6 . NAG C 3 . ? -27.669 19.796 34.096 1.00 85.85 ? 1322 NAG A C6 1 HETATM 3866 C C7 . NAG C 3 . ? -32.556 16.039 31.262 1.00 85.55 ? 1322 NAG A C7 1 HETATM 3867 C C8 . NAG C 3 . ? -34.017 15.704 31.422 1.00 83.59 ? 1322 NAG A C8 1 HETATM 3868 N N2 . NAG C 3 . ? -31.950 16.684 32.265 1.00 88.26 ? 1322 NAG A N2 1 HETATM 3869 O O3 . NAG C 3 . ? -29.677 15.295 33.641 1.00 93.26 ? 1322 NAG A O3 1 HETATM 3870 O O4 . NAG C 3 . ? -28.392 17.314 35.287 1.00 109.05 ? 1322 NAG A O4 1 HETATM 3871 O O5 . NAG C 3 . ? -29.151 19.075 32.263 1.00 77.80 ? 1322 NAG A O5 1 HETATM 3872 O O6 . NAG C 3 . ? -26.661 19.903 33.117 1.00 82.40 ? 1322 NAG A O6 1 HETATM 3873 O O7 . NAG C 3 . ? -31.969 15.723 30.231 1.00 83.34 ? 1322 NAG A O7 1 HETATM 3874 C C1 . NAG D 3 . ? -27.544 16.187 35.578 1.00 119.50 ? 1323 NAG A C1 1 HETATM 3875 C C2 . NAG D 3 . ? -26.961 16.287 36.977 1.00 119.14 ? 1323 NAG A C2 1 HETATM 3876 C C3 . NAG D 3 . ? -25.839 15.261 37.087 1.00 124.31 ? 1323 NAG A C3 1 HETATM 3877 C C4 . NAG D 3 . ? -26.383 13.861 36.766 1.00 127.00 ? 1323 NAG A C4 1 HETATM 3878 C C5 . NAG D 3 . ? -27.377 13.826 35.585 1.00 127.33 ? 1323 NAG A C5 1 HETATM 3879 C C6 . NAG D 3 . ? -28.248 12.564 35.607 1.00 125.74 ? 1323 NAG A C6 1 HETATM 3880 C C7 . NAG D 3 . ? -27.446 18.627 37.597 1.00 105.66 ? 1323 NAG A C7 1 HETATM 3881 C C8 . NAG D 3 . ? -28.938 18.377 37.636 1.00 100.35 ? 1323 NAG A C8 1 HETATM 3882 N N2 . NAG D 3 . ? -26.573 17.652 37.298 1.00 113.53 ? 1323 NAG A N2 1 HETATM 3883 O O3 . NAG D 3 . ? -25.309 15.296 38.394 1.00 127.18 ? 1323 NAG A O3 1 HETATM 3884 O O4 . NAG D 3 . ? -25.305 12.990 36.481 1.00 126.55 ? 1323 NAG A O4 1 HETATM 3885 O O5 . NAG D 3 . ? -28.231 14.960 35.549 1.00 126.47 ? 1323 NAG A O5 1 HETATM 3886 O O6 . NAG D 3 . ? -29.517 12.810 35.038 1.00 121.07 ? 1323 NAG A O6 1 HETATM 3887 O O7 . NAG D 3 . ? -27.044 19.758 37.849 1.00 100.56 ? 1323 NAG A O7 1 HETATM 3888 C C1 . NAG E 3 . ? -45.615 59.547 89.065 1.00 76.21 ? 1324 NAG A C1 1 HETATM 3889 C C2 . NAG E 3 . ? -47.098 59.534 89.401 1.00 82.43 ? 1324 NAG A C2 1 HETATM 3890 C C3 . NAG E 3 . ? -47.830 60.474 88.461 1.00 86.58 ? 1324 NAG A C3 1 HETATM 3891 C C4 . NAG E 3 . ? -47.244 61.865 88.559 1.00 91.14 ? 1324 NAG A C4 1 HETATM 3892 C C5 . NAG E 3 . ? -45.759 61.826 88.220 1.00 89.82 ? 1324 NAG A C5 1 HETATM 3893 C C6 . NAG E 3 . ? -45.061 63.190 88.380 1.00 94.30 ? 1324 NAG A C6 1 HETATM 3894 C C7 . NAG E 3 . ? -48.416 57.543 90.063 1.00 85.25 ? 1324 NAG A C7 1 HETATM 3895 C C8 . NAG E 3 . ? -48.981 56.244 89.566 1.00 86.70 ? 1324 NAG A C8 1 HETATM 3896 N N2 . NAG E 3 . ? -47.703 58.244 89.169 1.00 83.25 ? 1324 NAG A N2 1 HETATM 3897 O O3 . NAG E 3 . ? -49.217 60.482 88.730 1.00 84.96 ? 1324 NAG A O3 1 HETATM 3898 O O4 . NAG E 3 . ? -47.970 62.695 87.685 1.00 101.42 ? 1324 NAG A O4 1 HETATM 3899 O O5 . NAG E 3 . ? -45.128 60.883 89.060 1.00 82.40 ? 1324 NAG A O5 1 HETATM 3900 O O6 . NAG E 3 . ? -44.008 63.185 89.331 1.00 88.75 ? 1324 NAG A O6 1 HETATM 3901 O O7 . NAG E 3 . ? -48.624 57.859 91.236 1.00 84.21 ? 1324 NAG A O7 1 HETATM 3902 C C1 . NAG F 3 . ? -48.493 63.800 88.432 1.00 112.88 ? 1325 NAG A C1 1 HETATM 3903 C C2 . NAG F 3 . ? -49.372 64.635 87.511 1.00 116.12 ? 1325 NAG A C2 1 HETATM 3904 C C3 . NAG F 3 . ? -50.240 65.653 88.264 1.00 120.23 ? 1325 NAG A C3 1 HETATM 3905 C C4 . NAG F 3 . ? -50.702 65.190 89.653 1.00 123.44 ? 1325 NAG A C4 1 HETATM 3906 C C5 . NAG F 3 . ? -49.574 64.449 90.395 1.00 122.81 ? 1325 NAG A C5 1 HETATM 3907 C C6 . NAG F 3 . ? -49.891 63.904 91.801 1.00 119.86 ? 1325 NAG A C6 1 HETATM 3908 C C7 . NAG F 3 . ? -47.624 64.731 85.788 1.00 118.96 ? 1325 NAG A C7 1 HETATM 3909 C C8 . NAG F 3 . ? -46.713 65.624 84.997 1.00 117.21 ? 1325 NAG A C8 1 HETATM 3910 N N2 . NAG F 3 . ? -48.437 65.339 86.660 1.00 118.76 ? 1325 NAG A N2 1 HETATM 3911 O O3 . NAG F 3 . ? -51.356 66.045 87.484 1.00 118.40 ? 1325 NAG A O3 1 HETATM 3912 O O4 . NAG F 3 . ? -51.126 66.338 90.361 1.00 126.33 ? 1325 NAG A O4 1 HETATM 3913 O O5 . NAG F 3 . ? -49.183 63.367 89.580 1.00 117.05 ? 1325 NAG A O5 1 HETATM 3914 O O6 . NAG F 3 . ? -51.265 63.925 92.124 1.00 120.59 ? 1325 NAG A O6 1 HETATM 3915 O O7 . NAG F 3 . ? -47.593 63.517 85.586 1.00 116.49 ? 1325 NAG A O7 1 HETATM 3916 C C1 . SIA G 4 . ? -23.057 29.673 96.254 1.00 86.83 ? 1326 SIA A C1 1 HETATM 3917 C C2 . SIA G 4 . ? -23.197 29.136 97.653 1.00 85.20 ? 1326 SIA A C2 1 HETATM 3918 C C3 . SIA G 4 . ? -22.301 29.982 98.551 1.00 82.09 ? 1326 SIA A C3 1 HETATM 3919 C C4 . SIA G 4 . ? -22.817 31.416 98.506 1.00 81.15 ? 1326 SIA A C4 1 HETATM 3920 C C5 . SIA G 4 . ? -24.255 31.424 98.976 1.00 79.68 ? 1326 SIA A C5 1 HETATM 3921 C C6 . SIA G 4 . ? -25.091 30.518 98.086 1.00 76.63 ? 1326 SIA A C6 1 HETATM 3922 C C7 . SIA G 4 . ? -26.554 30.486 98.472 1.00 74.52 ? 1326 SIA A C7 1 HETATM 3923 C C8 . SIA G 4 . ? -27.259 29.271 97.896 1.00 75.65 ? 1326 SIA A C8 1 HETATM 3924 C C9 . SIA G 4 . ? -28.770 29.470 97.912 1.00 73.55 ? 1326 SIA A C9 1 HETATM 3925 C C10 . SIA G 4 . ? -25.758 33.290 99.357 1.00 86.11 ? 1326 SIA A C10 1 HETATM 3926 C C11 . SIA G 4 . ? -26.101 34.713 99.029 1.00 86.28 ? 1326 SIA A C11 1 HETATM 3927 N N5 . SIA G 4 . ? -24.696 32.786 98.744 1.00 83.46 ? 1326 SIA A N5 1 HETATM 3928 O O1A . SIA G 4 . ? -21.903 29.839 95.793 1.00 87.71 ? 1326 SIA A O1A 1 HETATM 3929 O O1B . SIA G 4 . ? -24.097 29.932 95.614 1.00 89.52 ? 1326 SIA A O1B 1 HETATM 3930 O O4 . SIA G 4 . ? -22.029 32.282 99.320 1.00 80.53 ? 1326 SIA A O4 1 HETATM 3931 O O6 . SIA G 4 . ? -24.553 29.197 98.107 1.00 77.76 ? 1326 SIA A O6 1 HETATM 3932 O O7 . SIA G 4 . ? -26.661 30.487 99.887 1.00 70.10 ? 1326 SIA A O7 1 HETATM 3933 O O8 . SIA G 4 . ? -26.812 29.069 96.551 1.00 75.61 ? 1326 SIA A O8 1 HETATM 3934 O O9 . SIA G 4 . ? -29.408 28.362 97.283 1.00 73.59 ? 1326 SIA A O9 1 HETATM 3935 O O10 . SIA G 4 . ? -26.418 32.633 100.137 1.00 82.95 ? 1326 SIA A O10 1 HETATM 3936 C C1 . GAL H 5 . ? -22.052 25.137 100.093 1.00 106.33 ? 1327 GAL A C1 1 HETATM 3937 C C2 . GAL H 5 . ? -21.805 26.135 98.977 1.00 101.48 ? 1327 GAL A C2 1 HETATM 3938 C C3 . GAL H 5 . ? -22.957 27.113 98.844 1.00 97.75 ? 1327 GAL A C3 1 HETATM 3939 C C4 . GAL H 5 . ? -24.283 26.387 98.800 1.00 98.59 ? 1327 GAL A C4 1 HETATM 3940 C C5 . GAL H 5 . ? -24.402 25.445 99.988 1.00 101.18 ? 1327 GAL A C5 1 HETATM 3941 C C6 . GAL H 5 . ? -25.730 24.690 99.996 1.00 94.64 ? 1327 GAL A C6 1 HETATM 3942 O O2 . GAL H 5 . ? -20.586 26.826 99.252 1.00 99.46 ? 1327 GAL A O2 1 HETATM 3943 O O3 . GAL H 5 . ? -22.758 27.790 97.618 1.00 90.36 ? 1327 GAL A O3 1 HETATM 3944 O O4 . GAL H 5 . ? -24.315 25.640 97.589 1.00 97.43 ? 1327 GAL A O4 1 HETATM 3945 O O5 . GAL H 5 . ? -23.324 24.513 99.935 1.00 108.23 ? 1327 GAL A O5 1 HETATM 3946 O O6 . GAL H 5 . ? -25.512 23.331 100.390 1.00 89.38 ? 1327 GAL A O6 1 HETATM 3947 C C1 . NAG I 3 . ? -19.844 20.760 101.861 1.00 120.12 ? 1328 NAG A C1 1 HETATM 3948 C C2 . NAG I 3 . ? -21.331 20.817 101.549 1.00 119.96 ? 1328 NAG A C2 1 HETATM 3949 C C3 . NAG I 3 . ? -21.613 21.925 100.550 1.00 120.66 ? 1328 NAG A C3 1 HETATM 3950 C C4 . NAG I 3 . ? -21.027 23.233 101.055 1.00 121.37 ? 1328 NAG A C4 1 HETATM 3951 C C5 . NAG I 3 . ? -19.586 23.084 101.549 1.00 121.73 ? 1328 NAG A C5 1 HETATM 3952 C C6 . NAG I 3 . ? -19.088 24.365 102.214 1.00 117.84 ? 1328 NAG A C6 1 HETATM 3953 C C7 . NAG I 3 . ? -21.798 18.463 101.683 1.00 115.80 ? 1328 NAG A C7 1 HETATM 3954 C C8 . NAG I 3 . ? -22.082 17.174 100.973 1.00 112.88 ? 1328 NAG A C8 1 HETATM 3955 N N2 . NAG I 3 . ? -21.622 19.540 100.920 1.00 118.76 ? 1328 NAG A N2 1 HETATM 3956 O O1 . NAG I 3 . ? -19.573 19.657 102.730 1.00 118.12 ? 1328 NAG A O1 1 HETATM 3957 O O3 . NAG I 3 . ? -23.023 22.084 100.366 1.00 119.26 ? 1328 NAG A O3 1 HETATM 3958 O O4 . NAG I 3 . ? -21.031 24.160 99.979 1.00 118.41 ? 1328 NAG A O4 1 HETATM 3959 O O5 . NAG I 3 . ? -19.477 21.996 102.469 1.00 121.20 ? 1328 NAG A O5 1 HETATM 3960 O O6 . NAG I 3 . ? -20.144 24.955 102.977 1.00 115.17 ? 1328 NAG A O6 1 HETATM 3961 O O7 . NAG I 3 . ? -21.730 18.522 102.900 1.00 116.13 ? 1328 NAG A O7 1 HETATM 3962 C C1 . NAG J 3 . ? -37.698 51.485 0.108 1.00 83.43 ? 1163 NAG B C1 1 HETATM 3963 C C2 . NAG J 3 . ? -38.302 52.897 0.091 1.00 94.68 ? 1163 NAG B C2 1 HETATM 3964 C C3 . NAG J 3 . ? -38.406 53.586 -1.273 1.00 101.84 ? 1163 NAG B C3 1 HETATM 3965 C C4 . NAG J 3 . ? -37.346 53.073 -2.245 1.00 109.53 ? 1163 NAG B C4 1 HETATM 3966 C C5 . NAG J 3 . ? -37.348 51.550 -2.233 1.00 101.84 ? 1163 NAG B C5 1 HETATM 3967 C C6 . NAG J 3 . ? -36.500 50.917 -3.346 1.00 101.23 ? 1163 NAG B C6 1 HETATM 3968 C C7 . NAG J 3 . ? -39.724 53.028 2.044 1.00 93.69 ? 1163 NAG B C7 1 HETATM 3969 C C8 . NAG J 3 . ? -41.112 53.001 2.624 1.00 91.35 ? 1163 NAG B C8 1 HETATM 3970 N N2 . NAG J 3 . ? -39.607 52.883 0.726 1.00 92.39 ? 1163 NAG B N2 1 HETATM 3971 O O3 . NAG J 3 . ? -38.247 54.979 -1.091 1.00 100.68 ? 1163 NAG B O3 1 HETATM 3972 O O4 . NAG J 3 . ? -37.519 53.631 -3.537 1.00 119.47 ? 1163 NAG B O4 1 HETATM 3973 O O5 . NAG J 3 . ? -36.825 51.224 -0.967 1.00 90.21 ? 1163 NAG B O5 1 HETATM 3974 O O6 . NAG J 3 . ? -35.265 50.446 -2.851 1.00 97.76 ? 1163 NAG B O6 1 HETATM 3975 O O7 . NAG J 3 . ? -38.751 53.175 2.784 1.00 90.93 ? 1163 NAG B O7 1 HETATM 3976 C C1 . NAG K 3 . ? -36.378 54.456 -3.843 1.00 123.17 ? 1164 NAG B C1 1 HETATM 3977 C C2 . NAG K 3 . ? -36.593 55.086 -5.215 1.00 122.47 ? 1164 NAG B C2 1 HETATM 3978 C C3 . NAG K 3 . ? -35.526 56.151 -5.527 1.00 128.33 ? 1164 NAG B C3 1 HETATM 3979 C C4 . NAG K 3 . ? -35.177 57.019 -4.315 1.00 130.34 ? 1164 NAG B C4 1 HETATM 3980 C C5 . NAG K 3 . ? -34.958 56.157 -3.068 1.00 127.32 ? 1164 NAG B C5 1 HETATM 3981 C C6 . NAG K 3 . ? -34.643 56.964 -1.813 1.00 121.84 ? 1164 NAG B C6 1 HETATM 3982 C C7 . NAG K 3 . ? -37.551 53.061 -6.218 1.00 112.61 ? 1164 NAG B C7 1 HETATM 3983 C C8 . NAG K 3 . ? -37.390 51.932 -7.192 1.00 108.75 ? 1164 NAG B C8 1 HETATM 3984 N N2 . NAG K 3 . ? -36.561 53.962 -6.139 1.00 117.78 ? 1164 NAG B N2 1 HETATM 3985 O O3 . NAG K 3 . ? -35.936 57.005 -6.576 1.00 130.97 ? 1164 NAG B O3 1 HETATM 3986 O O4 . NAG K 3 . ? -34.023 57.778 -4.616 1.00 132.84 ? 1164 NAG B O4 1 HETATM 3987 O O5 . NAG K 3 . ? -36.144 55.426 -2.842 1.00 130.31 ? 1164 NAG B O5 1 HETATM 3988 O O6 . NAG K 3 . ? -35.663 57.910 -1.595 1.00 115.70 ? 1164 NAG B O6 1 HETATM 3989 O O7 . NAG K 3 . ? -38.579 53.114 -5.545 1.00 112.44 ? 1164 NAG B O7 1 HETATM 3990 N N1 . EPE L 6 . ? -30.932 29.272 3.604 1.00 79.80 ? 1165 EPE B N1 1 HETATM 3991 C C2 . EPE L 6 . ? -31.010 28.629 2.312 1.00 82.49 ? 1165 EPE B C2 1 HETATM 3992 C C3 . EPE L 6 . ? -31.899 27.429 2.569 1.00 82.20 ? 1165 EPE B C3 1 HETATM 3993 N N4 . EPE L 6 . ? -31.140 26.520 3.423 1.00 80.30 ? 1165 EPE B N4 1 HETATM 3994 C C5 . EPE L 6 . ? -30.234 27.079 4.429 1.00 84.98 ? 1165 EPE B C5 1 HETATM 3995 C C6 . EPE L 6 . ? -30.763 28.474 4.815 1.00 84.75 ? 1165 EPE B C6 1 HETATM 3996 C C7 . EPE L 6 . ? -31.303 25.072 3.294 1.00 80.81 ? 1165 EPE B C7 1 HETATM 3997 C C8 . EPE L 6 . ? -31.163 24.632 1.828 1.00 82.91 ? 1165 EPE B C8 1 HETATM 3998 O O8 . EPE L 6 . ? -32.436 24.198 1.309 1.00 81.88 ? 1165 EPE B O8 1 HETATM 3999 C C9 . EPE L 6 . ? -31.047 30.709 3.681 1.00 86.60 ? 1165 EPE B C9 1 HETATM 4000 C C10 . EPE L 6 . ? -29.845 31.269 2.935 1.00 97.09 ? 1165 EPE B C10 1 HETATM 4001 S S . EPE L 6 . ? -28.473 31.192 3.876 1.00 112.87 ? 1165 EPE B S 1 HETATM 4002 O O1S . EPE L 6 . ? -27.264 31.371 3.033 1.00 114.38 ? 1165 EPE B O1S 1 HETATM 4003 O O2S . EPE L 6 . ? -28.359 29.898 4.593 1.00 113.56 ? 1165 EPE B O2S 1 HETATM 4004 O O3S . EPE L 6 . ? -28.525 32.303 4.855 1.00 117.75 ? 1165 EPE B O3S 1 HETATM 4005 O O . HOH M 7 . ? -34.117 34.700 -10.006 1.00 56.01 ? 2001 HOH A O 1 HETATM 4006 O O . HOH M 7 . ? -31.371 32.376 -7.151 1.00 61.51 ? 2002 HOH A O 1 HETATM 4007 O O . HOH M 7 . ? -29.321 39.715 -9.978 1.00 68.58 ? 2003 HOH A O 1 HETATM 4008 O O . HOH M 7 . ? -30.575 34.433 -0.248 1.00 57.80 ? 2004 HOH A O 1 HETATM 4009 O O . HOH M 7 . ? -32.737 28.451 -1.077 1.00 56.32 ? 2005 HOH A O 1 HETATM 4010 O O . HOH M 7 . ? -21.432 25.008 21.024 1.00 62.76 ? 2006 HOH A O 1 HETATM 4011 O O . HOH M 7 . ? -34.375 30.787 5.382 1.00 47.60 ? 2007 HOH A O 1 HETATM 4012 O O . HOH M 7 . ? -32.627 31.447 9.683 1.00 42.40 ? 2008 HOH A O 1 HETATM 4013 O O . HOH M 7 . ? -33.511 26.750 15.809 1.00 59.26 ? 2009 HOH A O 1 HETATM 4014 O O . HOH M 7 . ? -31.204 29.909 16.332 1.00 46.29 ? 2010 HOH A O 1 HETATM 4015 O O . HOH M 7 . ? -26.143 37.537 20.386 1.00 57.06 ? 2011 HOH A O 1 HETATM 4016 O O . HOH M 7 . ? -18.774 31.855 17.769 1.00 61.83 ? 2012 HOH A O 1 HETATM 4017 O O . HOH M 7 . ? -24.992 26.343 21.132 1.00 59.58 ? 2013 HOH A O 1 HETATM 4018 O O . HOH M 7 . ? -26.562 34.109 25.811 1.00 58.03 ? 2014 HOH A O 1 HETATM 4019 O O . HOH M 7 . ? -27.423 27.914 31.154 1.00 56.91 ? 2015 HOH A O 1 HETATM 4020 O O . HOH M 7 . ? -24.236 30.070 29.813 1.00 62.51 ? 2016 HOH A O 1 HETATM 4021 O O . HOH M 7 . ? -28.176 35.665 27.659 1.00 59.59 ? 2017 HOH A O 1 HETATM 4022 O O . HOH M 7 . ? -32.469 23.972 31.571 1.00 59.08 ? 2018 HOH A O 1 HETATM 4023 O O . HOH M 7 . ? -35.505 27.387 32.868 1.00 42.09 ? 2019 HOH A O 1 HETATM 4024 O O . HOH M 7 . ? -33.300 20.017 33.638 1.00 68.43 ? 2020 HOH A O 1 HETATM 4025 O O . HOH M 7 . ? -34.554 24.807 35.522 1.00 55.30 ? 2021 HOH A O 1 HETATM 4026 O O . HOH M 7 . ? -39.640 19.974 32.520 1.00 46.69 ? 2022 HOH A O 1 HETATM 4027 O O . HOH M 7 . ? -40.562 17.122 23.997 1.00 57.76 ? 2023 HOH A O 1 HETATM 4028 O O . HOH M 7 . ? -40.597 21.299 22.970 1.00 44.10 ? 2024 HOH A O 1 HETATM 4029 O O . HOH M 7 . ? -31.342 41.078 24.098 1.00 57.82 ? 2025 HOH A O 1 HETATM 4030 O O . HOH M 7 . ? -34.422 42.406 34.164 1.00 58.48 ? 2026 HOH A O 1 HETATM 4031 O O . HOH M 7 . ? -31.977 39.688 29.910 1.00 54.13 ? 2027 HOH A O 1 HETATM 4032 O O . HOH M 7 . ? -28.707 36.202 33.316 1.00 61.26 ? 2028 HOH A O 1 HETATM 4033 O O . HOH M 7 . ? -30.693 29.941 38.329 1.00 41.23 ? 2029 HOH A O 1 HETATM 4034 O O . HOH M 7 . ? -25.050 37.667 47.114 1.00 62.54 ? 2030 HOH A O 1 HETATM 4035 O O . HOH M 7 . ? -18.397 30.537 56.679 1.00 55.99 ? 2031 HOH A O 1 HETATM 4036 O O . HOH M 7 . ? -21.381 42.616 68.980 1.00 63.80 ? 2032 HOH A O 1 HETATM 4037 O O . HOH M 7 . ? -21.488 50.943 74.213 1.00 71.19 ? 2033 HOH A O 1 HETATM 4038 O O . HOH M 7 . ? -25.302 52.497 83.941 1.00 60.63 ? 2034 HOH A O 1 HETATM 4039 O O . HOH M 7 . ? -28.193 26.819 96.133 1.00 57.98 ? 2035 HOH A O 1 HETATM 4040 O O . HOH M 7 . ? -42.510 37.568 83.490 1.00 51.31 ? 2036 HOH A O 1 HETATM 4041 O O . HOH M 7 . ? -46.377 33.567 86.247 1.00 66.71 ? 2037 HOH A O 1 HETATM 4042 O O . HOH M 7 . ? -42.838 33.473 76.479 1.00 38.64 ? 2038 HOH A O 1 HETATM 4043 O O . HOH M 7 . ? -44.567 38.470 81.857 1.00 63.73 ? 2039 HOH A O 1 HETATM 4044 O O . HOH M 7 . ? -40.069 34.577 70.292 1.00 57.68 ? 2040 HOH A O 1 HETATM 4045 O O . HOH M 7 . ? -44.614 40.025 73.969 1.00 63.67 ? 2041 HOH A O 1 HETATM 4046 O O . HOH M 7 . ? -30.475 25.550 51.769 1.00 70.42 ? 2042 HOH A O 1 HETATM 4047 O O . HOH M 7 . ? -42.625 42.367 66.416 1.00 66.45 ? 2043 HOH A O 1 HETATM 4048 O O . HOH M 7 . ? -31.481 48.052 94.277 1.00 66.60 ? 2044 HOH A O 1 HETATM 4049 O O . HOH M 7 . ? -34.265 48.810 102.841 1.00 65.24 ? 2045 HOH A O 1 HETATM 4050 O O . HOH M 7 . ? -26.186 40.829 100.068 1.00 70.57 ? 2046 HOH A O 1 HETATM 4051 O O . HOH M 7 . ? -18.351 46.130 86.348 1.00 57.53 ? 2047 HOH A O 1 HETATM 4052 O O . HOH M 7 . ? -32.333 43.971 110.480 1.00 86.29 ? 2048 HOH A O 1 HETATM 4053 O O . HOH M 7 . ? -25.866 45.407 115.090 1.00 63.97 ? 2049 HOH A O 1 HETATM 4054 O O . HOH M 7 . ? -37.287 48.837 102.624 1.00 64.71 ? 2050 HOH A O 1 HETATM 4055 O O . HOH M 7 . ? -47.704 45.153 105.399 1.00 59.05 ? 2051 HOH A O 1 HETATM 4056 O O . HOH M 7 . ? -43.764 60.430 82.133 1.00 69.58 ? 2052 HOH A O 1 HETATM 4057 O O . HOH M 7 . ? -34.768 46.007 86.534 1.00 82.71 ? 2053 HOH A O 1 HETATM 4058 O O . HOH M 7 . ? -48.863 36.419 90.960 1.00 71.30 ? 2054 HOH A O 1 HETATM 4059 O O . HOH M 7 . ? -29.653 17.972 96.282 1.00 55.75 ? 2055 HOH A O 1 HETATM 4060 O O . HOH M 7 . ? -24.771 22.579 85.510 1.00 65.07 ? 2056 HOH A O 1 HETATM 4061 O O . HOH M 7 . ? -19.964 24.880 87.548 1.00 65.38 ? 2057 HOH A O 1 HETATM 4062 O O . HOH M 7 . ? -44.547 30.393 88.214 1.00 72.94 ? 2058 HOH A O 1 HETATM 4063 O O . HOH M 7 . ? -39.164 50.826 61.690 1.00 72.52 ? 2059 HOH A O 1 HETATM 4064 O O . HOH M 7 . ? -31.643 31.988 61.717 1.00 54.36 ? 2060 HOH A O 1 HETATM 4065 O O . HOH M 7 . ? -16.376 46.618 59.250 1.00 77.73 ? 2061 HOH A O 1 HETATM 4066 O O . HOH M 7 . ? -16.889 47.270 56.590 1.00 64.49 ? 2062 HOH A O 1 HETATM 4067 O O . HOH M 7 . ? -21.604 46.208 47.838 1.00 69.48 ? 2063 HOH A O 1 HETATM 4068 O O . HOH M 7 . ? -28.057 28.273 50.644 1.00 72.16 ? 2064 HOH A O 1 HETATM 4069 O O . HOH M 7 . ? -29.651 26.428 49.126 1.00 59.41 ? 2065 HOH A O 1 HETATM 4070 O O . HOH M 7 . ? -35.628 40.871 54.263 1.00 68.93 ? 2066 HOH A O 1 HETATM 4071 O O . HOH M 7 . ? -35.850 27.305 35.785 1.00 39.95 ? 2067 HOH A O 1 HETATM 4072 O O . HOH M 7 . ? -39.690 33.306 29.120 1.00 38.38 ? 2068 HOH A O 1 HETATM 4073 O O . HOH M 7 . ? -33.783 40.531 25.464 1.00 49.38 ? 2069 HOH A O 1 HETATM 4074 O O . HOH M 7 . ? -38.219 29.625 19.642 1.00 34.83 ? 2070 HOH A O 1 HETATM 4075 O O . HOH M 7 . ? -39.076 27.058 19.084 1.00 39.36 ? 2071 HOH A O 1 HETATM 4076 O O . HOH M 7 . ? -32.004 23.920 17.224 1.00 70.48 ? 2072 HOH A O 1 HETATM 4077 O O . HOH M 7 . ? -27.335 25.123 19.911 1.00 66.12 ? 2073 HOH A O 1 HETATM 4078 O O . HOH N 7 . ? -39.416 22.297 18.517 1.00 57.69 ? 2001 HOH B O 1 HETATM 4079 O O . HOH N 7 . ? -41.817 25.526 14.949 1.00 42.94 ? 2002 HOH B O 1 HETATM 4080 O O . HOH N 7 . ? -39.153 25.435 17.416 1.00 50.39 ? 2003 HOH B O 1 HETATM 4081 O O . HOH N 7 . ? -42.986 21.041 17.652 1.00 65.59 ? 2004 HOH B O 1 HETATM 4082 O O . HOH N 7 . ? -44.430 23.166 20.387 1.00 47.20 ? 2005 HOH B O 1 HETATM 4083 O O . HOH N 7 . ? -48.805 25.716 13.213 1.00 51.00 ? 2006 HOH B O 1 HETATM 4084 O O . HOH N 7 . ? -42.906 22.973 10.325 1.00 48.39 ? 2007 HOH B O 1 HETATM 4085 O O . HOH N 7 . ? -36.235 21.566 10.892 1.00 48.51 ? 2008 HOH B O 1 HETATM 4086 O O . HOH N 7 . ? -32.215 27.353 7.552 1.00 57.61 ? 2009 HOH B O 1 HETATM 4087 O O . HOH N 7 . ? -28.897 27.261 9.547 1.00 53.73 ? 2010 HOH B O 1 HETATM 4088 O O . HOH N 7 . ? -25.615 32.549 8.896 1.00 58.19 ? 2011 HOH B O 1 HETATM 4089 O O . HOH N 7 . ? -21.408 28.578 17.271 1.00 71.34 ? 2012 HOH B O 1 HETATM 4090 O O . HOH N 7 . ? -31.471 43.570 19.019 1.00 73.63 ? 2013 HOH B O 1 HETATM 4091 O O . HOH N 7 . ? -30.539 40.445 18.976 1.00 48.61 ? 2014 HOH B O 1 HETATM 4092 O O . HOH N 7 . ? -30.766 41.340 2.989 1.00 56.64 ? 2015 HOH B O 1 HETATM 4093 O O . HOH N 7 . ? -24.335 35.750 2.346 1.00 60.32 ? 2016 HOH B O 1 HETATM 4094 O O . HOH N 7 . ? -25.815 44.122 0.652 0.50 38.06 ? 2017 HOH B O 1 HETATM 4095 O O . HOH N 7 . ? -50.702 29.275 21.578 0.33 41.26 ? 2018 HOH B O 1 HETATM 4096 O O . HOH N 7 . ? -43.980 40.948 10.737 1.00 57.61 ? 2019 HOH B O 1 HETATM 4097 O O . HOH N 7 . ? -38.472 47.099 9.780 1.00 61.69 ? 2020 HOH B O 1 HETATM 4098 O O . HOH N 7 . ? -44.239 42.805 13.669 1.00 68.47 ? 2021 HOH B O 1 HETATM 4099 O O . HOH N 7 . ? -39.227 47.181 25.768 1.00 78.11 ? 2022 HOH B O 1 HETATM 4100 O O . HOH N 7 . ? -35.167 41.190 27.430 1.00 48.33 ? 2023 HOH B O 1 HETATM 4101 O O . HOH N 7 . ? -44.510 44.562 33.470 1.00 62.00 ? 2024 HOH B O 1 HETATM 4102 O O . HOH N 7 . ? -39.731 44.513 36.903 1.00 70.96 ? 2025 HOH B O 1 HETATM 4103 O O . HOH N 7 . ? -49.350 40.037 43.081 1.00 59.57 ? 2026 HOH B O 1 HETATM 4104 O O . HOH N 7 . ? -49.372 38.732 45.890 1.00 60.96 ? 2027 HOH B O 1 HETATM 4105 O O . HOH N 7 . ? -43.721 34.989 59.066 1.00 64.12 ? 2028 HOH B O 1 HETATM 4106 O O . HOH N 7 . ? -40.119 31.254 62.584 1.00 66.35 ? 2029 HOH B O 1 HETATM 4107 O O . HOH N 7 . ? -40.728 27.053 64.644 1.00 49.13 ? 2030 HOH B O 1 HETATM 4108 O O . HOH N 7 . ? -45.909 22.602 55.528 1.00 71.36 ? 2031 HOH B O 1 HETATM 4109 O O . HOH N 7 . ? -47.129 24.047 51.112 1.00 46.41 ? 2032 HOH B O 1 HETATM 4110 O O . HOH N 7 . ? -47.175 30.741 38.879 1.00 46.52 ? 2033 HOH B O 1 HETATM 4111 O O . HOH N 7 . ? -50.701 29.273 44.059 0.33 33.49 ? 2034 HOH B O 1 HETATM 4112 O O . HOH N 7 . ? -38.722 26.310 36.493 1.00 37.65 ? 2035 HOH B O 1 HETATM 4113 O O . HOH N 7 . ? -42.402 26.264 23.565 1.00 39.94 ? 2036 HOH B O 1 HETATM 4114 O O . HOH N 7 . ? -46.637 32.216 22.774 1.00 44.84 ? 2037 HOH B O 1 HETATM 4115 O O . HOH N 7 . ? -49.223 29.253 28.803 1.00 59.11 ? 2038 HOH B O 1 HETATM 4116 O O . HOH N 7 . ? -52.544 31.823 22.891 1.00 47.91 ? 2039 HOH B O 1 HETATM 4117 O O . HOH N 7 . ? -45.094 24.838 22.590 1.00 42.51 ? 2040 HOH B O 1 HETATM 4118 O O . HOH N 7 . ? -46.342 36.730 17.479 1.00 57.67 ? 2041 HOH B O 1 HETATM 4119 O O . HOH N 7 . ? -43.496 39.061 12.765 1.00 53.12 ? 2042 HOH B O 1 HETATM 4120 O O . HOH N 7 . ? -44.760 41.051 17.864 1.00 50.43 ? 2043 HOH B O 1 HETATM 4121 O O . HOH N 7 . ? -48.890 34.528 9.626 1.00 44.84 ? 2044 HOH B O 1 HETATM 4122 O O . HOH N 7 . ? -47.892 40.276 12.174 1.00 59.09 ? 2045 HOH B O 1 HETATM 4123 O O . HOH N 7 . ? -39.789 28.774 1.140 1.00 51.43 ? 2046 HOH B O 1 HETATM 4124 O O . HOH N 7 . ? -47.582 41.997 3.064 1.00 48.05 ? 2047 HOH B O 1 HETATM 4125 O O . HOH N 7 . ? -52.673 32.756 3.448 1.00 58.94 ? 2048 HOH B O 1 HETATM 4126 O O . HOH N 7 . ? -51.920 31.204 0.257 1.00 51.86 ? 2049 HOH B O 1 HETATM 4127 O O . HOH N 7 . ? -48.449 42.672 -3.426 1.00 54.31 ? 2050 HOH B O 1 HETATM 4128 O O . HOH N 7 . ? -45.482 30.648 -5.773 1.00 60.86 ? 2051 HOH B O 1 HETATM 4129 O O . HOH N 7 . ? -44.270 28.312 -5.769 1.00 56.18 ? 2052 HOH B O 1 HETATM 4130 O O . HOH N 7 . ? -43.485 25.419 -1.206 1.00 73.38 ? 2053 HOH B O 1 HETATM 4131 O O . HOH N 7 . ? -29.149 43.901 2.990 1.00 54.68 ? 2054 HOH B O 1 HETATM 4132 O O . HOH N 7 . ? -42.270 44.922 -17.144 1.00 74.37 ? 2055 HOH B O 1 HETATM 4133 O O . HOH N 7 . ? -46.617 40.617 -14.407 1.00 63.20 ? 2056 HOH B O 1 HETATM 4134 O O . HOH N 7 . ? -27.909 27.965 -2.917 1.00 70.75 ? 2057 HOH B O 1 HETATM 4135 O O . HOH N 7 . ? -32.550 45.231 24.539 1.00 56.96 ? 2058 HOH B O 1 HETATM 4136 O O . HOH N 7 . ? -18.618 48.157 84.148 1.00 68.37 ? 2059 HOH B O 1 HETATM 4137 O O . HOH N 7 . ? -34.538 51.839 -11.629 1.00 80.05 ? 2060 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 ? 0.5881 0.8599 0.7770 -0.1772 0.0916 0.1127 1 ASP A N 2 C CA . ASP A 1 ? 0.6209 0.8597 0.7909 -0.1928 0.0856 0.1146 1 ASP A CA 3 C C . ASP A 1 ? 0.6051 0.8109 0.7786 -0.1725 0.0828 0.1103 1 ASP A C 4 O O . ASP A 1 ? 0.5825 0.7642 0.7568 -0.1547 0.0843 0.1075 1 ASP A O 5 C CB . ASP A 1 ? 0.6569 0.8492 0.7921 -0.2130 0.0834 0.1191 1 ASP A CB 6 C CG . ASP A 1 ? 0.6599 0.8777 0.7842 -0.2396 0.0858 0.1239 1 ASP A CG 7 O OD1 . ASP A 1 ? 0.6260 0.9027 0.7735 -0.2386 0.0899 0.1232 1 ASP A OD1 8 O OD2 . ASP A 1 ? 0.7207 0.8976 0.8097 -0.2610 0.0834 0.1283 1 ASP A OD2 9 N N . GLN A 2 ? 0.6268 0.8332 0.8009 -0.1773 0.0788 0.1099 2 GLN A N 10 C CA . GLN A 2 ? 0.6108 0.7884 0.7873 -0.1605 0.0759 0.1060 2 GLN A CA 11 C C . GLN A 2 ? 0.6025 0.7610 0.7655 -0.1740 0.0702 0.1071 2 GLN A C 12 O O . GLN A 2 ? 0.6113 0.7913 0.7693 -0.1956 0.0686 0.1101 2 GLN A O 13 C CB . GLN A 2 ? 0.6093 0.8170 0.8118 -0.1379 0.0788 0.1015 2 GLN A CB 14 C CG . GLN A 2 ? 0.6185 0.8756 0.8361 -0.1405 0.0787 0.1020 2 GLN A CG 15 C CD . GLN A 2 ? 0.6228 0.8950 0.8574 -0.1137 0.0809 0.0974 2 GLN A CD 16 O OE1 . GLN A 2 ? 0.6589 0.9380 0.8986 -0.1082 0.0782 0.0960 2 GLN A OE1 17 N NE2 . GLN A 2 ? 0.6149 0.8880 0.8546 -0.0972 0.0858 0.0949 2 GLN A NE2 18 N N . ILE A 3 ? 0.5778 0.6974 0.7334 -0.1619 0.0672 0.1042 3 ILE A N 19 C CA . ILE A 3 ? 0.5777 0.6777 0.7222 -0.1696 0.0619 0.1041 3 ILE A CA 20 C C . ILE A 3 ? 0.5501 0.6537 0.7131 -0.1485 0.0615 0.0991 3 ILE A C 21 O O . ILE A 3 ? 0.5424 0.6370 0.7128 -0.1297 0.0640 0.0955 3 ILE A O 22 C CB . ILE A 3 ? 0.6065 0.6495 0.7156 -0.1773 0.0577 0.1056 3 ILE A CB 23 C CG1 . ILE A 3 ? 0.6342 0.6595 0.7271 -0.1916 0.0522 0.1064 3 ILE A CG1 24 C CG2 . ILE A 3 ? 0.5955 0.6090 0.7026 -0.1534 0.0577 0.1015 3 ILE A CG2 25 C CD1 . ILE A 3 ? 0.6745 0.6447 0.7228 -0.2073 0.0480 0.1094 3 ILE A CD1 26 N N . CYS A 4 ? 0.5440 0.6620 0.7130 -0.1534 0.0586 0.0989 4 CYS A N 27 C CA . CYS A 4 ? 0.5224 0.6442 0.7066 -0.1350 0.0582 0.0946 4 CYS A CA 28 C C . CYS A 4 ? 0.5270 0.6206 0.6979 -0.1404 0.0527 0.0939 4 CYS A C 29 O O . CYS A 4 ? 0.5560 0.6407 0.7101 -0.1607 0.0490 0.0970 4 CYS A O 30 C CB . CYS A 4 ? 0.5090 0.6795 0.7144 -0.1298 0.0599 0.0945 4 CYS A CB 31 S SG . CYS A 4 ? 0.5214 0.7307 0.7402 -0.1232 0.0663 0.0953 4 CYS A SG 32 N N . ILE A 5 ? 0.5026 0.5815 0.6787 -0.1237 0.0522 0.0896 5 ILE A N 33 C CA . ILE A 5 ? 0.5062 0.5648 0.6736 -0.1260 0.0473 0.0883 5 ILE A CA 34 C C . ILE A 5 ? 0.4896 0.5778 0.6756 -0.1195 0.0472 0.0870 5 ILE A C 35 O O . ILE A 5 ? 0.4535 0.5571 0.6540 -0.1033 0.0509 0.0847 5 ILE A O 36 C CB . ILE A 5 ? 0.5058 0.5304 0.6643 -0.1121 0.0465 0.0840 5 ILE A CB 37 C CG1 . ILE A 5 ? 0.5388 0.5364 0.6778 -0.1132 0.0466 0.0850 5 ILE A CG1 38 C CG2 . ILE A 5 ? 0.5067 0.5112 0.6552 -0.1139 0.0414 0.0824 5 ILE A CG2 39 C CD1 . ILE A 5 ? 0.5877 0.5624 0.7002 -0.1324 0.0428 0.0894 5 ILE A CD1 40 N N . GLY A 6 ? 0.4905 0.5835 0.6719 -0.1321 0.0428 0.0886 6 GLY A N 41 C CA . GLY A 6 ? 0.4834 0.6034 0.6793 -0.1257 0.0417 0.0876 6 GLY A CA 42 C C . GLY A 6 ? 0.4950 0.6015 0.6807 -0.1364 0.0360 0.0875 6 GLY A C 43 O O . GLY A 6 ? 0.5399 0.6111 0.7048 -0.1476 0.0329 0.0879 6 GLY A O 44 N N . TYR A 7 ? 0.4766 0.6104 0.6743 -0.1318 0.0345 0.0871 7 TYR A N 45 C CA . TYR A 7 ? 0.4875 0.6122 0.6781 -0.1396 0.0293 0.0866 7 TYR A CA 46 C C . TYR A 7 ? 0.4934 0.6656 0.6939 -0.1479 0.0272 0.0886 7 TYR A C 47 O O . TYR A 7 ? 0.4529 0.6682 0.6686 -0.1404 0.0299 0.0896 7 TYR A O 48 C CB . TYR A 7 ? 0.4773 0.5800 0.6706 -0.1207 0.0292 0.0826 7 TYR A CB 49 C CG . TYR A 7 ? 0.4564 0.5808 0.6652 -0.0999 0.0328 0.0812 7 TYR A CG 50 C CD1 . TYR A 7 ? 0.4504 0.5682 0.6624 -0.0871 0.0380 0.0797 7 TYR A CD1 51 C CD2 . TYR A 7 ? 0.4500 0.5982 0.6661 -0.0927 0.0310 0.0813 7 TYR A CD2 52 C CE1 . TYR A 7 ? 0.4381 0.5672 0.6567 -0.0686 0.0413 0.0783 7 TYR A CE1 53 C CE2 . TYR A 7 ? 0.4540 0.6140 0.6766 -0.0717 0.0340 0.0801 7 TYR A CE2 54 C CZ . TYR A 7 ? 0.4443 0.5922 0.6664 -0.0602 0.0393 0.0786 7 TYR A CZ 55 O OH . TYR A 7 ? 0.4553 0.6084 0.6770 -0.0398 0.0422 0.0773 7 TYR A OH 56 N N . HIS A 8 ? 0.5188 0.6839 0.7094 -0.1620 0.0221 0.0887 8 HIS A N 57 C CA . HIS A 8 ? 0.5391 0.7499 0.7355 -0.1751 0.0191 0.0904 8 HIS A CA 58 C C . HIS A 8 ? 0.5109 0.7599 0.7271 -0.1526 0.0195 0.0892 8 HIS A C 59 O O . HIS A 8 ? 0.5127 0.7391 0.7312 -0.1325 0.0199 0.0868 8 HIS A O 60 C CB . HIS A 8 ? 0.5556 0.7409 0.7330 -0.1949 0.0135 0.0901 8 HIS A CB 61 C CG . HIS A 8 ? 0.5771 0.8094 0.7582 -0.2118 0.0100 0.0914 8 HIS A CG 62 N ND1 . HIS A 8 ? 0.5877 0.8646 0.7694 -0.2335 0.0106 0.0940 8 HIS A ND1 63 C CD2 . HIS A 8 ? 0.5782 0.8227 0.7617 -0.2118 0.0058 0.0902 8 HIS A CD2 64 C CE1 . HIS A 8 ? 0.5848 0.9029 0.7697 -0.2462 0.0069 0.0941 8 HIS A CE1 65 N NE2 . HIS A 8 ? 0.5752 0.8732 0.7612 -0.2327 0.0038 0.0920 8 HIS A NE2 66 N N . ALA A 9 ? 0.5132 0.8211 0.7407 -0.1560 0.0193 0.0908 9 ALA A N 67 C CA . ALA A 9 ? 0.5065 0.8533 0.7474 -0.1350 0.0182 0.0898 9 ALA A CA 68 C C . ALA A 9 ? 0.5141 0.9160 0.7579 -0.1547 0.0143 0.0912 9 ALA A C 69 O O . ALA A 9 ? 0.5504 0.9641 0.7866 -0.1844 0.0136 0.0930 9 ALA A O 70 C CB . ALA A 9 ? 0.4939 0.8656 0.7463 -0.1084 0.0231 0.0894 9 ALA A CB 71 N N . ASN A 10 ? 0.5050 0.9400 0.7569 -0.1393 0.0115 0.0903 10 ASN A N 72 C CA . ASN A 10 ? 0.5129 1.0064 0.7683 -0.1569 0.0073 0.0910 10 ASN A CA 73 C C . ASN A 10 ? 0.5234 1.0620 0.7903 -0.1269 0.0057 0.0899 10 ASN A C 74 O O . ASN A 10 ? 0.5149 1.0320 0.7831 -0.0942 0.0080 0.0889 10 ASN A O 75 C CB . ASN A 10 ? 0.5313 0.9918 0.7710 -0.1855 0.0025 0.0909 10 ASN A CB 76 C CG . ASN A 10 ? 0.5360 0.9646 0.7737 -0.1679 -0.0005 0.0891 10 ASN A CG 77 O OD1 . ASN A 10 ? 0.5429 0.9704 0.7886 -0.1357 0.0008 0.0881 10 ASN A OD1 78 N ND2 . ASN A 10 ? 0.5592 0.9587 0.7827 -0.1896 -0.0046 0.0886 10 ASN A ND2 79 N N . ASN A 11 ? 0.5599 1.1589 0.8317 -0.1381 0.0015 0.0901 11 ASN A N 80 C CA . ASN A 11 ? 0.5872 1.2385 0.8684 -0.1074 -0.0004 0.0891 11 ASN A CA 81 C C . ASN A 11 ? 0.5835 1.2065 0.8584 -0.0965 -0.0050 0.0881 11 ASN A C 82 O O . ASN A 11 ? 0.5929 1.2585 0.8719 -0.0746 -0.0079 0.0875 11 ASN A O 83 C CB . ASN A 11 ? 0.6090 1.3556 0.9007 -0.1212 -0.0022 0.0893 11 ASN A CB 84 C CG . ASN A 11 ? 0.6564 1.4198 0.9422 -0.1624 -0.0071 0.0895 11 ASN A CG 85 O OD1 . ASN A 11 ? 0.7088 1.4177 0.9835 -0.1722 -0.0101 0.0893 11 ASN A OD1 86 N ND2 . ASN A 11 ? 0.6685 1.5078 0.9594 -0.1882 -0.0077 0.0897 11 ASN A ND2 87 N N . SER A 12 ? 0.5851 1.1374 0.8489 -0.1102 -0.0056 0.0878 12 SER A N 88 C CA . SER A 12 ? 0.5841 1.1052 0.8409 -0.1032 -0.0097 0.0868 12 SER A CA 89 C C . SER A 12 ? 0.6063 1.1118 0.8613 -0.0619 -0.0086 0.0861 12 SER A C 90 O O . SER A 12 ? 0.6089 1.0855 0.8614 -0.0432 -0.0038 0.0858 12 SER A O 91 C CB . SER A 12 ? 0.5570 1.0035 0.8006 -0.1222 -0.0098 0.0861 12 SER A CB 92 O OG . SER A 12 ? 0.5189 0.9327 0.7562 -0.1104 -0.0126 0.0848 12 SER A OG 93 N N . THR A 13 ? 0.6205 1.1414 0.8733 -0.0493 -0.0131 0.0857 13 THR A N 94 C CA . THR A 13 ? 0.6319 1.1288 0.8753 -0.0122 -0.0127 0.0852 13 THR A CA 95 C C . THR A 13 ? 0.6433 1.0765 0.8748 -0.0152 -0.0143 0.0842 13 THR A C 96 O O . THR A 13 ? 0.6607 1.0651 0.8799 0.0111 -0.0139 0.0839 13 THR A O 97 C CB . THR A 13 ? 0.6556 1.2151 0.9010 0.0100 -0.0170 0.0855 13 THR A CB 98 O OG1 . THR A 13 ? 0.6831 1.2796 0.9351 -0.0164 -0.0225 0.0854 13 THR A OG1 99 C CG2 . THR A 13 ? 0.6541 1.2765 0.9077 0.0272 -0.0148 0.0858 13 THR A CG2 100 N N . GLU A 14 ? 0.6355 1.0449 0.8671 -0.0466 -0.0159 0.0837 14 GLU A N 101 C CA . GLU A 14 ? 0.6510 1.0075 0.8718 -0.0497 -0.0178 0.0823 14 GLU A CA 102 C C . GLU A 14 ? 0.6190 0.9156 0.8294 -0.0327 -0.0130 0.0811 14 GLU A C 103 O O . GLU A 14 ? 0.6125 0.8919 0.8243 -0.0337 -0.0082 0.0809 14 GLU A O 104 C CB . GLU A 14 ? 0.7012 1.0377 0.9196 -0.0843 -0.0200 0.0814 14 GLU A CB 105 C CG . GLU A 14 ? 0.7566 1.1428 0.9788 -0.1068 -0.0253 0.0821 14 GLU A CG 106 C CD . GLU A 14 ? 0.8390 1.1974 1.0509 -0.1232 -0.0299 0.0805 14 GLU A CD 107 O OE1 . GLU A 14 ? 0.8446 1.1990 1.0542 -0.1064 -0.0324 0.0800 14 GLU A OE1 108 O OE2 . GLU A 14 ? 0.9415 1.2784 1.1442 -0.1523 -0.0311 0.0799 14 GLU A OE2 109 N N . GLN A 15 ? 0.5969 0.8632 0.7956 -0.0191 -0.0143 0.0802 15 GLN A N 110 C CA . GLN A 15 ? 0.5790 0.7921 0.7639 -0.0043 -0.0099 0.0789 15 GLN A CA 111 C C . GLN A 15 ? 0.5561 0.7257 0.7330 -0.0168 -0.0111 0.0767 15 GLN A C 112 O O . GLN A 15 ? 0.5607 0.7391 0.7380 -0.0254 -0.0160 0.0766 15 GLN A O 113 C CB . GLN A 15 ? 0.6067 0.8208 0.7773 0.0270 -0.0097 0.0799 15 GLN A CB 114 C CG . GLN A 15 ? 0.6295 0.8843 0.8040 0.0460 -0.0081 0.0815 15 GLN A CG 115 C CD . GLN A 15 ? 0.6606 0.9166 0.8155 0.0807 -0.0091 0.0825 15 GLN A CD 116 O OE1 . GLN A 15 ? 0.6825 0.9463 0.8294 0.1033 -0.0062 0.0829 15 GLN A OE1 117 N NE2 . GLN A 15 ? 0.6843 0.9303 0.8282 0.0865 -0.0133 0.0828 15 GLN A NE2 118 N N . VAL A 16 ? 0.5318 0.6575 0.7011 -0.0179 -0.0065 0.0745 16 VAL A N 119 C CA . VAL A 16 ? 0.5155 0.6029 0.6762 -0.0271 -0.0069 0.0717 16 VAL A CA 120 C C . VAL A 16 ? 0.5174 0.5680 0.6614 -0.0136 -0.0022 0.0703 16 VAL A C 121 O O . VAL A 16 ? 0.5154 0.5626 0.6553 -0.0023 0.0019 0.0709 16 VAL A O 122 C CB . VAL A 16 ? 0.4976 0.5705 0.6637 -0.0473 -0.0061 0.0696 16 VAL A CB 123 C CG1 . VAL A 16 ? 0.5016 0.6053 0.6776 -0.0638 -0.0102 0.0713 16 VAL A CG1 124 C CG2 . VAL A 16 ? 0.4924 0.5507 0.6590 -0.0447 -0.0001 0.0686 16 VAL A CG2 125 N N . ASP A 17 ? 0.5294 0.5521 0.6614 -0.0161 -0.0030 0.0682 17 ASP A N 126 C CA . ASP A 17 ? 0.5550 0.5396 0.6671 -0.0097 0.0017 0.0662 17 ASP A CA 127 C C . ASP A 17 ? 0.5343 0.4987 0.6479 -0.0246 0.0050 0.0621 17 ASP A C 128 O O . ASP A 17 ? 0.5129 0.4825 0.6363 -0.0372 0.0024 0.0603 17 ASP A O 129 C CB . ASP A 17 ? 0.5899 0.5572 0.6844 -0.0042 -0.0007 0.0663 17 ASP A CB 130 C CG . ASP A 17 ? 0.6162 0.5983 0.7023 0.0157 -0.0036 0.0700 17 ASP A CG 131 O OD1 . ASP A 17 ? 0.6385 0.6260 0.7196 0.0310 -0.0012 0.0718 17 ASP A OD1 132 O OD2 . ASP A 17 ? 0.6365 0.6248 0.7192 0.0177 -0.0084 0.0710 17 ASP A OD2 133 N N . THR A 18 ? 0.5568 0.4977 0.6573 -0.0219 0.0108 0.0603 18 THR A N 134 C CA . THR A 18 ? 0.5470 0.4706 0.6442 -0.0338 0.0145 0.0556 18 THR A CA 135 C C . THR A 18 ? 0.5882 0.4807 0.6586 -0.0327 0.0181 0.0538 18 THR A C 136 O O . THR A 18 ? 0.6242 0.5039 0.6771 -0.0218 0.0174 0.0564 18 THR A O 137 C CB . THR A 18 ? 0.5217 0.4495 0.6267 -0.0355 0.0189 0.0548 18 THR A CB 138 O OG1 . THR A 18 ? 0.5358 0.4486 0.6249 -0.0258 0.0234 0.0558 18 THR A OG1 139 C CG2 . THR A 18 ? 0.5036 0.4589 0.6291 -0.0358 0.0160 0.0577 18 THR A CG2 140 N N . ILE A 19 ? 0.6176 0.4982 0.6816 -0.0441 0.0222 0.0491 19 ILE A N 141 C CA . ILE A 19 ? 0.6483 0.5003 0.6842 -0.0495 0.0261 0.0466 19 ILE A CA 142 C C . ILE A 19 ? 0.6726 0.4997 0.6848 -0.0428 0.0309 0.0481 19 ILE A C 143 O O . ILE A 19 ? 0.6871 0.4830 0.6679 -0.0407 0.0324 0.0488 19 ILE A O 144 C CB . ILE A 19 ? 0.6597 0.5164 0.6976 -0.0652 0.0294 0.0405 19 ILE A CB 145 C CG1 . ILE A 19 ? 0.6598 0.5349 0.7139 -0.0694 0.0246 0.0384 19 ILE A CG1 146 C CG2 . ILE A 19 ? 0.6878 0.5185 0.6946 -0.0760 0.0344 0.0373 19 ILE A CG2 147 C CD1 . ILE A 19 ? 0.6875 0.5511 0.7271 -0.0723 0.0223 0.0381 19 ILE A CD1 148 N N . MET A 20 ? 0.6715 0.5086 0.6948 -0.0398 0.0335 0.0484 20 MET A N 149 C CA . MET A 20 ? 0.7055 0.5178 0.7051 -0.0335 0.0384 0.0490 20 MET A CA 150 C C . MET A 20 ? 0.7248 0.5399 0.7229 -0.0117 0.0361 0.0542 20 MET A C 151 O O . MET A 20 ? 0.7351 0.5227 0.7055 -0.0014 0.0394 0.0551 20 MET A O 152 C CB . MET A 20 ? 0.7010 0.5232 0.7114 -0.0417 0.0430 0.0461 20 MET A CB 153 C CG . MET A 20 ? 0.7103 0.5316 0.7162 -0.0613 0.0464 0.0402 20 MET A CG 154 S SD . MET A 20 ? 0.7281 0.5609 0.7425 -0.0678 0.0518 0.0370 20 MET A SD 155 C CE . MET A 20 ? 0.7487 0.6021 0.7704 -0.0863 0.0528 0.0302 20 MET A CE 156 N N . GLU A 21 ? 0.7029 0.5521 0.7283 -0.0047 0.0306 0.0571 21 GLU A N 157 C CA . GLU A 21 ? 0.7263 0.5916 0.7551 0.0152 0.0283 0.0614 21 GLU A CA 158 C C . GLU A 21 ? 0.7293 0.6248 0.7753 0.0203 0.0214 0.0642 21 GLU A C 159 O O . GLU A 21 ? 0.6767 0.5938 0.7462 0.0065 0.0183 0.0633 21 GLU A O 160 C CB . GLU A 21 ? 0.7161 0.6050 0.7657 0.0155 0.0306 0.0616 21 GLU A CB 161 C CG . GLU A 21 ? 0.7481 0.6521 0.7953 0.0374 0.0299 0.0651 21 GLU A CG 162 C CD . GLU A 21 ? 0.7544 0.6808 0.8203 0.0363 0.0328 0.0652 21 GLU A CD 163 O OE1 . GLU A 21 ? 0.7418 0.6701 0.8221 0.0187 0.0349 0.0628 21 GLU A OE1 164 O OE2 . GLU A 21 ? 0.7450 0.6887 0.8102 0.0542 0.0327 0.0675 21 GLU A OE2 165 N N . LYS A 22 ? 0.7343 0.6304 0.7655 0.0412 0.0190 0.0674 22 LYS A N 166 C CA . LYS A 22 ? 0.7393 0.6664 0.7829 0.0477 0.0124 0.0701 22 LYS A CA 167 C C . LYS A 22 ? 0.7088 0.6818 0.7711 0.0608 0.0101 0.0729 22 LYS A C 168 O O . LYS A 22 ? 0.7077 0.6808 0.7644 0.0728 0.0136 0.0733 22 LYS A O 169 C CB . LYS A 22 ? 0.8069 0.7046 0.8177 0.0624 0.0106 0.0714 22 LYS A CB 170 C CG . LYS A 22 ? 0.8521 0.7143 0.8480 0.0452 0.0117 0.0687 22 LYS A CG 171 C CD . LYS A 22 ? 0.9281 0.7556 0.8862 0.0591 0.0102 0.0704 22 LYS A CD 172 C CE . LYS A 22 ? 0.9461 0.7777 0.9099 0.0476 0.0059 0.0699 22 LYS A CE 173 N NZ . LYS A 22 ? 0.9748 0.7744 0.9018 0.0613 0.0038 0.0721 22 LYS A NZ 174 N N . ASN A 23 ? 0.7118 0.7261 0.7956 0.0570 0.0045 0.0745 23 ASN A N 175 C CA . ASN A 23 ? 0.7337 0.8007 0.8350 0.0670 0.0019 0.0769 23 ASN A CA 176 C C . ASN A 23 ? 0.6737 0.7578 0.7924 0.0590 0.0057 0.0765 23 ASN A C 177 O O . ASN A 23 ? 0.6712 0.7814 0.7913 0.0750 0.0067 0.0779 23 ASN A O 178 C CB . ASN A 23 ? 0.8171 0.8872 0.8954 0.0998 0.0009 0.0790 23 ASN A CB 179 C CG . ASN A 23 ? 0.9039 0.9700 0.9677 0.1097 -0.0041 0.0801 23 ASN A CG 180 O OD1 . ASN A 23 ? 0.8848 0.9607 0.9625 0.0915 -0.0078 0.0797 23 ASN A OD1 181 N ND2 . ASN A 23 ? 1.0519 1.1015 1.0847 0.1399 -0.0046 0.0816 23 ASN A ND2 182 N N . VAL A 24 ? 0.6398 0.7105 0.7704 0.0357 0.0077 0.0745 24 VAL A N 183 C CA . VAL A 24 ? 0.5998 0.6855 0.7467 0.0256 0.0108 0.0743 24 VAL A CA 184 C C . VAL A 24 ? 0.5650 0.7009 0.7347 0.0133 0.0067 0.0762 24 VAL A C 185 O O . VAL A 24 ? 0.5711 0.7127 0.7475 -0.0029 0.0026 0.0760 24 VAL A O 186 C CB . VAL A 24 ? 0.5800 0.6331 0.7280 0.0071 0.0139 0.0712 24 VAL A CB 187 C CG1 . VAL A 24 ? 0.5615 0.6295 0.7245 -0.0027 0.0165 0.0714 24 VAL A CG1 188 C CG2 . VAL A 24 ? 0.5990 0.6074 0.7235 0.0143 0.0185 0.0689 24 VAL A CG2 189 N N . THR A 25 ? 0.5409 0.7124 0.7199 0.0196 0.0081 0.0778 25 THR A N 190 C CA . THR A 25 ? 0.5218 0.7447 0.7194 0.0052 0.0047 0.0796 25 THR A CA 191 C C . THR A 25 ? 0.5050 0.7178 0.7114 -0.0210 0.0060 0.0791 25 THR A C 192 O O . THR A 25 ? 0.5200 0.7140 0.7257 -0.0205 0.0107 0.0784 25 THR A O 193 C CB . THR A 25 ? 0.5241 0.7947 0.7277 0.0216 0.0060 0.0813 25 THR A CB 194 O OG1 . THR A 25 ? 0.5606 0.8318 0.7492 0.0523 0.0053 0.0815 25 THR A OG1 195 C CG2 . THR A 25 ? 0.5161 0.8477 0.7365 0.0051 0.0019 0.0828 25 THR A CG2 196 N N . VAL A 26 ? 0.4946 0.7183 0.7060 -0.0435 0.0016 0.0794 26 VAL A N 197 C CA . VAL A 26 ? 0.4853 0.6900 0.6971 -0.0675 0.0021 0.0789 26 VAL A CA 198 C C . VAL A 26 ? 0.4890 0.7346 0.7073 -0.0887 -0.0006 0.0810 26 VAL A C 199 O O . VAL A 26 ? 0.5008 0.7889 0.7242 -0.0891 -0.0041 0.0822 26 VAL A O 200 C CB . VAL A 26 ? 0.4834 0.6460 0.6851 -0.0777 -0.0002 0.0766 26 VAL A CB 201 C CG1 . VAL A 26 ? 0.4884 0.6115 0.6825 -0.0621 0.0034 0.0740 26 VAL A CG1 202 C CG2 . VAL A 26 ? 0.4907 0.6686 0.6910 -0.0824 -0.0059 0.0768 26 VAL A CG2 203 N N . THR A 27 ? 0.4954 0.7282 0.7110 -0.1074 0.0008 0.0815 27 THR A N 204 C CA . THR A 27 ? 0.4991 0.7651 0.7153 -0.1324 -0.0011 0.0835 27 THR A CA 205 C C . THR A 27 ? 0.5144 0.7769 0.7207 -0.1538 -0.0069 0.0832 27 THR A C 206 O O . THR A 27 ? 0.5346 0.8422 0.7433 -0.1701 -0.0098 0.0845 27 THR A O 207 C CB . THR A 27 ? 0.5077 0.7493 0.7167 -0.1473 0.0018 0.0842 27 THR A CB 208 O OG1 . THR A 27 ? 0.5136 0.6966 0.7070 -0.1519 0.0010 0.0822 27 THR A OG1 209 C CG2 . THR A 27 ? 0.5003 0.7482 0.7191 -0.1281 0.0076 0.0845 27 THR A CG2 210 N N . HIS A 28 ? 0.5205 0.7320 0.7144 -0.1543 -0.0084 0.0810 28 HIS A N 211 C CA . HIS A 28 ? 0.5412 0.7404 0.7220 -0.1727 -0.0139 0.0801 28 HIS A CA 212 C C . HIS A 28 ? 0.5515 0.7180 0.7289 -0.1573 -0.0153 0.0774 28 HIS A C 213 O O . HIS A 28 ? 0.5588 0.6952 0.7367 -0.1399 -0.0119 0.0757 28 HIS A O 214 C CB . HIS A 28 ? 0.5598 0.7208 0.7181 -0.1980 -0.0149 0.0800 28 HIS A CB 215 C CG . HIS A 28 ? 0.5730 0.7580 0.7300 -0.2161 -0.0130 0.0827 28 HIS A CG 216 N ND1 . HIS A 28 ? 0.5630 0.7479 0.7280 -0.2054 -0.0078 0.0838 28 HIS A ND1 217 C CD2 . HIS A 28 ? 0.5905 0.8028 0.7382 -0.2459 -0.0153 0.0846 28 HIS A CD2 218 C CE1 . HIS A 28 ? 0.5723 0.7828 0.7337 -0.2267 -0.0071 0.0862 28 HIS A CE1 219 N NE2 . HIS A 28 ? 0.5923 0.8204 0.7426 -0.2525 -0.0115 0.0868 28 HIS A NE2 220 N N . ALA A 29 ? 0.5765 0.7503 0.7490 -0.1657 -0.0203 0.0768 29 ALA A N 221 C CA . ALA A 29 ? 0.5913 0.7385 0.7601 -0.1528 -0.0220 0.0743 29 ALA A CA 222 C C . ALA A 29 ? 0.6101 0.7536 0.7663 -0.1722 -0.0279 0.0733 29 ALA A C 223 O O . ALA A 29 ? 0.6382 0.8036 0.7885 -0.1959 -0.0306 0.0747 29 ALA A O 224 C CB . ALA A 29 ? 0.5849 0.7584 0.7673 -0.1276 -0.0210 0.0750 29 ALA A CB 225 N N . GLN A 30 ? 0.6056 0.7213 0.7553 -0.1640 -0.0298 0.0707 30 GLN A N 226 C CA . GLN A 30 ? 0.6368 0.7443 0.7726 -0.1809 -0.0353 0.0693 30 GLN A CA 227 C C . GLN A 30 ? 0.6294 0.7400 0.7701 -0.1657 -0.0374 0.0681 30 GLN A C 228 O O . GLN A 30 ? 0.6179 0.6969 0.7562 -0.1502 -0.0355 0.0658 30 GLN A O 229 C CB . GLN A 30 ? 0.6712 0.7239 0.7823 -0.1931 -0.0361 0.0666 30 GLN A CB 230 C CG . GLN A 30 ? 0.7086 0.7516 0.7990 -0.2166 -0.0419 0.0655 30 GLN A CG 231 C CD . GLN A 30 ? 0.7478 0.7306 0.8067 -0.2254 -0.0432 0.0626 30 GLN A CD 232 O OE1 . GLN A 30 ? 0.7769 0.7349 0.8242 -0.2281 -0.0407 0.0629 30 GLN A OE1 233 N NE2 . GLN A 30 ? 0.7665 0.7243 0.8088 -0.2286 -0.0472 0.0595 30 GLN A NE2 234 N N . ASP A 31 ? 0.6264 0.7781 0.7728 -0.1710 -0.0415 0.0695 31 ASP A N 235 C CA . ASP A 31 ? 0.6265 0.7822 0.7743 -0.1590 -0.0444 0.0686 31 ASP A CA 236 C C . ASP A 31 ? 0.6365 0.7541 0.7653 -0.1741 -0.0481 0.0654 31 ASP A C 237 O O . ASP A 31 ? 0.6608 0.7729 0.7755 -0.1990 -0.0510 0.0648 31 ASP A O 238 C CB . ASP A 31 ? 0.6245 0.8413 0.7835 -0.1590 -0.0478 0.0711 31 ASP A CB 239 C CG . ASP A 31 ? 0.6322 0.8557 0.7922 -0.1422 -0.0507 0.0708 31 ASP A CG 240 O OD1 . ASP A 31 ? 0.6489 0.8294 0.8014 -0.1318 -0.0496 0.0689 31 ASP A OD1 241 O OD2 . ASP A 31 ? 0.6438 0.9178 0.8111 -0.1390 -0.0542 0.0725 31 ASP A OD2 242 N N . ILE A 32 ? 0.6154 0.7044 0.7405 -0.1596 -0.0479 0.0630 32 ILE A N 243 C CA . ILE A 32 ? 0.6311 0.6833 0.7375 -0.1697 -0.0511 0.0593 32 ILE A CA 244 C C . ILE A 32 ? 0.6294 0.6903 0.7363 -0.1633 -0.0547 0.0586 32 ILE A C 245 O O . ILE A 32 ? 0.6398 0.6713 0.7323 -0.1676 -0.0571 0.0552 32 ILE A O 246 C CB . ILE A 32 ? 0.6362 0.6415 0.7332 -0.1601 -0.0473 0.0559 32 ILE A CB 247 C CG1 . ILE A 32 ? 0.6210 0.6281 0.7313 -0.1367 -0.0425 0.0562 32 ILE A CG1 248 C CG2 . ILE A 32 ? 0.6418 0.6305 0.7307 -0.1699 -0.0452 0.0561 32 ILE A CG2 249 C CD1 . ILE A 32 ? 0.6308 0.6007 0.7317 -0.1281 -0.0397 0.0517 32 ILE A CD1 250 N N . LEU A 33 ? 0.6119 0.7129 0.7332 -0.1514 -0.0553 0.0616 33 LEU A N 251 C CA . LEU A 33 ? 0.6095 0.7210 0.7304 -0.1428 -0.0588 0.0616 33 LEU A CA 252 C C . LEU A 33 ? 0.6290 0.7898 0.7543 -0.1550 -0.0642 0.0635 33 LEU A C 253 O O . LEU A 33 ? 0.6294 0.8346 0.7669 -0.1527 -0.0639 0.0664 33 LEU A O 254 C CB . LEU A 33 ? 0.5918 0.7065 0.7198 -0.1155 -0.0553 0.0635 33 LEU A CB 255 C CG . LEU A 33 ? 0.5870 0.7057 0.7105 -0.1028 -0.0583 0.0640 33 LEU A CG 256 C CD1 . LEU A 33 ? 0.5878 0.6660 0.6986 -0.1085 -0.0589 0.0600 33 LEU A CD1 257 C CD2 . LEU A 33 ? 0.5840 0.7026 0.7075 -0.0764 -0.0548 0.0666 33 LEU A CD2 258 N N . GLU A 34 ? 0.6477 0.8044 0.7627 -0.1675 -0.0692 0.0615 34 GLU A N 259 C CA . GLU A 34 ? 0.6598 0.8660 0.7777 -0.1808 -0.0747 0.0627 34 GLU A CA 260 C C . GLU A 34 ? 0.6491 0.8868 0.7760 -0.1568 -0.0766 0.0648 34 GLU A C 261 O O . GLU A 34 ? 0.6568 0.8690 0.7766 -0.1465 -0.0777 0.0636 34 GLU A O 262 C CB . GLU A 34 ? 0.6831 0.8679 0.7820 -0.2070 -0.0793 0.0593 34 GLU A CB 263 C CG . GLU A 34 ? 0.6970 0.9344 0.7965 -0.2256 -0.0851 0.0599 34 GLU A CG 264 C CD . GLU A 34 ? 0.7010 0.9895 0.8105 -0.2382 -0.0845 0.0624 34 GLU A CD 265 O OE1 . GLU A 34 ? 0.7369 1.0090 0.8331 -0.2648 -0.0838 0.0614 34 GLU A OE1 266 O OE2 . GLU A 34 ? 0.6790 1.0223 0.8073 -0.2200 -0.0845 0.0652 34 GLU A OE2 267 N N . LYS A 35 ? 0.6417 0.9352 0.7818 -0.1470 -0.0772 0.0679 35 LYS A N 268 C CA . LYS A 35 ? 0.6422 0.9650 0.7866 -0.1189 -0.0791 0.0702 35 LYS A CA 269 C C . LYS A 35 ? 0.6584 1.0383 0.8052 -0.1267 -0.0860 0.0705 35 LYS A C 270 O O . LYS A 35 ? 0.6648 1.0678 0.8117 -0.1022 -0.0885 0.0723 35 LYS A O 271 C CB . LYS A 35 ? 0.6262 0.9718 0.7800 -0.0938 -0.0752 0.0733 35 LYS A CB 272 C CG . LYS A 35 ? 0.6165 0.9063 0.7640 -0.0742 -0.0690 0.0735 35 LYS A CG 273 C CD . LYS A 35 ? 0.6103 0.9195 0.7642 -0.0529 -0.0650 0.0760 35 LYS A CD 274 C CE . LYS A 35 ? 0.6056 0.8970 0.7658 -0.0665 -0.0598 0.0752 35 LYS A CE 275 N NZ . LYS A 35 ? 0.5949 0.9016 0.7601 -0.1002 -0.0617 0.0737 35 LYS A NZ 276 N N . THR A 36 ? 0.6679 1.0686 0.8130 -0.1604 -0.0892 0.0686 36 THR A N 277 C CA . THR A 36 ? 0.6951 1.1588 0.8428 -0.1712 -0.0956 0.0685 36 THR A CA 278 C C . THR A 36 ? 0.7202 1.1633 0.8531 -0.1994 -0.1002 0.0652 36 THR A C 279 O O . THR A 36 ? 0.7132 1.1010 0.8320 -0.2200 -0.0986 0.0627 36 THR A O 280 C CB . THR A 36 ? 0.6972 1.2295 0.8553 -0.1896 -0.0963 0.0691 36 THR A CB 281 O OG1 . THR A 36 ? 0.7063 1.2083 0.8543 -0.2254 -0.0944 0.0672 36 THR A OG1 282 C CG2 . THR A 36 ? 0.6842 1.2476 0.8568 -0.1597 -0.0925 0.0720 36 THR A CG2 283 N N . HIS A 37 ? 0.7372 1.2276 0.8715 -0.1984 -0.1060 0.0652 37 HIS A N 284 C CA . HIS A 37 ? 0.7625 1.2458 0.8828 -0.2251 -0.1112 0.0621 37 HIS A CA 285 C C . HIS A 37 ? 0.7919 1.3621 0.9191 -0.2379 -0.1169 0.0622 37 HIS A C 286 O O . HIS A 37 ? 0.7863 1.4189 0.9296 -0.2154 -0.1173 0.0648 37 HIS A O 287 C CB . HIS A 37 ? 0.7553 1.1961 0.8680 -0.2045 -0.1125 0.0616 37 HIS A CB 288 C CG . HIS A 37 ? 0.7432 1.2212 0.8651 -0.1682 -0.1143 0.0648 37 HIS A CG 289 N ND1 . HIS A 37 ? 0.7453 1.2675 0.8662 -0.1661 -0.1207 0.0648 37 HIS A ND1 290 C CD2 . HIS A 37 ? 0.7337 1.2076 0.8614 -0.1320 -0.1108 0.0681 37 HIS A CD2 291 C CE1 . HIS A 37 ? 0.7435 1.2863 0.8685 -0.1281 -0.1212 0.0681 37 HIS A CE1 292 N NE2 . HIS A 37 ? 0.7362 1.2477 0.8636 -0.1072 -0.1152 0.0702 37 HIS A NE2 293 N N . ASN A 38 ? 0.8253 1.4016 0.9386 -0.2733 -0.1215 0.0590 38 ASN A N 294 C CA . ASN A 38 ? 0.8369 1.5015 0.9557 -0.2913 -0.1270 0.0584 38 ASN A CA 295 C C . ASN A 38 ? 0.8318 1.5427 0.9593 -0.2623 -0.1320 0.0596 38 ASN A C 296 O O . ASN A 38 ? 0.8487 1.6466 0.9866 -0.2631 -0.1361 0.0598 38 ASN A O 297 C CB . ASN A 38 ? 0.8564 1.5117 0.9524 -0.3432 -0.1301 0.0544 38 ASN A CB 298 C CG . ASN A 38 ? 0.8572 1.4677 0.9355 -0.3492 -0.1340 0.0517 38 ASN A CG 299 O OD1 . ASN A 38 ? 0.8634 1.4763 0.9497 -0.3182 -0.1359 0.0528 38 ASN A OD1 300 N ND2 . ASN A 38 ? 0.8727 1.4402 0.9232 -0.3893 -0.1352 0.0480 38 ASN A ND2 301 N N . GLY A 39 ? 0.8283 1.4829 0.9497 -0.2376 -0.1319 0.0601 39 GLY A N 302 C CA . GLY A 39 ? 0.8019 1.4876 0.9272 -0.2061 -0.1363 0.0618 39 GLY A CA 303 C C . GLY A 39 ? 0.8048 1.5000 0.9187 -0.2271 -0.1426 0.0589 39 GLY A C 304 O O . GLY A 39 ? 0.7779 1.5133 0.8945 -0.2057 -0.1474 0.0602 39 GLY A O 305 N N . LYS A 40 ? 0.8199 1.4747 0.9178 -0.2675 -0.1428 0.0551 40 LYS A N 306 C CA . LYS A 40 ? 0.8453 1.5107 0.9289 -0.2958 -0.1488 0.0516 40 LYS A CA 307 C C . LYS A 40 ? 0.8755 1.4502 0.9361 -0.3116 -0.1477 0.0482 40 LYS A C 308 O O . LYS A 40 ? 0.9027 1.4157 0.9541 -0.3200 -0.1428 0.0472 40 LYS A O 309 C CB . LYS A 40 ? 0.8643 1.5883 0.9441 -0.3397 -0.1513 0.0491 40 LYS A CB 310 C CG . LYS A 40 ? 0.8600 1.6922 0.9615 -0.3282 -0.1539 0.0512 40 LYS A CG 311 C CD . LYS A 40 ? 0.8725 1.7544 0.9728 -0.3695 -0.1533 0.0494 40 LYS A CD 312 C CE . LYS A 40 ? 0.8650 1.8633 0.9884 -0.3546 -0.1558 0.0510 40 LYS A CE 313 N NZ . LYS A 40 ? 0.8813 1.9310 1.0051 -0.3933 -0.1541 0.0495 40 LYS A NZ 314 N N . LEU A 41 ? 0.8985 1.4681 0.9489 -0.3142 -0.1525 0.0462 41 LEU A N 315 C CA . LEU A 41 ? 0.9195 1.4160 0.9441 -0.3357 -0.1529 0.0418 41 LEU A CA 316 C C . LEU A 41 ? 0.9255 1.4285 0.9293 -0.3857 -0.1551 0.0379 41 LEU A C 317 O O . LEU A 41 ? 0.9224 1.4999 0.9308 -0.4060 -0.1591 0.0377 41 LEU A O 318 C CB . LEU A 41 ? 0.9499 1.4463 0.9696 -0.3246 -0.1577 0.0408 41 LEU A CB 319 C CG . LEU A 41 ? 0.9496 1.4396 0.9835 -0.2775 -0.1561 0.0449 41 LEU A CG 320 C CD1 . LEU A 41 ? 0.9693 1.4758 0.9979 -0.2702 -0.1619 0.0444 41 LEU A CD1 321 C CD2 . LEU A 41 ? 0.9398 1.3481 0.9683 -0.2613 -0.1496 0.0448 41 LEU A CD2 322 N N . CYS A 42 ? 0.9288 1.3536 0.9067 -0.4050 -0.1523 0.0347 42 CYS A N 323 C CA . CYS A 42 ? 0.9566 1.3694 0.9080 -0.4507 -0.1528 0.0317 42 CYS A CA 324 C C . CYS A 42 ? 0.9728 1.3018 0.8840 -0.4716 -0.1539 0.0265 42 CYS A C 325 O O . CYS A 42 ? 0.9614 1.2348 0.8694 -0.4465 -0.1524 0.0254 42 CYS A O 326 C CB . CYS A 42 ? 0.9671 1.3625 0.9243 -0.4479 -0.1467 0.0341 42 CYS A CB 327 S SG . CYS A 42 ? 0.9401 1.4387 0.9356 -0.4358 -0.1456 0.0391 42 CYS A SG 328 N N . ASP A 43 ? 1.0104 1.3288 0.8876 -0.5178 -0.1564 0.0230 43 ASP A N 329 C CA . ASP A 43 ? 1.0517 1.2783 0.8812 -0.5382 -0.1570 0.0177 43 ASP A CA 330 C C . ASP A 43 ? 1.0427 1.1951 0.8642 -0.5186 -0.1511 0.0181 43 ASP A C 331 O O . ASP A 43 ? 1.0222 1.1939 0.8631 -0.5108 -0.1469 0.0218 43 ASP A O 332 C CB . ASP A 43 ? 1.1061 1.3306 0.8941 -0.5944 -0.1603 0.0143 43 ASP A CB 333 C CG . ASP A 43 ? 1.1099 1.4064 0.9005 -0.6186 -0.1667 0.0128 43 ASP A CG 334 O OD1 . ASP A 43 ? 1.0764 1.4082 0.8938 -0.5908 -0.1691 0.0136 43 ASP A OD1 335 O OD2 . ASP A 43 ? 1.1386 1.4568 0.9022 -0.6668 -0.1692 0.0106 43 ASP A OD2 336 N N . LEU A 44 ? 1.0758 1.1467 0.8684 -0.5097 -0.1507 0.0141 44 LEU A N 337 C CA . LEU A 44 ? 1.0979 1.1009 0.8819 -0.4878 -0.1453 0.0138 44 LEU A CA 338 C C . LEU A 44 ? 1.1808 1.1007 0.9062 -0.5147 -0.1458 0.0091 44 LEU A C 339 O O . LEU A 44 ? 1.1976 1.0620 0.8876 -0.5179 -0.1485 0.0040 44 LEU A O 340 C CB . LEU A 44 ? 1.0732 1.0503 0.8734 -0.4461 -0.1434 0.0128 44 LEU A CB 341 C CG . LEU A 44 ? 1.0768 0.9955 0.8728 -0.4204 -0.1377 0.0123 44 LEU A CG 342 C CD1 . LEU A 44 ? 1.0373 0.9956 0.8713 -0.4036 -0.1328 0.0180 44 LEU A CD1 343 C CD2 . LEU A 44 ? 1.0603 0.9469 0.8593 -0.3884 -0.1366 0.0093 44 LEU A CD2 344 N N . ASP A 45 ? 1.2458 1.1528 0.9581 -0.5316 -0.1431 0.0110 45 ASP A N 345 C CA . ASP A 45 ? 1.3421 1.1701 0.9915 -0.5619 -0.1440 0.0072 45 ASP A CA 346 C C . ASP A 45 ? 1.3617 1.1999 0.9760 -0.6092 -0.1497 0.0042 45 ASP A C 347 O O . ASP A 45 ? 1.4088 1.1720 0.9644 -0.6291 -0.1523 -0.0008 45 ASP A O 348 C CB . ASP A 45 ? 1.4026 1.1405 1.0199 -0.5355 -0.1431 0.0024 45 ASP A CB 349 C CG . ASP A 45 ? 1.4854 1.1394 1.0483 -0.5467 -0.1415 0.0005 45 ASP A CG 350 O OD1 . ASP A 45 ? 1.5000 1.1629 1.0789 -0.5405 -0.1373 0.0045 45 ASP A OD1 351 O OD2 . ASP A 45 ? 1.5560 1.1335 1.0582 -0.5602 -0.1444 -0.0048 45 ASP A OD2 352 N N . GLY A 46 ? 1.3190 1.2513 0.9680 -0.6253 -0.1517 0.0071 46 GLY A N 353 C CA . GLY A 46 ? 1.3418 1.3033 0.9651 -0.6712 -0.1572 0.0044 46 GLY A CA 354 C C . GLY A 46 ? 1.3284 1.2952 0.9525 -0.6630 -0.1619 0.0009 46 GLY A C 355 O O . GLY A 46 ? 1.3259 1.3322 0.9377 -0.6975 -0.1667 -0.0010 46 GLY A O 356 N N . VAL A 47 ? 1.2968 1.2273 0.9352 -0.6190 -0.1604 0.0000 47 VAL A N 357 C CA . VAL A 47 ? 1.2830 1.2061 0.9178 -0.6084 -0.1644 -0.0035 47 VAL A CA 358 C C . VAL A 47 ? 1.2177 1.2287 0.9137 -0.5795 -0.1651 0.0004 47 VAL A C 359 O O . VAL A 47 ? 1.1853 1.2121 0.9209 -0.5404 -0.1609 0.0043 47 VAL A O 360 C CB . VAL A 47 ? 1.2797 1.1139 0.8916 -0.5769 -0.1624 -0.0074 47 VAL A CB 361 C CG1 . VAL A 47 ? 1.2788 1.1112 0.8901 -0.5652 -0.1661 -0.0111 47 VAL A CG1 362 C CG2 . VAL A 47 ? 1.3439 1.0832 0.8885 -0.5998 -0.1621 -0.0117 47 VAL A CG2 363 N N . LYS A 48 ? 1.2200 1.2844 0.9193 -0.5985 -0.1705 -0.0006 48 LYS A N 364 C CA . LYS A 48 ? 1.1728 1.3258 0.9243 -0.5741 -0.1720 0.0034 48 LYS A CA 365 C C . LYS A 48 ? 1.1382 1.2663 0.9101 -0.5278 -0.1704 0.0039 48 LYS A C 366 O O . LYS A 48 ? 1.1533 1.2155 0.8957 -0.5251 -0.1712 -0.0008 48 LYS A O 367 C CB . LYS A 48 ? 1.2010 1.4155 0.9468 -0.6056 -0.1786 0.0015 48 LYS A CB 368 C CG . LYS A 48 ? 1.1743 1.5025 0.9661 -0.5995 -0.1802 0.0063 48 LYS A CG 369 C CD . LYS A 48 ? 1.1737 1.5645 0.9732 -0.6058 -0.1868 0.0050 48 LYS A CD 370 C CE . LYS A 48 ? 1.1378 1.6395 0.9844 -0.5868 -0.1881 0.0101 48 LYS A CE 371 N NZ . LYS A 48 ? 1.1498 1.7156 1.0039 -0.5891 -0.1948 0.0089 48 LYS A NZ 372 N N . PRO A 49 ? 1.0898 1.2696 0.9090 -0.4916 -0.1681 0.0094 49 PRO A N 373 C CA . PRO A 49 ? 1.0522 1.2192 0.8893 -0.4526 -0.1672 0.0101 49 PRO A CA 374 C C . PRO A 49 ? 1.0433 1.2443 0.8787 -0.4588 -0.1734 0.0085 49 PRO A C 375 O O . PRO A 49 ? 1.0412 1.3066 0.8807 -0.4819 -0.1779 0.0091 49 PRO A O 376 C CB . PRO A 49 ? 0.9972 1.2166 0.8786 -0.4196 -0.1638 0.0168 49 PRO A CB 377 C CG . PRO A 49 ? 1.0016 1.2948 0.8942 -0.4424 -0.1662 0.0191 49 PRO A CG 378 C CD . PRO A 49 ? 1.0530 1.3063 0.9078 -0.4853 -0.1664 0.0150 49 PRO A CD 379 N N . LEU A 50 ? 1.0284 1.1905 0.8581 -0.4383 -0.1736 0.0063 50 LEU A N 380 C CA . LEU A 50 ? 1.0180 1.2153 0.8524 -0.4356 -0.1789 0.0058 50 LEU A CA 381 C C . LEU A 50 ? 0.9694 1.2292 0.8447 -0.4016 -0.1784 0.0125 50 LEU A C 382 O O . LEU A 50 ? 0.9557 1.1914 0.8453 -0.3680 -0.1741 0.0150 50 LEU A O 383 C CB . LEU A 50 ? 1.0320 1.1646 0.8448 -0.4245 -0.1788 0.0011 50 LEU A CB 384 C CG . LEU A 50 ? 1.0178 1.1803 0.8426 -0.4078 -0.1826 0.0020 50 LEU A CG 385 C CD1 . LEU A 50 ? 1.0241 1.2612 0.8547 -0.4292 -0.1893 0.0030 50 LEU A CD1 386 C CD2 . LEU A 50 ? 1.0427 1.1409 0.8379 -0.4078 -0.1831 -0.0042 50 LEU A CD2 387 N N . ILE A 51 ? 0.9638 1.3034 0.8548 -0.4099 -0.1829 0.0151 51 ILE A N 388 C CA . ILE A 51 ? 0.9460 1.3438 0.8701 -0.3744 -0.1831 0.0214 51 ILE A CA 389 C C . ILE A 51 ? 0.9527 1.3796 0.8773 -0.3644 -0.1889 0.0215 51 ILE A C 390 O O . ILE A 51 ? 0.9911 1.4683 0.9100 -0.3882 -0.1950 0.0195 51 ILE A O 391 C CB . ILE A 51 ? 0.9403 1.4148 0.8845 -0.3804 -0.1838 0.0249 51 ILE A CB 392 C CG1 . ILE A 51 ? 0.9516 1.3909 0.8943 -0.3889 -0.1777 0.0250 51 ILE A CG1 393 C CG2 . ILE A 51 ? 0.9119 1.4440 0.8845 -0.3395 -0.1846 0.0311 51 ILE A CG2 394 C CD1 . ILE A 51 ? 0.9382 1.4408 0.9070 -0.3783 -0.1759 0.0298 51 ILE A CD1 395 N N . LEU A 52 ? 0.9353 1.3319 0.8655 -0.3303 -0.1868 0.0238 52 LEU A N 396 C CA . LEU A 52 ? 0.9369 1.3519 0.8649 -0.3181 -0.1917 0.0242 52 LEU A CA 397 C C . LEU A 52 ? 0.9392 1.4384 0.8871 -0.2995 -0.1962 0.0295 52 LEU A C 398 O O . LEU A 52 ? 0.9485 1.4831 0.8930 -0.2994 -0.2022 0.0292 52 LEU A O 399 C CB . LEU A 52 ? 0.9182 1.2730 0.8425 -0.2894 -0.1877 0.0251 52 LEU A CB 400 C CG . LEU A 52 ? 0.9277 1.2044 0.8312 -0.3040 -0.1836 0.0191 52 LEU A CG 401 C CD1 . LEU A 52 ? 0.9160 1.1433 0.8159 -0.2779 -0.1797 0.0192 52 LEU A CD1 402 C CD2 . LEU A 52 ? 0.9597 1.2276 0.8379 -0.3398 -0.1886 0.0125 52 LEU A CD2 403 N N . ARG A 53 ? 0.9413 1.4740 0.9082 -0.2827 -0.1936 0.0340 53 ARG A N 404 C CA . ARG A 53 ? 0.9519 1.5647 0.9351 -0.2594 -0.1977 0.0388 53 ARG A CA 405 C C . ARG A 53 ? 0.9619 1.5562 0.9416 -0.2210 -0.1987 0.0427 53 ARG A C 406 O O . ARG A 53 ? 0.9917 1.5220 0.9674 -0.2010 -0.1930 0.0445 53 ARG A O 407 C CB . ARG A 53 ? 0.9866 1.6754 0.9688 -0.2902 -0.2051 0.0356 53 ARG A CB 408 C CG . ARG A 53 ? 1.0004 1.7846 1.0025 -0.2808 -0.2076 0.0387 53 ARG A CG 409 C CD . ARG A 53 ? 1.0264 1.8976 1.0287 -0.2950 -0.2162 0.0368 53 ARG A CD 410 N NE . ARG A 53 ? 1.0407 1.9888 1.0512 -0.3265 -0.2179 0.0345 53 ARG A NE 411 C CZ . ARG A 53 ? 1.0638 2.0032 1.0600 -0.3792 -0.2180 0.0289 53 ARG A CZ 412 N NH1 . ARG A 53 ? 1.0833 1.9383 1.0552 -0.4044 -0.2165 0.0248 53 ARG A NH1 413 N NH2 . ARG A 53 ? 1.0703 2.0854 1.0731 -0.4072 -0.2194 0.0273 53 ARG A NH2 414 N N . ASP A 54 ? 0.9718 1.6206 0.9506 -0.2118 -0.2057 0.0439 54 ASP A N 415 C CA . ASP A 54 ? 0.9735 1.6033 0.9441 -0.1760 -0.2071 0.0479 54 ASP A CA 416 C C . ASP A 54 ? 0.9759 1.5335 0.9288 -0.1854 -0.2057 0.0447 54 ASP A C 417 O O . ASP A 54 ? 1.0024 1.5231 0.9463 -0.1578 -0.2041 0.0481 54 ASP A O 418 C CB . ASP A 54 ? 0.9948 1.7063 0.9676 -0.1622 -0.2155 0.0500 54 ASP A CB 419 C CG . ASP A 54 ? 1.0026 1.7862 0.9909 -0.1385 -0.2168 0.0541 54 ASP A CG 420 O OD1 . ASP A 54 ? 0.9841 1.7394 0.9764 -0.1145 -0.2111 0.0578 54 ASP A OD1 421 O OD2 . ASP A 54 ? 1.0107 1.8819 1.0060 -0.1432 -0.2236 0.0532 54 ASP A OD2 422 N N . CYS A 55 ? 0.9645 1.5005 0.9090 -0.2238 -0.2062 0.0381 55 CYS A N 423 C CA . CYS A 55 ? 0.9748 1.4421 0.9014 -0.2317 -0.2045 0.0342 55 CYS A CA 424 C C . CYS A 55 ? 0.9359 1.3269 0.8596 -0.2216 -0.1959 0.0341 55 CYS A C 425 O O . CYS A 55 ? 0.9210 1.3058 0.8552 -0.2175 -0.1910 0.0357 55 CYS A O 426 C CB . CYS A 55 ? 1.0050 1.4701 0.9178 -0.2743 -0.2081 0.0267 55 CYS A CB 427 S SG . CYS A 55 ? 1.0533 1.5994 0.9641 -0.2874 -0.2185 0.0258 55 CYS A SG 428 N N . SER A 56 ? 0.9119 1.2492 0.8210 -0.2180 -0.1941 0.0317 56 SER A N 429 C CA . SER A 56 ? 0.8861 1.1564 0.7906 -0.2093 -0.1862 0.0307 56 SER A CA 430 C C . SER A 56 ? 0.8808 1.1021 0.7681 -0.2327 -0.1851 0.0227 56 SER A C 431 O O . SER A 56 ? 0.8913 1.1207 0.7663 -0.2511 -0.1904 0.0186 56 SER A O 432 C CB . SER A 56 ? 0.8853 1.1351 0.7848 -0.1784 -0.1840 0.0355 56 SER A CB 433 O OG . SER A 56 ? 0.8849 1.1138 0.7686 -0.1830 -0.1863 0.0323 56 SER A OG 434 N N . VAL A 57 ? 0.8734 1.0430 0.7574 -0.2298 -0.1783 0.0203 57 VAL A N 435 C CA . VAL A 57 ? 0.8824 1.0039 0.7471 -0.2478 -0.1770 0.0123 57 VAL A CA 436 C C . VAL A 57 ? 0.9000 1.0154 0.7493 -0.2501 -0.1811 0.0093 57 VAL A C 437 O O . VAL A 57 ? 0.9081 1.0094 0.7389 -0.2722 -0.1846 0.0029 57 VAL A O 438 C CB . VAL A 57 ? 0.8656 0.9370 0.7290 -0.2359 -0.1689 0.0104 57 VAL A CB 439 C CG1 . VAL A 57 ? 0.8879 0.9115 0.7279 -0.2490 -0.1681 0.0017 57 VAL A CG1 440 C CG2 . VAL A 57 ? 0.8533 0.9297 0.7306 -0.2355 -0.1651 0.0130 57 VAL A CG2 441 N N . ALA A 58 ? 0.8931 1.0170 0.7467 -0.2279 -0.1809 0.0140 58 ALA A N 442 C CA . ALA A 58 ? 0.9056 1.0285 0.7458 -0.2281 -0.1849 0.0121 58 ALA A CA 443 C C . ALA A 58 ? 0.9187 1.0891 0.7571 -0.2447 -0.1936 0.0119 58 ALA A C 444 O O . ALA A 58 ? 0.9249 1.0847 0.7464 -0.2645 -0.1973 0.0057 58 ALA A O 445 C CB . ALA A 58 ? 0.8925 1.0125 0.7342 -0.2013 -0.1826 0.0181 58 ALA A CB 446 N N . GLY A 59 ? 0.9093 1.1334 0.7634 -0.2362 -0.1968 0.0182 59 GLY A N 447 C CA . GLY A 59 ? 0.9114 1.1929 0.7665 -0.2520 -0.2050 0.0180 59 GLY A CA 448 C C . GLY A 59 ? 0.9370 1.2092 0.7790 -0.2894 -0.2071 0.0103 59 GLY A C 449 O O . GLY A 59 ? 0.9771 1.2597 0.8046 -0.3089 -0.2127 0.0061 59 GLY A O 450 N N . TRP A 60 ? 0.9298 1.1780 0.7731 -0.2998 -0.2025 0.0085 60 TRP A N 451 C CA . TRP A 60 ? 0.9465 1.1747 0.7707 -0.3352 -0.2038 0.0016 60 TRP A CA 452 C C . TRP A 60 ? 0.9827 1.1520 0.7779 -0.3456 -0.2038 -0.0059 60 TRP A C 453 O O . TRP A 60 ? 1.0282 1.1999 0.8024 -0.3722 -0.2091 -0.0110 60 TRP A O 454 C CB . TRP A 60 ? 0.9354 1.1419 0.7651 -0.3382 -0.1981 0.0020 60 TRP A CB 455 C CG . TRP A 60 ? 0.9628 1.1221 0.7643 -0.3687 -0.1976 -0.0051 60 TRP A CG 456 C CD1 . TRP A 60 ? 0.9961 1.1543 0.7710 -0.4031 -0.2029 -0.0107 60 TRP A CD1 457 C CD2 . TRP A 60 ? 0.9600 1.0636 0.7525 -0.3671 -0.1914 -0.0075 60 TRP A CD2 458 N NE1 . TRP A 60 ? 1.0244 1.1233 0.7705 -0.4224 -0.2005 -0.0163 60 TRP A NE1 459 C CE2 . TRP A 60 ? 0.9987 1.0648 0.7559 -0.3994 -0.1936 -0.0144 60 TRP A CE2 460 C CE3 . TRP A 60 ? 0.9400 1.0205 0.7481 -0.3415 -0.1844 -0.0047 60 TRP A CE3 461 C CZ2 . TRP A 60 ? 1.0247 1.0302 0.7608 -0.4039 -0.1892 -0.0182 60 TRP A CZ2 462 C CZ3 . TRP A 60 ? 0.9521 0.9787 0.7435 -0.3470 -0.1801 -0.0087 60 TRP A CZ3 463 C CH2 . TRP A 60 ? 0.9987 0.9878 0.7541 -0.3763 -0.1826 -0.0152 60 TRP A CH2 464 N N . LEU A 61 ? 0.9810 1.1000 0.7736 -0.3247 -0.1980 -0.0070 61 LEU A N 465 C CA . LEU A 61 ? 1.0017 1.0622 0.7654 -0.3318 -0.1971 -0.0151 61 LEU A CA 466 C C . LEU A 61 ? 1.0115 1.0772 0.7632 -0.3326 -0.2018 -0.0175 61 LEU A C 467 O O . LEU A 61 ? 1.0505 1.0837 0.7731 -0.3506 -0.2042 -0.0250 61 LEU A O 468 C CB . LEU A 61 ? 0.9928 1.0062 0.7580 -0.3094 -0.1892 -0.0162 61 LEU A CB 469 C CG . LEU A 61 ? 0.9868 0.9791 0.7549 -0.3112 -0.1844 -0.0162 61 LEU A CG 470 C CD1 . LEU A 61 ? 0.9839 0.9285 0.7469 -0.2913 -0.1775 -0.0196 61 LEU A CD1 471 C CD2 . LEU A 61 ? 1.0182 0.9918 0.7604 -0.3425 -0.1876 -0.0214 61 LEU A CD2 472 N N . LEU A 62 ? 0.9848 1.0873 0.7550 -0.3127 -0.2030 -0.0113 62 LEU A N 473 C CA . LEU A 62 ? 0.9882 1.1041 0.7482 -0.3143 -0.2083 -0.0127 62 LEU A CA 474 C C . LEU A 62 ? 1.0117 1.1753 0.7673 -0.3405 -0.2164 -0.0135 62 LEU A C 475 O O . LEU A 62 ? 1.0200 1.1870 0.7590 -0.3530 -0.2215 -0.0173 62 LEU A O 476 C CB . LEU A 62 ? 0.9564 1.0937 0.7327 -0.2846 -0.2074 -0.0053 62 LEU A CB 477 C CG . LEU A 62 ? 0.9371 1.0299 0.7139 -0.2626 -0.1994 -0.0050 62 LEU A CG 478 C CD1 . LEU A 62 ? 0.9176 1.0309 0.7087 -0.2357 -0.1978 0.0039 62 LEU A CD1 479 C CD2 . LEU A 62 ? 0.9552 1.0088 0.7098 -0.2660 -0.1987 -0.0123 62 LEU A CD2 480 N N . GLY A 63 ? 1.0126 1.2160 0.7825 -0.3499 -0.2175 -0.0101 63 GLY A N 481 C CA . GLY A 63 ? 1.0319 1.2917 0.7999 -0.3762 -0.2249 -0.0107 63 GLY A CA 482 C C . GLY A 63 ? 1.0166 1.3447 0.8046 -0.3572 -0.2297 -0.0040 63 GLY A C 483 O O . GLY A 63 ? 1.0293 1.3878 0.8085 -0.3688 -0.2362 -0.0059 63 GLY A O 484 N N . ASN A 64 ? 0.9981 1.3480 0.8098 -0.3266 -0.2268 0.0036 64 ASN A N 485 C CA . ASN A 64 ? 0.9828 1.4003 0.8105 -0.3055 -0.2317 0.0104 64 ASN A CA 486 C C . ASN A 64 ? 1.0111 1.4994 0.8407 -0.3338 -0.2388 0.0083 64 ASN A C 487 O O . ASN A 64 ? 1.0148 1.5086 0.8437 -0.3604 -0.2378 0.0053 64 ASN A O 488 C CB . ASN A 64 ? 0.9458 1.3717 0.7938 -0.2729 -0.2270 0.0181 64 ASN A CB 489 C CG . ASN A 64 ? 0.9261 1.4196 0.7863 -0.2461 -0.2321 0.0252 64 ASN A CG 490 O OD1 . ASN A 64 ? 0.9270 1.4905 0.7934 -0.2583 -0.2385 0.0249 64 ASN A OD1 491 N ND2 . ASN A 64 ? 0.9091 1.3824 0.7700 -0.2092 -0.2292 0.0316 64 ASN A ND2 492 N N . PRO A 65 ? 1.0490 1.5925 0.8787 -0.3298 -0.2461 0.0097 65 PRO A N 493 C CA . PRO A 65 ? 1.0766 1.6961 0.9071 -0.3588 -0.2534 0.0070 65 PRO A CA 494 C C . PRO A 65 ? 1.0803 1.7646 0.9321 -0.3581 -0.2534 0.0105 65 PRO A C 495 O O . PRO A 65 ? 1.1014 1.8314 0.9507 -0.3939 -0.2566 0.0065 65 PRO A O 496 C CB . PRO A 65 ? 1.0779 1.7460 0.9087 -0.3405 -0.2605 0.0098 65 PRO A CB 497 C CG . PRO A 65 ? 1.0602 1.6896 0.8950 -0.2953 -0.2566 0.0164 65 PRO A CG 498 C CD . PRO A 65 ? 1.0533 1.5931 0.8804 -0.2988 -0.2481 0.0137 65 PRO A CD 499 N N . MET A 66 ? 1.0791 1.7669 0.9490 -0.3189 -0.2496 0.0177 66 MET A N 500 C CA . MET A 66 ? 1.0723 1.8200 0.9626 -0.3135 -0.2491 0.0211 66 MET A CA 501 C C . MET A 66 ? 1.0479 1.7478 0.9400 -0.3300 -0.2417 0.0193 66 MET A C 502 O O . MET A 66 ? 1.0160 1.7542 0.9248 -0.3245 -0.2399 0.0221 66 MET A O 503 C CB . MET A 66 ? 1.0710 1.8482 0.9754 -0.2616 -0.2494 0.0295 66 MET A CB 504 C CG . MET A 66 ? 1.0926 1.9376 0.9956 -0.2451 -0.2580 0.0316 66 MET A CG 505 S SD . MET A 66 ? 1.1324 2.0425 1.0499 -0.1902 -0.2601 0.0406 66 MET A SD 506 C CE . MET A 66 ? 1.1286 2.1491 1.0465 -0.1905 -0.2717 0.0396 66 MET A CE 507 N N . CYS A 67 ? 1.0626 1.6804 0.9360 -0.3490 -0.2377 0.0143 67 CYS A N 508 C CA . CYS A 67 ? 1.0698 1.6363 0.9384 -0.3676 -0.2313 0.0115 67 CYS A CA 509 C C . CYS A 67 ? 1.0881 1.6405 0.9313 -0.4178 -0.2338 0.0035 67 CYS A C 510 O O . CYS A 67 ? 1.0723 1.5507 0.8952 -0.4342 -0.2296 -0.0010 67 CYS A O 511 C CB . CYS A 67 ? 1.0783 1.5576 0.9413 -0.3452 -0.2243 0.0119 67 CYS A CB 512 S SG . CYS A 67 ? 1.0718 1.5593 0.9570 -0.2910 -0.2208 0.0213 67 CYS A SG 513 N N . ASP A 68 ? 1.0949 1.7192 0.9362 -0.4416 -0.2409 0.0017 68 ASP A N 514 C CA . ASP A 68 ? 1.1204 1.7370 0.9323 -0.4935 -0.2442 -0.0059 68 ASP A CA 515 C C . ASP A 68 ? 1.1209 1.7241 0.9241 -0.5247 -0.2406 -0.0081 68 ASP A C 516 O O . ASP A 68 ? 1.1533 1.7044 0.9216 -0.5636 -0.2404 -0.0146 68 ASP A O 517 C CB . ASP A 68 ? 1.1275 1.8357 0.9414 -0.5118 -0.2527 -0.0071 68 ASP A CB 518 C CG . ASP A 68 ? 1.1318 1.8289 0.9351 -0.5020 -0.2572 -0.0087 68 ASP A CG 519 O OD1 . ASP A 68 ? 1.1236 1.7584 0.9267 -0.4707 -0.2537 -0.0069 68 ASP A OD1 520 O OD2 . ASP A 68 ? 1.1572 1.9096 0.9516 -0.5272 -0.2641 -0.0120 68 ASP A OD2 521 N N . GLU A 69 ? 1.0758 1.7221 0.9070 -0.5071 -0.2377 -0.0026 69 GLU A N 522 C CA . GLU A 69 ? 1.0706 1.7012 0.8962 -0.5314 -0.2333 -0.0036 69 GLU A CA 523 C C . GLU A 69 ? 1.0872 1.6052 0.8847 -0.5388 -0.2277 -0.0074 69 GLU A C 524 O O . GLU A 69 ? 1.1033 1.5885 0.8748 -0.5752 -0.2261 -0.0113 69 GLU A O 525 C CB . GLU A 69 ? 1.0253 1.7010 0.8870 -0.4987 -0.2297 0.0034 69 GLU A CB 526 C CG . GLU A 69 ? 1.0263 1.6751 0.8834 -0.5185 -0.2242 0.0029 69 GLU A CG 527 C CD . GLU A 69 ? 0.9842 1.6858 0.8758 -0.4898 -0.2210 0.0093 69 GLU A CD 528 O OE1 . GLU A 69 ? 0.9493 1.7029 0.8667 -0.4506 -0.2229 0.0144 69 GLU A OE1 529 O OE2 . GLU A 69 ? 0.9767 1.6640 0.8662 -0.5062 -0.2167 0.0092 69 GLU A OE2 530 N N . PHE A 70 ? 1.0776 1.5380 0.8774 -0.5041 -0.2248 -0.0064 70 PHE A N 531 C CA . PHE A 70 ? 1.0931 1.4562 0.8737 -0.4989 -0.2186 -0.0091 70 PHE A CA 532 C C . PHE A 70 ? 1.1467 1.4382 0.8877 -0.5148 -0.2201 -0.0165 70 PHE A C 533 O O . PHE A 70 ? 1.1384 1.3543 0.8663 -0.4992 -0.2154 -0.0187 70 PHE A O 534 C CB . PHE A 70 ? 1.0477 1.3945 0.8569 -0.4500 -0.2130 -0.0033 70 PHE A CB 535 C CG . PHE A 70 ? 1.0016 1.4122 0.8453 -0.4313 -0.2115 0.0036 70 PHE A CG 536 C CD1 . PHE A 70 ? 0.9974 1.4107 0.8433 -0.4470 -0.2082 0.0041 70 PHE A CD1 537 C CD2 . PHE A 70 ? 0.9663 1.4333 0.8364 -0.3982 -0.2137 0.0095 70 PHE A CD2 538 C CE1 . PHE A 70 ? 0.9647 1.4376 0.8412 -0.4292 -0.2068 0.0101 70 PHE A CE1 539 C CE2 . PHE A 70 ? 0.9372 1.4608 0.8346 -0.3787 -0.2125 0.0155 70 PHE A CE2 540 C CZ . PHE A 70 ? 0.9350 1.4634 0.8370 -0.3943 -0.2090 0.0156 70 PHE A CZ 541 N N . ILE A 71 ? 1.2007 1.5167 0.9210 -0.5459 -0.2266 -0.0208 71 ILE A N 542 C CA . ILE A 71 ? 1.2707 1.5134 0.9444 -0.5692 -0.2280 -0.0289 71 ILE A CA 543 C C . ILE A 71 ? 1.3367 1.5220 0.9742 -0.6013 -0.2253 -0.0330 71 ILE A C 544 O O . ILE A 71 ? 1.3547 1.5806 0.9980 -0.6239 -0.2253 -0.0309 71 ILE A O 545 C CB . ILE A 71 ? 1.3184 1.6007 0.9747 -0.5993 -0.2357 -0.0328 71 ILE A CB 546 C CG1 . ILE A 71 ? 1.2853 1.6240 0.9741 -0.5669 -0.2390 -0.0285 71 ILE A CG1 547 C CG2 . ILE A 71 ? 1.3871 1.5844 0.9889 -0.6244 -0.2369 -0.0417 71 ILE A CG2 548 C CD1 . ILE A 71 ? 1.2926 1.6744 0.9667 -0.5928 -0.2468 -0.0322 71 ILE A CD1 549 N N . ASN A 72 ? 1.3843 1.4753 0.9825 -0.6015 -0.2230 -0.0389 72 ASN A N 550 C CA . ASN A 72 ? 1.4342 1.4540 0.9877 -0.6283 -0.2206 -0.0433 72 ASN A CA 551 C C . ASN A 72 ? 1.4019 1.4396 0.9731 -0.6311 -0.2164 -0.0384 72 ASN A C 552 O O . ASN A 72 ? 1.4399 1.4622 0.9786 -0.6704 -0.2171 -0.0407 72 ASN A O 553 C CB . ASN A 72 ? 1.5119 1.5181 1.0141 -0.6808 -0.2263 -0.0499 72 ASN A CB 554 C CG . ASN A 72 ? 1.5728 1.5376 1.0453 -0.6795 -0.2298 -0.0562 72 ASN A CG 555 O OD1 . ASN A 72 ? 1.5942 1.5112 1.0686 -0.6431 -0.2269 -0.0575 72 ASN A OD1 556 N ND2 . ASN A 72 ? 1.6244 1.6100 1.0687 -0.7201 -0.2359 -0.0604 72 ASN A ND2 557 N N . VAL A 73 ? 1.3279 1.3951 0.9471 -0.5909 -0.2120 -0.0319 73 VAL A N 558 C CA . VAL A 73 ? 1.2987 1.3819 0.9373 -0.5889 -0.2075 -0.0271 73 VAL A CA 559 C C . VAL A 73 ? 1.3331 1.3260 0.9282 -0.6016 -0.2038 -0.0312 73 VAL A C 560 O O . VAL A 73 ? 1.3544 1.2715 0.9241 -0.5843 -0.2019 -0.0355 73 VAL A O 561 C CB . VAL A 73 ? 1.2330 1.3446 0.9233 -0.5400 -0.2027 -0.0202 73 VAL A CB 562 C CG1 . VAL A 73 ? 1.1928 1.3946 0.9233 -0.5249 -0.2064 -0.0151 73 VAL A CG1 563 C CG2 . VAL A 73 ? 1.2238 1.2654 0.9081 -0.5058 -0.1986 -0.0224 73 VAL A CG2 564 N N . PRO A 74 ? 1.3346 1.3366 0.9198 -0.6302 -0.2027 -0.0298 74 PRO A N 565 C CA . PRO A 74 ? 1.3742 1.2871 0.9134 -0.6419 -0.1994 -0.0333 74 PRO A CA 566 C C . PRO A 74 ? 1.3392 1.2188 0.9015 -0.5980 -0.1928 -0.0303 74 PRO A C 567 O O . PRO A 74 ? 1.2647 1.1933 0.8793 -0.5625 -0.1904 -0.0251 74 PRO A O 568 C CB . PRO A 74 ? 1.3899 1.3370 0.9186 -0.6853 -0.2001 -0.0315 74 PRO A CB 569 C CG . PRO A 74 ? 1.3302 1.3900 0.9209 -0.6740 -0.2007 -0.0249 74 PRO A CG 570 C CD . PRO A 74 ? 1.3042 1.3995 0.9216 -0.6476 -0.2039 -0.0247 74 PRO A CD 571 N N . GLU A 75 ? 1.3776 1.1721 0.8965 -0.6016 -0.1900 -0.0338 75 GLU A N 572 C CA . GLU A 75 ? 1.3385 1.0997 0.8720 -0.5669 -0.1837 -0.0316 75 GLU A CA 573 C C . GLU A 75 ? 1.2789 1.1156 0.8713 -0.5526 -0.1803 -0.0235 75 GLU A C 574 O O . GLU A 75 ? 1.2515 1.1450 0.8548 -0.5806 -0.1820 -0.0203 75 GLU A O 575 C CB . GLU A 75 ? 1.4027 1.0769 0.8763 -0.5859 -0.1824 -0.0355 75 GLU A CB 576 C CG . GLU A 75 ? 1.3920 1.0327 0.8758 -0.5549 -0.1763 -0.0333 75 GLU A CG 577 C CD . GLU A 75 ? 1.4659 1.0025 0.8811 -0.5611 -0.1756 -0.0389 75 GLU A CD 578 O OE1 . GLU A 75 ? 1.5408 1.0305 0.8966 -0.5974 -0.1798 -0.0436 75 GLU A OE1 579 O OE2 . GLU A 75 ? 1.4516 0.9517 0.8690 -0.5291 -0.1711 -0.0388 75 GLU A OE2 580 N N . TRP A 76 ? 1.2465 1.0851 0.8748 -0.5093 -0.1755 -0.0206 76 TRP A N 581 C CA . TRP A 76 ? 1.2016 1.1026 0.8826 -0.4904 -0.1719 -0.0132 76 TRP A CA 582 C C . TRP A 76 ? 1.1936 1.0508 0.8773 -0.4666 -0.1655 -0.0122 76 TRP A C 583 O O . TRP A 76 ? 1.2409 1.0280 0.8949 -0.4537 -0.1637 -0.0170 76 TRP A O 584 C CB . TRP A 76 ? 1.1555 1.1139 0.8814 -0.4609 -0.1724 -0.0096 76 TRP A CB 585 C CG . TRP A 76 ? 1.1730 1.0894 0.9000 -0.4269 -0.1697 -0.0120 76 TRP A CG 586 C CD1 . TRP A 76 ? 1.1498 1.0506 0.8979 -0.3931 -0.1637 -0.0100 76 TRP A CD1 587 C CD2 . TRP A 76 ? 1.2040 1.0928 0.9096 -0.4246 -0.1728 -0.0173 76 TRP A CD2 588 N NE1 . TRP A 76 ? 1.1459 1.0140 0.8869 -0.3714 -0.1628 -0.0139 76 TRP A NE1 589 C CE2 . TRP A 76 ? 1.1814 1.0410 0.8969 -0.3890 -0.1683 -0.0183 76 TRP A CE2 590 C CE3 . TRP A 76 ? 1.2386 1.1256 0.9165 -0.4505 -0.1790 -0.0216 76 TRP A CE3 591 C CZ2 . TRP A 76 ? 1.1978 1.0292 0.8976 -0.3776 -0.1696 -0.0233 76 TRP A CZ2 592 C CZ3 . TRP A 76 ? 1.2509 1.1056 0.9126 -0.4380 -0.1804 -0.0265 76 TRP A CZ3 593 C CH2 . TRP A 76 ? 1.2306 1.0588 0.9038 -0.4014 -0.1756 -0.0273 76 TRP A CH2 594 N N . SER A 77 ? 1.1447 1.0459 0.8626 -0.4603 -0.1622 -0.0063 77 SER A N 595 C CA . SER A 77 ? 1.1313 1.0013 0.8571 -0.4379 -0.1560 -0.0047 77 SER A CA 596 C C . SER A 77 ? 1.0819 0.9725 0.8480 -0.3963 -0.1524 -0.0019 77 SER A C 597 O O . SER A 77 ? 1.0847 0.9311 0.8462 -0.3721 -0.1484 -0.0042 77 SER A O 598 C CB . SER A 77 ? 1.1165 1.0243 0.8578 -0.4533 -0.1542 0.0002 77 SER A CB 599 O OG . SER A 77 ? 1.0814 1.0742 0.8568 -0.4597 -0.1568 0.0046 77 SER A OG 600 N N . TYR A 78 ? 1.0273 0.9867 0.8300 -0.3888 -0.1539 0.0028 78 TYR A N 601 C CA . TYR A 78 ? 0.9626 0.9420 0.7976 -0.3534 -0.1512 0.0057 78 TYR A CA 602 C C . TYR A 78 ? 0.9392 0.9767 0.7908 -0.3544 -0.1562 0.0081 78 TYR A C 603 O O . TYR A 78 ? 0.9452 1.0192 0.7911 -0.3811 -0.1610 0.0082 78 TYR A O 604 C CB . TYR A 78 ? 0.9176 0.9173 0.7834 -0.3332 -0.1456 0.0111 78 TYR A CB 605 C CG . TYR A 78 ? 0.8813 0.9435 0.7679 -0.3451 -0.1468 0.0164 78 TYR A CG 606 C CD1 . TYR A 78 ? 0.8882 0.9483 0.7601 -0.3733 -0.1470 0.0159 78 TYR A CD1 607 C CD2 . TYR A 78 ? 0.8430 0.9663 0.7615 -0.3267 -0.1475 0.0217 78 TYR A CD2 608 C CE1 . TYR A 78 ? 0.8704 0.9946 0.7623 -0.3843 -0.1478 0.0202 78 TYR A CE1 609 C CE2 . TYR A 78 ? 0.8255 1.0113 0.7628 -0.3339 -0.1487 0.0259 78 TYR A CE2 610 C CZ . TYR A 78 ? 0.8370 1.0267 0.7628 -0.3633 -0.1488 0.0250 78 TYR A CZ 611 O OH . TYR A 78 ? 0.8087 1.0680 0.7544 -0.3701 -0.1498 0.0289 78 TYR A OH 612 N N . ILE A 79 ? 0.8994 0.9457 0.7691 -0.3261 -0.1551 0.0100 79 ILE A N 613 C CA . ILE A 79 ? 0.8814 0.9782 0.7646 -0.3215 -0.1598 0.0126 79 ILE A CA 614 C C . ILE A 79 ? 0.8431 0.9866 0.7594 -0.2951 -0.1575 0.0198 79 ILE A C 615 O O . ILE A 79 ? 0.8149 0.9372 0.7420 -0.2735 -0.1517 0.0219 79 ILE A O 616 C CB . ILE A 79 ? 0.8936 0.9605 0.7658 -0.3088 -0.1606 0.0093 79 ILE A CB 617 C CG1 . ILE A 79 ? 0.9373 0.9548 0.7723 -0.3317 -0.1632 0.0016 79 ILE A CG1 618 C CG2 . ILE A 79 ? 0.8779 0.9955 0.7636 -0.3005 -0.1653 0.0128 79 ILE A CG2 619 C CD1 . ILE A 79 ? 0.9466 0.9279 0.7690 -0.3170 -0.1627 -0.0025 79 ILE A CD1 620 N N . VAL A 80 ? 0.8428 1.0493 0.7722 -0.2958 -0.1624 0.0233 80 VAL A N 621 C CA . VAL A 80 ? 0.8210 1.0728 0.7762 -0.2681 -0.1612 0.0301 80 VAL A CA 622 C C . VAL A 80 ? 0.8186 1.0986 0.7765 -0.2510 -0.1656 0.0324 80 VAL A C 623 O O . VAL A 80 ? 0.8361 1.1529 0.7890 -0.2669 -0.1720 0.0309 80 VAL A O 624 C CB . VAL A 80 ? 0.8133 1.1260 0.7826 -0.2796 -0.1628 0.0328 80 VAL A CB 625 C CG1 . VAL A 80 ? 0.7910 1.1493 0.7831 -0.2464 -0.1619 0.0394 80 VAL A CG1 626 C CG2 . VAL A 80 ? 0.8186 1.1005 0.7827 -0.2972 -0.1584 0.0309 80 VAL A CG2 627 N N . GLU A 81 ? 0.8090 1.0705 0.7723 -0.2197 -0.1622 0.0359 81 GLU A N 628 C CA . GLU A 81 ? 0.8138 1.0894 0.7745 -0.2004 -0.1656 0.0386 81 GLU A CA 629 C C . GLU A 81 ? 0.8111 1.1083 0.7833 -0.1676 -0.1636 0.0455 81 GLU A C 630 O O . GLU A 81 ? 0.8095 1.0790 0.7863 -0.1558 -0.1573 0.0472 81 GLU A O 631 C CB . GLU A 81 ? 0.8178 1.0338 0.7632 -0.1960 -0.1628 0.0355 81 GLU A CB 632 C CG . GLU A 81 ? 0.8229 1.0460 0.7606 -0.1807 -0.1665 0.0375 81 GLU A CG 633 C CD . GLU A 81 ? 0.8292 0.9959 0.7533 -0.1738 -0.1623 0.0351 81 GLU A CD 634 O OE1 . GLU A 81 ? 0.8020 0.9353 0.7273 -0.1614 -0.1555 0.0361 81 GLU A OE1 635 O OE2 . GLU A 81 ? 0.8456 1.0041 0.7570 -0.1816 -0.1658 0.0318 81 GLU A OE2 636 N N . LYS A 82 ? 0.8320 1.1771 0.8058 -0.1520 -0.1691 0.0493 82 LYS A N 637 C CA . LYS A 82 ? 0.8501 1.2099 0.8266 -0.1161 -0.1680 0.0560 82 LYS A CA 638 C C . LYS A 82 ? 0.8671 1.1655 0.8280 -0.0946 -0.1632 0.0582 82 LYS A C 639 O O . LYS A 82 ? 0.8503 1.1048 0.8008 -0.1061 -0.1615 0.0546 82 LYS A O 640 C CB . LYS A 82 ? 0.8759 1.3023 0.8532 -0.1025 -0.1758 0.0590 82 LYS A CB 641 C CG . LYS A 82 ? 0.8812 1.3825 0.8753 -0.1155 -0.1797 0.0584 82 LYS A CG 642 C CD . LYS A 82 ? 0.9004 1.4734 0.8947 -0.1002 -0.1877 0.0608 82 LYS A CD 643 C CE . LYS A 82 ? 0.9049 1.5560 0.9154 -0.0917 -0.1898 0.0627 82 LYS A CE 644 N NZ . LYS A 82 ? 0.9051 1.5922 0.9283 -0.1334 -0.1903 0.0579 82 LYS A NZ 645 N N . ALA A 83 ? 0.8998 1.1959 0.8565 -0.0639 -0.1610 0.0640 83 ALA A N 646 C CA . ALA A 83 ? 0.9380 1.1769 0.8744 -0.0443 -0.1564 0.0667 83 ALA A CA 647 C C . ALA A 83 ? 0.9754 1.2104 0.8923 -0.0342 -0.1613 0.0684 83 ALA A C 648 O O . ALA A 83 ? 0.9915 1.1769 0.8925 -0.0368 -0.1581 0.0673 83 ALA A O 649 C CB . ALA A 83 ? 0.9347 1.1672 0.8657 -0.0154 -0.1528 0.0724 83 ALA A CB 650 N N . ASN A 84 ? 1.0120 1.3022 0.9299 -0.0232 -0.1689 0.0708 84 ASN A N 651 C CA . ASN A 84 ? 1.0523 1.3446 0.9515 -0.0121 -0.1744 0.0727 84 ASN A CA 652 C C . ASN A 84 ? 1.0471 1.4046 0.9583 -0.0267 -0.1828 0.0700 84 ASN A C 653 O O . ASN A 84 ? 1.0550 1.4633 0.9633 -0.0060 -0.1891 0.0735 84 ASN A O 654 C CB . ASN A 84 ? 1.0972 1.3826 0.9731 0.0283 -0.1753 0.0801 84 ASN A CB 655 C CG . ASN A 84 ? 1.1414 1.3523 0.9957 0.0389 -0.1672 0.0826 84 ASN A CG 656 O OD1 . ASN A 84 ? 1.1674 1.3290 1.0059 0.0292 -0.1642 0.0813 84 ASN A OD1 657 N ND2 . ASN A 84 ? 1.1492 1.3534 1.0017 0.0574 -0.1634 0.0858 84 ASN A ND2 658 N N . PRO A 85 ? 1.0422 1.3984 0.9640 -0.0623 -0.1830 0.0634 85 PRO A N 659 C CA . PRO A 85 ? 1.0442 1.4598 0.9745 -0.0822 -0.1907 0.0602 85 PRO A CA 660 C C . PRO A 85 ? 1.0712 1.5034 0.9863 -0.0680 -0.1972 0.0623 85 PRO A C 661 O O . PRO A 85 ? 1.1006 1.4811 0.9985 -0.0638 -0.1953 0.0624 85 PRO A O 662 C CB . PRO A 85 ? 1.0374 1.4211 0.9699 -0.1205 -0.1884 0.0527 85 PRO A CB 663 C CG . PRO A 85 ? 1.0205 1.3419 0.9523 -0.1189 -0.1796 0.0521 85 PRO A CG 664 C CD . PRO A 85 ? 1.0279 1.3247 0.9488 -0.0843 -0.1765 0.0585 85 PRO A CD 665 N N . VAL A 86 ? 1.0639 1.5698 0.9847 -0.0606 -0.2048 0.0638 86 VAL A N 666 C CA . VAL A 86 ? 1.0710 1.5975 0.9764 -0.0429 -0.2115 0.0663 86 VAL A CA 667 C C . VAL A 86 ? 1.0484 1.5611 0.9479 -0.0725 -0.2144 0.0608 86 VAL A C 668 O O . VAL A 86 ? 1.0584 1.5398 0.9393 -0.0609 -0.2156 0.0624 86 VAL A O 669 C CB . VAL A 86 ? 1.0894 1.7072 1.0019 -0.0241 -0.2194 0.0690 86 VAL A CB 670 C CG1 . VAL A 86 ? 1.0910 1.7223 1.0062 0.0089 -0.2168 0.0742 86 VAL A CG1 671 C CG2 . VAL A 86 ? 1.0791 1.7660 1.0110 -0.0613 -0.2241 0.0631 86 VAL A CG2 672 N N . ASN A 87 ? 1.0056 1.5384 0.9176 -0.1108 -0.2154 0.0543 87 ASN A N 673 C CA . ASN A 87 ? 0.9905 1.5122 0.8943 -0.1408 -0.2186 0.0483 87 ASN A CA 674 C C . ASN A 87 ? 0.9765 1.4156 0.8709 -0.1546 -0.2116 0.0443 87 ASN A C 675 O O . ASN A 87 ? 0.9673 1.3874 0.8646 -0.1841 -0.2091 0.0386 87 ASN A O 676 C CB . ASN A 87 ? 0.9895 1.5670 0.9033 -0.1774 -0.2231 0.0428 87 ASN A CB 677 C CG . ASN A 87 ? 0.9936 1.6642 0.9156 -0.1677 -0.2311 0.0453 87 ASN A CG 678 O OD1 . ASN A 87 ? 1.0340 1.7312 0.9473 -0.1592 -0.2373 0.0460 87 ASN A OD1 679 N ND2 . ASN A 87 ? 0.9830 1.7075 0.9214 -0.1685 -0.2310 0.0463 87 ASN A ND2 680 N N . ASP A 88 ? 0.9765 1.3676 0.8568 -0.1327 -0.2086 0.0473 88 ASP A N 681 C CA . ASP A 88 ? 0.9669 1.2864 0.8373 -0.1420 -0.2021 0.0435 88 ASP A CA 682 C C . ASP A 88 ? 0.9807 1.2873 0.8353 -0.1518 -0.2059 0.0401 88 ASP A C 683 O O . ASP A 88 ? 0.9729 1.3132 0.8277 -0.1730 -0.2119 0.0359 88 ASP A O 684 C CB . ASP A 88 ? 0.9583 1.2345 0.8223 -0.1143 -0.1952 0.0490 88 ASP A CB 685 C CG . ASP A 88 ? 0.9531 1.1649 0.8114 -0.1247 -0.1873 0.0447 88 ASP A CG 686 O OD1 . ASP A 88 ? 0.9483 1.1476 0.8093 -0.1502 -0.1866 0.0376 88 ASP A OD1 687 O OD2 . ASP A 88 ? 0.9640 1.1374 0.8117 -0.1070 -0.1819 0.0482 88 ASP A OD2 688 N N . LEU A 89 ? 0.9876 1.2458 0.8269 -0.1385 -0.2020 0.0414 89 LEU A N 689 C CA . LEU A 89 ? 0.9940 1.2416 0.8167 -0.1411 -0.2054 0.0396 89 LEU A CA 690 C C . LEU A 89 ? 1.0042 1.2990 0.8216 -0.1221 -0.2132 0.0455 89 LEU A C 691 O O . LEU A 89 ? 1.0107 1.2932 0.8155 -0.0937 -0.2124 0.0524 89 LEU A O 692 C CB . LEU A 89 ? 0.9888 1.1759 0.7956 -0.1305 -0.1985 0.0404 89 LEU A CB 693 C CG . LEU A 89 ? 0.9676 1.1079 0.7703 -0.1491 -0.1927 0.0326 89 LEU A CG 694 C CD1 . LEU A 89 ? 0.9465 1.0909 0.7609 -0.1731 -0.1925 0.0256 89 LEU A CD1 695 C CD2 . LEU A 89 ? 0.9624 1.0586 0.7592 -0.1356 -0.1839 0.0351 89 LEU A CD2 696 N N . CYS A 90 ? 1.0169 1.3643 0.8406 -0.1382 -0.2207 0.0425 90 CYS A N 697 C CA . CYS A 90 ? 1.0363 1.4399 0.8565 -0.1210 -0.2290 0.0472 90 CYS A CA 698 C C . CYS A 90 ? 1.0453 1.4210 0.8427 -0.1062 -0.2306 0.0497 90 CYS A C 699 O O . CYS A 90 ? 1.0612 1.4438 0.8462 -0.0747 -0.2327 0.0570 90 CYS A O 700 C CB . CYS A 90 ? 1.0454 1.5126 0.8763 -0.1479 -0.2363 0.0421 90 CYS A CB 701 S SG . CYS A 90 ? 1.0612 1.4935 0.8842 -0.1916 -0.2358 0.0315 90 CYS A SG 702 N N . TYR A 91 ? 1.0441 1.3843 0.8326 -0.1276 -0.2293 0.0436 91 TYR A N 703 C CA . TYR A 91 ? 1.0677 1.3705 0.8339 -0.1163 -0.2287 0.0455 91 TYR A CA 704 C C . TYR A 91 ? 1.0619 1.3003 0.8197 -0.1068 -0.2191 0.0472 91 TYR A C 705 O O . TYR A 91 ? 1.0578 1.2647 0.8225 -0.1251 -0.2131 0.0413 91 TYR A O 706 C CB . TYR A 91 ? 1.0901 1.3840 0.8499 -0.1433 -0.2310 0.0375 91 TYR A CB 707 C CG . TYR A 91 ? 1.1314 1.4081 0.8693 -0.1327 -0.2332 0.0396 91 TYR A CG 708 C CD1 . TYR A 91 ? 1.1522 1.3698 0.8742 -0.1273 -0.2263 0.0399 91 TYR A CD1 709 C CD2 . TYR A 91 ? 1.1443 1.4669 0.8763 -0.1293 -0.2422 0.0411 91 TYR A CD2 710 C CE1 . TYR A 91 ? 1.1795 1.3811 0.8793 -0.1198 -0.2281 0.0418 91 TYR A CE1 711 C CE2 . TYR A 91 ? 1.1711 1.4768 0.8815 -0.1197 -0.2443 0.0432 91 TYR A CE2 712 C CZ . TYR A 91 ? 1.1832 1.4267 0.8770 -0.1153 -0.2371 0.0437 91 TYR A CZ 713 O OH . TYR A 91 ? 1.2224 1.4486 0.8929 -0.1076 -0.2390 0.0458 91 TYR A OH 714 N N . PRO A 92 ? 1.0704 1.2875 0.8097 -0.0788 -0.2176 0.0551 92 PRO A N 715 C CA . PRO A 92 ? 1.0686 1.2297 0.7989 -0.0711 -0.2083 0.0573 92 PRO A CA 716 C C . PRO A 92 ? 1.0709 1.1865 0.7960 -0.0916 -0.2019 0.0506 92 PRO A C 717 O O . PRO A 92 ? 1.0864 1.2026 0.8048 -0.1042 -0.2048 0.0463 92 PRO A O 718 C CB . PRO A 92 ? 1.0955 1.2380 0.7959 -0.0410 -0.2094 0.0665 92 PRO A CB 719 C CG . PRO A 92 ? 1.1145 1.2870 0.8050 -0.0385 -0.2179 0.0670 92 PRO A CG 720 C CD . PRO A 92 ? 1.0954 1.3293 0.8142 -0.0562 -0.2241 0.0614 92 PRO A CD 721 N N . GLY A 93 ? 1.0786 1.1581 0.8065 -0.0941 -0.1933 0.0495 93 GLY A N 722 C CA . GLY A 93 ? 1.0822 1.1233 0.8048 -0.1103 -0.1867 0.0429 93 GLY A CA 723 C C . GLY A 93 ? 1.0709 1.0852 0.8022 -0.1134 -0.1779 0.0411 93 GLY A C 724 O O . GLY A 93 ? 1.0584 1.0633 0.7872 -0.0986 -0.1748 0.0472 93 GLY A O 725 N N . ASP A 94 ? 1.0677 1.0685 0.8062 -0.1313 -0.1740 0.0324 94 ASP A N 726 C CA . ASP A 94 ? 1.0533 1.0340 0.8019 -0.1358 -0.1662 0.0290 94 ASP A CA 727 C C . ASP A 94 ? 1.0393 1.0272 0.8016 -0.1529 -0.1673 0.0199 94 ASP A C 728 O O . ASP A 94 ? 1.0513 1.0486 0.8091 -0.1633 -0.1725 0.0152 94 ASP A O 729 C CB . ASP A 94 ? 1.0651 1.0110 0.7974 -0.1370 -0.1582 0.0272 94 ASP A CB 730 C CG . ASP A 94 ? 1.1036 1.0312 0.8133 -0.1231 -0.1563 0.0360 94 ASP A CG 731 O OD1 . ASP A 94 ? 1.1184 1.0410 0.8285 -0.1111 -0.1545 0.0422 94 ASP A OD1 732 O OD2 . ASP A 94 ? 1.1547 1.0699 0.8428 -0.1242 -0.1566 0.0367 94 ASP A OD2 733 N N . PHE A 95 ? 1.0150 0.9950 0.7903 -0.1556 -0.1627 0.0175 95 PHE A N 734 C CA . PHE A 95 ? 0.9883 0.9636 0.7699 -0.1701 -0.1626 0.0088 95 PHE A CA 735 C C . PHE A 95 ? 0.9814 0.9283 0.7600 -0.1686 -0.1540 0.0041 95 PHE A C 736 O O . PHE A 95 ? 0.9730 0.9135 0.7599 -0.1621 -0.1486 0.0071 95 PHE A O 737 C CB . PHE A 95 ? 0.9726 0.9673 0.7707 -0.1743 -0.1652 0.0105 95 PHE A CB 738 C CG . PHE A 95 ? 0.9768 0.9674 0.7733 -0.1924 -0.1679 0.0025 95 PHE A CG 739 C CD1 . PHE A 95 ? 0.9807 0.9397 0.7695 -0.1966 -0.1632 -0.0054 95 PHE A CD1 740 C CD2 . PHE A 95 ? 0.9803 0.9986 0.7795 -0.2052 -0.1752 0.0027 95 PHE A CD2 741 C CE1 . PHE A 95 ? 0.9954 0.9419 0.7750 -0.2117 -0.1659 -0.0126 95 PHE A CE1 742 C CE2 . PHE A 95 ? 0.9921 0.9997 0.7828 -0.2247 -0.1776 -0.0045 95 PHE A CE2 743 C CZ . PHE A 95 ? 1.0068 0.9741 0.7855 -0.2271 -0.1730 -0.0121 95 PHE A CZ 744 N N . ASN A 96 ? 0.9849 0.9180 0.7509 -0.1741 -0.1527 -0.0033 96 ASN A N 745 C CA . ASN A 96 ? 0.9740 0.8883 0.7352 -0.1716 -0.1447 -0.0085 96 ASN A CA 746 C C . ASN A 96 ? 0.9531 0.8587 0.7240 -0.1725 -0.1414 -0.0133 96 ASN A C 747 O O . ASN A 96 ? 0.9437 0.8472 0.7150 -0.1794 -0.1456 -0.0174 96 ASN A O 748 C CB . ASN A 96 ? 0.9966 0.9041 0.7414 -0.1758 -0.1451 -0.0163 96 ASN A CB 749 C CG . ASN A 96 ? 1.0047 0.9031 0.7428 -0.1724 -0.1367 -0.0208 96 ASN A CG 750 O OD1 . ASN A 96 ? 0.9941 0.8920 0.7284 -0.1699 -0.1322 -0.0156 96 ASN A OD1 751 N ND2 . ASN A 96 ? 1.0175 0.9088 0.7508 -0.1724 -0.1347 -0.0309 96 ASN A ND2 752 N N . ASP A 97 ? 0.9359 0.8347 0.7114 -0.1664 -0.1338 -0.0128 97 ASP A N 753 C CA . ASP A 97 ? 0.9264 0.8178 0.7109 -0.1648 -0.1299 -0.0167 97 ASP A CA 754 C C . ASP A 97 ? 0.9029 0.7994 0.6996 -0.1684 -0.1344 -0.0132 97 ASP A C 755 O O . ASP A 97 ? 0.8987 0.7850 0.6944 -0.1722 -0.1352 -0.0186 97 ASP A O 756 C CB . ASP A 97 ? 0.9600 0.8394 0.7325 -0.1648 -0.1283 -0.0279 97 ASP A CB 757 C CG . ASP A 97 ? 0.9712 0.8528 0.7375 -0.1598 -0.1209 -0.0321 97 ASP A CG 758 O OD1 . ASP A 97 ? 0.9803 0.8667 0.7539 -0.1578 -0.1152 -0.0273 97 ASP A OD1 759 O OD2 . ASP A 97 ? 0.9928 0.8726 0.7454 -0.1585 -0.1207 -0.0403 97 ASP A OD2 760 N N . TYR A 98 ? 0.8858 0.7980 0.6911 -0.1664 -0.1373 -0.0043 98 TYR A N 761 C CA . TYR A 98 ? 0.8816 0.8088 0.6988 -0.1706 -0.1421 -0.0006 98 TYR A CA 762 C C . TYR A 98 ? 0.8618 0.7822 0.6909 -0.1692 -0.1376 -0.0009 98 TYR A C 763 O O . TYR A 98 ? 0.8644 0.7857 0.6967 -0.1778 -0.1404 -0.0029 98 TYR A O 764 C CB . TYR A 98 ? 0.8849 0.8344 0.7073 -0.1632 -0.1453 0.0089 98 TYR A CB 765 C CG . TYR A 98 ? 0.8879 0.8659 0.7225 -0.1669 -0.1513 0.0131 98 TYR A CG 766 C CD1 . TYR A 98 ? 0.8923 0.8791 0.7255 -0.1833 -0.1569 0.0083 98 TYR A CD1 767 C CD2 . TYR A 98 ? 0.8729 0.8699 0.7170 -0.1544 -0.1515 0.0215 98 TYR A CD2 768 C CE1 . TYR A 98 ? 0.8885 0.9075 0.7321 -0.1900 -0.1620 0.0117 98 TYR A CE1 769 C CE2 . TYR A 98 ? 0.8711 0.9024 0.7270 -0.1570 -0.1569 0.0248 98 TYR A CE2 770 C CZ . TYR A 98 ? 0.8811 0.9263 0.7380 -0.1762 -0.1620 0.0199 98 TYR A CZ 771 O OH . TYR A 98 ? 0.8873 0.9725 0.7552 -0.1822 -0.1671 0.0227 98 TYR A OH 772 N N . GLU A 99 ? 0.8512 0.7636 0.6840 -0.1599 -0.1305 0.0009 99 GLU A N 773 C CA . GLU A 99 ? 0.8391 0.7472 0.6839 -0.1570 -0.1260 0.0014 99 GLU A CA 774 C C . GLU A 99 ? 0.8459 0.7365 0.6851 -0.1605 -0.1239 -0.0074 99 GLU A C 775 O O . GLU A 99 ? 0.8478 0.7341 0.6934 -0.1626 -0.1235 -0.0082 99 GLU A O 776 C CB . GLU A 99 ? 0.8368 0.7401 0.6832 -0.1477 -0.1189 0.0057 99 GLU A CB 777 C CG . GLU A 99 ? 0.8424 0.7555 0.6896 -0.1402 -0.1207 0.0153 99 GLU A CG 778 C CD . GLU A 99 ? 0.8596 0.7754 0.6923 -0.1391 -0.1246 0.0176 99 GLU A CD 779 O OE1 . GLU A 99 ? 0.8774 0.7826 0.6976 -0.1432 -0.1226 0.0128 99 GLU A OE1 780 O OE2 . GLU A 99 ? 0.8515 0.7823 0.6846 -0.1332 -0.1298 0.0241 99 GLU A OE2 781 N N . GLU A 100 ? 0.8555 0.7360 0.6806 -0.1598 -0.1226 -0.0143 100 GLU A N 782 C CA . GLU A 100 ? 0.8613 0.7239 0.6753 -0.1590 -0.1215 -0.0237 100 GLU A CA 783 C C . GLU A 100 ? 0.8717 0.7230 0.6754 -0.1693 -0.1284 -0.0263 100 GLU A C 784 O O . GLU A 100 ? 0.8840 0.7151 0.6780 -0.1696 -0.1283 -0.0315 100 GLU A O 785 C CB . GLU A 100 ? 0.8688 0.7282 0.6685 -0.1541 -0.1188 -0.0308 100 GLU A CB 786 C CG . GLU A 100 ? 0.8619 0.7300 0.6670 -0.1468 -0.1105 -0.0311 100 GLU A CG 787 C CD . GLU A 100 ? 0.8645 0.7273 0.6733 -0.1396 -0.1059 -0.0356 100 GLU A CD 788 O OE1 . GLU A 100 ? 0.8861 0.7351 0.6820 -0.1348 -0.1075 -0.0435 100 GLU A OE1 789 O OE2 . GLU A 100 ? 0.8577 0.7279 0.6793 -0.1377 -0.1007 -0.0315 100 GLU A OE2 790 N N . LEU A 101 ? 0.8721 0.7356 0.6749 -0.1784 -0.1346 -0.0227 101 LEU A N 791 C CA . LEU A 101 ? 0.8850 0.7411 0.6760 -0.1929 -0.1413 -0.0250 101 LEU A CA 792 C C . LEU A 101 ? 0.8665 0.7315 0.6705 -0.1999 -0.1422 -0.0199 101 LEU A C 793 O O . LEU A 101 ? 0.8636 0.7083 0.6545 -0.2094 -0.1438 -0.0238 101 LEU A O 794 C CB . LEU A 101 ? 0.8899 0.7632 0.6767 -0.2015 -0.1477 -0.0229 101 LEU A CB 795 C CG . LEU A 101 ? 0.9145 0.7840 0.6867 -0.2209 -0.1549 -0.0254 101 LEU A CG 796 C CD1 . LEU A 101 ? 0.9339 0.7615 0.6763 -0.2255 -0.1553 -0.0353 101 LEU A CD1 797 C CD2 . LEU A 101 ? 0.9282 0.8211 0.6986 -0.2276 -0.1609 -0.0232 101 LEU A CD2 798 N N . LYS A 102 ? 0.8348 0.7280 0.6609 -0.1949 -0.1411 -0.0115 102 LYS A N 799 C CA . LYS A 102 ? 0.8319 0.7390 0.6727 -0.1990 -0.1412 -0.0065 102 LYS A CA 800 C C . LYS A 102 ? 0.8353 0.7172 0.6743 -0.1958 -0.1361 -0.0100 102 LYS A C 801 O O . LYS A 102 ? 0.8354 0.7127 0.6726 -0.2062 -0.1375 -0.0101 102 LYS A O 802 C CB . LYS A 102 ? 0.8150 0.7506 0.6762 -0.1874 -0.1395 0.0023 102 LYS A CB 803 C CG . LYS A 102 ? 0.8315 0.7981 0.6950 -0.1896 -0.1458 0.0071 102 LYS A CG 804 C CD . LYS A 102 ? 0.8274 0.8141 0.7033 -0.1728 -0.1440 0.0155 102 LYS A CD 805 C CE . LYS A 102 ? 0.8235 0.8440 0.7147 -0.1732 -0.1467 0.0211 102 LYS A CE 806 N NZ . LYS A 102 ? 0.8203 0.8555 0.7179 -0.1528 -0.1453 0.0291 102 LYS A NZ 807 N N . HIS A 103 ? 0.8409 0.7084 0.6787 -0.1822 -0.1301 -0.0131 103 HIS A N 808 C CA . HIS A 103 ? 0.8561 0.7021 0.6905 -0.1764 -0.1253 -0.0173 103 HIS A CA 809 C C . HIS A 103 ? 0.8921 0.7062 0.6996 -0.1841 -0.1287 -0.0250 103 HIS A C 810 O O . HIS A 103 ? 0.9211 0.7169 0.7224 -0.1855 -0.1276 -0.0265 103 HIS A O 811 C CB . HIS A 103 ? 0.8513 0.6950 0.6877 -0.1614 -0.1185 -0.0202 103 HIS A CB 812 C CG . HIS A 103 ? 0.8521 0.6788 0.6844 -0.1531 -0.1138 -0.0252 103 HIS A CG 813 N ND1 . HIS A 103 ? 0.8354 0.6685 0.6841 -0.1488 -0.1093 -0.0212 103 HIS A ND1 814 C CD2 . HIS A 103 ? 0.8623 0.6656 0.6736 -0.1467 -0.1134 -0.0340 103 HIS A CD2 815 C CE1 . HIS A 103 ? 0.8355 0.6520 0.6751 -0.1408 -0.1062 -0.0272 103 HIS A CE1 816 N NE2 . HIS A 103 ? 0.8522 0.6503 0.6682 -0.1382 -0.1087 -0.0350 103 HIS A NE2 817 N N . LEU A 104 ? 0.9209 0.7245 0.7088 -0.1886 -0.1327 -0.0299 104 LEU A N 818 C CA . LEU A 104 ? 0.9775 0.7440 0.7323 -0.1958 -0.1364 -0.0374 104 LEU A CA 819 C C . LEU A 104 ? 1.0124 0.7730 0.7601 -0.2169 -0.1410 -0.0346 104 LEU A C 820 O O . LEU A 104 ? 1.0454 0.7688 0.7662 -0.2224 -0.1419 -0.0391 104 LEU A O 821 C CB . LEU A 104 ? 1.0066 0.7668 0.7425 -0.1985 -0.1403 -0.0423 104 LEU A CB 822 C CG . LEU A 104 ? 1.0413 0.7622 0.7420 -0.1896 -0.1404 -0.0529 104 LEU A CG 823 C CD1 . LEU A 104 ? 1.0282 0.7508 0.7347 -0.1660 -0.1335 -0.0567 104 LEU A CD1 824 C CD2 . LEU A 104 ? 1.0541 0.7758 0.7405 -0.1947 -0.1447 -0.0563 104 LEU A CD2 825 N N . LEU A 105 ? 1.0202 0.8183 0.7893 -0.2283 -0.1438 -0.0273 105 LEU A N 826 C CA . LEU A 105 ? 1.0322 0.8392 0.7985 -0.2510 -0.1482 -0.0241 105 LEU A CA 827 C C . LEU A 105 ? 1.0313 0.8333 0.8054 -0.2515 -0.1448 -0.0214 105 LEU A C 828 O O . LEU A 105 ? 1.0733 0.8685 0.8342 -0.2721 -0.1478 -0.0211 105 LEU A O 829 C CB . LEU A 105 ? 1.0050 0.8646 0.7967 -0.2572 -0.1515 -0.0168 105 LEU A CB 830 C CG . LEU A 105 ? 1.0123 0.8867 0.7942 -0.2690 -0.1578 -0.0179 105 LEU A CG 831 C CD1 . LEU A 105 ? 0.9935 0.9250 0.8019 -0.2719 -0.1608 -0.0099 105 LEU A CD1 832 C CD2 . LEU A 105 ? 1.0669 0.9112 0.8133 -0.2943 -0.1628 -0.0241 105 LEU A CD2 833 N N . SER A 106 ? 1.1422 1.0791 0.7237 -0.3615 -0.1539 0.0222 106 SER A N 834 C CA . SER A 106 ? 1.1781 1.1150 0.7384 -0.3689 -0.1547 0.0268 106 SER A CA 835 C C . SER A 106 ? 1.2195 1.1192 0.7489 -0.3707 -0.1704 0.0376 106 SER A C 836 O O . SER A 106 ? 1.2423 1.1358 0.7464 -0.3795 -0.1720 0.0463 106 SER A O 837 C CB . SER A 106 ? 1.1648 1.1215 0.7370 -0.3572 -0.1503 0.0150 106 SER A CB 838 O OG . SER A 106 ? 1.1731 1.1148 0.7495 -0.3411 -0.1612 0.0093 106 SER A OG 839 N N . ARG A 107 ? 1.2511 1.1257 0.7820 -0.3612 -0.1811 0.0371 107 ARG A N 840 C CA . ARG A 107 ? 1.3209 1.1560 0.8255 -0.3611 -0.1961 0.0473 107 ARG A CA 841 C C . ARG A 107 ? 1.3119 1.1240 0.8071 -0.3759 -0.1980 0.0562 107 ARG A C 842 O O . ARG A 107 ? 1.3305 1.1056 0.8061 -0.3761 -0.2095 0.0643 107 ARG A O 843 C CB . ARG A 107 ? 1.3625 1.1823 0.8757 -0.3402 -0.2069 0.0395 107 ARG A CB 844 C CG . ARG A 107 ? 1.4029 1.2336 0.9185 -0.3262 -0.2116 0.0330 107 ARG A CG 845 C CD . ARG A 107 ? 1.4968 1.2975 0.9846 -0.3205 -0.2284 0.0424 107 ARG A CD 846 N NE . ARG A 107 ? 1.5410 1.3471 1.0416 -0.3004 -0.2376 0.0319 107 ARG A NE 847 C CZ . ARG A 107 ? 1.6032 1.3957 1.0854 -0.2910 -0.2528 0.0364 107 ARG A CZ 848 N NH1 . ARG A 107 ? 1.6507 1.4195 1.0964 -0.2991 -0.2602 0.0533 107 ARG A NH1 849 N NH2 . ARG A 107 ? 1.6064 1.4097 1.1075 -0.2728 -0.2605 0.0241 107 ARG A NH2 850 N N . ILE A 108 ? 1.2675 1.1012 0.7779 -0.3880 -0.1873 0.0541 108 ILE A N 851 C CA . ILE A 108 ? 1.2707 1.0878 0.7788 -0.4022 -0.1897 0.0586 108 ILE A CA 852 C C . ILE A 108 ? 1.2683 1.1011 0.7739 -0.4255 -0.1793 0.0663 108 ILE A C 853 O O . ILE A 108 ? 1.2371 1.1072 0.7581 -0.4286 -0.1669 0.0624 108 ILE A O 854 C CB . ILE A 108 ? 1.2403 1.0691 0.7721 -0.3943 -0.1891 0.0470 108 ILE A CB 855 C CG1 . ILE A 108 ? 1.2268 1.0407 0.7622 -0.3717 -0.1969 0.0392 108 ILE A CG1 856 C CG2 . ILE A 108 ? 1.2582 1.0704 0.7870 -0.4095 -0.1936 0.0492 108 ILE A CG2 857 C CD1 . ILE A 108 ? 1.1967 1.0223 0.7514 -0.3617 -0.1947 0.0286 108 ILE A CD1 858 N N . ASN A 109 ? 1.2963 1.1000 0.7847 -0.4420 -0.1835 0.0769 109 ASN A N 859 C CA . ASN A 109 ? 1.3039 1.1196 0.7915 -0.4666 -0.1729 0.0848 109 ASN A CA 860 C C . ASN A 109 ? 1.2946 1.1111 0.7989 -0.4811 -0.1736 0.0809 109 ASN A C 861 O O . ASN A 109 ? 1.2866 1.1267 0.8021 -0.4999 -0.1632 0.0829 109 ASN A O 862 C CB . ASN A 109 ? 1.3589 1.1422 0.8133 -0.4782 -0.1740 0.1020 109 ASN A CB 863 C CG . ASN A 109 ? 1.3665 1.1564 0.8023 -0.4670 -0.1726 0.1061 109 ASN A CG 864 O OD1 . ASN A 109 ? 1.3544 1.1793 0.7953 -0.4709 -0.1601 0.1040 109 ASN A OD1 865 N ND2 . ASN A 109 ? 1.3931 1.1505 0.8079 -0.4524 -0.1860 0.1106 109 ASN A ND2 866 N N . HIS A 110 ? 1.2865 1.0787 0.7930 -0.4729 -0.1858 0.0741 110 HIS A N 867 C CA . HIS A 110 ? 1.2864 1.0791 0.8076 -0.4863 -0.1887 0.0679 110 HIS A CA 868 C C . HIS A 110 ? 1.2663 1.0496 0.7954 -0.4695 -0.1998 0.0545 110 HIS A C 869 O O . HIS A 110 ? 1.2603 1.0102 0.7751 -0.4549 -0.2093 0.0539 110 HIS A O 870 C CB . HIS A 110 ? 1.3422 1.0975 0.8471 -0.5091 -0.1909 0.0789 110 HIS A CB 871 C CG . HIS A 110 ? 1.3462 1.1097 0.8700 -0.5294 -0.1912 0.0722 110 HIS A CG 872 N ND1 . HIS A 110 ? 1.3885 1.1115 0.9035 -0.5463 -0.1973 0.0754 110 HIS A ND1 873 C CD2 . HIS A 110 ? 1.3119 1.1198 0.8641 -0.5353 -0.1868 0.0617 110 HIS A CD2 874 C CE1 . HIS A 110 ? 1.3868 1.1309 0.9253 -0.5631 -0.1969 0.0657 110 HIS A CE1 875 N NE2 . HIS A 110 ? 1.3345 1.1313 0.8956 -0.5561 -0.1912 0.0576 110 HIS A NE2 876 N N . PHE A 111 ? 1.2507 1.0657 0.8023 -0.4711 -0.1984 0.0438 111 PHE A N 877 C CA . PHE A 111 ? 1.2565 1.0654 0.8136 -0.4587 -0.2082 0.0309 111 PHE A CA 878 C C . PHE A 111 ? 1.2919 1.0901 0.8529 -0.4794 -0.2149 0.0262 111 PHE A C 879 O O . PHE A 111 ? 1.3010 1.1190 0.8735 -0.5008 -0.2089 0.0296 111 PHE A O 880 C CB . PHE A 111 ? 1.2121 1.0655 0.7904 -0.4444 -0.2029 0.0222 111 PHE A CB 881 C CG . PHE A 111 ? 1.1754 1.0359 0.7538 -0.4208 -0.1977 0.0220 111 PHE A CG 882 C CD1 . PHE A 111 ? 1.1839 1.0127 0.7486 -0.4043 -0.2044 0.0203 111 PHE A CD1 883 C CD2 . PHE A 111 ? 1.1355 1.0358 0.7311 -0.4148 -0.1859 0.0221 111 PHE A CD2 884 C CE1 . PHE A 111 ? 1.1478 0.9861 0.7172 -0.3840 -0.1991 0.0186 111 PHE A CE1 885 C CE2 . PHE A 111 ? 1.1082 1.0146 0.7072 -0.3947 -0.1803 0.0205 111 PHE A CE2 886 C CZ . PHE A 111 ? 1.1148 0.9911 0.7014 -0.3800 -0.1869 0.0186 111 PHE A CZ 887 N N . GLU A 112 ? 1.3209 1.0895 0.8741 -0.4732 -0.2268 0.0168 112 GLU A N 888 C CA . GLU A 112 ? 1.3598 1.1220 0.9196 -0.4904 -0.2348 0.0071 112 GLU A CA 889 C C . GLU A 112 ? 1.3325 1.1112 0.8985 -0.4726 -0.2423 -0.0092 112 GLU A C 890 O O . GLU A 112 ? 1.3259 1.0792 0.8784 -0.4538 -0.2482 -0.0147 112 GLU A O 891 C CB . GLU A 112 ? 1.4273 1.1320 0.9685 -0.5016 -0.2422 0.0104 112 GLU A CB 892 C CG . GLU A 112 ? 1.4706 1.1665 1.0204 -0.5321 -0.2442 0.0080 112 GLU A CG 893 C CD . GLU A 112 ? 1.5117 1.2003 1.0672 -0.5336 -0.2570 -0.0119 112 GLU A CD 894 O OE1 . GLU A 112 ? 1.5040 1.2293 1.0707 -0.5208 -0.2604 -0.0246 112 GLU A OE1 895 O OE2 . GLU A 112 ? 1.5737 1.2185 1.1214 -0.5471 -0.2636 -0.0153 112 GLU A OE2 896 N N . LYS A 113 ? 1.3074 1.1304 0.8935 -0.4773 -0.2415 -0.0164 113 LYS A N 897 C CA . LYS A 113 ? 1.2898 1.1339 0.8797 -0.4591 -0.2477 -0.0298 113 LYS A CA 898 C C . LYS A 113 ? 1.3214 1.1384 0.9018 -0.4634 -0.2622 -0.0450 113 LYS A C 899 O O . LYS A 113 ? 1.3528 1.1627 0.9398 -0.4874 -0.2678 -0.0497 113 LYS A O 900 C CB . LYS A 113 ? 1.2586 1.1588 0.8729 -0.4630 -0.2439 -0.0318 113 LYS A CB 901 C CG . LYS A 113 ? 1.2464 1.1723 0.8636 -0.4451 -0.2510 -0.0439 113 LYS A CG 902 C CD . LYS A 113 ? 1.2117 1.1859 0.8463 -0.4318 -0.2411 -0.0383 113 LYS A CD 903 C CE . LYS A 113 ? 1.1999 1.2120 0.8606 -0.4516 -0.2356 -0.0342 113 LYS A CE 904 N NZ . LYS A 113 ? 1.1656 1.2161 0.8415 -0.4362 -0.2230 -0.0267 113 LYS A NZ 905 N N . ILE A 114 ? 1.3247 1.1260 0.8902 -0.4409 -0.2674 -0.0537 114 ILE A N 906 C CA . ILE A 114 ? 1.3786 1.1595 0.9344 -0.4423 -0.2810 -0.0714 114 ILE A CA 907 C C . ILE A 114 ? 1.3712 1.1724 0.9202 -0.4180 -0.2846 -0.0829 114 ILE A C 908 O O . ILE A 114 ? 1.3466 1.1596 0.8924 -0.3955 -0.2758 -0.0763 114 ILE A O 909 C CB . ILE A 114 ? 1.4270 1.1478 0.9638 -0.4431 -0.2860 -0.0733 114 ILE A CB 910 C CG1 . ILE A 114 ? 1.4213 1.1234 0.9450 -0.4174 -0.2797 -0.0659 114 ILE A CG1 911 C CG2 . ILE A 114 ? 1.4564 1.1517 0.9970 -0.4706 -0.2849 -0.0637 114 ILE A CG2 912 C CD1 . ILE A 114 ? 1.4623 1.1121 0.9678 -0.4095 -0.2870 -0.0740 114 ILE A CD1 913 N N . GLN A 115 ? 1.3873 1.1913 0.9332 -0.4234 -0.2974 -0.1005 115 GLN A N 914 C CA . GLN A 115 ? 1.3825 1.2076 0.9184 -0.4023 -0.3024 -0.1123 115 GLN A CA 915 C C . GLN A 115 ? 1.4020 1.1865 0.9129 -0.3836 -0.3041 -0.1208 115 GLN A C 916 O O . GLN A 115 ? 1.4238 1.1697 0.9251 -0.3933 -0.3127 -0.1322 115 GLN A O 917 C CB . GLN A 115 ? 1.4066 1.2550 0.9495 -0.4168 -0.3171 -0.1294 115 GLN A CB 918 C CG . GLN A 115 ? 1.4043 1.2831 0.9360 -0.3955 -0.3236 -0.1403 115 GLN A CG 919 C CD . GLN A 115 ? 1.4257 1.3229 0.9617 -0.4102 -0.3416 -0.1608 115 GLN A CD 920 O OE1 . GLN A 115 ? 1.4106 1.3564 0.9617 -0.4114 -0.3465 -0.1620 115 GLN A OE1 921 N NE2 . GLN A 115 ? 1.4616 1.3203 0.9857 -0.4212 -0.3521 -0.1782 115 GLN A NE2 922 N N . ILE A 116 ? 1.3885 1.1814 0.8906 -0.3569 -0.2947 -0.1156 116 ILE A N 923 C CA . ILE A 116 ? 1.4164 1.1752 0.8970 -0.3371 -0.2938 -0.1236 116 ILE A CA 924 C C . ILE A 116 ? 1.4417 1.2151 0.9044 -0.3208 -0.2994 -0.1390 116 ILE A C 925 O O . ILE A 116 ? 1.4771 1.2206 0.9205 -0.3136 -0.3051 -0.1543 116 ILE A O 926 C CB . ILE A 116 ? 1.3755 1.1274 0.8573 -0.3180 -0.2785 -0.1092 116 ILE A CB 927 C CG1 . ILE A 116 ? 1.3268 1.1225 0.8243 -0.3116 -0.2670 -0.0948 116 ILE A CG1 928 C CG2 . ILE A 116 ? 1.3772 1.0921 0.8629 -0.3284 -0.2777 -0.1011 116 ILE A CG2 929 C CD1 . ILE A 116 ? 1.3037 1.1001 0.8002 -0.2876 -0.2522 -0.0869 116 ILE A CD1 930 N N . ILE A 117 ? 1.4263 1.2450 0.8940 -0.3138 -0.2978 -0.1351 117 ILE A N 931 C CA . ILE A 117 ? 1.4476 1.2843 0.8959 -0.2992 -0.3048 -0.1485 117 ILE A CA 932 C C . ILE A 117 ? 1.4488 1.3272 0.9094 -0.3127 -0.3170 -0.1530 117 ILE A C 933 O O . ILE A 117 ? 1.4236 1.3383 0.9023 -0.3117 -0.3107 -0.1387 117 ILE A O 934 C CB . ILE A 117 ? 1.4269 1.2787 0.8644 -0.2699 -0.2900 -0.1385 117 ILE A CB 935 C CG1 . ILE A 117 ? 1.4174 1.2329 0.8498 -0.2576 -0.2769 -0.1339 117 ILE A CG1 936 C CG2 . ILE A 117 ? 1.4544 1.3211 0.8656 -0.2540 -0.2975 -0.1521 117 ILE A CG2 937 C CD1 . ILE A 117 ? 1.3951 1.2225 0.8205 -0.2308 -0.2596 -0.1241 117 ILE A CD1 938 N N . PRO A 118 ? 1.4847 1.3586 0.9378 -0.3256 -0.3348 -0.1741 118 PRO A N 939 C CA . PRO A 118 ? 1.4918 1.4081 0.9588 -0.3388 -0.3488 -0.1817 118 PRO A CA 940 C C . PRO A 118 ? 1.4881 1.4489 0.9446 -0.3154 -0.3501 -0.1791 118 PRO A C 941 O O . PRO A 118 ? 1.5063 1.4591 0.9336 -0.2912 -0.3470 -0.1826 118 PRO A O 942 C CB . PRO A 118 ? 1.5391 1.4328 0.9962 -0.3547 -0.3670 -0.2082 118 PRO A CB 943 C CG . PRO A 118 ? 1.5457 1.3814 0.9955 -0.3596 -0.3606 -0.2087 118 PRO A CG 944 C CD . PRO A 118 ? 1.5234 1.3495 0.9616 -0.3333 -0.3426 -0.1918 118 PRO A CD 945 N N . LYS A 119 ? 1.4680 1.4749 0.9483 -0.3221 -0.3538 -0.1724 119 LYS A N 946 C CA . LYS A 119 ? 1.4659 1.5168 0.9391 -0.3000 -0.3559 -0.1674 119 LYS A CA 947 C C . LYS A 119 ? 1.5233 1.5816 0.9690 -0.2927 -0.3753 -0.1903 119 LYS A C 948 O O . LYS A 119 ? 1.5557 1.6280 0.9747 -0.2660 -0.3745 -0.1882 119 LYS A O 949 C CB . LYS A 119 ? 1.4400 1.5387 0.9488 -0.3113 -0.3583 -0.1584 119 LYS A CB 950 C CG . LYS A 119 ? 1.4182 1.5544 0.9280 -0.2857 -0.3498 -0.1410 119 LYS A CG 951 C CD . LYS A 119 ? 1.3965 1.5777 0.9455 -0.2979 -0.3512 -0.1330 119 LYS A CD 952 C CE . LYS A 119 ? 1.3899 1.6145 0.9383 -0.2716 -0.3507 -0.1216 119 LYS A CE 953 N NZ . LYS A 119 ? 1.3662 1.6357 0.9555 -0.2814 -0.3508 -0.1140 119 LYS A NZ 954 N N . SER A 120 ? 1.5489 1.5964 1.0001 -0.3168 -0.3921 -0.2123 120 SER A N 955 C CA . SER A 120 ? 1.5814 1.6327 1.0071 -0.3135 -0.4123 -0.2387 120 SER A CA 956 C C . SER A 120 ? 1.6094 1.6267 0.9923 -0.2886 -0.4052 -0.2432 120 SER A C 957 O O . SER A 120 ? 1.6492 1.6824 1.0018 -0.2703 -0.4149 -0.2547 120 SER A O 958 C CB . SER A 120 ? 1.5970 1.6285 1.0375 -0.3460 -0.4275 -0.2621 120 SER A CB 959 O OG . SER A 120 ? 1.5989 1.5706 1.0274 -0.3511 -0.4187 -0.2655 120 SER A OG 960 N N . SER A 121 ? 1.6087 1.5808 0.9891 -0.2874 -0.3881 -0.2342 121 SER A N 961 C CA . SER A 121 ? 1.6386 1.5738 0.9831 -0.2674 -0.3807 -0.2416 121 SER A CA 962 C C . SER A 121 ? 1.6260 1.5799 0.9408 -0.2335 -0.3705 -0.2314 121 SER A C 963 O O . SER A 121 ? 1.6453 1.5765 0.9265 -0.2168 -0.3673 -0.2422 121 SER A O 964 C CB . SER A 121 ? 1.6370 1.5249 0.9903 -0.2713 -0.3638 -0.2314 121 SER A CB 965 O OG . SER A 121 ? 1.6796 1.5323 1.0428 -0.2962 -0.3733 -0.2468 121 SER A OG 966 N N . TRP A 122 ? 1.5895 1.5824 0.9158 -0.2229 -0.3641 -0.2105 122 TRP A N 967 C CA . TRP A 122 ? 1.5907 1.5978 0.8893 -0.1907 -0.3517 -0.1972 122 TRP A CA 968 C C . TRP A 122 ? 1.6344 1.6705 0.9012 -0.1777 -0.3700 -0.2122 122 TRP A C 969 O O . TRP A 122 ? 1.6400 1.7185 0.9087 -0.1674 -0.3754 -0.2018 122 TRP A O 970 C CB . TRP A 122 ? 1.5445 1.5775 0.8675 -0.1830 -0.3362 -0.1684 122 TRP A CB 971 C CG . TRP A 122 ? 1.5096 1.5149 0.8578 -0.1915 -0.3172 -0.1540 122 TRP A CG 972 C CD1 . TRP A 122 ? 1.4786 1.4911 0.8648 -0.2115 -0.3151 -0.1442 122 TRP A CD1 973 C CD2 . TRP A 122 ? 1.5064 1.4740 0.8436 -0.1800 -0.2982 -0.1491 122 TRP A CD2 974 N NE1 . TRP A 122 ? 1.4671 1.4488 0.8642 -0.2126 -0.2971 -0.1332 122 TRP A NE1 975 C CE2 . TRP A 122 ? 1.4791 1.4337 0.8487 -0.1936 -0.2870 -0.1363 122 TRP A CE2 976 C CE3 . TRP A 122 ? 1.5297 1.4754 0.8333 -0.1592 -0.2891 -0.1546 122 TRP A CE3 977 C CZ2 . TRP A 122 ? 1.4598 1.3819 0.8310 -0.1870 -0.2691 -0.1295 122 TRP A CZ2 978 C CZ3 . TRP A 122 ? 1.5226 1.4358 0.8304 -0.1531 -0.2696 -0.1478 122 TRP A CZ3 979 C CH2 . TRP A 122 ? 1.4887 1.3912 0.8310 -0.1669 -0.2608 -0.1356 122 TRP A CH2 980 N N . SER A 123 ? 1.6766 1.6893 0.9134 -0.1772 -0.3799 -0.2373 123 SER A N 981 C CA . SER A 123 ? 1.7177 1.7558 0.9228 -0.1687 -0.4014 -0.2578 123 SER A CA 982 C C . SER A 123 ? 1.7370 1.7943 0.9031 -0.1337 -0.3919 -0.2438 123 SER A C 983 O O . SER A 123 ? 1.7621 1.8595 0.9128 -0.1235 -0.4082 -0.2467 123 SER A O 984 C CB . SER A 123 ? 1.7577 1.7608 0.9407 -0.1778 -0.4127 -0.2902 123 SER A CB 985 O OG . SER A 123 ? 1.7593 1.7198 0.9211 -0.1632 -0.3918 -0.2874 123 SER A OG 986 N N . SER A 124 ? 1.7234 1.7532 0.8748 -0.1155 -0.3655 -0.2280 124 SER A N 987 C CA . SER A 124 ? 1.7295 1.7701 0.8409 -0.0824 -0.3520 -0.2137 124 SER A CA 988 C C . SER A 124 ? 1.6840 1.7514 0.8130 -0.0691 -0.3373 -0.1801 124 SER A C 989 O O . SER A 124 ? 1.6834 1.7593 0.7821 -0.0418 -0.3242 -0.1639 124 SER A O 990 C CB . SER A 124 ? 1.7429 1.7410 0.8311 -0.0693 -0.3289 -0.2147 124 SER A CB 991 O OG . SER A 124 ? 1.7721 1.7383 0.8565 -0.0850 -0.3393 -0.2436 124 SER A OG 992 N N . HIS A 125 ? 1.6382 1.7166 0.8152 -0.0883 -0.3381 -0.1694 125 HIS A N 993 C CA . HIS A 125 ? 1.6026 1.7064 0.8013 -0.0780 -0.3255 -0.1401 125 HIS A CA 994 C C . HIS A 125 ? 1.5913 1.7344 0.8247 -0.0953 -0.3463 -0.1423 125 HIS A C 995 O O . HIS A 125 ? 1.5940 1.7369 0.8451 -0.1210 -0.3649 -0.1634 125 HIS A O 996 C CB . HIS A 125 ? 1.5510 1.6268 0.7784 -0.0823 -0.2983 -0.1218 125 HIS A CB 997 C CG . HIS A 125 ? 1.5590 1.5981 0.7607 -0.0673 -0.2764 -0.1202 125 HIS A CG 998 N ND1 . HIS A 125 ? 1.5720 1.5757 0.7657 -0.0774 -0.2778 -0.1405 125 HIS A ND1 999 C CD2 . HIS A 125 ? 1.5578 1.5902 0.7426 -0.0430 -0.2514 -0.1007 125 HIS A CD2 1000 C CE1 . HIS A 125 ? 1.5838 1.5634 0.7577 -0.0595 -0.2552 -0.1344 125 HIS A CE1 1001 N NE2 . HIS A 125 ? 1.5759 1.5723 0.7441 -0.0393 -0.2384 -0.1103 125 HIS A NE2 1002 N N . GLU A 126 ? 1.5796 1.7561 0.8240 -0.0811 -0.3424 -0.1205 126 GLU A N 1003 C CA . GLU A 126 ? 1.5607 1.7774 0.8440 -0.0957 -0.3584 -0.1197 126 GLU A CA 1004 C C . GLU A 126 ? 1.5014 1.7045 0.8315 -0.1160 -0.3426 -0.1085 126 GLU A C 1005 O O . GLU A 126 ? 1.4828 1.6696 0.8190 -0.1051 -0.3177 -0.0874 126 GLU A O 1006 C CB . GLU A 126 ? 1.5785 1.8353 0.8550 -0.0696 -0.3598 -0.1003 126 GLU A CB 1007 C CG . GLU A 126 ? 1.5674 1.8692 0.8873 -0.0815 -0.3744 -0.0981 126 GLU A CG 1008 C CD . GLU A 126 ? 1.6107 1.9425 0.9351 -0.0987 -0.4076 -0.1262 126 GLU A CD 1009 O OE1 . GLU A 126 ? 1.6453 1.9807 0.9287 -0.0877 -0.4241 -0.1424 126 GLU A OE1 1010 O OE2 . GLU A 126 ? 1.5978 1.9507 0.9675 -0.1235 -0.4168 -0.1328 126 GLU A OE2 1011 N N . ALA A 127 ? 1.4725 1.6824 0.8350 -0.1458 -0.3567 -0.1229 127 ALA A N 1012 C CA . ALA A 127 ? 1.4140 1.6091 0.8164 -0.1669 -0.3429 -0.1142 127 ALA A CA 1013 C C . ALA A 127 ? 1.3853 1.6222 0.8308 -0.1801 -0.3495 -0.1083 127 ALA A C 1014 O O . ALA A 127 ? 1.3673 1.5965 0.8453 -0.1968 -0.3376 -0.1001 127 ALA A O 1015 C CB . ALA A 127 ? 1.4177 1.5752 0.8220 -0.1924 -0.3478 -0.1334 127 ALA A CB 1016 N N . SER A 128 ? 1.3958 1.6781 0.8417 -0.1718 -0.3680 -0.1123 128 SER A N 1017 C CA . SER A 128 ? 1.3679 1.6943 0.8577 -0.1863 -0.3774 -0.1114 128 SER A CA 1018 C C . SER A 128 ? 1.3513 1.7171 0.8503 -0.1609 -0.3730 -0.0909 128 SER A C 1019 O O . SER A 128 ? 1.3294 1.7371 0.8650 -0.1687 -0.3812 -0.0901 128 SER A O 1020 C CB . SER A 128 ? 1.3963 1.7478 0.8923 -0.2056 -0.4068 -0.1384 128 SER A CB 1021 O OG . SER A 128 ? 1.3926 1.7137 0.9036 -0.2381 -0.4073 -0.1529 128 SER A OG 1022 N N . LEU A 129 ? 1.3620 1.7136 0.8298 -0.1306 -0.3586 -0.0739 129 LEU A N 1023 C CA . LEU A 129 ? 1.3628 1.7430 0.8378 -0.1046 -0.3505 -0.0512 129 LEU A CA 1024 C C . LEU A 129 ? 1.3368 1.6886 0.8249 -0.0989 -0.3189 -0.0291 129 LEU A C 1025 O O . LEU A 129 ? 1.3386 1.7022 0.8300 -0.0757 -0.3063 -0.0081 129 LEU A O 1026 C CB . LEU A 129 ? 1.4178 1.8064 0.8460 -0.0720 -0.3581 -0.0463 129 LEU A CB 1027 C CG . LEU A 129 ? 1.4637 1.8596 0.8587 -0.0749 -0.3852 -0.0717 129 LEU A CG 1028 C CD1 . LEU A 129 ? 1.5086 1.9017 0.8488 -0.0404 -0.3855 -0.0634 129 LEU A CD1 1029 C CD2 . LEU A 129 ? 1.4646 1.9114 0.8866 -0.0893 -0.4153 -0.0898 129 LEU A CD2 1030 N N . GLY A 130 ? 1.3266 1.6410 0.8233 -0.1200 -0.3066 -0.0342 130 GLY A N 1031 C CA . GLY A 130 ? 1.2910 1.5774 0.8008 -0.1175 -0.2782 -0.0171 130 GLY A CA 1032 C C . GLY A 130 ? 1.2616 1.5684 0.8185 -0.1309 -0.2705 -0.0097 130 GLY A C 1033 O O . GLY A 130 ? 1.2219 1.5118 0.7993 -0.1550 -0.2644 -0.0149 130 GLY A O 1034 N N . VAL A 131 ? 1.2679 1.6107 0.8407 -0.1141 -0.2702 0.0029 131 VAL A N 1035 C CA . VAL A 131 ? 1.2404 1.6082 0.8586 -0.1241 -0.2630 0.0090 131 VAL A CA 1036 C C . VAL A 131 ? 1.2319 1.6105 0.8593 -0.0966 -0.2460 0.0312 131 VAL A C 1037 O O . VAL A 131 ? 1.2574 1.6299 0.8558 -0.0693 -0.2427 0.0427 131 VAL A O 1038 C CB . VAL A 131 ? 1.2505 1.6651 0.8937 -0.1395 -0.2871 -0.0048 131 VAL A CB 1039 C CG1 . VAL A 131 ? 1.2714 1.6738 0.9024 -0.1647 -0.3054 -0.0275 131 VAL A CG1 1040 C CG2 . VAL A 131 ? 1.2666 1.7223 0.9030 -0.1133 -0.3023 0.0001 131 VAL A CG2 1041 N N . SER A 132 ? 1.2062 1.5998 0.8734 -0.1039 -0.2343 0.0372 132 SER A N 1042 C CA . SER A 132 ? 1.1926 1.5947 0.8747 -0.0800 -0.2166 0.0569 132 SER A CA 1043 C C . SER A 132 ? 1.1767 1.6205 0.9045 -0.0869 -0.2184 0.0566 132 SER A C 1044 O O . SER A 132 ? 1.1558 1.6130 0.9069 -0.1144 -0.2253 0.0429 132 SER A O 1045 C CB . SER A 132 ? 1.1694 1.5288 0.8509 -0.0787 -0.1883 0.0667 132 SER A CB 1046 O OG . SER A 132 ? 1.1472 1.5155 0.8538 -0.0625 -0.1701 0.0824 132 SER A OG 1047 N N . SER A 133 ? 1.1805 1.6434 0.9213 -0.0611 -0.2105 0.0725 133 SER A N 1048 C CA . SER A 133 ? 1.1566 1.6605 0.9425 -0.0629 -0.2101 0.0733 133 SER A CA 1049 C C . SER A 133 ? 1.1291 1.6156 0.9433 -0.0801 -0.1866 0.0730 133 SER A C 1050 O O . SER A 133 ? 1.1084 1.6256 0.9604 -0.0921 -0.1857 0.0678 133 SER A O 1051 C CB . SER A 133 ? 1.1682 1.6931 0.9583 -0.0272 -0.2074 0.0916 133 SER A CB 1052 O OG . SER A 133 ? 1.1620 1.6520 0.9509 -0.0115 -0.1793 0.1085 133 SER A OG 1053 N N . ALA A 134 ? 1.1287 1.5681 0.9251 -0.0808 -0.1676 0.0780 134 ALA A N 1054 C CA . ALA A 134 ? 1.1189 1.5398 0.9381 -0.0963 -0.1461 0.0765 134 ALA A CA 1055 C C . ALA A 134 ? 1.1014 1.5258 0.9319 -0.1314 -0.1532 0.0598 134 ALA A C 1056 O O . ALA A 134 ? 1.0803 1.5158 0.9404 -0.1446 -0.1425 0.0568 134 ALA A O 1057 C CB . ALA A 134 ? 1.1222 1.4943 0.9201 -0.0884 -0.1263 0.0843 134 ALA A CB 1058 N N . CYS A 135 ? 1.1080 1.5211 0.9139 -0.1459 -0.1701 0.0493 135 CYS A N 1059 C CA . CYS A 135 ? 1.0995 1.5165 0.9146 -0.1785 -0.1793 0.0346 135 CYS A CA 1060 C C . CYS A 135 ? 1.0980 1.5590 0.9252 -0.1855 -0.2028 0.0251 135 CYS A C 1061 O O . CYS A 135 ? 1.1049 1.5626 0.9083 -0.1870 -0.2215 0.0174 135 CYS A O 1062 C CB . CYS A 135 ? 1.1226 1.4960 0.9050 -0.1910 -0.1828 0.0279 135 CYS A CB 1063 S SG . CYS A 135 ? 1.1662 1.4893 0.9321 -0.1814 -0.1590 0.0368 135 CYS A SG 1064 N N . PRO A 136 ? 1.0736 1.5776 0.9394 -0.1889 -0.2019 0.0245 136 PRO A N 1065 C CA . PRO A 136 ? 1.0930 1.6457 0.9792 -0.1958 -0.2232 0.0147 136 PRO A CA 1066 C C . PRO A 136 ? 1.0983 1.6644 1.0065 -0.2323 -0.2282 0.0004 136 PRO A C 1067 O O . PRO A 136 ? 1.0782 1.6411 1.0064 -0.2472 -0.2110 0.0016 136 PRO A O 1068 C CB . PRO A 136 ? 1.0825 1.6750 1.0014 -0.1742 -0.2160 0.0243 136 PRO A CB 1069 C CG . PRO A 136 ? 1.0502 1.6190 0.9802 -0.1752 -0.1884 0.0322 136 PRO A CG 1070 C CD . PRO A 136 ? 1.0531 1.5654 0.9447 -0.1754 -0.1803 0.0355 136 PRO A CD 1071 N N . TYR A 137 ? 1.1296 1.7109 1.0340 -0.2462 -0.2512 -0.0131 137 TYR A N 1072 C CA . TYR A 137 ? 1.1420 1.7374 1.0689 -0.2815 -0.2569 -0.0267 137 TYR A CA 1073 C C . TYR A 137 ? 1.1467 1.8016 1.1049 -0.2842 -0.2768 -0.0373 137 TYR A C 1074 O O . TYR A 137 ? 1.1789 1.8464 1.1219 -0.2719 -0.2983 -0.0434 137 TYR A O 1075 C CB . TYR A 137 ? 1.1688 1.7208 1.0640 -0.3020 -0.2658 -0.0365 137 TYR A CB 1076 C CG . TYR A 137 ? 1.1782 1.7416 1.0954 -0.3390 -0.2724 -0.0502 137 TYR A CG 1077 C CD1 . TYR A 137 ? 1.1643 1.7174 1.0978 -0.3620 -0.2541 -0.0469 137 TYR A CD1 1078 C CD2 . TYR A 137 ? 1.1928 1.7770 1.1141 -0.3514 -0.2964 -0.0665 137 TYR A CD2 1079 C CE1 . TYR A 137 ? 1.1681 1.7293 1.1208 -0.3964 -0.2579 -0.0574 137 TYR A CE1 1080 C CE2 . TYR A 137 ? 1.1998 1.7926 1.1438 -0.3867 -0.3008 -0.0789 137 TYR A CE2 1081 C CZ . TYR A 137 ? 1.1858 1.7660 1.1451 -0.4091 -0.2807 -0.0732 137 TYR A CZ 1082 O OH . TYR A 137 ? 1.1976 1.7840 1.1783 -0.4446 -0.2830 -0.0836 137 TYR A OH 1083 N N . GLN A 138 ? 1.1390 1.8317 1.1411 -0.3008 -0.2698 -0.0406 138 GLN A N 1084 C CA . GLN A 138 ? 1.1540 1.9091 1.1950 -0.3071 -0.2876 -0.0524 138 GLN A CA 1085 C C . GLN A 138 ? 1.1585 1.9505 1.2012 -0.2711 -0.3030 -0.0481 138 GLN A C 1086 O O . GLN A 138 ? 1.1718 2.0006 1.2229 -0.2708 -0.3282 -0.0604 138 GLN A O 1087 C CB . GLN A 138 ? 1.1871 1.9400 1.2253 -0.3379 -0.3069 -0.0711 138 GLN A CB 1088 C CG . GLN A 138 ? 1.1936 1.9470 1.2594 -0.3769 -0.2948 -0.0775 138 GLN A CG 1089 C CD . GLN A 138 ? 1.2258 1.9693 1.2881 -0.4083 -0.3118 -0.0953 138 GLN A CD 1090 O OE1 . GLN A 138 ? 1.2462 1.9970 1.2951 -0.4021 -0.3360 -0.1069 138 GLN A OE1 1091 N NE2 . GLN A 138 ? 1.2325 1.9582 1.3061 -0.4422 -0.2988 -0.0975 138 GLN A NE2 1092 N N . GLY A 139 ? 1.1423 1.9235 1.1768 -0.2406 -0.2876 -0.0306 139 GLY A N 1093 C CA . GLY A 139 ? 1.1372 1.9497 1.1730 -0.2034 -0.2983 -0.0220 139 GLY A CA 1094 C C . GLY A 139 ? 1.1414 1.9263 1.1265 -0.1823 -0.3131 -0.0186 139 GLY A C 1095 O O . GLY A 139 ? 1.1487 1.9517 1.1254 -0.1489 -0.3209 -0.0085 139 GLY A O 1096 N N . LYS A 140 ? 1.1358 1.8762 1.0862 -0.2007 -0.3161 -0.0264 140 LYS A N 1097 C CA . LYS A 140 ? 1.1666 1.8804 1.0675 -0.1844 -0.3302 -0.0267 140 LYS A CA 1098 C C . LYS A 140 ? 1.1666 1.8156 1.0305 -0.1803 -0.3091 -0.0154 140 LYS A C 1099 O O . LYS A 140 ? 1.1643 1.7835 1.0336 -0.2038 -0.2935 -0.0172 140 LYS A O 1100 C CB . LYS A 140 ? 1.1833 1.9026 1.0760 -0.2094 -0.3549 -0.0495 140 LYS A CB 1101 C CG . LYS A 140 ? 1.1960 1.9808 1.1176 -0.2086 -0.3819 -0.0631 140 LYS A CG 1102 C CD . LYS A 140 ? 1.2023 1.9995 1.1449 -0.2484 -0.3963 -0.0873 140 LYS A CD 1103 C CE . LYS A 140 ? 1.1993 2.0701 1.1912 -0.2542 -0.4161 -0.1006 140 LYS A CE 1104 N NZ . LYS A 140 ? 1.2265 2.1308 1.2014 -0.2328 -0.4472 -0.1101 140 LYS A NZ 1105 N N . SER A 141 ? 1.1866 1.8148 1.0128 -0.1502 -0.3085 -0.0037 141 SER A N 1106 C CA . SER A 141 ? 1.1778 1.7469 0.9696 -0.1446 -0.2890 0.0061 141 SER A CA 1107 C C . SER A 141 ? 1.1750 1.7079 0.9462 -0.1726 -0.2941 -0.0092 141 SER A C 1108 O O . SER A 141 ? 1.2111 1.7499 0.9648 -0.1791 -0.3160 -0.0239 141 SER A O 1109 C CB . SER A 141 ? 1.2042 1.7608 0.9569 -0.1091 -0.2900 0.0194 141 SER A CB 1110 O OG . SER A 141 ? 1.2080 1.7946 0.9783 -0.0812 -0.2853 0.0355 141 SER A OG 1111 N N . SER A 142 ? 1.1458 1.6419 0.9201 -0.1886 -0.2743 -0.0064 142 SER A N 1112 C CA . SER A 142 ? 1.1364 1.5934 0.8928 -0.2138 -0.2762 -0.0182 142 SER A CA 1113 C C . SER A 142 ? 1.1186 1.5246 0.8503 -0.2039 -0.2552 -0.0071 142 SER A C 1114 O O . SER A 142 ? 1.1105 1.5112 0.8313 -0.1767 -0.2438 0.0070 142 SER A O 1115 C CB . SER A 142 ? 1.1183 1.5865 0.9087 -0.2474 -0.2745 -0.0269 142 SER A CB 1116 O OG . SER A 142 ? 1.1203 1.5481 0.8939 -0.2712 -0.2757 -0.0363 142 SER A OG 1117 N N . PHE A 143 ? 1.1054 1.4742 0.8293 -0.2255 -0.2500 -0.0133 143 PHE A N 1118 C CA . PHE A 143 ? 1.0876 1.4103 0.7917 -0.2181 -0.2316 -0.0052 143 PHE A CA 1119 C C . PHE A 143 ? 1.0761 1.3688 0.7839 -0.2455 -0.2264 -0.0113 143 PHE A C 1120 O O . PHE A 143 ? 1.0859 1.3859 0.8034 -0.2699 -0.2384 -0.0223 143 PHE A O 1121 C CB . PHE A 143 ? 1.1055 1.4035 0.7693 -0.2003 -0.2374 -0.0068 143 PHE A CB 1122 C CG . PHE A 143 ? 1.0906 1.3506 0.7379 -0.1854 -0.2167 0.0038 143 PHE A CG 1123 C CD1 . PHE A 143 ? 1.0743 1.3401 0.7291 -0.1630 -0.1990 0.0201 143 PHE A CD1 1124 C CD2 . PHE A 143 ? 1.0933 1.3119 0.7195 -0.1935 -0.2148 -0.0028 143 PHE A CD2 1125 C CE1 . PHE A 143 ? 1.0650 1.2970 0.7081 -0.1508 -0.1793 0.0288 143 PHE A CE1 1126 C CE2 . PHE A 143 ? 1.0872 1.2748 0.7021 -0.1800 -0.1959 0.0057 143 PHE A CE2 1127 C CZ . PHE A 143 ? 1.0704 1.2651 0.6944 -0.1596 -0.1779 0.0212 143 PHE A CZ 1128 N N . PHE A 144 ? 1.0521 1.3116 0.7531 -0.2411 -0.2086 -0.0037 144 PHE A N 1129 C CA . PHE A 144 ? 1.0442 1.2700 0.7411 -0.2624 -0.2051 -0.0084 144 PHE A CA 1130 C C . PHE A 144 ? 1.0640 1.2748 0.7437 -0.2789 -0.2244 -0.0226 144 PHE A C 1131 O O . PHE A 144 ? 1.0914 1.2846 0.7443 -0.2674 -0.2321 -0.0277 144 PHE A O 1132 C CB . PHE A 144 ? 1.0358 1.2240 0.7168 -0.2495 -0.1898 -0.0021 144 PHE A CB 1133 C CG . PHE A 144 ? 1.0105 1.2072 0.7086 -0.2343 -0.1695 0.0100 144 PHE A CG 1134 C CD1 . PHE A 144 ? 0.9893 1.1959 0.7124 -0.2466 -0.1586 0.0128 144 PHE A CD1 1135 C CD2 . PHE A 144 ? 1.0052 1.1978 0.6933 -0.2080 -0.1600 0.0185 144 PHE A CD2 1136 C CE1 . PHE A 144 ? 0.9705 1.1831 0.7100 -0.2329 -0.1398 0.0217 144 PHE A CE1 1137 C CE2 . PHE A 144 ? 0.9854 1.1824 0.6910 -0.1949 -0.1404 0.0291 144 PHE A CE2 1138 C CZ . PHE A 144 ? 0.9665 1.1734 0.6986 -0.2074 -0.1307 0.0298 144 PHE A CZ 1139 N N . ARG A 145 ? 1.0598 1.2765 0.7549 -0.3059 -0.2308 -0.0290 145 ARG A N 1140 C CA . ARG A 145 ? 1.0872 1.2924 0.7720 -0.3245 -0.2491 -0.0434 145 ARG A CA 1141 C C . ARG A 145 ? 1.1194 1.2733 0.7755 -0.3270 -0.2512 -0.0486 145 ARG A C 1142 O O . ARG A 145 ? 1.1637 1.3051 0.8051 -0.3339 -0.2666 -0.0618 145 ARG A O 1143 C CB . ARG A 145 ? 1.0794 1.2998 0.7900 -0.3546 -0.2515 -0.0469 145 ARG A CB 1144 C CG . ARG A 145 ? 1.0648 1.3402 0.8080 -0.3561 -0.2528 -0.0460 145 ARG A CG 1145 C CD . ARG A 145 ? 1.0792 1.3694 0.8440 -0.3879 -0.2612 -0.0554 145 ARG A CD 1146 N NE . ARG A 145 ? 1.0718 1.4158 0.8736 -0.3917 -0.2588 -0.0539 145 ARG A NE 1147 C CZ . ARG A 145 ? 1.0745 1.4627 0.8910 -0.3814 -0.2719 -0.0600 145 ARG A CZ 1148 N NH1 . ARG A 145 ? 1.0977 1.4826 0.8915 -0.3664 -0.2885 -0.0679 145 ARG A NH1 1149 N NH2 . ARG A 145 ? 1.0623 1.4998 0.9160 -0.3848 -0.2684 -0.0584 145 ARG A NH2 1150 N N . ASN A 146 ? 1.1285 1.2531 0.7782 -0.3220 -0.2365 -0.0399 146 ASN A N 1151 C CA . ASN A 146 ? 1.1540 1.2309 0.7812 -0.3260 -0.2387 -0.0447 146 ASN A CA 1152 C C . ASN A 146 ? 1.1581 1.2154 0.7592 -0.3020 -0.2387 -0.0477 146 ASN A C 1153 O O . ASN A 146 ? 1.1671 1.1872 0.7491 -0.3031 -0.2427 -0.0545 146 ASN A O 1154 C CB . ASN A 146 ? 1.1441 1.1990 0.7769 -0.3338 -0.2254 -0.0354 146 ASN A CB 1155 C CG . ASN A 146 ? 1.1606 1.2231 0.8105 -0.3612 -0.2263 -0.0340 146 ASN A CG 1156 O OD1 . ASN A 146 ? 1.2087 1.2670 0.8584 -0.3800 -0.2387 -0.0426 146 ASN A OD1 1157 N ND2 . ASN A 146 ? 1.1520 1.2252 0.8167 -0.3641 -0.2123 -0.0238 146 ASN A ND2 1158 N N . VAL A 147 ? 1.1429 1.2246 0.7431 -0.2799 -0.2335 -0.0421 147 VAL A N 1159 C CA . VAL A 147 ? 1.1566 1.2228 0.7315 -0.2559 -0.2304 -0.0429 147 VAL A CA 1160 C C . VAL A 147 ? 1.1628 1.2586 0.7272 -0.2415 -0.2403 -0.0461 147 VAL A C 1161 O O . VAL A 147 ? 1.1512 1.2845 0.7338 -0.2402 -0.2418 -0.0407 147 VAL A O 1162 C CB . VAL A 147 ? 1.1403 1.1986 0.7200 -0.2385 -0.2088 -0.0295 147 VAL A CB 1163 C CG1 . VAL A 147 ? 1.1313 1.1584 0.7160 -0.2498 -0.2018 -0.0287 147 VAL A CG1 1164 C CG2 . VAL A 147 ? 1.1165 1.2096 0.7202 -0.2325 -0.1985 -0.0173 147 VAL A CG2 1165 N N . VAL A 148 ? 1.1901 1.2697 0.7245 -0.2297 -0.2473 -0.0552 148 VAL A N 1166 C CA . VAL A 148 ? 1.2130 1.3186 0.7304 -0.2152 -0.2594 -0.0600 148 VAL A CA 1167 C C . VAL A 148 ? 1.2113 1.3193 0.7124 -0.1847 -0.2442 -0.0464 148 VAL A C 1168 O O . VAL A 148 ? 1.2137 1.2910 0.6972 -0.1736 -0.2318 -0.0448 148 VAL A O 1169 C CB . VAL A 148 ? 1.2516 1.3394 0.7421 -0.2205 -0.2774 -0.0805 148 VAL A CB 1170 C CG1 . VAL A 148 ? 1.2830 1.4044 0.7584 -0.2094 -0.2940 -0.0879 148 VAL A CG1 1171 C CG2 . VAL A 148 ? 1.2561 1.3290 0.7612 -0.2513 -0.2888 -0.0931 148 VAL A CG2 1172 N N . TRP A 149 ? 1.2051 1.3493 0.7132 -0.1712 -0.2443 -0.0363 149 TRP A N 1173 C CA . TRP A 149 ? 1.2169 1.3639 0.7081 -0.1416 -0.2300 -0.0214 149 TRP A CA 1174 C C . TRP A 149 ? 1.2682 1.4192 0.7197 -0.1254 -0.2433 -0.0297 149 TRP A C 1175 O O . TRP A 149 ? 1.2766 1.4617 0.7236 -0.1178 -0.2582 -0.0304 149 TRP A O 1176 C CB . TRP A 149 ? 1.1921 1.3735 0.7089 -0.1325 -0.2233 -0.0052 149 TRP A CB 1177 C CG . TRP A 149 ? 1.1957 1.3773 0.6991 -0.1025 -0.2058 0.0134 149 TRP A CG 1178 C CD1 . TRP A 149 ? 1.2218 1.3795 0.6916 -0.0835 -0.1955 0.0173 149 TRP A CD1 1179 C CD2 . TRP A 149 ? 1.1745 1.3804 0.6980 -0.0882 -0.1955 0.0311 149 TRP A CD2 1180 N NE1 . TRP A 149 ? 1.2218 1.3860 0.6891 -0.0592 -0.1787 0.0376 149 TRP A NE1 1181 C CE2 . TRP A 149 ? 1.1932 1.3857 0.6933 -0.0611 -0.1788 0.0463 149 TRP A CE2 1182 C CE3 . TRP A 149 ? 1.1480 1.3848 0.7077 -0.0953 -0.1975 0.0355 149 TRP A CE3 1183 C CZ2 . TRP A 149 ? 1.1852 1.3912 0.6967 -0.0410 -0.1647 0.0665 149 TRP A CZ2 1184 C CZ3 . TRP A 149 ? 1.1474 1.3996 0.7193 -0.0744 -0.1842 0.0540 149 TRP A CZ3 1185 C CH2 . TRP A 149 ? 1.1671 1.4023 0.7148 -0.0475 -0.1681 0.0697 149 TRP A CH2 1186 N N . LEU A 150 ? 1.3046 1.4220 0.7273 -0.1191 -0.2379 -0.0364 150 LEU A N 1187 C CA . LEU A 150 ? 1.3567 1.4734 0.7377 -0.1055 -0.2500 -0.0477 150 LEU A CA 1188 C C . LEU A 150 ? 1.3792 1.5088 0.7361 -0.0744 -0.2391 -0.0305 150 LEU A C 1189 O O . LEU A 150 ? 1.3618 1.4774 0.7233 -0.0615 -0.2142 -0.0127 150 LEU A O 1190 C CB . LEU A 150 ? 1.3782 1.4534 0.7376 -0.1085 -0.2457 -0.0611 150 LEU A CB 1191 C CG . LEU A 150 ? 1.3757 1.4310 0.7510 -0.1369 -0.2578 -0.0790 150 LEU A CG 1192 C CD1 . LEU A 150 ? 1.3935 1.4061 0.7507 -0.1348 -0.2490 -0.0883 150 LEU A CD1 1193 C CD2 . LEU A 150 ? 1.4005 1.4751 0.7712 -0.1513 -0.2858 -0.0986 150 LEU A CD2 1194 N N . ILE A 151 ? 1.4256 1.5816 0.7570 -0.0630 -0.2579 -0.0361 151 ILE A N 1195 C CA . ILE A 151 ? 1.4530 1.6206 0.7514 -0.0313 -0.2509 -0.0205 151 ILE A CA 1196 C C . ILE A 151 ? 1.5048 1.6682 0.7522 -0.0199 -0.2647 -0.0366 151 ILE A C 1197 O O . ILE A 151 ? 1.5143 1.6708 0.7556 -0.0373 -0.2830 -0.0617 151 ILE A O 1198 C CB . ILE A 151 ? 1.4400 1.6510 0.7548 -0.0212 -0.2599 -0.0066 151 ILE A CB 1199 C CG1 . ILE A 151 ? 1.4599 1.7067 0.7722 -0.0304 -0.2939 -0.0263 151 ILE A CG1 1200 C CG2 . ILE A 151 ? 1.3872 1.6033 0.7529 -0.0339 -0.2470 0.0057 151 ILE A CG2 1201 C CD1 . ILE A 151 ? 1.4570 1.7505 0.7874 -0.0190 -0.3048 -0.0142 151 ILE A CD1 1202 N N . LYS A 152 ? 1.5454 1.7119 0.7555 0.0094 -0.2550 -0.0220 152 LYS A N 1203 C CA . LYS A 152 ? 1.6071 1.7688 0.7622 0.0244 -0.2642 -0.0349 152 LYS A CA 1204 C C . LYS A 152 ? 1.6456 1.8424 0.7872 0.0200 -0.3004 -0.0558 152 LYS A C 1205 O O . LYS A 152 ? 1.6214 1.8549 0.7888 0.0165 -0.3160 -0.0516 152 LYS A O 1206 C CB . LYS A 152 ? 1.6336 1.7926 0.7516 0.0581 -0.2435 -0.0101 152 LYS A CB 1207 C CG . LYS A 152 ? 1.6439 1.8416 0.7594 0.0772 -0.2531 0.0086 152 LYS A CG 1208 C CD . LYS A 152 ? 1.6705 1.8594 0.7540 0.1096 -0.2280 0.0381 152 LYS A CD 1209 C CE . LYS A 152 ? 1.6931 1.9213 0.7638 0.1317 -0.2439 0.0534 152 LYS A CE 1210 N NZ . LYS A 152 ? 1.7262 1.9434 0.7648 0.1642 -0.2187 0.0852 152 LYS A NZ 1211 N N . LYS A 153 ? 1.7087 1.8950 0.8110 0.0206 -0.3132 -0.0794 153 LYS A N 1212 C CA . LYS A 153 ? 1.7626 1.9807 0.8467 0.0174 -0.3480 -0.1030 153 LYS A CA 1213 C C . LYS A 153 ? 1.8194 2.0410 0.8377 0.0463 -0.3517 -0.1057 153 LYS A C 1214 O O . LYS A 153 ? 1.8423 2.0299 0.8270 0.0536 -0.3364 -0.1117 153 LYS A O 1215 C CB . LYS A 153 ? 1.7716 1.9745 0.8731 -0.0142 -0.3649 -0.1356 153 LYS A CB 1216 C CG . LYS A 153 ? 1.7940 2.0364 0.9086 -0.0298 -0.4007 -0.1581 153 LYS A CG 1217 C CD . LYS A 153 ? 1.7960 2.0174 0.9300 -0.0627 -0.4141 -0.1888 153 LYS A CD 1218 C CE . LYS A 153 ? 1.8447 2.0357 0.9313 -0.0574 -0.4170 -0.2128 153 LYS A CE 1219 N NZ . LYS A 153 ? 1.8520 2.0234 0.9566 -0.0887 -0.4330 -0.2444 153 LYS A NZ 1220 N N . ASN A 154 ? 1.8426 2.1066 0.8428 0.0631 -0.3723 -0.1017 154 ASN A N 1221 C CA . ASN A 154 ? 1.9034 2.1764 0.8382 0.0951 -0.3756 -0.0981 154 ASN A CA 1222 C C . ASN A 154 ? 1.9050 2.1462 0.8124 0.1198 -0.3372 -0.0681 154 ASN A C 1223 O O . ASN A 154 ? 1.9325 2.1533 0.7878 0.1357 -0.3269 -0.0725 154 ASN A O 1224 C CB . ASN A 154 ? 1.9497 2.2177 0.8450 0.0889 -0.3972 -0.1354 154 ASN A CB 1225 C CG . ASN A 154 ? 2.0221 2.3287 0.8666 0.1126 -0.4233 -0.1422 154 ASN A CG 1226 O OD1 . ASN A 154 ? 2.0345 2.3846 0.8929 0.1202 -0.4419 -0.1322 154 ASN A OD1 1227 N ND2 . ASN A 154 ? 2.0766 2.3689 0.8617 0.1250 -0.4257 -0.1602 154 ASN A ND2 1228 N N . SER A 155 ? 1.8624 2.1002 0.8077 0.1218 -0.3154 -0.0387 155 SER A N 1229 C CA . SER A 155 ? 1.8627 2.0737 0.7920 0.1436 -0.2780 -0.0075 155 SER A CA 1230 C C . SER A 155 ? 1.8552 2.0196 0.7822 0.1348 -0.2508 -0.0140 155 SER A C 1231 O O . SER A 155 ? 1.9010 2.0432 0.8030 0.1540 -0.2214 0.0055 155 SER A O 1232 C CB . SER A 155 ? 1.9177 2.1429 0.7842 0.1800 -0.2782 0.0088 155 SER A CB 1233 O OG . SER A 155 ? 1.9010 2.1532 0.7815 0.1967 -0.2795 0.0369 155 SER A OG 1234 N N . THR A 156 ? 1.8141 1.9629 0.7680 0.1065 -0.2592 -0.0404 156 THR A N 1235 C CA . THR A 156 ? 1.7930 1.8993 0.7450 0.1000 -0.2355 -0.0479 156 THR A CA 1236 C C . THR A 156 ? 1.7372 1.8269 0.7471 0.0693 -0.2342 -0.0572 156 THR A C 1237 O O . THR A 156 ? 1.7428 1.8461 0.7770 0.0471 -0.2601 -0.0762 156 THR A O 1238 C CB . THR A 156 ? 1.8415 1.9360 0.7454 0.1024 -0.2474 -0.0777 156 THR A CB 1239 O OG1 . THR A 156 ? 1.8868 2.0113 0.7417 0.1221 -0.2680 -0.0809 156 THR A OG1 1240 C CG2 . THR A 156 ? 1.8530 1.9103 0.7333 0.1141 -0.2146 -0.0739 156 THR A CG2 1241 N N . TYR A 157 ? 1.6933 1.7542 0.7248 0.0682 -0.2037 -0.0435 157 TYR A N 1242 C CA . TYR A 157 ? 1.6204 1.6616 0.7011 0.0421 -0.1997 -0.0514 157 TYR A CA 1243 C C . TYR A 157 ? 1.6246 1.6293 0.6901 0.0417 -0.1852 -0.0659 157 TYR A C 1244 O O . TYR A 157 ? 1.6121 1.5980 0.6769 0.0537 -0.1553 -0.0513 157 TYR A O 1245 C CB . TYR A 157 ? 1.5740 1.6148 0.6969 0.0413 -0.1773 -0.0246 157 TYR A CB 1246 C CG . TYR A 157 ? 1.5116 1.5441 0.6878 0.0135 -0.1801 -0.0305 157 TYR A CG 1247 C CD1 . TYR A 157 ? 1.4940 1.4948 0.6833 0.0006 -0.1716 -0.0432 157 TYR A CD1 1248 C CD2 . TYR A 157 ? 1.4733 1.5305 0.6858 0.0017 -0.1907 -0.0226 157 TYR A CD2 1249 C CE1 . TYR A 157 ? 1.4513 1.4445 0.6852 -0.0231 -0.1745 -0.0467 157 TYR A CE1 1250 C CE2 . TYR A 157 ? 1.4307 1.4808 0.6878 -0.0228 -0.1920 -0.0269 157 TYR A CE2 1251 C CZ . TYR A 157 ? 1.4161 1.4338 0.6823 -0.0350 -0.1843 -0.0384 157 TYR A CZ 1252 O OH . TYR A 157 ? 1.3645 1.3756 0.6713 -0.0581 -0.1864 -0.0410 157 TYR A OH 1253 N N . PRO A 158 ? 1.6399 1.6350 0.6938 0.0287 -0.2058 -0.0956 158 PRO A N 1254 C CA . PRO A 158 ? 1.6490 1.6089 0.6928 0.0281 -0.1932 -0.1112 158 PRO A CA 1255 C C . PRO A 158 ? 1.5911 1.5284 0.6847 0.0099 -0.1816 -0.1086 158 PRO A C 1256 O O . PRO A 158 ? 1.5504 1.4969 0.6830 -0.0093 -0.1927 -0.1050 158 PRO A O 1257 C CB . PRO A 158 ? 1.6859 1.6437 0.7052 0.0185 -0.2218 -0.1443 158 PRO A CB 1258 C CG . PRO A 158 ? 1.6757 1.6646 0.7136 0.0033 -0.2501 -0.1472 158 PRO A CG 1259 C CD . PRO A 158 ? 1.6609 1.6784 0.7044 0.0179 -0.2408 -0.1168 158 PRO A CD 1260 N N . THR A 159 ? 1.5903 1.4998 0.6824 0.0167 -0.1591 -0.1103 159 THR A N 1261 C CA . THR A 159 ? 1.5432 1.4323 0.6806 0.0023 -0.1482 -0.1079 159 THR A CA 1262 C C . THR A 159 ? 1.5360 1.4174 0.6957 -0.0235 -0.1744 -0.1268 159 THR A C 1263 O O . THR A 159 ? 1.5548 1.4275 0.6919 -0.0285 -0.1932 -0.1506 159 THR A O 1264 C CB . THR A 159 ? 1.5502 1.4117 0.6821 0.0134 -0.1242 -0.1129 159 THR A CB 1265 O OG1 . THR A 159 ? 1.5625 1.4308 0.6737 0.0364 -0.0976 -0.0944 159 THR A OG1 1266 C CG2 . THR A 159 ? 1.5070 1.3517 0.6878 0.0000 -0.1143 -0.1091 159 THR A CG2 1267 N N . ILE A 160 ? 1.5031 1.3882 0.7064 -0.0400 -0.1748 -0.1154 160 ILE A N 1268 C CA . ILE A 160 ? 1.4871 1.3611 0.7171 -0.0656 -0.1938 -0.1280 160 ILE A CA 1269 C C . ILE A 160 ? 1.4904 1.3303 0.7364 -0.0685 -0.1825 -0.1343 160 ILE A C 1270 O O . ILE A 160 ? 1.4685 1.3042 0.7317 -0.0600 -0.1601 -0.1201 160 ILE A O 1271 C CB . ILE A 160 ? 1.4359 1.3313 0.7035 -0.0803 -0.1972 -0.1112 160 ILE A CB 1272 C CG1 . ILE A 160 ? 1.4447 1.3756 0.7008 -0.0795 -0.2134 -0.1086 160 ILE A CG1 1273 C CG2 . ILE A 160 ? 1.4167 1.2953 0.7142 -0.1058 -0.2094 -0.1196 160 ILE A CG2 1274 C CD1 . ILE A 160 ? 1.4030 1.3597 0.6937 -0.0883 -0.2127 -0.0902 160 ILE A CD1 1275 N N . LYS A 161 ? 1.5234 1.3390 0.7646 -0.0801 -0.1981 -0.1560 161 LYS A N 1276 C CA . LYS A 161 ? 1.5244 1.3067 0.7832 -0.0838 -0.1916 -0.1627 161 LYS A CA 1277 C C . LYS A 161 ? 1.5272 1.2929 0.8031 -0.1086 -0.2133 -0.1736 161 LYS A C 1278 O O . LYS A 161 ? 1.5625 1.3130 0.8202 -0.1152 -0.2299 -0.1945 161 LYS A O 1279 C CB . LYS A 161 ? 1.5724 1.3327 0.8022 -0.0664 -0.1833 -0.1795 161 LYS A CB 1280 C CG . LYS A 161 ? 1.5762 1.3418 0.8022 -0.0438 -0.1542 -0.1667 161 LYS A CG 1281 C CD . LYS A 161 ? 1.6189 1.3653 0.8147 -0.0263 -0.1448 -0.1844 161 LYS A CD 1282 C CE . LYS A 161 ? 1.6321 1.3924 0.8119 -0.0033 -0.1168 -0.1706 161 LYS A CE 1283 N NZ . LYS A 161 ? 1.6794 1.4239 0.8283 0.0148 -0.1044 -0.1871 161 LYS A NZ 1284 N N . ARG A 162 ? 1.4970 1.2649 0.8075 -0.1227 -0.2123 -0.1594 162 ARG A N 1285 C CA . ARG A 162 ? 1.5030 1.2577 0.8300 -0.1474 -0.2308 -0.1652 162 ARG A CA 1286 C C . ARG A 162 ? 1.4857 1.2166 0.8398 -0.1538 -0.2248 -0.1582 162 ARG A C 1287 O O . ARG A 162 ? 1.4650 1.2021 0.8353 -0.1438 -0.2076 -0.1442 162 ARG A O 1288 C CB . ARG A 162 ? 1.4859 1.2736 0.8253 -0.1622 -0.2406 -0.1554 162 ARG A CB 1289 C CG . ARG A 162 ? 1.5211 1.3346 0.8346 -0.1565 -0.2510 -0.1636 162 ARG A CG 1290 C CD . ARG A 162 ? 1.5696 1.3650 0.8627 -0.1657 -0.2709 -0.1897 162 ARG A CD 1291 N NE . ARG A 162 ? 1.5666 1.3701 0.8779 -0.1923 -0.2900 -0.1944 162 ARG A NE 1292 C CZ . ARG A 162 ? 1.5737 1.4112 0.8825 -0.1990 -0.3043 -0.1982 162 ARG A CZ 1293 N NH1 . ARG A 162 ? 1.5921 1.4585 0.8774 -0.1796 -0.3035 -0.1971 162 ARG A NH1 1294 N NH2 . ARG A 162 ? 1.5659 1.4094 0.8960 -0.2250 -0.3196 -0.2030 162 ARG A NH2 1295 N N . SER A 163 ? 1.5022 1.2056 0.8608 -0.1708 -0.2398 -0.1682 163 SER A N 1296 C CA . SER A 163 ? 1.4894 1.1640 0.8669 -0.1748 -0.2374 -0.1642 163 SER A CA 1297 C C . SER A 163 ? 1.4935 1.1525 0.8821 -0.2009 -0.2539 -0.1644 163 SER A C 1298 O O . SER A 163 ? 1.5128 1.1591 0.8886 -0.2126 -0.2688 -0.1796 163 SER A O 1299 C CB . SER A 163 ? 1.5197 1.1617 0.8831 -0.1592 -0.2341 -0.1801 163 SER A CB 1300 O OG . SER A 163 ? 1.5375 1.1508 0.9189 -0.1609 -0.2337 -0.1768 163 SER A OG 1301 N N . TYR A 164 ? 1.4694 1.1302 0.8814 -0.2105 -0.2508 -0.1480 164 TYR A N 1302 C CA . TYR A 164 ? 1.4778 1.1188 0.8992 -0.2342 -0.2634 -0.1457 164 TYR A CA 1303 C C . TYR A 164 ? 1.4935 1.1006 0.9243 -0.2317 -0.2617 -0.1401 164 TYR A C 1304 O O . TYR A 164 ? 1.4724 1.0892 0.9166 -0.2206 -0.2503 -0.1284 164 TYR A O 1305 C CB . TYR A 164 ? 1.4342 1.1071 0.8723 -0.2516 -0.2640 -0.1309 164 TYR A CB 1306 C CG . TYR A 164 ? 1.4493 1.0995 0.8963 -0.2754 -0.2736 -0.1265 164 TYR A CG 1307 C CD1 . TYR A 164 ? 1.4854 1.1206 0.9261 -0.2946 -0.2878 -0.1385 164 TYR A CD1 1308 C CD2 . TYR A 164 ? 1.4397 1.0812 0.9004 -0.2786 -0.2683 -0.1110 164 TYR A CD2 1309 C CE1 . TYR A 164 ? 1.5064 1.1174 0.9549 -0.3171 -0.2944 -0.1331 164 TYR A CE1 1310 C CE2 . TYR A 164 ? 1.4555 1.0738 0.9204 -0.2994 -0.2759 -0.1049 164 TYR A CE2 1311 C CZ . TYR A 164 ? 1.4946 1.0967 0.9536 -0.3189 -0.2879 -0.1150 164 TYR A CZ 1312 O OH . TYR A 164 ? 1.5145 1.0913 0.9776 -0.3404 -0.2931 -0.1073 164 TYR A OH 1313 N N . ASN A 165 ? 1.5434 1.1110 0.9678 -0.2424 -0.2736 -0.1487 165 ASN A N 1314 C CA . ASN A 165 ? 1.5833 1.1145 1.0141 -0.2403 -0.2751 -0.1431 165 ASN A CA 1315 C C . ASN A 165 ? 1.5584 1.0822 0.9988 -0.2643 -0.2816 -0.1285 165 ASN A C 1316 O O . ASN A 165 ? 1.5845 1.1004 1.0210 -0.2854 -0.2910 -0.1328 165 ASN A O 1317 C CB . ASN A 165 ? 1.6694 1.1569 1.0854 -0.2342 -0.2826 -0.1619 165 ASN A CB 1318 C CG . ASN A 165 ? 1.7470 1.1942 1.1686 -0.2276 -0.2848 -0.1569 165 ASN A CG 1319 O OD1 . ASN A 165 ? 1.7274 1.1666 1.1586 -0.2388 -0.2877 -0.1406 165 ASN A OD1 1320 N ND2 . ASN A 165 ? 1.8732 1.2950 1.2879 -0.2083 -0.2835 -0.1711 165 ASN A ND2 1321 N N . ASN A 166 ? 1.5135 1.0411 0.9665 -0.2613 -0.2762 -0.1118 166 ASN A N 1322 C CA . ASN A 166 ? 1.5008 1.0213 0.9595 -0.2821 -0.2806 -0.0964 166 ASN A CA 1323 C C . ASN A 166 ? 1.5313 0.9985 0.9816 -0.2883 -0.2906 -0.0966 166 ASN A C 1324 O O . ASN A 166 ? 1.5219 0.9676 0.9736 -0.2761 -0.2908 -0.0893 166 ASN A O 1325 C CB . ASN A 166 ? 1.4650 1.0097 0.9375 -0.2763 -0.2719 -0.0796 166 ASN A CB 1326 C CG . ASN A 166 ? 1.4761 1.0207 0.9516 -0.2984 -0.2745 -0.0637 166 ASN A CG 1327 O OD1 . ASN A 166 ? 1.4994 1.0378 0.9710 -0.3199 -0.2800 -0.0643 166 ASN A OD1 1328 N ND2 . ASN A 166 ? 1.4545 1.0074 0.9374 -0.2935 -0.2701 -0.0502 166 ASN A ND2 1329 N N . THR A 167 ? 1.5536 0.9998 0.9962 -0.3072 -0.2992 -0.1051 167 THR A N 1330 C CA . THR A 167 ? 1.5984 0.9896 1.0331 -0.3158 -0.3080 -0.1050 167 THR A CA 1331 C C . THR A 167 ? 1.5984 0.9796 1.0359 -0.3368 -0.3088 -0.0839 167 THR A C 1332 O O . THR A 167 ? 1.6527 0.9867 1.0830 -0.3420 -0.3144 -0.0778 167 THR A O 1333 C CB . THR A 167 ? 1.6329 1.0015 1.0594 -0.3284 -0.3164 -0.1254 167 THR A CB 1334 O OG1 . THR A 167 ? 1.6205 1.0208 1.0532 -0.3522 -0.3176 -0.1262 167 THR A OG1 1335 C CG2 . THR A 167 ? 1.6323 1.0046 1.0506 -0.3063 -0.3157 -0.1470 167 THR A CG2 1336 N N . ASN A 168 ? 1.5422 0.9666 0.9892 -0.3479 -0.3025 -0.0724 168 ASN A N 1337 C CA . ASN A 168 ? 1.5315 0.9525 0.9797 -0.3660 -0.3006 -0.0517 168 ASN A CA 1338 C C . ASN A 168 ? 1.5239 0.9266 0.9674 -0.3495 -0.3001 -0.0370 168 ASN A C 1339 O O . ASN A 168 ? 1.5113 0.9222 0.9578 -0.3247 -0.2984 -0.0419 168 ASN A O 1340 C CB . ASN A 168 ? 1.4825 0.9583 0.9432 -0.3767 -0.2924 -0.0446 168 ASN A CB 1341 C CG . ASN A 168 ? 1.4696 0.9749 0.9376 -0.3862 -0.2935 -0.0600 168 ASN A CG 1342 O OD1 . ASN A 168 ? 1.4964 0.9941 0.9665 -0.4098 -0.2980 -0.0638 168 ASN A OD1 1343 N ND2 . ASN A 168 ? 1.4346 0.9745 0.9068 -0.3679 -0.2895 -0.0687 168 ASN A ND2 1344 N N . GLN A 169 ? 1.5345 0.9138 0.9705 -0.3632 -0.3014 -0.0189 169 GLN A N 1345 C CA . GLN A 169 ? 1.5356 0.9018 0.9653 -0.3482 -0.3025 -0.0034 169 GLN A CA 1346 C C . GLN A 169 ? 1.4766 0.8940 0.9163 -0.3404 -0.2945 0.0036 169 GLN A C 1347 O O . GLN A 169 ? 1.4639 0.8815 0.9029 -0.3227 -0.2959 0.0104 169 GLN A O 1348 C CB . GLN A 169 ? 1.5768 0.9034 0.9914 -0.3651 -0.3056 0.0157 169 GLN A CB 1349 C CG . GLN A 169 ? 1.6343 0.8977 1.0362 -0.3580 -0.3149 0.0162 169 GLN A CG 1350 C CD . GLN A 169 ? 1.6740 0.9039 1.0584 -0.3622 -0.3174 0.0413 169 GLN A CD 1351 O OE1 . GLN A 169 ? 1.7001 0.8981 1.0744 -0.3851 -0.3164 0.0520 169 GLN A OE1 1352 N NE2 . GLN A 169 ? 1.6608 0.9000 1.0415 -0.3406 -0.3202 0.0512 169 GLN A NE2 1353 N N . GLU A 170 ? 1.4358 0.8964 0.8862 -0.3533 -0.2866 0.0008 170 GLU A N 1354 C CA . GLU A 170 ? 1.3850 0.8924 0.8456 -0.3505 -0.2777 0.0077 170 GLU A CA 1355 C C . GLU A 170 ? 1.3457 0.8872 0.8211 -0.3284 -0.2721 -0.0040 170 GLU A C 1356 O O . GLU A 170 ? 1.3551 0.8899 0.8324 -0.3163 -0.2739 -0.0182 170 GLU A O 1357 C CB . GLU A 170 ? 1.3582 0.8952 0.8250 -0.3754 -0.2708 0.0117 170 GLU A CB 1358 C CG . GLU A 170 ? 1.3909 0.9023 0.8453 -0.3991 -0.2718 0.0269 170 GLU A CG 1359 C CD . GLU A 170 ? 1.4344 0.9087 0.8837 -0.4160 -0.2780 0.0213 170 GLU A CD 1360 O OE1 . GLU A 170 ? 1.4414 0.9019 0.8926 -0.4070 -0.2841 0.0049 170 GLU A OE1 1361 O OE2 . GLU A 170 ? 1.4322 0.8900 0.8752 -0.4392 -0.2760 0.0330 170 GLU A OE2 1362 N N . ASP A 171 ? 1.3135 0.8899 0.7987 -0.3234 -0.2645 0.0020 171 ASP A N 1363 C CA . ASP A 171 ? 1.2741 0.8884 0.7763 -0.3084 -0.2555 -0.0068 171 ASP A CA 1364 C C . ASP A 171 ? 1.2674 0.9100 0.7760 -0.3222 -0.2498 -0.0109 171 ASP A C 1365 O O . ASP A 171 ? 1.2673 0.9154 0.7736 -0.3433 -0.2495 -0.0036 171 ASP A O 1366 C CB . ASP A 171 ? 1.2405 0.8831 0.7532 -0.3018 -0.2486 0.0001 171 ASP A CB 1367 C CG . ASP A 171 ? 1.2524 0.8746 0.7617 -0.2863 -0.2556 0.0033 171 ASP A CG 1368 O OD1 . ASP A 171 ? 1.2733 0.8691 0.7803 -0.2718 -0.2620 -0.0033 171 ASP A OD1 1369 O OD2 . ASP A 171 ? 1.2412 0.8765 0.7509 -0.2876 -0.2547 0.0116 171 ASP A OD2 1370 N N . LEU A 172 ? 1.2673 0.9289 0.7839 -0.3097 -0.2451 -0.0221 172 LEU A N 1371 C CA . LEU A 172 ? 1.2710 0.9626 0.7938 -0.3184 -0.2410 -0.0263 172 LEU A CA 1372 C C . LEU A 172 ? 1.2262 0.9583 0.7651 -0.3060 -0.2282 -0.0255 172 LEU A C 1373 O O . LEU A 172 ? 1.2059 0.9393 0.7495 -0.2863 -0.2229 -0.0298 172 LEU A O 1374 C CB . LEU A 172 ? 1.3167 0.9939 0.8306 -0.3146 -0.2476 -0.0402 172 LEU A CB 1375 C CG . LEU A 172 ? 1.3435 1.0407 0.8589 -0.3311 -0.2505 -0.0448 172 LEU A CG 1376 C CD1 . LEU A 172 ? 1.3894 1.0611 0.8988 -0.3556 -0.2595 -0.0424 172 LEU A CD1 1377 C CD2 . LEU A 172 ? 1.3590 1.0587 0.8673 -0.3196 -0.2538 -0.0600 172 LEU A CD2 1378 N N . LEU A 173 ? 1.2017 0.9657 0.7505 -0.3179 -0.2224 -0.0201 173 LEU A N 1379 C CA . LEU A 173 ? 1.1680 0.9692 0.7328 -0.3075 -0.2099 -0.0194 173 LEU A CA 1380 C C . LEU A 173 ? 1.1773 0.9940 0.7413 -0.3026 -0.2101 -0.0268 173 LEU A C 1381 O O . LEU A 173 ? 1.2140 1.0431 0.7782 -0.3170 -0.2151 -0.0277 173 LEU A O 1382 C CB . LEU A 173 ? 1.1558 0.9841 0.7320 -0.3212 -0.2032 -0.0106 173 LEU A CB 1383 C CG . LEU A 173 ? 1.1275 0.9946 0.7219 -0.3123 -0.1902 -0.0100 173 LEU A CG 1384 C CD1 . LEU A 173 ? 1.1095 0.9776 0.7124 -0.2924 -0.1808 -0.0114 173 LEU A CD1 1385 C CD2 . LEU A 173 ? 1.1182 1.0107 0.7237 -0.3270 -0.1840 -0.0029 173 LEU A CD2 1386 N N . VAL A 174 ? 1.1630 0.9804 0.7262 -0.2822 -0.2046 -0.0322 174 VAL A N 1387 C CA . VAL A 174 ? 1.1488 0.9809 0.7070 -0.2737 -0.2041 -0.0383 174 VAL A CA 1388 C C . VAL A 174 ? 1.1080 0.9748 0.6818 -0.2630 -0.1896 -0.0319 174 VAL A C 1389 O O . VAL A 174 ? 1.0772 0.9467 0.6626 -0.2533 -0.1781 -0.0279 174 VAL A O 1390 C CB . VAL A 174 ? 1.1733 0.9814 0.7170 -0.2567 -0.2056 -0.0481 174 VAL A CB 1391 C CG1 . VAL A 174 ? 1.1922 1.0136 0.7241 -0.2490 -0.2074 -0.0552 174 VAL A CG1 1392 C CG2 . VAL A 174 ? 1.2010 0.9700 0.7322 -0.2645 -0.2183 -0.0539 174 VAL A CG2 1393 N N . LEU A 175 ? 1.1009 0.9938 0.6760 -0.2648 -0.1905 -0.0316 175 LEU A N 1394 C CA . LEU A 175 ? 1.0732 0.9972 0.6615 -0.2532 -0.1774 -0.0249 175 LEU A CA 1395 C C . LEU A 175 ? 1.0844 1.0171 0.6593 -0.2375 -0.1777 -0.0284 175 LEU A C 1396 O O . LEU A 175 ? 1.1045 1.0337 0.6642 -0.2425 -0.1914 -0.0365 175 LEU A O 1397 C CB . LEU A 175 ? 1.0560 1.0090 0.6600 -0.2678 -0.1778 -0.0192 175 LEU A CB 1398 C CG . LEU A 175 ? 1.0426 0.9941 0.6589 -0.2831 -0.1749 -0.0142 175 LEU A CG 1399 C CD1 . LEU A 175 ? 1.0360 1.0165 0.6654 -0.2989 -0.1764 -0.0109 175 LEU A CD1 1400 C CD2 . LEU A 175 ? 1.0219 0.9770 0.6519 -0.2715 -0.1594 -0.0095 175 LEU A CD2 1401 N N . TRP A 176 ? 1.0727 1.0161 0.6526 -0.2187 -0.1624 -0.0224 176 TRP A N 1402 C CA . TRP A 176 ? 1.0832 1.0387 0.6489 -0.2019 -0.1603 -0.0220 176 TRP A CA 1403 C C . TRP A 176 ? 1.0637 1.0388 0.6439 -0.1867 -0.1414 -0.0100 176 TRP A C 1404 O O . TRP A 176 ? 1.0411 1.0203 0.6438 -0.1902 -0.1303 -0.0043 176 TRP A O 1405 C CB . TRP A 176 ? 1.1107 1.0404 0.6530 -0.1898 -0.1614 -0.0307 176 TRP A CB 1406 C CG . TRP A 176 ? 1.1028 1.0161 0.6522 -0.1775 -0.1449 -0.0285 176 TRP A CG 1407 C CD1 . TRP A 176 ? 1.0982 1.0149 0.6461 -0.1579 -0.1273 -0.0229 176 TRP A CD1 1408 C CD2 . TRP A 176 ? 1.0965 0.9886 0.6568 -0.1840 -0.1445 -0.0319 176 TRP A CD2 1409 N NE1 . TRP A 176 ? 1.0869 0.9876 0.6475 -0.1531 -0.1155 -0.0241 176 TRP A NE1 1410 C CE2 . TRP A 176 ? 1.0906 0.9771 0.6589 -0.1680 -0.1269 -0.0299 176 TRP A CE2 1411 C CE3 . TRP A 176 ? 1.1024 0.9798 0.6662 -0.2013 -0.1572 -0.0357 176 TRP A CE3 1412 C CZ2 . TRP A 176 ? 1.0902 0.9604 0.6722 -0.1685 -0.1234 -0.0333 176 TRP A CZ2 1413 C CZ3 . TRP A 176 ? 1.1008 0.9595 0.6743 -0.2003 -0.1540 -0.0372 176 TRP A CZ3 1414 C CH2 . TRP A 176 ? 1.0919 0.9489 0.6755 -0.1839 -0.1382 -0.0369 176 TRP A CH2 1415 N N . GLY A 177 ? 1.0846 1.0707 0.6508 -0.1697 -0.1377 -0.0062 177 GLY A N 1416 C CA . GLY A 177 ? 1.0740 1.0752 0.6518 -0.1537 -0.1190 0.0068 177 GLY A CA 1417 C C . GLY A 177 ? 1.0950 1.0945 0.6501 -0.1309 -0.1106 0.0117 177 GLY A C 1418 O O . GLY A 177 ? 1.1119 1.1040 0.6390 -0.1266 -0.1215 0.0038 177 GLY A O 1419 N N . ILE A 178 ? 1.0950 1.1001 0.6618 -0.1166 -0.0901 0.0248 178 ILE A N 1420 C CA . ILE A 178 ? 1.1210 1.1256 0.6676 -0.0935 -0.0775 0.0343 178 ILE A CA 1421 C C . ILE A 178 ? 1.1190 1.1488 0.6753 -0.0847 -0.0734 0.0485 178 ILE A C 1422 O O . ILE A 178 ? 1.0915 1.1322 0.6776 -0.0931 -0.0689 0.0523 178 ILE A O 1423 C CB . ILE A 178 ? 1.1224 1.1061 0.6770 -0.0834 -0.0524 0.0388 178 ILE A CB 1424 C CG1 . ILE A 178 ? 1.1528 1.1348 0.6863 -0.0596 -0.0355 0.0517 178 ILE A CG1 1425 C CG2 . ILE A 178 ? 1.0879 1.0738 0.6812 -0.0902 -0.0374 0.0439 178 ILE A CG2 1426 C CD1 . ILE A 178 ? 1.1867 1.1494 0.6917 -0.0502 -0.0316 0.0449 178 ILE A CD1 1427 N N . HIS A 179 ? 1.1554 1.1948 0.6856 -0.0667 -0.0753 0.0561 179 HIS A N 1428 C CA . HIS A 179 ? 1.1700 1.2319 0.7082 -0.0541 -0.0706 0.0716 179 HIS A CA 1429 C C . HIS A 179 ? 1.1881 1.2378 0.7202 -0.0315 -0.0444 0.0890 179 HIS A C 1430 O O . HIS A 179 ? 1.2202 1.2556 0.7218 -0.0181 -0.0381 0.0910 179 HIS A O 1431 C CB . HIS A 179 ? 1.1985 1.2853 0.7137 -0.0488 -0.0938 0.0695 179 HIS A CB 1432 C CG . HIS A 179 ? 1.2066 1.3162 0.7249 -0.0303 -0.0896 0.0869 179 HIS A CG 1433 N ND1 . HIS A 179 ? 1.2459 1.3614 0.7303 -0.0067 -0.0909 0.0970 179 HIS A ND1 1434 C CD2 . HIS A 179 ? 1.1872 1.3145 0.7378 -0.0302 -0.0837 0.0963 179 HIS A CD2 1435 C CE1 . HIS A 179 ? 1.2506 1.3862 0.7467 0.0075 -0.0871 0.1130 179 HIS A CE1 1436 N NE2 . HIS A 179 ? 1.2162 1.3591 0.7537 -0.0063 -0.0822 0.1123 179 HIS A NE2 1437 N N . HIS A 180 ? 1.1758 1.2305 0.7369 -0.0276 -0.0282 0.1015 180 HIS A N 1438 C CA . HIS A 180 ? 1.2057 1.2481 0.7656 -0.0072 -0.0017 0.1201 180 HIS A CA 1439 C C . HIS A 180 ? 1.2295 1.2926 0.7776 0.0123 -0.0059 0.1365 180 HIS A C 1440 O O . HIS A 180 ? 1.2190 1.3031 0.7917 0.0088 -0.0123 0.1389 180 HIS A O 1441 C CB . HIS A 180 ? 1.1866 1.2182 0.7881 -0.0150 0.0198 0.1222 180 HIS A CB 1442 C CG . HIS A 180 ? 1.1740 1.1898 0.7900 -0.0338 0.0210 0.1057 180 HIS A CG 1443 N ND1 . HIS A 180 ? 1.1929 1.1859 0.8004 -0.0299 0.0357 0.1036 180 HIS A ND1 1444 C CD2 . HIS A 180 ? 1.1510 1.1714 0.7886 -0.0554 0.0091 0.0911 180 HIS A CD2 1445 C CE1 . HIS A 180 ? 1.1687 1.1539 0.7938 -0.0474 0.0315 0.0880 180 HIS A CE1 1446 N NE2 . HIS A 180 ? 1.1454 1.1458 0.7870 -0.0630 0.0153 0.0809 180 HIS A NE2 1447 N N . PRO A 181 ? 1.2617 1.3201 0.7711 0.0338 -0.0027 0.1478 181 PRO A N 1448 C CA . PRO A 181 ? 1.2890 1.3672 0.7815 0.0554 -0.0089 0.1643 181 PRO A CA 1449 C C . PRO A 181 ? 1.2870 1.3553 0.7976 0.0723 0.0183 0.1875 181 PRO A C 1450 O O . PRO A 181 ? 1.2781 1.3199 0.8047 0.0703 0.0451 0.1919 181 PRO A O 1451 C CB . PRO A 181 ? 1.3403 1.4126 0.7800 0.0714 -0.0140 0.1661 181 PRO A CB 1452 C CG . PRO A 181 ? 1.3416 1.3815 0.7778 0.0668 0.0079 0.1622 181 PRO A CG 1453 C CD . PRO A 181 ? 1.2941 1.3279 0.7736 0.0406 0.0090 0.1465 181 PRO A CD 1454 N N . ASN A 182 ? 1.2960 1.3856 0.8058 0.0889 0.0113 0.2017 182 ASN A N 1455 C CA . ASN A 182 ? 1.3029 1.3825 0.8299 0.1071 0.0360 0.2251 182 ASN A CA 1456 C C . ASN A 182 ? 1.3401 1.3903 0.8364 0.1289 0.0619 0.2461 182 ASN A C 1457 O O . ASN A 182 ? 1.3248 1.3499 0.8430 0.1323 0.0920 0.2584 182 ASN A O 1458 C CB . ASN A 182 ? 1.3126 1.4242 0.8445 0.1221 0.0196 0.2353 182 ASN A CB 1459 C CG . ASN A 182 ? 1.2721 1.4106 0.8448 0.1009 0.0030 0.2181 182 ASN A CG 1460 O OD1 . ASN A 182 ? 1.2411 1.3709 0.8534 0.0895 0.0188 0.2155 182 ASN A OD1 1461 N ND2 . ASN A 182 ? 1.2716 1.4431 0.8349 0.0947 -0.0280 0.2054 182 ASN A ND2 1462 N N . ASP A 183 ? 1.3821 1.4358 0.8280 0.1428 0.0506 0.2491 183 ASP A N 1463 C CA . ASP A 183 ? 1.4351 1.4645 0.8432 0.1665 0.0736 0.2711 183 ASP A CA 1464 C C . ASP A 183 ? 1.4575 1.4863 0.8136 0.1698 0.0616 0.2615 183 ASP A C 1465 O O . ASP A 183 ? 1.4440 1.4933 0.7913 0.1565 0.0321 0.2391 183 ASP A O 1466 C CB . ASP A 183 ? 1.4751 1.5134 0.8689 0.1961 0.0752 0.2988 183 ASP A CB 1467 C CG . ASP A 183 ? 1.4962 1.5732 0.8623 0.2060 0.0378 0.2941 183 ASP A CG 1468 O OD1 . ASP A 183 ? 1.5154 1.6029 0.8505 0.1988 0.0170 0.2761 183 ASP A OD1 1469 O OD2 . ASP A 183 ? 1.4985 1.5959 0.8758 0.2211 0.0291 0.3073 183 ASP A OD2 1470 N N . ALA A 184 ? 1.4944 1.4990 0.8158 0.1877 0.0855 0.2785 184 ALA A N 1471 C CA . ALA A 184 ? 1.5259 1.5266 0.7952 0.1931 0.0793 0.2702 184 ALA A CA 1472 C C . ALA A 184 ? 1.5456 1.5782 0.7748 0.2038 0.0428 0.2638 184 ALA A C 1473 O O . ALA A 184 ? 1.5444 1.5848 0.7500 0.1944 0.0227 0.2412 184 ALA A O 1474 C CB . ALA A 184 ? 1.5644 1.5358 0.8017 0.2141 0.1139 0.2942 184 ALA A CB 1475 N N . ALA A 185 ? 1.5639 1.6151 0.7875 0.2237 0.0339 0.2828 185 ALA A N 1476 C CA . ALA A 185 ? 1.5895 1.6762 0.7799 0.2350 -0.0021 0.2771 185 ALA A CA 1477 C C . ALA A 185 ? 1.5355 1.6496 0.7557 0.2075 -0.0346 0.2457 185 ALA A C 1478 O O . ALA A 185 ? 1.5384 1.6719 0.7297 0.2040 -0.0626 0.2266 185 ALA A O 1479 C CB . ALA A 185 ? 1.6171 1.7197 0.8056 0.2616 -0.0045 0.3042 185 ALA A CB 1480 N N . GLU A 186 ? 1.4872 1.6016 0.7645 0.1875 -0.0295 0.2402 186 GLU A N 1481 C CA . GLU A 186 ? 1.4501 1.5870 0.7593 0.1595 -0.0556 0.2128 186 GLU A CA 1482 C C . GLU A 186 ? 1.4352 1.5572 0.7323 0.1384 -0.0612 0.1873 186 GLU A C 1483 O O . GLU A 186 ? 1.4221 1.5637 0.7153 0.1236 -0.0899 0.1646 186 GLU A O 1484 C CB . GLU A 186 ? 1.4078 1.5441 0.7775 0.1437 -0.0441 0.2139 186 GLU A CB 1485 C CG . GLU A 186 ? 1.3757 1.5356 0.7780 0.1152 -0.0690 0.1885 186 GLU A CG 1486 C CD . GLU A 186 ? 1.3486 1.5263 0.8013 0.1095 -0.0672 0.1933 186 GLU A CD 1487 O OE1 . GLU A 186 ? 1.3270 1.4847 0.8143 0.0979 -0.0452 0.1946 186 GLU A OE1 1488 O OE2 . GLU A 186 ? 1.3512 1.5646 0.8097 0.1165 -0.0882 0.1944 186 GLU A OE2 1489 N N . GLN A 187 ? 1.4363 1.5234 0.7295 0.1372 -0.0331 0.1909 187 GLN A N 1490 C CA . GLN A 187 ? 1.4403 1.5105 0.7217 0.1209 -0.0353 0.1684 187 GLN A CA 1491 C C . GLN A 187 ? 1.4905 1.5694 0.7164 0.1312 -0.0556 0.1576 187 GLN A C 1492 O O . GLN A 187 ? 1.4818 1.5670 0.7033 0.1141 -0.0785 0.1320 187 GLN A O 1493 C CB . GLN A 187 ? 1.4372 1.4716 0.7249 0.1220 0.0008 0.1767 187 GLN A CB 1494 C CG . GLN A 187 ? 1.4431 1.4589 0.7075 0.1148 0.0027 0.1582 187 GLN A CG 1495 C CD . GLN A 187 ? 1.3981 1.4148 0.6898 0.0863 -0.0159 0.1305 187 GLN A CD 1496 O OE1 . GLN A 187 ? 1.3466 1.3599 0.6844 0.0691 -0.0103 0.1278 187 GLN A OE1 1497 N NE2 . GLN A 187 ? 1.4150 1.4347 0.6769 0.0815 -0.0375 0.1100 187 GLN A NE2 1498 N N . THR A 188 ? 1.5555 1.6330 0.7382 0.1593 -0.0463 0.1772 188 THR A N 1499 C CA . THR A 188 ? 1.6099 1.6955 0.7341 0.1725 -0.0635 0.1680 188 THR A CA 1500 C C . THR A 188 ? 1.6081 1.7325 0.7306 0.1673 -0.1041 0.1525 188 THR A C 1501 O O . THR A 188 ? 1.6185 1.7507 0.7193 0.1579 -0.1274 0.1273 188 THR A O 1502 C CB . THR A 188 ? 1.6724 1.7510 0.7459 0.2063 -0.0459 0.1952 188 THR A CB 1503 O OG1 . THR A 188 ? 1.7100 1.8217 0.7511 0.2238 -0.0746 0.1983 188 THR A OG1 1504 C CG2 . THR A 188 ? 1.6713 1.7313 0.7693 0.2176 -0.0116 0.2265 188 THR A CG2 1505 N N . LYS A 189 ? 1.5955 1.7443 0.7437 0.1735 -0.1115 0.1669 189 LYS A N 1506 C CA . LYS A 189 ? 1.5966 1.7871 0.7518 0.1689 -0.1485 0.1539 189 LYS A CA 1507 C C . LYS A 189 ? 1.5682 1.7650 0.7523 0.1350 -0.1692 0.1218 189 LYS A C 1508 O O . LYS A 189 ? 1.5819 1.8010 0.7490 0.1287 -0.1993 0.1005 189 LYS A O 1509 C CB . LYS A 189 ? 1.5732 1.7855 0.7655 0.1774 -0.1476 0.1739 189 LYS A CB 1510 C CG . LYS A 189 ? 1.5616 1.8194 0.7774 0.1673 -0.1831 0.1585 189 LYS A CG 1511 C CD . LYS A 189 ? 1.5511 1.8309 0.8024 0.1796 -0.1801 0.1794 189 LYS A CD 1512 C CE . LYS A 189 ? 1.5304 1.8570 0.8149 0.1655 -0.2128 0.1620 189 LYS A CE 1513 N NZ . LYS A 189 ? 1.5039 1.8485 0.8357 0.1708 -0.2058 0.1781 189 LYS A NZ 1514 N N . LEU A 190 ? 1.5306 1.7074 0.7584 0.1133 -0.1531 0.1184 190 LEU A N 1515 C CA . LEU A 190 ? 1.5065 1.6873 0.7645 0.0812 -0.1707 0.0919 190 LEU A CA 1516 C C . LEU A 190 ? 1.5176 1.6739 0.7494 0.0700 -0.1742 0.0697 190 LEU A C 1517 O O . LEU A 190 ? 1.5010 1.6669 0.7349 0.0511 -0.1989 0.0452 190 LEU A O 1518 C CB . LEU A 190 ? 1.4670 1.6360 0.7788 0.0632 -0.1530 0.0968 190 LEU A CB 1519 C CG . LEU A 190 ? 1.4605 1.6582 0.8101 0.0650 -0.1561 0.1094 190 LEU A CG 1520 C CD1 . LEU A 190 ? 1.4255 1.6036 0.8167 0.0569 -0.1289 0.1203 190 LEU A CD1 1521 C CD2 . LEU A 190 ? 1.4479 1.6794 0.8193 0.0444 -0.1870 0.0896 190 LEU A CD2 1522 N N . TYR A 191 ? 1.5393 1.6636 0.7491 0.0813 -0.1482 0.0779 191 TYR A N 1523 C CA . TYR A 191 ? 1.5506 1.6473 0.7453 0.0700 -0.1457 0.0577 191 TYR A CA 1524 C C . TYR A 191 ? 1.6244 1.7075 0.7621 0.0923 -0.1368 0.0589 191 TYR A C 1525 O O . TYR A 191 ? 1.6488 1.7091 0.7711 0.0860 -0.1334 0.0418 191 TYR A O 1526 C CB . TYR A 191 ? 1.5117 1.5801 0.7444 0.0563 -0.1204 0.0611 191 TYR A CB 1527 C CG . TYR A 191 ? 1.4523 1.5321 0.7388 0.0364 -0.1244 0.0625 191 TYR A CG 1528 C CD1 . TYR A 191 ? 1.4321 1.5219 0.7387 0.0113 -0.1488 0.0418 191 TYR A CD1 1529 C CD2 . TYR A 191 ? 1.4193 1.4994 0.7357 0.0424 -0.1031 0.0842 191 TYR A CD2 1530 C CE1 . TYR A 191 ? 1.3811 1.4819 0.7339 -0.0067 -0.1511 0.0433 191 TYR A CE1 1531 C CE2 . TYR A 191 ? 1.3768 1.4681 0.7401 0.0247 -0.1063 0.0838 191 TYR A CE2 1532 C CZ . TYR A 191 ? 1.3543 1.4568 0.7343 0.0004 -0.1301 0.0637 191 TYR A CZ 1533 O OH . TYR A 191 ? 1.3123 1.4266 0.7358 -0.0170 -0.1320 0.0636 191 TYR A OH 1534 N N . GLN A 192 ? 1.6692 1.7660 0.7750 0.1191 -0.1328 0.0793 192 GLN A N 1535 C CA . GLN A 192 ? 1.7181 1.8025 0.7661 0.1439 -0.1198 0.0863 192 GLN A CA 1536 C C . GLN A 192 ? 1.7044 1.7530 0.7547 0.1496 -0.0798 0.0998 192 GLN A C 1537 O O . GLN A 192 ? 1.7265 1.7684 0.7613 0.1711 -0.0557 0.1269 192 GLN A O 1538 C CB . GLN A 192 ? 1.7671 1.8554 0.7740 0.1410 -0.1443 0.0570 192 GLN A CB 1539 C CG . GLN A 192 ? 1.8433 1.9360 0.7823 0.1707 -0.1429 0.0644 192 GLN A CG 1540 C CD . GLN A 192 ? 1.8918 2.0211 0.8009 0.1772 -0.1809 0.0515 192 GLN A CD 1541 O OE1 . GLN A 192 ? 1.8902 2.0495 0.8097 0.1857 -0.1946 0.0659 192 GLN A OE1 1542 N NE2 . GLN A 192 ? 1.9427 2.0704 0.8138 0.1747 -0.1980 0.0234 192 GLN A NE2 1543 N N . ASN A 193 ? 1.6729 1.6991 0.7448 0.1304 -0.0726 0.0818 193 ASN A N 1544 C CA . ASN A 193 ? 1.6741 1.6694 0.7502 0.1344 -0.0366 0.0899 193 ASN A CA 1545 C C . ASN A 193 ? 1.6315 1.6211 0.7506 0.1347 -0.0110 0.1151 193 ASN A C 1546 O O . ASN A 193 ? 1.5953 1.5971 0.7570 0.1200 -0.0220 0.1153 193 ASN A O 1547 C CB . ASN A 193 ? 1.6594 1.6350 0.7566 0.1132 -0.0376 0.0640 193 ASN A CB 1548 C CG . ASN A 193 ? 1.6903 1.6719 0.7616 0.1047 -0.0692 0.0343 193 ASN A CG 1549 O OD1 . ASN A 193 ? 1.7227 1.6878 0.7662 0.1081 -0.0651 0.0183 193 ASN A OD1 1550 N ND2 . ASN A 193 ? 1.6835 1.6886 0.7668 0.0926 -0.0999 0.0257 193 ASN A ND2 1551 N N . PRO A 194 ? 1.6429 1.6135 0.7517 0.1508 0.0239 0.1357 194 PRO A N 1552 C CA . PRO A 194 ? 1.6087 1.5713 0.7588 0.1510 0.0497 0.1586 194 PRO A CA 1553 C C . PRO A 194 ? 1.5528 1.4975 0.7546 0.1298 0.0661 0.1484 194 PRO A C 1554 O O . PRO A 194 ? 1.5123 1.4588 0.7611 0.1190 0.0713 0.1550 194 PRO A O 1555 C CB . PRO A 194 ? 1.6631 1.6120 0.7755 0.1775 0.0802 0.1846 194 PRO A CB 1556 C CG . PRO A 194 ? 1.7023 1.6414 0.7702 0.1831 0.0823 0.1693 194 PRO A CG 1557 C CD . PRO A 194 ? 1.6980 1.6536 0.7564 0.1696 0.0428 0.1389 194 PRO A CD 1558 N N . THR A 195 ? 1.5501 1.4788 0.7436 0.1251 0.0739 0.1318 195 THR A N 1559 C CA . THR A 195 ? 1.5011 1.4148 0.7420 0.1069 0.0877 0.1208 195 THR A CA 1560 C C . THR A 195 ? 1.4680 1.3851 0.7184 0.0871 0.0580 0.0918 195 THR A C 1561 O O . THR A 195 ? 1.4880 1.4009 0.7044 0.0901 0.0472 0.0751 195 THR A O 1562 C CB . THR A 195 ? 1.5236 1.4165 0.7552 0.1167 0.1216 0.1242 195 THR A CB 1563 O OG1 . THR A 195 ? 1.5515 1.4392 0.7661 0.1364 0.1494 0.1529 195 THR A OG1 1564 C CG2 . THR A 195 ? 1.4814 1.3626 0.7682 0.0995 0.1369 0.1151 195 THR A CG2 1565 N N . THR A 196 ? 1.4148 1.3379 0.7101 0.0672 0.0457 0.0859 196 THR A N 1566 C CA . THR A 196 ? 1.3912 1.3167 0.6964 0.0474 0.0169 0.0615 196 THR A CA 1567 C C . THR A 196 ? 1.3462 1.2606 0.6999 0.0287 0.0224 0.0522 196 THR A C 1568 O O . THR A 196 ? 1.3224 1.2306 0.7066 0.0294 0.0471 0.0632 196 THR A O 1569 C CB . THR A 196 ? 1.3822 1.3312 0.6870 0.0397 -0.0129 0.0600 196 THR A CB 1570 O OG1 . THR A 196 ? 1.3460 1.3057 0.6864 0.0365 -0.0052 0.0765 196 THR A OG1 1571 C CG2 . THR A 196 ? 1.4327 1.3952 0.6870 0.0577 -0.0247 0.0639 196 THR A CG2 1572 N N . TYR A 197 ? 1.3341 1.2457 0.6937 0.0122 -0.0010 0.0317 197 TYR A N 1573 C CA . TYR A 197 ? 1.2963 1.1969 0.6955 -0.0043 -0.0001 0.0213 197 TYR A CA 1574 C C . TYR A 197 ? 1.2926 1.1932 0.6933 -0.0227 -0.0310 0.0034 197 TYR A C 1575 O O . TYR A 197 ? 1.3200 1.2246 0.6892 -0.0218 -0.0506 -0.0055 197 TYR A O 1576 C CB . TYR A 197 ? 1.3045 1.1859 0.7025 0.0028 0.0186 0.0135 197 TYR A CB 1577 C CG . TYR A 197 ? 1.3305 1.2011 0.6925 0.0064 0.0044 -0.0051 197 TYR A CG 1578 C CD1 . TYR A 197 ? 1.3755 1.2481 0.6902 0.0235 0.0064 -0.0035 197 TYR A CD1 1579 C CD2 . TYR A 197 ? 1.3138 1.1710 0.6879 -0.0064 -0.0109 -0.0246 197 TYR A CD2 1580 C CE1 . TYR A 197 ? 1.4072 1.2696 0.6885 0.0267 -0.0065 -0.0231 197 TYR A CE1 1581 C CE2 . TYR A 197 ? 1.3490 1.1936 0.6918 -0.0029 -0.0233 -0.0429 197 TYR A CE2 1582 C CZ . TYR A 197 ? 1.3948 1.2423 0.6916 0.0131 -0.0210 -0.0432 197 TYR A CZ 1583 O OH . TYR A 197 ? 1.4260 1.2606 0.6913 0.0163 -0.0333 -0.0639 197 TYR A OH 1584 N N . ILE A 198 ? 1.2581 1.1538 0.6952 -0.0394 -0.0348 -0.0018 198 ILE A N 1585 C CA . ILE A 198 ? 1.2532 1.1420 0.6929 -0.0570 -0.0601 -0.0181 198 ILE A CA 1586 C C . ILE A 198 ? 1.2385 1.1081 0.7016 -0.0627 -0.0546 -0.0274 198 ILE A C 1587 O O . ILE A 198 ? 1.2205 1.0928 0.7180 -0.0695 -0.0458 -0.0218 198 ILE A O 1588 C CB . ILE A 198 ? 1.2307 1.1357 0.6912 -0.0742 -0.0755 -0.0140 198 ILE A CB 1589 C CG1 . ILE A 198 ? 1.2452 1.1740 0.6907 -0.0677 -0.0804 -0.0034 198 ILE A CG1 1590 C CG2 . ILE A 198 ? 1.2368 1.1320 0.6955 -0.0924 -0.1004 -0.0297 198 ILE A CG2 1591 C CD1 . ILE A 198 ? 1.2192 1.1674 0.6938 -0.0804 -0.0856 0.0047 198 ILE A CD1 1592 N N . SER A 199 ? 1.2545 1.1055 0.6994 -0.0594 -0.0605 -0.0426 199 SER A N 1593 C CA . SER A 199 ? 1.2432 1.0763 0.7098 -0.0639 -0.0594 -0.0527 199 SER A CA 1594 C C . SER A 199 ? 1.2417 1.0646 0.7123 -0.0825 -0.0854 -0.0627 199 SER A C 1595 O O . SER A 199 ? 1.2612 1.0771 0.7064 -0.0867 -0.1034 -0.0726 199 SER A O 1596 C CB . SER A 199 ? 1.2683 1.0852 0.7174 -0.0485 -0.0485 -0.0635 199 SER A CB 1597 O OG . SER A 199 ? 1.2985 1.1123 0.7058 -0.0415 -0.0579 -0.0713 199 SER A OG 1598 N N . VAL A 200 ? 1.2310 1.0533 0.7336 -0.0938 -0.0869 -0.0599 200 VAL A N 1599 C CA . VAL A 200 ? 1.2343 1.0441 0.7420 -0.1109 -0.1085 -0.0667 200 VAL A CA 1600 C C . VAL A 200 ? 1.2490 1.0398 0.7739 -0.1081 -0.1064 -0.0743 200 VAL A C 1601 O O . VAL A 200 ? 1.2462 1.0437 0.7947 -0.1003 -0.0893 -0.0704 200 VAL A O 1602 C CB . VAL A 200 ? 1.2036 1.0302 0.7320 -0.1266 -0.1134 -0.0561 200 VAL A CB 1603 C CG1 . VAL A 200 ? 1.2170 1.0316 0.7414 -0.1453 -0.1362 -0.0617 200 VAL A CG1 1604 C CG2 . VAL A 200 ? 1.1997 1.0514 0.7222 -0.1241 -0.1078 -0.0453 200 VAL A CG2 1605 N N . GLY A 201 ? 1.2733 1.0406 0.7883 -0.1143 -0.1240 -0.0852 201 GLY A N 1606 C CA . GLY A 201 ? 1.2760 1.0242 0.8061 -0.1095 -0.1245 -0.0926 201 GLY A CA 1607 C C . GLY A 201 ? 1.2867 1.0119 0.8136 -0.1233 -0.1466 -0.0971 201 GLY A C 1608 O O . GLY A 201 ? 1.3245 1.0378 0.8291 -0.1319 -0.1609 -0.1024 201 GLY A O 1609 N N . THR A 202 ? 1.2656 0.9851 0.8152 -0.1256 -0.1493 -0.0947 202 THR A N 1610 C CA . THR A 202 ? 1.2781 0.9705 0.8245 -0.1345 -0.1682 -0.0978 202 THR A CA 1611 C C . THR A 202 ? 1.2903 0.9704 0.8537 -0.1196 -0.1650 -0.1041 202 THR A C 1612 O O . THR A 202 ? 1.3003 0.9890 0.8718 -0.1034 -0.1492 -0.1097 202 THR A O 1613 C CB . THR A 202 ? 1.2530 0.9530 0.8085 -0.1531 -0.1775 -0.0860 202 THR A CB 1614 O OG1 . THR A 202 ? 1.2139 0.9323 0.7967 -0.1491 -0.1681 -0.0799 202 THR A OG1 1615 C CG2 . THR A 202 ? 1.2382 0.9576 0.7838 -0.1664 -0.1779 -0.0796 202 THR A CG2 1616 N N . SER A 203 ? 1.2959 0.9569 0.8653 -0.1242 -0.1793 -0.1029 203 SER A N 1617 C CA . SER A 203 ? 1.2954 0.9489 0.8850 -0.1093 -0.1782 -0.1080 203 SER A CA 1618 C C . SER A 203 ? 1.2563 0.9418 0.8774 -0.1049 -0.1649 -0.1030 203 SER A C 1619 O O . SER A 203 ? 1.2654 0.9566 0.9086 -0.0897 -0.1566 -0.1097 203 SER A O 1620 C CB . SER A 203 ? 1.3169 0.9420 0.9031 -0.1147 -0.1982 -0.1055 203 SER A CB 1621 O OG . SER A 203 ? 1.2884 0.9263 0.8821 -0.1286 -0.2040 -0.0927 203 SER A OG 1622 N N . THR A 204 ? 1.2204 0.9273 0.8459 -0.1186 -0.1626 -0.0924 204 THR A N 1623 C CA . THR A 204 ? 1.1794 0.9157 0.8352 -0.1170 -0.1503 -0.0887 204 THR A CA 1624 C C . THR A 204 ? 1.1565 0.9161 0.8150 -0.1162 -0.1303 -0.0854 204 THR A C 1625 O O . THR A 204 ? 1.1631 0.9396 0.8447 -0.1060 -0.1124 -0.0879 204 THR A O 1626 C CB . THR A 204 ? 1.1546 0.8980 0.8154 -0.1320 -0.1616 -0.0796 204 THR A CB 1627 O OG1 . THR A 204 ? 1.1525 0.9054 0.7988 -0.1470 -0.1604 -0.0712 204 THR A OG1 1628 C CG2 . THR A 204 ? 1.1658 0.8810 0.8138 -0.1351 -0.1830 -0.0787 204 THR A CG2 1629 N N . LEU A 205 ? 1.1461 0.9066 0.7818 -0.1267 -0.1331 -0.0794 205 LEU A N 1630 C CA . LEU A 205 ? 1.1189 0.9014 0.7548 -0.1259 -0.1163 -0.0735 205 LEU A CA 1631 C C . LEU A 205 ? 1.1237 0.9057 0.7535 -0.1090 -0.0998 -0.0789 205 LEU A C 1632 O O . LEU A 205 ? 1.1369 0.8994 0.7465 -0.1021 -0.1056 -0.0876 205 LEU A O 1633 C CB . LEU A 205 ? 1.1253 0.9097 0.7382 -0.1397 -0.1262 -0.0671 205 LEU A CB 1634 C CG . LEU A 205 ? 1.1198 0.9295 0.7348 -0.1412 -0.1129 -0.0580 205 LEU A CG 1635 C CD1 . LEU A 205 ? 1.0862 0.9160 0.7315 -0.1447 -0.1022 -0.0518 205 LEU A CD1 1636 C CD2 . LEU A 205 ? 1.1296 0.9417 0.7237 -0.1545 -0.1261 -0.0541 205 LEU A CD2 1637 N N . ASN A 206 ? 1.1056 0.9079 0.7528 -0.1026 -0.0782 -0.0739 206 ASN A N 1638 C CA . ASN A 206 ? 1.1179 0.9226 0.7579 -0.0873 -0.0583 -0.0753 206 ASN A CA 1639 C C . ASN A 206 ? 1.1109 0.9350 0.7513 -0.0869 -0.0412 -0.0629 206 ASN A C 1640 O O . ASN A 206 ? 1.0989 0.9347 0.7618 -0.0800 -0.0192 -0.0592 206 ASN A O 1641 C CB . ASN A 206 ? 1.1152 0.9210 0.7833 -0.0752 -0.0441 -0.0831 206 ASN A CB 1642 C CG . ASN A 206 ? 1.1423 0.9461 0.7982 -0.0590 -0.0242 -0.0862 206 ASN A CG 1643 O OD1 . ASN A 206 ? 1.1802 0.9731 0.8002 -0.0548 -0.0286 -0.0880 206 ASN A OD1 1644 N ND2 . ASN A 206 ? 1.1354 0.9503 0.8211 -0.0501 -0.0018 -0.0876 206 ASN A ND2 1645 N N . GLN A 207 ? 1.1267 0.9538 0.7432 -0.0941 -0.0513 -0.0566 207 GLN A N 1646 C CA . GLN A 207 ? 1.1292 0.9745 0.7456 -0.0936 -0.0386 -0.0436 207 GLN A CA 1647 C C . GLN A 207 ? 1.1696 1.0150 0.7571 -0.0791 -0.0270 -0.0400 207 GLN A C 1648 O O . GLN A 207 ? 1.1918 1.0245 0.7505 -0.0738 -0.0360 -0.0484 207 GLN A O 1649 C CB . GLN A 207 ? 1.1238 0.9766 0.7337 -0.1091 -0.0565 -0.0387 207 GLN A CB 1650 C CG . GLN A 207 ? 1.1217 0.9941 0.7319 -0.1087 -0.0472 -0.0256 207 GLN A CG 1651 C CD . GLN A 207 ? 1.1236 1.0059 0.7337 -0.1250 -0.0645 -0.0225 207 GLN A CD 1652 O OE1 . GLN A 207 ? 1.1544 1.0424 0.7426 -0.1272 -0.0753 -0.0206 207 GLN A OE1 1653 N NE2 . GLN A 207 ? 1.0910 0.9768 0.7256 -0.1367 -0.0674 -0.0231 207 GLN A NE2 1654 N N . ARG A 208 ? 1.1795 1.0381 0.7741 -0.0721 -0.0065 -0.0274 208 ARG A N 1655 C CA . ARG A 208 ? 1.2232 1.0848 0.7865 -0.0588 0.0028 -0.0194 208 ARG A CA 1656 C C . ARG A 208 ? 1.2224 1.1002 0.7964 -0.0575 0.0160 -0.0024 208 ARG A C 1657 O O . ARG A 208 ? 1.2248 1.1052 0.8239 -0.0527 0.0396 0.0048 208 ARG A O 1658 C CB . ARG A 208 ? 1.2541 1.1066 0.8091 -0.0424 0.0236 -0.0223 208 ARG A CB 1659 C CG . ARG A 208 ? 1.2970 1.1496 0.8087 -0.0279 0.0287 -0.0167 208 ARG A CG 1660 C CD . ARG A 208 ? 1.3270 1.1754 0.8356 -0.0111 0.0589 -0.0121 208 ARG A CD 1661 N NE . ARG A 208 ? 1.3664 1.2122 0.8266 0.0037 0.0612 -0.0102 208 ARG A NE 1662 C CZ . ARG A 208 ? 1.4009 1.2360 0.8307 0.0083 0.0493 -0.0258 208 ARG A CZ 1663 N NH1 . ARG A 208 ? 1.3904 1.2139 0.8339 -0.0001 0.0345 -0.0435 208 ARG A NH1 1664 N NH2 . ARG A 208 ? 1.4533 1.2882 0.8372 0.0225 0.0520 -0.0240 208 ARG A NH2 1665 N N . LEU A 209 ? 1.2258 1.1142 0.7830 -0.0617 0.0010 0.0032 209 LEU A N 1666 C CA . LEU A 209 ? 1.2049 1.1089 0.7729 -0.0600 0.0107 0.0190 209 LEU A CA 1667 C C . LEU A 209 ? 1.2292 1.1357 0.7669 -0.0412 0.0232 0.0314 209 LEU A C 1668 O O . LEU A 209 ? 1.2554 1.1573 0.7572 -0.0336 0.0143 0.0260 209 LEU A O 1669 C CB . LEU A 209 ? 1.1896 1.1072 0.7589 -0.0742 -0.0120 0.0186 209 LEU A CB 1670 C CG . LEU A 209 ? 1.1780 1.0917 0.7661 -0.0935 -0.0289 0.0068 209 LEU A CG 1671 C CD1 . LEU A 209 ? 1.1726 1.0981 0.7513 -0.1064 -0.0522 0.0054 209 LEU A CD1 1672 C CD2 . LEU A 209 ? 1.1452 1.0621 0.7728 -0.1000 -0.0158 0.0087 209 LEU A CD2 1673 N N . VAL A 210 ? 1.2257 1.1381 0.7771 -0.0331 0.0443 0.0478 210 VAL A N 1674 C CA . VAL A 210 ? 1.2598 1.1764 0.7818 -0.0147 0.0545 0.0639 210 VAL A CA 1675 C C . VAL A 210 ? 1.2421 1.1742 0.7788 -0.0153 0.0541 0.0780 210 VAL A C 1676 O O . VAL A 210 ? 1.1980 1.1329 0.7729 -0.0263 0.0596 0.0780 210 VAL A O 1677 C CB . VAL A 210 ? 1.2849 1.1884 0.8046 0.0007 0.0871 0.0738 210 VAL A CB 1678 C CG1 . VAL A 210 ? 1.3032 1.1939 0.8034 0.0044 0.0879 0.0599 210 VAL A CG1 1679 C CG2 . VAL A 210 ? 1.2628 1.1624 0.8304 -0.0053 0.1104 0.0784 210 VAL A CG2 1680 N N . PRO A 211 ? 1.2744 1.2178 0.7811 -0.0026 0.0470 0.0892 211 PRO A N 1681 C CA . PRO A 211 ? 1.2679 1.2271 0.7903 -0.0006 0.0469 0.1029 211 PRO A CA 1682 C C . PRO A 211 ? 1.2722 1.2220 0.8137 0.0110 0.0791 0.1215 211 PRO A C 1683 O O . PRO A 211 ? 1.3043 1.2419 0.8242 0.0276 0.0986 0.1331 211 PRO A O 1684 C CB . PRO A 211 ? 1.2961 1.2709 0.7785 0.0121 0.0289 0.1086 211 PRO A CB 1685 C CG . PRO A 211 ? 1.3166 1.2842 0.7644 0.0118 0.0152 0.0934 211 PRO A CG 1686 C CD . PRO A 211 ? 1.3123 1.2569 0.7703 0.0102 0.0358 0.0877 211 PRO A CD 1687 N N . ARG A 212 ? 1.2417 1.1956 0.8237 0.0013 0.0856 0.1232 212 ARG A N 1688 C CA . ARG A 212 ? 1.2517 1.1982 0.8555 0.0112 0.1134 0.1408 212 ARG A CA 1689 C C . ARG A 212 ? 1.2562 1.2165 0.8486 0.0258 0.1093 0.1586 212 ARG A C 1690 O O . ARG A 212 ? 1.2242 1.2039 0.8292 0.0181 0.0908 0.1544 212 ARG A O 1691 C CB . ARG A 212 ? 1.2303 1.1749 0.8840 -0.0060 0.1218 0.1315 212 ARG A CB 1692 C CG . ARG A 212 ? 1.2309 1.1610 0.9020 -0.0157 0.1331 0.1182 212 ARG A CG 1693 C CD . ARG A 212 ? 1.2045 1.1370 0.9219 -0.0337 0.1352 0.1057 212 ARG A CD 1694 N NE . ARG A 212 ? 1.1971 1.1409 0.9139 -0.0504 0.1066 0.0884 212 ARG A NE 1695 C CZ . ARG A 212 ? 1.2001 1.1593 0.9275 -0.0608 0.0908 0.0848 212 ARG A CZ 1696 N NH1 . ARG A 212 ? 1.2196 1.1866 0.9615 -0.0558 0.0994 0.0958 212 ARG A NH1 1697 N NH2 . ARG A 212 ? 1.1812 1.1474 0.9053 -0.0761 0.0670 0.0703 212 ARG A NH2 1698 N N . ILE A 213 ? 1.2938 1.2442 0.8624 0.0477 0.1273 0.1790 213 ILE A N 1699 C CA . ILE A 213 ? 1.3028 1.2639 0.8605 0.0657 0.1261 0.1990 213 ILE A CA 1700 C C . ILE A 213 ? 1.2840 1.2340 0.8812 0.0683 0.1521 0.2122 213 ILE A C 1701 O O . ILE A 213 ? 1.2760 1.2028 0.8900 0.0680 0.1808 0.2168 213 ILE A O 1702 C CB . ILE A 213 ? 1.3506 1.3063 0.8570 0.0904 0.1308 0.2164 213 ILE A CB 1703 C CG1 . ILE A 213 ? 1.3592 1.3305 0.8264 0.0883 0.1003 0.2013 213 ILE A CG1 1704 C CG2 . ILE A 213 ? 1.3739 1.3368 0.8721 0.1124 0.1344 0.2410 213 ILE A CG2 1705 C CD1 . ILE A 213 ? 1.4054 1.3659 0.8209 0.1074 0.1078 0.2100 213 ILE A CD1 1706 N N . ALA A 214 ? 1.2686 1.2358 0.8827 0.0703 0.1420 0.2168 214 ALA A N 1707 C CA . ALA A 214 ? 1.2698 1.2272 0.9191 0.0759 0.1649 0.2300 214 ALA A CA 1708 C C . ALA A 214 ? 1.2681 1.2491 0.9206 0.0864 0.1493 0.2386 214 ALA A C 1709 O O . ALA A 214 ? 1.2560 1.2645 0.8948 0.0821 0.1195 0.2289 214 ALA A O 1710 C CB . ALA A 214 ? 1.2347 1.1853 0.9318 0.0527 0.1745 0.2119 214 ALA A CB 1711 N N . THR A 215 ? 1.2827 1.2529 0.9556 0.1001 0.1701 0.2564 215 THR A N 1712 C CA . THR A 215 ? 1.2793 1.2714 0.9604 0.1127 0.1582 0.2656 215 THR A CA 1713 C C . THR A 215 ? 1.2302 1.2337 0.9594 0.0926 0.1557 0.2477 215 THR A C 1714 O O . THR A 215 ? 1.2187 1.2015 0.9818 0.0842 0.1791 0.2443 215 THR A O 1715 C CB . THR A 215 ? 1.3240 1.2968 1.0012 0.1408 0.1820 0.2957 215 THR A CB 1716 O OG1 . THR A 215 ? 1.3497 1.2980 0.9898 0.1541 0.1984 0.3116 215 THR A OG1 1717 C CG2 . THR A 215 ? 1.3383 1.3393 1.0031 0.1618 0.1616 0.3087 215 THR A CG2 1718 N N . ARG A 216 ? 1.2078 1.2449 0.9400 0.0845 0.1276 0.2354 216 ARG A N 1719 C CA . ARG A 216 ? 1.1655 1.2164 0.9371 0.0627 0.1226 0.2157 216 ARG A CA 1720 C C . ARG A 216 ? 1.1657 1.2463 0.9541 0.0714 0.1108 0.2196 216 ARG A C 1721 O O . ARG A 216 ? 1.1718 1.2739 0.9371 0.0873 0.0932 0.2296 216 ARG A O 1722 C CB . ARG A 216 ? 1.1333 1.1969 0.8956 0.0381 0.1001 0.1928 216 ARG A CB 1723 C CG . ARG A 216 ? 1.1410 1.1817 0.8787 0.0331 0.1050 0.1891 216 ARG A CG 1724 C CD . ARG A 216 ? 1.1216 1.1757 0.8445 0.0132 0.0790 0.1690 216 ARG A CD 1725 N NE . ARG A 216 ? 1.1545 1.2161 0.8340 0.0234 0.0612 0.1730 216 ARG A NE 1726 C CZ . ARG A 216 ? 1.1708 1.2138 0.8206 0.0273 0.0652 0.1734 216 ARG A CZ 1727 N NH1 . ARG A 216 ? 1.1658 1.1826 0.8265 0.0219 0.0866 0.1707 216 ARG A NH1 1728 N NH2 . ARG A 216 ? 1.1987 1.2511 0.8084 0.0368 0.0475 0.1751 216 ARG A NH2 1729 N N . SER A 217 ? 1.1453 1.2288 0.9747 0.0611 0.1203 0.2101 217 SER A N 1730 C CA . SER A 217 ? 1.1501 1.2644 1.0013 0.0661 0.1100 0.2096 217 SER A CA 1731 C C . SER A 217 ? 1.1388 1.2895 0.9766 0.0528 0.0779 0.1961 217 SER A C 1732 O O . SER A 217 ? 1.1257 1.2754 0.9561 0.0300 0.0681 0.1792 217 SER A O 1733 C CB . SER A 217 ? 1.1267 1.2372 1.0222 0.0524 0.1256 0.1962 217 SER A CB 1734 O OG . SER A 217 ? 1.1434 1.2161 1.0528 0.0576 0.1555 0.2031 217 SER A OG 1735 N N . LYS A 218 ? 1.1639 1.3463 0.9995 0.0673 0.0614 0.2035 218 LYS A N 1736 C CA . LYS A 218 ? 1.1533 1.3733 0.9836 0.0528 0.0318 0.1892 218 LYS A CA 1737 C C . LYS A 218 ? 1.1095 1.3404 0.9714 0.0254 0.0317 0.1684 218 LYS A C 1738 O O . LYS A 218 ? 1.1005 1.3304 0.9957 0.0261 0.0482 0.1672 218 LYS A O 1739 C CB . LYS A 218 ? 1.1803 1.4376 1.0132 0.0731 0.0157 0.1993 218 LYS A CB 1740 C CG . LYS A 218 ? 1.2266 1.4859 1.0178 0.0955 0.0027 0.2146 218 LYS A CG 1741 C CD . LYS A 218 ? 1.2528 1.5458 1.0507 0.1216 -0.0089 0.2282 218 LYS A CD 1742 C CE . LYS A 218 ? 1.2778 1.5496 1.0898 0.1490 0.0164 0.2508 218 LYS A CE 1743 N NZ . LYS A 218 ? 1.3174 1.5600 1.0889 0.1742 0.0257 0.2742 218 LYS A NZ 1744 N N . VAL A 219 ? 1.0860 1.3253 0.9358 0.0016 0.0140 0.1521 219 VAL A N 1745 C CA . VAL A 219 ? 1.0470 1.3029 0.9208 -0.0241 0.0092 0.1337 219 VAL A CA 1746 C C . VAL A 219 ? 1.0397 1.3302 0.9041 -0.0349 -0.0188 0.1256 219 VAL A C 1747 O O . VAL A 219 ? 1.0354 1.3205 0.8693 -0.0390 -0.0341 0.1233 219 VAL A O 1748 C CB . VAL A 219 ? 1.0376 1.2644 0.9075 -0.0460 0.0169 0.1209 219 VAL A CB 1749 C CG1 . VAL A 219 ? 1.0172 1.2620 0.8937 -0.0740 0.0025 0.1030 219 VAL A CG1 1750 C CG2 . VAL A 219 ? 1.0316 1.2345 0.9259 -0.0424 0.0444 0.1220 219 VAL A CG2 1751 N N . ASN A 220 ? 1.0338 1.3600 0.9261 -0.0401 -0.0248 0.1201 220 ASN A N 1752 C CA . ASN A 220 ? 1.0344 1.3980 0.9246 -0.0504 -0.0504 0.1123 220 ASN A CA 1753 C C . ASN A 220 ? 1.0457 1.4217 0.9121 -0.0279 -0.0665 0.1236 220 ASN A C 1754 O O . ASN A 220 ? 1.0600 1.4506 0.9077 -0.0369 -0.0890 0.1161 220 ASN A O 1755 C CB . ASN A 220 ? 1.0359 1.3899 0.9103 -0.0804 -0.0624 0.0967 220 ASN A CB 1756 C CG . ASN A 220 ? 1.0199 1.3853 0.9200 -0.1055 -0.0578 0.0835 220 ASN A CG 1757 O OD1 . ASN A 220 ? 1.0084 1.3680 0.9309 -0.1046 -0.0384 0.0833 220 ASN A OD1 1758 N ND2 . ASN A 220 ? 1.0214 1.4016 0.9169 -0.1288 -0.0752 0.0720 220 ASN A ND2 1759 N N . GLY A 221 ? 1.0491 1.4174 0.9146 0.0015 -0.0545 0.1415 221 GLY A N 1760 C CA . GLY A 221 ? 1.0735 1.4543 0.9144 0.0270 -0.0686 0.1548 221 GLY A CA 1761 C C . GLY A 221 ? 1.0916 1.4409 0.8863 0.0334 -0.0707 0.1604 221 GLY A C 1762 O O . GLY A 221 ? 1.1090 1.4691 0.8769 0.0531 -0.0845 0.1697 221 GLY A O 1763 N N . GLN A 222 ? 1.0781 1.3901 0.8629 0.0180 -0.0575 0.1544 222 GLN A N 1764 C CA . GLN A 222 ? 1.0988 1.3810 0.8421 0.0237 -0.0571 0.1585 222 GLN A CA 1765 C C . GLN A 222 ? 1.0979 1.3367 0.8420 0.0264 -0.0280 0.1657 222 GLN A C 1766 O O . GLN A 222 ? 1.0806 1.3086 0.8522 0.0102 -0.0144 0.1573 222 GLN A O 1767 C CB . GLN A 222 ? 1.0919 1.3757 0.8173 -0.0011 -0.0772 0.1392 222 GLN A CB 1768 C CG . GLN A 222 ? 1.0992 1.4251 0.8240 -0.0064 -0.1067 0.1298 222 GLN A CG 1769 C CD . GLN A 222 ? 1.1348 1.4764 0.8309 0.0207 -0.1201 0.1414 222 GLN A CD 1770 O OE1 . GLN A 222 ? 1.1570 1.4725 0.8232 0.0407 -0.1090 0.1552 222 GLN A OE1 1771 N NE2 . GLN A 222 ? 1.1399 1.5254 0.8450 0.0216 -0.1440 0.1357 222 GLN A NE2 1772 N N . SER A 223 ? 1.1342 1.3495 0.8481 0.0469 -0.0183 0.1809 223 SER A N 1773 C CA . SER A 223 ? 1.1384 1.3125 0.8523 0.0494 0.0100 0.1878 223 SER A CA 1774 C C . SER A 223 ? 1.1370 1.2890 0.8254 0.0346 0.0074 0.1762 223 SER A C 1775 O O . SER A 223 ? 1.1214 1.2426 0.8146 0.0307 0.0286 0.1764 223 SER A O 1776 C CB . SER A 223 ? 1.1817 1.3402 0.8807 0.0808 0.0274 0.2136 223 SER A CB 1777 O OG . SER A 223 ? 1.1866 1.3510 0.9190 0.0925 0.0404 0.2241 223 SER A OG 1778 N N . GLY A 224 ? 1.1531 1.3214 0.8169 0.0267 -0.0184 0.1649 224 GLY A N 1779 C CA . GLY A 224 ? 1.1635 1.3123 0.8042 0.0124 -0.0235 0.1516 224 GLY A CA 1780 C C . GLY A 224 ? 1.1338 1.2782 0.8004 -0.0162 -0.0251 0.1333 224 GLY A C 1781 O O . GLY A 224 ? 1.1276 1.2924 0.8233 -0.0277 -0.0301 0.1276 224 GLY A O 1782 N N . ARG A 225 ? 1.1369 1.2555 0.7924 -0.0267 -0.0206 0.1241 225 ARG A N 1783 C CA . ARG A 225 ? 1.1051 1.2155 0.7826 -0.0516 -0.0206 0.1084 225 ARG A CA 1784 C C . ARG A 225 ? 1.1084 1.2104 0.7639 -0.0667 -0.0385 0.0930 225 ARG A C 1785 O O . ARG A 225 ? 1.1342 1.2251 0.7585 -0.0573 -0.0421 0.0935 225 ARG A O 1786 C CB . ARG A 225 ? 1.0896 1.1740 0.7863 -0.0505 0.0062 0.1114 225 ARG A CB 1787 C CG . ARG A 225 ? 1.0877 1.1754 0.8129 -0.0397 0.0260 0.1236 225 ARG A CG 1788 C CD . ARG A 225 ? 1.0631 1.1688 0.8209 -0.0558 0.0221 0.1142 225 ARG A CD 1789 N NE . ARG A 225 ? 1.0645 1.1713 0.8502 -0.0444 0.0420 0.1243 225 ARG A NE 1790 C CZ . ARG A 225 ? 1.0777 1.2021 0.8666 -0.0272 0.0416 0.1373 225 ARG A CZ 1791 N NH1 . ARG A 225 ? 1.0873 1.2333 0.8534 -0.0193 0.0210 0.1415 225 ARG A NH1 1792 N NH2 . ARG A 225 ? 1.0820 1.2026 0.8983 -0.0171 0.0615 0.1454 225 ARG A NH2 1793 N N . MET A 226 ? 1.0971 1.2033 0.7685 -0.0898 -0.0487 0.0795 226 MET A N 1794 C CA . MET A 226 ? 1.1000 1.1943 0.7551 -0.1059 -0.0645 0.0650 226 MET A CA 1795 C C . MET A 226 ? 1.0709 1.1463 0.7443 -0.1204 -0.0553 0.0574 226 MET A C 1796 O O . MET A 226 ? 1.0645 1.1497 0.7630 -0.1325 -0.0530 0.0550 226 MET A O 1797 C CB . MET A 226 ? 1.1081 1.2255 0.7627 -0.1214 -0.0884 0.0564 226 MET A CB 1798 C CG . MET A 226 ? 1.1406 1.2790 0.7749 -0.1095 -0.1035 0.0593 226 MET A CG 1799 S SD . MET A 226 ? 1.1873 1.3069 0.7785 -0.1052 -0.1172 0.0502 226 MET A SD 1800 C CE . MET A 226 ? 1.2173 1.3737 0.7953 -0.0986 -0.1406 0.0492 226 MET A CE 1801 N N . GLU A 227 ? 1.0619 1.1120 0.7226 -0.1184 -0.0504 0.0529 227 GLU A N 1802 C CA . GLU A 227 ? 1.0303 1.0634 0.7068 -0.1305 -0.0444 0.0446 227 GLU A CA 1803 C C . GLU A 227 ? 1.0186 1.0414 0.6792 -0.1457 -0.0645 0.0320 227 GLU A C 1804 O O . GLU A 227 ? 1.0304 1.0425 0.6652 -0.1401 -0.0727 0.0284 227 GLU A O 1805 C CB . GLU A 227 ? 1.0434 1.0564 0.7221 -0.1173 -0.0237 0.0480 227 GLU A CB 1806 C CG . GLU A 227 ? 1.0330 1.0339 0.7357 -0.1271 -0.0148 0.0400 227 GLU A CG 1807 C CD . GLU A 227 ? 1.0462 1.0319 0.7582 -0.1143 0.0082 0.0436 227 GLU A CD 1808 O OE1 . GLU A 227 ? 1.0666 1.0473 0.7607 -0.0981 0.0171 0.0526 227 GLU A OE1 1809 O OE2 . GLU A 227 ? 1.0464 1.0262 0.7839 -0.1206 0.0179 0.0373 227 GLU A OE2 1810 N N . PHE A 228 ? 0.9848 1.0096 0.6592 -0.1642 -0.0719 0.0255 228 PHE A N 1811 C CA . PHE A 228 ? 0.9775 0.9915 0.6375 -0.1798 -0.0912 0.0157 228 PHE A CA 1812 C C . PHE A 228 ? 0.9658 0.9570 0.6304 -0.1851 -0.0889 0.0090 228 PHE A C 1813 O O . PHE A 228 ? 0.9461 0.9388 0.6321 -0.1872 -0.0776 0.0095 228 PHE A O 1814 C CB . PHE A 228 ? 0.9670 1.0000 0.6352 -0.1975 -0.1029 0.0146 228 PHE A CB 1815 C CG . PHE A 228 ? 0.9691 1.0268 0.6328 -0.1936 -0.1103 0.0185 228 PHE A CG 1816 C CD1 . PHE A 228 ? 0.9921 1.0491 0.6343 -0.1971 -0.1281 0.0126 228 PHE A CD1 1817 C CD2 . PHE A 228 ? 0.9615 1.0436 0.6436 -0.1853 -0.0998 0.0272 228 PHE A CD2 1818 C CE1 . PHE A 228 ? 1.0000 1.0834 0.6395 -0.1930 -0.1368 0.0147 228 PHE A CE1 1819 C CE2 . PHE A 228 ? 0.9680 1.0756 0.6474 -0.1797 -0.1081 0.0309 228 PHE A CE2 1820 C CZ . PHE A 228 ? 0.9863 1.0961 0.6445 -0.1836 -0.1272 0.0244 228 PHE A CZ 1821 N N . PHE A 229 ? 0.9815 0.9522 0.6263 -0.1866 -0.1002 0.0016 229 PHE A N 1822 C CA . PHE A 229 ? 0.9805 0.9290 0.6278 -0.1894 -0.1009 -0.0050 229 PHE A CA 1823 C C . PHE A 229 ? 0.9938 0.9284 0.6280 -0.2055 -0.1206 -0.0113 229 PHE A C 1824 O O . PHE A 229 ? 1.0090 0.9475 0.6291 -0.2132 -0.1334 -0.0125 229 PHE A O 1825 C CB . PHE A 229 ? 0.9912 0.9235 0.6285 -0.1728 -0.0931 -0.0079 229 PHE A CB 1826 C CG . PHE A 229 ? 0.9908 0.9316 0.6420 -0.1576 -0.0709 -0.0008 229 PHE A CG 1827 C CD1 . PHE A 229 ? 0.9971 0.9509 0.6389 -0.1466 -0.0645 0.0077 229 PHE A CD1 1828 C CD2 . PHE A 229 ? 0.9862 0.9222 0.6608 -0.1542 -0.0563 -0.0024 229 PHE A CD2 1829 C CE1 . PHE A 229 ? 0.9981 0.9562 0.6518 -0.1324 -0.0424 0.0165 229 PHE A CE1 1830 C CE2 . PHE A 229 ? 0.9802 0.9219 0.6700 -0.1418 -0.0340 0.0042 229 PHE A CE2 1831 C CZ . PHE A 229 ? 0.9892 0.9401 0.6677 -0.1307 -0.0262 0.0147 229 PHE A CZ 1832 N N . TRP A 230 ? 0.9892 0.9073 0.6285 -0.2103 -0.1232 -0.0153 230 TRP A N 1833 C CA . TRP A 230 ? 1.0022 0.9022 0.6284 -0.2245 -0.1405 -0.0193 230 TRP A CA 1834 C C . TRP A 230 ? 1.0062 0.8805 0.6301 -0.2189 -0.1436 -0.0251 230 TRP A C 1835 O O . TRP A 230 ? 0.9971 0.8723 0.6350 -0.2068 -0.1319 -0.0266 230 TRP A O 1836 C CB . TRP A 230 ? 0.9930 0.9051 0.6286 -0.2418 -0.1435 -0.0147 230 TRP A CB 1837 C CG . TRP A 230 ? 0.9762 0.8959 0.6313 -0.2402 -0.1330 -0.0133 230 TRP A CG 1838 C CD1 . TRP A 230 ? 0.9639 0.9063 0.6390 -0.2353 -0.1178 -0.0103 230 TRP A CD1 1839 C CD2 . TRP A 230 ? 0.9807 0.8856 0.6374 -0.2434 -0.1378 -0.0159 230 TRP A CD2 1840 N NE1 . TRP A 230 ? 0.9553 0.8984 0.6452 -0.2364 -0.1126 -0.0127 230 TRP A NE1 1841 C CE2 . TRP A 230 ? 0.9691 0.8910 0.6474 -0.2410 -0.1255 -0.0160 230 TRP A CE2 1842 C CE3 . TRP A 230 ? 1.0065 0.8849 0.6484 -0.2473 -0.1517 -0.0183 230 TRP A CE3 1843 C CZ2 . TRP A 230 ? 0.9747 0.8911 0.6595 -0.2426 -0.1281 -0.0194 230 TRP A CZ2 1844 C CZ3 . TRP A 230 ? 1.0094 0.8814 0.6573 -0.2473 -0.1542 -0.0196 230 TRP A CZ3 1845 C CH2 . TRP A 230 ? 0.9903 0.8827 0.6591 -0.2451 -0.1431 -0.0206 230 TRP A CH2 1846 N N . THR A 231 ? 1.0232 0.8743 0.6311 -0.2276 -0.1592 -0.0287 231 THR A N 1847 C CA . THR A 231 ? 1.0330 0.8596 0.6400 -0.2238 -0.1649 -0.0328 231 THR A CA 1848 C C . THR A 231 ? 1.0629 0.8687 0.6559 -0.2400 -0.1813 -0.0311 231 THR A C 1849 O O . THR A 231 ? 1.0839 0.8924 0.6675 -0.2542 -0.1878 -0.0288 231 THR A O 1850 C CB . THR A 231 ? 1.0403 0.8493 0.6390 -0.2074 -0.1636 -0.0412 231 THR A CB 1851 O OG1 . THR A 231 ? 1.0346 0.8256 0.6396 -0.2005 -0.1667 -0.0451 231 THR A OG1 1852 C CG2 . THR A 231 ? 1.0673 0.8589 0.6420 -0.2121 -0.1759 -0.0464 231 THR A CG2 1853 N N . ILE A 232 ? 1.0762 0.8622 0.6692 -0.2379 -0.1876 -0.0316 232 ILE A N 1854 C CA . ILE A 232 ? 1.1065 0.8639 0.6827 -0.2497 -0.2028 -0.0293 232 ILE A CA 1855 C C . ILE A 232 ? 1.1348 0.8619 0.6999 -0.2383 -0.2096 -0.0380 232 ILE A C 1856 O O . ILE A 232 ? 1.1288 0.8493 0.7020 -0.2221 -0.2071 -0.0428 232 ILE A O 1857 C CB . ILE A 232 ? 1.1063 0.8591 0.6854 -0.2540 -0.2072 -0.0226 232 ILE A CB 1858 C CG1 . ILE A 232 ? 1.0930 0.8633 0.6710 -0.2729 -0.2057 -0.0136 232 ILE A CG1 1859 C CG2 . ILE A 232 ? 1.1474 0.8612 0.7097 -0.2550 -0.2220 -0.0213 232 ILE A CG2 1860 C CD1 . ILE A 232 ? 1.0672 0.8731 0.6593 -0.2748 -0.1927 -0.0137 232 ILE A CD1 1861 N N . LEU A 233 ? 1.1784 0.8889 0.7269 -0.2469 -0.2179 -0.0415 233 LEU A N 1862 C CA . LEU A 233 ? 1.2168 0.8951 0.7527 -0.2379 -0.2253 -0.0513 233 LEU A CA 1863 C C . LEU A 233 ? 1.2482 0.8914 0.7750 -0.2452 -0.2381 -0.0469 233 LEU A C 1864 O O . LEU A 233 ? 1.2531 0.8881 0.7716 -0.2645 -0.2448 -0.0398 233 LEU A O 1865 C CB . LEU A 233 ? 1.2347 0.9114 0.7568 -0.2440 -0.2289 -0.0595 233 LEU A CB 1866 C CG . LEU A 233 ? 1.2685 0.9161 0.7765 -0.2328 -0.2343 -0.0733 233 LEU A CG 1867 C CD1 . LEU A 233 ? 1.2563 0.9115 0.7716 -0.2086 -0.2225 -0.0793 233 LEU A CD1 1868 C CD2 . LEU A 233 ? 1.2864 0.9369 0.7803 -0.2420 -0.2398 -0.0821 233 LEU A CD2 1869 N N . LYS A 234 ? 1.2798 0.9027 0.8091 -0.2292 -0.2409 -0.0503 234 LYS A N 1870 C CA . LYS A 234 ? 1.3446 0.9321 0.8646 -0.2321 -0.2535 -0.0444 234 LYS A CA 1871 C C . LYS A 234 ? 1.3903 0.9400 0.8921 -0.2400 -0.2632 -0.0503 234 LYS A C 1872 O O . LYS A 234 ? 1.3951 0.9472 0.8925 -0.2385 -0.2608 -0.0621 234 LYS A O 1873 C CB . LYS A 234 ? 1.3765 0.9564 0.9077 -0.2102 -0.2544 -0.0474 234 LYS A CB 1874 C CG . LYS A 234 ? 1.3584 0.9772 0.9122 -0.2012 -0.2435 -0.0463 234 LYS A CG 1875 C CD . LYS A 234 ? 1.3755 0.9921 0.9362 -0.1958 -0.2509 -0.0392 234 LYS A CD 1876 C CE . LYS A 234 ? 1.4021 1.0213 0.9509 -0.2154 -0.2558 -0.0251 234 LYS A CE 1877 N NZ . LYS A 234 ? 1.4275 1.0435 0.9772 -0.2098 -0.2648 -0.0177 234 LYS A NZ 1878 N N . PRO A 235 ? 1.4433 0.9571 0.9334 -0.2488 -0.2742 -0.0421 235 PRO A N 1879 C CA . PRO A 235 ? 1.4840 0.9571 0.9589 -0.2562 -0.2829 -0.0490 235 PRO A CA 1880 C C . PRO A 235 ? 1.5087 0.9608 0.9835 -0.2340 -0.2842 -0.0645 235 PRO A C 1881 O O . PRO A 235 ? 1.4945 0.9506 0.9800 -0.2136 -0.2821 -0.0650 235 PRO A O 1882 C CB . PRO A 235 ? 1.5148 0.9530 0.9787 -0.2669 -0.2921 -0.0338 235 PRO A CB 1883 C CG . PRO A 235 ? 1.4942 0.9491 0.9662 -0.2546 -0.2909 -0.0230 235 PRO A CG 1884 C CD . PRO A 235 ? 1.4426 0.9501 0.9308 -0.2528 -0.2789 -0.0261 235 PRO A CD 1885 N N . ASN A 236 ? 1.5467 0.9796 1.0111 -0.2382 -0.2873 -0.0784 236 ASN A N 1886 C CA . ASN A 236 ? 1.5874 1.0014 1.0493 -0.2179 -0.2871 -0.0958 236 ASN A CA 1887 C C . ASN A 236 ? 1.5646 1.0147 1.0378 -0.1976 -0.2744 -0.1040 236 ASN A C 1888 O O . ASN A 236 ? 1.5957 1.0331 1.0691 -0.1781 -0.2718 -0.1171 236 ASN A O 1889 C CB . ASN A 236 ? 1.6339 1.0040 1.0946 -0.2051 -0.2954 -0.0935 236 ASN A CB 1890 C CG . ASN A 236 ? 1.7214 1.0404 1.1665 -0.2162 -0.3058 -0.0992 236 ASN A CG 1891 O OD1 . ASN A 236 ? 1.7444 1.0615 1.1807 -0.2324 -0.3069 -0.1090 236 ASN A OD1 1892 N ND2 . ASN A 236 ? 1.7752 1.0519 1.2179 -0.2071 -0.3138 -0.0937 236 ASN A ND2 1893 N N . ASP A 237 ? 1.5199 1.0136 1.0029 -0.2020 -0.2652 -0.0963 237 ASP A N 1894 C CA . ASP A 237 ? 1.4954 1.0227 0.9872 -0.1860 -0.2512 -0.1031 237 ASP A CA 1895 C C . ASP A 237 ? 1.4803 1.0256 0.9599 -0.1954 -0.2486 -0.1099 237 ASP A C 1896 O O . ASP A 237 ? 1.4796 1.0238 0.9517 -0.2162 -0.2564 -0.1064 237 ASP A O 1897 C CB . ASP A 237 ? 1.4624 1.0251 0.9749 -0.1827 -0.2417 -0.0909 237 ASP A CB 1898 C CG . ASP A 237 ? 1.4427 1.0321 0.9691 -0.1627 -0.2256 -0.0974 237 ASP A CG 1899 O OD1 . ASP A 237 ? 1.4539 1.0314 0.9744 -0.1480 -0.2218 -0.1105 237 ASP A OD1 1900 O OD2 . ASP A 237 ? 1.4101 1.0318 0.9536 -0.1622 -0.2155 -0.0895 237 ASP A OD2 1901 N N . ALA A 238 ? 1.4595 1.0221 0.9371 -0.1796 -0.2377 -0.1195 238 ALA A N 1902 C CA . ALA A 238 ? 1.4482 1.0310 0.9122 -0.1840 -0.2355 -0.1258 238 ALA A CA 1903 C C . ALA A 238 ? 1.3928 1.0173 0.8679 -0.1754 -0.2194 -0.1176 238 ALA A C 1904 O O . ALA A 238 ? 1.3686 1.0012 0.8585 -0.1600 -0.2074 -0.1150 238 ALA A O 1905 C CB . ALA A 238 ? 1.4798 1.0421 0.9243 -0.1722 -0.2370 -0.1452 238 ALA A CB 1906 N N . ILE A 239 ? 1.3681 1.0189 0.8382 -0.1855 -0.2193 -0.1137 239 ILE A N 1907 C CA . ILE A 239 ? 1.3278 1.0155 0.8048 -0.1761 -0.2039 -0.1063 239 ILE A CA 1908 C C . ILE A 239 ? 1.3487 1.0439 0.8031 -0.1648 -0.2006 -0.1168 239 ILE A C 1909 O O . ILE A 239 ? 1.3771 1.0623 0.8126 -0.1728 -0.2137 -0.1276 239 ILE A O 1910 C CB . ILE A 239 ? 1.2847 1.0004 0.7743 -0.1920 -0.2043 -0.0925 239 ILE A CB 1911 C CG1 . ILE A 239 ? 1.2542 1.0030 0.7553 -0.1802 -0.1865 -0.0835 239 ILE A CG1 1912 C CG2 . ILE A 239 ? 1.3009 1.0222 0.7775 -0.2085 -0.2176 -0.0963 239 ILE A CG2 1913 C CD1 . ILE A 239 ? 1.2221 0.9964 0.7411 -0.1927 -0.1840 -0.0701 239 ILE A CD1 1914 N N . ASN A 240 ? 1.3376 1.0498 0.7934 -0.1465 -0.1828 -0.1140 240 ASN A N 1915 C CA . ASN A 240 ? 1.3677 1.0860 0.7984 -0.1324 -0.1772 -0.1226 240 ASN A CA 1916 C C . ASN A 240 ? 1.3514 1.1038 0.7823 -0.1250 -0.1634 -0.1100 240 ASN A C 1917 O O . ASN A 240 ? 1.3277 1.0912 0.7756 -0.1145 -0.1449 -0.1002 240 ASN A O 1918 C CB . ASN A 240 ? 1.3862 1.0864 0.8126 -0.1130 -0.1657 -0.1325 240 ASN A CB 1919 C CG . ASN A 240 ? 1.4222 1.0858 0.8435 -0.1161 -0.1793 -0.1472 240 ASN A CG 1920 O OD1 . ASN A 240 ? 1.4405 1.0894 0.8432 -0.1264 -0.1956 -0.1580 240 ASN A OD1 1921 N ND2 . ASN A 240 ? 1.4235 1.0721 0.8629 -0.1069 -0.1729 -0.1483 240 ASN A ND2 1922 N N . PHE A 241 ? 1.3609 1.1296 0.7740 -0.1300 -0.1727 -0.1107 241 PHE A N 1923 C CA . PHE A 241 ? 1.3508 1.1504 0.7600 -0.1207 -0.1615 -0.0985 241 PHE A CA 1924 C C . PHE A 241 ? 1.3846 1.1851 0.7614 -0.1012 -0.1542 -0.1053 241 PHE A C 1925 O O . PHE A 241 ? 1.4341 1.2187 0.7863 -0.1003 -0.1658 -0.1224 241 PHE A O 1926 C CB . PHE A 241 ? 1.3410 1.1630 0.7521 -0.1361 -0.1762 -0.0939 241 PHE A CB 1927 C CG . PHE A 241 ? 1.3125 1.1405 0.7547 -0.1532 -0.1782 -0.0836 241 PHE A CG 1928 C CD1 . PHE A 241 ? 1.2882 1.1327 0.7532 -0.1484 -0.1614 -0.0682 241 PHE A CD1 1929 C CD2 . PHE A 241 ? 1.3221 1.1379 0.7700 -0.1742 -0.1957 -0.0897 241 PHE A CD2 1930 C CE1 . PHE A 241 ? 1.2650 1.1156 0.7562 -0.1635 -0.1630 -0.0603 241 PHE A CE1 1931 C CE2 . PHE A 241 ? 1.2979 1.1194 0.7709 -0.1895 -0.1962 -0.0796 241 PHE A CE2 1932 C CZ . PHE A 241 ? 1.2686 1.1084 0.7623 -0.1838 -0.1803 -0.0656 241 PHE A CZ 1933 N N . GLU A 242 ? 1.3727 1.1904 0.7489 -0.0854 -0.1341 -0.0920 242 GLU A N 1934 C CA . GLU A 242 ? 1.4081 1.2319 0.7495 -0.0663 -0.1260 -0.0939 242 GLU A CA 1935 C C . GLU A 242 ? 1.3922 1.2421 0.7360 -0.0561 -0.1106 -0.0730 242 GLU A C 1936 O O . GLU A 242 ? 1.3709 1.2238 0.7418 -0.0532 -0.0914 -0.0595 242 GLU A O 1937 C CB . GLU A 242 ? 1.4382 1.2410 0.7703 -0.0509 -0.1098 -0.1028 242 GLU A CB 1938 C CG . GLU A 242 ? 1.4818 1.2906 0.7755 -0.0296 -0.0970 -0.1031 242 GLU A CG 1939 C CD . GLU A 242 ? 1.4989 1.2896 0.7870 -0.0143 -0.0772 -0.1110 242 GLU A CD 1940 O OE1 . GLU A 242 ? 1.5078 1.2766 0.8082 -0.0194 -0.0830 -0.1257 242 GLU A OE1 1941 O OE2 . GLU A 242 ? 1.5084 1.3065 0.7796 0.0035 -0.0550 -0.1022 242 GLU A OE2 1942 N N . SER A 243 ? 1.4030 1.2715 0.7195 -0.0502 -0.1194 -0.0708 243 SER A N 1943 C CA . SER A 243 ? 1.3967 1.2883 0.7126 -0.0381 -0.1058 -0.0499 243 SER A CA 1944 C C . SER A 243 ? 1.4352 1.3407 0.7073 -0.0220 -0.1112 -0.0498 243 SER A C 1945 O O . SER A 243 ? 1.4773 1.3832 0.7248 -0.0262 -0.1331 -0.0671 243 SER A O 1946 C CB . SER A 243 ? 1.3591 1.2703 0.7064 -0.0532 -0.1148 -0.0395 243 SER A CB 1947 O OG . SER A 243 ? 1.3474 1.2786 0.6970 -0.0404 -0.1009 -0.0190 243 SER A OG 1948 N N . ASN A 244 ? 1.4349 1.3513 0.6973 -0.0035 -0.0912 -0.0301 244 ASN A N 1949 C CA . ASN A 244 ? 1.4727 1.4048 0.6915 0.0152 -0.0945 -0.0249 244 ASN A CA 1950 C C . ASN A 244 ? 1.4563 1.4155 0.6844 0.0200 -0.0958 -0.0038 244 ASN A C 1951 O O . ASN A 244 ? 1.4854 1.4555 0.6837 0.0406 -0.0883 0.0101 244 ASN A O 1952 C CB . ASN A 244 ? 1.4966 1.4149 0.6872 0.0373 -0.0671 -0.0181 244 ASN A CB 1953 C CG . ASN A 244 ? 1.4695 1.3835 0.6893 0.0434 -0.0357 0.0044 244 ASN A CG 1954 O OD1 . ASN A 244 ? 1.4222 1.3372 0.6867 0.0290 -0.0338 0.0093 244 ASN A OD1 1955 N ND2 . ASN A 244 ? 1.4969 1.4059 0.6915 0.0643 -0.0103 0.0178 244 ASN A ND2 1956 N N . GLY A 245 ? 1.4208 1.3901 0.6893 0.0018 -0.1050 -0.0014 245 GLY A N 1957 C CA . GLY A 245 ? 1.4059 1.4011 0.6907 0.0048 -0.1064 0.0167 245 GLY A CA 1958 C C . GLY A 245 ? 1.3566 1.3517 0.6923 -0.0109 -0.0982 0.0240 245 GLY A C 1959 O O . GLY A 245 ? 1.3309 1.3051 0.6880 -0.0186 -0.0841 0.0210 245 GLY A O 1960 N N . ASN A 246 ? 1.3395 1.3601 0.6943 -0.0150 -0.1077 0.0326 246 ASN A N 1961 C CA . ASN A 246 ? 1.2947 1.3199 0.6954 -0.0279 -0.0997 0.0406 246 ASN A CA 1962 C C . ASN A 246 ? 1.2666 1.2822 0.6924 -0.0542 -0.1111 0.0243 246 ASN A C 1963 O O . ASN A 246 ? 1.2336 1.2465 0.6940 -0.0648 -0.1015 0.0286 246 ASN A O 1964 C CB . ASN A 246 ? 1.2855 1.2959 0.7017 -0.0163 -0.0675 0.0576 246 ASN A CB 1965 C CG . ASN A 246 ? 1.3191 1.3351 0.7108 0.0099 -0.0530 0.0774 246 ASN A CG 1966 O OD1 . ASN A 246 ? 1.3507 1.3566 0.7050 0.0250 -0.0476 0.0777 246 ASN A OD1 1967 N ND2 . ASN A 246 ? 1.3066 1.3374 0.7186 0.0164 -0.0455 0.0946 246 ASN A ND2 1968 N N . PHE A 247 ? 1.2858 1.2958 0.6933 -0.0644 -0.1319 0.0056 247 PHE A N 1969 C CA . PHE A 247 ? 1.2511 1.2463 0.6771 -0.0879 -0.1424 -0.0089 247 PHE A CA 1970 C C . PHE A 247 ? 1.2308 1.2482 0.6748 -0.1072 -0.1630 -0.0135 247 PHE A C 1971 O O . PHE A 247 ? 1.2553 1.2918 0.6839 -0.1074 -0.1815 -0.0200 247 PHE A O 1972 C CB . PHE A 247 ? 1.2815 1.2529 0.6797 -0.0885 -0.1512 -0.0270 247 PHE A CB 1973 C CG . PHE A 247 ? 1.2644 1.2156 0.6780 -0.1104 -0.1621 -0.0409 247 PHE A CG 1974 C CD1 . PHE A 247 ? 1.2284 1.1691 0.6730 -0.1199 -0.1514 -0.0355 247 PHE A CD1 1975 C CD2 . PHE A 247 ? 1.2853 1.2265 0.6808 -0.1206 -0.1829 -0.0597 247 PHE A CD2 1976 C CE1 . PHE A 247 ? 1.2202 1.1411 0.6754 -0.1380 -0.1616 -0.0463 247 PHE A CE1 1977 C CE2 . PHE A 247 ? 1.2785 1.1973 0.6868 -0.1396 -0.1918 -0.0706 247 PHE A CE2 1978 C CZ . PHE A 247 ? 1.2474 1.1560 0.6844 -0.1476 -0.1812 -0.0627 247 PHE A CZ 1979 N N . ILE A 248 ? 1.2029 1.2194 0.6801 -0.1233 -0.1590 -0.0105 248 ILE A N 1980 C CA . ILE A 248 ? 1.1861 1.2199 0.6831 -0.1449 -0.1754 -0.0154 248 ILE A CA 1981 C C . ILE A 248 ? 1.1849 1.1916 0.6817 -0.1641 -0.1850 -0.0296 248 ILE A C 1982 O O . ILE A 248 ? 1.1531 1.1399 0.6637 -0.1693 -0.1745 -0.0275 248 ILE A O 1983 C CB . ILE A 248 ? 1.1496 1.1999 0.6812 -0.1496 -0.1633 -0.0024 248 ILE A CB 1984 C CG1 . ILE A 248 ? 1.1535 1.2192 0.6862 -0.1266 -0.1471 0.0139 248 ILE A CG1 1985 C CG2 . ILE A 248 ? 1.1421 1.2175 0.6924 -0.1691 -0.1790 -0.0063 248 ILE A CG2 1986 C CD1 . ILE A 248 ? 1.1899 1.2765 0.6981 -0.1108 -0.1579 0.0158 248 ILE A CD1 1987 N N . ALA A 249 ? 1.2126 1.2177 0.6935 -0.1740 -0.2053 -0.0443 249 ALA A N 1988 C CA . ALA A 249 ? 1.2336 1.2068 0.7085 -0.1886 -0.2142 -0.0583 249 ALA A CA 1989 C C . ALA A 249 ? 1.2246 1.1976 0.7232 -0.2152 -0.2228 -0.0599 249 ALA A C 1990 O O . ALA A 249 ? 1.2086 1.2114 0.7238 -0.2251 -0.2285 -0.0563 249 ALA A O 1991 C CB . ALA A 249 ? 1.2758 1.2422 0.7209 -0.1864 -0.2306 -0.0753 249 ALA A CB 1992 N N . PRO A 250 ? 1.2348 1.1747 0.7349 -0.2260 -0.2231 -0.0646 250 PRO A N 1993 C CA . PRO A 250 ? 1.2359 1.1708 0.7519 -0.2518 -0.2322 -0.0664 250 PRO A CA 1994 C C . PRO A 250 ? 1.2732 1.2129 0.7820 -0.2673 -0.2521 -0.0804 250 PRO A C 1995 O O . PRO A 250 ? 1.3108 1.2369 0.7970 -0.2608 -0.2611 -0.0939 250 PRO A O 1996 C CB . PRO A 250 ? 1.2326 1.1267 0.7450 -0.2545 -0.2291 -0.0685 250 PRO A CB 1997 C CG . PRO A 250 ? 1.2432 1.1202 0.7352 -0.2327 -0.2235 -0.0742 250 PRO A CG 1998 C CD . PRO A 250 ? 1.2363 1.1434 0.7259 -0.2142 -0.2135 -0.0667 250 PRO A CD 1999 N N . GLU A 251 ? 1.2776 1.2382 0.8069 -0.2877 -0.2582 -0.0784 251 GLU A N 2000 C CA . GLU A 251 ? 1.3107 1.2734 0.8407 -0.3086 -0.2764 -0.0923 251 GLU A CA 2001 C C . GLU A 251 ? 1.3088 1.2395 0.8469 -0.3313 -0.2767 -0.0912 251 GLU A C 2002 O O . GLU A 251 ? 1.3219 1.2163 0.8463 -0.3387 -0.2850 -0.1023 251 GLU A O 2003 C CB . GLU A 251 ? 1.3054 1.3171 0.8560 -0.3159 -0.2819 -0.0904 251 GLU A CB 2004 C CG . GLU A 251 ? 1.3403 1.3731 0.8819 -0.3162 -0.3005 -0.1066 251 GLU A CG 2005 C CD . GLU A 251 ? 1.3653 1.3987 0.9208 -0.3463 -0.3157 -0.1201 251 GLU A CD 2006 O OE1 . GLU A 251 ? 1.3889 1.3845 0.9308 -0.3570 -0.3234 -0.1329 251 GLU A OE1 2007 O OE2 . GLU A 251 ? 1.3562 1.4286 0.9377 -0.3588 -0.3196 -0.1185 251 GLU A OE2 2008 N N . TYR A 252 ? 1.2793 1.2225 0.8383 -0.3407 -0.2666 -0.0773 252 TYR A N 2009 C CA . TYR A 252 ? 1.2878 1.2043 0.8531 -0.3607 -0.2646 -0.0720 252 TYR A CA 2010 C C . TYR A 252 ? 1.2675 1.1675 0.8313 -0.3480 -0.2502 -0.0596 252 TYR A C 2011 O O . TYR A 252 ? 1.2406 1.1628 0.8110 -0.3314 -0.2389 -0.0520 252 TYR A O 2012 C CB . TYR A 252 ? 1.2851 1.2312 0.8748 -0.3831 -0.2637 -0.0664 252 TYR A CB 2013 C CG . TYR A 252 ? 1.3192 1.2905 0.9184 -0.3975 -0.2776 -0.0790 252 TYR A CG 2014 C CD1 . TYR A 252 ? 1.3601 1.3074 0.9573 -0.4203 -0.2891 -0.0900 252 TYR A CD1 2015 C CD2 . TYR A 252 ? 1.3045 1.3240 0.9162 -0.3881 -0.2795 -0.0801 252 TYR A CD2 2016 C CE1 . TYR A 252 ? 1.3767 1.3494 0.9860 -0.4350 -0.3026 -0.1038 252 TYR A CE1 2017 C CE2 . TYR A 252 ? 1.3212 1.3680 0.9438 -0.4008 -0.2941 -0.0929 252 TYR A CE2 2018 C CZ . TYR A 252 ? 1.3566 1.3810 0.9790 -0.4251 -0.3057 -0.1057 252 TYR A CZ 2019 O OH . TYR A 252 ? 1.3636 1.4169 1.0001 -0.4392 -0.3209 -0.1208 252 TYR A OH 2020 N N . ALA A 253 ? 1.2805 1.1411 0.8363 -0.3558 -0.2512 -0.0580 253 ALA A N 2021 C CA . ALA A 253 ? 1.2563 1.1023 0.8127 -0.3472 -0.2403 -0.0470 253 ALA A CA 2022 C C . ALA A 253 ? 1.2610 1.0870 0.8194 -0.3687 -0.2415 -0.0392 253 ALA A C 2023 O O . ALA A 253 ? 1.2813 1.0860 0.8343 -0.3865 -0.2513 -0.0440 253 ALA A O 2024 C CB . ALA A 253 ? 1.2750 1.0898 0.8153 -0.3276 -0.2406 -0.0527 253 ALA A CB 2025 N N . TYR A 254 ? 1.2255 1.0577 0.7908 -0.3669 -0.2312 -0.0275 254 TYR A N 2026 C CA . TYR A 254 ? 1.2225 1.0437 0.7884 -0.3865 -0.2299 -0.0176 254 TYR A CA 2027 C C . TYR A 254 ? 1.2573 1.0319 0.8061 -0.3846 -0.2348 -0.0142 254 TYR A C 2028 O O . TYR A 254 ? 1.2599 1.0236 0.8044 -0.3652 -0.2326 -0.0144 254 TYR A O 2029 C CB . TYR A 254 ? 1.1755 1.0279 0.7552 -0.3854 -0.2169 -0.0077 254 TYR A CB 2030 C CG . TYR A 254 ? 1.1417 1.0399 0.7410 -0.3905 -0.2114 -0.0085 254 TYR A CG 2031 C CD1 . TYR A 254 ? 1.1446 1.0588 0.7538 -0.4137 -0.2106 -0.0051 254 TYR A CD1 2032 C CD2 . TYR A 254 ? 1.1108 1.0365 0.7197 -0.3715 -0.2060 -0.0117 254 TYR A CD2 2033 C CE1 . TYR A 254 ? 1.1229 1.0818 0.7533 -0.4172 -0.2058 -0.0063 254 TYR A CE1 2034 C CE2 . TYR A 254 ? 1.0961 1.0635 0.7236 -0.3738 -0.2017 -0.0115 254 TYR A CE2 2035 C CZ . TYR A 254 ? 1.1051 1.0903 0.7444 -0.3963 -0.2021 -0.0094 254 TYR A CZ 2036 O OH . TYR A 254 ? 1.0987 1.1280 0.7596 -0.3977 -0.1982 -0.0098 254 TYR A OH 2037 N N . LYS A 255 ? 1.2975 1.0452 0.8383 -0.4047 -0.2409 -0.0108 255 LYS A N 2038 C CA . LYS A 255 ? 1.3327 1.0338 0.8563 -0.4037 -0.2461 -0.0051 255 LYS A CA 2039 C C . LYS A 255 ? 1.3282 1.0338 0.8499 -0.4096 -0.2387 0.0105 255 LYS A C 2040 O O . LYS A 255 ? 1.3142 1.0442 0.8440 -0.4268 -0.2319 0.0169 255 LYS A O 2041 C CB . LYS A 255 ? 1.3861 1.0525 0.9013 -0.4229 -0.2555 -0.0085 255 LYS A CB 2042 C CG . LYS A 255 ? 1.4285 1.0433 0.9269 -0.4129 -0.2648 -0.0128 255 LYS A CG 2043 C CD . LYS A 255 ? 1.4592 1.0465 0.9540 -0.4291 -0.2741 -0.0237 255 LYS A CD 2044 C CE . LYS A 255 ? 1.4748 1.0619 0.9751 -0.4601 -0.2721 -0.0155 255 LYS A CE 2045 N NZ . LYS A 255 ? 1.5322 1.0722 1.0250 -0.4760 -0.2805 -0.0212 255 LYS A NZ 2046 N N . ILE A 256 ? 1.3315 1.0161 0.8429 -0.3947 -0.2400 0.0157 256 ILE A N 2047 C CA . ILE A 256 ? 1.3251 1.0142 0.8312 -0.3973 -0.2347 0.0291 256 ILE A CA 2048 C C . ILE A 256 ? 1.3767 1.0224 0.8618 -0.4099 -0.2410 0.0410 256 ILE A C 2049 O O . ILE A 256 ? 1.3910 1.0018 0.8629 -0.3971 -0.2492 0.0432 256 ILE A O 2050 C CB . ILE A 256 ? 1.3028 0.9988 0.8116 -0.3731 -0.2333 0.0274 256 ILE A CB 2051 C CG1 . ILE A 256 ? 1.2605 0.9955 0.7900 -0.3605 -0.2249 0.0171 256 ILE A CG1 2052 C CG2 . ILE A 256 ? 1.3013 1.0046 0.8032 -0.3762 -0.2292 0.0392 256 ILE A CG2 2053 C CD1 . ILE A 256 ? 1.2393 0.9799 0.7760 -0.3373 -0.2225 0.0128 256 ILE A CD1 2054 N N . VAL A 257 ? 1.4118 1.0596 0.8946 -0.4345 -0.2365 0.0495 257 VAL A N 2055 C CA . VAL A 257 ? 1.4806 1.0829 0.9432 -0.4492 -0.2410 0.0619 257 VAL A CA 2056 C C . VAL A 257 ? 1.5015 1.0958 0.9451 -0.4480 -0.2380 0.0792 257 VAL A C 2057 O O . VAL A 257 ? 1.5397 1.0920 0.9629 -0.4408 -0.2462 0.0882 257 VAL A O 2058 C CB . VAL A 257 ? 1.5062 1.1069 0.9754 -0.4784 -0.2379 0.0622 257 VAL A CB 2059 C CG1 . VAL A 257 ? 1.4975 1.1077 0.9834 -0.4775 -0.2436 0.0431 257 VAL A CG1 2060 C CG2 . VAL A 257 ? 1.4883 1.1302 0.9676 -0.4961 -0.2244 0.0694 257 VAL A CG2 2061 N N . LYS A 258 ? 1.4827 1.1170 0.9321 -0.4537 -0.2268 0.0835 258 LYS A N 2062 C CA . LYS A 258 ? 1.5070 1.1397 0.9365 -0.4519 -0.2235 0.0981 258 LYS A CA 2063 C C . LYS A 258 ? 1.4532 1.1205 0.8923 -0.4311 -0.2215 0.0905 258 LYS A C 2064 O O . LYS A 258 ? 1.4082 1.1174 0.8697 -0.4308 -0.2126 0.0807 258 LYS A O 2065 C CB . LYS A 258 ? 1.5259 1.1739 0.9505 -0.4773 -0.2105 0.1098 258 LYS A CB 2066 C CG . LYS A 258 ? 1.6053 1.2087 1.0092 -0.4973 -0.2113 0.1254 258 LYS A CG 2067 C CD . LYS A 258 ? 1.6585 1.2248 1.0278 -0.4882 -0.2172 0.1428 258 LYS A CD 2068 C CE . LYS A 258 ? 1.6689 1.2588 1.0217 -0.4945 -0.2059 0.1553 258 LYS A CE 2069 N NZ . LYS A 258 ? 1.6954 1.2821 1.0414 -0.5243 -0.1919 0.1686 258 LYS A NZ 2070 N N . LYS A 259 ? 1.4612 1.1103 0.8850 -0.4136 -0.2300 0.0946 259 LYS A N 2071 C CA . LYS A 259 ? 1.4312 1.1110 0.8619 -0.3968 -0.2282 0.0887 259 LYS A CA 2072 C C . LYS A 259 ? 1.4576 1.1383 0.8635 -0.4026 -0.2259 0.1025 259 LYS A C 2073 O O . LYS A 259 ? 1.5207 1.1659 0.8991 -0.4099 -0.2311 0.1183 259 LYS A O 2074 C CB . LYS A 259 ? 1.4269 1.0912 0.8613 -0.3715 -0.2404 0.0810 259 LYS A CB 2075 C CG . LYS A 259 ? 1.4065 1.0733 0.8637 -0.3622 -0.2411 0.0661 259 LYS A CG 2076 C CD . LYS A 259 ? 1.4088 1.0621 0.8708 -0.3374 -0.2511 0.0586 259 LYS A CD 2077 C CE . LYS A 259 ? 1.4039 1.0527 0.8821 -0.3293 -0.2513 0.0453 259 LYS A CE 2078 N NZ . LYS A 259 ? 1.4054 1.0454 0.8924 -0.3049 -0.2581 0.0364 259 LYS A NZ 2079 N N . GLY A 260 ? 1.4277 1.1479 0.8420 -0.3989 -0.2178 0.0967 260 GLY A N 2080 C CA . GLY A 260 ? 1.4357 1.1613 0.8249 -0.4024 -0.2157 0.1071 260 GLY A CA 2081 C C . GLY A 260 ? 1.3829 1.1563 0.7866 -0.4038 -0.2025 0.0974 260 GLY A C 2082 O O . GLY A 260 ? 1.3229 1.1245 0.7580 -0.3984 -0.1962 0.0827 260 GLY A O 2083 N N . ASP A 261 ? 1.3959 1.1769 0.7751 -0.4109 -0.1977 0.1061 261 ASP A N 2084 C CA . ASP A 261 ? 1.3685 1.1926 0.7579 -0.4117 -0.1853 0.0962 261 ASP A CA 2085 C C . ASP A 261 ? 1.3306 1.1832 0.7455 -0.4268 -0.1681 0.0911 261 ASP A C 2086 O O . ASP A 261 ? 1.3604 1.2050 0.7678 -0.4461 -0.1611 0.1022 261 ASP A O 2087 C CB . ASP A 261 ? 1.4203 1.2440 0.7723 -0.4175 -0.1833 0.1076 261 ASP A CB 2088 C CG . ASP A 261 ? 1.4482 1.2618 0.7812 -0.3979 -0.1999 0.1064 261 ASP A CG 2089 O OD1 . ASP A 261 ? 1.4201 1.2462 0.7786 -0.3806 -0.2071 0.0901 261 ASP A OD1 2090 O OD2 . ASP A 261 ? 1.4971 1.2914 0.7901 -0.3998 -0.2056 0.1219 261 ASP A OD2 2091 N N . SER A 262 ? 1.2587 1.1447 0.7055 -0.4176 -0.1614 0.0744 262 SER A N 2092 C CA . SER A 262 ? 1.2258 1.1445 0.6989 -0.4277 -0.1454 0.0683 262 SER A CA 2093 C C . SER A 262 ? 1.1883 1.1414 0.6867 -0.4143 -0.1377 0.0514 262 SER A C 2094 O O . SER A 262 ? 1.1914 1.1426 0.6865 -0.3998 -0.1448 0.0443 262 SER A O 2095 C CB . SER A 262 ? 1.2108 1.1206 0.7037 -0.4311 -0.1481 0.0678 262 SER A CB 2096 O OG . SER A 262 ? 1.1792 1.1241 0.7019 -0.4356 -0.1352 0.0599 262 SER A OG 2097 N N . THR A 263 ? 1.1147 0.9524 0.7547 -0.0682 -0.1188 -0.0662 263 THR A N 2098 C CA . THR A 263 ? 1.0157 0.9428 0.7311 -0.0809 -0.1167 -0.0587 263 THR A CA 2099 C C . THR A 263 ? 0.9932 0.9211 0.7303 -0.1184 -0.1313 -0.0544 263 THR A C 2100 O O . THR A 263 ? 1.0274 0.9111 0.7484 -0.1428 -0.1426 -0.0544 263 THR A O 2101 C CB . THR A 263 ? 0.9556 0.9226 0.7263 -0.0857 -0.1125 -0.0521 263 THR A CB 2102 O OG1 . THR A 263 ? 0.8918 0.9301 0.7117 -0.0937 -0.1102 -0.0456 263 THR A OG1 2103 C CG2 . THR A 263 ? 0.9513 0.8947 0.7432 -0.1184 -0.1237 -0.0479 263 THR A CG2 2104 N N . ILE A 264 ? 0.9449 0.9240 0.7111 -0.1249 -0.1321 -0.0504 264 ILE A N 2105 C CA . ILE A 264 ? 0.9132 0.8980 0.7026 -0.1542 -0.1473 -0.0452 264 ILE A CA 2106 C C . ILE A 264 ? 0.8647 0.8869 0.7061 -0.1627 -0.1503 -0.0375 264 ILE A C 2107 O O . ILE A 264 ? 0.8263 0.8828 0.6825 -0.1615 -0.1463 -0.0330 264 ILE A O 2108 C CB . ILE A 264 ? 0.9059 0.9047 0.6793 -0.1587 -0.1499 -0.0452 264 ILE A CB 2109 C CG1 . ILE A 264 ? 0.9583 0.9213 0.6744 -0.1421 -0.1448 -0.0542 264 ILE A CG1 2110 C CG2 . ILE A 264 ? 0.8939 0.8865 0.6809 -0.1838 -0.1682 -0.0405 264 ILE A CG2 2111 C CD1 . ILE A 264 ? 0.9729 0.9489 0.6690 -0.1480 -0.1472 -0.0550 264 ILE A CD1 2112 N N . MET A 265 ? 0.8747 0.8893 0.7355 -0.1735 -0.1579 -0.0360 265 MET A N 2113 C CA . MET A 265 ? 0.8510 0.8974 0.7550 -0.1761 -0.1626 -0.0301 265 MET A CA 2114 C C . MET A 265 ? 0.8506 0.9073 0.7614 -0.1843 -0.1792 -0.0265 265 MET A C 2115 O O . MET A 265 ? 0.8702 0.9154 0.7646 -0.1952 -0.1895 -0.0284 265 MET A O 2116 C CB . MET A 265 ? 0.8551 0.9003 0.7720 -0.1842 -0.1639 -0.0307 265 MET A CB 2117 C CG . MET A 265 ? 0.8277 0.9088 0.7867 -0.1789 -0.1638 -0.0263 265 MET A CG 2118 S SD . MET A 265 ? 0.8537 0.9336 0.8167 -0.1930 -0.1604 -0.0275 265 MET A SD 2119 C CE . MET A 265 ? 0.8613 0.8946 0.7894 -0.1759 -0.1428 -0.0314 265 MET A CE 2120 N N . LYS A 266 ? 0.8503 0.9208 0.7753 -0.1776 -0.1831 -0.0213 266 LYS A N 2121 C CA . LYS A 266 ? 0.8958 0.9614 0.8112 -0.1770 -0.2008 -0.0181 266 LYS A CA 2122 C C . LYS A 266 ? 0.8895 0.9776 0.8294 -0.1623 -0.2107 -0.0163 266 LYS A C 2123 O O . LYS A 266 ? 0.8772 0.9650 0.8236 -0.1510 -0.2071 -0.0134 266 LYS A O 2124 C CB . LYS A 266 ? 0.9496 0.9939 0.8335 -0.1814 -0.2013 -0.0136 266 LYS A CB 2125 C CG . LYS A 266 ? 1.0023 1.0389 0.8583 -0.1950 -0.1959 -0.0157 266 LYS A CG 2126 C CD . LYS A 266 ? 1.0686 1.0783 0.8833 -0.2076 -0.2090 -0.0110 266 LYS A CD 2127 C CE . LYS A 266 ? 1.1278 1.1267 0.9235 -0.2150 -0.2154 -0.0146 266 LYS A CE 2128 N NZ . LYS A 266 ? 1.1999 1.1636 0.9575 -0.2212 -0.2357 -0.0105 266 LYS A NZ 2129 N N . SER A 267 ? 0.9020 1.0157 0.8523 -0.1623 -0.2234 -0.0180 267 SER A N 2130 C CA . SER A 267 ? 0.8951 1.0548 0.8720 -0.1450 -0.2324 -0.0176 267 SER A CA 2131 C C . SER A 267 ? 0.9097 1.0998 0.8819 -0.1384 -0.2524 -0.0183 267 SER A C 2132 O O . SER A 267 ? 0.9215 1.1062 0.8815 -0.1590 -0.2567 -0.0196 267 SER A O 2133 C CB . SER A 267 ? 0.8819 1.0784 0.8906 -0.1598 -0.2212 -0.0194 267 SER A CB 2134 O OG . SER A 267 ? 0.8915 1.1488 0.9289 -0.1443 -0.2277 -0.0190 267 SER A OG 2135 N N . GLU A 268 ? 0.9177 1.1416 0.8952 -0.1059 -0.2654 -0.0179 268 GLU A N 2136 C CA . GLU A 268 ? 0.9361 1.2125 0.9141 -0.0916 -0.2851 -0.0190 268 GLU A CA 2137 C C . GLU A 268 ? 0.9153 1.2864 0.9371 -0.1107 -0.2832 -0.0203 268 GLU A C 2138 O O . GLU A 268 ? 0.9320 1.3662 0.9600 -0.1138 -0.2974 -0.0209 268 GLU A O 2139 C CB . GLU A 268 ? 0.9709 1.2458 0.9242 -0.0383 -0.3016 -0.0190 268 GLU A CB 2140 C CG . GLU A 268 ? 1.0238 1.1926 0.9150 -0.0256 -0.3066 -0.0163 268 GLU A CG 2141 C CD . GLU A 268 ? 1.0598 1.1796 0.9174 -0.0500 -0.3126 -0.0150 268 GLU A CD 2142 O OE1 . GLU A 268 ? 1.0784 1.2211 0.9242 -0.0371 -0.3304 -0.0162 268 GLU A OE1 2143 O OE2 . GLU A 268 ? 1.0597 1.1260 0.9025 -0.0807 -0.2994 -0.0128 268 GLU A OE2 2144 N N . LEU A 269 ? 0.8940 1.2771 0.9412 -0.1274 -0.2666 -0.0203 269 LEU A N 2145 C CA . LEU A 269 ? 0.8881 1.3610 0.9688 -0.1505 -0.2650 -0.0204 269 LEU A CA 2146 C C . LEU A 269 ? 0.9086 1.3900 0.9782 -0.2027 -0.2677 -0.0199 269 LEU A C 2147 O O . LEU A 269 ? 0.9124 1.3163 0.9501 -0.2212 -0.2648 -0.0205 269 LEU A O 2148 C CB . LEU A 269 ? 0.8674 1.3347 0.9672 -0.1592 -0.2467 -0.0199 269 LEU A CB 2149 C CG . LEU A 269 ? 0.8561 1.3257 0.9675 -0.1138 -0.2431 -0.0201 269 LEU A CG 2150 C CD1 . LEU A 269 ? 0.8386 1.3162 0.9719 -0.1311 -0.2257 -0.0195 269 LEU A CD1 2151 C CD2 . LEU A 269 ? 0.8620 1.4164 0.9849 -0.0699 -0.2589 -0.0218 269 LEU A CD2 2152 N N . GLU A 270 ? 0.9273 1.5073 1.0178 -0.2276 -0.2739 -0.0187 270 GLU A N 2153 C CA . GLU A 270 ? 0.9765 1.5688 1.0461 -0.2876 -0.2789 -0.0172 270 GLU A CA 2154 C C . GLU A 270 ? 0.9744 1.5552 1.0352 -0.3356 -0.2658 -0.0155 270 GLU A C 2155 O O . GLU A 270 ? 0.9692 1.5389 1.0475 -0.3180 -0.2527 -0.0158 270 GLU A O 2156 C CB . GLU A 270 ? 0.9922 1.7100 1.0795 -0.2922 -0.2988 -0.0157 270 GLU A CB 2157 C CG . GLU A 270 ? 0.9758 1.8158 1.1071 -0.2429 -0.3049 -0.0164 270 GLU A CG 2158 C CD . GLU A 270 ? 0.9927 1.9791 1.1414 -0.2459 -0.3244 -0.0153 270 GLU A CD 2159 O OE1 . GLU A 270 ? 1.0185 1.9977 1.1450 -0.2691 -0.3370 -0.0142 270 GLU A OE1 2160 O OE2 . GLU A 270 ? 0.9765 2.0943 1.1610 -0.2229 -0.3272 -0.0157 270 GLU A OE2 2161 N N . TYR A 271 ? 1.0007 1.5715 1.0235 -0.3978 -0.2707 -0.0134 271 TYR A N 2162 C CA . TYR A 271 ? 1.0294 1.5699 1.0198 -0.4519 -0.2623 -0.0112 271 TYR A CA 2163 C C . TYR A 271 ? 1.0067 1.6740 1.0394 -0.4651 -0.2617 -0.0078 271 TYR A C 2164 O O . TYR A 271 ? 0.9663 1.7690 1.0366 -0.4622 -0.2738 -0.0061 271 TYR A O 2165 C CB . TYR A 271 ? 1.1054 1.6044 1.0290 -0.5200 -0.2729 -0.0090 271 TYR A CB 2166 C CG . TYR A 271 ? 1.1701 1.5821 1.0235 -0.5776 -0.2668 -0.0072 271 TYR A CG 2167 C CD1 . TYR A 271 ? 1.1981 1.4619 0.9987 -0.5598 -0.2545 -0.0114 271 TYR A CD1 2168 C CD2 . TYR A 271 ? 1.2078 1.6846 1.0369 -0.6510 -0.2750 -0.0010 271 TYR A CD2 2169 C CE1 . TYR A 271 ? 1.2829 1.4492 1.0019 -0.6053 -0.2514 -0.0104 271 TYR A CE1 2170 C CE2 . TYR A 271 ? 1.2954 1.6705 1.0394 -0.7085 -0.2721 0.0012 271 TYR A CE2 2171 C CZ . TYR A 271 ? 1.3369 1.5483 1.0222 -0.6818 -0.2608 -0.0038 271 TYR A CZ 2172 O OH . TYR A 271 ? 1.4246 1.5194 1.0096 -0.7317 -0.2602 -0.0021 271 TYR A OH 2173 N N . GLY A 272 ? 1.0231 1.6523 1.0474 -0.4771 -0.2478 -0.0071 272 GLY A N 2174 C CA . GLY A 272 ? 1.0066 1.7517 1.0690 -0.4899 -0.2447 -0.0041 272 GLY A CA 2175 C C . GLY A 272 ? 1.0728 1.8418 1.0895 -0.5788 -0.2481 0.0017 272 GLY A C 2176 O O . GLY A 272 ? 1.0543 1.9370 1.1005 -0.5994 -0.2461 0.0049 272 GLY A O 2177 N N . ASN A 273 ? 1.1502 1.8078 1.0858 -0.6334 -0.2536 0.0032 273 ASN A N 2178 C CA . ASN A 273 ? 1.2295 1.8712 1.0929 -0.7270 -0.2588 0.0095 273 ASN A CA 2179 C C . ASN A 273 ? 1.2226 1.8278 1.0736 -0.7364 -0.2449 0.0109 273 ASN A C 2180 O O . ASN A 273 ? 1.2358 1.9353 1.0893 -0.7895 -0.2461 0.0167 273 ASN A O 2181 C CB . ASN A 273 ? 1.2294 2.0471 1.1153 -0.7833 -0.2742 0.0158 273 ASN A CB 2182 C CG . ASN A 273 ? 1.3118 2.0922 1.1339 -0.8379 -0.2913 0.0183 273 ASN A CG 2183 O OD1 . ASN A 273 ? 1.2826 2.1297 1.1451 -0.8057 -0.3009 0.0163 273 ASN A OD1 2184 N ND2 . ASN A 273 ? 1.4232 2.0847 1.1344 -0.9209 -0.2966 0.0227 273 ASN A ND2 2185 N N . CYS A 274 ? 1.2025 1.6738 1.0379 -0.6849 -0.2320 0.0056 274 CYS A N 2186 C CA . CYS A 274 ? 1.2067 1.6255 1.0329 -0.6758 -0.2178 0.0056 274 CYS A CA 2187 C C . CYS A 274 ? 1.2528 1.4807 0.9973 -0.6577 -0.2121 0.0012 274 CYS A C 2188 O O . CYS A 274 ? 1.2785 1.4310 0.9879 -0.6428 -0.2172 -0.0025 274 CYS A O 2189 C CB . CYS A 274 ? 1.1104 1.6060 1.0361 -0.5961 -0.2056 0.0020 274 CYS A CB 2190 S SG . CYS A 274 ? 1.0852 1.5308 1.0407 -0.5187 -0.2054 -0.0046 274 CYS A SG 2191 N N . ASN A 275 ? 1.2605 1.4188 0.9770 -0.6516 -0.2012 0.0010 275 ASN A N 2192 C CA . ASN A 275 ? 1.3094 1.2966 0.9462 -0.6229 -0.1950 -0.0038 275 ASN A CA 2193 C C . ASN A 275 ? 1.2477 1.2346 0.9364 -0.5611 -0.1780 -0.0065 275 ASN A C 2194 O O . ASN A 275 ? 1.1960 1.2771 0.9450 -0.5650 -0.1722 -0.0031 275 ASN A O 2195 C CB . ASN A 275 ? 1.4322 1.2955 0.9340 -0.6949 -0.2040 -0.0002 275 ASN A CB 2196 C CG . ASN A 275 ? 1.5076 1.1845 0.9063 -0.6582 -0.2007 -0.0066 275 ASN A CG 2197 O OD1 . ASN A 275 ? 1.5510 1.1494 0.9039 -0.6338 -0.2049 -0.0120 275 ASN A OD1 2198 N ND2 . ASN A 275 ? 1.5452 1.1547 0.9037 -0.6504 -0.1935 -0.0063 275 ASN A ND2 2199 N N . THR A 276 ? 1.2577 1.1465 0.9210 -0.5045 -0.1702 -0.0125 276 THR A N 2200 C CA . THR A 276 ? 1.2032 1.0944 0.9113 -0.4481 -0.1550 -0.0146 276 THR A CA 2201 C C . THR A 276 ? 1.2736 1.0307 0.9046 -0.4072 -0.1495 -0.0205 276 THR A C 2202 O O . THR A 276 ? 1.3625 1.0235 0.9083 -0.4126 -0.1570 -0.0241 276 THR A O 2203 C CB . THR A 276 ? 1.0861 1.0861 0.9057 -0.3976 -0.1491 -0.0157 276 THR A CB 2204 O OG1 . THR A 276 ? 1.0261 1.0557 0.8949 -0.3630 -0.1365 -0.0152 276 THR A OG1 2205 C CG2 . THR A 276 ? 1.0834 1.0440 0.8978 -0.3558 -0.1489 -0.0208 276 THR A CG2 2206 N N . LYS A 277 ? 1.2528 1.0076 0.9098 -0.3638 -0.1369 -0.0217 277 LYS A N 2207 C CA . LYS A 277 ? 1.3218 0.9821 0.9223 -0.3097 -0.1301 -0.0278 277 LYS A CA 2208 C C . LYS A 277 ? 1.2113 0.9414 0.8926 -0.2503 -0.1196 -0.0305 277 LYS A C 2209 O O . LYS A 277 ? 1.2379 0.9252 0.8889 -0.2012 -0.1128 -0.0356 277 LYS A O 2210 C CB . LYS A 277 ? 1.3988 1.0012 0.9551 -0.3052 -0.1247 -0.0267 277 LYS A CB 2211 C CG . LYS A 277 ? 1.5783 1.0559 1.0053 -0.3563 -0.1365 -0.0254 277 LYS A CG 2212 C CD . LYS A 277 ? 1.6740 1.0632 1.0335 -0.3358 -0.1322 -0.0261 277 LYS A CD 2213 C CE . LYS A 277 ? 1.7486 1.0401 1.0351 -0.2607 -0.1293 -0.0350 277 LYS A CE 2214 N NZ . LYS A 277 ? 1.9037 1.0611 1.0586 -0.2664 -0.1425 -0.0403 277 LYS A NZ 2215 N N . CYS A 278 ? 1.1023 0.9408 0.8781 -0.2552 -0.1192 -0.0271 278 CYS A N 2216 C CA . CYS A 278 ? 1.0273 0.9259 0.8695 -0.2116 -0.1115 -0.0278 278 CYS A CA 2217 C C . CYS A 278 ? 0.9510 0.9305 0.8564 -0.2248 -0.1187 -0.0251 278 CYS A C 2218 O O . CYS A 278 ? 0.9132 0.9533 0.8592 -0.2473 -0.1223 -0.0213 278 CYS A O 2219 C CB . CYS A 278 ? 1.0013 0.9341 0.8858 -0.1904 -0.1006 -0.0252 278 CYS A CB 2220 S SG . CYS A 278 ? 0.9445 0.9564 0.9061 -0.1546 -0.0938 -0.0234 278 CYS A SG 2221 N N . GLN A 279 ? 0.9283 0.9115 0.8375 -0.2077 -0.1212 -0.0274 279 GLN A N 2222 C CA . GLN A 279 ? 0.8835 0.9267 0.8357 -0.2172 -0.1308 -0.0254 279 GLN A CA 2223 C C . GLN A 279 ? 0.8145 0.8927 0.8067 -0.1857 -0.1275 -0.0244 279 GLN A C 2224 O O . GLN A 279 ? 0.8082 0.8632 0.7836 -0.1631 -0.1196 -0.0264 279 GLN A O 2225 C CB . GLN A 279 ? 0.9354 0.9431 0.8428 -0.2382 -0.1412 -0.0280 279 GLN A CB 2226 C CG . GLN A 279 ? 0.9106 0.9813 0.8569 -0.2484 -0.1533 -0.0259 279 GLN A CG 2227 C CD . GLN A 279 ? 0.9086 1.0446 0.8817 -0.2791 -0.1612 -0.0223 279 GLN A CD 2228 O OE1 . GLN A 279 ? 0.9734 1.0902 0.9074 -0.3201 -0.1657 -0.0215 279 GLN A OE1 2229 N NE2 . GLN A 279 ? 0.8560 1.0695 0.8871 -0.2600 -0.1640 -0.0201 279 GLN A NE2 2230 N N . THR A 280 ? 0.7740 0.9088 0.8104 -0.1846 -0.1345 -0.0213 280 THR A N 2231 C CA . THR A 280 ? 0.7609 0.9116 0.8151 -0.1634 -0.1367 -0.0196 280 THR A CA 2232 C C . THR A 280 ? 0.7860 0.9598 0.8451 -0.1681 -0.1521 -0.0193 280 THR A C 2233 O O . THR A 280 ? 0.7808 0.9862 0.8478 -0.1846 -0.1605 -0.0196 280 THR A O 2234 C CB . THR A 280 ? 0.7232 0.9009 0.8081 -0.1467 -0.1330 -0.0161 280 THR A CB 2235 O OG1 . THR A 280 ? 0.7232 0.9444 0.8316 -0.1431 -0.1438 -0.0152 280 THR A OG1 2236 C CG2 . THR A 280 ? 0.7145 0.8854 0.8033 -0.1468 -0.1204 -0.0160 280 THR A CG2 2237 N N . PRO A 281 ? 0.8047 0.9678 0.8556 -0.1556 -0.1569 -0.0181 281 PRO A N 2238 C CA . PRO A 281 ? 0.8278 1.0043 0.8756 -0.1530 -0.1732 -0.0177 281 PRO A CA 2239 C C . PRO A 281 ? 0.8323 1.0569 0.9040 -0.1375 -0.1841 -0.0166 281 PRO A C 2240 O O . PRO A 281 ? 0.8404 1.0854 0.9077 -0.1305 -0.1992 -0.0170 281 PRO A O 2241 C CB . PRO A 281 ? 0.8401 0.9845 0.8642 -0.1439 -0.1745 -0.0153 281 PRO A CB 2242 C CG . PRO A 281 ? 0.8350 0.9633 0.8517 -0.1470 -0.1580 -0.0153 281 PRO A CG 2243 C CD . PRO A 281 ? 0.8066 0.9448 0.8417 -0.1473 -0.1473 -0.0170 281 PRO A CD 2244 N N . MET A 282 ? 0.8233 1.0691 0.9167 -0.1276 -0.1769 -0.0157 282 MET A N 2245 C CA . MET A 282 ? 0.8222 1.1242 0.9367 -0.1061 -0.1854 -0.0160 282 MET A CA 2246 C C . MET A 282 ? 0.7794 1.1476 0.9229 -0.1261 -0.1822 -0.0170 282 MET A C 2247 O O . MET A 282 ? 0.7391 1.1793 0.9028 -0.1108 -0.1899 -0.0178 282 MET A O 2248 C CB . MET A 282 ? 0.8559 1.1383 0.9676 -0.0800 -0.1810 -0.0143 282 MET A CB 2249 C CG . MET A 282 ? 0.9213 1.1334 0.9939 -0.0745 -0.1827 -0.0114 282 MET A CG 2250 S SD . MET A 282 ? 1.0205 1.1984 1.0596 -0.0383 -0.1915 -0.0094 282 MET A SD 2251 C CE . MET A 282 ? 0.9619 1.1937 1.0448 -0.0289 -0.1790 -0.0110 282 MET A CE 2252 N N . GLY A 283 ? 0.7778 1.1215 0.9149 -0.1595 -0.1714 -0.0169 283 GLY A N 2253 C CA . GLY A 283 ? 0.7718 1.1610 0.9203 -0.1896 -0.1681 -0.0166 283 GLY A CA 2254 C C . GLY A 283 ? 0.7870 1.1131 0.9127 -0.2098 -0.1541 -0.0163 283 GLY A C 2255 O O . GLY A 283 ? 0.7613 1.0292 0.8740 -0.1919 -0.1458 -0.0168 283 GLY A O 2256 N N . ALA A 284 ? 0.8055 1.1449 0.9191 -0.2478 -0.1525 -0.0154 284 ALA A N 2257 C CA . ALA A 284 ? 0.8297 1.0953 0.9044 -0.2652 -0.1419 -0.0155 284 ALA A CA 2258 C C . ALA A 284 ? 0.7968 1.0778 0.8948 -0.2532 -0.1308 -0.0139 284 ALA A C 2259 O O . ALA A 284 ? 0.7457 1.1022 0.8873 -0.2405 -0.1315 -0.0127 284 ALA A O 2260 C CB . ALA A 284 ? 0.8919 1.1348 0.9167 -0.3190 -0.1481 -0.0145 284 ALA A CB 2261 N N . ILE A 285 ? 0.8236 1.0308 0.8858 -0.2536 -0.1212 -0.0144 285 ILE A N 2262 C CA . ILE A 285 ? 0.8028 1.0095 0.8802 -0.2396 -0.1100 -0.0130 285 ILE A CA 2263 C C . ILE A 285 ? 0.8643 1.0201 0.8905 -0.2738 -0.1070 -0.0120 285 ILE A C 2264 O O . ILE A 285 ? 0.9128 0.9845 0.8723 -0.2863 -0.1092 -0.0139 285 ILE A O 2265 C CB . ILE A 285 ? 0.7821 0.9495 0.8615 -0.1992 -0.1013 -0.0141 285 ILE A CB 2266 C CG1 . ILE A 285 ? 0.7340 0.9513 0.8601 -0.1716 -0.1032 -0.0129 285 ILE A CG1 2267 C CG2 . ILE A 285 ? 0.7883 0.9228 0.8542 -0.1917 -0.0901 -0.0133 285 ILE A CG2 2268 C CD1 . ILE A 285 ? 0.7209 0.9096 0.8416 -0.1457 -0.0981 -0.0127 285 ILE A CD1 2269 N N . ASN A 286 ? 0.8615 1.0612 0.9095 -0.2872 -0.1027 -0.0092 286 ASN A N 2270 C CA . ASN A 286 ? 0.9383 1.0846 0.9329 -0.3206 -0.0997 -0.0073 286 ASN A CA 2271 C C . ASN A 286 ? 0.9049 1.0721 0.9319 -0.2998 -0.0886 -0.0058 286 ASN A C 2272 O O . ASN A 286 ? 0.8622 1.1162 0.9364 -0.3073 -0.0870 -0.0038 286 ASN A O 2273 C CB . ASN A 286 ? 0.9823 1.1728 0.9573 -0.3834 -0.1087 -0.0039 286 ASN A CB 2274 C CG . ASN A 286 ? 1.0791 1.1873 0.9708 -0.4307 -0.1092 -0.0011 286 ASN A CG 2275 O OD1 . ASN A 286 ? 1.1355 1.1244 0.9595 -0.4154 -0.1073 -0.0033 286 ASN A OD1 2276 N ND2 . ASN A 286 ? 1.1110 1.2834 0.9994 -0.4879 -0.1127 0.0037 286 ASN A ND2 2277 N N . SER A 287 ? 0.9142 1.0094 0.9155 -0.2698 -0.0810 -0.0072 287 SER A N 2278 C CA . SER A 287 ? 0.8823 0.9867 0.9044 -0.2538 -0.0710 -0.0053 287 SER A CA 2279 C C . SER A 287 ? 0.9275 0.9407 0.8951 -0.2313 -0.0656 -0.0067 287 SER A C 2280 O O . SER A 287 ? 0.9511 0.9011 0.8719 -0.2138 -0.0682 -0.0101 287 SER A O 2281 C CB . SER A 287 ? 0.8013 0.9768 0.8965 -0.2167 -0.0665 -0.0051 287 SER A CB 2282 O OG . SER A 287 ? 0.7774 0.9338 0.8763 -0.1854 -0.0672 -0.0071 287 SER A OG 2283 N N . SER A 288 ? 0.9488 0.9604 0.9206 -0.2277 -0.0583 -0.0044 288 SER A N 2284 C CA . SER A 288 ? 1.0091 0.9491 0.9356 -0.1979 -0.0530 -0.0055 288 SER A CA 2285 C C . SER A 288 ? 0.9299 0.9170 0.9125 -0.1521 -0.0447 -0.0054 288 SER A C 2286 O O . SER A 288 ? 0.9534 0.9058 0.9094 -0.1209 -0.0400 -0.0062 288 SER A O 2287 C CB . SER A 288 ? 1.0858 0.9880 0.9726 -0.2248 -0.0512 -0.0024 288 SER A CB 2288 O OG . SER A 288 ? 1.0494 1.0379 0.9954 -0.2533 -0.0483 0.0011 288 SER A OG 2289 N N . MET A 289 ? 0.8390 0.9022 0.8891 -0.1483 -0.0444 -0.0042 289 MET A N 2290 C CA . MET A 289 ? 0.7857 0.8870 0.8769 -0.1176 -0.0387 -0.0025 289 MET A CA 2291 C C . MET A 289 ? 0.7853 0.8686 0.8548 -0.0893 -0.0378 -0.0046 289 MET A C 2292 O O . MET A 289 ? 0.8388 0.8982 0.8813 -0.0900 -0.0430 -0.0079 289 MET A O 2293 C CB . MET A 289 ? 0.7531 0.9150 0.8958 -0.1192 -0.0422 -0.0013 289 MET A CB 2294 C CG . MET A 289 ? 0.7547 0.9587 0.9231 -0.1383 -0.0437 -0.0006 289 MET A CG 2295 S SD . MET A 289 ? 0.7440 0.9646 0.9315 -0.1310 -0.0345 0.0022 289 MET A SD 2296 C CE . MET A 289 ? 0.7011 0.9931 0.9306 -0.1228 -0.0394 0.0013 289 MET A CE 2297 N N . PRO A 290 ? 0.7410 0.8440 0.8206 -0.0652 -0.0314 -0.0026 290 PRO A N 2298 C CA . PRO A 290 ? 0.7311 0.8450 0.7951 -0.0385 -0.0298 -0.0043 290 PRO A CA 2299 C C . PRO A 290 ? 0.6908 0.8489 0.7843 -0.0452 -0.0333 -0.0027 290 PRO A C 2300 O O . PRO A 290 ? 0.7158 0.8879 0.7939 -0.0304 -0.0330 -0.0046 290 PRO A O 2301 C CB . PRO A 290 ? 0.7099 0.8499 0.7797 -0.0184 -0.0225 -0.0012 290 PRO A CB 2302 C CG . PRO A 290 ? 0.6789 0.8337 0.7854 -0.0392 -0.0211 0.0032 290 PRO A CG 2303 C CD . PRO A 290 ? 0.6981 0.8184 0.7977 -0.0623 -0.0252 0.0011 290 PRO A CD 2304 N N . PHE A 291 ? 0.6566 0.8349 0.7844 -0.0644 -0.0372 0.0003 291 PHE A N 2305 C CA . PHE A 291 ? 0.6461 0.8488 0.7876 -0.0716 -0.0431 0.0023 291 PHE A CA 2306 C C . PHE A 291 ? 0.6204 0.8183 0.7748 -0.0848 -0.0519 0.0010 291 PHE A C 2307 O O . PHE A 291 ? 0.6123 0.8096 0.7778 -0.0914 -0.0520 0.0001 291 PHE A O 2308 C CB . PHE A 291 ? 0.6493 0.8757 0.8040 -0.0755 -0.0422 0.0083 291 PHE A CB 2309 C CG . PHE A 291 ? 0.6555 0.9103 0.8021 -0.0677 -0.0350 0.0114 291 PHE A CG 2310 C CD1 . PHE A 291 ? 0.6698 0.9580 0.8048 -0.0719 -0.0359 0.0136 291 PHE A CD1 2311 C CD2 . PHE A 291 ? 0.6715 0.9293 0.8213 -0.0580 -0.0279 0.0125 291 PHE A CD2 2312 C CE1 . PHE A 291 ? 0.6607 0.9988 0.7903 -0.0661 -0.0294 0.0169 291 PHE A CE1 2313 C CE2 . PHE A 291 ? 0.6741 0.9724 0.8174 -0.0483 -0.0221 0.0156 291 PHE A CE2 2314 C CZ . PHE A 291 ? 0.6571 1.0024 0.7920 -0.0524 -0.0228 0.0178 291 PHE A CZ 2315 N N . HIS A 292 ? 0.6036 0.8062 0.7549 -0.0884 -0.0596 0.0012 292 HIS A N 2316 C CA . HIS A 292 ? 0.5849 0.7914 0.7461 -0.0932 -0.0701 0.0003 292 HIS A CA 2317 C C . HIS A 292 ? 0.5869 0.7879 0.7335 -0.0933 -0.0782 0.0034 292 HIS A C 2318 O O . HIS A 292 ? 0.6037 0.8057 0.7346 -0.0983 -0.0752 0.0064 292 HIS A O 2319 C CB . HIS A 292 ? 0.5911 0.7922 0.7466 -0.1020 -0.0748 -0.0038 292 HIS A CB 2320 C CG . HIS A 292 ? 0.6059 0.7937 0.7404 -0.1023 -0.0776 -0.0052 292 HIS A CG 2321 N ND1 . HIS A 292 ? 0.6008 0.7909 0.7319 -0.1054 -0.0880 -0.0052 292 HIS A ND1 2322 C CD2 . HIS A 292 ? 0.6315 0.8057 0.7430 -0.0959 -0.0713 -0.0071 292 HIS A CD2 2323 C CE1 . HIS A 292 ? 0.6271 0.8070 0.7376 -0.1063 -0.0873 -0.0065 292 HIS A CE1 2324 N NE2 . HIS A 292 ? 0.6305 0.8043 0.7291 -0.0983 -0.0769 -0.0081 292 HIS A NE2 2325 N N . ASN A 293 ? 0.5850 0.7822 0.7295 -0.0881 -0.0895 0.0028 293 ASN A N 2326 C CA . ASN A 293 ? 0.6035 0.7745 0.7156 -0.0886 -0.1006 0.0058 293 ASN A CA 2327 C C . ASN A 293 ? 0.6268 0.7943 0.7315 -0.0820 -0.1138 0.0027 293 ASN A C 2328 O O . ASN A 293 ? 0.6739 0.8127 0.7468 -0.0712 -0.1267 0.0039 293 ASN A O 2329 C CB . ASN A 293 ? 0.6256 0.7730 0.7173 -0.0792 -0.1047 0.0090 293 ASN A CB 2330 C CG . ASN A 293 ? 0.6146 0.7759 0.7199 -0.0540 -0.1098 0.0047 293 ASN A CG 2331 O OD1 . ASN A 293 ? 0.6158 0.8179 0.7540 -0.0514 -0.1080 0.0004 293 ASN A OD1 2332 N ND2 . ASN A 293 ? 0.6496 0.7790 0.7225 -0.0363 -0.1168 0.0058 293 ASN A ND2 2333 N N . ILE A 294 ? 0.6202 0.8096 0.7446 -0.0881 -0.1120 -0.0010 294 ILE A N 2334 C CA . ILE A 294 ? 0.6496 0.8492 0.7731 -0.0837 -0.1245 -0.0040 294 ILE A CA 2335 C C . ILE A 294 ? 0.6792 0.8485 0.7708 -0.0902 -0.1328 -0.0026 294 ILE A C 2336 O O . ILE A 294 ? 0.7049 0.8564 0.7721 -0.0783 -0.1471 -0.0023 294 ILE A O 2337 C CB . ILE A 294 ? 0.6373 0.8668 0.7832 -0.0975 -0.1210 -0.0077 294 ILE A CB 2338 C CG1 . ILE A 294 ? 0.6242 0.8846 0.7949 -0.0991 -0.1133 -0.0083 294 ILE A CG1 2339 C CG2 . ILE A 294 ? 0.6596 0.9121 0.8057 -0.0966 -0.1347 -0.0101 294 ILE A CG2 2340 C CD1 . ILE A 294 ? 0.6281 0.9203 0.8108 -0.0759 -0.1187 -0.0085 294 ILE A CD1 2341 N N . HIS A 295 ? 0.6828 0.8464 0.7687 -0.1059 -0.1242 -0.0021 295 HIS A N 2342 C CA . HIS A 295 ? 0.7148 0.8607 0.7722 -0.1164 -0.1298 -0.0010 295 HIS A CA 2343 C C . HIS A 295 ? 0.7058 0.8645 0.7610 -0.1254 -0.1161 -0.0013 295 HIS A C 2344 O O . HIS A 295 ? 0.6954 0.8638 0.7654 -0.1200 -0.1069 -0.0051 295 HIS A O 2345 C CB . HIS A 295 ? 0.7453 0.8944 0.8047 -0.1155 -0.1400 -0.0049 295 HIS A CB 2346 C CG . HIS A 295 ? 0.7865 0.9135 0.8137 -0.1245 -0.1485 -0.0038 295 HIS A CG 2347 N ND1 . HIS A 295 ? 0.8007 0.9292 0.8156 -0.1374 -0.1403 -0.0041 295 HIS A ND1 2348 C CD2 . HIS A 295 ? 0.8167 0.9207 0.8171 -0.1202 -0.1649 -0.0027 295 HIS A CD2 2349 C CE1 . HIS A 295 ? 0.8391 0.9490 0.8243 -0.1463 -0.1504 -0.0027 295 HIS A CE1 2350 N NE2 . HIS A 295 ? 0.8483 0.9372 0.8219 -0.1369 -0.1660 -0.0017 295 HIS A NE2 2351 N N . PRO A 296 ? 0.7134 0.8731 0.7421 -0.1384 -0.1156 0.0026 296 PRO A N 2352 C CA . PRO A 296 ? 0.6945 0.8883 0.7219 -0.1395 -0.1020 0.0020 296 PRO A CA 2353 C C . PRO A 296 ? 0.6984 0.8949 0.7226 -0.1287 -0.0978 -0.0049 296 PRO A C 2354 O O . PRO A 296 ? 0.6936 0.9034 0.7185 -0.1122 -0.0868 -0.0087 296 PRO A O 2355 C CB . PRO A 296 ? 0.7116 0.9169 0.7064 -0.1641 -0.1052 0.0087 296 PRO A CB 2356 C CG . PRO A 296 ? 0.7457 0.9019 0.7141 -0.1740 -0.1224 0.0109 296 PRO A CG 2357 C CD . PRO A 296 ? 0.7464 0.8777 0.7363 -0.1536 -0.1282 0.0083 296 PRO A CD 2358 N N . LEU A 297 ? 0.7215 0.8985 0.7326 -0.1357 -0.1077 -0.0066 297 LEU A N 2359 C CA . LEU A 297 ? 0.7405 0.9088 0.7377 -0.1279 -0.1057 -0.0132 297 LEU A CA 2360 C C . LEU A 297 ? 0.7471 0.8872 0.7514 -0.1216 -0.1069 -0.0180 297 LEU A C 2361 O O . LEU A 297 ? 0.7724 0.9012 0.7870 -0.1315 -0.1179 -0.0178 297 LEU A O 2362 C CB . LEU A 297 ? 0.7589 0.9146 0.7370 -0.1413 -0.1169 -0.0129 297 LEU A CB 2363 C CG . LEU A 297 ? 0.7739 0.9490 0.7313 -0.1588 -0.1184 -0.0070 297 LEU A CG 2364 C CD1 . LEU A 297 ? 0.8110 0.9594 0.7448 -0.1724 -0.1323 -0.0064 297 LEU A CD1 2365 C CD2 . LEU A 297 ? 0.7763 1.0024 0.7236 -0.1533 -0.1036 -0.0083 297 LEU A CD2 2366 N N . THR A 298 ? 0.7538 0.8845 0.7457 -0.1061 -0.0967 -0.0220 298 THR A N 2367 C CA . THR A 298 ? 0.7680 0.8585 0.7469 -0.1091 -0.0990 -0.0258 298 THR A CA 2368 C C . THR A 298 ? 0.8233 0.8706 0.7479 -0.0931 -0.0951 -0.0328 298 THR A C 2369 O O . THR A 298 ? 0.8106 0.8742 0.7161 -0.0702 -0.0879 -0.0355 298 THR A O 2370 C CB . THR A 298 ? 0.7367 0.8301 0.7341 -0.1064 -0.0932 -0.0236 298 THR A CB 2371 O OG1 . THR A 298 ? 0.7373 0.8238 0.7112 -0.0812 -0.0818 -0.0262 298 THR A OG1 2372 C CG2 . THR A 298 ? 0.6948 0.8277 0.7342 -0.1112 -0.0946 -0.0175 298 THR A CG2 2373 N N . ILE A 299 ? 0.8713 0.8642 0.7632 -0.1062 -0.1009 -0.0357 299 ILE A N 2374 C CA . ILE A 299 ? 0.9641 0.8871 0.7818 -0.0915 -0.1003 -0.0428 299 ILE A CA 2375 C C . ILE A 299 ? 1.0289 0.8969 0.8139 -0.1028 -0.1014 -0.0428 299 ILE A C 2376 O O . ILE A 299 ? 1.0006 0.8864 0.8180 -0.1369 -0.1069 -0.0379 299 ILE A O 2377 C CB . ILE A 299 ? 1.0133 0.9039 0.7991 -0.1104 -0.1111 -0.0456 299 ILE A CB 2378 C CG1 . ILE A 299 ? 1.1115 0.9049 0.8001 -0.0985 -0.1133 -0.0533 299 ILE A CG1 2379 C CG2 . ILE A 299 ? 0.9948 0.9018 0.8126 -0.1541 -0.1233 -0.0406 299 ILE A CG2 2380 C CD1 . ILE A 299 ? 1.1490 0.9345 0.7953 -0.0456 -0.1036 -0.0606 299 ILE A CD1 2381 N N . GLY A 300 ? 1.1230 0.9271 0.8386 -0.0719 -0.0967 -0.0484 300 GLY A N 2382 C CA . GLY A 300 ? 1.2168 0.9440 0.8757 -0.0823 -0.0992 -0.0488 300 GLY A CA 2383 C C . GLY A 300 ? 1.2351 0.9819 0.9098 -0.0519 -0.0887 -0.0476 300 GLY A C 2384 O O . GLY A 300 ? 1.1680 0.9863 0.8878 -0.0187 -0.0791 -0.0475 300 GLY A O 2385 N N . GLU A 301 ? 1.3186 1.0031 0.9512 -0.0683 -0.0914 -0.0463 301 GLU A N 2386 C CA . GLU A 301 ? 1.3264 1.0217 0.9697 -0.0442 -0.0829 -0.0446 301 GLU A CA 2387 C C . GLU A 301 ? 1.1870 0.9756 0.9321 -0.0729 -0.0790 -0.0367 301 GLU A C 2388 O O . GLU A 301 ? 1.1755 0.9574 0.9289 -0.1155 -0.0838 -0.0324 301 GLU A O 2389 C CB . GLU A 301 ? 1.4861 1.0619 1.0278 -0.0521 -0.0889 -0.0463 301 GLU A CB 2390 C CG . GLU A 301 ? 1.5670 1.1159 1.0704 0.0027 -0.0818 -0.0495 301 GLU A CG 2391 C CD . GLU A 301 ? 1.6492 1.1797 1.0969 0.0714 -0.0790 -0.0586 301 GLU A CD 2392 O OE1 . GLU A 301 ? 1.7757 1.1887 1.1077 0.0871 -0.0879 -0.0656 301 GLU A OE1 2393 O OE2 . GLU A 301 ? 1.6104 1.2468 1.1249 0.1083 -0.0684 -0.0588 301 GLU A OE2 2394 N N . CYS A 302 ? 1.0814 0.9567 0.8952 -0.0501 -0.0709 -0.0346 302 CYS A N 2395 C CA . CYS A 302 ? 0.9720 0.9257 0.8705 -0.0715 -0.0691 -0.0279 302 CYS A CA 2396 C C . CYS A 302 ? 0.9076 0.9062 0.8400 -0.0490 -0.0592 -0.0247 302 CYS A C 2397 O O . CYS A 302 ? 0.9001 0.9043 0.8098 -0.0125 -0.0527 -0.0274 302 CYS A O 2398 C CB . CYS A 302 ? 0.9262 0.9341 0.8672 -0.0781 -0.0725 -0.0265 302 CYS A CB 2399 S SG . CYS A 302 ? 0.9824 0.9565 0.8969 -0.1072 -0.0853 -0.0291 302 CYS A SG 2400 N N . PRO A 303 ? 0.8404 0.8782 0.8257 -0.0688 -0.0583 -0.0192 303 PRO A N 2401 C CA . PRO A 303 ? 0.7872 0.8745 0.8091 -0.0540 -0.0506 -0.0152 303 PRO A CA 2402 C C . PRO A 303 ? 0.7571 0.8976 0.8012 -0.0468 -0.0497 -0.0133 303 PRO A C 2403 O O . PRO A 303 ? 0.7512 0.8926 0.7927 -0.0554 -0.0557 -0.0147 303 PRO A O 2404 C CB . PRO A 303 ? 0.7550 0.8641 0.8195 -0.0778 -0.0523 -0.0107 303 PRO A CB 2405 C CG . PRO A 303 ? 0.7678 0.8660 0.8312 -0.1040 -0.0614 -0.0121 303 PRO A CG 2406 C CD . PRO A 303 ? 0.8358 0.8750 0.8403 -0.1041 -0.0645 -0.0169 303 PRO A CD 2407 N N . LYS A 304 ? 0.7264 0.9117 0.7875 -0.0362 -0.0431 -0.0094 304 LYS A N 2408 C CA . LYS A 304 ? 0.7012 0.9409 0.7732 -0.0396 -0.0426 -0.0060 304 LYS A CA 2409 C C . LYS A 304 ? 0.6462 0.8926 0.7436 -0.0683 -0.0500 -0.0002 304 LYS A C 2410 O O . LYS A 304 ? 0.6240 0.8615 0.7395 -0.0761 -0.0511 0.0027 304 LYS A O 2411 C CB . LYS A 304 ? 0.7312 1.0239 0.8029 -0.0226 -0.0338 -0.0033 304 LYS A CB 2412 C CG . LYS A 304 ? 0.8152 1.0989 0.8500 0.0192 -0.0279 -0.0102 304 LYS A CG 2413 C CD . LYS A 304 ? 0.8668 1.1697 0.8728 0.0389 -0.0275 -0.0156 304 LYS A CD 2414 C CE . LYS A 304 ? 0.9578 1.1927 0.9048 0.0780 -0.0278 -0.0251 304 LYS A CE 2415 N NZ . LYS A 304 ? 1.0148 1.2939 0.9274 0.1187 -0.0237 -0.0312 304 LYS A NZ 2416 N N . TYR A 305 ? 0.6224 0.8784 0.7126 -0.0809 -0.0561 0.0008 305 TYR A N 2417 C CA . TYR A 305 ? 0.6073 0.8511 0.7018 -0.1023 -0.0661 0.0054 305 TYR A CA 2418 C C . TYR A 305 ? 0.6015 0.8672 0.6897 -0.1176 -0.0653 0.0131 305 TYR A C 2419 O O . TYR A 305 ? 0.6037 0.9160 0.6818 -0.1236 -0.0594 0.0162 305 TYR A O 2420 C CB . TYR A 305 ? 0.6150 0.8518 0.6925 -0.1125 -0.0744 0.0046 305 TYR A CB 2421 C CG . TYR A 305 ? 0.6213 0.8333 0.6854 -0.1298 -0.0871 0.0094 305 TYR A CG 2422 C CD1 . TYR A 305 ? 0.6207 0.8027 0.6932 -0.1224 -0.0963 0.0075 305 TYR A CD1 2423 C CD2 . TYR A 305 ? 0.6332 0.8513 0.6664 -0.1529 -0.0911 0.0160 305 TYR A CD2 2424 C CE1 . TYR A 305 ? 0.6484 0.7976 0.6944 -0.1270 -0.1099 0.0108 305 TYR A CE1 2425 C CE2 . TYR A 305 ? 0.6743 0.8458 0.6735 -0.1673 -0.1054 0.0204 305 TYR A CE2 2426 C CZ . TYR A 305 ? 0.6757 0.8079 0.6791 -0.1488 -0.1152 0.0172 305 TYR A CZ 2427 O OH . TYR A 305 ? 0.7107 0.7871 0.6667 -0.1521 -0.1313 0.0204 305 TYR A OH 2428 N N . VAL A 306 ? 0.5871 0.8230 0.6760 -0.1238 -0.0714 0.0162 306 VAL A N 2429 C CA . VAL A 306 ? 0.6049 0.8363 0.6683 -0.1451 -0.0753 0.0241 306 VAL A CA 2430 C C . VAL A 306 ? 0.6418 0.8139 0.6754 -0.1497 -0.0904 0.0256 306 VAL A C 2431 O O . VAL A 306 ? 0.6516 0.8040 0.7009 -0.1291 -0.0949 0.0203 306 VAL A O 2432 C CB . VAL A 306 ? 0.5964 0.8429 0.6739 -0.1408 -0.0669 0.0266 306 VAL A CB 2433 C CG1 . VAL A 306 ? 0.5735 0.8822 0.6645 -0.1339 -0.0544 0.0265 306 VAL A CG1 2434 C CG2 . VAL A 306 ? 0.5742 0.7963 0.6784 -0.1187 -0.0654 0.0217 306 VAL A CG2 2435 N N . LYS A 307 ? 0.6944 0.8385 0.6762 -0.1770 -0.0993 0.0329 307 LYS A N 2436 C CA . LYS A 307 ? 0.7729 0.8399 0.7016 -0.1768 -0.1164 0.0345 307 LYS A CA 2437 C C . LYS A 307 ? 0.7971 0.8275 0.7167 -0.1587 -0.1184 0.0343 307 LYS A C 2438 O O . LYS A 307 ? 0.8819 0.8406 0.7443 -0.1498 -0.1333 0.0349 307 LYS A O 2439 C CB . LYS A 307 ? 0.8395 0.8702 0.6936 -0.2195 -0.1274 0.0434 307 LYS A CB 2440 C CG . LYS A 307 ? 0.8578 0.8897 0.6966 -0.2313 -0.1335 0.0428 307 LYS A CG 2441 C CD . LYS A 307 ? 0.9464 0.9475 0.7048 -0.2842 -0.1437 0.0531 307 LYS A CD 2442 C CE . LYS A 307 ? 1.0172 0.9694 0.7280 -0.2931 -0.1582 0.0531 307 LYS A CE 2443 N NZ . LYS A 307 ? 1.1192 1.0111 0.7266 -0.3501 -0.1727 0.0643 307 LYS A NZ 2444 N N . SER A 308 ? 0.7636 0.8376 0.7310 -0.1494 -0.1045 0.0329 308 SER A N 2445 C CA . SER A 308 ? 0.7744 0.8210 0.7354 -0.1331 -0.1047 0.0325 308 SER A CA 2446 C C . SER A 308 ? 0.7866 0.8166 0.7585 -0.0938 -0.1110 0.0249 308 SER A C 2447 O O . SER A 308 ? 0.7406 0.8085 0.7556 -0.0799 -0.1085 0.0192 308 SER A O 2448 C CB . SER A 308 ? 0.7088 0.8100 0.7209 -0.1318 -0.0880 0.0325 308 SER A CB 2449 O OG . SER A 308 ? 0.7222 0.8503 0.7198 -0.1631 -0.0834 0.0398 308 SER A OG 2450 N N . ASN A 309 ? 0.8452 0.8222 0.7726 -0.0755 -0.1198 0.0247 309 ASN A N 2451 C CA . ASN A 309 ? 0.8627 0.8497 0.8068 -0.0311 -0.1230 0.0168 309 ASN A CA 2452 C C . ASN A 309 ? 0.8010 0.8432 0.8033 -0.0215 -0.1077 0.0141 309 ASN A C 2453 O O . ASN A 309 ? 0.7548 0.8493 0.8009 0.0008 -0.1042 0.0079 309 ASN A O 2454 C CB . ASN A 309 ? 0.9664 0.8679 0.8242 -0.0035 -0.1409 0.0160 309 ASN A CB 2455 C CG . ASN A 309 ? 1.0379 0.8881 0.8399 0.0014 -0.1588 0.0158 309 ASN A CG 2456 O OD1 . ASN A 309 ? 0.9856 0.8854 0.8306 0.0118 -0.1592 0.0115 309 ASN A OD1 2457 N ND2 . ASN A 309 ? 1.1559 0.8999 0.8534 -0.0102 -0.1749 0.0211 309 ASN A ND2 2458 N N . ARG A 310 ? 0.7900 0.8255 0.7898 -0.0429 -0.0990 0.0195 310 ARG A N 2459 C CA . ARG A 310 ? 0.7525 0.8279 0.7963 -0.0363 -0.0853 0.0179 310 ARG A CA 2460 C C . ARG A 310 ? 0.6940 0.7942 0.7606 -0.0663 -0.0728 0.0235 310 ARG A C 2461 O O . ARG A 310 ? 0.7132 0.7883 0.7423 -0.0908 -0.0756 0.0304 310 ARG A O 2462 C CB . ARG A 310 ? 0.8336 0.8624 0.8318 -0.0140 -0.0908 0.0173 310 ARG A CB 2463 C CG . ARG A 310 ? 0.8367 0.9092 0.8773 0.0014 -0.0785 0.0139 310 ARG A CG 2464 C CD . ARG A 310 ? 0.9090 0.9282 0.8948 0.0245 -0.0839 0.0133 310 ARG A CD 2465 N NE . ARG A 310 ? 0.8982 0.9512 0.9190 0.0234 -0.0699 0.0133 310 ARG A NE 2466 C CZ . ARG A 310 ? 0.8667 0.9825 0.9333 0.0450 -0.0613 0.0073 310 ARG A CZ 2467 N NH1 . ARG A 310 ? 0.8753 1.0396 0.9629 0.0698 -0.0651 0.0006 310 ARG A NH1 2468 N NH2 . ARG A 310 ? 0.8481 0.9847 0.9377 0.0388 -0.0493 0.0083 310 ARG A NH2 2469 N N . LEU A 311 ? 0.6208 0.7708 0.7407 -0.0652 -0.0604 0.0208 311 LEU A N 2470 C CA . LEU A 311 ? 0.5910 0.7636 0.7271 -0.0797 -0.0490 0.0247 311 LEU A CA 2471 C C . LEU A 311 ? 0.5583 0.7504 0.7257 -0.0690 -0.0390 0.0218 311 LEU A C 2472 O O . LEU A 311 ? 0.5693 0.7823 0.7626 -0.0653 -0.0353 0.0173 311 LEU A O 2473 C CB . LEU A 311 ? 0.5723 0.7725 0.7221 -0.0883 -0.0451 0.0245 311 LEU A CB 2474 C CG . LEU A 311 ? 0.5884 0.7884 0.7103 -0.1059 -0.0515 0.0286 311 LEU A CG 2475 C CD1 . LEU A 311 ? 0.5671 0.8028 0.7047 -0.1039 -0.0456 0.0264 311 LEU A CD1 2476 C CD2 . LEU A 311 ? 0.6168 0.8163 0.7074 -0.1285 -0.0526 0.0368 311 LEU A CD2 2477 N N . VAL A 312 ? 0.5438 0.7254 0.7019 -0.0689 -0.0356 0.0248 312 VAL A N 2478 C CA . VAL A 312 ? 0.5197 0.7177 0.7023 -0.0611 -0.0264 0.0226 312 VAL A CA 2479 C C . VAL A 312 ? 0.5073 0.7056 0.6860 -0.0700 -0.0193 0.0279 312 VAL A C 2480 O O . VAL A 312 ? 0.5334 0.7117 0.6836 -0.0780 -0.0231 0.0328 312 VAL A O 2481 C CB . VAL A 312 ? 0.5348 0.7251 0.7092 -0.0423 -0.0297 0.0191 312 VAL A CB 2482 C CG1 . VAL A 312 ? 0.5121 0.7288 0.7117 -0.0394 -0.0190 0.0174 312 VAL A CG1 2483 C CG2 . VAL A 312 ? 0.5425 0.7455 0.7194 -0.0272 -0.0381 0.0136 312 VAL A CG2 2484 N N . LEU A 313 ? 0.4810 0.6965 0.6791 -0.0696 -0.0106 0.0270 313 LEU A N 2485 C CA . LEU A 313 ? 0.4792 0.7011 0.6741 -0.0717 -0.0041 0.0314 313 LEU A CA 2486 C C . LEU A 313 ? 0.4827 0.6975 0.6841 -0.0687 0.0017 0.0309 313 LEU A C 2487 O O . LEU A 313 ? 0.4870 0.7043 0.7015 -0.0669 0.0051 0.0267 313 LEU A O 2488 C CB . LEU A 313 ? 0.4701 0.7013 0.6667 -0.0646 0.0003 0.0299 313 LEU A CB 2489 C CG . LEU A 313 ? 0.4842 0.7380 0.6713 -0.0619 -0.0022 0.0312 313 LEU A CG 2490 C CD1 . LEU A 313 ? 0.4976 0.7446 0.6732 -0.0433 0.0011 0.0271 313 LEU A CD1 2491 C CD2 . LEU A 313 ? 0.4870 0.7745 0.6651 -0.0701 -0.0023 0.0383 313 LEU A CD2 2492 N N . ALA A 314 ? 0.4850 0.6949 0.6740 -0.0726 0.0029 0.0358 314 ALA A N 2493 C CA . ALA A 314 ? 0.4753 0.6804 0.6690 -0.0696 0.0099 0.0360 314 ALA A CA 2494 C C . ALA A 314 ? 0.4647 0.6756 0.6644 -0.0668 0.0166 0.0359 314 ALA A C 2495 O O . ALA A 314 ? 0.4832 0.7056 0.6752 -0.0625 0.0161 0.0384 314 ALA A O 2496 C CB . ALA A 314 ? 0.4809 0.6737 0.6523 -0.0768 0.0084 0.0417 314 ALA A CB 2497 N N . THR A 315 ? 0.4696 0.6727 0.6750 -0.0681 0.0218 0.0330 315 THR A N 2498 C CA . THR A 315 ? 0.4954 0.6816 0.6870 -0.0673 0.0267 0.0337 315 THR A CA 2499 C C . THR A 315 ? 0.4907 0.6735 0.6822 -0.0707 0.0325 0.0360 315 THR A C 2500 O O . THR A 315 ? 0.4984 0.6725 0.6762 -0.0649 0.0345 0.0396 315 THR A O 2501 C CB . THR A 315 ? 0.5197 0.6876 0.7014 -0.0779 0.0268 0.0295 315 THR A CB 2502 O OG1 . THR A 315 ? 0.5201 0.7141 0.7227 -0.0902 0.0278 0.0266 315 THR A OG1 2503 C CG2 . THR A 315 ? 0.5374 0.6962 0.7082 -0.0725 0.0212 0.0271 315 THR A CG2 2504 N N . GLY A 316 ? 0.4757 0.6707 0.6804 -0.0765 0.0349 0.0335 316 GLY A N 2505 C CA . GLY A 316 ? 0.4870 0.6819 0.6906 -0.0780 0.0409 0.0349 316 GLY A CA 2506 C C . GLY A 316 ? 0.4899 0.6791 0.6858 -0.0709 0.0386 0.0386 316 GLY A C 2507 O O . GLY A 316 ? 0.4917 0.6788 0.6797 -0.0704 0.0324 0.0417 316 GLY A O 2508 N N . LEU A 317 ? 0.4993 0.6854 0.6906 -0.0696 0.0432 0.0386 317 LEU A N 2509 C CA . LEU A 317 ? 0.5249 0.6916 0.6945 -0.0677 0.0402 0.0426 317 LEU A CA 2510 C C . LEU A 317 ? 0.5316 0.6865 0.6855 -0.0536 0.0366 0.0380 317 LEU A C 2511 O O . LEU A 317 ? 0.5167 0.6947 0.6850 -0.0415 0.0376 0.0315 317 LEU A O 2512 C CB . LEU A 317 ? 0.5426 0.7016 0.7049 -0.0724 0.0466 0.0463 317 LEU A CB 2513 C CG . LEU A 317 ? 0.5504 0.7204 0.7242 -0.0734 0.0560 0.0426 317 LEU A CG 2514 C CD1 . LEU A 317 ? 0.5718 0.7329 0.7320 -0.0697 0.0608 0.0427 317 LEU A CD1 2515 C CD2 . LEU A 317 ? 0.5687 0.7309 0.7403 -0.0824 0.0587 0.0456 317 LEU A CD2 2516 N N . ARG A 318 ? 0.5628 0.6799 0.6781 -0.0548 0.0310 0.0416 318 ARG A N 2517 C CA . ARG A 318 ? 0.6153 0.6952 0.6898 -0.0359 0.0245 0.0374 318 ARG A CA 2518 C C . ARG A 318 ? 0.6230 0.7249 0.7073 -0.0123 0.0332 0.0302 318 ARG A C 2519 O O . ARG A 318 ? 0.6222 0.7238 0.7059 -0.0171 0.0406 0.0320 318 ARG A O 2520 C CB . ARG A 318 ? 0.6706 0.6920 0.6865 -0.0514 0.0162 0.0443 318 ARG A CB 2521 C CG . ARG A 318 ? 0.7633 0.7153 0.7084 -0.0305 0.0063 0.0404 318 ARG A CG 2522 C CD . ARG A 318 ? 0.8393 0.7234 0.7138 -0.0588 -0.0030 0.0490 318 ARG A CD 2523 N NE . ARG A 318 ? 0.8600 0.7265 0.7065 -0.0932 -0.0147 0.0568 318 ARG A NE 2524 C CZ . ARG A 318 ? 0.9542 0.7447 0.7234 -0.0959 -0.0301 0.0571 318 ARG A CZ 2525 N NH1 . ARG A 318 ? 1.0244 0.7433 0.7320 -0.0571 -0.0367 0.0491 318 ARG A NH1 2526 N NH2 . ARG A 318 ? 0.9724 0.7581 0.7183 -0.1357 -0.0397 0.0654 318 ARG A NH2 2527 N N . ASN A 319 ? 0.6386 0.7685 0.7316 0.0132 0.0322 0.0222 319 ASN A N 2528 C CA . ASN A 319 ? 0.6601 0.8395 0.7676 0.0374 0.0408 0.0145 319 ASN A CA 2529 C C . ASN A 319 ? 0.7685 0.9047 0.8175 0.0744 0.0368 0.0096 319 ASN A C 2530 O O . ASN A 319 ? 0.8456 0.9149 0.8366 0.0927 0.0236 0.0087 319 ASN A O 2531 C CB . ASN A 319 ? 0.6279 0.8727 0.7683 0.0498 0.0403 0.0081 319 ASN A CB 2532 C CG . ASN A 319 ? 0.6051 0.9324 0.7693 0.0658 0.0504 0.0012 319 ASN A CG 2533 O OD1 . ASN A 319 ? 0.5944 0.9365 0.7639 0.0563 0.0604 0.0022 319 ASN A OD1 2534 N ND2 . ASN A 319 ? 0.6041 0.9948 0.7824 0.0888 0.0476 -0.0056 319 ASN A ND2 2535 N N . SER A 320 ? 0.8345 1.0037 0.8901 0.0858 0.0474 0.0061 320 SER A N 2536 C CA . SER A 320 ? 0.9486 1.0703 0.9418 0.1222 0.0452 0.0013 320 SER A CA 2537 C C . SER A 320 ? 1.0101 1.1753 0.9855 0.1819 0.0437 -0.0112 320 SER A C 2538 O O . SER A 320 ? 0.9413 1.2103 0.9729 0.1865 0.0505 -0.0158 320 SER A O 2539 C CB . SER A 320 ? 0.9288 1.0667 0.9357 0.1060 0.0581 0.0038 320 SER A CB 2540 O OG . SER A 320 ? 0.8955 1.0204 0.9309 0.0566 0.0604 0.0143 320 SER A OG 2541 N N . PRO A 321 ? 1.1391 1.2237 1.0272 0.2286 0.0333 -0.0168 321 PRO A N 2542 C CA . PRO A 321 ? 1.2026 1.3212 1.0558 0.3012 0.0307 -0.0302 321 PRO A CA 2543 C C . PRO A 321 ? 1.1653 1.4223 1.0772 0.3189 0.0484 -0.0374 321 PRO A C 2544 O O . PRO A 321 ? 1.1456 1.4110 1.0661 0.3019 0.0599 -0.0353 321 PRO A O 2545 C CB . PRO A 321 ? 1.3197 1.3009 1.0543 0.3364 0.0186 -0.0327 321 PRO A CB 2546 C CG . PRO A 321 ? 1.3360 1.2049 1.0353 0.2800 0.0072 -0.0200 321 PRO A CG 2547 C CD . PRO A 321 ? 1.2185 1.1644 1.0218 0.2137 0.0196 -0.0100 321 PRO A CD 2548 N N . GLY B 1 ? 0.6449 0.4772 0.6868 -0.0344 0.2119 0.0404 1 GLY B N 2549 C CA . GLY B 1 ? 0.5989 0.4633 0.6572 -0.0390 0.1692 0.0367 1 GLY B CA 2550 C C . GLY B 1 ? 0.5875 0.4526 0.6400 -0.0754 0.1625 0.0089 1 GLY B C 2551 O O . GLY B 1 ? 0.6118 0.4628 0.6465 -0.1048 0.1830 -0.0094 1 GLY B O 2552 N N . LEU B 2 ? 0.5373 0.4258 0.6049 -0.0746 0.1337 0.0058 2 LEU B N 2553 C CA . LEU B 2 ? 0.5202 0.4232 0.5885 -0.1035 0.1279 -0.0170 2 LEU B CA 2554 C C . LEU B 2 ? 0.5150 0.4528 0.5838 -0.1324 0.1066 -0.0262 2 LEU B C 2555 O O . LEU B 2 ? 0.5312 0.4817 0.5908 -0.1648 0.1162 -0.0475 2 LEU B O 2556 C CB . LEU B 2 ? 0.4837 0.4098 0.5722 -0.0903 0.1008 -0.0148 2 LEU B CB 2557 C CG . LEU B 2 ? 0.4903 0.3865 0.5723 -0.0746 0.1264 -0.0147 2 LEU B CG 2558 C CD1 . LEU B 2 ? 0.4572 0.3781 0.5582 -0.0634 0.0998 -0.0146 2 LEU B CD1 2559 C CD2 . LEU B 2 ? 0.5349 0.4014 0.5967 -0.1003 0.1682 -0.0363 2 LEU B CD2 2560 N N . PHE B 3 ? 0.4839 0.4397 0.5602 -0.1238 0.0796 -0.0100 3 PHE B N 2561 C CA . PHE B 3 ? 0.4790 0.4706 0.5555 -0.1458 0.0533 -0.0123 3 PHE B CA 2562 C C . PHE B 3 ? 0.5052 0.4875 0.5598 -0.1669 0.0720 -0.0170 3 PHE B C 2563 O O . PHE B 3 ? 0.5183 0.5307 0.5662 -0.1897 0.0545 -0.0199 3 PHE B O 2564 C CB . PHE B 3 ? 0.4473 0.4599 0.5418 -0.1268 0.0121 0.0069 3 PHE B CB 2565 C CG . PHE B 3 ? 0.4299 0.4536 0.5425 -0.1123 -0.0034 0.0062 3 PHE B CG 2566 C CD1 . PHE B 3 ? 0.4200 0.4806 0.5425 -0.1223 -0.0198 0.0004 3 PHE B CD1 2567 C CD2 . PHE B 3 ? 0.4242 0.4266 0.5431 -0.0891 0.0026 0.0107 3 PHE B CD2 2568 C CE1 . PHE B 3 ? 0.4128 0.4853 0.5543 -0.1067 -0.0289 -0.0009 3 PHE B CE1 2569 C CE2 . PHE B 3 ? 0.4066 0.4161 0.5393 -0.0776 -0.0065 0.0070 3 PHE B CE2 2570 C CZ . PHE B 3 ? 0.4028 0.4455 0.5482 -0.0854 -0.0210 0.0007 3 PHE B CZ 2571 N N . GLY B 4 ? 0.5321 0.4731 0.5740 -0.1575 0.1098 -0.0164 4 GLY B N 2572 C CA . GLY B 4 ? 0.5667 0.4878 0.5840 -0.1772 0.1401 -0.0253 4 GLY B CA 2573 C C . GLY B 4 ? 0.5552 0.4926 0.5748 -0.1730 0.1247 -0.0096 4 GLY B C 2574 O O . GLY B 4 ? 0.5875 0.5101 0.5858 -0.1906 0.1508 -0.0179 4 GLY B O 2575 N N . ALA B 5 ? 0.5185 0.4832 0.5602 -0.1538 0.0862 0.0108 5 ALA B N 2576 C CA . ALA B 5 ? 0.5105 0.4934 0.5524 -0.1569 0.0703 0.0241 5 ALA B CA 2577 C C . ALA B 5 ? 0.5109 0.4868 0.5628 -0.1301 0.0897 0.0398 5 ALA B C 2578 O O . ALA B 5 ? 0.5251 0.4915 0.5664 -0.1336 0.1180 0.0390 5 ALA B O 2579 C CB . ALA B 5 ? 0.4820 0.4924 0.5360 -0.1559 0.0236 0.0368 5 ALA B CB 2580 N N . ILE B 6 ? 0.4983 0.4839 0.5703 -0.1033 0.0759 0.0540 6 ILE B N 2581 C CA . ILE B 6 ? 0.5103 0.5099 0.5963 -0.0757 0.0880 0.0732 6 ILE B CA 2582 C C . ILE B 6 ? 0.5460 0.5137 0.6243 -0.0555 0.1384 0.0741 6 ILE B C 2583 O O . ILE B 6 ? 0.5531 0.4872 0.6225 -0.0496 0.1575 0.0656 6 ILE B O 2584 C CB . ILE B 6 ? 0.4873 0.5096 0.5909 -0.0564 0.0620 0.0859 6 ILE B CB 2585 C CG1 . ILE B 6 ? 0.4751 0.5228 0.5832 -0.0737 0.0219 0.0891 6 ILE B CG1 2586 C CG2 . ILE B 6 ? 0.4986 0.5445 0.6156 -0.0246 0.0800 0.1069 6 ILE B CG2 2587 C CD1 . ILE B 6 ? 0.4661 0.5236 0.5821 -0.0661 -0.0037 0.0925 6 ILE B CD1 2588 N N . ALA B 7 ? 0.5656 0.5414 0.6463 -0.0439 0.1629 0.0852 7 ALA B N 2589 C CA . ALA B 7 ? 0.6258 0.5617 0.6956 -0.0212 0.2190 0.0882 7 ALA B CA 2590 C C . ALA B 7 ? 0.6695 0.5449 0.7067 -0.0494 0.2482 0.0589 7 ALA B C 2591 O O . ALA B 7 ? 0.7141 0.5398 0.7366 -0.0352 0.2887 0.0559 7 ALA B O 2592 C CB . ALA B 7 ? 0.6328 0.5729 0.7166 0.0228 0.2304 0.1117 7 ALA B CB 2593 N N . GLY B 8 ? 0.6710 0.5545 0.6948 -0.0914 0.2272 0.0382 8 GLY B N 2594 C CA . GLY B 8 ? 0.7180 0.5656 0.7113 -0.1284 0.2461 0.0078 8 GLY B CA 2595 C C . GLY B 8 ? 0.7578 0.6073 0.7281 -0.1635 0.2551 -0.0075 8 GLY B C 2596 O O . GLY B 8 ? 0.8357 0.6599 0.7950 -0.1551 0.2957 -0.0059 8 GLY B O 2597 N N . PHE B 9 ? 0.7349 0.6165 0.6968 -0.2006 0.2194 -0.0203 9 PHE B N 2598 C CA . PHE B 9 ? 0.7452 0.6379 0.6833 -0.2347 0.2220 -0.0313 9 PHE B CA 2599 C C . PHE B 9 ? 0.7305 0.6548 0.6886 -0.2165 0.2004 -0.0065 9 PHE B C 2600 O O . PHE B 9 ? 0.7809 0.7031 0.7229 -0.2302 0.2197 -0.0100 9 PHE B O 2601 C CB . PHE B 9 ? 0.7384 0.6642 0.6586 -0.2787 0.1920 -0.0487 9 PHE B CB 2602 C CG . PHE B 9 ? 0.6841 0.6601 0.6298 -0.2696 0.1319 -0.0289 9 PHE B CG 2603 C CD1 . PHE B 9 ? 0.6725 0.6786 0.6183 -0.2746 0.1013 -0.0125 9 PHE B CD1 2604 C CD2 . PHE B 9 ? 0.6564 0.6438 0.6218 -0.2572 0.1103 -0.0271 9 PHE B CD2 2605 C CE1 . PHE B 9 ? 0.6370 0.6749 0.6003 -0.2648 0.0531 0.0065 9 PHE B CE1 2606 C CE2 . PHE B 9 ? 0.6283 0.6525 0.6143 -0.2459 0.0614 -0.0088 9 PHE B CE2 2607 C CZ . PHE B 9 ? 0.6110 0.6562 0.5946 -0.2488 0.0342 0.0084 9 PHE B CZ 2608 N N . ILE B 10 ? 0.6894 0.6427 0.6797 -0.1895 0.1633 0.0162 10 ILE B N 2609 C CA . ILE B 10 ? 0.6808 0.6635 0.6912 -0.1723 0.1513 0.0384 10 ILE B CA 2610 C C . ILE B 10 ? 0.7021 0.6766 0.7325 -0.1312 0.1832 0.0525 10 ILE B C 2611 O O . ILE B 10 ? 0.6729 0.6518 0.7221 -0.1055 0.1725 0.0631 10 ILE B O 2612 C CB . ILE B 10 ? 0.6297 0.6471 0.6593 -0.1697 0.0988 0.0540 10 ILE B CB 2613 C CG1 . ILE B 10 ? 0.6340 0.6586 0.6443 -0.2014 0.0679 0.0466 10 ILE B CG1 2614 C CG2 . ILE B 10 ? 0.6109 0.6605 0.6563 -0.1619 0.0917 0.0723 10 ILE B CG2 2615 C CD1 . ILE B 10 ? 0.6074 0.6470 0.6319 -0.1942 0.0240 0.0601 10 ILE B CD1 2616 N N . GLU B 11 ? 0.7591 0.7245 0.7846 -0.1230 0.2236 0.0545 11 GLU B N 2617 C CA . GLU B 11 ? 0.7956 0.7439 0.8337 -0.0796 0.2672 0.0687 11 GLU B CA 2618 C C . GLU B 11 ? 0.7454 0.7492 0.8230 -0.0411 0.2458 0.0997 11 GLU B C 2619 O O . GLU B 11 ? 0.7513 0.7461 0.8398 -0.0025 0.2668 0.1150 11 GLU B O 2620 C CB . GLU B 11 ? 0.8802 0.8083 0.9051 -0.0770 0.3183 0.0652 11 GLU B CB 2621 C CG . GLU B 11 ? 0.9762 0.8320 0.9560 -0.1052 0.3641 0.0339 11 GLU B CG 2622 C CD . GLU B 11 ? 1.0761 0.8988 1.0433 -0.0900 0.4276 0.0334 11 GLU B CD 2623 O OE1 . GLU B 11 ? 1.0653 0.9315 1.0459 -0.0905 0.4220 0.0430 11 GLU B OE1 2624 O OE2 . GLU B 11 ? 1.1364 0.8872 1.0797 -0.0768 0.4859 0.0239 11 GLU B OE2 2625 N N . GLY B 12 ? 0.6859 0.7473 0.7810 -0.0537 0.2070 0.1092 12 GLY B N 2626 C CA . GLY B 12 ? 0.6502 0.7772 0.7804 -0.0270 0.1872 0.1354 12 GLY B CA 2627 C C . GLY B 12 ? 0.6105 0.7835 0.7490 -0.0557 0.1362 0.1367 12 GLY B C 2628 O O . GLY B 12 ? 0.6038 0.7633 0.7235 -0.0920 0.1193 0.1234 12 GLY B O 2629 N N . GLY B 13 ? 0.5772 0.8031 0.7399 -0.0404 0.1138 0.1534 13 GLY B N 2630 C CA . GLY B 13 ? 0.5577 0.8223 0.7247 -0.0694 0.0721 0.1535 13 GLY B CA 2631 C C . GLY B 13 ? 0.5619 0.8793 0.7402 -0.0849 0.0752 0.1606 13 GLY B C 2632 O O . GLY B 13 ? 0.5813 0.9126 0.7688 -0.0680 0.1097 0.1675 13 GLY B O 2633 N N . TRP B 14 ? 0.5448 0.8870 0.7200 -0.1183 0.0426 0.1581 14 TRP B N 2634 C CA . TRP B 14 ? 0.5409 0.9292 0.7217 -0.1434 0.0426 0.1616 14 TRP B CA 2635 C C . TRP B 14 ? 0.5493 1.0222 0.7549 -0.1489 0.0253 0.1728 14 TRP B C 2636 O O . TRP B 14 ? 0.5476 1.0156 0.7417 -0.1733 -0.0037 0.1659 14 TRP B O 2637 C CB . TRP B 14 ? 0.5335 0.8728 0.6807 -0.1865 0.0225 0.1482 14 TRP B CB 2638 C CG . TRP B 14 ? 0.5414 0.8199 0.6625 -0.1906 0.0382 0.1378 14 TRP B CG 2639 C CD1 . TRP B 14 ? 0.5444 0.8134 0.6668 -0.1721 0.0749 0.1356 14 TRP B CD1 2640 C CD2 . TRP B 14 ? 0.5435 0.7668 0.6302 -0.2172 0.0194 0.1284 14 TRP B CD2 2641 N NE1 . TRP B 14 ? 0.5612 0.7763 0.6499 -0.1923 0.0785 0.1215 14 TRP B NE1 2642 C CE2 . TRP B 14 ? 0.5587 0.7520 0.6275 -0.2178 0.0426 0.1194 14 TRP B CE2 2643 C CE3 . TRP B 14 ? 0.5437 0.7401 0.6113 -0.2391 -0.0120 0.1282 14 TRP B CE3 2644 C CZ2 . TRP B 14 ? 0.5761 0.7286 0.6112 -0.2405 0.0300 0.1117 14 TRP B CZ2 2645 C CZ3 . TRP B 14 ? 0.5596 0.7094 0.5959 -0.2542 -0.0220 0.1246 14 TRP B CZ3 2646 C CH2 . TRP B 14 ? 0.5731 0.7089 0.5948 -0.2553 -0.0036 0.1172 14 TRP B CH2 2647 N N . GLN B 15 ? 0.5823 1.1363 0.8209 -0.1275 0.0451 0.1898 15 GLN B N 2648 C CA . GLN B 15 ? 0.6028 1.2601 0.8668 -0.1410 0.0283 0.2001 15 GLN B CA 2649 C C . GLN B 15 ? 0.6214 1.2789 0.8655 -0.2009 0.0086 0.1855 15 GLN B C 2650 O O . GLN B 15 ? 0.6424 1.3499 0.8879 -0.2314 -0.0134 0.1824 15 GLN B O 2651 C CB . GLN B 15 ? 0.6163 1.3720 0.9231 -0.1059 0.0560 0.2241 15 GLN B CB 2652 C CG . GLN B 15 ? 0.6353 1.3932 0.9613 -0.0409 0.0832 0.2451 15 GLN B CG 2653 C CD . GLN B 15 ? 0.6367 1.4571 0.9786 -0.0205 0.0629 0.2609 15 GLN B CD 2654 O OE1 . GLN B 15 ? 0.6685 1.4255 0.9907 -0.0086 0.0551 0.2556 15 GLN B OE1 2655 N NE2 . GLN B 15 ? 0.6019 1.5539 0.9790 -0.0181 0.0546 0.2805 15 GLN B NE2 2656 N N . GLY B 16 ? 0.6338 1.2333 0.8548 -0.2201 0.0193 0.1763 16 GLY B N 2657 C CA . GLY B 16 ? 0.6505 1.2390 0.8472 -0.2745 0.0067 0.1660 16 GLY B CA 2658 C C . GLY B 16 ? 0.6648 1.1759 0.8214 -0.3074 -0.0205 0.1524 16 GLY B C 2659 O O . GLY B 16 ? 0.7062 1.2030 0.8387 -0.3526 -0.0283 0.1459 16 GLY B O 2660 N N . MET B 17 ? 0.6357 1.0930 0.7833 -0.2849 -0.0315 0.1487 17 MET B N 2661 C CA . MET B 17 ? 0.6535 1.0383 0.7661 -0.3093 -0.0536 0.1378 17 MET B CA 2662 C C . MET B 17 ? 0.6451 1.0590 0.7635 -0.3144 -0.0694 0.1330 17 MET B C 2663 O O . MET B 17 ? 0.6342 1.0406 0.7620 -0.2829 -0.0731 0.1338 17 MET B O 2664 C CB . MET B 17 ? 0.6524 0.9541 0.7465 -0.2862 -0.0554 0.1350 17 MET B CB 2665 C CG . MET B 17 ? 0.6900 0.9171 0.7493 -0.3058 -0.0743 0.1283 17 MET B CG 2666 S SD . MET B 17 ? 0.6858 0.8367 0.7271 -0.2815 -0.0777 0.1284 17 MET B SD 2667 C CE . MET B 17 ? 0.6632 0.8422 0.7372 -0.2385 -0.0695 0.1260 17 MET B CE 2668 N N . VAL B 18 ? 0.6770 1.1208 0.7847 -0.3592 -0.0770 0.1260 18 VAL B N 2669 C CA . VAL B 18 ? 0.6762 1.1639 0.7861 -0.3749 -0.0899 0.1183 18 VAL B CA 2670 C C . VAL B 18 ? 0.7174 1.1149 0.7824 -0.4062 -0.1005 0.1010 18 VAL B C 2671 O O . VAL B 18 ? 0.7234 1.1324 0.7822 -0.4146 -0.1094 0.0909 18 VAL B O 2672 C CB . VAL B 18 ? 0.6846 1.2879 0.8152 -0.4082 -0.0882 0.1197 18 VAL B CB 2673 C CG1 . VAL B 18 ? 0.6537 1.3416 0.8301 -0.3705 -0.0724 0.1400 18 VAL B CG1 2674 C CG2 . VAL B 18 ? 0.7383 1.3121 0.8361 -0.4693 -0.0854 0.1073 18 VAL B CG2 2675 N N . ASP B 19 ? 0.7624 1.0685 0.7939 -0.4208 -0.0971 0.0991 19 ASP B N 2676 C CA . ASP B 19 ? 0.8322 1.0423 0.8185 -0.4458 -0.1005 0.0868 19 ASP B CA 2677 C C . ASP B 19 ? 0.8056 0.9444 0.7863 -0.4049 -0.1068 0.0869 19 ASP B C 2678 O O . ASP B 19 ? 0.8519 0.9076 0.7979 -0.4157 -0.1066 0.0790 19 ASP B O 2679 C CB . ASP B 19 ? 0.9114 1.0544 0.8600 -0.4787 -0.0916 0.0896 19 ASP B CB 2680 C CG . ASP B 19 ? 0.9103 1.0494 0.8691 -0.4535 -0.0872 0.1067 19 ASP B CG 2681 O OD1 . ASP B 19 ? 0.8625 1.0432 0.8555 -0.4133 -0.0878 0.1136 19 ASP B OD1 2682 O OD2 . ASP B 19 ? 0.9876 1.0776 0.9150 -0.4766 -0.0805 0.1127 19 ASP B OD2 2683 N N . GLY B 20 ? 0.7300 0.8987 0.7432 -0.3587 -0.1087 0.0956 20 GLY B N 2684 C CA . GLY B 20 ? 0.7124 0.8238 0.7231 -0.3234 -0.1135 0.0944 20 GLY B CA 2685 C C . GLY B 20 ? 0.6510 0.8013 0.6959 -0.2791 -0.1111 0.1015 20 GLY B C 2686 O O . GLY B 20 ? 0.6228 0.8398 0.6938 -0.2697 -0.1032 0.1097 20 GLY B O 2687 N N . TRP B 21 ? 0.6354 0.7415 0.6792 -0.2514 -0.1142 0.0988 21 TRP B N 2688 C CA . TRP B 21 ? 0.5911 0.7207 0.6608 -0.2133 -0.1075 0.1035 21 TRP B CA 2689 C C . TRP B 21 ? 0.5661 0.6729 0.6370 -0.2005 -0.0999 0.1090 21 TRP B C 2690 O O . TRP B 21 ? 0.5362 0.6721 0.6255 -0.1809 -0.0856 0.1133 21 TRP B O 2691 C CB . TRP B 21 ? 0.5890 0.6914 0.6581 -0.1928 -0.1117 0.0959 21 TRP B CB 2692 C CG . TRP B 21 ? 0.5907 0.7435 0.6690 -0.1905 -0.1132 0.0935 21 TRP B CG 2693 C CD1 . TRP B 21 ? 0.5760 0.8074 0.6756 -0.1840 -0.1081 0.1038 21 TRP B CD1 2694 C CD2 . TRP B 21 ? 0.6152 0.7480 0.6804 -0.1926 -0.1194 0.0819 21 TRP B CD2 2695 N NE1 . TRP B 21 ? 0.5774 0.8453 0.6768 -0.1833 -0.1139 0.1011 21 TRP B NE1 2696 C CE2 . TRP B 21 ? 0.6039 0.8091 0.6802 -0.1911 -0.1203 0.0854 21 TRP B CE2 2697 C CE3 . TRP B 21 ? 0.6543 0.7172 0.6989 -0.1937 -0.1225 0.0700 21 TRP B CE3 2698 C CZ2 . TRP B 21 ? 0.6377 0.8465 0.7011 -0.1959 -0.1254 0.0749 21 TRP B CZ2 2699 C CZ3 . TRP B 21 ? 0.6782 0.7378 0.7115 -0.1968 -0.1241 0.0580 21 TRP B CZ3 2700 C CH2 . TRP B 21 ? 0.6724 0.8041 0.7130 -0.2005 -0.1262 0.0592 21 TRP B CH2 2701 N N . TYR B 22 ? 0.5681 0.6228 0.6164 -0.2118 -0.1071 0.1098 22 TYR B N 2702 C CA . TYR B 22 ? 0.5604 0.6000 0.6040 -0.2056 -0.1032 0.1146 22 TYR B CA 2703 C C . TYR B 22 ? 0.5877 0.6066 0.6063 -0.2320 -0.1071 0.1224 22 TYR B C 2704 O O . TYR B 22 ? 0.6193 0.6040 0.6173 -0.2487 -0.1144 0.1240 22 TYR B O 2705 C CB . TYR B 22 ? 0.5669 0.5705 0.6077 -0.1858 -0.1104 0.1125 22 TYR B CB 2706 C CG . TYR B 22 ? 0.5546 0.5573 0.6096 -0.1656 -0.1109 0.1041 22 TYR B CG 2707 C CD1 . TYR B 22 ? 0.5262 0.5607 0.6014 -0.1491 -0.0980 0.1001 22 TYR B CD1 2708 C CD2 . TYR B 22 ? 0.5832 0.5481 0.6283 -0.1620 -0.1205 0.1013 22 TYR B CD2 2709 C CE1 . TYR B 22 ? 0.5247 0.5580 0.6091 -0.1316 -0.0976 0.0941 22 TYR B CE1 2710 C CE2 . TYR B 22 ? 0.5695 0.5341 0.6251 -0.1455 -0.1193 0.0924 22 TYR B CE2 2711 C CZ . TYR B 22 ? 0.5447 0.5457 0.6195 -0.1315 -0.1093 0.0891 22 TYR B CZ 2712 O OH . TYR B 22 ? 0.5513 0.5525 0.6333 -0.1157 -0.1070 0.0819 22 TYR B OH 2713 N N . GLY B 23 ? 0.5815 0.6135 0.5962 -0.2373 -0.0992 0.1267 23 GLY B N 2714 C CA . GLY B 23 ? 0.6224 0.6334 0.6090 -0.2617 -0.1024 0.1363 23 GLY B CA 2715 C C . GLY B 23 ? 0.6281 0.6567 0.6084 -0.2671 -0.0924 0.1385 23 GLY B C 2716 O O . GLY B 23 ? 0.5976 0.6415 0.5904 -0.2514 -0.0836 0.1311 23 GLY B O 2717 N N . TYR B 24 ? 0.6691 0.6917 0.6255 -0.2930 -0.0908 0.1470 24 TYR B N 2718 C CA . TYR B 24 ? 0.6932 0.7276 0.6332 -0.3050 -0.0815 0.1495 24 TYR B CA 2719 C C . TYR B 24 ? 0.6904 0.7605 0.6362 -0.3248 -0.0624 0.1467 24 TYR B C 2720 O O . TYR B 24 ? 0.6877 0.7666 0.6366 -0.3407 -0.0627 0.1490 24 TYR B O 2721 C CB . TYR B 24 ? 0.7539 0.7511 0.6547 -0.3177 -0.0953 0.1665 24 TYR B CB 2722 C CG . TYR B 24 ? 0.7854 0.7466 0.6811 -0.2961 -0.1140 0.1757 24 TYR B CG 2723 C CD1 . TYR B 24 ? 0.8223 0.7433 0.7141 -0.2935 -0.1198 0.1802 24 TYR B CD1 2724 C CD2 . TYR B 24 ? 0.7969 0.7674 0.6911 -0.2797 -0.1232 0.1788 24 TYR B CD2 2725 C CE1 . TYR B 24 ? 0.8537 0.7376 0.7410 -0.2696 -0.1319 0.1893 24 TYR B CE1 2726 C CE2 . TYR B 24 ? 0.8179 0.7649 0.7127 -0.2556 -0.1389 0.1895 24 TYR B CE2 2727 C CZ . TYR B 24 ? 0.8469 0.7472 0.7388 -0.2477 -0.1420 0.1956 24 TYR B CZ 2728 O OH . TYR B 24 ? 0.8678 0.7402 0.7604 -0.2200 -0.1525 0.2067 24 TYR B OH 2729 N N . HIS B 25 ? 0.6869 0.7796 0.6331 -0.3260 -0.0430 0.1401 25 HIS B N 2730 C CA . HIS B 25 ? 0.6941 0.8178 0.6399 -0.3456 -0.0223 0.1396 25 HIS B CA 2731 C C . HIS B 25 ? 0.7293 0.8393 0.6371 -0.3673 -0.0172 0.1417 25 HIS B C 2732 O O . HIS B 25 ? 0.7468 0.8522 0.6446 -0.3620 -0.0104 0.1332 25 HIS B O 2733 C CB . HIS B 25 ? 0.6645 0.8284 0.6440 -0.3256 0.0057 0.1300 25 HIS B CB 2734 C CG . HIS B 25 ? 0.6867 0.8886 0.6706 -0.3409 0.0301 0.1307 25 HIS B CG 2735 N ND1 . HIS B 25 ? 0.7112 0.9095 0.6753 -0.3512 0.0549 0.1236 25 HIS B ND1 2736 C CD2 . HIS B 25 ? 0.6844 0.9335 0.6896 -0.3506 0.0348 0.1363 25 HIS B CD2 2737 C CE1 . HIS B 25 ? 0.7206 0.9590 0.6959 -0.3621 0.0756 0.1259 25 HIS B CE1 2738 N NE2 . HIS B 25 ? 0.7045 0.9792 0.7070 -0.3619 0.0629 0.1343 25 HIS B NE2 2739 N N . HIS B 26 ? 0.7631 0.8685 0.6465 -0.3958 -0.0189 0.1519 26 HIS B N 2740 C CA . HIS B 26 ? 0.8004 0.8944 0.6412 -0.4195 -0.0155 0.1573 26 HIS B CA 2741 C C . HIS B 26 ? 0.8071 0.9353 0.6494 -0.4386 0.0148 0.1495 26 HIS B C 2742 O O . HIS B 26 ? 0.7866 0.9480 0.6606 -0.4375 0.0275 0.1467 26 HIS B O 2743 C CB . HIS B 26 ? 0.8479 0.9015 0.6513 -0.4366 -0.0366 0.1787 26 HIS B CB 2744 C CG . HIS B 26 ? 0.8747 0.9292 0.6740 -0.4631 -0.0285 0.1837 26 HIS B CG 2745 N ND1 . HIS B 26 ? 0.8735 0.9253 0.6948 -0.4628 -0.0336 0.1819 26 HIS B ND1 2746 C CD2 . HIS B 26 ? 0.9157 0.9764 0.6888 -0.4958 -0.0143 0.1886 26 HIS B CD2 2747 C CE1 . HIS B 26 ? 0.8973 0.9565 0.7071 -0.4965 -0.0229 0.1843 26 HIS B CE1 2748 N NE2 . HIS B 26 ? 0.9249 0.9884 0.7066 -0.5157 -0.0108 0.1893 26 HIS B NE2 2749 N N . SER B 27 ? 0.8341 0.9609 0.6426 -0.4564 0.0274 0.1456 27 SER B N 2750 C CA . SER B 27 ? 0.8580 1.0107 0.6592 -0.4787 0.0578 0.1395 27 SER B CA 2751 C C . SER B 27 ? 0.9068 1.0451 0.6506 -0.5100 0.0593 0.1432 27 SER B C 2752 O O . SER B 27 ? 0.9187 1.0491 0.6384 -0.5110 0.0572 0.1357 27 SER B O 2753 C CB . SER B 27 ? 0.8347 1.0173 0.6722 -0.4576 0.0938 0.1206 27 SER B CB 2754 O OG . SER B 27 ? 0.8707 1.0418 0.6798 -0.4659 0.1167 0.1046 27 SER B OG 2755 N N . ASN B 28 ? 0.9401 1.0792 0.6601 -0.5390 0.0630 0.1547 28 ASN B N 2756 C CA . ASN B 28 ? 0.9993 1.1252 0.6596 -0.5705 0.0624 0.1638 28 ASN B CA 2757 C C . ASN B 28 ? 1.0414 1.1861 0.6902 -0.6015 0.0894 0.1629 28 ASN B C 2758 O O . ASN B 28 ? 1.0166 1.1947 0.7088 -0.5957 0.1113 0.1525 28 ASN B O 2759 C CB . ASN B 28 ? 1.0222 1.1087 0.6472 -0.5710 0.0256 0.1921 28 ASN B CB 2760 C CG . ASN B 28 ? 1.0271 1.0871 0.6577 -0.5761 0.0166 0.2088 28 ASN B CG 2761 O OD1 . ASN B 28 ? 1.0270 1.1063 0.6744 -0.5938 0.0363 0.2020 28 ASN B OD1 2762 N ND2 . ASN B 28 ? 1.0376 1.0541 0.6528 -0.5619 -0.0105 0.2303 28 ASN B ND2 2763 N N . GLU B 29 ? 1.1162 1.2465 0.7076 -0.6334 0.0885 0.1754 29 GLU B N 2764 C CA . GLU B 29 ? 1.1692 1.3184 0.7462 -0.6661 0.1173 0.1728 29 GLU B CA 2765 C C . GLU B 29 ? 1.1714 1.3275 0.7757 -0.6751 0.1183 0.1813 29 GLU B C 2766 O O . GLU B 29 ? 1.1808 1.3755 0.8016 -0.6931 0.1471 0.1721 29 GLU B O 2767 C CB . GLU B 29 ? 1.2512 1.3793 0.7544 -0.7002 0.1132 0.1890 29 GLU B CB 2768 C CG . GLU B 29 ? 1.2816 1.4260 0.7509 -0.7130 0.1306 0.1711 29 GLU B CG 2769 C CD . GLU B 29 ? 1.3671 1.5055 0.7663 -0.7542 0.1364 0.1849 29 GLU B CD 2770 O OE1 . GLU B 29 ? 1.4192 1.5313 0.7731 -0.7591 0.1055 0.2155 29 GLU B OE1 2771 O OE2 . GLU B 29 ? 1.3921 1.5519 0.7812 -0.7793 0.1735 0.1676 29 GLU B OE2 2772 N N . GLN B 30 ? 1.1789 1.3003 0.7866 -0.6651 0.0893 0.1974 30 GLN B N 2773 C CA . GLN B 30 ? 1.1958 1.3132 0.8141 -0.6851 0.0898 0.2044 30 GLN B CA 2774 C C . GLN B 30 ? 1.1203 1.2796 0.8068 -0.6633 0.0897 0.1900 30 GLN B C 2775 O O . GLN B 30 ? 1.1246 1.2847 0.8215 -0.6811 0.0863 0.1925 30 GLN B O 2776 C CB . GLN B 30 ? 1.2718 1.3140 0.8422 -0.6924 0.0649 0.2309 30 GLN B CB 2777 C CG . GLN B 30 ? 1.3629 1.3647 0.8638 -0.7033 0.0578 0.2538 30 GLN B CG 2778 C CD . GLN B 30 ? 1.3844 1.3530 0.8718 -0.6679 0.0271 0.2699 30 GLN B CD 2779 O OE1 . GLN B 30 ? 1.4205 1.4072 0.8884 -0.6597 0.0204 0.2709 30 GLN B OE1 2780 N NE2 . GLN B 30 ? 1.3787 1.3028 0.8761 -0.6488 0.0099 0.2811 30 GLN B NE2 2781 N N . GLY B 31 ? 1.0571 1.2507 0.7857 -0.6276 0.0951 0.1750 31 GLY B N 2782 C CA . GLY B 31 ? 0.9897 1.2271 0.7812 -0.6008 0.0943 0.1654 31 GLY B CA 2783 C C . GLY B 31 ? 0.9437 1.1557 0.7516 -0.5609 0.0731 0.1635 31 GLY B C 2784 O O . GLY B 31 ? 0.9441 1.1085 0.7177 -0.5538 0.0574 0.1691 31 GLY B O 2785 N N . SER B 32 ? 0.8812 1.1328 0.7419 -0.5360 0.0723 0.1568 32 SER B N 2786 C CA . SER B 32 ? 0.8354 1.0707 0.7170 -0.4975 0.0572 0.1533 32 SER B CA 2787 C C . SER B 32 ? 0.8037 1.0563 0.7168 -0.4907 0.0405 0.1547 32 SER B C 2788 O O . SER B 32 ? 0.8068 1.1057 0.7374 -0.5119 0.0469 0.1545 32 SER B O 2789 C CB . SER B 32 ? 0.8087 1.0798 0.7231 -0.4662 0.0843 0.1414 32 SER B CB 2790 O OG . SER B 32 ? 0.7803 1.1214 0.7449 -0.4541 0.1009 0.1407 32 SER B OG 2791 N N . GLY B 33 ? 0.7821 1.0041 0.7022 -0.4638 0.0206 0.1543 33 GLY B N 2792 C CA . GLY B 33 ? 0.7633 1.0003 0.7091 -0.4582 0.0058 0.1530 33 GLY B CA 2793 C C . GLY B 33 ? 0.7371 0.9378 0.6889 -0.4268 -0.0133 0.1516 33 GLY B C 2794 O O . GLY B 33 ? 0.7374 0.8975 0.6724 -0.4099 -0.0189 0.1526 33 GLY B O 2795 N N . TYR B 34 ? 0.7255 0.9478 0.7008 -0.4225 -0.0231 0.1482 34 TYR B N 2796 C CA . TYR B 34 ? 0.7075 0.9006 0.6905 -0.3944 -0.0394 0.1455 34 TYR B CA 2797 C C . TYR B 34 ? 0.7468 0.8752 0.6958 -0.4142 -0.0568 0.1476 34 TYR B C 2798 O O . TYR B 34 ? 0.7895 0.9152 0.7218 -0.4506 -0.0550 0.1470 34 TYR B O 2799 C CB . TYR B 34 ? 0.6680 0.9278 0.6958 -0.3738 -0.0363 0.1410 34 TYR B CB 2800 C CG . TYR B 34 ? 0.6542 0.9682 0.7150 -0.3449 -0.0129 0.1428 34 TYR B CG 2801 C CD1 . TYR B 34 ? 0.6406 0.9306 0.7081 -0.3087 -0.0052 0.1406 34 TYR B CD1 2802 C CD2 . TYR B 34 ? 0.6652 1.0528 0.7496 -0.3540 0.0056 0.1464 34 TYR B CD2 2803 C CE1 . TYR B 34 ? 0.6357 0.9596 0.7269 -0.2819 0.0237 0.1418 34 TYR B CE1 2804 C CE2 . TYR B 34 ? 0.6504 1.0802 0.7640 -0.3218 0.0332 0.1502 34 TYR B CE2 2805 C CZ . TYR B 34 ? 0.6462 1.0372 0.7604 -0.2857 0.0439 0.1478 34 TYR B CZ 2806 O OH . TYR B 34 ? 0.6520 1.0704 0.7891 -0.2537 0.0785 0.1511 34 TYR B OH 2807 N N . ALA B 35 ? 0.7547 0.8288 0.6922 -0.3906 -0.0700 0.1499 35 ALA B N 2808 C CA . ALA B 35 ? 0.8056 0.8113 0.7132 -0.3988 -0.0818 0.1532 35 ALA B CA 2809 C C . ALA B 35 ? 0.7962 0.7850 0.7201 -0.3637 -0.0930 0.1484 35 ALA B C 2810 O O . ALA B 35 ? 0.7936 0.7778 0.7244 -0.3357 -0.0971 0.1517 35 ALA B O 2811 C CB . ALA B 35 ? 0.8546 0.7990 0.7191 -0.4059 -0.0842 0.1698 35 ALA B CB 2812 N N . ALA B 36 ? 0.8205 0.8036 0.7485 -0.3694 -0.0963 0.1387 36 ALA B N 2813 C CA . ALA B 36 ? 0.8078 0.7731 0.7483 -0.3392 -0.1048 0.1331 36 ALA B CA 2814 C C . ALA B 36 ? 0.8585 0.7436 0.7697 -0.3252 -0.1112 0.1433 36 ALA B C 2815 O O . ALA B 36 ? 0.9215 0.7506 0.7961 -0.3454 -0.1076 0.1519 36 ALA B O 2816 C CB . ALA B 36 ? 0.8202 0.8034 0.7667 -0.3549 -0.1051 0.1187 36 ALA B CB 2817 N N . ASP B 37 ? 0.8481 0.7304 0.7758 -0.2893 -0.1185 0.1440 37 ASP B N 2818 C CA . ASP B 37 ? 0.8964 0.7187 0.8073 -0.2669 -0.1249 0.1543 37 ASP B CA 2819 C C . ASP B 37 ? 0.9412 0.7278 0.8493 -0.2644 -0.1223 0.1418 37 ASP B C 2820 O O . ASP B 37 ? 0.8663 0.6840 0.8010 -0.2492 -0.1245 0.1284 37 ASP B O 2821 C CB . ASP B 37 ? 0.8713 0.7235 0.8054 -0.2347 -0.1324 0.1571 37 ASP B CB 2822 C CG . ASP B 37 ? 0.9099 0.7214 0.8332 -0.2080 -0.1403 0.1719 37 ASP B CG 2823 O OD1 . ASP B 37 ? 0.9476 0.7473 0.8498 -0.2067 -0.1450 0.1923 37 ASP B OD1 2824 O OD2 . ASP B 37 ? 0.9105 0.7079 0.8473 -0.1864 -0.1413 0.1647 37 ASP B OD2 2825 N N . LYS B 38 ? 1.0576 0.7740 0.9285 -0.2816 -0.1143 0.1454 38 LYS B N 2826 C CA . LYS B 38 ? 1.1094 0.7825 0.9672 -0.2895 -0.1060 0.1291 38 LYS B CA 2827 C C . LYS B 38 ? 1.1124 0.7598 0.9825 -0.2480 -0.1086 0.1293 38 LYS B C 2828 O O . LYS B 38 ? 1.1044 0.7616 0.9856 -0.2465 -0.1069 0.1105 38 LYS B O 2829 C CB . LYS B 38 ? 1.2176 0.8053 1.0245 -0.3199 -0.0894 0.1322 38 LYS B CB 2830 C CG . LYS B 38 ? 1.2637 0.8795 1.0569 -0.3721 -0.0830 0.1238 38 LYS B CG 2831 C CD . LYS B 38 ? 1.3987 0.9181 1.1347 -0.4076 -0.0613 0.1243 38 LYS B CD 2832 C CE . LYS B 38 ? 1.4333 0.9845 1.1552 -0.4609 -0.0546 0.1195 38 LYS B CE 2833 N NZ . LYS B 38 ? 1.5649 1.0204 1.2268 -0.5066 -0.0283 0.1124 38 LYS B NZ 2834 N N . GLU B 39 ? 1.1341 0.7574 1.0029 -0.2150 -0.1131 0.1515 39 GLU B N 2835 C CA . GLU B 39 ? 1.1313 0.7355 1.0138 -0.1729 -0.1145 0.1557 39 GLU B CA 2836 C C . GLU B 39 ? 1.0123 0.6835 0.9364 -0.1582 -0.1231 0.1388 39 GLU B C 2837 O O . GLU B 39 ? 1.0129 0.6690 0.9428 -0.1484 -0.1174 0.1240 39 GLU B O 2838 C CB . GLU B 39 ? 1.2029 0.8030 1.0836 -0.1419 -0.1223 0.1865 39 GLU B CB 2839 C CG . GLU B 39 ? 1.2595 0.8458 1.1553 -0.0953 -0.1228 0.1971 39 GLU B CG 2840 C CD . GLU B 39 ? 1.2866 0.9045 1.1886 -0.0667 -0.1359 0.2286 39 GLU B CD 2841 O OE1 . GLU B 39 ? 1.3599 0.9369 1.2291 -0.0663 -0.1326 0.2553 39 GLU B OE1 2842 O OE2 . GLU B 39 ? 1.2274 0.9140 1.1645 -0.0471 -0.1488 0.2270 39 GLU B OE2 2843 N N . SER B 40 ? 0.9081 0.6471 0.8567 -0.1579 -0.1329 0.1404 40 SER B N 2844 C CA . SER B 40 ? 0.8320 0.6251 0.8146 -0.1448 -0.1356 0.1260 40 SER B CA 2845 C C . SER B 40 ? 0.8143 0.6216 0.7999 -0.1631 -0.1299 0.1068 40 SER B C 2846 O O . SER B 40 ? 0.8042 0.6211 0.8042 -0.1491 -0.1280 0.0949 40 SER B O 2847 C CB . SER B 40 ? 0.7721 0.6231 0.7725 -0.1456 -0.1398 0.1292 40 SER B CB 2848 O OG . SER B 40 ? 0.7765 0.6419 0.7657 -0.1731 -0.1370 0.1316 40 SER B OG 2849 N N . THR B 41 ? 0.8131 0.6280 0.7843 -0.1955 -0.1271 0.1047 41 THR B N 2850 C CA . THR B 41 ? 0.7860 0.6344 0.7612 -0.2157 -0.1241 0.0891 41 THR B CA 2851 C C . THR B 41 ? 0.8119 0.6153 0.7688 -0.2193 -0.1189 0.0747 41 THR B C 2852 O O . THR B 41 ? 0.7619 0.5952 0.7317 -0.2127 -0.1192 0.0629 41 THR B O 2853 C CB . THR B 41 ? 0.8077 0.6771 0.7694 -0.2548 -0.1215 0.0895 41 THR B CB 2854 O OG1 . THR B 41 ? 0.7930 0.7030 0.7704 -0.2511 -0.1227 0.1013 41 THR B OG1 2855 C CG2 . THR B 41 ? 0.7885 0.7143 0.7581 -0.2758 -0.1209 0.0757 41 THR B CG2 2856 N N . GLN B 42 ? 0.8782 0.6049 0.8014 -0.2291 -0.1110 0.0764 42 GLN B N 2857 C CA . GLN B 42 ? 0.9392 0.6078 0.8369 -0.2360 -0.0991 0.0600 42 GLN B CA 2858 C C . GLN B 42 ? 0.9135 0.5781 0.8316 -0.1960 -0.0995 0.0572 42 GLN B C 2859 O O . GLN B 42 ? 0.9070 0.5682 0.8194 -0.2008 -0.0935 0.0385 42 GLN B O 2860 C CB . GLN B 42 ? 1.0437 0.6143 0.8982 -0.2466 -0.0833 0.0662 42 GLN B CB 2861 C CG . GLN B 42 ? 1.1292 0.6283 0.9472 -0.2640 -0.0630 0.0444 42 GLN B CG 2862 C CD . GLN B 42 ? 1.1583 0.7002 0.9630 -0.3159 -0.0619 0.0178 42 GLN B CD 2863 O OE1 . GLN B 42 ? 1.1525 0.7238 0.9634 -0.3177 -0.0629 -0.0007 42 GLN B OE1 2864 N NE2 . GLN B 42 ? 1.1819 0.7365 0.9686 -0.3598 -0.0603 0.0169 42 GLN B NE2 2865 N N . LYS B 43 ? 0.9000 0.5701 0.8402 -0.1598 -0.1060 0.0749 43 LYS B N 2866 C CA . LYS B 43 ? 0.8938 0.5769 0.8600 -0.1233 -0.1071 0.0728 43 LYS B CA 2867 C C . LYS B 43 ? 0.7954 0.5397 0.7829 -0.1264 -0.1105 0.0579 43 LYS B C 2868 O O . LYS B 43 ? 0.7911 0.5286 0.7819 -0.1143 -0.1046 0.0454 43 LYS B O 2869 C CB . LYS B 43 ? 0.9164 0.6245 0.9064 -0.0939 -0.1166 0.0930 43 LYS B CB 2870 C CG . LYS B 43 ? 1.0079 0.6868 1.0056 -0.0563 -0.1122 0.1015 43 LYS B CG 2871 C CD . LYS B 43 ? 1.0714 0.7795 1.0835 -0.0357 -0.1236 0.1261 43 LYS B CD 2872 C CE . LYS B 43 ? 1.1022 0.8117 1.1337 0.0056 -0.1220 0.1372 43 LYS B CE 2873 N NZ . LYS B 43 ? 1.2070 0.8393 1.2119 0.0248 -0.1093 0.1549 43 LYS B NZ 2874 N N . ALA B 44 ? 0.7282 0.5300 0.7282 -0.1406 -0.1174 0.0611 44 ALA B N 2875 C CA . ALA B 44 ? 0.6721 0.5327 0.6911 -0.1382 -0.1180 0.0540 44 ALA B CA 2876 C C . ALA B 44 ? 0.6935 0.5598 0.6940 -0.1615 -0.1152 0.0389 44 ALA B C 2877 O O . ALA B 44 ? 0.6843 0.5723 0.6909 -0.1516 -0.1131 0.0309 44 ALA B O 2878 C CB . ALA B 44 ? 0.6343 0.5502 0.6700 -0.1433 -0.1208 0.0644 44 ALA B CB 2879 N N . ILE B 45 ? 0.7419 0.5913 0.7163 -0.1964 -0.1143 0.0342 45 ILE B N 2880 C CA . ILE B 45 ? 0.7844 0.6468 0.7361 -0.2285 -0.1115 0.0163 45 ILE B CA 2881 C C . ILE B 45 ? 0.8327 0.6371 0.7643 -0.2213 -0.1010 -0.0003 45 ILE B C 2882 O O . ILE B 45 ? 0.8560 0.6889 0.7798 -0.2314 -0.1000 -0.0143 45 ILE B O 2883 C CB . ILE B 45 ? 0.8309 0.6802 0.7532 -0.2756 -0.1086 0.0104 45 ILE B CB 2884 C CG1 . ILE B 45 ? 0.7887 0.7155 0.7342 -0.2850 -0.1178 0.0246 45 ILE B CG1 2885 C CG2 . ILE B 45 ? 0.8695 0.7239 0.7599 -0.3168 -0.1030 -0.0137 45 ILE B CG2 2886 C CD1 . ILE B 45 ? 0.8360 0.7374 0.7582 -0.3226 -0.1136 0.0254 45 ILE B CD1 2887 N N . ASP B 46 ? 0.8673 0.5949 0.7905 -0.2020 -0.0920 0.0028 46 ASP B N 2888 C CA . ASP B 46 ? 0.9067 0.5751 0.8139 -0.1886 -0.0774 -0.0114 46 ASP B CA 2889 C C . ASP B 46 ? 0.8326 0.5422 0.7703 -0.1553 -0.0812 -0.0114 46 ASP B C 2890 O O . ASP B 46 ? 0.8454 0.5535 0.7707 -0.1598 -0.0737 -0.0287 46 ASP B O 2891 C CB . ASP B 46 ? 0.9713 0.5550 0.8671 -0.1673 -0.0653 -0.0009 46 ASP B CB 2892 C CG . ASP B 46 ? 1.0678 0.5934 0.9240 -0.2018 -0.0551 -0.0014 46 ASP B CG 2893 O OD1 . ASP B 46 ? 1.0878 0.6470 0.9283 -0.2465 -0.0587 -0.0133 46 ASP B OD1 2894 O OD2 . ASP B 46 ? 1.1602 0.6099 1.0003 -0.1848 -0.0422 0.0115 46 ASP B OD2 2895 N N . GLY B 47 ? 0.7541 0.5003 0.7278 -0.1264 -0.0908 0.0062 47 GLY B N 2896 C CA . GLY B 47 ? 0.7143 0.4968 0.7148 -0.0991 -0.0909 0.0058 47 GLY B CA 2897 C C . GLY B 47 ? 0.6950 0.5276 0.6914 -0.1118 -0.0921 -0.0027 47 GLY B C 2898 O O . GLY B 47 ? 0.7066 0.5373 0.6993 -0.1027 -0.0846 -0.0137 47 GLY B O 2899 N N . VAL B 48 ? 0.6658 0.5479 0.6623 -0.1318 -0.1008 0.0043 48 VAL B N 2900 C CA . VAL B 48 ? 0.6297 0.5767 0.6274 -0.1369 -0.1037 0.0052 48 VAL B CA 2901 C C . VAL B 48 ? 0.6726 0.6176 0.6356 -0.1679 -0.1017 -0.0143 48 VAL B C 2902 O O . VAL B 48 ? 0.6663 0.6453 0.6240 -0.1641 -0.1005 -0.0180 48 VAL B O 2903 C CB . VAL B 48 ? 0.6036 0.6120 0.6173 -0.1432 -0.1116 0.0224 48 VAL B CB 2904 C CG1 . VAL B 48 ? 0.6041 0.6887 0.6142 -0.1537 -0.1161 0.0265 48 VAL B CG1 2905 C CG2 . VAL B 48 ? 0.5609 0.5756 0.6045 -0.1116 -0.1077 0.0382 48 VAL B CG2 2906 N N . THR B 49 ? 0.7072 0.6093 0.6420 -0.2010 -0.0989 -0.0276 49 THR B N 2907 C CA . THR B 49 ? 0.7777 0.6669 0.6716 -0.2384 -0.0921 -0.0522 49 THR B CA 2908 C C . THR B 49 ? 0.8161 0.6597 0.6996 -0.2190 -0.0786 -0.0666 49 THR B C 2909 O O . THR B 49 ? 0.8354 0.7161 0.7044 -0.2283 -0.0782 -0.0766 49 THR B O 2910 C CB . THR B 49 ? 0.8366 0.6611 0.6948 -0.2782 -0.0826 -0.0671 49 THR B CB 2911 O OG1 . THR B 49 ? 0.8094 0.6822 0.6771 -0.2998 -0.0941 -0.0548 49 THR B OG1 2912 C CG2 . THR B 49 ? 0.8980 0.7055 0.7079 -0.3238 -0.0710 -0.0976 49 THR B CG2 2913 N N . ASN B 50 ? 0.8390 0.6098 0.7308 -0.1907 -0.0674 -0.0654 50 ASN B N 2914 C CA . ASN B 50 ? 0.8627 0.5902 0.7496 -0.1685 -0.0515 -0.0783 50 ASN B CA 2915 C C . ASN B 50 ? 0.8023 0.5920 0.7096 -0.1479 -0.0568 -0.0729 50 ASN B C 2916 O O . ASN B 50 ? 0.8221 0.6079 0.7089 -0.1529 -0.0469 -0.0892 50 ASN B O 2917 C CB . ASN B 50 ? 0.8690 0.5367 0.7764 -0.1315 -0.0426 -0.0685 50 ASN B CB 2918 C CG . ASN B 50 ? 0.9529 0.5334 0.8283 -0.1455 -0.0268 -0.0754 50 ASN B CG 2919 O OD1 . ASN B 50 ? 1.0249 0.5564 0.8568 -0.1753 -0.0090 -0.0992 50 ASN B OD1 2920 N ND2 . ASN B 50 ? 0.9583 0.5160 0.8508 -0.1253 -0.0306 -0.0543 50 ASN B ND2 2921 N N . LYS B 51 ? 0.7425 0.5840 0.6853 -0.1265 -0.0693 -0.0500 51 LYS B N 2922 C CA . LYS B 51 ? 0.7034 0.5985 0.6633 -0.1059 -0.0706 -0.0400 51 LYS B CA 2923 C C . LYS B 51 ? 0.7159 0.6635 0.6494 -0.1283 -0.0744 -0.0446 51 LYS B C 2924 O O . LYS B 51 ? 0.7193 0.6729 0.6408 -0.1215 -0.0664 -0.0514 51 LYS B O 2925 C CB . LYS B 51 ? 0.6552 0.5898 0.6477 -0.0890 -0.0791 -0.0159 51 LYS B CB 2926 C CG . LYS B 51 ? 0.6367 0.6046 0.6478 -0.0620 -0.0728 -0.0030 51 LYS B CG 2927 C CD . LYS B 51 ? 0.6151 0.6115 0.6507 -0.0510 -0.0759 0.0175 51 LYS B CD 2928 C CE . LYS B 51 ? 0.5970 0.5958 0.6504 -0.0244 -0.0616 0.0263 51 LYS B CE 2929 N NZ . LYS B 51 ? 0.5983 0.5730 0.6730 -0.0170 -0.0586 0.0259 51 LYS B NZ 2930 N N . VAL B 52 ? 0.7142 0.7065 0.6382 -0.1564 -0.0868 -0.0401 52 VAL B N 2931 C CA . VAL B 52 ? 0.7247 0.7872 0.6256 -0.1805 -0.0942 -0.0412 52 VAL B CA 2932 C C . VAL B 52 ? 0.7925 0.8183 0.6492 -0.2092 -0.0835 -0.0723 52 VAL B C 2933 O O . VAL B 52 ? 0.8023 0.8658 0.6420 -0.2094 -0.0823 -0.0741 52 VAL B O 2934 C CB . VAL B 52 ? 0.7286 0.8499 0.6295 -0.2112 -0.1087 -0.0339 52 VAL B CB 2935 C CG1 . VAL B 52 ? 0.7558 0.9582 0.6276 -0.2472 -0.1178 -0.0401 52 VAL B CG1 2936 C CG2 . VAL B 52 ? 0.6716 0.8397 0.6144 -0.1791 -0.1153 -0.0019 52 VAL B CG2 2937 N N . ASN B 53 ? 0.8499 0.7968 0.6846 -0.2318 -0.0722 -0.0958 53 ASN B N 2938 C CA . ASN B 53 ? 0.9276 0.8205 0.7164 -0.2582 -0.0539 -0.1288 53 ASN B CA 2939 C C . ASN B 53 ? 0.9138 0.7730 0.7099 -0.2220 -0.0392 -0.1325 53 ASN B C 2940 O O . ASN B 53 ? 0.9491 0.8145 0.7131 -0.2372 -0.0302 -0.1502 53 ASN B O 2941 C CB . ASN B 53 ? 1.0019 0.7998 0.7648 -0.2826 -0.0372 -0.1499 53 ASN B CB 2942 C CG . ASN B 53 ? 1.0385 0.8642 0.7830 -0.3309 -0.0468 -0.1534 53 ASN B CG 2943 O OD1 . ASN B 53 ? 1.0484 0.9635 0.7812 -0.3635 -0.0615 -0.1543 53 ASN B OD1 2944 N ND2 . ASN B 53 ? 1.0804 0.8339 0.8218 -0.3359 -0.0377 -0.1540 53 ASN B ND2 2945 N N . SER B 54 ? 0.8752 0.7050 0.7124 -0.1776 -0.0363 -0.1167 54 SER B N 2946 C CA . SER B 54 ? 0.8828 0.6912 0.7336 -0.1437 -0.0220 -0.1190 54 SER B CA 2947 C C . SER B 54 ? 0.8639 0.7399 0.7115 -0.1382 -0.0269 -0.1096 54 SER B C 2948 O O . SER B 54 ? 0.8834 0.7468 0.7114 -0.1368 -0.0125 -0.1241 54 SER B O 2949 C CB . SER B 54 ? 0.8372 0.6275 0.7364 -0.1022 -0.0219 -0.1010 54 SER B CB 2950 O OG . SER B 54 ? 0.8830 0.6005 0.7819 -0.0953 -0.0093 -0.1103 54 SER B OG 2951 N N . ILE B 55 ? 0.8378 0.7829 0.7033 -0.1329 -0.0446 -0.0835 55 ILE B N 2952 C CA . ILE B 55 ? 0.8312 0.8436 0.6921 -0.1228 -0.0486 -0.0660 55 ILE B CA 2953 C C . ILE B 55 ? 0.8916 0.9428 0.7045 -0.1593 -0.0516 -0.0806 55 ILE B C 2954 O O . ILE B 55 ? 0.9129 0.9784 0.7051 -0.1544 -0.0435 -0.0826 55 ILE B O 2955 C CB . ILE B 55 ? 0.7878 0.8625 0.6768 -0.1071 -0.0630 -0.0326 55 ILE B CB 2956 C CG1 . ILE B 55 ? 0.7470 0.7889 0.6764 -0.0714 -0.0552 -0.0191 55 ILE B CG1 2957 C CG2 . ILE B 55 ? 0.7988 0.9496 0.6754 -0.0979 -0.0668 -0.0098 55 ILE B CG2 2958 C CD1 . ILE B 55 ? 0.7139 0.7948 0.6698 -0.0595 -0.0641 0.0072 55 ILE B CD1 2959 N N . ILE B 56 ? 0.9241 0.9955 0.7163 -0.1998 -0.0626 -0.0917 56 ILE B N 2960 C CA . ILE B 56 ? 0.9824 1.0975 0.7247 -0.2451 -0.0658 -0.1103 56 ILE B CA 2961 C C . ILE B 56 ? 1.0576 1.1021 0.7612 -0.2587 -0.0422 -0.1452 56 ILE B C 2962 O O . ILE B 56 ? 1.0929 1.1766 0.7620 -0.2730 -0.0403 -0.1517 56 ILE B O 2963 C CB . ILE B 56 ? 1.0148 1.1530 0.7400 -0.2948 -0.0770 -0.1231 56 ILE B CB 2964 C CG1 . ILE B 56 ? 0.9592 1.1969 0.7188 -0.2829 -0.1005 -0.0866 56 ILE B CG1 2965 C CG2 . ILE B 56 ? 1.0911 1.2566 0.7557 -0.3544 -0.0745 -0.1545 56 ILE B CG2 2966 C CD1 . ILE B 56 ? 0.9803 1.2422 0.7347 -0.3270 -0.1108 -0.0955 56 ILE B CD1 2967 N N . ASP B 57 ? 1.1008 1.0443 0.8099 -0.2510 -0.0227 -0.1652 57 ASP B N 2968 C CA . ASP B 57 ? 1.1867 1.0564 0.8587 -0.2628 0.0052 -0.2000 57 ASP B CA 2969 C C . ASP B 57 ? 1.1688 1.0380 0.8527 -0.2257 0.0170 -0.1938 57 ASP B C 2970 O O . ASP B 57 ? 1.2022 1.0659 0.8453 -0.2437 0.0317 -0.2153 57 ASP B O 2971 C CB . ASP B 57 ? 1.2285 0.9909 0.9018 -0.2611 0.0261 -0.2191 57 ASP B CB 2972 C CG . ASP B 57 ? 1.3199 1.0593 0.9523 -0.3161 0.0279 -0.2406 57 ASP B CG 2973 O OD1 . ASP B 57 ? 1.4027 1.1520 0.9786 -0.3668 0.0362 -0.2696 57 ASP B OD1 2974 O OD2 . ASP B 57 ? 1.3081 1.0211 0.9610 -0.3130 0.0222 -0.2298 57 ASP B OD2 2975 N N . LYS B 58 ? 1.1139 0.9908 0.8499 -0.1786 0.0123 -0.1661 58 LYS B N 2976 C CA . LYS B 58 ? 1.1120 0.9917 0.8592 -0.1474 0.0253 -0.1597 58 LYS B CA 2977 C C . LYS B 58 ? 1.1369 1.0867 0.8507 -0.1592 0.0189 -0.1499 58 LYS B C 2978 O O . LYS B 58 ? 1.1760 1.1154 0.8682 -0.1559 0.0362 -0.1607 58 LYS B O 2979 C CB . LYS B 58 ? 1.0431 0.9243 0.8480 -0.1034 0.0221 -0.1330 58 LYS B CB 2980 C CG . LYS B 58 ? 1.0524 0.8700 0.8869 -0.0782 0.0413 -0.1455 58 LYS B CG 2981 C CD . LYS B 58 ? 1.1378 0.8887 0.9426 -0.0956 0.0608 -0.1783 58 LYS B CD 2982 C CE . LYS B 58 ? 1.1420 0.8370 0.9831 -0.0658 0.0747 -0.1813 58 LYS B CE 2983 N NZ . LYS B 58 ? 1.2124 0.8328 1.0209 -0.0767 0.1015 -0.2111 58 LYS B NZ 2984 N N . MET B 59 ? 1.1329 1.1581 0.8416 -0.1726 -0.0048 -0.1284 59 MET B N 2985 C CA . MET B 59 ? 1.1552 1.2629 0.8325 -0.1808 -0.0143 -0.1115 59 MET B CA 2986 C C . MET B 59 ? 1.2376 1.3621 0.8523 -0.2346 -0.0127 -0.1437 59 MET B C 2987 O O . MET B 59 ? 1.2532 1.4362 0.8324 -0.2435 -0.0152 -0.1366 59 MET B O 2988 C CB . MET B 59 ? 1.1079 1.3004 0.8080 -0.1700 -0.0392 -0.0725 59 MET B CB 2989 C CG . MET B 59 ? 1.0434 1.2181 0.7982 -0.1224 -0.0374 -0.0429 59 MET B CG 2990 S SD . MET B 59 ? 1.0370 1.1961 0.8018 -0.0757 -0.0163 -0.0190 59 MET B SD 2991 C CE . MET B 59 ? 1.0788 1.3134 0.7899 -0.0856 -0.0193 -0.0043 59 MET B CE 2992 N N . ASN B 60 ? 1.2973 1.3684 0.8947 -0.2715 -0.0064 -0.1785 60 ASN B N 2993 C CA . ASN B 60 ? 1.3965 1.4600 0.9279 -0.3313 0.0034 -0.2194 60 ASN B CA 2994 C C . ASN B 60 ? 1.4340 1.5010 0.9202 -0.3394 0.0201 -0.2346 60 ASN B C 2995 O O . ASN B 60 ? 1.4507 1.5958 0.8896 -0.3766 0.0092 -0.2377 60 ASN B O 2996 C CB . ASN B 60 ? 1.4563 1.4069 0.9786 -0.3506 0.0271 -0.2571 60 ASN B CB 2997 C CG . ASN B 60 ? 1.5757 1.4977 1.0244 -0.4163 0.0458 -0.3045 60 ASN B CG 2998 O OD1 . ASN B 60 ? 1.6334 1.5104 1.0454 -0.4236 0.0722 -0.3313 60 ASN B OD1 2999 N ND2 . ASN B 60 ? 1.6226 1.5663 1.0468 -0.4678 0.0358 -0.3181 60 ASN B ND2 3000 N N . THR B 61 ? 1.5678 1.2656 1.0511 -0.1989 0.0062 0.3560 61 THR B N 3001 C CA . THR B 61 ? 1.5287 1.1937 1.0409 -0.1586 -0.0012 0.3320 61 THR B CA 3002 C C . THR B 61 ? 1.3799 1.1779 0.9913 -0.1416 -0.0008 0.2951 61 THR B C 3003 O O . THR B 61 ? 1.3599 1.2238 0.9894 -0.1124 -0.0066 0.2926 61 THR B O 3004 C CB . THR B 61 ? 1.6087 1.1922 1.0675 -0.0848 -0.0075 0.3543 61 THR B CB 3005 O OG1 . THR B 61 ? 1.7654 1.2149 1.1077 -0.0882 -0.0042 0.3950 61 THR B OG1 3006 C CG2 . THR B 61 ? 1.6169 1.1339 1.0762 -0.0488 -0.0075 0.3369 61 THR B CG2 3007 N N . GLN B 62 ? 1.3110 1.1397 0.9722 -0.1657 0.0038 0.2694 62 GLN B N 3008 C CA . GLN B 62 ? 1.2045 1.1323 0.9393 -0.1511 0.0086 0.2355 62 GLN B CA 3009 C C . GLN B 62 ? 1.1738 1.0934 0.9488 -0.1567 0.0071 0.2147 62 GLN B C 3010 O O . GLN B 62 ? 1.2801 1.1392 1.0263 -0.1917 0.0034 0.2265 62 GLN B O 3011 C CB . GLN B 62 ? 1.1814 1.1950 0.9261 -0.1728 0.0282 0.2350 62 GLN B CB 3012 C CG . GLN B 62 ? 1.1071 1.1959 0.9066 -0.1656 0.0445 0.2087 62 GLN B CG 3013 C CD . GLN B 62 ? 1.1171 1.2854 0.9081 -0.1641 0.0737 0.2133 62 GLN B CD 3014 O OE1 . GLN B 62 ? 1.1541 1.3239 0.8988 -0.1726 0.0798 0.2311 62 GLN B OE1 3015 N NE2 . GLN B 62 ? 1.0852 1.3202 0.9134 -0.1443 0.0955 0.2007 62 GLN B NE2 3016 N N . PHE B 63 ? 1.0662 1.0357 0.8926 -0.1300 0.0075 0.1855 63 PHE B N 3017 C CA . PHE B 63 ? 1.0158 0.9789 0.8789 -0.1278 0.0047 0.1666 63 PHE B CA 3018 C C . PHE B 63 ? 1.0286 1.0208 0.9059 -0.1727 0.0103 0.1746 63 PHE B C 3019 O O . PHE B 63 ? 1.0413 1.1120 0.9321 -0.1928 0.0250 0.1876 63 PHE B O 3020 C CB . PHE B 63 ? 0.9233 0.9363 0.8290 -0.0995 0.0072 0.1375 63 PHE B CB 3021 C CG . PHE B 63 ? 0.8745 0.8783 0.8142 -0.0919 0.0034 0.1209 63 PHE B CG 3022 C CD1 . PHE B 63 ? 0.8616 0.8131 0.7940 -0.0717 -0.0081 0.1210 63 PHE B CD1 3023 C CD2 . PHE B 63 ? 0.8362 0.8903 0.8106 -0.0973 0.0142 0.1104 63 PHE B CD2 3024 C CE1 . PHE B 63 ? 0.8243 0.7640 0.7791 -0.0653 -0.0103 0.1061 63 PHE B CE1 3025 C CE2 . PHE B 63 ? 0.7954 0.8428 0.7968 -0.0914 0.0086 0.0980 63 PHE B CE2 3026 C CZ . PHE B 63 ? 0.7930 0.7780 0.7823 -0.0799 -0.0045 0.0936 63 PHE B CZ 3027 N N . GLU B 64 ? 1.0395 0.9766 0.9076 -0.1892 -0.0016 0.1714 64 GLU B N 3028 C CA . GLU B 64 ? 1.0409 1.0127 0.9174 -0.2463 -0.0064 0.1837 64 GLU B CA 3029 C C . GLU B 64 ? 0.9861 0.9673 0.8993 -0.2303 -0.0132 0.1611 64 GLU B C 3030 O O . GLU B 64 ? 0.9817 0.8690 0.8651 -0.2032 -0.0211 0.1447 64 GLU B O 3031 C CB . GLU B 64 ? 1.1602 1.0128 0.9427 -0.3076 -0.0219 0.2071 64 GLU B CB 3032 C CG . GLU B 64 ? 1.2389 1.0546 0.9673 -0.3225 -0.0163 0.2333 64 GLU B CG 3033 C CD . GLU B 64 ? 1.4057 1.0699 1.0125 -0.3903 -0.0311 0.2584 64 GLU B CD 3034 O OE1 . GLU B 64 ? 1.4678 1.0673 1.0296 -0.4421 -0.0479 0.2562 64 GLU B OE1 3035 O OE2 . GLU B 64 ? 1.4671 1.0618 1.0068 -0.3958 -0.0273 0.2813 64 GLU B OE2 3036 N N . ALA B 65 ? 0.9212 1.0237 0.8966 -0.2390 -0.0069 0.1653 65 ALA B N 3037 C CA . ALA B 65 ? 0.8784 1.0008 0.8891 -0.2219 -0.0130 0.1482 65 ALA B CA 3038 C C . ALA B 65 ? 0.9402 1.0278 0.9143 -0.2896 -0.0379 0.1610 65 ALA B C 3039 O O . ALA B 65 ? 0.9901 1.0966 0.9341 -0.3616 -0.0486 0.1911 65 ALA B O 3040 C CB . ALA B 65 ? 0.8092 1.0683 0.8893 -0.1853 0.0076 0.1511 65 ALA B CB 3041 N N . VAL B 66 ? 0.9365 0.9661 0.9002 -0.2738 -0.0484 0.1394 66 VAL B N 3042 C CA . VAL B 66 ? 1.0150 0.9945 0.9254 -0.3375 -0.0743 0.1451 66 VAL B CA 3043 C C . VAL B 66 ? 0.9507 1.0337 0.9291 -0.3188 -0.0776 0.1403 66 VAL B C 3044 O O . VAL B 66 ? 0.8827 0.9962 0.9146 -0.2464 -0.0596 0.1210 66 VAL B O 3045 C CB . VAL B 66 ? 1.1109 0.8881 0.9114 -0.3264 -0.0808 0.1235 66 VAL B CB 3046 C CG1 . VAL B 66 ? 1.2417 0.9295 0.9482 -0.4023 -0.1087 0.1259 66 VAL B CG1 3047 C CG2 . VAL B 66 ? 1.1929 0.8610 0.9230 -0.3180 -0.0720 0.1312 66 VAL B CG2 3048 N N . GLY B 67 ? 0.9982 1.1313 0.9637 -0.3908 -0.1031 0.1614 67 GLY B N 3049 C CA . GLY B 67 ? 0.9348 1.1620 0.9522 -0.3775 -0.1113 0.1628 67 GLY B CA 3050 C C . GLY B 67 ? 0.9481 1.0276 0.9031 -0.3544 -0.1188 0.1272 67 GLY B C 3051 O O . GLY B 67 ? 1.0577 0.9809 0.8994 -0.4009 -0.1360 0.1169 67 GLY B O 3052 N N . ARG B 68 ? 0.8477 0.9631 0.8611 -0.2795 -0.1024 0.1099 68 ARG B N 3053 C CA . ARG B 68 ? 0.8644 0.8725 0.8328 -0.2517 -0.1050 0.0820 68 ARG B CA 3054 C C . ARG B 68 ? 0.7859 0.9055 0.8216 -0.2226 -0.1053 0.0880 68 ARG B C 3055 O O . ARG B 68 ? 0.7038 0.9342 0.8160 -0.1783 -0.0871 0.0998 68 ARG B O 3056 C CB . ARG B 68 ? 0.8489 0.7633 0.8061 -0.1845 -0.0806 0.0572 68 ARG B CB 3057 C CG . ARG B 68 ? 0.9554 0.7311 0.8199 -0.1984 -0.0799 0.0542 68 ARG B CG 3058 C CD . ARG B 68 ? 0.9386 0.6555 0.7979 -0.1260 -0.0573 0.0415 68 ARG B CD 3059 N NE . ARG B 68 ? 0.8424 0.6568 0.7853 -0.0957 -0.0441 0.0451 68 ARG B NE 3060 C CZ . ARG B 68 ? 0.8394 0.6706 0.7871 -0.1057 -0.0402 0.0569 68 ARG B CZ 3061 N NH1 . ARG B 68 ? 0.9360 0.6955 0.8158 -0.1451 -0.0477 0.0694 68 ARG B NH1 3062 N NH2 . ARG B 68 ? 0.7871 0.6937 0.7921 -0.0806 -0.0290 0.0563 68 ARG B NH2 3063 N N . GLU B 69 ? 0.8407 0.9188 0.8315 -0.2445 -0.1245 0.0816 69 GLU B N 3064 C CA . GLU B 69 ? 0.7916 0.9831 0.8366 -0.2271 -0.1308 0.0963 69 GLU B CA 3065 C C . GLU B 69 ? 0.7669 0.8743 0.7888 -0.1780 -0.1214 0.0695 69 GLU B C 3066 O O . GLU B 69 ? 0.8350 0.8051 0.7778 -0.1819 -0.1211 0.0457 69 GLU B O 3067 C CB . GLU B 69 ? 0.8708 1.1312 0.8875 -0.3143 -0.1700 0.1249 69 GLU B CB 3068 C CG . GLU B 69 ? 0.8772 1.2871 0.9417 -0.3670 -0.1800 0.1677 69 GLU B CG 3069 C CD . GLU B 69 ? 0.8755 1.4975 1.0079 -0.3869 -0.1998 0.2169 69 GLU B CD 3070 O OE1 . GLU B 69 ? 0.8455 1.5241 1.0271 -0.3117 -0.1858 0.2188 69 GLU B OE1 3071 O OE2 . GLU B 69 ? 0.9252 1.6628 1.0578 -0.4791 -0.2299 0.2590 69 GLU B OE2 3072 N N . PHE B 70 ? 0.6971 0.8852 0.7785 -0.1272 -0.1104 0.0780 70 PHE B N 3073 C CA . PHE B 70 ? 0.6921 0.8145 0.7596 -0.0809 -0.0981 0.0583 70 PHE B CA 3074 C C . PHE B 70 ? 0.6686 0.8721 0.7596 -0.0653 -0.1072 0.0783 70 PHE B C 3075 O O . PHE B 70 ? 0.6154 0.9372 0.7614 -0.0430 -0.1034 0.1074 70 PHE B O 3076 C CB . PHE B 70 ? 0.6571 0.7557 0.7560 -0.0260 -0.0680 0.0461 70 PHE B CB 3077 C CG . PHE B 70 ? 0.6702 0.7158 0.7556 -0.0355 -0.0600 0.0342 70 PHE B CG 3078 C CD1 . PHE B 70 ? 0.6985 0.6506 0.7390 -0.0296 -0.0548 0.0174 70 PHE B CD1 3079 C CD2 . PHE B 70 ? 0.6537 0.7523 0.7683 -0.0426 -0.0549 0.0456 70 PHE B CD2 3080 C CE1 . PHE B 70 ? 0.7085 0.6211 0.7347 -0.0290 -0.0472 0.0140 70 PHE B CE1 3081 C CE2 . PHE B 70 ? 0.6624 0.7121 0.7598 -0.0509 -0.0490 0.0378 70 PHE B CE2 3082 C CZ . PHE B 70 ? 0.6935 0.6500 0.7471 -0.0436 -0.0466 0.0231 70 PHE B CZ 3083 N N . ASN B 71 ? 0.7115 0.8545 0.7557 -0.0675 -0.1154 0.0667 71 ASN B N 3084 C CA . ASN B 71 ? 0.7238 0.9409 0.7815 -0.0540 -0.1272 0.0889 71 ASN B CA 3085 C C . ASN B 71 ? 0.6796 0.9097 0.7759 0.0212 -0.0986 0.0953 71 ASN B C 3086 O O . ASN B 71 ? 0.6715 0.8592 0.7815 0.0513 -0.0735 0.0825 71 ASN B O 3087 C CB . ASN B 71 ? 0.7941 0.9349 0.7718 -0.0862 -0.1466 0.0752 71 ASN B CB 3088 C CG . ASN B 71 ? 0.8008 0.8349 0.7472 -0.0426 -0.1203 0.0494 71 ASN B CG 3089 O OD1 . ASN B 71 ? 0.7637 0.8084 0.7514 0.0068 -0.0975 0.0525 71 ASN B OD1 3090 N ND2 . ASN B 71 ? 0.8819 0.8085 0.7413 -0.0625 -0.1224 0.0275 71 ASN B ND2 3091 N N . ASN B 72 ? 0.7007 0.9734 0.7969 0.0466 -0.1040 0.1161 72 ASN B N 3092 C CA . ASN B 72 ? 0.7097 0.9740 0.8162 0.1185 -0.0771 0.1284 72 ASN B CA 3093 C C . ASN B 72 ? 0.7111 0.8433 0.7783 0.1347 -0.0557 0.1010 72 ASN B C 3094 O O . ASN B 72 ? 0.7210 0.8063 0.7725 0.1791 -0.0326 0.1055 72 ASN B O 3095 C CB . ASN B 72 ? 0.7544 1.1056 0.8650 0.1468 -0.0891 0.1667 72 ASN B CB 3096 C CG . ASN B 72 ? 0.8102 1.1683 0.9226 0.2351 -0.0579 0.1928 72 ASN B CG 3097 O OD1 . ASN B 72 ? 0.8202 1.2068 0.9527 0.2718 -0.0359 0.2015 72 ASN B OD1 3098 N ND2 . ASN B 72 ? 0.8718 1.1867 0.9455 0.2743 -0.0524 0.2062 72 ASN B ND2 3099 N N . LEU B 73 ? 0.7110 0.7824 0.7504 0.0985 -0.0621 0.0773 73 LEU B N 3100 C CA . LEU B 73 ? 0.7178 0.7050 0.7321 0.1050 -0.0432 0.0617 73 LEU B CA 3101 C C . LEU B 73 ? 0.6872 0.6449 0.7081 0.0844 -0.0361 0.0411 73 LEU B C 3102 O O . LEU B 73 ? 0.6781 0.6016 0.6805 0.0793 -0.0270 0.0331 73 LEU B O 3103 C CB . LEU B 73 ? 0.7639 0.7271 0.7394 0.0992 -0.0480 0.0625 73 LEU B CB 3104 C CG . LEU B 73 ? 0.8051 0.7892 0.7669 0.1253 -0.0530 0.0875 73 LEU B CG 3105 C CD1 . LEU B 73 ? 0.8421 0.8113 0.7594 0.1115 -0.0624 0.0874 73 LEU B CD1 3106 C CD2 . LEU B 73 ? 0.8289 0.7547 0.7739 0.1566 -0.0307 0.0970 73 LEU B CD2 3107 N N . GLU B 74 ? 0.6570 0.6422 0.7051 0.0781 -0.0382 0.0390 74 GLU B N 3108 C CA . GLU B 74 ? 0.6316 0.5935 0.6871 0.0662 -0.0304 0.0254 74 GLU B CA 3109 C C . GLU B 74 ? 0.6146 0.5880 0.6905 0.0781 -0.0206 0.0278 74 GLU B C 3110 O O . GLU B 74 ? 0.5777 0.5672 0.6690 0.0663 -0.0215 0.0238 74 GLU B O 3111 C CB . GLU B 74 ? 0.6301 0.5880 0.6706 0.0395 -0.0435 0.0186 74 GLU B CB 3112 C CG . GLU B 74 ? 0.6619 0.5730 0.6461 0.0303 -0.0503 0.0120 74 GLU B CG 3113 C CD . GLU B 74 ? 0.7212 0.5835 0.6523 -0.0023 -0.0634 0.0039 74 GLU B CD 3114 O OE1 . GLU B 74 ? 0.7137 0.6183 0.6596 -0.0370 -0.0816 0.0128 74 GLU B OE1 3115 O OE2 . GLU B 74 ? 0.7848 0.5625 0.6489 0.0081 -0.0531 -0.0074 74 GLU B OE2 3116 N N . ARG B 75 ? 0.6123 0.5597 0.6699 0.1037 -0.0090 0.0347 75 ARG B N 3117 C CA . ARG B 75 ? 0.6515 0.5798 0.6951 0.1263 0.0059 0.0359 75 ARG B CA 3118 C C . ARG B 75 ? 0.6486 0.5299 0.6749 0.0999 0.0100 0.0208 75 ARG B C 3119 O O . ARG B 75 ? 0.6740 0.5529 0.6943 0.1056 0.0177 0.0168 75 ARG B O 3120 C CB . ARG B 75 ? 0.7445 0.6153 0.7354 0.1688 0.0213 0.0476 75 ARG B CB 3121 C CG . ARG B 75 ? 0.7665 0.7090 0.7764 0.2116 0.0202 0.0739 75 ARG B CG 3122 C CD . ARG B 75 ? 0.7497 0.8132 0.8164 0.2200 0.0165 0.0894 75 ARG B CD 3123 N NE . ARG B 75 ? 0.8172 0.9826 0.9058 0.2644 0.0160 0.1271 75 ARG B NE 3124 C CZ . ARG B 75 ? 0.8172 1.1299 0.9626 0.2667 0.0092 0.1559 75 ARG B CZ 3125 N NH1 . ARG B 75 ? 0.7942 1.1460 0.9710 0.2250 0.0039 0.1470 75 ARG B NH1 3126 N NH2 . ARG B 75 ? 0.8272 1.2611 0.9980 0.3076 0.0066 0.2003 75 ARG B NH2 3127 N N . ARG B 76 ? 0.6357 0.4940 0.6530 0.0707 0.0050 0.0178 76 ARG B N 3128 C CA . ARG B 76 ? 0.6349 0.4815 0.6430 0.0380 0.0031 0.0132 76 ARG B CA 3129 C C . ARG B 76 ? 0.5864 0.4846 0.6352 0.0353 -0.0012 0.0095 76 ARG B C 3130 O O . ARG B 76 ? 0.6117 0.5001 0.6483 0.0265 0.0002 0.0049 76 ARG B O 3131 C CB . ARG B 76 ? 0.6202 0.4818 0.6285 0.0081 -0.0014 0.0239 76 ARG B CB 3132 C CG . ARG B 76 ? 0.6812 0.4755 0.6311 -0.0093 0.0008 0.0310 76 ARG B CG 3133 C CD . ARG B 76 ? 0.6620 0.5091 0.6284 -0.0394 -0.0023 0.0500 76 ARG B CD 3134 N NE . ARG B 76 ? 0.6047 0.5005 0.6097 -0.0041 0.0029 0.0524 76 ARG B NE 3135 C CZ . ARG B 76 ? 0.5633 0.5302 0.5963 -0.0015 0.0085 0.0673 76 ARG B CZ 3136 N NH1 . ARG B 76 ? 0.5769 0.6127 0.6268 -0.0317 0.0083 0.0896 76 ARG B NH1 3137 N NH2 . ARG B 76 ? 0.5331 0.5070 0.5689 0.0330 0.0151 0.0637 76 ARG B NH2 3138 N N . ILE B 77 ? 0.5551 0.4887 0.6329 0.0416 -0.0061 0.0113 77 ILE B N 3139 C CA . ILE B 77 ? 0.5467 0.4994 0.6393 0.0377 -0.0093 0.0102 77 ILE B CA 3140 C C . ILE B 77 ? 0.5519 0.5186 0.6523 0.0384 -0.0101 0.0087 77 ILE B C 3141 O O . ILE B 77 ? 0.5492 0.5235 0.6528 0.0303 -0.0095 0.0088 77 ILE B O 3142 C CB . ILE B 77 ? 0.5448 0.4907 0.6283 0.0454 -0.0105 0.0125 77 ILE B CB 3143 C CG1 . ILE B 77 ? 0.5831 0.5117 0.6485 0.0441 -0.0179 0.0084 77 ILE B CG1 3144 C CG2 . ILE B 77 ? 0.5594 0.5234 0.6429 0.0559 -0.0021 0.0234 77 ILE B CG2 3145 C CD1 . ILE B 77 ? 0.6423 0.5203 0.6582 0.0499 -0.0174 0.0055 77 ILE B CD1 3146 N N . GLU B 78 ? 0.5700 0.5565 0.6754 0.0503 -0.0103 0.0137 78 GLU B N 3147 C CA . GLU B 78 ? 0.5683 0.6049 0.6899 0.0574 -0.0065 0.0237 78 GLU B CA 3148 C C . GLU B 78 ? 0.5631 0.5736 0.6642 0.0727 0.0101 0.0182 78 GLU B C 3149 O O . GLU B 78 ? 0.5456 0.5829 0.6539 0.0672 0.0144 0.0214 78 GLU B O 3150 C CB . GLU B 78 ? 0.6096 0.6980 0.7430 0.0817 -0.0057 0.0409 78 GLU B CB 3151 C CG . GLU B 78 ? 0.6557 0.8373 0.8164 0.0978 0.0023 0.0641 78 GLU B CG 3152 C CD . GLU B 78 ? 0.7337 1.0128 0.9209 0.1145 -0.0045 0.0942 78 GLU B CD 3153 O OE1 . GLU B 78 ? 0.7919 1.0504 0.9605 0.1640 0.0081 0.1006 78 GLU B OE1 3154 O OE2 . GLU B 78 ? 0.7445 1.1210 0.9633 0.0729 -0.0250 0.1157 78 GLU B OE2 3155 N N . ASN B 79 ? 0.5975 0.5424 0.6568 0.0849 0.0186 0.0103 79 ASN B N 3156 C CA . ASN B 79 ? 0.6730 0.5575 0.6764 0.0920 0.0327 0.0017 79 ASN B CA 3157 C C . ASN B 79 ? 0.6584 0.5439 0.6642 0.0536 0.0221 -0.0051 79 ASN B C 3158 O O . ASN B 79 ? 0.6922 0.5669 0.6716 0.0550 0.0303 -0.0088 79 ASN B O 3159 C CB . ASN B 79 ? 0.7636 0.5479 0.6939 0.0947 0.0384 -0.0043 79 ASN B CB 3160 C CG . ASN B 79 ? 0.8763 0.5569 0.7090 0.0905 0.0504 -0.0168 79 ASN B CG 3161 O OD1 . ASN B 79 ? 0.9754 0.5844 0.7353 0.1393 0.0753 -0.0173 79 ASN B OD1 3162 N ND2 . ASN B 79 ? 0.8979 0.5692 0.7179 0.0360 0.0339 -0.0239 79 ASN B ND2 3163 N N . LEU B 80 ? 0.6164 0.5213 0.6494 0.0267 0.0063 -0.0025 80 LEU B N 3164 C CA . LEU B 80 ? 0.6124 0.5404 0.6539 0.0009 -0.0038 0.0013 80 LEU B CA 3165 C C . LEU B 80 ? 0.5833 0.5430 0.6478 0.0078 -0.0022 0.0046 80 LEU B C 3166 O O . LEU B 80 ? 0.6197 0.5817 0.6691 -0.0033 -0.0030 0.0056 80 LEU B O 3167 C CB . LEU B 80 ? 0.5911 0.5553 0.6624 -0.0053 -0.0124 0.0131 80 LEU B CB 3168 C CG . LEU B 80 ? 0.5935 0.6078 0.6789 -0.0170 -0.0204 0.0298 80 LEU B CG 3169 C CD1 . LEU B 80 ? 0.5859 0.6492 0.6948 -0.0071 -0.0197 0.0489 80 LEU B CD1 3170 C CD2 . LEU B 80 ? 0.5972 0.6169 0.6925 0.0001 -0.0184 0.0326 80 LEU B CD2 3171 N N . ASN B 81 ? 0.5465 0.5273 0.6376 0.0173 -0.0027 0.0086 81 ASN B N 3172 C CA . ASN B 81 ? 0.5383 0.5415 0.6391 0.0084 -0.0043 0.0162 81 ASN B CA 3173 C C . ASN B 81 ? 0.5620 0.5914 0.6578 0.0145 0.0086 0.0191 81 ASN B C 3174 O O . ASN B 81 ? 0.5575 0.5987 0.6493 0.0016 0.0091 0.0257 81 ASN B O 3175 C CB . ASN B 81 ? 0.5431 0.5575 0.6534 -0.0005 -0.0124 0.0219 81 ASN B CB 3176 C CG . ASN B 81 ? 0.5746 0.6069 0.6805 -0.0291 -0.0182 0.0344 81 ASN B CG 3177 O OD1 . ASN B 81 ? 0.6161 0.6013 0.6926 -0.0426 -0.0231 0.0367 81 ASN B OD1 3178 N ND2 . ASN B 81 ? 0.5663 0.6714 0.6963 -0.0372 -0.0163 0.0486 81 ASN B ND2 3179 N N . LYS B 82 ? 0.5848 0.6193 0.6719 0.0422 0.0230 0.0176 82 LYS B N 3180 C CA . LYS B 82 ? 0.6292 0.6869 0.6978 0.0695 0.0457 0.0238 82 LYS B CA 3181 C C . LYS B 82 ? 0.6835 0.6772 0.6938 0.0643 0.0520 0.0094 82 LYS B C 3182 O O . LYS B 82 ? 0.6780 0.6942 0.6760 0.0668 0.0634 0.0150 82 LYS B O 3183 C CB . LYS B 82 ? 0.6959 0.7492 0.7453 0.1198 0.0653 0.0282 82 LYS B CB 3184 C CG . LYS B 82 ? 0.7587 0.8651 0.7940 0.1725 0.0978 0.0466 82 LYS B CG 3185 C CD . LYS B 82 ? 0.9030 0.9030 0.8437 0.2334 0.1275 0.0360 82 LYS B CD 3186 C CE . LYS B 82 ? 0.9838 1.0524 0.9133 0.3190 0.1679 0.0658 82 LYS B CE 3187 N NZ . LYS B 82 ? 1.0266 1.1310 0.9306 0.3452 0.1971 0.0746 82 LYS B NZ 3188 N N . LYS B 83 ? 0.7333 0.6534 0.7022 0.0488 0.0423 -0.0057 83 LYS B N 3189 C CA . LYS B 83 ? 0.8097 0.6676 0.7083 0.0253 0.0394 -0.0173 83 LYS B CA 3190 C C . LYS B 83 ? 0.7524 0.6598 0.6813 -0.0038 0.0238 -0.0080 83 LYS B C 3191 O O . LYS B 83 ? 0.7871 0.6778 0.6702 -0.0127 0.0275 -0.0106 83 LYS B O 3192 C CB . LYS B 83 ? 0.8844 0.6769 0.7380 -0.0071 0.0237 -0.0258 83 LYS B CB 3193 C CG . LYS B 83 ? 1.0570 0.7192 0.7880 0.0001 0.0391 -0.0424 83 LYS B CG 3194 C CD . LYS B 83 ? 1.1310 0.7656 0.8407 0.0732 0.0734 -0.0419 83 LYS B CD 3195 C CE . LYS B 83 ? 1.3300 0.8153 0.8851 0.1006 0.1006 -0.0581 83 LYS B CE 3196 N NZ . LYS B 83 ? 1.4096 0.8724 0.9338 0.1928 0.1414 -0.0490 83 LYS B NZ 3197 N N . MET B 84 ? 0.7009 0.6573 0.6929 -0.0132 0.0085 0.0040 84 MET B N 3198 C CA . MET B 84 ? 0.6684 0.6585 0.6795 -0.0266 -0.0025 0.0186 84 MET B CA 3199 C C . MET B 84 ? 0.6480 0.6562 0.6572 -0.0219 0.0097 0.0252 84 MET B C 3200 O O . MET B 84 ? 0.6657 0.6767 0.6499 -0.0330 0.0078 0.0313 84 MET B O 3201 C CB . MET B 84 ? 0.6313 0.6385 0.6825 -0.0199 -0.0116 0.0301 84 MET B CB 3202 C CG . MET B 84 ? 0.6529 0.6782 0.7042 -0.0184 -0.0208 0.0503 84 MET B CG 3203 S SD . MET B 84 ? 0.7207 0.7070 0.7650 -0.0040 -0.0173 0.0617 84 MET B SD 3204 C CE . MET B 84 ? 0.7223 0.7111 0.7568 -0.0298 -0.0109 0.0604 84 MET B CE 3205 N N . GLU B 85 ? 0.9114 0.9159 0.6039 -0.1885 -0.0158 0.0652 85 GLU B N 3206 C CA . GLU B 85 ? 0.8705 0.9171 0.5922 -0.1855 -0.0353 0.0748 85 GLU B CA 3207 C C . GLU B 85 ? 0.8337 0.8810 0.5823 -0.1508 -0.0316 0.0962 85 GLU B C 3208 O O . GLU B 85 ? 0.8031 0.8570 0.5865 -0.1474 -0.0356 0.0890 85 GLU B O 3209 C CB . GLU B 85 ? 0.8983 1.0078 0.5993 -0.2005 -0.0565 0.0960 85 GLU B CB 3210 C CG . GLU B 85 ? 0.9539 1.0533 0.6134 -0.2396 -0.0593 0.0751 85 GLU B CG 3211 C CD . GLU B 85 ? 0.9815 1.1024 0.6238 -0.2814 -0.0764 0.0624 85 GLU B CD 3212 O OE1 . GLU B 85 ? 1.0129 1.2069 0.6397 -0.3041 -0.0962 0.0837 85 GLU B OE1 3213 O OE2 . GLU B 85 ? 0.9975 1.0611 0.6304 -0.2939 -0.0687 0.0317 85 GLU B OE2 3214 N N . ASP B 86 ? 0.8667 0.8956 0.5872 -0.1232 -0.0215 0.1231 86 ASP B N 3215 C CA . ASP B 86 ? 0.8670 0.8697 0.5897 -0.0849 -0.0106 0.1433 86 ASP B CA 3216 C C . ASP B 86 ? 0.8378 0.7858 0.5778 -0.0945 0.0058 0.1168 86 ASP B C 3217 O O . ASP B 86 ? 0.8078 0.7542 0.5730 -0.0764 0.0067 0.1211 86 ASP B O 3218 C CB . ASP B 86 ? 0.9565 0.9100 0.6140 -0.0526 0.0055 0.1739 86 ASP B CB 3219 C CG . ASP B 86 ? 0.9930 1.0164 0.6405 -0.0099 -0.0082 0.2167 86 ASP B CG 3220 O OD1 . ASP B 86 ? 0.9765 1.0791 0.6721 0.0000 -0.0249 0.2250 86 ASP B OD1 3221 O OD2 . ASP B 86 ? 1.0682 1.0756 0.6579 0.0149 -0.0020 0.2435 86 ASP B OD2 3222 N N . GLY B 87 ? 0.8441 0.7590 0.5694 -0.1237 0.0192 0.0905 87 GLY B N 3223 C CA . GLY B 87 ? 0.8297 0.7179 0.5700 -0.1381 0.0346 0.0658 87 GLY B CA 3224 C C . GLY B 87 ? 0.7623 0.6880 0.5602 -0.1360 0.0224 0.0491 87 GLY B C 3225 O O . GLY B 87 ? 0.7529 0.6664 0.5700 -0.1287 0.0284 0.0461 87 GLY B O 3226 N N . PHE B 88 ? 0.7390 0.6992 0.5523 -0.1444 0.0069 0.0382 88 PHE B N 3227 C CA . PHE B 88 ? 0.7061 0.6810 0.5537 -0.1429 -0.0021 0.0227 88 PHE B CA 3228 C C . PHE B 88 ? 0.7003 0.6934 0.5720 -0.1281 -0.0152 0.0435 88 PHE B C 3229 O O . PHE B 88 ? 0.6722 0.6625 0.5722 -0.1207 -0.0149 0.0360 88 PHE B O 3230 C CB . PHE B 88 ? 0.7272 0.7053 0.5567 -0.1588 -0.0106 0.0056 88 PHE B CB 3231 C CG . PHE B 88 ? 0.7457 0.7128 0.5588 -0.1617 0.0053 -0.0201 88 PHE B CG 3232 C CD1 . PHE B 88 ? 0.7262 0.7009 0.5615 -0.1481 0.0185 -0.0371 88 PHE B CD1 3233 C CD2 . PHE B 88 ? 0.7937 0.7558 0.5685 -0.1761 0.0073 -0.0261 88 PHE B CD2 3234 C CE1 . PHE B 88 ? 0.7371 0.7276 0.5598 -0.1441 0.0342 -0.0578 88 PHE B CE1 3235 C CE2 . PHE B 88 ? 0.8115 0.7742 0.5703 -0.1732 0.0243 -0.0488 88 PHE B CE2 3236 C CZ . PHE B 88 ? 0.7828 0.7663 0.5672 -0.1547 0.0381 -0.0638 88 PHE B CZ 3237 N N . LEU B 89 ? 0.7290 0.7522 0.5896 -0.1208 -0.0260 0.0714 89 LEU B N 3238 C CA . LEU B 89 ? 0.7301 0.7924 0.6146 -0.1020 -0.0364 0.0943 89 LEU B CA 3239 C C . LEU B 89 ? 0.7108 0.7351 0.6041 -0.0737 -0.0200 0.1003 89 LEU B C 3240 O O . LEU B 89 ? 0.6560 0.6900 0.5798 -0.0674 -0.0231 0.0981 89 LEU B O 3241 C CB . LEU B 89 ? 0.7878 0.9105 0.6562 -0.0890 -0.0478 0.1284 89 LEU B CB 3242 C CG . LEU B 89 ? 0.8426 1.0143 0.6967 -0.1285 -0.0669 0.1233 89 LEU B CG 3243 C CD1 . LEU B 89 ? 0.8820 1.1309 0.7183 -0.1138 -0.0776 0.1598 89 LEU B CD1 3244 C CD2 . LEU B 89 ? 0.8284 1.0252 0.6971 -0.1635 -0.0818 0.1084 89 LEU B CD2 3245 N N . ASP B 90 ? 0.7560 0.7270 0.6111 -0.0625 -0.0006 0.1065 90 ASP B N 3246 C CA . ASP B 90 ? 0.7788 0.6902 0.6178 -0.0473 0.0196 0.1081 90 ASP B CA 3247 C C . ASP B 90 ? 0.7351 0.6410 0.6088 -0.0693 0.0228 0.0779 90 ASP B C 3248 O O . ASP B 90 ? 0.7139 0.6086 0.6016 -0.0569 0.0268 0.0801 90 ASP B O 3249 C CB . ASP B 90 ? 0.8538 0.6889 0.6234 -0.0500 0.0430 0.1131 90 ASP B CB 3250 C CG . ASP B 90 ? 0.9241 0.7437 0.6428 -0.0099 0.0465 0.1505 90 ASP B CG 3251 O OD1 . ASP B 90 ? 0.9056 0.7887 0.6496 0.0253 0.0320 0.1753 90 ASP B OD1 3252 O OD2 . ASP B 90 ? 1.0073 0.7565 0.6559 -0.0132 0.0647 0.1566 90 ASP B OD2 3253 N N . VAL B 91 ? 0.7237 0.6429 0.6076 -0.0967 0.0221 0.0515 91 VAL B N 3254 C CA . VAL B 91 ? 0.6823 0.6153 0.5978 -0.1081 0.0246 0.0258 91 VAL B CA 3255 C C . VAL B 91 ? 0.6379 0.5964 0.5931 -0.0952 0.0083 0.0257 91 VAL B C 3256 O O . VAL B 91 ? 0.6421 0.5993 0.6182 -0.0905 0.0115 0.0197 91 VAL B O 3257 C CB . VAL B 91 ? 0.6744 0.6317 0.5895 -0.1254 0.0276 0.0014 91 VAL B CB 3258 C CG1 . VAL B 91 ? 0.6417 0.6295 0.5886 -0.1212 0.0287 -0.0196 91 VAL B CG1 3259 C CG2 . VAL B 91 ? 0.7176 0.6589 0.5939 -0.1482 0.0461 -0.0019 91 VAL B CG2 3260 N N . TRP B 92 ? 0.6290 0.6091 0.5868 -0.0963 -0.0084 0.0316 92 TRP B N 3261 C CA . TRP B 92 ? 0.6100 0.6056 0.5901 -0.0954 -0.0222 0.0307 92 TRP B CA 3262 C C . TRP B 92 ? 0.6013 0.6170 0.5996 -0.0791 -0.0265 0.0546 92 TRP B C 3263 O O . TRP B 92 ? 0.5940 0.6175 0.6141 -0.0779 -0.0323 0.0522 92 TRP B O 3264 C CB . TRP B 92 ? 0.6329 0.6372 0.5916 -0.1161 -0.0364 0.0265 92 TRP B CB 3265 C CG . TRP B 92 ? 0.6664 0.6375 0.6017 -0.1215 -0.0295 -0.0004 92 TRP B CG 3266 C CD1 . TRP B 92 ? 0.7001 0.6612 0.6038 -0.1308 -0.0249 -0.0097 92 TRP B CD1 3267 C CD2 . TRP B 92 ? 0.6730 0.6186 0.6089 -0.1087 -0.0237 -0.0193 92 TRP B CD2 3268 N NE1 . TRP B 92 ? 0.7288 0.6607 0.6119 -0.1212 -0.0151 -0.0334 92 TRP B NE1 3269 C CE2 . TRP B 92 ? 0.7174 0.6399 0.6181 -0.1043 -0.0142 -0.0385 92 TRP B CE2 3270 C CE3 . TRP B 92 ? 0.6579 0.5995 0.6163 -0.0959 -0.0247 -0.0203 92 TRP B CE3 3271 C CZ2 . TRP B 92 ? 0.7602 0.6576 0.6440 -0.0788 -0.0042 -0.0562 92 TRP B CZ2 3272 C CZ3 . TRP B 92 ? 0.7056 0.6210 0.6490 -0.0761 -0.0170 -0.0381 92 TRP B CZ3 3273 C CH2 . TRP B 92 ? 0.7467 0.6407 0.6510 -0.0636 -0.0063 -0.0548 92 TRP B CH2 3274 N N . THR B 93 ? 0.6142 0.6363 0.5969 -0.0613 -0.0216 0.0791 93 THR B N 3275 C CA . THR B 93 ? 0.6081 0.6500 0.5997 -0.0322 -0.0204 0.1043 93 THR B CA 3276 C C . THR B 93 ? 0.6053 0.5959 0.5995 -0.0233 -0.0037 0.0940 93 THR B C 3277 O O . THR B 93 ? 0.5833 0.5887 0.6009 -0.0123 -0.0062 0.0986 93 THR B O 3278 C CB . THR B 93 ? 0.6574 0.7077 0.6152 -0.0001 -0.0139 0.1363 93 THR B CB 3279 O OG1 . THR B 93 ? 0.6578 0.7816 0.6185 -0.0112 -0.0330 0.1490 93 THR B OG1 3280 C CG2 . THR B 93 ? 0.6752 0.7363 0.6310 0.0447 -0.0055 0.1632 93 THR B CG2 3281 N N . TYR B 94 ? 0.6326 0.5692 0.5987 -0.0348 0.0131 0.0795 94 TYR B N 3282 C CA . TYR B 94 ? 0.6438 0.5347 0.5997 -0.0407 0.0303 0.0672 94 TYR B CA 3283 C C . TYR B 94 ? 0.5882 0.5117 0.5907 -0.0525 0.0202 0.0469 94 TYR B C 3284 O O . TYR B 94 ? 0.5734 0.4900 0.5877 -0.0445 0.0231 0.0482 94 TYR B O 3285 C CB . TYR B 94 ? 0.6917 0.5377 0.6030 -0.0674 0.0488 0.0535 94 TYR B CB 3286 C CG . TYR B 94 ? 0.7047 0.5279 0.6053 -0.0943 0.0640 0.0339 94 TYR B CG 3287 C CD1 . TYR B 94 ? 0.6502 0.5324 0.5951 -0.1129 0.0563 0.0102 94 TYR B CD1 3288 C CD2 . TYR B 94 ? 0.7677 0.5103 0.6037 -0.1005 0.0875 0.0402 94 TYR B CD2 3289 C CE1 . TYR B 94 ? 0.6424 0.5299 0.5803 -0.1400 0.0680 -0.0055 94 TYR B CE1 3290 C CE2 . TYR B 94 ? 0.7877 0.5162 0.6061 -0.1378 0.1008 0.0210 94 TYR B CE2 3291 C CZ . TYR B 94 ? 0.7160 0.5307 0.5924 -0.1592 0.0891 -0.0014 94 TYR B CZ 3292 O OH . TYR B 94 ? 0.7232 0.5501 0.5853 -0.1989 0.1004 -0.0187 94 TYR B OH 3293 N N . ASN B 95 ? 0.5849 0.5373 0.6051 -0.0666 0.0100 0.0295 95 ASN B N 3294 C CA . ASN B 95 ? 0.5628 0.5359 0.6126 -0.0670 0.0015 0.0137 95 ASN B CA 3295 C C . ASN B 95 ? 0.5536 0.5355 0.6235 -0.0564 -0.0101 0.0262 95 ASN B C 3296 O O . ASN B 95 ? 0.5443 0.5258 0.6313 -0.0521 -0.0091 0.0206 95 ASN B O 3297 C CB . ASN B 95 ? 0.5569 0.5405 0.6008 -0.0719 -0.0052 -0.0014 95 ASN B CB 3298 C CG . ASN B 95 ? 0.5763 0.5729 0.6093 -0.0793 0.0079 -0.0176 95 ASN B CG 3299 O OD1 . ASN B 95 ? 0.5835 0.5826 0.6107 -0.0917 0.0212 -0.0189 95 ASN B OD1 3300 N ND2 . ASN B 95 ? 0.6005 0.6034 0.6206 -0.0750 0.0065 -0.0302 95 ASN B ND2 3301 N N . ALA B 96 ? 0.5681 0.5695 0.6348 -0.0553 -0.0211 0.0439 96 ALA B N 3302 C CA . ALA B 96 ? 0.5535 0.5838 0.6380 -0.0532 -0.0326 0.0568 96 ALA B CA 3303 C C . ALA B 96 ? 0.5423 0.5723 0.6379 -0.0294 -0.0224 0.0715 96 ALA B C 3304 O O . ALA B 96 ? 0.5360 0.5723 0.6502 -0.0286 -0.0253 0.0697 96 ALA B O 3305 C CB . ALA B 96 ? 0.5634 0.6414 0.6400 -0.0640 -0.0465 0.0743 96 ALA B CB 3306 N N . GLU B 97 ? 0.5570 0.5678 0.6295 -0.0085 -0.0080 0.0863 97 GLU B N 3307 C CA . GLU B 97 ? 0.5791 0.5717 0.6416 0.0206 0.0062 0.1020 97 GLU B CA 3308 C C . GLU B 97 ? 0.5868 0.5288 0.6450 0.0092 0.0190 0.0818 97 GLU B C 3309 O O . GLU B 97 ? 0.6074 0.5446 0.6719 0.0216 0.0240 0.0862 97 GLU B O 3310 C CB . GLU B 97 ? 0.6343 0.5955 0.6484 0.0529 0.0230 0.1250 97 GLU B CB 3311 C CG . GLU B 97 ? 0.6394 0.6778 0.6618 0.0714 0.0091 0.1513 97 GLU B CG 3312 C CD . GLU B 97 ? 0.7103 0.7182 0.6770 0.1137 0.0259 0.1779 97 GLU B CD 3313 O OE1 . GLU B 97 ? 0.7877 0.6917 0.6960 0.1224 0.0507 0.1736 97 GLU B OE1 3314 O OE2 . GLU B 97 ? 0.7274 0.8156 0.6999 0.1364 0.0151 0.2043 97 GLU B OE2 3315 N N . LEU B 98 ? 0.5925 0.5093 0.6394 -0.0163 0.0242 0.0602 98 LEU B N 3316 C CA . LEU B 98 ? 0.5831 0.4784 0.6267 -0.0348 0.0342 0.0411 98 LEU B CA 3317 C C . LEU B 98 ? 0.5316 0.4680 0.6206 -0.0357 0.0187 0.0318 98 LEU B C 3318 O O . LEU B 98 ? 0.5241 0.4529 0.6176 -0.0346 0.0233 0.0298 98 LEU B O 3319 C CB . LEU B 98 ? 0.5896 0.4829 0.6165 -0.0645 0.0413 0.0217 98 LEU B CB 3320 C CG . LEU B 98 ? 0.6140 0.4937 0.6196 -0.0938 0.0564 0.0053 98 LEU B CG 3321 C CD1 . LEU B 98 ? 0.6939 0.4861 0.6323 -0.0965 0.0800 0.0154 98 LEU B CD1 3322 C CD2 . LEU B 98 ? 0.6176 0.5299 0.6141 -0.1262 0.0611 -0.0124 98 LEU B CD2 3323 N N . LEU B 99 ? 0.5092 0.4771 0.6196 -0.0378 0.0022 0.0268 99 LEU B N 3324 C CA . LEU B 99 ? 0.4885 0.4724 0.6205 -0.0370 -0.0090 0.0182 99 LEU B CA 3325 C C . LEU B 99 ? 0.4793 0.4676 0.6241 -0.0286 -0.0128 0.0326 99 LEU B C 3326 O O . LEU B 99 ? 0.4608 0.4477 0.6162 -0.0269 -0.0120 0.0274 99 LEU B O 3327 C CB . LEU B 99 ? 0.5047 0.4913 0.6296 -0.0408 -0.0215 0.0123 99 LEU B CB 3328 C CG . LEU B 99 ? 0.5447 0.5185 0.6647 -0.0365 -0.0294 0.0035 99 LEU B CG 3329 C CD1 . LEU B 99 ? 0.5499 0.5353 0.6812 -0.0227 -0.0228 -0.0074 99 LEU B CD1 3330 C CD2 . LEU B 99 ? 0.5914 0.5384 0.6763 -0.0383 -0.0334 -0.0060 99 LEU B CD2 3331 N N . VAL B 100 ? 0.4906 0.4963 0.6341 -0.0220 -0.0164 0.0524 100 VAL B N 3332 C CA . VAL B 100 ? 0.4692 0.5016 0.6262 -0.0118 -0.0190 0.0692 100 VAL B CA 3333 C C . VAL B 100 ? 0.4901 0.4929 0.6397 0.0057 -0.0012 0.0713 100 VAL B C 3334 O O . VAL B 100 ? 0.4817 0.4889 0.6451 0.0051 -0.0025 0.0690 100 VAL B O 3335 C CB . VAL B 100 ? 0.4873 0.5723 0.6439 -0.0038 -0.0251 0.0933 100 VAL B CB 3336 C CG1 . VAL B 100 ? 0.4890 0.6163 0.6557 0.0224 -0.0194 0.1166 100 VAL B CG1 3337 C CG2 . VAL B 100 ? 0.4776 0.5930 0.6346 -0.0375 -0.0447 0.0889 100 VAL B CG2 3338 N N . LEU B 101 ? 0.5109 0.4717 0.6267 0.0172 0.0170 0.0747 101 LEU B N 3339 C CA . LEU B 101 ? 0.5468 0.4512 0.6289 0.0246 0.0390 0.0727 101 LEU B CA 3340 C C . LEU B 101 ? 0.5541 0.4535 0.6485 -0.0018 0.0375 0.0500 101 LEU B C 3341 O O . LEU B 101 ? 0.5872 0.4778 0.6815 0.0032 0.0429 0.0510 101 LEU B O 3342 C CB . LEU B 101 ? 0.6061 0.4410 0.6266 0.0244 0.0606 0.0731 101 LEU B CB 3343 C CG . LEU B 101 ? 0.6838 0.4693 0.6483 0.0680 0.0817 0.0994 101 LEU B CG 3344 C CD1 . LEU B 101 ? 0.6684 0.5331 0.6690 0.1093 0.0698 0.1269 101 LEU B CD1 3345 C CD2 . LEU B 101 ? 0.7435 0.4743 0.6528 0.0649 0.0941 0.1019 101 LEU B CD2 3346 N N . MET B 102 ? 0.5269 0.4409 0.6298 -0.0263 0.0312 0.0313 102 MET B N 3347 C CA . MET B 102 ? 0.5178 0.4499 0.6307 -0.0464 0.0300 0.0125 102 MET B CA 3348 C C . MET B 102 ? 0.4887 0.4514 0.6373 -0.0347 0.0144 0.0140 102 MET B C 3349 O O . MET B 102 ? 0.5078 0.4719 0.6578 -0.0391 0.0174 0.0096 102 MET B O 3350 C CB . MET B 102 ? 0.5120 0.4788 0.6296 -0.0638 0.0265 -0.0036 102 MET B CB 3351 C CG . MET B 102 ? 0.5803 0.5194 0.6551 -0.0887 0.0437 -0.0087 102 MET B CG 3352 S SD . MET B 102 ? 0.6109 0.6211 0.6917 -0.1178 0.0437 -0.0298 102 MET B SD 3353 C CE . MET B 102 ? 0.6089 0.6493 0.7252 -0.0834 0.0252 -0.0270 102 MET B CE 3354 N N . GLU B 103 ? 0.4624 0.4421 0.6289 -0.0251 -0.0010 0.0200 103 GLU B N 3355 C CA . GLU B 103 ? 0.4595 0.4499 0.6405 -0.0211 -0.0137 0.0200 103 GLU B CA 3356 C C . GLU B 103 ? 0.4644 0.4561 0.6523 -0.0163 -0.0124 0.0344 103 GLU B C 3357 O O . GLU B 103 ? 0.4582 0.4510 0.6520 -0.0166 -0.0156 0.0324 103 GLU B O 3358 C CB . GLU B 103 ? 0.4877 0.4749 0.6613 -0.0225 -0.0268 0.0190 103 GLU B CB 3359 C CG . GLU B 103 ? 0.5168 0.5037 0.6790 -0.0159 -0.0264 0.0036 103 GLU B CG 3360 C CD . GLU B 103 ? 0.5292 0.5288 0.6917 -0.0010 -0.0260 -0.0052 103 GLU B CD 3361 O OE1 . GLU B 103 ? 0.5215 0.5092 0.6838 0.0021 -0.0302 -0.0004 103 GLU B OE1 3362 O OE2 . GLU B 103 ? 0.6176 0.6498 0.7798 0.0087 -0.0212 -0.0155 103 GLU B OE2 3363 N N . ASN B 104 ? 0.4745 0.4726 0.6593 -0.0069 -0.0067 0.0508 104 ASN B N 3364 C CA . ASN B 104 ? 0.4650 0.4766 0.6537 0.0071 -0.0004 0.0665 104 ASN B CA 3365 C C . ASN B 104 ? 0.4849 0.4630 0.6610 0.0090 0.0136 0.0581 104 ASN B C 3366 O O . ASN B 104 ? 0.4643 0.4539 0.6504 0.0106 0.0121 0.0614 104 ASN B O 3367 C CB . ASN B 104 ? 0.4910 0.5132 0.6661 0.0329 0.0108 0.0873 104 ASN B CB 3368 C CG . ASN B 104 ? 0.4749 0.5637 0.6675 0.0301 -0.0044 0.1032 104 ASN B CG 3369 O OD1 . ASN B 104 ? 0.4470 0.5648 0.6540 0.0025 -0.0217 0.0991 104 ASN B OD1 3370 N ND2 . ASN B 104 ? 0.4834 0.5936 0.6633 0.0567 0.0031 0.1225 104 ASN B ND2 3371 N N . GLU B 105 ? 0.5108 0.4478 0.6581 0.0019 0.0279 0.0469 105 GLU B N 3372 C CA . GLU B 105 ? 0.5394 0.4428 0.6614 -0.0100 0.0422 0.0359 105 GLU B CA 3373 C C . GLU B 105 ? 0.4718 0.4110 0.6216 -0.0253 0.0273 0.0230 105 GLU B C 3374 O O . GLU B 105 ? 0.4495 0.3855 0.5965 -0.0280 0.0305 0.0214 105 GLU B O 3375 C CB . GLU B 105 ? 0.6283 0.4837 0.7013 -0.0318 0.0601 0.0239 105 GLU B CB 3376 C CG . GLU B 105 ? 0.7340 0.5345 0.7545 -0.0502 0.0813 0.0155 105 GLU B CG 3377 C CD . GLU B 105 ? 0.8971 0.6243 0.8410 -0.0790 0.1051 0.0063 105 GLU B CD 3378 O OE1 . GLU B 105 ? 0.9854 0.7477 0.9344 -0.1156 0.0991 -0.0089 105 GLU B OE1 3379 O OE2 . GLU B 105 ? 0.9938 0.6254 0.8632 -0.0643 0.1320 0.0152 105 GLU B OE2 3380 N N . ARG B 106 ? 0.4631 0.4339 0.6330 -0.0298 0.0125 0.0152 106 ARG B N 3381 C CA . ARG B 106 ? 0.4679 0.4690 0.6536 -0.0297 0.0000 0.0075 106 ARG B CA 3382 C C . ARG B 106 ? 0.4352 0.4321 0.6314 -0.0192 -0.0098 0.0181 106 ARG B C 3383 O O . ARG B 106 ? 0.4410 0.4457 0.6382 -0.0183 -0.0134 0.0155 106 ARG B O 3384 C CB . ARG B 106 ? 0.4947 0.5213 0.6857 -0.0235 -0.0093 -0.0003 106 ARG B CB 3385 C CG . ARG B 106 ? 0.5468 0.5965 0.7289 -0.0398 0.0000 -0.0116 106 ARG B CG 3386 C CD . ARG B 106 ? 0.5897 0.6989 0.7799 -0.0282 -0.0068 -0.0208 106 ARG B CD 3387 N NE . ARG B 106 ? 0.6279 0.7878 0.8203 -0.0382 -0.0053 -0.0264 106 ARG B NE 3388 C CZ . ARG B 106 ? 0.6718 0.8885 0.8721 -0.0129 -0.0135 -0.0267 106 ARG B CZ 3389 N NH1 . ARG B 106 ? 0.6708 0.8822 0.8665 0.0287 -0.0209 -0.0224 106 ARG B NH1 3390 N NH2 . ARG B 106 ? 0.7314 1.0071 0.9334 -0.0279 -0.0125 -0.0304 106 ARG B NH2 3391 N N . THR B 107 ? 0.4140 0.4064 0.6143 -0.0158 -0.0139 0.0307 107 THR B N 3392 C CA . THR B 107 ? 0.3996 0.3961 0.6026 -0.0187 -0.0227 0.0406 107 THR B CA 3393 C C . THR B 107 ? 0.3939 0.3960 0.6012 -0.0154 -0.0132 0.0470 107 THR B C 3394 O O . THR B 107 ? 0.3969 0.3976 0.6025 -0.0199 -0.0184 0.0472 107 THR B O 3395 C CB . THR B 107 ? 0.3962 0.4103 0.5999 -0.0270 -0.0294 0.0533 107 THR B CB 3396 O OG1 . THR B 107 ? 0.4066 0.4023 0.5948 -0.0336 -0.0378 0.0454 107 THR B OG1 3397 C CG2 . THR B 107 ? 0.4136 0.4418 0.6126 -0.0436 -0.0370 0.0630 107 THR B CG2 3398 N N . LEU B 108 ? 0.4023 0.4000 0.6044 -0.0045 0.0031 0.0525 108 LEU B N 3399 C CA . LEU B 108 ? 0.4165 0.4077 0.6101 0.0043 0.0168 0.0582 108 LEU B CA 3400 C C . LEU B 108 ? 0.4092 0.3817 0.5927 -0.0095 0.0182 0.0428 108 LEU B C 3401 O O . LEU B 108 ? 0.3788 0.3597 0.5667 -0.0119 0.0149 0.0448 108 LEU B O 3402 C CB . LEU B 108 ? 0.4620 0.4261 0.6276 0.0272 0.0400 0.0671 108 LEU B CB 3403 C CG . LEU B 108 ? 0.4616 0.4622 0.6361 0.0497 0.0394 0.0870 108 LEU B CG 3404 C CD1 . LEU B 108 ? 0.5321 0.4873 0.6603 0.0854 0.0671 0.0980 108 LEU B CD1 3405 C CD2 . LEU B 108 ? 0.4407 0.5162 0.6451 0.0525 0.0288 0.1042 108 LEU B CD2 3406 N N . ASP B 109 ? 0.4195 0.3780 0.5882 -0.0223 0.0224 0.0280 109 ASP B N 3407 C CA . ASP B 109 ? 0.4214 0.3907 0.5826 -0.0400 0.0208 0.0144 109 ASP B CA 3408 C C . ASP B 109 ? 0.3926 0.3947 0.5757 -0.0329 0.0007 0.0156 109 ASP B C 3409 O O . ASP B 109 ? 0.4117 0.4256 0.5905 -0.0373 -0.0011 0.0129 109 ASP B O 3410 C CB . ASP B 109 ? 0.4375 0.4167 0.5830 -0.0616 0.0253 -0.0003 109 ASP B CB 3411 C CG . ASP B 109 ? 0.4954 0.4160 0.5931 -0.0760 0.0492 -0.0033 109 ASP B CG 3412 O OD1 . ASP B 109 ? 0.5192 0.3851 0.5791 -0.0732 0.0680 0.0005 109 ASP B OD1 3413 O OD2 . ASP B 109 ? 0.5169 0.4392 0.6047 -0.0889 0.0515 -0.0096 109 ASP B OD2 3414 N N . PHE B 110 ? 0.3743 0.3801 0.5680 -0.0214 -0.0122 0.0198 110 PHE B N 3415 C CA . PHE B 110 ? 0.3746 0.3787 0.5626 -0.0102 -0.0263 0.0227 110 PHE B CA 3416 C C . PHE B 110 ? 0.3936 0.3832 0.5767 -0.0152 -0.0274 0.0323 110 PHE B C 3417 O O . PHE B 110 ? 0.4256 0.4146 0.5968 -0.0102 -0.0320 0.0324 110 PHE B O 3418 C CB . PHE B 110 ? 0.3840 0.3666 0.5621 -0.0035 -0.0344 0.0251 110 PHE B CB 3419 C CG . PHE B 110 ? 0.4278 0.3723 0.5712 0.0073 -0.0437 0.0289 110 PHE B CG 3420 C CD1 . PHE B 110 ? 0.4601 0.4090 0.5851 0.0337 -0.0463 0.0262 110 PHE B CD1 3421 C CD2 . PHE B 110 ? 0.4585 0.3612 0.5756 -0.0094 -0.0481 0.0361 110 PHE B CD2 3422 C CE1 . PHE B 110 ? 0.5232 0.4126 0.5947 0.0524 -0.0505 0.0318 110 PHE B CE1 3423 C CE2 . PHE B 110 ? 0.5354 0.3736 0.5945 -0.0057 -0.0524 0.0386 110 PHE B CE2 3424 C CZ . PHE B 110 ? 0.5693 0.3889 0.6003 0.0301 -0.0523 0.0369 110 PHE B CZ 3425 N N . HIS B 111 ? 0.3855 0.3739 0.5764 -0.0231 -0.0224 0.0421 111 HIS B N 3426 C CA . HIS B 111 ? 0.3951 0.3877 0.5844 -0.0304 -0.0206 0.0520 111 HIS B CA 3427 C C . HIS B 111 ? 0.4076 0.4020 0.5947 -0.0285 -0.0103 0.0476 111 HIS B C 3428 O O . HIS B 111 ? 0.4338 0.4259 0.6123 -0.0333 -0.0134 0.0509 111 HIS B O 3429 C CB . HIS B 111 ? 0.3899 0.4119 0.5928 -0.0321 -0.0141 0.0655 111 HIS B CB 3430 C CG . HIS B 111 ? 0.4012 0.4335 0.5997 -0.0483 -0.0260 0.0722 111 HIS B CG 3431 N ND1 . HIS B 111 ? 0.4328 0.4462 0.6039 -0.0738 -0.0370 0.0747 111 HIS B ND1 3432 C CD2 . HIS B 111 ? 0.3933 0.4476 0.6002 -0.0483 -0.0273 0.0768 111 HIS B CD2 3433 C CE1 . HIS B 111 ? 0.4526 0.4734 0.6114 -0.0949 -0.0442 0.0786 111 HIS B CE1 3434 N NE2 . HIS B 111 ? 0.4213 0.4758 0.6077 -0.0783 -0.0397 0.0806 111 HIS B NE2 3435 N N . ASP B 112 ? 0.3916 0.3814 0.5752 -0.0267 0.0035 0.0397 112 ASP B N 3436 C CA . ASP B 112 ? 0.3931 0.3722 0.5576 -0.0347 0.0165 0.0319 112 ASP B CA 3437 C C . ASP B 112 ? 0.4050 0.4061 0.5672 -0.0430 0.0036 0.0238 112 ASP B C 3438 O O . ASP B 112 ? 0.4234 0.4272 0.5764 -0.0479 0.0039 0.0246 112 ASP B O 3439 C CB . ASP B 112 ? 0.4161 0.3669 0.5554 -0.0410 0.0347 0.0230 112 ASP B CB 3440 C CG . ASP B 112 ? 0.4611 0.3744 0.5565 -0.0552 0.0556 0.0150 112 ASP B CG 3441 O OD1 . ASP B 112 ? 0.4520 0.3683 0.5439 -0.0559 0.0568 0.0173 112 ASP B OD1 3442 O OD2 . ASP B 112 ? 0.5175 0.3881 0.5704 -0.0702 0.0730 0.0054 112 ASP B OD2 3443 N N . SER B 113 ? 0.3995 0.4241 0.5682 -0.0395 -0.0070 0.0178 113 SER B N 3444 C CA . SER B 113 ? 0.3954 0.4586 0.5614 -0.0319 -0.0196 0.0153 113 SER B CA 3445 C C . SER B 113 ? 0.4217 0.4649 0.5775 -0.0149 -0.0304 0.0271 113 SER B C 3446 O O . SER B 113 ? 0.4390 0.5036 0.5837 -0.0114 -0.0347 0.0284 113 SER B O 3447 C CB . SER B 113 ? 0.3910 0.4840 0.5640 -0.0171 -0.0271 0.0115 113 SER B CB 3448 O OG . SER B 113 ? 0.4143 0.5489 0.5795 0.0087 -0.0385 0.0148 113 SER B OG 3449 N N . ASN B 114 ? 0.4224 0.4241 0.5732 -0.0097 -0.0342 0.0360 114 ASN B N 3450 C CA . ASN B 114 ? 0.4545 0.4190 0.5760 -0.0048 -0.0415 0.0464 114 ASN B CA 3451 C C . ASN B 114 ? 0.4511 0.4188 0.5736 -0.0211 -0.0358 0.0507 114 ASN B C 3452 O O . ASN B 114 ? 0.4615 0.4129 0.5571 -0.0162 -0.0410 0.0566 114 ASN B O 3453 C CB . ASN B 114 ? 0.4871 0.4051 0.5889 -0.0135 -0.0449 0.0531 114 ASN B CB 3454 C CG . ASN B 114 ? 0.5143 0.4135 0.6020 0.0038 -0.0492 0.0488 114 ASN B CG 3455 O OD1 . ASN B 114 ? 0.5422 0.4410 0.6104 0.0350 -0.0524 0.0467 114 ASN B OD1 3456 N ND2 . ASN B 114 ? 0.5260 0.4171 0.6205 -0.0130 -0.0484 0.0491 114 ASN B ND2 3457 N N . VAL B 115 ? 0.4211 0.4042 0.5657 -0.0351 -0.0230 0.0491 115 VAL B N 3458 C CA . VAL B 115 ? 0.4342 0.4209 0.5753 -0.0452 -0.0136 0.0529 115 VAL B CA 3459 C C . VAL B 115 ? 0.4506 0.4506 0.5801 -0.0470 -0.0128 0.0444 115 VAL B C 3460 O O . VAL B 115 ? 0.4690 0.4664 0.5831 -0.0504 -0.0152 0.0490 115 VAL B O 3461 C CB . VAL B 115 ? 0.4328 0.4280 0.5866 -0.0455 0.0052 0.0548 115 VAL B CB 3462 C CG1 . VAL B 115 ? 0.4514 0.4466 0.5925 -0.0489 0.0193 0.0563 115 VAL B CG1 3463 C CG2 . VAL B 115 ? 0.4315 0.4434 0.5994 -0.0458 0.0033 0.0675 115 VAL B CG2 3464 N N . LYS B 116 ? 0.4441 0.4640 0.5764 -0.0507 -0.0093 0.0323 116 LYS B N 3465 C CA . LYS B 116 ? 0.4734 0.5250 0.5909 -0.0643 -0.0088 0.0231 116 LYS B CA 3466 C C . LYS B 116 ? 0.4792 0.5638 0.5906 -0.0455 -0.0272 0.0303 116 LYS B C 3467 O O . LYS B 116 ? 0.4832 0.5897 0.5797 -0.0517 -0.0295 0.0312 116 LYS B O 3468 C CB . LYS B 116 ? 0.4869 0.5640 0.6009 -0.0827 -0.0026 0.0088 116 LYS B CB 3469 C CG . LYS B 116 ? 0.5509 0.6532 0.6358 -0.1171 0.0050 -0.0030 116 LYS B CG 3470 C CD . LYS B 116 ? 0.6082 0.7727 0.6875 -0.1426 0.0027 -0.0155 116 LYS B CD 3471 C CE . LYS B 116 ? 0.6648 0.8595 0.7033 -0.1925 0.0107 -0.0287 116 LYS B CE 3472 N NZ . LYS B 116 ? 0.7173 0.8105 0.7062 -0.2165 0.0372 -0.0366 116 LYS B NZ 3473 N N . ASN B 117 ? 0.4855 0.5689 0.5996 -0.0181 -0.0384 0.0364 117 ASN B N 3474 C CA . ASN B 117 ? 0.5121 0.6143 0.6047 0.0150 -0.0518 0.0462 117 ASN B CA 3475 C C . ASN B 117 ? 0.5637 0.6119 0.6246 0.0204 -0.0544 0.0589 117 ASN B C 3476 O O . ASN B 117 ? 0.6020 0.6707 0.6384 0.0390 -0.0613 0.0669 117 ASN B O 3477 C CB . ASN B 117 ? 0.5219 0.6111 0.6076 0.0484 -0.0574 0.0498 117 ASN B CB 3478 C CG . ASN B 117 ? 0.4931 0.6600 0.6054 0.0476 -0.0567 0.0391 117 ASN B CG 3479 O OD1 . ASN B 117 ? 0.4715 0.7143 0.5955 0.0262 -0.0556 0.0315 117 ASN B OD1 3480 N ND2 . ASN B 117 ? 0.5113 0.6615 0.6264 0.0644 -0.0568 0.0379 117 ASN B ND2 3481 N N . LEU B 118 ? 0.5573 0.5465 0.6162 0.0019 -0.0487 0.0619 118 LEU B N 3482 C CA . LEU B 118 ? 0.5898 0.5314 0.6164 -0.0071 -0.0487 0.0728 118 LEU B CA 3483 C C . LEU B 118 ? 0.5737 0.5495 0.6087 -0.0241 -0.0432 0.0700 118 LEU B C 3484 O O . LEU B 118 ? 0.6196 0.5815 0.6223 -0.0193 -0.0475 0.0787 118 LEU B O 3485 C CB . LEU B 118 ? 0.5895 0.4951 0.6196 -0.0332 -0.0429 0.0758 118 LEU B CB 3486 C CG . LEU B 118 ? 0.6224 0.4918 0.6200 -0.0577 -0.0408 0.0864 118 LEU B CG 3487 C CD1 . LEU B 118 ? 0.7051 0.5033 0.6305 -0.0434 -0.0486 0.0965 118 LEU B CD1 3488 C CD2 . LEU B 118 ? 0.6236 0.4904 0.6292 -0.0863 -0.0370 0.0895 118 LEU B CD2 3489 N N . TYR B 119 ? 0.5158 0.5241 0.5814 -0.0435 -0.0314 0.0578 119 TYR B N 3490 C CA . TYR B 119 ? 0.5076 0.5338 0.5671 -0.0628 -0.0220 0.0523 119 TYR B CA 3491 C C . TYR B 119 ? 0.5216 0.5959 0.5660 -0.0572 -0.0329 0.0511 119 TYR B C 3492 O O . TYR B 119 ? 0.5537 0.6322 0.5768 -0.0615 -0.0349 0.0562 119 TYR B O 3493 C CB . TYR B 119 ? 0.4944 0.5206 0.5645 -0.0811 -0.0027 0.0389 119 TYR B CB 3494 C CG . TYR B 119 ? 0.5215 0.5455 0.5659 -0.1036 0.0120 0.0302 119 TYR B CG 3495 C CD1 . TYR B 119 ? 0.5403 0.5396 0.5738 -0.1054 0.0245 0.0361 119 TYR B CD1 3496 C CD2 . TYR B 119 ? 0.5313 0.5809 0.5551 -0.1283 0.0152 0.0154 119 TYR B CD2 3497 C CE1 . TYR B 119 ? 0.5841 0.5698 0.5837 -0.1242 0.0413 0.0270 119 TYR B CE1 3498 C CE2 . TYR B 119 ? 0.5684 0.6023 0.5526 -0.1570 0.0311 0.0052 119 TYR B CE2 3499 C CZ . TYR B 119 ? 0.5945 0.5890 0.5650 -0.1514 0.0448 0.0108 119 TYR B CZ 3500 O OH . TYR B 119 ? 0.6398 0.6078 0.5616 -0.1774 0.0633 0.0000 119 TYR B OH 3501 N N . ASP B 120 ? 0.5121 0.6359 0.5674 -0.0470 -0.0404 0.0459 120 ASP B N 3502 C CA . ASP B 120 ? 0.5329 0.7360 0.5778 -0.0397 -0.0516 0.0474 120 ASP B CA 3503 C C . ASP B 120 ? 0.5614 0.7505 0.5769 0.0028 -0.0648 0.0677 120 ASP B C 3504 O O . ASP B 120 ? 0.5816 0.8088 0.5774 0.0048 -0.0706 0.0740 120 ASP B O 3505 C CB . ASP B 120 ? 0.5278 0.8063 0.5912 -0.0356 -0.0564 0.0402 120 ASP B CB 3506 C CG . ASP B 120 ? 0.5277 0.8171 0.5966 -0.0884 -0.0413 0.0193 120 ASP B CG 3507 O OD1 . ASP B 120 ? 0.5576 0.8304 0.6036 -0.1282 -0.0294 0.0095 120 ASP B OD1 3508 O OD2 . ASP B 120 ? 0.5230 0.8265 0.6073 -0.0908 -0.0391 0.0123 120 ASP B OD2 3509 N N . LYS B 121 ? 0.5912 0.7138 0.5916 0.0345 -0.0678 0.0781 121 LYS B N 3510 C CA . LYS B 121 ? 0.6750 0.7429 0.6201 0.0745 -0.0749 0.0979 121 LYS B CA 3511 C C . LYS B 121 ? 0.6990 0.7347 0.6190 0.0530 -0.0727 0.1040 121 LYS B C 3512 O O . LYS B 121 ? 0.7503 0.7929 0.6298 0.0812 -0.0798 0.1184 121 LYS B O 3513 C CB . LYS B 121 ? 0.7284 0.6946 0.6434 0.0873 -0.0720 0.1032 121 LYS B CB 3514 C CG . LYS B 121 ? 0.8564 0.7291 0.6856 0.1273 -0.0743 0.1226 121 LYS B CG 3515 C CD . LYS B 121 ? 0.9341 0.7015 0.7248 0.1229 -0.0688 0.1224 121 LYS B CD 3516 C CE . LYS B 121 ? 1.0893 0.7323 0.7660 0.1653 -0.0661 0.1400 121 LYS B CE 3517 N NZ . LYS B 121 ? 1.1854 0.7463 0.8010 0.1349 -0.0626 0.1497 121 LYS B NZ 3518 N N . VAL B 122 ? 0.6662 0.6727 0.6073 0.0081 -0.0616 0.0949 122 VAL B N 3519 C CA . VAL B 122 ? 0.6849 0.6685 0.6049 -0.0147 -0.0568 0.0996 122 VAL B CA 3520 C C . VAL B 122 ? 0.6772 0.7351 0.6064 -0.0274 -0.0574 0.0927 122 VAL B C 3521 O O . VAL B 122 ? 0.7131 0.7748 0.6088 -0.0211 -0.0627 0.1031 122 VAL B O 3522 C CB . VAL B 122 ? 0.6675 0.6190 0.6077 -0.0519 -0.0422 0.0938 122 VAL B CB 3523 C CG1 . VAL B 122 ? 0.6879 0.6385 0.6135 -0.0758 -0.0341 0.0959 122 VAL B CG1 3524 C CG2 . VAL B 122 ? 0.7002 0.5837 0.6157 -0.0528 -0.0436 0.1032 122 VAL B CG2 3525 N N . ARG B 123 ? 0.6458 0.7564 0.6097 -0.0504 -0.0508 0.0750 123 ARG B N 3526 C CA . ARG B 123 ? 0.6524 0.8303 0.6118 -0.0772 -0.0494 0.0647 123 ARG B CA 3527 C C . ARG B 123 ? 0.6817 0.9347 0.6218 -0.0484 -0.0682 0.0783 123 ARG B C 3528 O O . ARG B 123 ? 0.7209 1.0063 0.6385 -0.0621 -0.0708 0.0810 123 ARG B O 3529 C CB . ARG B 123 ? 0.6411 0.8549 0.6210 -0.1065 -0.0404 0.0447 123 ARG B CB 3530 C CG . ARG B 123 ? 0.6680 0.9316 0.6248 -0.1544 -0.0334 0.0291 123 ARG B CG 3531 C CD . ARG B 123 ? 0.6754 0.9514 0.6324 -0.1909 -0.0214 0.0089 123 ARG B CD 3532 N NE . ARG B 123 ? 0.6563 1.0044 0.6425 -0.1690 -0.0366 0.0130 123 ARG B NE 3533 C CZ . ARG B 123 ? 0.6690 1.1393 0.6580 -0.1659 -0.0537 0.0179 123 ARG B CZ 3534 N NH1 . ARG B 123 ? 0.6821 1.2200 0.6468 -0.1873 -0.0603 0.0196 123 ARG B NH1 3535 N NH2 . ARG B 123 ? 0.6418 1.1786 0.6573 -0.1388 -0.0639 0.0225 123 ARG B NH2 3536 N N . LEU B 124 ? 0.6929 0.9775 0.6376 -0.0034 -0.0799 0.0886 124 LEU B N 3537 C CA . LEU B 124 ? 0.7421 1.1173 0.6666 0.0407 -0.0963 0.1059 124 LEU B CA 3538 C C . LEU B 124 ? 0.8069 1.1258 0.6770 0.0800 -0.1021 0.1296 124 LEU B C 3539 O O . LEU B 124 ? 0.8448 1.2424 0.6910 0.1136 -0.1138 0.1457 124 LEU B O 3540 C CB . LEU B 124 ? 0.7393 1.1585 0.6749 0.0908 -0.1030 0.1128 124 LEU B CB 3541 C CG . LEU B 124 ? 0.6927 1.1996 0.6748 0.0520 -0.0999 0.0919 124 LEU B CG 3542 C CD1 . LEU B 124 ? 0.6975 1.1980 0.6937 0.0934 -0.1004 0.0946 124 LEU B CD1 3543 C CD2 . LEU B 124 ? 0.6889 1.3603 0.6772 0.0306 -0.1091 0.0901 124 LEU B CD2 3544 N N . GLN B 125 ? 0.8363 1.0249 0.6811 0.0742 -0.0935 0.1331 125 GLN B N 3545 C CA . GLN B 125 ? 0.9084 1.0236 0.6884 0.0972 -0.0956 0.1536 125 GLN B CA 3546 C C . GLN B 125 ? 0.8949 1.0342 0.6758 0.0530 -0.0927 0.1484 125 GLN B C 3547 O O . GLN B 125 ? 0.9571 1.1250 0.6993 0.0741 -0.1010 0.1640 125 GLN B O 3548 C CB . GLN B 125 ? 0.9583 0.9317 0.7027 0.0903 -0.0861 0.1574 125 GLN B CB 3549 C CG . GLN B 125 ? 0.9984 0.9204 0.7232 0.1301 -0.0864 0.1621 125 GLN B CG 3550 C CD . GLN B 125 ? 1.0746 0.8495 0.7368 0.1158 -0.0776 0.1683 125 GLN B CD 3551 O OE1 . GLN B 125 ? 1.1716 0.8545 0.7451 0.1348 -0.0762 0.1864 125 GLN B OE1 3552 N NE2 . GLN B 125 ? 1.0505 0.8023 0.7496 0.0779 -0.0710 0.1540 125 GLN B NE2 3553 N N . LEU B 126 ? 0.8396 0.9628 0.6573 -0.0030 -0.0791 0.1279 126 LEU B N 3554 C CA . LEU B 126 ? 0.8478 0.9759 0.6581 -0.0441 -0.0711 0.1213 126 LEU B CA 3555 C C . LEU B 126 ? 0.8639 1.1031 0.6772 -0.0577 -0.0788 0.1154 126 LEU B C 3556 O O . LEU B 126 ? 0.9265 1.1847 0.7079 -0.0633 -0.0829 0.1233 126 LEU B O 3557 C CB . LEU B 126 ? 0.8070 0.8954 0.6479 -0.0880 -0.0505 0.1025 126 LEU B CB 3558 C CG . LEU B 126 ? 0.8053 0.8119 0.6463 -0.0838 -0.0441 0.1093 126 LEU B CG 3559 C CD1 . LEU B 126 ? 0.7673 0.7609 0.6369 -0.1170 -0.0230 0.0961 126 LEU B CD1 3560 C CD2 . LEU B 126 ? 0.8827 0.8247 0.6660 -0.0739 -0.0490 0.1298 126 LEU B CD2 3561 N N . ARG B 127 ? 0.8536 1.1721 0.6992 -0.0678 -0.0814 0.1020 127 ARG B N 3562 C CA . ARG B 127 ? 0.8801 1.3212 0.7228 -0.0966 -0.0887 0.0944 127 ARG B CA 3563 C C . ARG B 127 ? 0.8963 1.3125 0.7160 -0.1583 -0.0734 0.0771 127 ARG B C 3564 O O . ARG B 127 ? 0.8867 1.2189 0.7101 -0.1877 -0.0519 0.0604 127 ARG B O 3565 C CB . ARG B 127 ? 0.9228 1.4561 0.7427 -0.0432 -0.1109 0.1213 127 ARG B CB 3566 C CG . ARG B 127 ? 0.9312 1.4992 0.7625 0.0246 -0.1219 0.1377 127 ARG B CG 3567 C CD . ARG B 127 ? 1.0040 1.5989 0.7889 0.1036 -0.1367 0.1721 127 ARG B CD 3568 N NE . ARG B 127 ? 1.0314 1.7853 0.8090 0.0998 -0.1509 0.1810 127 ARG B NE 3569 C CZ . ARG B 127 ? 1.1115 1.9273 0.8477 0.1735 -0.1646 0.2138 127 ARG B CZ 3570 N NH1 . ARG B 127 ? 1.1869 1.8928 0.8718 0.2576 -0.1628 0.2397 127 ARG B NH1 3571 N NH2 . ARG B 127 ? 1.1187 2.1036 0.8535 0.1637 -0.1787 0.2219 127 ARG B NH2 3572 N N . ASP B 128 ? 0.9326 1.4198 0.7225 -0.1732 -0.0826 0.0824 128 ASP B N 3573 C CA . ASP B 128 ? 0.9726 1.4306 0.7294 -0.2337 -0.0660 0.0643 128 ASP B CA 3574 C C . ASP B 128 ? 0.9766 1.3353 0.7124 -0.2208 -0.0566 0.0744 128 ASP B C 3575 O O . ASP B 128 ? 1.0096 1.3469 0.7122 -0.2610 -0.0432 0.0633 128 ASP B O 3576 C CB . ASP B 128 ? 1.0188 1.6062 0.7474 -0.2717 -0.0787 0.0616 128 ASP B CB 3577 C CG . ASP B 128 ? 1.0661 1.7246 0.7812 -0.2208 -0.1028 0.0931 128 ASP B CG 3578 O OD1 . ASP B 128 ? 1.0714 1.6950 0.7969 -0.1487 -0.1126 0.1178 128 ASP B OD1 3579 O OD2 . ASP B 128 ? 1.1263 1.8674 0.8093 -0.2530 -0.1103 0.0937 128 ASP B OD2 3580 N N . ASN B 129 ? 0.9661 1.2615 0.7123 -0.1711 -0.0615 0.0940 129 ASN B N 3581 C CA . ASN B 129 ? 0.9905 1.1965 0.7135 -0.1684 -0.0515 0.1036 129 ASN B CA 3582 C C . ASN B 129 ? 0.9663 1.0955 0.7075 -0.1917 -0.0252 0.0886 129 ASN B C 3583 O O . ASN B 129 ? 0.9835 1.0580 0.7096 -0.1941 -0.0155 0.0965 129 ASN B O 3584 C CB . ASN B 129 ? 1.0335 1.1946 0.7356 -0.1155 -0.0658 0.1319 129 ASN B CB 3585 C CG . ASN B 129 ? 1.1085 1.3248 0.7685 -0.0807 -0.0861 0.1546 129 ASN B CG 3586 O OD1 . ASN B 129 ? 1.1184 1.4475 0.7865 -0.0835 -0.0976 0.1519 129 ASN B OD1 3587 N ND2 . ASN B 129 ? 1.1754 1.3149 0.7819 -0.0497 -0.0895 0.1786 129 ASN B ND2 3588 N N . ALA B 130 ? 0.9191 1.0511 0.6866 -0.2074 -0.0129 0.0689 130 ALA B N 3589 C CA . ALA B 130 ? 0.8850 0.9562 0.6660 -0.2170 0.0136 0.0573 130 ALA B CA 3590 C C . ALA B 130 ? 0.8906 0.9593 0.6624 -0.2454 0.0318 0.0324 130 ALA B C 3591 O O . ALA B 130 ? 0.8976 1.0169 0.6715 -0.2574 0.0195 0.0252 130 ALA B O 3592 C CB . ALA B 130 ? 0.8473 0.8918 0.6649 -0.1871 0.0084 0.0687 130 ALA B CB 3593 N N . LYS B 131 ? 0.9011 0.9099 0.6539 -0.2544 0.0632 0.0206 131 LYS B N 3594 C CA . LYS B 131 ? 0.9318 0.9004 0.6514 -0.2772 0.0876 -0.0021 131 LYS B CA 3595 C C . LYS B 131 ? 0.8832 0.8333 0.6407 -0.2517 0.0911 -0.0012 131 LYS B C 3596 O O . LYS B 131 ? 0.8377 0.7732 0.6293 -0.2182 0.0963 0.0115 131 LYS B O 3597 C CB . LYS B 131 ? 1.0195 0.9140 0.6820 -0.2847 0.1257 -0.0130 131 LYS B CB 3598 C CG . LYS B 131 ? 1.1026 1.0051 0.7214 -0.3113 0.1269 -0.0151 131 LYS B CG 3599 C CD . LYS B 131 ? 1.2074 1.0316 0.7665 -0.3080 0.1684 -0.0243 131 LYS B CD 3600 C CE . LYS B 131 ? 1.2168 1.0651 0.7902 -0.2928 0.1671 -0.0079 131 LYS B CE 3601 N NZ . LYS B 131 ? 1.3308 1.1234 0.8255 -0.3093 0.2003 -0.0212 131 LYS B NZ 3602 N N . GLU B 132 ? 0.8774 0.8355 0.6254 -0.2729 0.0887 -0.0148 132 GLU B N 3603 C CA . GLU B 132 ? 0.8418 0.7742 0.6150 -0.2527 0.0951 -0.0160 132 GLU B CA 3604 C C . GLU B 132 ? 0.9220 0.7566 0.6378 -0.2505 0.1365 -0.0278 132 GLU B C 3605 O O . GLU B 132 ? 1.0075 0.7858 0.6453 -0.2896 0.1581 -0.0480 132 GLU B O 3606 C CB . GLU B 132 ? 0.8307 0.8120 0.6085 -0.2787 0.0787 -0.0255 132 GLU B CB 3607 C CG . GLU B 132 ? 0.7951 0.7667 0.6101 -0.2551 0.0773 -0.0233 132 GLU B CG 3608 C CD . GLU B 132 ? 0.7761 0.8192 0.6037 -0.2782 0.0581 -0.0300 132 GLU B CD 3609 O OE1 . GLU B 132 ? 0.7897 0.8997 0.5948 -0.3151 0.0470 -0.0364 132 GLU B OE1 3610 O OE2 . GLU B 132 ? 0.7367 0.7814 0.5969 -0.2597 0.0541 -0.0279 132 GLU B OE2 3611 N N . LEU B 133 ? 0.9040 0.7174 0.6472 -0.2045 0.1496 -0.0140 133 LEU B N 3612 C CA . LEU B 133 ? 0.9733 0.7013 0.6573 -0.1820 0.1922 -0.0186 133 LEU B CA 3613 C C . LEU B 133 ? 1.0229 0.6764 0.6611 -0.1794 0.2138 -0.0297 133 LEU B C 3614 O O . LEU B 133 ? 1.1189 0.6694 0.6669 -0.1707 0.2543 -0.0391 133 LEU B O 3615 C CB . LEU B 133 ? 0.9488 0.7098 0.6793 -0.1309 0.1990 0.0035 133 LEU B CB 3616 C CG . LEU B 133 ? 0.9752 0.7496 0.6900 -0.1291 0.2093 0.0091 133 LEU B CG 3617 C CD1 . LEU B 133 ? 0.9825 0.7736 0.6812 -0.1770 0.1885 -0.0001 133 LEU B CD1 3618 C CD2 . LEU B 133 ? 0.9161 0.7703 0.7004 -0.1014 0.1979 0.0332 133 LEU B CD2 3619 N N . GLY B 134 ? 0.9536 0.6476 0.6415 -0.1844 0.1899 -0.0282 134 GLY B N 3620 C CA . GLY B 134 ? 1.0044 0.6308 0.6493 -0.1868 0.2077 -0.0380 134 GLY B CA 3621 C C . GLY B 134 ? 0.9754 0.6064 0.6659 -0.1297 0.2118 -0.0203 134 GLY B C 3622 O O . GLY B 134 ? 1.0460 0.6141 0.6972 -0.1233 0.2286 -0.0252 134 GLY B O 3623 N N . ASN B 135 ? 0.8923 0.5993 0.6585 -0.0942 0.1964 0.0004 135 ASN B N 3624 C CA . ASN B 135 ? 0.8635 0.5978 0.6724 -0.0426 0.2010 0.0200 135 ASN B CA 3625 C C . ASN B 135 ? 0.7615 0.5950 0.6644 -0.0422 0.1633 0.0351 135 ASN B C 3626 O O . ASN B 135 ? 0.7398 0.6176 0.6818 -0.0103 0.1632 0.0524 135 ASN B O 3627 C CB . ASN B 135 ? 0.9153 0.6416 0.6976 0.0027 0.2325 0.0331 135 ASN B CB 3628 C CG . ASN B 135 ? 0.8877 0.6780 0.7022 -0.0108 0.2196 0.0394 135 ASN B CG 3629 O OD1 . ASN B 135 ? 0.8476 0.6738 0.6949 -0.0512 0.1882 0.0346 135 ASN B OD1 3630 N ND2 . ASN B 135 ? 0.9395 0.7442 0.7377 0.0265 0.2457 0.0516 135 ASN B ND2 3631 N N . GLY B 136 ? 0.7053 0.5718 0.6336 -0.0771 0.1333 0.0295 136 GLY B N 3632 C CA . GLY B 136 ? 0.6290 0.5568 0.6181 -0.0775 0.1020 0.0421 136 GLY B CA 3633 C C . GLY B 136 ? 0.6147 0.5724 0.6109 -0.0878 0.0916 0.0512 136 GLY B C 3634 O O . GLY B 136 ? 0.5707 0.5556 0.5931 -0.0944 0.0674 0.0608 136 GLY B O 3635 N N . CYS B 137 ? 0.6582 0.5974 0.6180 -0.0904 0.1119 0.0476 137 CYS B N 3636 C CA . CYS B 137 ? 0.6687 0.6334 0.6282 -0.1014 0.1061 0.0564 137 CYS B CA 3637 C C . CYS B 137 ? 0.6954 0.6457 0.6230 -0.1283 0.0966 0.0457 137 CYS B C 3638 O O . CYS B 137 ? 0.7335 0.6528 0.6244 -0.1427 0.1063 0.0290 137 CYS B O 3639 C CB . CYS B 137 ? 0.7071 0.6788 0.6504 -0.0807 0.1367 0.0632 137 CYS B CB 3640 S SG . CYS B 137 ? 0.6999 0.7295 0.6840 -0.0445 0.1472 0.0823 137 CYS B SG 3641 N N . PHE B 138 ? 0.6819 0.6547 0.6146 -0.1388 0.0783 0.0564 138 PHE B N 3642 C CA . PHE B 138 ? 0.7188 0.6914 0.6203 -0.1585 0.0695 0.0518 138 PHE B CA 3643 C C . PHE B 138 ? 0.7552 0.7297 0.6389 -0.1645 0.0807 0.0602 138 PHE B C 3644 O O . PHE B 138 ? 0.7715 0.7614 0.6711 -0.1630 0.0745 0.0757 138 PHE B O 3645 C CB . PHE B 138 ? 0.7082 0.6998 0.6187 -0.1565 0.0376 0.0606 138 PHE B CB 3646 C CG . PHE B 138 ? 0.6906 0.6958 0.6204 -0.1483 0.0261 0.0535 138 PHE B CG 3647 C CD1 . PHE B 138 ? 0.6959 0.7286 0.6099 -0.1641 0.0224 0.0402 138 PHE B CD1 3648 C CD2 . PHE B 138 ? 0.6621 0.6610 0.6223 -0.1310 0.0197 0.0597 138 PHE B CD2 3649 C CE1 . PHE B 138 ? 0.6830 0.7423 0.6148 -0.1606 0.0131 0.0339 138 PHE B CE1 3650 C CE2 . PHE B 138 ? 0.6462 0.6599 0.6231 -0.1229 0.0106 0.0531 138 PHE B CE2 3651 C CZ . PHE B 138 ? 0.6588 0.7055 0.6234 -0.1367 0.0077 0.0405 138 PHE B CZ 3652 N N . GLU B 139 ? 0.7996 0.7569 0.6425 -0.1774 0.0983 0.0490 139 GLU B N 3653 C CA . GLU B 139 ? 0.8365 0.7971 0.6572 -0.1838 0.1108 0.0553 139 GLU B CA 3654 C C . GLU B 139 ? 0.8648 0.8346 0.6626 -0.2053 0.0884 0.0586 139 GLU B C 3655 O O . GLU B 139 ? 0.8779 0.8480 0.6496 -0.2217 0.0828 0.0462 139 GLU B O 3656 C CB . GLU B 139 ? 0.9002 0.8234 0.6758 -0.1799 0.1480 0.0410 139 GLU B CB 3657 C CG . GLU B 139 ? 0.9436 0.8737 0.6939 -0.1809 0.1669 0.0466 139 GLU B CG 3658 C CD . GLU B 139 ? 1.0356 0.9086 0.7223 -0.1703 0.2081 0.0311 139 GLU B CD 3659 O OE1 . GLU B 139 ? 1.0616 0.8988 0.7357 -0.1409 0.2317 0.0264 139 GLU B OE1 3660 O OE2 . GLU B 139 ? 1.1093 0.9624 0.7471 -0.1897 0.2189 0.0240 139 GLU B OE2 3661 N N . PHE B 140 ? 0.8801 0.8600 0.6798 -0.2080 0.0764 0.0764 140 PHE B N 3662 C CA . PHE B 140 ? 0.9136 0.8940 0.6844 -0.2172 0.0534 0.0858 140 PHE B CA 3663 C C . PHE B 140 ? 0.9645 0.9465 0.6941 -0.2370 0.0644 0.0794 140 PHE B C 3664 O O . PHE B 140 ? 0.9787 0.9536 0.6977 -0.2433 0.0910 0.0742 140 PHE B O 3665 C CB . PHE B 140 ? 0.9143 0.8774 0.6768 -0.2180 0.0412 0.1071 140 PHE B CB 3666 C CG . PHE B 140 ? 0.8985 0.8461 0.6812 -0.2032 0.0264 0.1142 140 PHE B CG 3667 C CD1 . PHE B 140 ? 0.8844 0.8426 0.7021 -0.2047 0.0373 0.1138 140 PHE B CD1 3668 C CD2 . PHE B 140 ? 0.9221 0.8480 0.6825 -0.1837 0.0029 0.1230 140 PHE B CD2 3669 C CE1 . PHE B 140 ? 0.8751 0.8149 0.7042 -0.1965 0.0240 0.1192 140 PHE B CE1 3670 C CE2 . PHE B 140 ? 0.9190 0.8180 0.6861 -0.1678 -0.0075 0.1287 140 PHE B CE2 3671 C CZ . PHE B 140 ? 0.8958 0.7976 0.6966 -0.1790 0.0026 0.1254 140 PHE B CZ 3672 N N . TYR B 141 ? 1.0044 1.0031 0.7076 -0.2434 0.0447 0.0812 141 TYR B N 3673 C CA . TYR B 141 ? 1.0676 1.0720 0.7259 -0.2663 0.0510 0.0776 141 TYR B CA 3674 C C . TYR B 141 ? 1.0904 1.0786 0.7252 -0.2674 0.0465 0.0979 141 TYR B C 3675 O O . TYR B 141 ? 1.1686 1.1552 0.7690 -0.2867 0.0580 0.0959 141 TYR B O 3676 C CB . TYR B 141 ? 1.0852 1.1359 0.7220 -0.2764 0.0307 0.0736 141 TYR B CB 3677 C CG . TYR B 141 ? 1.0844 1.1513 0.7238 -0.2961 0.0393 0.0499 141 TYR B CG 3678 C CD1 . TYR B 141 ? 1.1351 1.1578 0.7414 -0.3233 0.0719 0.0272 141 TYR B CD1 3679 C CD2 . TYR B 141 ? 1.0633 1.1819 0.7264 -0.2875 0.0179 0.0504 141 TYR B CD2 3680 C CE1 . TYR B 141 ? 1.1608 1.1739 0.7464 -0.3491 0.0834 0.0047 141 TYR B CE1 3681 C CE2 . TYR B 141 ? 1.0772 1.2097 0.7336 -0.3164 0.0268 0.0281 141 TYR B CE2 3682 C CZ . TYR B 141 ? 1.1394 1.2105 0.7517 -0.3510 0.0598 0.0048 141 TYR B CZ 3683 O OH . TYR B 141 ? 1.1889 1.2504 0.7722 -0.3874 0.0721 -0.0181 141 TYR B OH 3684 N N . HIS B 142 ? 1.1222 1.4621 1.5456 -0.5318 -0.5472 0.1056 142 HIS B N 3685 C CA . HIS B 142 ? 1.1545 1.5039 1.4320 -0.5316 -0.5611 0.1485 142 HIS B CA 3686 C C . HIS B 142 ? 1.1461 1.3874 1.3690 -0.5567 -0.5503 0.1970 142 HIS B C 3687 O O . HIS B 142 ? 1.1310 1.2827 1.3929 -0.5607 -0.5353 0.2195 142 HIS B O 3688 C CB . HIS B 142 ? 1.2130 1.5280 1.3828 -0.4963 -0.5703 0.2130 142 HIS B CB 3689 C CG . HIS B 142 ? 1.2227 1.3950 1.3760 -0.4824 -0.5598 0.2653 142 HIS B CG 3690 N ND1 . HIS B 142 ? 1.2612 1.3017 1.3263 -0.4915 -0.5514 0.3260 142 HIS B ND1 3691 C CD2 . HIS B 142 ? 1.2026 1.3614 1.4223 -0.4613 -0.5555 0.2596 142 HIS B CD2 3692 C CE1 . HIS B 142 ? 1.2627 1.2238 1.3362 -0.4726 -0.5438 0.3512 142 HIS B CE1 3693 N NE2 . HIS B 142 ? 1.2255 1.2547 1.3898 -0.4526 -0.5460 0.3187 142 HIS B NE2 3694 N N . LYS B 143 ? 1.1634 1.4332 1.2993 -0.5732 -0.5565 0.2156 143 LYS B N 3695 C CA . LYS B 143 ? 1.1799 1.3597 1.2542 -0.6020 -0.5471 0.2605 143 LYS B CA 3696 C C . LYS B 143 ? 1.2045 1.2451 1.2096 -0.5917 -0.5409 0.3232 143 LYS B C 3697 O O . LYS B 143 ? 1.2563 1.2724 1.2113 -0.5633 -0.5461 0.3517 143 LYS B O 3698 C CB . LYS B 143 ? 1.2340 1.4705 1.2214 -0.6220 -0.5531 0.2806 143 LYS B CB 3699 C CG . LYS B 143 ? 1.2315 1.4706 1.2201 -0.6604 -0.5452 0.2753 143 LYS B CG 3700 C CD . LYS B 143 ? 1.2948 1.5721 1.1861 -0.6837 -0.5476 0.3154 143 LYS B CD 3701 C CE . LYS B 143 ? 1.3685 1.5038 1.1655 -0.7033 -0.5365 0.3893 143 LYS B CE 3702 N NZ . LYS B 143 ? 1.3603 1.4360 1.1598 -0.7415 -0.5259 0.3875 143 LYS B NZ 3703 N N . CYS B 144 ? 1.1653 1.1324 1.1738 -0.6096 -0.5286 0.3404 144 CYS B N 3704 C CA . CYS B 144 ? 1.1832 1.0418 1.1407 -0.5999 -0.5218 0.3806 144 CYS B CA 3705 C C . CYS B 144 ? 1.1928 1.0068 1.0934 -0.6388 -0.5130 0.3982 144 CYS B C 3706 O O . CYS B 144 ? 1.1329 0.9731 1.0803 -0.6500 -0.5043 0.3912 144 CYS B O 3707 C CB . CYS B 144 ? 1.1312 0.9900 1.1810 -0.5730 -0.5141 0.3740 144 CYS B CB 3708 S SG . CYS B 144 ? 1.1632 0.9285 1.1612 -0.5485 -0.5076 0.4121 144 CYS B SG 3709 N N . ASP B 145 ? 1.2754 1.0332 1.0837 -0.6592 -0.5121 0.4238 145 ASP B N 3710 C CA . ASP B 145 ? 1.3114 1.0297 1.0678 -0.7068 -0.5020 0.4320 145 ASP B CA 3711 C C . ASP B 145 ? 1.3337 0.9809 1.0757 -0.7053 -0.4925 0.4298 145 ASP B C 3712 O O . ASP B 145 ? 1.3105 0.9496 1.0858 -0.6649 -0.4940 0.4288 145 ASP B O 3713 C CB . ASP B 145 ? 1.4042 1.0804 1.0875 -0.7310 -0.4970 0.4646 145 ASP B CB 3714 C CG . ASP B 145 ? 1.4861 1.0657 1.1294 -0.6967 -0.4910 0.5000 145 ASP B CG 3715 O OD1 . ASP B 145 ? 1.4850 1.0218 1.1444 -0.6609 -0.4922 0.4911 145 ASP B OD1 3716 O OD2 . ASP B 145 ? 1.5622 1.1167 1.1627 -0.7008 -0.4821 0.5441 145 ASP B OD2 3717 N N . ASN B 146 ? 1.3872 0.9989 1.0840 -0.7505 -0.4821 0.4236 146 ASN B N 3718 C CA . ASN B 146 ? 1.4119 0.9888 1.0968 -0.7529 -0.4733 0.4040 146 ASN B CA 3719 C C . ASN B 146 ? 1.4910 0.9576 1.1472 -0.7200 -0.4685 0.4097 146 ASN B C 3720 O O . ASN B 146 ? 1.4894 0.9581 1.1580 -0.6914 -0.4670 0.3945 146 ASN B O 3721 C CB . ASN B 146 ? 1.4569 1.0353 1.1067 -0.8171 -0.4622 0.3797 146 ASN B CB 3722 C CG . ASN B 146 ? 1.3807 1.0863 1.0587 -0.8433 -0.4658 0.3748 146 ASN B CG 3723 O OD1 . ASN B 146 ? 1.2854 1.0738 1.0215 -0.8088 -0.4722 0.3858 146 ASN B OD1 3724 N ND2 . ASN B 146 ? 1.4265 1.1476 1.0733 -0.9049 -0.4578 0.3576 146 ASN B ND2 3725 N N . GLU B 147 ? 1.5785 0.9621 1.1998 -0.7180 -0.4636 0.4378 147 GLU B N 3726 C CA . GLU B 147 ? 1.6608 0.9446 1.2623 -0.6729 -0.4567 0.4552 147 GLU B CA 3727 C C . GLU B 147 ? 1.5740 0.9141 1.2136 -0.6106 -0.4720 0.4599 147 GLU B C 3728 O O . GLU B 147 ? 1.5979 0.8992 1.2372 -0.5740 -0.4688 0.4517 147 GLU B O 3729 C CB . GLU B 147 ? 1.7596 0.9819 1.3301 -0.6688 -0.4469 0.5072 147 GLU B CB 3730 C CG . GLU B 147 ? 1.8825 1.0183 1.4271 -0.7285 -0.4222 0.5146 147 GLU B CG 3731 C CD . GLU B 147 ? 2.0170 1.0074 1.5544 -0.7287 -0.3966 0.4946 147 GLU B CD 3732 O OE1 . GLU B 147 ? 2.1241 1.0140 1.6529 -0.6898 -0.3783 0.5421 147 GLU B OE1 3733 O OE2 . GLU B 147 ? 2.0355 1.0253 1.5809 -0.7639 -0.3931 0.4290 147 GLU B OE2 3734 N N . CYS B 148 ? 1.4742 0.9121 1.1542 -0.6013 -0.4866 0.4674 148 CYS B N 3735 C CA . CYS B 148 ? 1.3943 0.8958 1.1310 -0.5537 -0.4981 0.4654 148 CYS B CA 3736 C C . CYS B 148 ? 1.3302 0.8722 1.1192 -0.5456 -0.4954 0.4480 148 CYS B C 3737 O O . CYS B 148 ? 1.3151 0.8617 1.1302 -0.5038 -0.4960 0.4527 148 CYS B O 3738 C CB . CYS B 148 ? 1.3342 0.9389 1.1185 -0.5579 -0.5100 0.4577 148 CYS B CB 3739 S SG . CYS B 148 ? 1.2421 0.9404 1.1353 -0.5191 -0.5185 0.4343 148 CYS B SG 3740 N N . MET B 149 ? 1.2848 0.8728 1.0908 -0.5818 -0.4906 0.4356 149 MET B N 3741 C CA . MET B 149 ? 1.2264 0.8793 1.0828 -0.5694 -0.4835 0.4349 149 MET B CA 3742 C C . MET B 149 ? 1.2941 0.9020 1.1013 -0.5546 -0.4776 0.4250 149 MET B C 3743 O O . MET B 149 ? 1.2689 0.9219 1.1120 -0.5164 -0.4744 0.4344 149 MET B O 3744 C CB . MET B 149 ? 1.1864 0.9119 1.0594 -0.6071 -0.4772 0.4292 149 MET B CB 3745 C CG . MET B 149 ? 1.1202 0.9020 1.0538 -0.6187 -0.4795 0.4304 149 MET B CG 3746 S SD . MET B 149 ? 1.0264 0.8667 1.0965 -0.5746 -0.4738 0.4419 149 MET B SD 3747 C CE . MET B 149 ? 0.9775 0.8912 1.1236 -0.5973 -0.4674 0.4268 149 MET B CE 3748 N N . GLU B 150 ? 1.3944 0.9172 1.1286 -0.5855 -0.4730 0.4036 150 GLU B N 3749 C CA . GLU B 150 ? 1.4835 0.9564 1.1791 -0.5762 -0.4640 0.3746 150 GLU B CA 3750 C C . GLU B 150 ? 1.5038 0.9326 1.2016 -0.5151 -0.4661 0.3893 150 GLU B C 3751 O O . GLU B 150 ? 1.5265 0.9797 1.2243 -0.4864 -0.4617 0.3701 150 GLU B O 3752 C CB . GLU B 150 ? 1.6074 0.9711 1.2464 -0.6252 -0.4518 0.3466 150 GLU B CB 3753 C CG . GLU B 150 ? 1.7137 1.0109 1.3263 -0.6230 -0.4370 0.2959 150 GLU B CG 3754 C CD . GLU B 150 ? 1.6754 1.1048 1.3036 -0.6213 -0.4377 0.2521 150 GLU B CD 3755 O OE1 . GLU B 150 ? 1.5845 1.1494 1.2419 -0.6303 -0.4450 0.2687 150 GLU B OE1 3756 O OE2 . GLU B 150 ? 1.7528 1.1624 1.3680 -0.6062 -0.4284 0.2017 150 GLU B OE2 3757 N N . SER B 151 ? 1.5024 0.8897 1.2020 -0.4928 -0.4730 0.4212 151 SER B N 3758 C CA . SER B 151 ? 1.5274 0.8850 1.2268 -0.4332 -0.4751 0.4379 151 SER B CA 3759 C C . SER B 151 ? 1.4412 0.9077 1.2087 -0.3974 -0.4817 0.4476 151 SER B C 3760 O O . SER B 151 ? 1.4689 0.9369 1.2382 -0.3499 -0.4807 0.4515 151 SER B O 3761 C CB . SER B 151 ? 1.5520 0.8772 1.2382 -0.4168 -0.4807 0.4717 151 SER B CB 3762 O OG . SER B 151 ? 1.4575 0.8856 1.2011 -0.4211 -0.4946 0.4788 151 SER B OG 3763 N N . VAL B 152 ? 1.3494 0.9070 1.1822 -0.4185 -0.4843 0.4554 152 VAL B N 3764 C CA . VAL B 152 ? 1.2577 0.9155 1.1781 -0.3902 -0.4812 0.4754 152 VAL B CA 3765 C C . VAL B 152 ? 1.2690 0.9792 1.1799 -0.3758 -0.4710 0.4731 152 VAL B C 3766 O O . VAL B 152 ? 1.2507 1.0096 1.1908 -0.3328 -0.4676 0.4895 152 VAL B O 3767 C CB . VAL B 152 ? 1.1700 0.8995 1.1806 -0.4144 -0.4781 0.4864 152 VAL B CB 3768 C CG1 . VAL B 152 ? 1.1022 0.9259 1.2235 -0.3865 -0.4641 0.5194 152 VAL B CG1 3769 C CG2 . VAL B 152 ? 1.1642 0.8768 1.1934 -0.4225 -0.4893 0.4739 152 VAL B CG2 3770 N N . ARG B 153 ? 1.3081 1.0280 1.1780 -0.4114 -0.4663 0.4490 153 ARG B N 3771 C CA . ARG B 153 ? 1.3408 1.1424 1.1950 -0.3990 -0.4578 0.4322 153 ARG B CA 3772 C C . ARG B 153 ? 1.4703 1.1981 1.2614 -0.3734 -0.4579 0.3923 153 ARG B C 3773 O O . ARG B 153 ? 1.4720 1.2845 1.2668 -0.3385 -0.4529 0.3828 153 ARG B O 3774 C CB . ARG B 153 ? 1.3413 1.1895 1.1671 -0.4481 -0.4533 0.4021 153 ARG B CB 3775 C CG . ARG B 153 ? 1.2486 1.1713 1.1341 -0.4696 -0.4501 0.4395 153 ARG B CG 3776 C CD . ARG B 153 ? 1.2524 1.2580 1.1085 -0.5105 -0.4451 0.4112 153 ARG B CD 3777 N NE . ARG B 153 ? 1.2304 1.2010 1.0871 -0.5562 -0.4482 0.4126 153 ARG B NE 3778 C CZ . ARG B 153 ? 1.2967 1.1611 1.0903 -0.6057 -0.4538 0.3734 153 ARG B CZ 3779 N NH1 . ARG B 153 ? 1.3879 1.1509 1.1202 -0.6179 -0.4532 0.3287 153 ARG B NH1 3780 N NH2 . ARG B 153 ? 1.2786 1.1401 1.0791 -0.6416 -0.4562 0.3817 153 ARG B NH2 3781 N N . ASN B 154 ? 1.6125 1.1916 1.3517 -0.3871 -0.4601 0.3726 154 ASN B N 3782 C CA . ASN B 154 ? 1.7631 1.2427 1.4552 -0.3556 -0.4543 0.3422 154 ASN B CA 3783 C C . ASN B 154 ? 1.7198 1.2421 1.4360 -0.2873 -0.4579 0.3681 154 ASN B C 3784 O O . ASN B 154 ? 1.7972 1.3142 1.4897 -0.2524 -0.4512 0.3341 154 ASN B O 3785 C CB . ASN B 154 ? 1.9061 1.2292 1.5610 -0.3675 -0.4514 0.3529 154 ASN B CB 3786 C CG . ASN B 154 ? 2.1306 1.3497 1.7458 -0.4184 -0.4353 0.3058 154 ASN B CG 3787 O OD1 . ASN B 154 ? 2.2019 1.4596 1.8118 -0.4436 -0.4273 0.2451 154 ASN B OD1 3788 N ND2 . ASN B 154 ? 2.3346 1.4341 1.9287 -0.4345 -0.4277 0.3334 154 ASN B ND2 3789 N N . GLY B 155 ? 1.5976 1.1674 1.3676 -0.2709 -0.4671 0.4204 155 GLY B N 3790 C CA . GLY B 155 ? 1.5521 1.1451 1.3473 -0.2133 -0.4712 0.4478 155 GLY B CA 3791 C C . GLY B 155 ? 1.5786 1.0701 1.3424 -0.1992 -0.4767 0.4608 155 GLY B C 3792 O O . GLY B 155 ? 1.5760 1.0831 1.3495 -0.1496 -0.4805 0.4801 155 GLY B O 3793 N N . THR B 156 ? 1.6037 1.0143 1.3341 -0.2412 -0.4761 0.4567 156 THR B N 3794 C CA . THR B 156 ? 1.6702 0.9812 1.3560 -0.2258 -0.4739 0.4761 156 THR B CA 3795 C C . THR B 156 ? 1.6056 0.9672 1.3179 -0.2422 -0.4867 0.5039 156 THR B C 3796 O O . THR B 156 ? 1.6676 0.9835 1.3454 -0.2289 -0.4849 0.5305 156 THR B O 3797 C CB . THR B 156 ? 1.7751 0.9570 1.4071 -0.2622 -0.4565 0.4538 156 THR B CB 3798 O OG1 . THR B 156 ? 1.8463 0.9799 1.4594 -0.2423 -0.4421 0.4106 156 THR B OG1 3799 C CG2 . THR B 156 ? 1.8752 0.9584 1.4730 -0.2488 -0.4466 0.4952 156 THR B CG2 3800 N N . TYR B 157 ? 1.4936 0.9592 1.2750 -0.2673 -0.4963 0.4982 157 TYR B N 3801 C CA . TYR B 157 ? 1.4450 0.9699 1.2634 -0.2904 -0.5070 0.5025 157 TYR B CA 3802 C C . TYR B 157 ? 1.4783 1.0383 1.2914 -0.2460 -0.5154 0.5206 157 TYR B C 3803 O O . TYR B 157 ? 1.4367 1.0630 1.2945 -0.2101 -0.5199 0.5210 157 TYR B O 3804 C CB . TYR B 157 ? 1.3318 0.9587 1.2532 -0.3124 -0.5092 0.4895 157 TYR B CB 3805 C CG . TYR B 157 ? 1.2712 0.9714 1.2512 -0.3332 -0.5184 0.4734 157 TYR B CG 3806 C CD1 . TYR B 157 ? 1.2742 0.9670 1.2317 -0.3743 -0.5208 0.4623 157 TYR B CD1 3807 C CD2 . TYR B 157 ? 1.2151 1.0059 1.2785 -0.3139 -0.5238 0.4603 157 TYR B CD2 3808 C CE1 . TYR B 157 ? 1.2236 1.0029 1.2371 -0.3905 -0.5293 0.4350 157 TYR B CE1 3809 C CE2 . TYR B 157 ? 1.1754 1.0502 1.3023 -0.3355 -0.5314 0.4250 157 TYR B CE2 3810 C CZ . TYR B 157 ? 1.1776 1.0491 1.2776 -0.3713 -0.5346 0.4105 157 TYR B CZ 3811 O OH . TYR B 157 ? 1.1377 1.1121 1.3040 -0.3898 -0.5421 0.3634 157 TYR B OH 3812 N N . ASP B 158 ? 1.5713 1.1043 1.3323 -0.2467 -0.5156 0.5410 158 ASP B N 3813 C CA . ASP B 158 ? 1.6408 1.2290 1.3862 -0.1951 -0.5210 0.5690 158 ASP B CA 3814 C C . ASP B 158 ? 1.5770 1.3271 1.3964 -0.2065 -0.5388 0.5387 158 ASP B C 3815 O O . ASP B 158 ? 1.5741 1.3807 1.3972 -0.2370 -0.5447 0.5280 158 ASP B O 3816 C CB . ASP B 158 ? 1.7542 1.2691 1.4232 -0.1817 -0.5081 0.6190 158 ASP B CB 3817 C CG . ASP B 158 ? 1.8180 1.3799 1.4620 -0.1077 -0.5061 0.6670 158 ASP B CG 3818 O OD1 . ASP B 158 ? 1.8040 1.3961 1.4667 -0.0626 -0.5100 0.6608 158 ASP B OD1 3819 O OD2 . ASP B 158 ? 1.8978 1.4821 1.5053 -0.0906 -0.4990 0.7179 158 ASP B OD2 3820 N N . TYR B 159 ? 1.5410 1.3724 1.4272 -0.1834 -0.5452 0.5185 159 TYR B N 3821 C CA . TYR B 159 ? 1.4674 1.4510 1.4533 -0.2007 -0.5573 0.4708 159 TYR B CA 3822 C C . TYR B 159 ? 1.5169 1.6284 1.4800 -0.1762 -0.5697 0.4698 159 TYR B C 3823 O O . TYR B 159 ? 1.4886 1.7060 1.5004 -0.2100 -0.5784 0.4235 159 TYR B O 3824 C CB . TYR B 159 ? 1.4101 1.4427 1.4806 -0.1842 -0.5553 0.4562 159 TYR B CB 3825 C CG . TYR B 159 ? 1.3412 1.5361 1.5251 -0.1947 -0.5639 0.4025 159 TYR B CG 3826 C CD1 . TYR B 159 ? 1.3599 1.6773 1.5297 -0.1527 -0.5760 0.3986 159 TYR B CD1 3827 C CD2 . TYR B 159 ? 1.2619 1.4960 1.5790 -0.2455 -0.5562 0.3529 159 TYR B CD2 3828 C CE1 . TYR B 159 ? 1.3010 1.7879 1.5846 -0.1691 -0.5836 0.3323 159 TYR B CE1 3829 C CE2 . TYR B 159 ? 1.2125 1.5901 1.6550 -0.2626 -0.5591 0.2881 159 TYR B CE2 3830 C CZ . TYR B 159 ? 1.2258 1.7353 1.6503 -0.2282 -0.5744 0.2708 159 TYR B CZ 3831 O OH . TYR B 159 ? 1.1773 1.8487 1.7350 -0.2519 -0.5772 0.1901 159 TYR B OH 3832 N N . PRO B 160 ? 1.6141 1.7324 1.5067 -0.1123 -0.5687 0.5212 160 PRO B N 3833 C CA . PRO B 160 ? 1.6551 1.9252 1.5201 -0.0796 -0.5780 0.5358 160 PRO B CA 3834 C C . PRO B 160 ? 1.6918 1.9598 1.5040 -0.1028 -0.5754 0.5594 160 PRO B C 3835 O O . PRO B 160 ? 1.6924 2.1376 1.5065 -0.0902 -0.5859 0.5518 160 PRO B O 3836 C CB . PRO B 160 ? 1.7397 1.9804 1.5342 0.0017 -0.5686 0.6090 160 PRO B CB 3837 C CG . PRO B 160 ? 1.7224 1.8634 1.5418 0.0088 -0.5629 0.5982 160 PRO B CG 3838 C CD . PRO B 160 ? 1.6694 1.6932 1.5191 -0.0599 -0.5582 0.5637 160 PRO B CD 3839 N N . GLN B 161 ? 1.7217 1.8136 1.4900 -0.1359 -0.5610 0.5858 161 GLN B N 3840 C CA . GLN B 161 ? 1.7488 1.8359 1.4752 -0.1664 -0.5562 0.6093 161 GLN B CA 3841 C C . GLN B 161 ? 1.6348 1.8553 1.4327 -0.2201 -0.5728 0.5298 161 GLN B C 3842 O O . GLN B 161 ? 1.6382 1.9998 1.4250 -0.2201 -0.5798 0.5287 161 GLN B O 3843 C CB . GLN B 161 ? 1.8166 1.6922 1.4948 -0.1994 -0.5361 0.6406 161 GLN B CB 3844 C CG . GLN B 161 ? 1.8729 1.7356 1.5084 -0.2328 -0.5268 0.6752 161 GLN B CG 3845 C CD . GLN B 161 ? 1.9341 1.6032 1.5382 -0.2780 -0.5068 0.6876 161 GLN B CD 3846 O OE1 . GLN B 161 ? 1.9441 1.4949 1.5525 -0.2798 -0.5002 0.6682 161 GLN B OE1 3847 N NE2 . GLN B 161 ? 1.9774 1.6335 1.5529 -0.3159 -0.4968 0.7158 161 GLN B NE2 3848 N N . TYR B 162 ? 1.5217 1.7053 1.3991 -0.2615 -0.5755 0.4664 162 TYR B N 3849 C CA . TYR B 162 ? 1.4232 1.7116 1.3904 -0.3097 -0.5843 0.3864 162 TYR B CA 3850 C C . TYR B 162 ? 1.3473 1.7837 1.4254 -0.3020 -0.5945 0.3136 162 TYR B C 3851 O O . TYR B 162 ? 1.2934 1.8977 1.4336 -0.3169 -0.6050 0.2439 162 TYR B O 3852 C CB . TYR B 162 ? 1.3897 1.5515 1.3924 -0.3584 -0.5734 0.3711 162 TYR B CB 3853 C CG . TYR B 162 ? 1.4556 1.4689 1.3610 -0.3747 -0.5617 0.4297 162 TYR B CG 3854 C CD1 . TYR B 162 ? 1.4828 1.5166 1.3396 -0.4004 -0.5612 0.4437 162 TYR B CD1 3855 C CD2 . TYR B 162 ? 1.4836 1.3508 1.3548 -0.3680 -0.5496 0.4630 162 TYR B CD2 3856 C CE1 . TYR B 162 ? 1.5407 1.4421 1.3242 -0.4243 -0.5473 0.4905 162 TYR B CE1 3857 C CE2 . TYR B 162 ? 1.5419 1.2845 1.3398 -0.3907 -0.5369 0.4975 162 TYR B CE2 3858 C CZ . TYR B 162 ? 1.5701 1.3239 1.3279 -0.4218 -0.5349 0.5115 162 TYR B CZ 3859 O OH . TYR B 162 ? 1.6269 1.2592 1.3256 -0.4523 -0.5193 0.5399 162 TYR B OH # _database_PDB_caveat.id 1 _database_PDB_caveat.text 'NAG B1163 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 1322 1322 NAG NAG A . D 3 NAG 2 1323 1323 NAG NAG A . E 3 NAG 1 1324 1324 NAG NAG A . F 3 NAG 2 1325 1325 NAG NAG A . G 4 SIA 1 1326 1326 SIA SIA A . H 5 GAL 2 1327 1327 GAL GAL A . I 3 NAG 3 1328 1328 NAG NAG A . J 3 NAG 1 1163 1163 NAG NAG B . K 3 NAG 2 1164 1164 NAG NAG B . L 6 EPE 1 1165 1165 EPE EPE B . M 7 HOH 1 2001 2001 HOH HOH A . M 7 HOH 2 2002 2002 HOH HOH A . M 7 HOH 3 2003 2003 HOH HOH A . M 7 HOH 4 2004 2004 HOH HOH A . M 7 HOH 5 2005 2005 HOH HOH A . M 7 HOH 6 2006 2006 HOH HOH A . M 7 HOH 7 2007 2007 HOH HOH A . M 7 HOH 8 2008 2008 HOH HOH A . M 7 HOH 9 2009 2009 HOH HOH A . M 7 HOH 10 2010 2010 HOH HOH A . M 7 HOH 11 2011 2011 HOH HOH A . M 7 HOH 12 2012 2012 HOH HOH A . M 7 HOH 13 2013 2013 HOH HOH A . M 7 HOH 14 2014 2014 HOH HOH A . M 7 HOH 15 2015 2015 HOH HOH A . M 7 HOH 16 2016 2016 HOH HOH A . M 7 HOH 17 2017 2017 HOH HOH A . M 7 HOH 18 2018 2018 HOH HOH A . M 7 HOH 19 2019 2019 HOH HOH A . M 7 HOH 20 2020 2020 HOH HOH A . M 7 HOH 21 2021 2021 HOH HOH A . M 7 HOH 22 2022 2022 HOH HOH A . M 7 HOH 23 2023 2023 HOH HOH A . M 7 HOH 24 2024 2024 HOH HOH A . M 7 HOH 25 2025 2025 HOH HOH A . M 7 HOH 26 2026 2026 HOH HOH A . M 7 HOH 27 2027 2027 HOH HOH A . M 7 HOH 28 2028 2028 HOH HOH A . M 7 HOH 29 2029 2029 HOH HOH A . M 7 HOH 30 2030 2030 HOH HOH A . M 7 HOH 31 2031 2031 HOH HOH A . M 7 HOH 32 2032 2032 HOH HOH A . M 7 HOH 33 2033 2033 HOH HOH A . M 7 HOH 34 2034 2034 HOH HOH A . M 7 HOH 35 2035 2035 HOH HOH A . M 7 HOH 36 2036 2036 HOH HOH A . M 7 HOH 37 2037 2037 HOH HOH A . M 7 HOH 38 2038 2038 HOH HOH A . M 7 HOH 39 2039 2039 HOH HOH A . M 7 HOH 40 2040 2040 HOH HOH A . M 7 HOH 41 2041 2041 HOH HOH A . M 7 HOH 42 2042 2042 HOH HOH A . M 7 HOH 43 2043 2043 HOH HOH A . M 7 HOH 44 2044 2044 HOH HOH A . M 7 HOH 45 2045 2045 HOH HOH A . M 7 HOH 46 2046 2046 HOH HOH A . M 7 HOH 47 2047 2047 HOH HOH A . M 7 HOH 48 2048 2048 HOH HOH A . M 7 HOH 49 2049 2049 HOH HOH A . M 7 HOH 50 2050 2050 HOH HOH A . M 7 HOH 51 2051 2051 HOH HOH A . M 7 HOH 52 2052 2052 HOH HOH A . M 7 HOH 53 2053 2053 HOH HOH A . M 7 HOH 54 2054 2054 HOH HOH A . M 7 HOH 55 2055 2055 HOH HOH A . M 7 HOH 56 2056 2056 HOH HOH A . M 7 HOH 57 2057 2057 HOH HOH A . M 7 HOH 58 2058 2058 HOH HOH A . M 7 HOH 59 2059 2059 HOH HOH A . M 7 HOH 60 2060 2060 HOH HOH A . M 7 HOH 61 2061 2061 HOH HOH A . M 7 HOH 62 2062 2062 HOH HOH A . M 7 HOH 63 2063 2063 HOH HOH A . M 7 HOH 64 2064 2064 HOH HOH A . M 7 HOH 65 2065 2065 HOH HOH A . M 7 HOH 66 2066 2066 HOH HOH A . M 7 HOH 67 2067 2067 HOH HOH A . M 7 HOH 68 2068 2068 HOH HOH A . M 7 HOH 69 2069 2069 HOH HOH A . M 7 HOH 70 2070 2070 HOH HOH A . M 7 HOH 71 2071 2071 HOH HOH A . M 7 HOH 72 2072 2072 HOH HOH A . M 7 HOH 73 2073 2073 HOH HOH A . N 7 HOH 1 2001 2001 HOH HOH B . N 7 HOH 2 2002 2002 HOH HOH B . N 7 HOH 3 2003 2003 HOH HOH B . N 7 HOH 4 2004 2004 HOH HOH B . N 7 HOH 5 2005 2005 HOH HOH B . N 7 HOH 6 2006 2006 HOH HOH B . N 7 HOH 7 2007 2007 HOH HOH B . N 7 HOH 8 2008 2008 HOH HOH B . N 7 HOH 9 2009 2009 HOH HOH B . N 7 HOH 10 2010 2010 HOH HOH B . N 7 HOH 11 2011 2011 HOH HOH B . N 7 HOH 12 2012 2012 HOH HOH B . N 7 HOH 13 2013 2013 HOH HOH B . N 7 HOH 14 2014 2014 HOH HOH B . N 7 HOH 15 2015 2015 HOH HOH B . N 7 HOH 16 2016 2016 HOH HOH B . N 7 HOH 17 2017 2017 HOH HOH B . N 7 HOH 18 2018 2018 HOH HOH B . N 7 HOH 19 2019 2019 HOH HOH B . N 7 HOH 20 2020 2020 HOH HOH B . N 7 HOH 21 2021 2021 HOH HOH B . N 7 HOH 22 2022 2022 HOH HOH B . N 7 HOH 23 2023 2023 HOH HOH B . N 7 HOH 24 2024 2024 HOH HOH B . N 7 HOH 25 2025 2025 HOH HOH B . N 7 HOH 26 2026 2026 HOH HOH B . N 7 HOH 27 2027 2027 HOH HOH B . N 7 HOH 28 2028 2028 HOH HOH B . N 7 HOH 29 2029 2029 HOH HOH B . N 7 HOH 30 2030 2030 HOH HOH B . N 7 HOH 31 2031 2031 HOH HOH B . N 7 HOH 32 2032 2032 HOH HOH B . N 7 HOH 33 2033 2033 HOH HOH B . N 7 HOH 34 2034 2034 HOH HOH B . N 7 HOH 35 2035 2035 HOH HOH B . N 7 HOH 36 2036 2036 HOH HOH B . N 7 HOH 37 2037 2037 HOH HOH B . N 7 HOH 38 2038 2038 HOH HOH B . N 7 HOH 39 2039 2039 HOH HOH B . N 7 HOH 40 2040 2040 HOH HOH B . N 7 HOH 41 2041 2041 HOH HOH B . N 7 HOH 42 2042 2042 HOH HOH B . N 7 HOH 43 2043 2043 HOH HOH B . N 7 HOH 44 2044 2044 HOH HOH B . N 7 HOH 45 2045 2045 HOH HOH B . N 7 HOH 46 2046 2046 HOH HOH B . N 7 HOH 47 2047 2047 HOH HOH B . N 7 HOH 48 2048 2048 HOH HOH B . N 7 HOH 49 2049 2049 HOH HOH B . N 7 HOH 50 2050 2050 HOH HOH B . N 7 HOH 51 2051 2051 HOH HOH B . N 7 HOH 52 2052 2052 HOH HOH B . N 7 HOH 53 2053 2053 HOH HOH B . N 7 HOH 54 2054 2054 HOH HOH B . N 7 HOH 55 2055 2055 HOH HOH B . N 7 HOH 56 2056 2056 HOH HOH B . N 7 HOH 57 2057 2057 HOH HOH B . N 7 HOH 58 2058 2058 HOH HOH B . N 7 HOH 59 2059 2059 HOH HOH B . N 7 HOH 60 2060 2060 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,K,L,M,N # 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)' 35310 ? 1 MORE -73.3 ? 1 'SSA (A^2)' 61600 ? # 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_565 -y,x-y+1,z -0.5000000000 -0.8660254038 0.0000000000 -50.7015000000 0.8660254038 -0.5000000000 0.0000000000 87.8175740200 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_455 -x+y-1,-x,z -0.5000000000 0.8660254038 0.0000000000 -101.4030000000 -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 2018 ? N HOH . 2 1 B HOH 2034 ? N 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 2 'Structure model' 'Refinement description' 3 3 'Structure model' 'Database references' 4 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 -29.4250 35.8230 56.1846 0.3523 0.5294 0.3862 -0.2065 -0.1174 0.0458 0.3295 0.2096 4.5523 0.0416 0.0424 0.3007 -0.0197 -0.1751 0.0662 0.1819 -0.0428 -0.1846 -0.3640 1.2153 0.0625 'X-RAY DIFFRACTION' 2 ? refined -34.8932 41.3834 91.3924 0.7602 0.7496 0.2893 -0.1877 -0.1802 -0.0284 2.4582 2.1856 1.8952 -0.4432 -0.4803 0.5561 -0.4523 -0.5801 0.1394 0.5213 0.2305 -0.1246 -0.4025 0.5767 0.2217 'X-RAY DIFFRACTION' 3 ? refined -30.6045 35.1777 48.0547 0.2337 0.4413 0.3881 -0.1129 -0.0855 -0.0069 0.4246 0.9261 12.1588 0.2873 1.3939 -0.0854 0.1225 -0.1005 0.0704 0.2940 -0.0337 -0.3068 -0.3494 0.5023 -0.0888 'X-RAY DIFFRACTION' 4 ? refined -36.3729 37.7606 16.3815 0.2246 0.2730 0.2946 -0.1650 -0.1091 0.0961 4.2742 2.4325 7.5737 1.3166 -3.7530 -0.5055 -0.2636 -0.1322 0.2554 -0.1066 0.0499 -0.0728 -0.7002 0.9051 0.2136 'X-RAY DIFFRACTION' 5 ? refined -43.7693 28.2210 64.5760 0.1628 0.2122 0.2860 -0.0014 -0.0131 0.0279 3.6461 5.6449 21.2323 0.4752 -0.9868 -6.4150 -0.1575 0.1968 0.0715 0.0041 -0.2049 -0.3905 -0.2979 1.2787 0.3624 'X-RAY DIFFRACTION' 6 ? refined -43.0838 32.0345 18.3750 0.0580 0.0606 0.2410 -0.0300 -0.0049 0.0233 1.7975 1.5341 15.6874 0.8015 -2.5762 -1.2277 -0.3082 0.2126 -0.0129 -0.1584 -0.0991 -0.0831 0.1945 -0.4256 0.4073 'X-RAY DIFFRACTION' 7 ? refined -38.4636 44.4360 -5.4738 1.0285 0.5893 0.8424 -0.4561 -0.5106 0.4715 20.2040 0.5242 8.4604 -2.5997 -4.3986 0.2190 0.0593 0.8767 0.2296 -0.1879 0.1512 0.3480 -2.0763 -0.2336 -0.2105 # 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 4BGY _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 SER 155 ? ? NE2 A GLN 192 ? ? 1.10 2 1 O A SER 155 ? ? CD A GLN 192 ? ? 1.83 3 1 OE1 B GLU 150 ? ? NH1 B ARG 153 ? ? 2.08 # _pdbx_validate_symm_contact.id 1 _pdbx_validate_symm_contact.PDB_model_num 1 _pdbx_validate_symm_contact.auth_atom_id_1 OE2 _pdbx_validate_symm_contact.auth_asym_id_1 A _pdbx_validate_symm_contact.auth_comp_id_1 GLU _pdbx_validate_symm_contact.auth_seq_id_1 170 _pdbx_validate_symm_contact.PDB_ins_code_1 ? _pdbx_validate_symm_contact.label_alt_id_1 ? _pdbx_validate_symm_contact.site_symmetry_1 1_555 _pdbx_validate_symm_contact.auth_atom_id_2 OE2 _pdbx_validate_symm_contact.auth_asym_id_2 A _pdbx_validate_symm_contact.auth_comp_id_2 GLU _pdbx_validate_symm_contact.auth_seq_id_2 170 _pdbx_validate_symm_contact.PDB_ins_code_2 ? _pdbx_validate_symm_contact.label_alt_id_2 ? _pdbx_validate_symm_contact.site_symmetry_2 11_565 _pdbx_validate_symm_contact.dist 2.07 # 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 ? ? 62.85 -129.64 2 1 ASN A 72 ? ? 39.76 42.25 3 1 ASP A 88 ? ? -104.78 -129.56 4 1 LEU A 89 ? ? -68.79 94.84 5 1 SER A 142 ? ? -129.38 -159.30 6 1 PHE A 144 ? ? -38.54 114.19 7 1 GLN A 192 ? ? 66.63 -63.65 8 1 THR A 202 ? ? -128.73 -158.71 9 1 GLU A 251 ? ? -104.86 -62.77 10 1 HIS A 295 ? ? -173.68 137.81 11 1 ALA B 5 ? ? -91.43 -65.24 12 1 ARG B 127 ? ? 57.20 -132.87 # _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 1163 _pdbx_validate_chiral.PDB_ins_code ? _pdbx_validate_chiral.details 'WRONG HAND' _pdbx_validate_chiral.omega . # 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 #