data_3KU5 # _entry.id 3KU5 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3KU5 RCSB RCSB056450 WWPDB D_1000056450 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3KU3 . unspecified PDB 3KU6 . unspecified # _pdbx_database_status.entry_id 3KU5 _pdbx_database_status.status_code REL _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.recvd_initial_deposition_date 2009-11-26 _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xu, R.' 1 'Wilson, I.A.' 2 # _citation.id primary _citation.title 'Structure, receptor binding, and antigenicity of influenza virus hemagglutinins from the 1957 H2N2 pandemic.' _citation.journal_abbrev J.Virol. _citation.journal_volume 84 _citation.page_first 1715 _citation.page_last 1721 _citation.year 2010 _citation.journal_id_ASTM JOVIAM _citation.country US _citation.journal_id_ISSN 0022-538X _citation.journal_id_CSD 0825 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 20007271 _citation.pdbx_database_id_DOI 10.1128/JVI.02162-09 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Xu, R.' 1 primary 'McBride, R.' 2 primary 'Paulson, J.C.' 3 primary 'Basler, C.F.' 4 primary 'Wilson, I.A.' 5 # _cell.entry_id 3KU5 _cell.length_a 70.694 _cell.length_b 70.694 _cell.length_c 236.751 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 6 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3KU5 _symmetry.space_group_name_H-M 'P 63' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 173 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Hemagglutinin HA1 chain' 36519.281 1 ? 'Q226L, G228S' 'UNP residues 15-340' ? 2 polymer man 'Hemagglutinin HA2 chain' 20139.295 1 ? ? 'UNP residues 341-514' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 4 non-polymer syn 1,2-ETHANEDIOL 62.068 1 ? ? ? ? 5 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120 1 ? ? ? ? 6 water nat water 18.015 582 ? ? ? ? # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;PGDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSY IMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPV AKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGLGSRMEFSWTLLDMWDTI NFESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRN VPQIESR ; ;PGDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSY IMEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPV AKGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGLGSRMEFSWTLLDMWDTI NFESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRN VPQIESR ; A ? 2 'polypeptide(L)' no no ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP KYEEESKLNRNEIK ; ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP KYEEESKLNRNEIK ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 PRO n 1 2 GLY n 1 3 ASP n 1 4 GLN n 1 5 ILE n 1 6 CYS n 1 7 ILE n 1 8 GLY n 1 9 TYR n 1 10 HIS n 1 11 ALA n 1 12 ASN n 1 13 ASN n 1 14 SER n 1 15 THR n 1 16 GLU n 1 17 LYS n 1 18 VAL n 1 19 ASP n 1 20 THR n 1 21 ILE n 1 22 LEU n 1 23 GLU n 1 24 ARG n 1 25 ASN n 1 26 VAL n 1 27 THR n 1 28 VAL n 1 29 THR n 1 30 HIS n 1 31 ALA n 1 32 LYS n 1 33 ASP n 1 34 ILE n 1 35 LEU n 1 36 GLU n 1 37 LYS n 1 38 THR n 1 39 HIS n 1 40 ASN n 1 41 GLY n 1 42 LYS n 1 43 LEU n 1 44 CYS n 1 45 LYS n 1 46 LEU n 1 47 ASN n 1 48 GLY n 1 49 ILE n 1 50 PRO n 1 51 PRO n 1 52 LEU n 1 53 GLU n 1 54 LEU n 1 55 GLY n 1 56 ASP n 1 57 CYS n 1 58 SER n 1 59 ILE n 1 60 ALA n 1 61 GLY n 1 62 TRP n 1 63 LEU n 1 64 LEU n 1 65 GLY n 1 66 ASN n 1 67 PRO n 1 68 GLU n 1 69 CYS n 1 70 ASP n 1 71 ARG n 1 72 LEU n 1 73 LEU n 1 74 SER n 1 75 VAL n 1 76 PRO n 1 77 GLU n 1 78 TRP n 1 79 SER n 1 80 TYR n 1 81 ILE n 1 82 MET n 1 83 GLU n 1 84 LYS n 1 85 GLU n 1 86 ASN n 1 87 PRO n 1 88 ARG n 1 89 ASP n 1 90 GLY n 1 91 LEU n 1 92 CYS n 1 93 TYR n 1 94 PRO n 1 95 GLY n 1 96 SER n 1 97 PHE n 1 98 ASN n 1 99 ASP n 1 100 TYR n 1 101 GLU n 1 102 GLU n 1 103 LEU n 1 104 LYS n 1 105 HIS n 1 106 LEU n 1 107 LEU n 1 108 SER n 1 109 SER n 1 110 VAL n 1 111 LYS n 1 112 HIS n 1 113 PHE n 1 114 GLU n 1 115 LYS n 1 116 VAL n 1 117 LYS n 1 118 ILE n 1 119 LEU n 1 120 PRO n 1 121 LYS n 1 122 ASP n 1 123 ARG n 1 124 TRP n 1 125 THR n 1 126 GLN n 1 127 HIS n 1 128 THR n 1 129 THR n 1 130 THR n 1 131 GLY n 1 132 GLY n 1 133 SER n 1 134 ARG n 1 135 ALA n 1 136 CYS n 1 137 ALA n 1 138 VAL n 1 139 SER n 1 140 GLY n 1 141 ASN n 1 142 PRO n 1 143 SER n 1 144 PHE n 1 145 PHE n 1 146 ARG n 1 147 ASN n 1 148 MET n 1 149 VAL n 1 150 TRP n 1 151 LEU n 1 152 THR n 1 153 GLU n 1 154 LYS n 1 155 GLY n 1 156 SER n 1 157 ASN n 1 158 TYR n 1 159 PRO n 1 160 VAL n 1 161 ALA n 1 162 LYS n 1 163 GLY n 1 164 SER n 1 165 TYR n 1 166 ASN n 1 167 ASN n 1 168 THR n 1 169 SER n 1 170 GLY n 1 171 GLU n 1 172 GLN n 1 173 MET n 1 174 LEU n 1 175 ILE n 1 176 ILE n 1 177 TRP n 1 178 GLY n 1 179 VAL n 1 180 HIS n 1 181 HIS n 1 182 PRO n 1 183 ASN n 1 184 ASP n 1 185 GLU n 1 186 THR n 1 187 GLU n 1 188 GLN n 1 189 ARG n 1 190 THR n 1 191 LEU n 1 192 TYR n 1 193 GLN n 1 194 ASN n 1 195 VAL n 1 196 GLY n 1 197 THR n 1 198 TYR n 1 199 VAL n 1 200 SER n 1 201 VAL n 1 202 GLY n 1 203 THR n 1 204 SER n 1 205 THR n 1 206 LEU n 1 207 ASN n 1 208 LYS n 1 209 ARG n 1 210 SER n 1 211 THR n 1 212 PRO n 1 213 GLU n 1 214 ILE n 1 215 ALA n 1 216 THR n 1 217 ARG n 1 218 PRO n 1 219 LYS n 1 220 VAL n 1 221 ASN n 1 222 GLY n 1 223 LEU n 1 224 GLY n 1 225 SER n 1 226 ARG n 1 227 MET n 1 228 GLU n 1 229 PHE n 1 230 SER n 1 231 TRP n 1 232 THR n 1 233 LEU n 1 234 LEU n 1 235 ASP n 1 236 MET n 1 237 TRP n 1 238 ASP n 1 239 THR n 1 240 ILE n 1 241 ASN n 1 242 PHE n 1 243 GLU n 1 244 SER n 1 245 THR n 1 246 GLY n 1 247 ASN n 1 248 LEU n 1 249 ILE n 1 250 ALA n 1 251 PRO n 1 252 GLU n 1 253 TYR n 1 254 GLY n 1 255 PHE n 1 256 LYS n 1 257 ILE n 1 258 SER n 1 259 LYS n 1 260 ARG n 1 261 GLY n 1 262 SER n 1 263 SER n 1 264 GLY n 1 265 ILE n 1 266 MET n 1 267 LYS n 1 268 THR n 1 269 GLU n 1 270 GLY n 1 271 THR n 1 272 LEU n 1 273 GLU n 1 274 ASN n 1 275 CYS n 1 276 GLU n 1 277 THR n 1 278 LYS n 1 279 CYS n 1 280 GLN n 1 281 THR n 1 282 PRO n 1 283 LEU n 1 284 GLY n 1 285 ALA n 1 286 ILE n 1 287 ASN n 1 288 THR n 1 289 THR n 1 290 LEU n 1 291 PRO n 1 292 PHE n 1 293 HIS n 1 294 ASN n 1 295 VAL n 1 296 HIS n 1 297 PRO n 1 298 LEU n 1 299 THR n 1 300 ILE n 1 301 GLY n 1 302 GLU n 1 303 CYS n 1 304 PRO n 1 305 LYS n 1 306 TYR n 1 307 VAL n 1 308 LYS n 1 309 SER n 1 310 GLU n 1 311 LYS n 1 312 LEU n 1 313 VAL n 1 314 LEU n 1 315 ALA n 1 316 THR n 1 317 GLY n 1 318 LEU n 1 319 ARG n 1 320 ASN n 1 321 VAL n 1 322 PRO n 1 323 GLN n 1 324 ILE n 1 325 GLU n 1 326 SER n 1 327 ARG n 2 1 GLY n 2 2 LEU n 2 3 PHE n 2 4 GLY n 2 5 ALA n 2 6 ILE n 2 7 ALA n 2 8 GLY n 2 9 PHE n 2 10 ILE n 2 11 GLU n 2 12 GLY n 2 13 GLY n 2 14 TRP n 2 15 GLN n 2 16 GLY n 2 17 MET n 2 18 VAL n 2 19 ASP n 2 20 GLY n 2 21 TRP n 2 22 TYR n 2 23 GLY n 2 24 TYR n 2 25 HIS n 2 26 HIS n 2 27 SER n 2 28 ASN n 2 29 ASP n 2 30 GLN n 2 31 GLY n 2 32 SER n 2 33 GLY n 2 34 TYR n 2 35 ALA n 2 36 ALA n 2 37 ASP n 2 38 LYS n 2 39 GLU n 2 40 SER n 2 41 THR n 2 42 GLN n 2 43 LYS n 2 44 ALA n 2 45 PHE n 2 46 ASP n 2 47 GLY n 2 48 ILE n 2 49 THR n 2 50 ASN n 2 51 LYS n 2 52 VAL n 2 53 ASN n 2 54 SER n 2 55 VAL n 2 56 ILE n 2 57 GLU n 2 58 LYS n 2 59 MET n 2 60 ASN n 2 61 THR n 2 62 GLN n 2 63 PHE n 2 64 GLU n 2 65 ALA n 2 66 VAL n 2 67 GLY n 2 68 LYS n 2 69 GLU n 2 70 PHE n 2 71 SER n 2 72 ASN n 2 73 LEU n 2 74 GLU n 2 75 ARG n 2 76 ARG n 2 77 LEU n 2 78 GLU n 2 79 ASN n 2 80 LEU n 2 81 ASN n 2 82 LYS n 2 83 LYS n 2 84 MET n 2 85 GLU n 2 86 ASP n 2 87 GLY n 2 88 PHE n 2 89 LEU n 2 90 ASP n 2 91 VAL n 2 92 TRP n 2 93 THR n 2 94 TYR n 2 95 ASN n 2 96 ALA n 2 97 GLU n 2 98 LEU n 2 99 LEU n 2 100 VAL n 2 101 LEU n 2 102 MET n 2 103 GLU n 2 104 ASN n 2 105 GLU n 2 106 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 MET n 2 125 GLN n 2 126 LEU n 2 127 ARG n 2 128 ASP n 2 129 ASN n 2 130 VAL n 2 131 LYS n 2 132 GLU n 2 133 LEU n 2 134 GLY n 2 135 ASN n 2 136 GLY n 2 137 CYS n 2 138 PHE n 2 139 GLU n 2 140 PHE n 2 141 TYR n 2 142 HIS n 2 143 LYS n 2 144 CYS n 2 145 ASP n 2 146 ASP n 2 147 GLU n 2 148 CYS n 2 149 MET n 2 150 ASN n 2 151 SER n 2 152 VAL n 2 153 LYS n 2 154 ASN n 2 155 GLY n 2 156 THR n 2 157 TYR n 2 158 ASP n 2 159 TYR n 2 160 PRO n 2 161 LYS n 2 162 TYR n 2 163 GLU n 2 164 GLU n 2 165 GLU n 2 166 SER n 2 167 LYS n 2 168 LEU n 2 169 ASN n 2 170 ARG n 2 171 ASN n 2 172 GLU n 2 173 ILE n 2 174 LYS n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample ? ? ? ? ? 'HA, hemagglutinin' ? A/Japan/305/57 ? ? ? ? 'Influenza A virus' 387161 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? Baculovirus ? ? ? pFASTbac-HT ? ? 2 1 sample ? ? ? ? ? 'HA, hemagglutinin' ? A/Japan/305/57 ? ? ? ? 'Influenza A virus' 387161 ? ? ? ? ? ? ? ? 'Trichoplusia ni' 7111 ? ? ? ? ? ? Hi5 ? ? ? ? ? ? ? Baculovirus ? ? ? pFASTbac-HT ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP C7S226_I57A0 C7S226 1 ;GDQICIGYHANNSTEKVDTILERNVTVTHAKDILEKTHNGKLCKLNGIPPLELGDCSIAGWLLGNPECDRLLSVPEWSYI MEKENPRDGLCYPGSFNDYEELKHLLSSVKHFEKVKILPKDRWTQHTTTGGSRACAVSGNPSFFRNMVWLTEKGSNYPVA KGSYNNTSGEQMLIIWGVHHPNDETEQRTLYQNVGTYVSVGTSTLNKRSTPEIATRPKVNGQGGRMEFSWTLLDMWDTIN FESTGNLIAPEYGFKISKRGSSGIMKTEGTLENCETKCQTPLGAINTTLPFHNVHPLTIGECPKYVKSEKLVLATGLRNV PQIESR ; 15 ? 2 UNP C7S226_I57A0 C7S226 2 ;GLFGAIAGFIEGGWQGMVDGWYGYHHSNDQGSGYAADKESTQKAFDGITNKVNSVIEKMNTQFEAVGKEFSNLERRLENL NKKMEDGFLDVWTYNAELLVLMENERTLDFHDSNVKNLYDKVRMQLRDNVKELGNGCFEFYHKCDDECMNSVKNGTYDYP KYEEESKLNRNEIK ; 341 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3KU5 A 2 ? 327 ? C7S226 15 ? 340 ? 10 329 2 2 3KU5 B 1 ? 174 ? C7S226 341 ? 514 ? 1 174 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 3KU5 PRO A 1 ? UNP C7S226 ? ? 'EXPRESSION TAG' 9 1 1 3KU5 LEU A 223 ? UNP C7S226 GLN 236 ENGINEERED 226 2 1 3KU5 SER A 225 ? UNP C7S226 GLY 238 ENGINEERED 228 3 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PEG non-polymer . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3' 106.120 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 3KU5 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.01 _exptl_crystal.density_percent_sol 59.19 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 295 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.8 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '26% PEG 3000, 0.1M Tris, pH 7.8, vapor diffusion, sitting drop, temperature 295K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MARMOSAIC 300 mm CCD' _diffrn_detector.pdbx_collection_date 2008-10-17 _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 'monochromator Si(111)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.03333 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'APS BEAMLINE 23-ID-B' _diffrn_source.pdbx_synchrotron_site APS _diffrn_source.pdbx_synchrotron_beamline 23-ID-B _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.03333 # _reflns.entry_id 3KU5 _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 40 _reflns.d_resolution_high 1.73 _reflns.number_obs 67767 _reflns.number_all ? _reflns.percent_possible_obs 97.7 _reflns.pdbx_Rmerge_I_obs 0.086 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 13 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 6.5 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.73 _reflns_shell.d_res_low 1.79 _reflns_shell.percent_possible_all 99.0 _reflns_shell.Rmerge_I_obs 0.534 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 3.1 _reflns_shell.pdbx_redundancy 5.9 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3KU5 _refine.ls_number_reflns_obs 64327 _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 40.00 _refine.ls_d_res_high 1.73 _refine.ls_percent_reflns_obs 97.56 _refine.ls_R_factor_obs 0.18927 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.18747 _refine.ls_R_factor_R_free 0.22251 _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 3427 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min 0.33 _refine.occupancy_max 1.00 _refine.correlation_coeff_Fo_to_Fc 0.959 _refine.correlation_coeff_Fo_to_Fc_free 0.942 _refine.B_iso_mean 29.377 _refine.aniso_B[1][1] 0.01 _refine.aniso_B[2][2] 0.01 _refine.aniso_B[3][3] -0.02 _refine.aniso_B[1][2] 0.01 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.106 _refine.pdbx_overall_ESU_R_Free 0.106 _refine.overall_SU_ML 0.068 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 3.936 _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_TLS_residual_ADP_flag 'LIKELY RESIDUAL' _refine.pdbx_diffrn_id 1 _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 3914 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 67 _refine_hist.number_atoms_solvent 582 _refine_hist.number_atoms_total 4563 _refine_hist.d_res_high 1.73 _refine_hist.d_res_low 40.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.013 0.022 ? 4147 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.437 1.966 ? 5628 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.735 5.000 ? 515 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 34.272 25.025 ? 197 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.839 15.000 ? 721 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 16.973 15.000 ? 19 'X-RAY DIFFRACTION' ? r_chiral_restr 0.098 0.200 ? 609 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.020 ? 3134 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined 0.202 0.200 ? 1919 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.309 0.200 ? 2803 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.134 0.200 ? 490 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.190 0.200 ? 82 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.208 0.200 ? 47 '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 0.945 1.500 ? 2562 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.480 2.000 ? 4018 'X-RAY DIFFRACTION' ? r_scbond_it 2.271 3.000 ? 1818 'X-RAY DIFFRACTION' ? r_scangle_it 3.557 4.500 ? 1599 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.730 _refine_ls_shell.d_res_low 1.775 _refine_ls_shell.number_reflns_R_work 4692 _refine_ls_shell.R_factor_R_work 0.254 _refine_ls_shell.percent_reflns_obs 96.30 _refine_ls_shell.R_factor_R_free 0.273 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 251 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # _struct.entry_id 3KU5 _struct.title 'Crystal structure of a H2N2 influenza virus hemagglutinin, human like' _struct.pdbx_descriptor 'Hemagglutinin HA1 chain, Hemagglutinin HA2 chain' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3KU5 _struct_keywords.text 'viral envelope protein, hemagglutinin, viral fusion protein, Envelope protein, VIRAL PROTEIN' _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 4 ? G N N 3 ? H N N 5 ? I N N 6 ? J N N 6 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 SER A 58 ? GLY A 65 ? SER A 65 GLY A 72 1 ? 8 HELX_P HELX_P2 2 ASN A 66 ? LEU A 73 ? ASN A 73 LEU A 80 5 ? 8 HELX_P HELX_P3 3 ASP A 99 ? SER A 108 ? ASP A 104 SER A 113 1 ? 10 HELX_P HELX_P4 4 PRO A 120 ? TRP A 124 ? PRO A 122 TRP A 127 5 ? 5 HELX_P HELX_P5 5 ASP A 184 ? GLN A 193 ? ASP A 187 GLN A 196 1 ? 10 HELX_P HELX_P6 6 ASP B 37 ? MET B 59 ? ASP B 37 MET B 59 1 ? 23 HELX_P HELX_P7 7 GLU B 74 ? ARG B 127 ? GLU B 74 ARG B 127 1 ? 54 HELX_P HELX_P8 8 ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 HELX_P HELX_P9 9 ASP B 158 ? GLU B 172 ? ASP B 158 GLU B 172 1 ? 15 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 6 SG ? ? ? 1_555 B CYS 137 SG ? ? A CYS 14 B CYS 137 1_555 ? ? ? ? ? ? ? 2.064 ? disulf2 disulf ? ? A CYS 44 SG ? ? ? 1_555 A CYS 275 SG ? ? A CYS 52 A CYS 277 1_555 ? ? ? ? ? ? ? 2.086 ? disulf3 disulf ? ? A CYS 57 SG ? ? ? 1_555 A CYS 69 SG ? ? A CYS 64 A CYS 76 1_555 ? ? ? ? ? ? ? 2.070 ? disulf4 disulf ? ? A CYS 92 SG ? ? ? 1_555 A CYS 136 SG ? ? A CYS 97 A CYS 139 1_555 ? ? ? ? ? ? ? 2.185 ? disulf5 disulf ? ? A CYS 279 SG ? ? ? 1_555 A CYS 303 SG ? ? A CYS 281 A CYS 305 1_555 ? ? ? ? ? ? ? 2.066 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.052 ? covale1 covale ? ? A ASN 166 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 169 A NAG 330 1_555 ? ? ? ? ? ? ? 1.440 ? covale2 covale ? ? A ASN 25 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 33 A NAG 332 1_555 ? ? ? ? ? ? ? 1.445 ? covale3 covale ? ? B ASN 154 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 154 B NAG 175 1_555 ? ? ? ? ? ? ? 1.451 ? covale4 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 330 A NAG 331 1_555 ? ? ? ? ? ? ? 1.456 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 5 ? B ? 2 ? C ? 2 ? D ? 3 ? E ? 2 ? F ? 3 ? G ? 5 ? H ? 5 ? I ? 2 ? J ? 4 ? K ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? parallel D 2 3 ? parallel E 1 2 ? parallel F 1 2 ? parallel F 2 3 ? parallel G 1 2 ? parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel G 4 5 ? anti-parallel H 1 2 ? parallel H 2 3 ? anti-parallel H 3 4 ? anti-parallel H 4 5 ? anti-parallel I 1 2 ? anti-parallel J 1 2 ? anti-parallel J 2 3 ? anti-parallel J 3 4 ? anti-parallel K 1 2 ? anti-parallel K 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 SER B 32 ? ALA B 36 ? SER B 32 ALA B 36 A 2 TYR B 22 ? SER B 27 ? TYR B 22 SER B 27 A 3 GLN A 4 ? TYR A 9 ? GLN A 12 TYR A 17 A 4 CYS B 137 ? PHE B 140 ? CYS B 137 PHE B 140 A 5 VAL B 130 ? GLU B 132 ? VAL B 130 GLU B 132 B 1 LYS A 17 ? VAL A 18 ? LYS A 25 VAL A 26 B 2 VAL A 26 ? THR A 27 ? VAL A 34 THR A 35 C 1 ALA A 31 ? ASP A 33 ? ALA A 39 ASP A 41 C 2 VAL A 313 ? ALA A 315 ? VAL A 315 ALA A 317 D 1 LEU A 35 ? GLU A 36 ? LEU A 43 GLU A 44 D 2 PHE A 292 ? HIS A 293 ? PHE A 294 HIS A 295 D 3 LYS A 305 ? TYR A 306 ? LYS A 307 TYR A 308 E 1 LEU A 43 ? LEU A 46 A LEU A 51 LEU A 53 E 2 LEU A 272 ? THR A 277 ? LEU A 274 THR A 279 F 1 LEU A 52 ? GLU A 53 ? LEU A 59 GLU A 60 F 2 ILE A 81 ? GLU A 83 ? ILE A 87 GLU A 89 F 3 ILE A 265 ? LYS A 267 ? ILE A 267 LYS A 269 G 1 GLY A 95 ? PHE A 97 ? GLY A 100 PHE A 102 G 2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 G 3 MET A 173 ? HIS A 181 ? MET A 176 HIS A 184 G 4 GLY A 254 ? ARG A 260 ? GLY A 257 ARG A 263 G 5 VAL A 110 ? VAL A 116 ? VAL A 115 VAL A 118 H 1 GLY A 95 ? PHE A 97 ? GLY A 100 PHE A 102 H 2 ARG A 226 ? LEU A 234 ? ARG A 229 LEU A 237 H 3 MET A 173 ? HIS A 181 ? MET A 176 HIS A 184 H 4 LEU A 248 ? PRO A 251 ? LEU A 251 PRO A 254 H 5 MET A 148 ? TRP A 150 ? MET A 151 TRP A 153 I 1 SER A 133 ? VAL A 138 ? SER A 136 VAL A 141 I 2 ASN A 141 ? SER A 143 ? ASN A 144 SER A 146 J 1 ALA A 161 ? ASN A 166 ? ALA A 164 ASN A 169 J 2 THR A 239 ? SER A 244 ? THR A 242 SER A 247 J 3 VAL A 199 ? GLY A 202 ? VAL A 202 GLY A 205 J 4 ASN A 207 ? SER A 210 ? ASN A 210 SER A 213 K 1 GLY A 284 ? ILE A 286 ? GLY A 286 ILE A 288 K 2 CYS A 279 ? THR A 281 ? CYS A 281 THR A 283 K 3 ILE A 300 ? GLY A 301 ? ILE A 302 GLY A 303 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O ALA B 35 ? O ALA B 35 N TYR B 24 ? N TYR B 24 A 2 3 O SER B 27 ? O SER B 27 N GLN A 4 ? N GLN A 12 A 3 4 N ILE A 5 ? N ILE A 13 O PHE B 138 ? O PHE B 138 A 4 5 O GLU B 139 ? O GLU B 139 N LYS B 131 ? N LYS B 131 B 1 2 N VAL A 18 ? N VAL A 26 O VAL A 26 ? O VAL A 34 C 1 2 N LYS A 32 ? N LYS A 40 O LEU A 314 ? O LEU A 316 D 1 2 N GLU A 36 ? N GLU A 44 O PHE A 292 ? O PHE A 294 D 2 3 N HIS A 293 ? N HIS A 295 O LYS A 305 ? O LYS A 307 E 1 2 N LYS A 45 ? N LYS A 53 O CYS A 275 ? O CYS A 277 F 1 2 N LEU A 52 ? N LEU A 59 O MET A 82 ? O MET A 88 F 2 3 N ILE A 81 ? N ILE A 87 O MET A 266 ? O MET A 268 G 1 2 N SER A 96 ? N SER A 101 O PHE A 229 ? O PHE A 232 G 2 3 O LEU A 234 ? O LEU A 237 N MET A 173 ? N MET A 176 G 3 4 N LEU A 174 ? N LEU A 177 O PHE A 255 ? O PHE A 258 G 4 5 O GLY A 254 ? O GLY A 257 N VAL A 116 ? N VAL A 118 H 1 2 N SER A 96 ? N SER A 101 O PHE A 229 ? O PHE A 232 H 2 3 O LEU A 234 ? O LEU A 237 N MET A 173 ? N MET A 176 H 3 4 N GLY A 178 ? N GLY A 181 O ILE A 249 ? O ILE A 252 H 4 5 O ALA A 250 ? O ALA A 253 N VAL A 149 ? N VAL A 152 I 1 2 N SER A 133 ? N SER A 136 O SER A 143 ? O SER A 146 J 1 2 N GLY A 163 ? N GLY A 166 O PHE A 242 ? O PHE A 245 J 2 3 O GLU A 243 ? O GLU A 246 N SER A 200 ? N SER A 203 J 3 4 N VAL A 201 ? N VAL A 204 O LYS A 208 ? O LYS A 211 K 1 2 O ILE A 286 ? O ILE A 288 N CYS A 279 ? N CYS A 281 K 2 3 N GLN A 280 ? N GLN A 282 O ILE A 300 ? O ILE A 302 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 330' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG A 331' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 332' AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE EDO A 1' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG B 175' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE PEG B 176' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 7 ASN A 166 ? ASN A 169 . ? 1_555 ? 2 AC1 7 TRP A 237 ? TRP A 240 . ? 1_555 ? 3 AC1 7 NAG D . ? NAG A 331 . ? 1_555 ? 4 AC1 7 HOH I . ? HOH A 359 . ? 1_555 ? 5 AC1 7 HOH I . ? HOH A 438 . ? 1_555 ? 6 AC1 7 HOH I . ? HOH A 449 . ? 1_555 ? 7 AC1 7 HOH I . ? HOH A 611 . ? 1_555 ? 8 AC2 5 TRP A 237 ? TRP A 240 . ? 1_555 ? 9 AC2 5 NAG C . ? NAG A 330 . ? 1_555 ? 10 AC2 5 HOH I . ? HOH A 380 . ? 1_555 ? 11 AC2 5 HOH I . ? HOH A 612 . ? 1_555 ? 12 AC2 5 HOH I . ? HOH A 661 . ? 1_555 ? 13 AC3 3 LYS A 17 ? LYS A 25 . ? 1_555 ? 14 AC3 3 ASN A 25 ? ASN A 33 . ? 1_555 ? 15 AC3 3 HOH I . ? HOH A 601 . ? 1_555 ? 16 AC4 7 LEU A 119 ? LEU A 121 . ? 1_555 ? 17 AC4 7 PRO A 120 ? PRO A 122 . ? 1_555 ? 18 AC4 7 ARG A 123 ? ARG A 126 . ? 1_555 ? 19 AC4 7 TRP A 124 ? TRP A 127 . ? 1_555 ? 20 AC4 7 HOH I . ? HOH A 557 . ? 1_555 ? 21 AC4 7 HOH I . ? HOH A 657 . ? 1_555 ? 22 AC4 7 HOH I . ? HOH A 753 . ? 1_555 ? 23 AC5 4 GLU B 147 ? GLU B 147 . ? 1_555 ? 24 AC5 4 ASN B 150 ? ASN B 150 . ? 1_555 ? 25 AC5 4 ASN B 154 ? ASN B 154 . ? 1_555 ? 26 AC5 4 THR B 156 ? THR B 156 . ? 1_555 ? 27 AC6 3 TRP B 14 ? TRP B 14 . ? 1_555 ? 28 AC6 3 HIS B 25 ? HIS B 25 . ? 1_555 ? 29 AC6 3 TYR B 34 ? TYR B 34 . ? 1_555 ? # _atom_sites.entry_id 3KU5 _atom_sites.fract_transf_matrix[1][1] 0.014145 _atom_sites.fract_transf_matrix[1][2] 0.008167 _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] 0.016334 _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] 0.004224 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . PRO A 1 1 ? -28.510 3.340 -48.764 1.00 25.24 ? 9 PRO A N 1 ATOM 2 C CA . PRO A 1 1 ? -27.959 2.884 -47.485 1.00 25.12 ? 9 PRO A CA 1 ATOM 3 C C . PRO A 1 1 ? -26.551 3.445 -47.213 1.00 24.79 ? 9 PRO A C 1 ATOM 4 O O . PRO A 1 1 ? -25.558 2.952 -47.782 1.00 24.82 ? 9 PRO A O 1 ATOM 5 C CB . PRO A 1 1 ? -27.923 1.357 -47.649 1.00 25.23 ? 9 PRO A CB 1 ATOM 6 C CG . PRO A 1 1 ? -29.043 1.060 -48.600 1.00 25.62 ? 9 PRO A CG 1 ATOM 7 C CD . PRO A 1 1 ? -29.163 2.249 -49.517 1.00 25.43 ? 9 PRO A CD 1 ATOM 8 N N . GLY A 1 2 ? -26.475 4.451 -46.320 1.00 24.44 ? 10 GLY A N 1 ATOM 9 C CA . GLY A 1 2 ? -25.226 5.177 -46.052 1.00 23.40 ? 10 GLY A CA 1 ATOM 10 C C . GLY A 1 2 ? -24.609 5.023 -44.657 1.00 22.42 ? 10 GLY A C 1 ATOM 11 O O . GLY A 1 2 ? -25.162 4.268 -43.812 1.00 22.45 ? 10 GLY A O 1 ATOM 12 N N . ASP A 1 3 ? -23.458 5.764 -44.451 1.00 21.78 ? 11 ASP A N 1 ATOM 13 C CA . ASP A 1 3 ? -22.742 5.734 -43.239 1.00 20.31 ? 11 ASP A CA 1 ATOM 14 C C . ASP A 1 3 ? -23.500 6.333 -42.126 1.00 20.29 ? 11 ASP A C 1 ATOM 15 O O . ASP A 1 3 ? -24.420 7.135 -42.339 1.00 19.80 ? 11 ASP A O 1 ATOM 16 C CB . ASP A 1 3 ? -21.415 6.462 -43.358 1.00 21.33 ? 11 ASP A CB 1 ATOM 17 C CG . ASP A 1 3 ? -20.443 5.746 -44.401 1.00 20.42 ? 11 ASP A CG 1 ATOM 18 O OD1 . ASP A 1 3 ? -20.676 4.565 -44.705 1.00 22.07 ? 11 ASP A OD1 1 ATOM 19 O OD2 . ASP A 1 3 ? -19.419 6.374 -44.952 1.00 25.55 ? 11 ASP A OD2 1 ATOM 20 N N . GLN A 1 4 ? -23.084 5.941 -40.848 1.00 19.29 ? 12 GLN A N 1 ATOM 21 C CA . GLN A 1 4 ? -23.759 6.421 -39.647 1.00 18.76 ? 12 GLN A CA 1 ATOM 22 C C . GLN A 1 4 ? -22.829 6.755 -38.490 1.00 18.11 ? 12 GLN A C 1 ATOM 23 O O . GLN A 1 4 ? -21.864 6.029 -38.216 1.00 17.43 ? 12 GLN A O 1 ATOM 24 C CB . GLN A 1 4 ? -24.801 5.400 -39.157 1.00 18.65 ? 12 GLN A CB 1 ATOM 25 C CG . GLN A 1 4 ? -25.886 5.086 -40.177 1.00 19.62 ? 12 GLN A CG 1 ATOM 26 C CD . GLN A 1 4 ? -27.060 4.344 -39.579 1.00 18.88 ? 12 GLN A CD 1 ATOM 27 O OE1 . GLN A 1 4 ? -27.182 4.216 -38.340 1.00 19.86 ? 12 GLN A OE1 1 ATOM 28 N NE2 . GLN A 1 4 ? -27.948 3.856 -40.451 1.00 19.40 ? 12 GLN A NE2 1 ATOM 29 N N . ILE A 1 5 ? -23.144 7.876 -37.777 1.00 16.52 ? 13 ILE A N 1 ATOM 30 C CA . ILE A 1 5 ? -22.633 8.082 -36.463 1.00 16.30 ? 13 ILE A CA 1 ATOM 31 C C . ILE A 1 5 ? -23.872 8.118 -35.569 1.00 15.24 ? 13 ILE A C 1 ATOM 32 O O . ILE A 1 5 ? -24.905 8.685 -35.947 1.00 15.07 ? 13 ILE A O 1 ATOM 33 C CB . ILE A 1 5 ? -21.711 9.334 -36.355 1.00 16.07 ? 13 ILE A CB 1 ATOM 34 C CG1 . ILE A 1 5 ? -20.862 9.241 -35.078 1.00 16.36 ? 13 ILE A CG1 1 ATOM 35 C CG2 . ILE A 1 5 ? -22.516 10.641 -36.503 1.00 16.81 ? 13 ILE A CG2 1 ATOM 36 C CD1 . ILE A 1 5 ? -19.764 10.274 -34.967 1.00 16.51 ? 13 ILE A CD1 1 ATOM 37 N N . CYS A 1 6 ? -23.787 7.414 -34.448 1.00 15.30 ? 14 CYS A N 1 ATOM 38 C CA . CYS A 1 6 ? -24.854 7.444 -33.461 1.00 14.54 ? 14 CYS A CA 1 ATOM 39 C C . CYS A 1 6 ? -24.316 7.983 -32.160 1.00 13.85 ? 14 CYS A C 1 ATOM 40 O O . CYS A 1 6 ? -23.144 7.792 -31.816 1.00 12.39 ? 14 CYS A O 1 ATOM 41 C CB . CYS A 1 6 ? -25.459 6.056 -33.248 1.00 16.07 ? 14 CYS A CB 1 ATOM 42 S SG . CYS A 1 6 ? -25.896 5.155 -34.784 1.00 18.99 ? 14 CYS A SG 1 ATOM 43 N N . ILE A 1 7 ? -25.199 8.690 -31.458 1.00 12.31 ? 15 ILE A N 1 ATOM 44 C CA . ILE A 1 7 ? -24.943 9.165 -30.118 1.00 12.09 ? 15 ILE A CA 1 ATOM 45 C C . ILE A 1 7 ? -25.623 8.154 -29.223 1.00 11.53 ? 15 ILE A C 1 ATOM 46 O O . ILE A 1 7 ? -26.736 7.699 -29.515 1.00 10.86 ? 15 ILE A O 1 ATOM 47 C CB . ILE A 1 7 ? -25.574 10.563 -29.883 1.00 12.10 ? 15 ILE A CB 1 ATOM 48 C CG1 . ILE A 1 7 ? -25.161 11.563 -30.973 1.00 14.02 ? 15 ILE A CG1 1 ATOM 49 C CG2 . ILE A 1 7 ? -25.283 11.090 -28.461 1.00 12.27 ? 15 ILE A CG2 1 ATOM 50 C CD1 . ILE A 1 7 ? -23.701 11.569 -31.330 1.00 16.75 ? 15 ILE A CD1 1 ATOM 51 N N . GLY A 1 8 ? -24.948 7.817 -28.136 1.00 11.40 ? 16 GLY A N 1 ATOM 52 C CA . GLY A 1 8 ? -25.483 6.888 -27.173 1.00 11.99 ? 16 GLY A CA 1 ATOM 53 C C . GLY A 1 8 ? -24.848 7.040 -25.820 1.00 12.35 ? 16 GLY A C 1 ATOM 54 O O . GLY A 1 8 ? -24.043 7.953 -25.567 1.00 12.00 ? 16 GLY A O 1 ATOM 55 N N . TYR A 1 9 ? -25.208 6.110 -24.947 1.00 13.14 ? 17 TYR A N 1 ATOM 56 C CA . TYR A 1 9 ? -24.773 6.134 -23.573 1.00 13.37 ? 17 TYR A CA 1 ATOM 57 C C . TYR A 1 9 ? -24.417 4.735 -23.109 1.00 14.72 ? 17 TYR A C 1 ATOM 58 O O . TYR A 1 9 ? -24.864 3.735 -23.679 1.00 15.03 ? 17 TYR A O 1 ATOM 59 C CB . TYR A 1 9 ? -25.863 6.736 -22.669 1.00 13.13 ? 17 TYR A CB 1 ATOM 60 C CG . TYR A 1 9 ? -27.237 6.163 -22.914 1.00 10.97 ? 17 TYR A CG 1 ATOM 61 C CD1 . TYR A 1 9 ? -27.703 5.054 -22.187 1.00 12.08 ? 17 TYR A CD1 1 ATOM 62 C CD2 . TYR A 1 9 ? -28.080 6.736 -23.833 1.00 9.49 ? 17 TYR A CD2 1 ATOM 63 C CE1 . TYR A 1 9 ? -28.986 4.538 -22.420 1.00 11.78 ? 17 TYR A CE1 1 ATOM 64 C CE2 . TYR A 1 9 ? -29.344 6.223 -24.089 1.00 11.25 ? 17 TYR A CE2 1 ATOM 65 C CZ . TYR A 1 9 ? -29.788 5.122 -23.360 1.00 11.67 ? 17 TYR A CZ 1 ATOM 66 O OH . TYR A 1 9 ? -31.054 4.642 -23.638 1.00 13.00 ? 17 TYR A OH 1 ATOM 67 N N . HIS A 1 10 ? -23.610 4.718 -22.063 1.00 15.55 ? 18 HIS A N 1 ATOM 68 C CA . HIS A 1 10 ? -23.079 3.534 -21.406 1.00 17.36 ? 18 HIS A CA 1 ATOM 69 C C . HIS A 1 10 ? -24.195 2.683 -20.804 1.00 18.13 ? 18 HIS A C 1 ATOM 70 O O . HIS A 1 10 ? -25.221 3.198 -20.333 1.00 18.66 ? 18 HIS A O 1 ATOM 71 C CB . HIS A 1 10 ? -22.117 4.026 -20.327 1.00 17.37 ? 18 HIS A CB 1 ATOM 72 C CG . HIS A 1 10 ? -21.487 2.954 -19.494 1.00 19.35 ? 18 HIS A CG 1 ATOM 73 N ND1 . HIS A 1 10 ? -20.526 2.092 -19.982 1.00 20.88 ? 18 HIS A ND1 1 ATOM 74 C CD2 . HIS A 1 10 ? -21.634 2.650 -18.183 1.00 20.03 ? 18 HIS A CD2 1 ATOM 75 C CE1 . HIS A 1 10 ? -20.126 1.290 -19.012 1.00 21.17 ? 18 HIS A CE1 1 ATOM 76 N NE2 . HIS A 1 10 ? -20.778 1.610 -17.908 1.00 21.18 ? 18 HIS A NE2 1 ATOM 77 N N . ALA A 1 11 ? -23.993 1.374 -20.866 1.00 18.94 ? 19 ALA A N 1 ATOM 78 C CA . ALA A 1 11 ? -24.741 0.436 -20.058 1.00 19.82 ? 19 ALA A CA 1 ATOM 79 C C . ALA A 1 11 ? -23.763 -0.610 -19.557 1.00 20.43 ? 19 ALA A C 1 ATOM 80 O O . ALA A 1 11 ? -22.682 -0.787 -20.118 1.00 20.61 ? 19 ALA A O 1 ATOM 81 C CB . ALA A 1 11 ? -25.883 -0.187 -20.852 1.00 19.33 ? 19 ALA A CB 1 ATOM 82 N N . ASN A 1 12 ? -24.119 -1.269 -18.465 1.00 21.21 ? 20 ASN A N 1 ATOM 83 C CA . ASN A 1 12 ? -23.275 -2.322 -17.916 1.00 22.22 ? 20 ASN A CA 1 ATOM 84 C C . ASN A 1 12 ? -24.126 -3.386 -17.244 1.00 23.27 ? 20 ASN A C 1 ATOM 85 O O . ASN A 1 12 ? -25.340 -3.425 -17.444 1.00 22.95 ? 20 ASN A O 1 ATOM 86 C CB . ASN A 1 12 ? -22.203 -1.750 -16.978 1.00 21.99 ? 20 ASN A CB 1 ATOM 87 C CG . ASN A 1 12 ? -22.798 -1.008 -15.790 1.00 21.16 ? 20 ASN A CG 1 ATOM 88 O OD1 . ASN A 1 12 ? -23.971 -1.187 -15.454 1.00 21.28 ? 20 ASN A OD1 1 ATOM 89 N ND2 . ASN A 1 12 ? -22.001 -0.150 -15.174 1.00 21.60 ? 20 ASN A ND2 1 ATOM 90 N N . ASN A 1 13 ? -23.491 -4.263 -16.474 1.00 25.30 ? 21 ASN A N 1 ATOM 91 C CA . ASN A 1 13 ? -24.220 -5.323 -15.774 1.00 27.47 ? 21 ASN A CA 1 ATOM 92 C C . ASN A 1 13 ? -24.474 -4.998 -14.300 1.00 28.01 ? 21 ASN A C 1 ATOM 93 O O . ASN A 1 13 ? -24.638 -5.906 -13.484 1.00 28.69 ? 21 ASN A O 1 ATOM 94 C CB . ASN A 1 13 ? -23.506 -6.681 -15.916 1.00 28.42 ? 21 ASN A CB 1 ATOM 95 C CG . ASN A 1 13 ? -22.016 -6.612 -15.588 1.00 31.03 ? 21 ASN A CG 1 ATOM 96 O OD1 . ASN A 1 13 ? -21.541 -5.650 -14.982 1.00 35.93 ? 21 ASN A OD1 1 ATOM 97 N ND2 . ASN A 1 13 ? -21.268 -7.647 -15.993 1.00 34.03 ? 21 ASN A ND2 1 ATOM 98 N N . SER A 1 14 ? -24.491 -3.706 -13.966 1.00 28.35 ? 22 SER A N 1 ATOM 99 C CA . SER A 1 14 ? -24.788 -3.263 -12.603 1.00 28.57 ? 22 SER A CA 1 ATOM 100 C C . SER A 1 14 ? -26.242 -3.561 -12.278 1.00 29.23 ? 22 SER A C 1 ATOM 101 O O . SER A 1 14 ? -27.125 -3.439 -13.139 1.00 28.77 ? 22 SER A O 1 ATOM 102 C CB . SER A 1 14 ? -24.491 -1.767 -12.425 1.00 28.79 ? 22 SER A CB 1 ATOM 103 O OG . SER A 1 14 ? -25.033 -1.247 -11.209 1.00 26.87 ? 22 SER A OG 1 ATOM 104 N N . THR A 1 15 ? -26.464 -3.971 -11.029 1.00 30.37 ? 23 THR A N 1 ATOM 105 C CA . THR A 1 15 ? -27.793 -4.255 -10.499 1.00 31.13 ? 23 THR A CA 1 ATOM 106 C C . THR A 1 15 ? -28.111 -3.292 -9.355 1.00 31.14 ? 23 THR A C 1 ATOM 107 O O . THR A 1 15 ? -29.124 -3.444 -8.668 1.00 31.45 ? 23 THR A O 1 ATOM 108 C CB . THR A 1 15 ? -27.880 -5.706 -9.979 1.00 31.48 ? 23 THR A CB 1 ATOM 109 O OG1 . THR A 1 15 ? -26.682 -6.020 -9.259 1.00 32.79 ? 23 THR A OG1 1 ATOM 110 C CG2 . THR A 1 15 ? -28.054 -6.681 -11.137 1.00 31.90 ? 23 THR A CG2 1 ATOM 111 N N . GLU A 1 16 ? -27.229 -2.308 -9.168 1.00 31.30 ? 24 GLU A N 1 ATOM 112 C CA . GLU A 1 16 ? -27.364 -1.274 -8.137 1.00 31.33 ? 24 GLU A CA 1 ATOM 113 C C . GLU A 1 16 ? -28.646 -0.493 -8.325 1.00 30.70 ? 24 GLU A C 1 ATOM 114 O O . GLU A 1 16 ? -28.932 -0.003 -9.415 1.00 29.89 ? 24 GLU A O 1 ATOM 115 C CB . GLU A 1 16 ? -26.178 -0.298 -8.179 1.00 31.80 ? 24 GLU A CB 1 ATOM 116 C CG . GLU A 1 16 ? -24.811 -0.943 -7.996 1.00 34.58 ? 24 GLU A CG 1 ATOM 117 C CD . GLU A 1 16 ? -24.674 -1.642 -6.655 1.00 38.54 ? 24 GLU A CD 1 ATOM 118 O OE1 . GLU A 1 16 ? -24.733 -0.946 -5.609 1.00 40.42 ? 24 GLU A OE1 1 ATOM 119 O OE2 . GLU A 1 16 ? -24.506 -2.884 -6.650 1.00 41.10 ? 24 GLU A OE2 1 ATOM 120 N N . LYS A 1 17 ? -29.412 -0.367 -7.248 1.00 29.85 ? 25 LYS A N 1 ATOM 121 C CA . LYS A 1 17 ? -30.694 0.312 -7.307 1.00 29.53 ? 25 LYS A CA 1 ATOM 122 C C . LYS A 1 17 ? -30.716 1.584 -6.473 1.00 28.62 ? 25 LYS A C 1 ATOM 123 O O . LYS A 1 17 ? -30.051 1.674 -5.438 1.00 28.66 ? 25 LYS A O 1 ATOM 124 C CB . LYS A 1 17 ? -31.814 -0.644 -6.894 1.00 30.02 ? 25 LYS A CB 1 ATOM 125 C CG . LYS A 1 17 ? -32.165 -1.625 -7.999 1.00 31.93 ? 25 LYS A CG 1 ATOM 126 C CD . LYS A 1 17 ? -32.509 -2.993 -7.442 1.00 35.83 ? 25 LYS A CD 1 ATOM 127 C CE . LYS A 1 17 ? -32.666 -4.029 -8.560 1.00 36.78 ? 25 LYS A CE 1 ATOM 128 N NZ . LYS A 1 17 ? -33.563 -3.569 -9.670 1.00 38.34 ? 25 LYS A NZ 1 ATOM 129 N N . VAL A 1 18 ? -31.470 2.571 -6.954 1.00 28.01 ? 26 VAL A N 1 ATOM 130 C CA . VAL A 1 18 ? -31.703 3.819 -6.217 1.00 26.80 ? 26 VAL A CA 1 ATOM 131 C C . VAL A 1 18 ? -33.178 4.214 -6.283 1.00 26.87 ? 26 VAL A C 1 ATOM 132 O O . VAL A 1 18 ? -33.935 3.695 -7.112 1.00 26.79 ? 26 VAL A O 1 ATOM 133 C CB . VAL A 1 18 ? -30.820 5.001 -6.730 1.00 26.42 ? 26 VAL A CB 1 ATOM 134 C CG1 . VAL A 1 18 ? -29.333 4.663 -6.651 1.00 24.63 ? 26 VAL A CG1 1 ATOM 135 C CG2 . VAL A 1 18 ? -31.224 5.440 -8.156 1.00 25.91 ? 26 VAL A CG2 1 ATOM 136 N N . ASP A 1 19 ? -33.580 5.138 -5.409 1.00 26.70 ? 27 ASP A N 1 ATOM 137 C CA . ASP A 1 19 ? -34.934 5.694 -5.448 1.00 26.85 ? 27 ASP A CA 1 ATOM 138 C C . ASP A 1 19 ? -34.899 7.162 -5.850 1.00 26.59 ? 27 ASP A C 1 ATOM 139 O O . ASP A 1 19 ? -33.913 7.847 -5.603 1.00 26.35 ? 27 ASP A O 1 ATOM 140 C CB . ASP A 1 19 ? -35.598 5.576 -4.068 1.00 27.03 ? 27 ASP A CB 1 ATOM 141 C CG . ASP A 1 19 ? -35.846 4.140 -3.650 1.00 29.07 ? 27 ASP A CG 1 ATOM 142 O OD1 . ASP A 1 19 ? -36.004 3.256 -4.520 1.00 29.87 ? 27 ASP A OD1 1 ATOM 143 O OD2 . ASP A 1 19 ? -35.885 3.897 -2.423 1.00 32.77 ? 27 ASP A OD2 1 ATOM 144 N N . THR A 1 20 ? -35.981 7.637 -6.456 1.00 26.74 ? 28 THR A N 1 ATOM 145 C CA . THR A 1 20 ? -36.185 9.066 -6.673 1.00 27.42 ? 28 THR A CA 1 ATOM 146 C C . THR A 1 20 ? -37.556 9.433 -6.098 1.00 28.21 ? 28 THR A C 1 ATOM 147 O O . THR A 1 20 ? -38.255 8.568 -5.572 1.00 28.49 ? 28 THR A O 1 ATOM 148 C CB . THR A 1 20 ? -36.055 9.451 -8.179 1.00 27.20 ? 28 THR A CB 1 ATOM 149 O OG1 . THR A 1 20 ? -37.156 8.917 -8.921 1.00 26.43 ? 28 THR A OG1 1 ATOM 150 C CG2 . THR A 1 20 ? -34.750 8.915 -8.757 1.00 27.04 ? 28 THR A CG2 1 ATOM 151 N N . ILE A 1 21 ? -37.930 10.704 -6.179 1.00 29.57 ? 29 ILE A N 1 ATOM 152 C CA . ILE A 1 21 ? -39.274 11.148 -5.776 1.00 30.55 ? 29 ILE A CA 1 ATOM 153 C C . ILE A 1 21 ? -40.344 10.600 -6.732 1.00 30.95 ? 29 ILE A C 1 ATOM 154 O O . ILE A 1 21 ? -41.452 10.244 -6.322 1.00 31.32 ? 29 ILE A O 1 ATOM 155 C CB . ILE A 1 21 ? -39.339 12.703 -5.705 1.00 30.86 ? 29 ILE A CB 1 ATOM 156 C CG1 . ILE A 1 21 ? -38.469 13.244 -4.560 1.00 31.56 ? 29 ILE A CG1 1 ATOM 157 C CG2 . ILE A 1 21 ? -40.794 13.221 -5.619 1.00 30.71 ? 29 ILE A CG2 1 ATOM 158 C CD1 . ILE A 1 21 ? -38.936 12.868 -3.168 1.00 32.91 ? 29 ILE A CD1 1 ATOM 159 N N . LEU A 1 22 ? -39.993 10.528 -8.015 1.00 30.72 ? 30 LEU A N 1 ATOM 160 C CA . LEU A 1 22 ? -40.910 10.137 -9.077 1.00 30.91 ? 30 LEU A CA 1 ATOM 161 C C . LEU A 1 22 ? -40.940 8.628 -9.311 1.00 30.66 ? 30 LEU A C 1 ATOM 162 O O . LEU A 1 22 ? -41.941 8.089 -9.772 1.00 30.42 ? 30 LEU A O 1 ATOM 163 C CB . LEU A 1 22 ? -40.488 10.843 -10.368 1.00 30.77 ? 30 LEU A CB 1 ATOM 164 C CG . LEU A 1 22 ? -41.478 11.344 -11.406 1.00 31.31 ? 30 LEU A CG 1 ATOM 165 C CD1 . LEU A 1 22 ? -42.563 12.225 -10.795 1.00 31.21 ? 30 LEU A CD1 1 ATOM 166 C CD2 . LEU A 1 22 ? -40.683 12.130 -12.440 1.00 30.74 ? 30 LEU A CD2 1 ATOM 167 N N . GLU A 1 23 ? -39.841 7.955 -8.987 1.00 31.18 ? 31 GLU A N 1 ATOM 168 C CA . GLU A 1 23 ? -39.694 6.524 -9.247 1.00 31.86 ? 31 GLU A CA 1 ATOM 169 C C . GLU A 1 23 ? -38.880 5.815 -8.162 1.00 32.05 ? 31 GLU A C 1 ATOM 170 O O . GLU A 1 23 ? -37.992 6.408 -7.538 1.00 32.43 ? 31 GLU A O 1 ATOM 171 C CB . GLU A 1 23 ? -39.045 6.304 -10.623 1.00 31.66 ? 31 GLU A CB 1 ATOM 172 C CG . GLU A 1 23 ? -39.090 4.863 -11.113 1.00 32.15 ? 31 GLU A CG 1 ATOM 173 C CD . GLU A 1 23 ? -38.689 4.707 -12.577 1.00 32.79 ? 31 GLU A CD 1 ATOM 174 O OE1 . GLU A 1 23 ? -38.468 5.735 -13.272 1.00 31.36 ? 31 GLU A OE1 1 ATOM 175 O OE2 . GLU A 1 23 ? -38.598 3.539 -13.024 1.00 33.33 ? 31 GLU A OE2 1 ATOM 176 N N . ARG A 1 24 ? -39.197 4.545 -7.934 1.00 32.37 ? 32 ARG A N 1 ATOM 177 C CA . ARG A 1 24 ? -38.455 3.711 -6.986 1.00 32.66 ? 32 ARG A CA 1 ATOM 178 C C . ARG A 1 24 ? -37.798 2.542 -7.705 1.00 32.48 ? 32 ARG A C 1 ATOM 179 O O . ARG A 1 24 ? -38.250 2.149 -8.783 1.00 32.44 ? 32 ARG A O 1 ATOM 180 C CB . ARG A 1 24 ? -39.389 3.190 -5.890 1.00 33.50 ? 32 ARG A CB 1 ATOM 181 C CG . ARG A 1 24 ? -39.770 4.248 -4.862 1.00 35.10 ? 32 ARG A CG 1 ATOM 182 C CD . ARG A 1 24 ? -41.141 3.991 -4.257 1.00 39.36 ? 32 ARG A CD 1 ATOM 183 N NE . ARG A 1 24 ? -41.596 5.128 -3.449 1.00 42.02 ? 32 ARG A NE 1 ATOM 184 C CZ . ARG A 1 24 ? -42.824 5.262 -2.940 1.00 44.30 ? 32 ARG A CZ 1 ATOM 185 N NH1 . ARG A 1 24 ? -43.753 4.335 -3.154 1.00 45.23 ? 32 ARG A NH1 1 ATOM 186 N NH2 . ARG A 1 24 ? -43.130 6.335 -2.216 1.00 44.62 ? 32 ARG A NH2 1 ATOM 187 N N . ASN A 1 25 ? -36.723 2.011 -7.120 1.00 32.20 ? 33 ASN A N 1 ATOM 188 C CA . ASN A 1 25 ? -36.114 0.764 -7.594 1.00 32.10 ? 33 ASN A CA 1 ATOM 189 C C . ASN A 1 25 ? -35.508 0.911 -9.009 1.00 30.25 ? 33 ASN A C 1 ATOM 190 O O . ASN A 1 25 ? -35.667 0.033 -9.860 1.00 29.89 ? 33 ASN A O 1 ATOM 191 C CB . ASN A 1 25 ? -37.177 -0.355 -7.525 1.00 33.42 ? 33 ASN A CB 1 ATOM 192 C CG . ASN A 1 25 ? -36.605 -1.756 -7.689 1.00 38.54 ? 33 ASN A CG 1 ATOM 193 O OD1 . ASN A 1 25 ? -35.400 -1.989 -7.522 1.00 41.35 ? 33 ASN A OD1 1 ATOM 194 N ND2 . ASN A 1 25 ? -37.494 -2.707 -8.010 1.00 46.42 ? 33 ASN A ND2 1 ATOM 195 N N . VAL A 1 26 ? -34.831 2.035 -9.254 1.00 27.79 ? 34 VAL A N 1 ATOM 196 C CA . VAL A 1 26 ? -34.218 2.305 -10.562 1.00 25.16 ? 34 VAL A CA 1 ATOM 197 C C . VAL A 1 26 ? -32.810 1.720 -10.597 1.00 24.26 ? 34 VAL A C 1 ATOM 198 O O . VAL A 1 26 ? -32.015 1.968 -9.699 1.00 23.60 ? 34 VAL A O 1 ATOM 199 C CB . VAL A 1 26 ? -34.144 3.820 -10.888 1.00 24.90 ? 34 VAL A CB 1 ATOM 200 C CG1 . VAL A 1 26 ? -33.617 4.042 -12.313 1.00 24.14 ? 34 VAL A CG1 1 ATOM 201 C CG2 . VAL A 1 26 ? -35.509 4.486 -10.743 1.00 24.53 ? 34 VAL A CG2 1 ATOM 202 N N . THR A 1 27 ? -32.509 0.936 -11.635 1.00 22.67 ? 35 THR A N 1 ATOM 203 C CA . THR A 1 27 ? -31.160 0.421 -11.834 1.00 21.87 ? 35 THR A CA 1 ATOM 204 C C . THR A 1 27 ? -30.278 1.487 -12.497 1.00 20.80 ? 35 THR A C 1 ATOM 205 O O . THR A 1 27 ? -30.657 2.097 -13.485 1.00 20.38 ? 35 THR A O 1 ATOM 206 C CB . THR A 1 27 ? -31.155 -0.888 -12.691 1.00 22.06 ? 35 THR A CB 1 ATOM 207 O OG1 . THR A 1 27 ? -32.008 -1.867 -12.079 1.00 23.28 ? 35 THR A OG1 1 ATOM 208 C CG2 . THR A 1 27 ? -29.766 -1.469 -12.780 1.00 21.61 ? 35 THR A CG2 1 ATOM 209 N N . VAL A 1 28 ? -29.102 1.700 -11.925 1.00 20.51 ? 36 VAL A N 1 ATOM 210 C CA . VAL A 1 28 ? -28.173 2.708 -12.396 1.00 19.78 ? 36 VAL A CA 1 ATOM 211 C C . VAL A 1 28 ? -26.822 2.075 -12.699 1.00 20.01 ? 36 VAL A C 1 ATOM 212 O O . VAL A 1 28 ? -26.469 1.034 -12.145 1.00 20.45 ? 36 VAL A O 1 ATOM 213 C CB . VAL A 1 28 ? -28.031 3.899 -11.383 1.00 19.83 ? 36 VAL A CB 1 ATOM 214 C CG1 . VAL A 1 28 ? -29.355 4.666 -11.249 1.00 18.70 ? 36 VAL A CG1 1 ATOM 215 C CG2 . VAL A 1 28 ? -27.555 3.406 -10.021 1.00 20.54 ? 36 VAL A CG2 1 ATOM 216 N N . THR A 1 29 ? -26.056 2.702 -13.581 1.00 19.80 ? 37 THR A N 1 ATOM 217 C CA . THR A 1 29 ? -24.756 2.147 -13.957 1.00 20.20 ? 37 THR A CA 1 ATOM 218 C C . THR A 1 29 ? -23.713 2.222 -12.831 1.00 20.38 ? 37 THR A C 1 ATOM 219 O O . THR A 1 29 ? -22.821 1.365 -12.740 1.00 20.44 ? 37 THR A O 1 ATOM 220 C CB . THR A 1 29 ? -24.204 2.815 -15.226 1.00 19.80 ? 37 THR A CB 1 ATOM 221 O OG1 . THR A 1 29 ? -23.916 4.191 -14.954 1.00 19.94 ? 37 THR A OG1 1 ATOM 222 C CG2 . THR A 1 29 ? -25.220 2.718 -16.366 1.00 19.51 ? 37 THR A CG2 1 ATOM 223 N N . HIS A 1 30 ? -23.838 3.249 -11.985 1.00 20.32 ? 38 HIS A N 1 ATOM 224 C CA . HIS A 1 30 ? -22.917 3.491 -10.868 1.00 21.11 ? 38 HIS A CA 1 ATOM 225 C C . HIS A 1 30 ? -23.690 4.138 -9.745 1.00 20.73 ? 38 HIS A C 1 ATOM 226 O O . HIS A 1 30 ? -24.572 4.957 -9.981 1.00 19.57 ? 38 HIS A O 1 ATOM 227 C CB . HIS A 1 30 ? -21.776 4.430 -11.286 1.00 21.17 ? 38 HIS A CB 1 ATOM 228 C CG . HIS A 1 30 ? -20.976 3.929 -12.448 1.00 23.72 ? 38 HIS A CG 1 ATOM 229 N ND1 . HIS A 1 30 ? -21.315 4.202 -13.755 1.00 23.79 ? 38 HIS A ND1 1 ATOM 230 C CD2 . HIS A 1 30 ? -19.873 3.147 -12.498 1.00 24.89 ? 38 HIS A CD2 1 ATOM 231 C CE1 . HIS A 1 30 ? -20.446 3.621 -14.561 1.00 25.61 ? 38 HIS A CE1 1 ATOM 232 N NE2 . HIS A 1 30 ? -19.561 2.975 -13.823 1.00 25.70 ? 38 HIS A NE2 1 ATOM 233 N N . ALA A 1 31 ? -23.322 3.807 -8.511 1.00 21.77 ? 39 ALA A N 1 ATOM 234 C CA . ALA A 1 31 ? -23.993 4.390 -7.364 1.00 22.45 ? 39 ALA A CA 1 ATOM 235 C C . ALA A 1 31 ? -23.031 4.430 -6.193 1.00 22.81 ? 39 ALA A C 1 ATOM 236 O O . ALA A 1 31 ? -22.020 3.718 -6.197 1.00 22.91 ? 39 ALA A O 1 ATOM 237 C CB . ALA A 1 31 ? -25.244 3.591 -7.022 1.00 22.49 ? 39 ALA A CB 1 ATOM 238 N N . LYS A 1 32 ? -23.344 5.258 -5.197 1.00 23.97 ? 40 LYS A N 1 ATOM 239 C CA . LYS A 1 32 ? -22.490 5.416 -4.013 1.00 24.76 ? 40 LYS A CA 1 ATOM 240 C C . LYS A 1 32 ? -23.332 5.255 -2.758 1.00 25.02 ? 40 LYS A C 1 ATOM 241 O O . LYS A 1 32 ? -24.197 6.085 -2.455 1.00 24.87 ? 40 LYS A O 1 ATOM 242 C CB . LYS A 1 32 ? -21.778 6.779 -4.037 1.00 25.61 ? 40 LYS A CB 1 ATOM 243 C CG . LYS A 1 32 ? -20.833 7.055 -2.862 1.00 27.18 ? 40 LYS A CG 1 ATOM 244 C CD . LYS A 1 32 ? -19.688 6.060 -2.822 1.00 32.62 ? 40 LYS A CD 1 ATOM 245 C CE . LYS A 1 32 ? -18.912 6.148 -1.514 1.00 33.53 ? 40 LYS A CE 1 ATOM 246 N NZ . LYS A 1 32 ? -17.735 5.224 -1.572 1.00 36.44 ? 40 LYS A NZ 1 ATOM 247 N N . ASP A 1 33 ? -23.079 4.164 -2.045 1.00 25.59 ? 41 ASP A N 1 ATOM 248 C CA . ASP A 1 33 ? -23.746 3.894 -0.780 1.00 26.29 ? 41 ASP A CA 1 ATOM 249 C C . ASP A 1 33 ? -23.039 4.726 0.292 1.00 25.82 ? 41 ASP A C 1 ATOM 250 O O . ASP A 1 33 ? -21.823 4.582 0.501 1.00 25.84 ? 41 ASP A O 1 ATOM 251 C CB . ASP A 1 33 ? -23.678 2.395 -0.481 1.00 26.88 ? 41 ASP A CB 1 ATOM 252 C CG . ASP A 1 33 ? -24.362 2.007 0.836 1.00 28.77 ? 41 ASP A CG 1 ATOM 253 O OD1 . ASP A 1 33 ? -24.853 2.888 1.578 1.00 29.82 ? 41 ASP A OD1 1 ATOM 254 O OD2 . ASP A 1 33 ? -24.405 0.791 1.118 1.00 32.52 ? 41 ASP A OD2 1 ATOM 255 N N . ILE A 1 34 ? -23.790 5.596 0.961 1.00 25.60 ? 42 ILE A N 1 ATOM 256 C CA . ILE A 1 34 ? -23.174 6.512 1.936 1.00 25.25 ? 42 ILE A CA 1 ATOM 257 C C . ILE A 1 34 ? -23.527 6.198 3.394 1.00 25.01 ? 42 ILE A C 1 ATOM 258 O O . ILE A 1 34 ? -23.261 7.009 4.267 1.00 25.09 ? 42 ILE A O 1 ATOM 259 C CB . ILE A 1 34 ? -23.448 8.018 1.613 1.00 24.95 ? 42 ILE A CB 1 ATOM 260 C CG1 . ILE A 1 34 ? -24.950 8.356 1.710 1.00 25.15 ? 42 ILE A CG1 1 ATOM 261 C CG2 . ILE A 1 34 ? -22.843 8.391 0.232 1.00 25.79 ? 42 ILE A CG2 1 ATOM 262 C CD1 . ILE A 1 34 ? -25.314 9.849 1.454 1.00 24.81 ? 42 ILE A CD1 1 ATOM 263 N N . LEU A 1 35 ? -24.089 5.011 3.626 1.00 24.85 ? 43 LEU A N 1 ATOM 264 C CA . LEU A 1 35 ? -24.539 4.569 4.947 1.00 24.58 ? 43 LEU A CA 1 ATOM 265 C C . LEU A 1 35 ? -23.799 3.333 5.476 1.00 24.74 ? 43 LEU A C 1 ATOM 266 O O . LEU A 1 35 ? -23.891 2.234 4.912 1.00 24.75 ? 43 LEU A O 1 ATOM 267 C CB . LEU A 1 35 ? -26.061 4.322 4.944 1.00 24.35 ? 43 LEU A CB 1 ATOM 268 C CG . LEU A 1 35 ? -26.680 3.969 6.312 1.00 24.85 ? 43 LEU A CG 1 ATOM 269 C CD1 . LEU A 1 35 ? -26.670 5.192 7.221 1.00 25.78 ? 43 LEU A CD1 1 ATOM 270 C CD2 . LEU A 1 35 ? -28.076 3.389 6.213 1.00 24.66 ? 43 LEU A CD2 1 ATOM 271 N N . GLU A 1 36 ? -23.070 3.510 6.577 1.00 24.44 ? 44 GLU A N 1 ATOM 272 C CA . GLU A 1 36 ? -22.439 2.384 7.259 1.00 24.59 ? 44 GLU A CA 1 ATOM 273 C C . GLU A 1 36 ? -23.458 1.663 8.133 1.00 24.75 ? 44 GLU A C 1 ATOM 274 O O . GLU A 1 36 ? -24.120 2.276 8.985 1.00 23.87 ? 44 GLU A O 1 ATOM 275 C CB . GLU A 1 36 ? -21.257 2.854 8.120 1.00 24.74 ? 44 GLU A CB 1 ATOM 276 C CG . GLU A 1 36 ? -20.443 1.715 8.757 1.00 26.23 ? 44 GLU A CG 1 ATOM 277 C CD . GLU A 1 36 ? -19.928 0.719 7.721 1.00 29.27 ? 44 GLU A CD 1 ATOM 278 O OE1 . GLU A 1 36 ? -19.100 1.115 6.877 1.00 30.19 ? 44 GLU A OE1 1 ATOM 279 O OE2 . GLU A 1 36 ? -20.373 -0.456 7.735 1.00 30.28 ? 44 GLU A OE2 1 ATOM 280 N N . LYS A 1 37 ? -23.566 0.356 7.936 1.00 25.17 ? 45 LYS A N 1 ATOM 281 C CA . LYS A 1 37 ? -24.525 -0.453 8.681 1.00 26.47 ? 45 LYS A CA 1 ATOM 282 C C . LYS A 1 37 ? -23.824 -1.549 9.504 1.00 26.96 ? 45 LYS A C 1 ATOM 283 O O . LYS A 1 37 ? -24.493 -2.332 10.182 1.00 27.73 ? 45 LYS A O 1 ATOM 284 C CB . LYS A 1 37 ? -25.548 -1.083 7.708 1.00 26.61 ? 45 LYS A CB 1 ATOM 285 C CG . LYS A 1 37 ? -26.255 -0.056 6.817 1.00 27.69 ? 45 LYS A CG 1 ATOM 286 C CD . LYS A 1 37 ? -27.032 -0.718 5.662 1.00 28.74 ? 45 LYS A CD 1 ATOM 287 C CE . LYS A 1 37 ? -26.148 -0.969 4.447 1.00 32.92 ? 45 LYS A CE 1 ATOM 288 N NZ . LYS A 1 37 ? -25.481 0.244 3.851 1.00 33.51 ? 45 LYS A NZ 1 ATOM 289 N N . THR A 1 38 ? -22.491 -1.602 9.460 1.00 26.82 ? 46 THR A N 1 ATOM 290 C CA . THR A 1 38 ? -21.768 -2.685 10.143 1.00 27.05 ? 46 THR A CA 1 ATOM 291 C C . THR A 1 38 ? -20.915 -2.181 11.314 1.00 27.09 ? 46 THR A C 1 ATOM 292 O O . THR A 1 38 ? -20.547 -1.013 11.371 1.00 26.25 ? 46 THR A O 1 ATOM 293 C CB . THR A 1 38 ? -20.895 -3.536 9.194 1.00 27.29 ? 46 THR A CB 1 ATOM 294 O OG1 . THR A 1 38 ? -19.692 -2.827 8.865 1.00 28.00 ? 46 THR A OG1 1 ATOM 295 C CG2 . THR A 1 38 ? -21.653 -3.875 7.916 1.00 26.79 ? 46 THR A CG2 1 ATOM 296 N N . HIS A 1 39 ? -20.605 -3.094 12.223 1.00 27.27 ? 47 HIS A N 1 ATOM 297 C CA . HIS A 1 39 ? -19.764 -2.805 13.391 1.00 27.11 ? 47 HIS A CA 1 ATOM 298 C C . HIS A 1 39 ? -19.163 -4.147 13.796 1.00 26.87 ? 47 HIS A C 1 ATOM 299 O O . HIS A 1 39 ? -19.607 -5.183 13.292 1.00 27.29 ? 47 HIS A O 1 ATOM 300 C CB . HIS A 1 39 ? -20.606 -2.208 14.517 1.00 26.76 ? 47 HIS A CB 1 ATOM 301 C CG . HIS A 1 39 ? -21.696 -3.113 15.011 1.00 28.72 ? 47 HIS A CG 1 ATOM 302 N ND1 . HIS A 1 39 ? -21.464 -4.147 15.895 1.00 31.17 ? 47 HIS A ND1 1 ATOM 303 C CD2 . HIS A 1 39 ? -23.028 -3.119 14.769 1.00 30.25 ? 47 HIS A CD2 1 ATOM 304 C CE1 . HIS A 1 39 ? -22.602 -4.764 16.159 1.00 32.51 ? 47 HIS A CE1 1 ATOM 305 N NE2 . HIS A 1 39 ? -23.569 -4.157 15.492 1.00 32.23 ? 47 HIS A NE2 1 ATOM 306 N N . ASN A 1 40 ? -18.170 -4.147 14.693 1.00 25.60 ? 48 ASN A N 1 ATOM 307 C CA . ASN A 1 40 ? -17.408 -5.379 14.977 1.00 25.11 ? 48 ASN A CA 1 ATOM 308 C C . ASN A 1 40 ? -17.909 -6.171 16.183 1.00 24.62 ? 48 ASN A C 1 ATOM 309 O O . ASN A 1 40 ? -17.332 -7.195 16.532 1.00 24.96 ? 48 ASN A O 1 ATOM 310 C CB . ASN A 1 40 ? -15.910 -5.088 15.099 1.00 24.84 ? 48 ASN A CB 1 ATOM 311 C CG . ASN A 1 40 ? -15.564 -4.338 16.364 1.00 25.14 ? 48 ASN A CG 1 ATOM 312 O OD1 . ASN A 1 40 ? -16.445 -4.015 17.171 1.00 25.64 ? 48 ASN A OD1 1 ATOM 313 N ND2 . ASN A 1 40 ? -14.282 -4.045 16.538 1.00 25.05 ? 48 ASN A ND2 1 ATOM 314 N N . GLY A 1 41 ? -18.984 -5.674 16.788 1.00 24.59 ? 49 GLY A N 1 ATOM 315 C CA . GLY A 1 41 ? -19.681 -6.318 17.901 1.00 24.32 ? 49 GLY A CA 1 ATOM 316 C C . GLY A 1 41 ? -18.919 -6.311 19.214 1.00 24.16 ? 49 GLY A C 1 ATOM 317 O O . GLY A 1 41 ? -19.291 -7.014 20.151 1.00 24.99 ? 49 GLY A O 1 ATOM 318 N N . LYS A 1 42 ? -17.849 -5.522 19.285 1.00 22.77 ? 50 LYS A N 1 ATOM 319 C CA . LYS A 1 42 ? -16.960 -5.575 20.448 1.00 21.97 ? 50 LYS A CA 1 ATOM 320 C C . LYS A 1 42 ? -16.828 -4.206 21.098 1.00 20.75 ? 50 LYS A C 1 ATOM 321 O O . LYS A 1 42 ? -16.995 -3.184 20.435 1.00 20.36 ? 50 LYS A O 1 ATOM 322 C CB . LYS A 1 42 ? -15.585 -6.016 20.003 1.00 21.58 ? 50 LYS A CB 1 ATOM 323 C CG . LYS A 1 42 ? -15.504 -7.462 19.491 1.00 24.62 ? 50 LYS A CG 1 ATOM 324 C CD . LYS A 1 42 ? -14.130 -7.721 18.955 1.00 27.67 ? 50 LYS A CD 1 ATOM 325 C CE . LYS A 1 42 ? -14.001 -9.127 18.434 1.00 32.42 ? 50 LYS A CE 1 ATOM 326 N NZ . LYS A 1 42 ? -12.657 -9.317 17.850 1.00 35.01 ? 50 LYS A NZ 1 ATOM 327 N N . LEU A 1 43 ? -16.512 -4.198 22.394 1.00 21.05 ? 51 LEU A N 1 ATOM 328 C CA . LEU A 1 43 ? -16.101 -2.972 23.086 1.00 20.73 ? 51 LEU A CA 1 ATOM 329 C C . LEU A 1 43 ? -14.581 -2.922 23.052 1.00 19.45 ? 51 LEU A C 1 ATOM 330 O O . LEU A 1 43 ? -13.921 -3.912 23.357 1.00 19.36 ? 51 LEU A O 1 ATOM 331 C CB . LEU A 1 43 ? -16.597 -2.982 24.533 1.00 20.84 ? 51 LEU A CB 1 ATOM 332 C CG . LEU A 1 43 ? -18.129 -3.050 24.610 1.00 23.38 ? 51 LEU A CG 1 ATOM 333 C CD1 . LEU A 1 43 ? -18.640 -3.401 25.995 1.00 25.94 ? 51 LEU A CD1 1 ATOM 334 C CD2 . LEU A 1 43 ? -18.738 -1.731 24.126 1.00 26.80 ? 51 LEU A CD2 1 ATOM 335 N N . CYS A 1 44 ? -14.043 -1.779 22.631 1.00 19.59 ? 52 CYS A N 1 ATOM 336 C CA . CYS A 1 44 ? -12.626 -1.665 22.298 1.00 19.44 ? 52 CYS A CA 1 ATOM 337 C C . CYS A 1 44 ? -11.929 -0.501 23.024 1.00 18.58 ? 52 CYS A C 1 ATOM 338 O O . CYS A 1 44 ? -12.577 0.361 23.623 1.00 18.46 ? 52 CYS A O 1 ATOM 339 C CB . CYS A 1 44 ? -12.470 -1.456 20.795 1.00 19.99 ? 52 CYS A CB 1 ATOM 340 S SG . CYS A 1 44 ? -13.155 -2.817 19.802 1.00 23.44 ? 52 CYS A SG 1 ATOM 341 N N . LYS A 1 45 ? -10.602 -0.458 22.893 1.00 18.64 ? 53 LYS A N 1 ATOM 342 C CA . LYS A 1 45 ? -9.859 0.746 23.246 1.00 20.08 ? 53 LYS A CA 1 ATOM 343 C C . LYS A 1 45 ? -10.244 1.836 22.268 1.00 21.51 ? 53 LYS A C 1 ATOM 344 O O . LYS A 1 45 ? -10.539 1.534 21.118 1.00 22.12 ? 53 LYS A O 1 ATOM 345 C CB . LYS A 1 45 ? -8.357 0.503 23.151 1.00 19.83 ? 53 LYS A CB 1 ATOM 346 C CG . LYS A 1 45 ? -7.822 -0.475 24.178 1.00 20.99 ? 53 LYS A CG 1 ATOM 347 C CD . LYS A 1 45 ? -6.283 -0.660 24.036 1.00 22.54 ? 53 LYS A CD 1 ATOM 348 C CE . LYS A 1 45 ? -5.951 -1.731 22.994 1.00 31.13 ? 53 LYS A CE 1 ATOM 349 N NZ . LYS A 1 45 ? -6.252 -3.096 23.531 1.00 31.71 ? 53 LYS A NZ 1 ATOM 350 N N . LEU A 1 46 A -10.247 3.086 22.725 1.00 22.05 ? 53 LEU A N 1 ATOM 351 C CA . LEU A 1 46 A -10.586 4.230 21.864 1.00 24.15 ? 53 LEU A CA 1 ATOM 352 C C . LEU A 1 46 A -9.314 5.027 21.665 1.00 25.37 ? 53 LEU A C 1 ATOM 353 O O . LEU A 1 46 A -8.817 5.649 22.605 1.00 25.01 ? 53 LEU A O 1 ATOM 354 C CB . LEU A 1 46 A -11.683 5.093 22.495 1.00 24.90 ? 53 LEU A CB 1 ATOM 355 C CG . LEU A 1 46 A -12.247 6.270 21.669 1.00 24.16 ? 53 LEU A CG 1 ATOM 356 C CD1 . LEU A 1 46 A -13.029 5.775 20.475 1.00 26.75 ? 53 LEU A CD1 1 ATOM 357 C CD2 . LEU A 1 46 A -13.140 7.151 22.513 1.00 25.96 ? 53 LEU A CD2 1 ATOM 358 N N . ASN A 1 47 ? -8.756 4.950 20.458 1.00 26.64 ? 54 ASN A N 1 ATOM 359 C CA . ASN A 1 47 ? -7.445 5.528 20.185 1.00 27.68 ? 54 ASN A CA 1 ATOM 360 C C . ASN A 1 47 ? -6.356 5.025 21.112 1.00 27.41 ? 54 ASN A C 1 ATOM 361 O O . ASN A 1 47 ? -5.538 5.814 21.589 1.00 29.27 ? 54 ASN A O 1 ATOM 362 C CB . ASN A 1 47 ? -7.518 7.043 20.294 1.00 29.06 ? 54 ASN A CB 1 ATOM 363 C CG . ASN A 1 47 ? -8.471 7.638 19.315 1.00 31.63 ? 54 ASN A CG 1 ATOM 364 O OD1 . ASN A 1 47 ? -9.404 8.339 19.690 1.00 35.61 ? 54 ASN A OD1 1 ATOM 365 N ND2 . ASN A 1 47 ? -8.242 7.366 18.037 1.00 34.91 ? 54 ASN A ND2 1 ATOM 366 N N . GLY A 1 48 ? -6.375 3.733 21.405 1.00 25.00 ? 55 GLY A N 1 ATOM 367 C CA . GLY A 1 48 ? -5.392 3.107 22.268 1.00 24.31 ? 55 GLY A CA 1 ATOM 368 C C . GLY A 1 48 ? -5.601 3.314 23.759 1.00 22.88 ? 55 GLY A C 1 ATOM 369 O O . GLY A 1 48 ? -4.811 2.804 24.554 1.00 23.59 ? 55 GLY A O 1 ATOM 370 N N . ILE A 1 49 ? -6.640 4.061 24.148 1.00 21.11 ? 56 ILE A N 1 ATOM 371 C CA . ILE A 1 49 ? -6.907 4.299 25.572 1.00 20.13 ? 56 ILE A CA 1 ATOM 372 C C . ILE A 1 49 ? -8.100 3.421 25.984 1.00 19.17 ? 56 ILE A C 1 ATOM 373 O O . ILE A 1 49 ? -9.200 3.586 25.428 1.00 19.79 ? 56 ILE A O 1 ATOM 374 C CB . ILE A 1 49 ? -7.195 5.791 25.884 1.00 19.97 ? 56 ILE A CB 1 ATOM 375 C CG1 . ILE A 1 49 ? -6.002 6.653 25.386 1.00 20.65 ? 56 ILE A CG1 1 ATOM 376 C CG2 . ILE A 1 49 ? -7.519 5.996 27.399 1.00 21.20 ? 56 ILE A CG2 1 ATOM 377 C CD1 . ILE A 1 49 ? -6.262 8.138 25.408 1.00 24.23 ? 56 ILE A CD1 1 ATOM 378 N N . PRO A 1 50 ? -7.899 2.520 26.953 1.00 18.84 ? 57 PRO A N 1 ATOM 379 C CA . PRO A 1 50 ? -9.012 1.635 27.317 1.00 18.33 ? 57 PRO A CA 1 ATOM 380 C C . PRO A 1 50 ? -10.098 2.339 28.119 1.00 17.09 ? 57 PRO A C 1 ATOM 381 O O . PRO A 1 50 ? -9.846 3.349 28.797 1.00 18.01 ? 57 PRO A O 1 ATOM 382 C CB . PRO A 1 50 ? -8.362 0.546 28.173 1.00 17.91 ? 57 PRO A CB 1 ATOM 383 C CG . PRO A 1 50 ? -6.851 0.810 28.115 1.00 21.58 ? 57 PRO A CG 1 ATOM 384 C CD . PRO A 1 50 ? -6.680 2.240 27.741 1.00 18.89 ? 57 PRO A CD 1 ATOM 385 N N . PRO A 1 51 ? -11.322 1.842 28.023 1.00 16.78 ? 58 PRO A N 1 ATOM 386 C CA . PRO A 1 51 ? -12.359 2.347 28.938 1.00 16.28 ? 58 PRO A CA 1 ATOM 387 C C . PRO A 1 51 ? -12.116 1.867 30.376 1.00 15.70 ? 58 PRO A C 1 ATOM 388 O O . PRO A 1 51 ? -11.285 0.957 30.603 1.00 16.09 ? 58 PRO A O 1 ATOM 389 C CB . PRO A 1 51 ? -13.639 1.681 28.419 1.00 16.70 ? 58 PRO A CB 1 ATOM 390 C CG . PRO A 1 51 ? -13.141 0.365 27.802 1.00 16.00 ? 58 PRO A CG 1 ATOM 391 C CD . PRO A 1 51 ? -11.821 0.789 27.118 1.00 17.47 ? 58 PRO A CD 1 ATOM 392 N N . LEU A 1 52 ? -12.840 2.492 31.311 1.00 16.41 ? 59 LEU A N 1 ATOM 393 C CA . LEU A 1 52 ? -12.897 2.057 32.703 1.00 16.58 ? 59 LEU A CA 1 ATOM 394 C C . LEU A 1 52 ? -14.023 1.066 32.744 1.00 16.93 ? 59 LEU A C 1 ATOM 395 O O . LEU A 1 52 ? -15.160 1.427 32.455 1.00 17.72 ? 59 LEU A O 1 ATOM 396 C CB . LEU A 1 52 ? -13.201 3.240 33.647 1.00 16.09 ? 59 LEU A CB 1 ATOM 397 C CG . LEU A 1 52 ? -13.528 2.953 35.124 1.00 15.99 ? 59 LEU A CG 1 ATOM 398 C CD1 . LEU A 1 52 ? -12.424 2.081 35.759 1.00 19.10 ? 59 LEU A CD1 1 ATOM 399 C CD2 . LEU A 1 52 ? -13.664 4.280 35.875 1.00 14.27 ? 59 LEU A CD2 1 ATOM 400 N N . GLU A 1 53 ? -13.694 -0.188 33.053 1.00 16.85 ? 60 GLU A N 1 ATOM 401 C CA . GLU A 1 53 ? -14.708 -1.225 33.085 1.00 18.06 ? 60 GLU A CA 1 ATOM 402 C C . GLU A 1 53 ? -15.126 -1.435 34.540 1.00 16.76 ? 60 GLU A C 1 ATOM 403 O O . GLU A 1 53 ? -14.371 -1.981 35.366 1.00 16.26 ? 60 GLU A O 1 ATOM 404 C CB . GLU A 1 53 ? -14.198 -2.515 32.412 1.00 18.99 ? 60 GLU A CB 1 ATOM 405 C CG . GLU A 1 53 ? -15.240 -3.648 32.492 1.00 20.17 ? 60 GLU A CG 1 ATOM 406 C CD . GLU A 1 53 ? -14.932 -4.847 31.622 1.00 21.35 ? 60 GLU A CD 1 ATOM 407 O OE1 . GLU A 1 53 ? -14.103 -4.726 30.694 1.00 22.48 ? 60 GLU A OE1 1 ATOM 408 O OE2 . GLU A 1 53 ? -15.525 -5.927 31.890 1.00 22.77 ? 60 GLU A OE2 1 ATOM 409 N N . LEU A 1 54 ? -16.324 -0.949 34.868 1.00 16.13 ? 61 LEU A N 1 ATOM 410 C CA . LEU A 1 54 ? -16.820 -1.054 36.259 1.00 15.59 ? 61 LEU A CA 1 ATOM 411 C C . LEU A 1 54 ? -17.187 -2.480 36.669 1.00 16.16 ? 61 LEU A C 1 ATOM 412 O O . LEU A 1 54 ? -17.238 -2.770 37.879 1.00 17.01 ? 61 LEU A O 1 ATOM 413 C CB . LEU A 1 54 ? -18.031 -0.124 36.475 1.00 15.75 ? 61 LEU A CB 1 ATOM 414 C CG . LEU A 1 54 ? -17.697 1.354 36.292 1.00 14.50 ? 61 LEU A CG 1 ATOM 415 C CD1 . LEU A 1 54 ? -18.964 2.182 36.458 1.00 16.21 ? 61 LEU A CD1 1 ATOM 416 C CD2 . LEU A 1 54 ? -16.603 1.809 37.289 1.00 18.24 ? 61 LEU A CD2 1 ATOM 417 N N . GLY A 1 55 ? -17.477 -3.350 35.685 1.00 16.71 ? 62 GLY A N 1 ATOM 418 C CA . GLY A 1 55 ? -17.881 -4.739 35.970 1.00 18.09 ? 62 GLY A CA 1 ATOM 419 C C . GLY A 1 55 ? -19.212 -4.775 36.689 1.00 17.19 ? 62 GLY A C 1 ATOM 420 O O . GLY A 1 55 ? -20.212 -4.278 36.142 1.00 18.90 ? 62 GLY A O 1 ATOM 421 N N . ASP A 1 56 ? -19.241 -5.327 37.914 1.00 17.74 ? 63 ASP A N 1 ATOM 422 C CA . ASP A 1 56 ? -20.503 -5.357 38.658 1.00 17.77 ? 63 ASP A CA 1 ATOM 423 C C . ASP A 1 56 ? -20.702 -4.119 39.534 1.00 17.77 ? 63 ASP A C 1 ATOM 424 O O . ASP A 1 56 ? -21.621 -4.098 40.335 1.00 18.45 ? 63 ASP A O 1 ATOM 425 C CB . ASP A 1 56 ? -20.604 -6.618 39.519 1.00 17.98 ? 63 ASP A CB 1 ATOM 426 C CG . ASP A 1 56 ? -20.713 -7.877 38.678 1.00 19.25 ? 63 ASP A CG 1 ATOM 427 O OD1 . ASP A 1 56 ? -21.523 -7.909 37.732 1.00 21.05 ? 63 ASP A OD1 1 ATOM 428 O OD2 . ASP A 1 56 ? -19.955 -8.817 38.964 1.00 23.20 ? 63 ASP A OD2 1 ATOM 429 N N . CYS A 1 57 ? -19.810 -3.130 39.424 1.00 17.27 ? 64 CYS A N 1 ATOM 430 C CA . CYS A 1 57 ? -19.845 -1.981 40.326 1.00 17.79 ? 64 CYS A CA 1 ATOM 431 C C . CYS A 1 57 ? -20.596 -0.828 39.690 1.00 17.20 ? 64 CYS A C 1 ATOM 432 O O . CYS A 1 57 ? -20.506 -0.624 38.487 1.00 17.25 ? 64 CYS A O 1 ATOM 433 C CB . CYS A 1 57 ? -18.406 -1.524 40.674 1.00 19.08 ? 64 CYS A CB 1 ATOM 434 S SG . CYS A 1 57 ? -17.622 -2.748 41.724 1.00 22.13 ? 64 CYS A SG 1 ATOM 435 N N . SER A 1 58 ? -21.306 -0.043 40.495 1.00 16.33 ? 65 SER A N 1 ATOM 436 C CA . SER A 1 58 ? -21.864 1.203 40.000 1.00 16.42 ? 65 SER A CA 1 ATOM 437 C C . SER A 1 58 ? -20.866 2.338 40.186 1.00 15.53 ? 65 SER A C 1 ATOM 438 O O . SER A 1 58 ? -19.858 2.169 40.896 1.00 14.75 ? 65 SER A O 1 ATOM 439 C CB . SER A 1 58 ? -23.128 1.590 40.752 1.00 17.90 ? 65 SER A CB 1 ATOM 440 O OG . SER A 1 58 ? -22.868 1.895 42.116 1.00 14.11 ? 65 SER A OG 1 ATOM 441 N N . ILE A 1 59 ? -21.159 3.483 39.578 1.00 15.15 ? 66 ILE A N 1 ATOM 442 C CA . ILE A 1 59 ? -20.357 4.706 39.838 1.00 15.85 ? 66 ILE A CA 1 ATOM 443 C C . ILE A 1 59 ? -20.222 4.941 41.356 1.00 14.63 ? 66 ILE A C 1 ATOM 444 O O . ILE A 1 59 ? -19.132 5.217 41.870 1.00 14.44 ? 66 ILE A O 1 ATOM 445 C CB . ILE A 1 59 ? -21.015 5.926 39.090 1.00 16.70 ? 66 ILE A CB 1 ATOM 446 C CG1 . ILE A 1 59 ? -20.845 5.738 37.572 1.00 17.63 ? 66 ILE A CG1 1 ATOM 447 C CG2 . ILE A 1 59 ? -20.374 7.248 39.538 1.00 17.50 ? 66 ILE A CG2 1 ATOM 448 C CD1 . ILE A 1 59 ? -19.395 5.735 37.103 1.00 21.87 ? 66 ILE A CD1 1 ATOM 449 N N . ALA A 1 60 ? -21.342 4.850 42.080 1.00 14.98 ? 67 ALA A N 1 ATOM 450 C CA . ALA A 1 60 ? -21.340 5.054 43.535 1.00 15.06 ? 67 ALA A CA 1 ATOM 451 C C . ALA A 1 60 ? -20.478 3.993 44.234 1.00 15.57 ? 67 ALA A C 1 ATOM 452 O O . ALA A 1 60 ? -19.675 4.291 45.136 1.00 14.47 ? 67 ALA A O 1 ATOM 453 C CB . ALA A 1 60 ? -22.790 4.968 44.080 1.00 16.00 ? 67 ALA A CB 1 ATOM 454 N N . GLY A 1 61 ? -20.653 2.732 43.843 1.00 15.18 ? 68 GLY A N 1 ATOM 455 C CA . GLY A 1 61 ? -19.807 1.688 44.410 1.00 15.51 ? 68 GLY A CA 1 ATOM 456 C C . GLY A 1 61 ? -18.319 1.926 44.233 1.00 15.07 ? 68 GLY A C 1 ATOM 457 O O . GLY A 1 61 ? -17.525 1.711 45.141 1.00 16.38 ? 68 GLY A O 1 ATOM 458 N N . TRP A 1 62 ? -17.939 2.395 43.057 1.00 14.21 ? 69 TRP A N 1 ATOM 459 C CA . TRP A 1 62 ? -16.560 2.754 42.812 1.00 13.45 ? 69 TRP A CA 1 ATOM 460 C C . TRP A 1 62 ? -16.097 3.907 43.717 1.00 14.08 ? 69 TRP A C 1 ATOM 461 O O . TRP A 1 62 ? -15.099 3.775 44.451 1.00 14.04 ? 69 TRP A O 1 ATOM 462 C CB . TRP A 1 62 ? -16.416 3.086 41.319 1.00 13.85 ? 69 TRP A CB 1 ATOM 463 C CG . TRP A 1 62 ? -15.166 3.847 40.894 1.00 13.58 ? 69 TRP A CG 1 ATOM 464 C CD1 . TRP A 1 62 ? -13.888 3.735 41.397 1.00 15.84 ? 69 TRP A CD1 1 ATOM 465 C CD2 . TRP A 1 62 ? -15.123 4.875 39.895 1.00 14.24 ? 69 TRP A CD2 1 ATOM 466 N NE1 . TRP A 1 62 ? -13.047 4.604 40.723 1.00 15.18 ? 69 TRP A NE1 1 ATOM 467 C CE2 . TRP A 1 62 ? -13.778 5.316 39.802 1.00 14.08 ? 69 TRP A CE2 1 ATOM 468 C CE3 . TRP A 1 62 ? -16.083 5.428 39.028 1.00 14.61 ? 69 TRP A CE3 1 ATOM 469 C CZ2 . TRP A 1 62 ? -13.379 6.324 38.892 1.00 15.00 ? 69 TRP A CZ2 1 ATOM 470 C CZ3 . TRP A 1 62 ? -15.700 6.448 38.134 1.00 14.50 ? 69 TRP A CZ3 1 ATOM 471 C CH2 . TRP A 1 62 ? -14.352 6.869 38.063 1.00 16.57 ? 69 TRP A CH2 1 ATOM 472 N N . LEU A 1 63 ? -16.817 5.029 43.675 1.00 13.40 ? 70 LEU A N 1 ATOM 473 C CA . LEU A 1 63 ? -16.281 6.234 44.298 1.00 14.39 ? 70 LEU A CA 1 ATOM 474 C C . LEU A 1 63 ? -16.312 6.145 45.835 1.00 14.02 ? 70 LEU A C 1 ATOM 475 O O . LEU A 1 63 ? -15.424 6.662 46.489 1.00 15.24 ? 70 LEU A O 1 ATOM 476 C CB . LEU A 1 63 ? -17.002 7.489 43.789 1.00 14.89 ? 70 LEU A CB 1 ATOM 477 C CG . LEU A 1 63 ? -16.792 7.708 42.279 1.00 14.24 ? 70 LEU A CG 1 ATOM 478 C CD1 . LEU A 1 63 ? -17.744 8.784 41.733 1.00 18.25 ? 70 LEU A CD1 1 ATOM 479 C CD2 . LEU A 1 63 ? -15.300 8.003 41.932 1.00 18.93 ? 70 LEU A CD2 1 ATOM 480 N N . LEU A 1 64 ? -17.334 5.480 46.370 1.00 13.49 ? 71 LEU A N 1 ATOM 481 C CA . LEU A 1 64 ? -17.443 5.292 47.831 1.00 13.04 ? 71 LEU A CA 1 ATOM 482 C C . LEU A 1 64 ? -16.422 4.230 48.282 1.00 14.56 ? 71 LEU A C 1 ATOM 483 O O . LEU A 1 64 ? -15.955 4.272 49.429 1.00 13.65 ? 71 LEU A O 1 ATOM 484 C CB . LEU A 1 64 ? -18.837 4.808 48.236 1.00 13.75 ? 71 LEU A CB 1 ATOM 485 C CG . LEU A 1 64 ? -19.960 5.842 48.081 1.00 13.08 ? 71 LEU A CG 1 ATOM 486 C CD1 . LEU A 1 64 ? -21.286 5.159 48.232 1.00 15.50 ? 71 LEU A CD1 1 ATOM 487 C CD2 . LEU A 1 64 ? -19.758 6.970 49.044 1.00 16.67 ? 71 LEU A CD2 1 ATOM 488 N N . GLY A 1 65 ? -16.149 3.253 47.402 1.00 13.50 ? 72 GLY A N 1 ATOM 489 C CA . GLY A 1 65 ? -15.246 2.171 47.733 1.00 14.72 ? 72 GLY A CA 1 ATOM 490 C C . GLY A 1 65 ? -15.913 0.949 48.331 1.00 14.36 ? 72 GLY A C 1 ATOM 491 O O . GLY A 1 65 ? -15.409 0.342 49.281 1.00 13.77 ? 72 GLY A O 1 ATOM 492 N N . ASN A 1 66 ? -17.040 0.575 47.756 1.00 13.95 ? 73 ASN A N 1 ATOM 493 C CA . ASN A 1 66 ? -17.682 -0.690 48.153 1.00 13.31 ? 73 ASN A CA 1 ATOM 494 C C . ASN A 1 66 ? -16.586 -1.777 48.110 1.00 13.53 ? 73 ASN A C 1 ATOM 495 O O . ASN A 1 66 ? -15.860 -1.837 47.119 1.00 14.16 ? 73 ASN A O 1 ATOM 496 C CB . ASN A 1 66 ? -18.749 -0.976 47.114 1.00 13.26 ? 73 ASN A CB 1 ATOM 497 C CG . ASN A 1 66 ? -19.502 -2.278 47.363 1.00 13.67 ? 73 ASN A CG 1 ATOM 498 O OD1 . ASN A 1 66 ? -18.905 -3.279 47.728 1.00 17.50 ? 73 ASN A OD1 1 ATOM 499 N ND2 . ASN A 1 66 ? -20.832 -2.272 47.101 1.00 15.23 ? 73 ASN A ND2 1 ATOM 500 N N . PRO A 1 67 ? -16.424 -2.571 49.187 1.00 14.27 ? 74 PRO A N 1 ATOM 501 C CA . PRO A 1 67 ? -15.322 -3.578 49.157 1.00 16.12 ? 74 PRO A CA 1 ATOM 502 C C . PRO A 1 67 ? -15.362 -4.568 47.990 1.00 16.76 ? 74 PRO A C 1 ATOM 503 O O . PRO A 1 67 ? -14.323 -5.185 47.670 1.00 19.15 ? 74 PRO A O 1 ATOM 504 C CB . PRO A 1 67 ? -15.420 -4.288 50.520 1.00 17.17 ? 74 PRO A CB 1 ATOM 505 C CG . PRO A 1 67 ? -16.158 -3.319 51.415 1.00 17.71 ? 74 PRO A CG 1 ATOM 506 C CD . PRO A 1 67 ? -17.087 -2.535 50.506 1.00 15.78 ? 74 PRO A CD 1 ATOM 507 N N . GLU A 1 68 ? -16.511 -4.744 47.367 1.00 16.44 ? 75 GLU A N 1 ATOM 508 C CA . GLU A 1 68 ? -16.576 -5.624 46.177 1.00 18.40 ? 75 GLU A CA 1 ATOM 509 C C . GLU A 1 68 ? -15.933 -4.969 44.938 1.00 18.46 ? 75 GLU A C 1 ATOM 510 O O . GLU A 1 68 ? -15.830 -5.598 43.841 1.00 20.49 ? 75 GLU A O 1 ATOM 511 C CB . GLU A 1 68 ? -18.027 -6.018 45.885 1.00 18.88 ? 75 GLU A CB 1 ATOM 512 C CG . GLU A 1 68 ? -18.714 -6.810 46.993 1.00 19.83 ? 75 GLU A CG 1 ATOM 513 C CD . GLU A 1 68 ? -18.088 -8.185 47.277 1.00 28.70 ? 75 GLU A CD 1 ATOM 514 O OE1 . GLU A 1 68 ? -17.571 -8.852 46.345 1.00 28.82 ? 75 GLU A OE1 1 ATOM 515 O OE2 . GLU A 1 68 ? -18.117 -8.600 48.459 1.00 33.01 ? 75 GLU A OE2 1 ATOM 516 N N . CYS A 1 69 ? -15.482 -3.719 45.088 1.00 17.62 ? 76 CYS A N 1 ATOM 517 C CA . CYS A 1 69 ? -14.990 -2.930 43.956 1.00 18.10 ? 76 CYS A CA 1 ATOM 518 C C . CYS A 1 69 ? -13.505 -2.604 44.125 1.00 17.55 ? 76 CYS A C 1 ATOM 519 O O . CYS A 1 69 ? -13.002 -1.663 43.519 1.00 17.22 ? 76 CYS A O 1 ATOM 520 C CB . CYS A 1 69 ? -15.793 -1.635 43.807 1.00 17.78 ? 76 CYS A CB 1 ATOM 521 S SG . CYS A 1 69 ? -17.575 -1.941 43.630 1.00 21.17 ? 76 CYS A SG 1 ATOM 522 N N . ASP A 1 70 ? -12.808 -3.407 44.936 1.00 17.37 ? 77 ASP A N 1 ATOM 523 C CA . ASP A 1 70 ? -11.443 -3.076 45.325 1.00 18.79 ? 77 ASP A CA 1 ATOM 524 C C . ASP A 1 70 ? -10.473 -3.004 44.128 1.00 18.03 ? 77 ASP A C 1 ATOM 525 O O . ASP A 1 70 ? -9.426 -2.354 44.210 1.00 17.77 ? 77 ASP A O 1 ATOM 526 C CB . ASP A 1 70 ? -10.919 -4.084 46.349 1.00 20.35 ? 77 ASP A CB 1 ATOM 527 C CG . ASP A 1 70 ? -11.312 -3.744 47.777 1.00 24.69 ? 77 ASP A CG 1 ATOM 528 O OD1 . ASP A 1 70 ? -11.973 -2.708 48.006 1.00 26.00 ? 77 ASP A OD1 1 ATOM 529 O OD2 . ASP A 1 70 ? -10.934 -4.540 48.671 1.00 29.07 ? 77 ASP A OD2 1 ATOM 530 N N . ARG A 1 71 ? -10.792 -3.689 43.028 1.00 18.06 ? 78 ARG A N 1 ATOM 531 C CA . ARG A 1 71 ? -9.932 -3.570 41.848 1.00 19.15 ? 78 ARG A CA 1 ATOM 532 C C . ARG A 1 71 ? -9.892 -2.149 41.266 1.00 19.22 ? 78 ARG A C 1 ATOM 533 O O . ARG A 1 71 ? -9.006 -1.846 40.432 1.00 20.77 ? 78 ARG A O 1 ATOM 534 C CB . ARG A 1 71 ? -10.349 -4.516 40.739 1.00 20.37 ? 78 ARG A CB 1 ATOM 535 C CG . ARG A 1 71 ? -11.763 -4.314 40.337 1.00 23.18 ? 78 ARG A CG 1 ATOM 536 C CD . ARG A 1 71 ? -12.228 -5.415 39.392 1.00 32.96 ? 78 ARG A CD 1 ATOM 537 N NE . ARG A 1 71 ? -13.657 -5.263 39.066 1.00 36.02 ? 78 ARG A NE 1 ATOM 538 C CZ . ARG A 1 71 ? -14.656 -5.327 39.954 1.00 40.61 ? 78 ARG A CZ 1 ATOM 539 N NH1 . ARG A 1 71 ? -14.400 -5.520 41.251 1.00 40.15 ? 78 ARG A NH1 1 ATOM 540 N NH2 . ARG A 1 71 ? -15.926 -5.198 39.548 1.00 42.75 ? 78 ARG A NH2 1 ATOM 541 N N . LEU A 1 72 ? -10.836 -1.308 41.694 1.00 17.09 ? 79 LEU A N 1 ATOM 542 C CA . LEU A 1 72 ? -10.998 0.027 41.164 1.00 16.10 ? 79 LEU A CA 1 ATOM 543 C C . LEU A 1 72 ? -10.397 1.078 42.105 1.00 16.06 ? 79 LEU A C 1 ATOM 544 O O . LEU A 1 72 ? -10.647 2.275 41.902 1.00 16.84 ? 79 LEU A O 1 ATOM 545 C CB . LEU A 1 72 ? -12.494 0.353 40.968 1.00 15.65 ? 79 LEU A CB 1 ATOM 546 C CG . LEU A 1 72 ? -13.334 -0.590 40.082 1.00 14.87 ? 79 LEU A CG 1 ATOM 547 C CD1 . LEU A 1 72 ? -14.740 -0.011 39.948 1.00 15.37 ? 79 LEU A CD1 1 ATOM 548 C CD2 . LEU A 1 72 ? -12.648 -0.790 38.702 1.00 19.52 ? 79 LEU A CD2 1 ATOM 549 N N . LEU A 1 73 ? -9.682 0.642 43.152 1.00 15.06 ? 80 LEU A N 1 ATOM 550 C CA . LEU A 1 73 ? -9.125 1.594 44.136 1.00 16.18 ? 80 LEU A CA 1 ATOM 551 C C . LEU A 1 73 ? -8.142 2.613 43.570 1.00 15.93 ? 80 LEU A C 1 ATOM 552 O O . LEU A 1 73 ? -8.002 3.727 44.136 1.00 17.86 ? 80 LEU A O 1 ATOM 553 C CB . LEU A 1 73 ? -8.531 0.890 45.356 1.00 16.71 ? 80 LEU A CB 1 ATOM 554 C CG . LEU A 1 73 ? -9.537 0.258 46.331 1.00 15.32 ? 80 LEU A CG 1 ATOM 555 C CD1 . LEU A 1 73 ? -8.872 -0.724 47.261 1.00 18.85 ? 80 LEU A CD1 1 ATOM 556 C CD2 . LEU A 1 73 ? -10.272 1.336 47.169 1.00 17.90 ? 80 LEU A CD2 1 ATOM 557 N N . SER A 1 74 ? -7.469 2.242 42.482 1.00 16.10 ? 81 SER A N 1 ATOM 558 C CA . SER A 1 74 ? -6.651 3.199 41.743 1.00 17.95 ? 81 SER A CA 1 ATOM 559 C C . SER A 1 74 ? -6.803 2.811 40.293 1.00 17.29 ? 81 SER A C 1 ATOM 560 O O . SER A 1 74 ? -6.507 1.666 39.933 1.00 18.39 ? 81 SER A O 1 ATOM 561 C CB . SER A 1 74 ? -5.202 3.086 42.184 1.00 19.12 ? 81 SER A CB 1 ATOM 562 O OG . SER A 1 74 ? -4.353 3.941 41.422 1.00 22.42 ? 81 SER A OG 1 ATOM 563 N N . VAL A 1 75 A -7.307 3.723 39.472 1.00 17.50 ? 81 VAL A N 1 ATOM 564 C CA . VAL A 1 75 A -7.478 3.399 38.045 1.00 17.69 ? 81 VAL A CA 1 ATOM 565 C C . VAL A 1 75 A -6.841 4.483 37.161 1.00 17.82 ? 81 VAL A C 1 ATOM 566 O O . VAL A 1 75 A -6.853 5.684 37.526 1.00 16.90 ? 81 VAL A O 1 ATOM 567 C CB . VAL A 1 75 A -8.966 3.187 37.660 1.00 18.78 ? 81 VAL A CB 1 ATOM 568 C CG1 . VAL A 1 75 A -9.570 2.009 38.447 1.00 18.78 ? 81 VAL A CG1 1 ATOM 569 C CG2 . VAL A 1 75 A -9.771 4.429 37.913 1.00 18.05 ? 81 VAL A CG2 1 ATOM 570 N N . PRO A 1 76 ? -6.253 4.072 36.020 1.00 18.32 ? 82 PRO A N 1 ATOM 571 C CA . PRO A 1 76 ? -5.584 5.020 35.124 1.00 18.27 ? 82 PRO A CA 1 ATOM 572 C C . PRO A 1 76 ? -6.576 5.761 34.249 1.00 18.44 ? 82 PRO A C 1 ATOM 573 O O . PRO A 1 76 ? -7.778 5.497 34.329 1.00 18.12 ? 82 PRO A O 1 ATOM 574 C CB . PRO A 1 76 ? -4.701 4.113 34.264 1.00 18.20 ? 82 PRO A CB 1 ATOM 575 C CG . PRO A 1 76 ? -5.452 2.798 34.215 1.00 18.16 ? 82 PRO A CG 1 ATOM 576 C CD . PRO A 1 76 ? -6.108 2.668 35.566 1.00 18.49 ? 82 PRO A CD 1 ATOM 577 N N . GLU A 1 77 ? -6.088 6.714 33.459 1.00 18.28 ? 83 GLU A N 1 ATOM 578 C CA . GLU A 1 77 ? -6.943 7.479 32.590 1.00 19.19 ? 83 GLU A CA 1 ATOM 579 C C . GLU A 1 77 ? -7.786 6.552 31.711 1.00 17.88 ? 83 GLU A C 1 ATOM 580 O O . GLU A 1 77 ? -7.302 5.517 31.264 1.00 18.27 ? 83 GLU A O 1 ATOM 581 C CB . GLU A 1 77 ? -6.070 8.413 31.727 1.00 20.30 ? 83 GLU A CB 1 ATOM 582 C CG . GLU A 1 77 ? -6.861 9.166 30.695 1.00 25.54 ? 83 GLU A CG 1 ATOM 583 C CD . GLU A 1 77 ? -5.994 9.806 29.589 1.00 25.49 ? 83 GLU A CD 1 ATOM 584 O OE1 . GLU A 1 77 ? -4.757 9.739 29.669 1.00 31.37 ? 83 GLU A OE1 1 ATOM 585 O OE2 . GLU A 1 77 ? -6.599 10.417 28.677 1.00 34.93 ? 83 GLU A OE2 1 ATOM 586 N N . TRP A 1 78 ? -9.025 6.955 31.448 1.00 17.28 ? 84 TRP A N 1 ATOM 587 C CA . TRP A 1 78 ? -9.955 6.179 30.593 1.00 16.75 ? 84 TRP A CA 1 ATOM 588 C C . TRP A 1 78 ? -10.475 7.008 29.419 1.00 17.13 ? 84 TRP A C 1 ATOM 589 O O . TRP A 1 78 ? -10.449 8.238 29.462 1.00 17.90 ? 84 TRP A O 1 ATOM 590 C CB . TRP A 1 78 ? -11.149 5.651 31.416 1.00 17.71 ? 84 TRP A CB 1 ATOM 591 C CG . TRP A 1 78 ? -11.944 6.740 32.083 1.00 16.96 ? 84 TRP A CG 1 ATOM 592 C CD1 . TRP A 1 78 ? -12.953 7.456 31.528 1.00 18.30 ? 84 TRP A CD1 1 ATOM 593 C CD2 . TRP A 1 78 ? -11.774 7.264 33.433 1.00 16.12 ? 84 TRP A CD2 1 ATOM 594 N NE1 . TRP A 1 78 ? -13.438 8.397 32.432 1.00 18.92 ? 84 TRP A NE1 1 ATOM 595 C CE2 . TRP A 1 78 ? -12.727 8.287 33.603 1.00 16.38 ? 84 TRP A CE2 1 ATOM 596 C CE3 . TRP A 1 78 ? -10.910 6.946 34.508 1.00 15.61 ? 84 TRP A CE3 1 ATOM 597 C CZ2 . TRP A 1 78 ? -12.862 9.010 34.819 1.00 16.28 ? 84 TRP A CZ2 1 ATOM 598 C CZ3 . TRP A 1 78 ? -11.020 7.675 35.709 1.00 15.85 ? 84 TRP A CZ3 1 ATOM 599 C CH2 . TRP A 1 78 ? -11.994 8.708 35.849 1.00 16.51 ? 84 TRP A CH2 1 ATOM 600 N N . SER A 1 79 ? -11.030 6.324 28.414 1.00 17.43 ? 85 SER A N 1 ATOM 601 C CA . SER A 1 79 ? -11.656 6.986 27.246 1.00 18.04 ? 85 SER A CA 1 ATOM 602 C C . SER A 1 79 ? -13.190 7.029 27.309 1.00 18.08 ? 85 SER A C 1 ATOM 603 O O . SER A 1 79 ? -13.807 7.895 26.702 1.00 19.88 ? 85 SER A O 1 ATOM 604 C CB . SER A 1 79 ? -11.232 6.243 25.990 1.00 18.26 ? 85 SER A CB 1 ATOM 605 O OG . SER A 1 79 ? -11.412 4.850 26.172 1.00 18.50 ? 85 SER A OG 1 ATOM 606 N N . TYR A 1 80 ? -13.786 6.095 28.043 1.00 17.92 ? 86 TYR A N 1 ATOM 607 C CA . TYR A 1 80 ? -15.233 6.073 28.342 1.00 16.89 ? 86 TYR A CA 1 ATOM 608 C C . TYR A 1 80 ? -15.398 5.130 29.526 1.00 17.52 ? 86 TYR A C 1 ATOM 609 O O . TYR A 1 80 ? -14.457 4.427 29.899 1.00 16.58 ? 86 TYR A O 1 ATOM 610 C CB . TYR A 1 80 ? -16.077 5.620 27.107 1.00 17.24 ? 86 TYR A CB 1 ATOM 611 C CG . TYR A 1 80 ? -15.759 4.274 26.495 1.00 18.25 ? 86 TYR A CG 1 ATOM 612 C CD1 . TYR A 1 80 ? -16.596 3.189 26.715 1.00 17.87 ? 86 TYR A CD1 1 ATOM 613 C CD2 . TYR A 1 80 ? -14.676 4.112 25.601 1.00 18.32 ? 86 TYR A CD2 1 ATOM 614 C CE1 . TYR A 1 80 ? -16.332 1.955 26.165 1.00 17.54 ? 86 TYR A CE1 1 ATOM 615 C CE2 . TYR A 1 80 ? -14.399 2.854 25.028 1.00 18.80 ? 86 TYR A CE2 1 ATOM 616 C CZ . TYR A 1 80 ? -15.247 1.789 25.304 1.00 17.51 ? 86 TYR A CZ 1 ATOM 617 O OH . TYR A 1 80 ? -15.034 0.567 24.758 1.00 18.92 ? 86 TYR A OH 1 ATOM 618 N N . ILE A 1 81 ? -16.553 5.172 30.168 1.00 16.62 ? 87 ILE A N 1 ATOM 619 C CA . ILE A 1 81 ? -16.806 4.320 31.328 1.00 17.17 ? 87 ILE A CA 1 ATOM 620 C C . ILE A 1 81 ? -17.883 3.342 30.959 1.00 17.74 ? 87 ILE A C 1 ATOM 621 O O . ILE A 1 81 ? -18.920 3.755 30.428 1.00 18.99 ? 87 ILE A O 1 ATOM 622 C CB . ILE A 1 81 ? -17.258 5.158 32.528 1.00 17.03 ? 87 ILE A CB 1 ATOM 623 C CG1 . ILE A 1 81 ? -16.127 6.122 32.917 1.00 17.37 ? 87 ILE A CG1 1 ATOM 624 C CG2 . ILE A 1 81 ? -17.631 4.260 33.719 1.00 18.29 ? 87 ILE A CG2 1 ATOM 625 C CD1 . ILE A 1 81 ? -16.546 7.135 34.034 1.00 18.11 ? 87 ILE A CD1 1 ATOM 626 N N . MET A 1 82 ? -17.653 2.077 31.257 1.00 16.26 ? 88 MET A N 1 ATOM 627 C CA . MET A 1 82 ? -18.655 1.022 30.989 1.00 18.25 ? 88 MET A CA 1 ATOM 628 C C . MET A 1 82 ? -19.397 0.699 32.260 1.00 17.10 ? 88 MET A C 1 ATOM 629 O O . MET A 1 82 ? -18.775 0.276 33.236 1.00 17.62 ? 88 MET A O 1 ATOM 630 C CB . MET A 1 82 ? -18.024 -0.252 30.430 1.00 18.07 ? 88 MET A CB 1 ATOM 631 C CG . MET A 1 82 ? -17.338 -0.079 29.060 1.00 18.55 ? 88 MET A CG 1 ATOM 632 S SD . MET A 1 82 ? -16.108 -1.348 28.801 1.00 22.02 ? 88 MET A SD 1 ATOM 633 C CE . MET A 1 82 ? -16.957 -2.871 29.210 1.00 22.75 ? 88 MET A CE 1 ATOM 634 N N . GLU A 1 83 ? -20.727 0.876 32.264 1.00 16.77 ? 89 GLU A N 1 ATOM 635 C CA . GLU A 1 83 ? -21.502 0.576 33.463 1.00 17.20 ? 89 GLU A CA 1 ATOM 636 C C . GLU A 1 83 ? -22.658 -0.344 33.070 1.00 18.33 ? 89 GLU A C 1 ATOM 637 O O . GLU A 1 83 ? -23.266 -0.124 32.029 1.00 18.68 ? 89 GLU A O 1 ATOM 638 C CB . GLU A 1 83 ? -22.043 1.859 34.125 1.00 17.41 ? 89 GLU A CB 1 ATOM 639 C CG . GLU A 1 83 ? -22.609 1.571 35.554 1.00 18.36 ? 89 GLU A CG 1 ATOM 640 C CD . GLU A 1 83 ? -23.298 2.764 36.211 1.00 19.44 ? 89 GLU A CD 1 ATOM 641 O OE1 . GLU A 1 83 ? -24.039 3.491 35.508 1.00 20.34 ? 89 GLU A OE1 1 ATOM 642 O OE2 . GLU A 1 83 ? -23.135 2.954 37.455 1.00 19.27 ? 89 GLU A OE2 1 ATOM 643 N N . LYS A 1 84 ? -22.953 -1.344 33.893 1.00 18.70 ? 90 LYS A N 1 ATOM 644 C CA . LYS A 1 84 ? -24.108 -2.212 33.628 1.00 20.13 ? 90 LYS A CA 1 ATOM 645 C C . LYS A 1 84 ? -25.416 -1.492 33.932 1.00 21.57 ? 90 LYS A C 1 ATOM 646 O O . LYS A 1 84 ? -25.429 -0.469 34.590 1.00 21.19 ? 90 LYS A O 1 ATOM 647 C CB . LYS A 1 84 ? -24.017 -3.527 34.399 1.00 19.79 ? 90 LYS A CB 1 ATOM 648 C CG . LYS A 1 84 ? -22.838 -4.409 33.955 1.00 20.29 ? 90 LYS A CG 1 ATOM 649 C CD . LYS A 1 84 ? -22.851 -5.745 34.630 1.00 21.70 ? 90 LYS A CD 1 ATOM 650 C CE . LYS A 1 84 ? -21.662 -6.565 34.151 1.00 24.77 ? 90 LYS A CE 1 ATOM 651 N NZ . LYS A 1 84 ? -21.587 -7.859 34.923 1.00 28.26 ? 90 LYS A NZ 1 ATOM 652 N N . GLU A 1 85 ? -26.517 -2.041 33.424 1.00 23.62 ? 91 GLU A N 1 ATOM 653 C CA . GLU A 1 85 ? -27.820 -1.413 33.604 1.00 25.20 ? 91 GLU A CA 1 ATOM 654 C C . GLU A 1 85 ? -28.212 -1.412 35.075 1.00 24.53 ? 91 GLU A C 1 ATOM 655 O O . GLU A 1 85 ? -28.727 -0.412 35.582 1.00 25.86 ? 91 GLU A O 1 ATOM 656 C CB . GLU A 1 85 ? -28.873 -2.142 32.750 1.00 25.91 ? 91 GLU A CB 1 ATOM 657 C CG . GLU A 1 85 ? -30.308 -1.614 32.916 1.00 31.11 ? 91 GLU A CG 1 ATOM 658 C CD . GLU A 1 85 ? -30.500 -0.150 32.501 1.00 38.27 ? 91 GLU A CD 1 ATOM 659 O OE1 . GLU A 1 85 ? -29.684 0.409 31.726 1.00 40.17 ? 91 GLU A OE1 1 ATOM 660 O OE2 . GLU A 1 85 ? -31.517 0.444 32.946 1.00 43.00 ? 91 GLU A OE2 1 ATOM 661 N N . ASN A 1 86 ? -27.933 -2.521 35.761 1.00 24.17 ? 92 ASN A N 1 ATOM 662 C CA . ASN A 1 86 ? -28.293 -2.688 37.162 1.00 24.41 ? 92 ASN A CA 1 ATOM 663 C C . ASN A 1 86 ? -27.137 -3.313 37.925 1.00 23.36 ? 92 ASN A C 1 ATOM 664 O O . ASN A 1 86 ? -27.204 -4.477 38.283 1.00 21.99 ? 92 ASN A O 1 ATOM 665 C CB . ASN A 1 86 ? -29.537 -3.591 37.265 1.00 26.44 ? 92 ASN A CB 1 ATOM 666 C CG . ASN A 1 86 ? -30.754 -2.982 36.572 1.00 29.39 ? 92 ASN A CG 1 ATOM 667 O OD1 . ASN A 1 86 ? -31.358 -3.600 35.670 1.00 37.28 ? 92 ASN A OD1 1 ATOM 668 N ND2 . ASN A 1 86 ? -31.107 -1.768 36.971 1.00 33.85 ? 92 ASN A ND2 1 ATOM 669 N N . PRO A 1 87 ? -26.050 -2.545 38.155 1.00 21.75 ? 93 PRO A N 1 ATOM 670 C CA . PRO A 1 87 ? -24.876 -3.125 38.784 1.00 20.83 ? 93 PRO A CA 1 ATOM 671 C C . PRO A 1 87 ? -25.214 -3.600 40.190 1.00 21.04 ? 93 PRO A C 1 ATOM 672 O O . PRO A 1 87 ? -25.919 -2.911 40.942 1.00 21.26 ? 93 PRO A O 1 ATOM 673 C CB . PRO A 1 87 ? -23.887 -1.945 38.865 1.00 20.85 ? 93 PRO A CB 1 ATOM 674 C CG . PRO A 1 87 ? -24.376 -0.965 37.919 1.00 21.47 ? 93 PRO A CG 1 ATOM 675 C CD . PRO A 1 87 ? -25.865 -1.100 37.910 1.00 22.32 ? 93 PRO A CD 1 ATOM 676 N N . ARG A 1 88 ? -24.710 -4.781 40.519 1.00 20.36 ? 94 ARG A N 1 ATOM 677 C CA . ARG A 1 88 ? -24.932 -5.405 41.817 1.00 20.91 ? 94 ARG A CA 1 ATOM 678 C C . ARG A 1 88 ? -24.277 -4.687 42.999 1.00 20.96 ? 94 ARG A C 1 ATOM 679 O O . ARG A 1 88 ? -24.816 -4.696 44.106 1.00 21.73 ? 94 ARG A O 1 ATOM 680 C CB . ARG A 1 88 ? -24.402 -6.829 41.760 1.00 22.16 ? 94 ARG A CB 1 ATOM 681 C CG . ARG A 1 88 ? -24.717 -7.675 42.970 1.00 26.12 ? 94 ARG A CG 1 ATOM 682 C CD . ARG A 1 88 ? -24.226 -9.127 42.725 1.00 34.60 ? 94 ARG A CD 1 ATOM 683 N NE . ARG A 1 88 ? -24.737 -9.630 41.446 1.00 38.60 ? 94 ARG A NE 1 ATOM 684 C CZ . ARG A 1 88 ? -23.981 -9.947 40.395 1.00 40.93 ? 94 ARG A CZ 1 ATOM 685 N NH1 . ARG A 1 88 ? -22.656 -9.859 40.465 1.00 42.52 ? 94 ARG A NH1 1 ATOM 686 N NH2 . ARG A 1 88 ? -24.550 -10.379 39.277 1.00 41.77 ? 94 ARG A NH2 1 ATOM 687 N N . ASP A 1 89 ? -23.104 -4.086 42.758 1.00 19.56 ? 95 ASP A N 1 ATOM 688 C CA . ASP A 1 89 ? -22.249 -3.548 43.829 1.00 18.88 ? 95 ASP A CA 1 ATOM 689 C C . ASP A 1 89 ? -22.251 -2.027 43.833 1.00 18.66 ? 95 ASP A C 1 ATOM 690 O O . ASP A 1 89 ? -21.461 -1.374 43.151 1.00 18.24 ? 95 ASP A O 1 ATOM 691 C CB . ASP A 1 89 ? -20.848 -4.123 43.723 1.00 18.93 ? 95 ASP A CB 1 ATOM 692 C CG . ASP A 1 89 ? -20.875 -5.630 43.812 1.00 19.07 ? 95 ASP A CG 1 ATOM 693 O OD1 . ASP A 1 89 ? -21.479 -6.120 44.808 1.00 17.32 ? 95 ASP A OD1 1 ATOM 694 O OD2 . ASP A 1 89 ? -20.371 -6.314 42.860 1.00 20.91 ? 95 ASP A OD2 1 ATOM 695 N N . GLY A 1 90 A -23.158 -1.485 44.638 1.00 17.57 ? 95 GLY A N 1 ATOM 696 C CA . GLY A 1 90 A -23.314 -0.031 44.732 1.00 16.63 ? 95 GLY A CA 1 ATOM 697 C C . GLY A 1 90 A -23.254 0.341 46.203 1.00 16.55 ? 95 GLY A C 1 ATOM 698 O O . GLY A 1 90 A -22.216 0.259 46.843 1.00 16.03 ? 95 GLY A O 1 ATOM 699 N N . LEU A 1 91 ? -24.397 0.784 46.734 1.00 16.88 ? 96 LEU A N 1 ATOM 700 C CA . LEU A 1 91 ? -24.477 1.104 48.158 1.00 18.03 ? 96 LEU A CA 1 ATOM 701 C C . LEU A 1 91 ? -24.659 -0.191 48.961 1.00 17.91 ? 96 LEU A C 1 ATOM 702 O O . LEU A 1 91 ? -25.830 -0.596 49.219 1.00 18.88 ? 96 LEU A O 1 ATOM 703 C CB . LEU A 1 91 ? -25.687 2.033 48.379 1.00 18.87 ? 96 LEU A CB 1 ATOM 704 C CG . LEU A 1 91 ? -25.479 3.561 48.367 1.00 23.06 ? 96 LEU A CG 1 ATOM 705 C CD1 . LEU A 1 91 ? -24.454 4.102 47.437 1.00 24.05 ? 96 LEU A CD1 1 ATOM 706 C CD2 . LEU A 1 91 ? -26.838 4.290 48.171 1.00 22.01 ? 96 LEU A CD2 1 ATOM 707 N N . CYS A 1 92 ? -23.546 -0.815 49.392 1.00 16.85 ? 97 CYS A N 1 ATOM 708 C CA . CYS A 1 92 ? -23.671 -2.078 50.180 1.00 17.79 ? 97 CYS A CA 1 ATOM 709 C C . CYS A 1 92 ? -24.449 -1.822 51.459 1.00 17.07 ? 97 CYS A C 1 ATOM 710 O O . CYS A 1 92 ? -25.324 -2.613 51.837 1.00 17.95 ? 97 CYS A O 1 ATOM 711 C CB . CYS A 1 92 ? -22.303 -2.721 50.492 1.00 17.78 ? 97 CYS A CB 1 ATOM 712 S SG . CYS A 1 92 ? -21.016 -1.623 51.150 1.00 21.59 ? 97 CYS A SG 1 ATOM 713 N N . TYR A 1 93 ? -24.153 -0.688 52.093 1.00 16.34 ? 98 TYR A N 1 ATOM 714 C CA . TYR A 1 93 ? -24.964 -0.192 53.201 1.00 15.50 ? 98 TYR A CA 1 ATOM 715 C C . TYR A 1 93 ? -26.042 0.621 52.498 1.00 16.30 ? 98 TYR A C 1 ATOM 716 O O . TYR A 1 93 ? -25.693 1.571 51.793 1.00 16.69 ? 98 TYR A O 1 ATOM 717 C CB . TYR A 1 93 ? -24.154 0.722 54.154 1.00 15.41 ? 98 TYR A CB 1 ATOM 718 C CG . TYR A 1 93 ? -24.819 0.861 55.498 1.00 16.27 ? 98 TYR A CG 1 ATOM 719 C CD1 . TYR A 1 93 ? -24.317 0.211 56.622 1.00 16.79 ? 98 TYR A CD1 1 ATOM 720 C CD2 . TYR A 1 93 ? -26.009 1.621 55.644 1.00 14.67 ? 98 TYR A CD2 1 ATOM 721 C CE1 . TYR A 1 93 ? -24.949 0.292 57.843 1.00 16.07 ? 98 TYR A CE1 1 ATOM 722 C CE2 . TYR A 1 93 ? -26.656 1.715 56.905 1.00 14.50 ? 98 TYR A CE2 1 ATOM 723 C CZ . TYR A 1 93 ? -26.114 1.074 57.987 1.00 15.52 ? 98 TYR A CZ 1 ATOM 724 O OH . TYR A 1 93 ? -26.734 1.139 59.222 1.00 16.05 ? 98 TYR A OH 1 ATOM 725 N N . PRO A 1 94 ? -27.326 0.223 52.662 1.00 15.74 ? 99 PRO A N 1 ATOM 726 C CA . PRO A 1 94 ? -28.417 0.795 51.831 1.00 16.43 ? 99 PRO A CA 1 ATOM 727 C C . PRO A 1 94 ? -28.597 2.277 52.090 1.00 15.94 ? 99 PRO A C 1 ATOM 728 O O . PRO A 1 94 ? -28.267 2.765 53.166 1.00 15.04 ? 99 PRO A O 1 ATOM 729 C CB . PRO A 1 94 ? -29.674 0.025 52.282 1.00 17.13 ? 99 PRO A CB 1 ATOM 730 C CG . PRO A 1 94 ? -29.385 -0.392 53.704 1.00 16.49 ? 99 PRO A CG 1 ATOM 731 C CD . PRO A 1 94 ? -27.857 -0.744 53.651 1.00 15.89 ? 99 PRO A CD 1 ATOM 732 N N . GLY A 1 95 ? -29.105 2.977 51.084 1.00 15.93 ? 100 GLY A N 1 ATOM 733 C CA . GLY A 1 95 ? -29.443 4.384 51.286 1.00 17.28 ? 100 GLY A CA 1 ATOM 734 C C . GLY A 1 95 ? -29.679 5.093 49.997 1.00 16.77 ? 100 GLY A C 1 ATOM 735 O O . GLY A 1 95 ? -30.329 4.582 49.081 1.00 17.75 ? 100 GLY A O 1 ATOM 736 N N . SER A 1 96 ? -29.130 6.298 49.906 1.00 14.88 ? 101 SER A N 1 ATOM 737 C CA . SER A 1 96 ? -29.398 7.133 48.737 1.00 16.04 ? 101 SER A CA 1 ATOM 738 C C . SER A 1 96 ? -28.182 8.000 48.419 1.00 16.14 ? 101 SER A C 1 ATOM 739 O O . SER A 1 96 ? -27.274 8.108 49.231 1.00 15.26 ? 101 SER A O 1 ATOM 740 C CB . SER A 1 96 ? -30.624 8.006 48.998 1.00 16.99 ? 101 SER A CB 1 ATOM 741 O OG . SER A 1 96 ? -30.377 8.894 50.078 1.00 17.06 ? 101 SER A OG 1 ATOM 742 N N . PHE A 1 97 ? -28.178 8.601 47.225 1.00 15.16 ? 102 PHE A N 1 ATOM 743 C CA . PHE A 1 97 ? -27.032 9.402 46.781 1.00 14.76 ? 102 PHE A CA 1 ATOM 744 C C . PHE A 1 97 ? -27.644 10.627 46.143 1.00 16.20 ? 102 PHE A C 1 ATOM 745 O O . PHE A 1 97 ? -28.211 10.543 45.020 1.00 16.07 ? 102 PHE A O 1 ATOM 746 C CB . PHE A 1 97 ? -26.170 8.599 45.760 1.00 15.29 ? 102 PHE A CB 1 ATOM 747 C CG . PHE A 1 97 ? -24.743 9.078 45.659 1.00 16.69 ? 102 PHE A CG 1 ATOM 748 C CD1 . PHE A 1 97 ? -23.695 8.247 46.061 1.00 15.91 ? 102 PHE A CD1 1 ATOM 749 C CD2 . PHE A 1 97 ? -24.452 10.355 45.156 1.00 19.07 ? 102 PHE A CD2 1 ATOM 750 C CE1 . PHE A 1 97 ? -22.349 8.663 45.977 1.00 17.26 ? 102 PHE A CE1 1 ATOM 751 C CE2 . PHE A 1 97 ? -23.078 10.799 45.055 1.00 16.50 ? 102 PHE A CE2 1 ATOM 752 C CZ . PHE A 1 97 ? -22.019 9.916 45.477 1.00 17.12 ? 102 PHE A CZ 1 ATOM 753 N N . ASN A 1 98 ? -27.606 11.739 46.862 1.00 16.26 ? 103 ASN A N 1 ATOM 754 C CA . ASN A 1 98 ? -28.164 12.997 46.358 1.00 16.37 ? 103 ASN A CA 1 ATOM 755 C C . ASN A 1 98 ? -27.477 13.509 45.104 1.00 16.92 ? 103 ASN A C 1 ATOM 756 O O . ASN A 1 98 ? -26.241 13.466 45.022 1.00 16.80 ? 103 ASN A O 1 ATOM 757 C CB . ASN A 1 98 ? -28.091 14.071 47.439 1.00 17.07 ? 103 ASN A CB 1 ATOM 758 C CG . ASN A 1 98 ? -28.995 13.745 48.613 1.00 15.81 ? 103 ASN A CG 1 ATOM 759 O OD1 . ASN A 1 98 ? -30.184 13.398 48.412 1.00 18.47 ? 103 ASN A OD1 1 ATOM 760 N ND2 . ASN A 1 98 ? -28.475 13.880 49.826 1.00 16.47 ? 103 ASN A ND2 1 ATOM 761 N N . ASP A 1 99 ? -28.283 14.004 44.147 1.00 16.43 ? 104 ASP A N 1 ATOM 762 C CA . ASP A 1 99 ? -27.742 14.570 42.887 1.00 17.49 ? 104 ASP A CA 1 ATOM 763 C C . ASP A 1 99 ? -26.801 13.592 42.141 1.00 16.19 ? 104 ASP A C 1 ATOM 764 O O . ASP A 1 99 ? -25.763 13.963 41.552 1.00 18.02 ? 104 ASP A O 1 ATOM 765 C CB . ASP A 1 99 ? -27.027 15.902 43.136 1.00 17.05 ? 104 ASP A CB 1 ATOM 766 C CG . ASP A 1 99 ? -27.832 16.843 43.969 1.00 25.57 ? 104 ASP A CG 1 ATOM 767 O OD1 . ASP A 1 99 ? -28.882 17.285 43.500 1.00 28.25 ? 104 ASP A OD1 1 ATOM 768 O OD2 . ASP A 1 99 ? -27.372 17.158 45.084 1.00 29.45 ? 104 ASP A OD2 1 ATOM 769 N N . TYR A 1 100 ? -27.192 12.324 42.161 1.00 16.62 ? 105 TYR A N 1 ATOM 770 C CA . TYR A 1 100 ? -26.360 11.249 41.570 1.00 15.70 ? 105 TYR A CA 1 ATOM 771 C C . TYR A 1 100 ? -26.236 11.382 40.067 1.00 15.48 ? 105 TYR A C 1 ATOM 772 O O . TYR A 1 100 ? -25.169 11.215 39.502 1.00 14.19 ? 105 TYR A O 1 ATOM 773 C CB . TYR A 1 100 ? -27.008 9.909 41.896 1.00 14.52 ? 105 TYR A CB 1 ATOM 774 C CG . TYR A 1 100 ? -26.191 8.682 41.578 1.00 15.26 ? 105 TYR A CG 1 ATOM 775 C CD1 . TYR A 1 100 ? -24.792 8.622 41.848 1.00 16.06 ? 105 TYR A CD1 1 ATOM 776 C CD2 . TYR A 1 100 ? -26.804 7.560 41.035 1.00 16.30 ? 105 TYR A CD2 1 ATOM 777 C CE1 . TYR A 1 100 ? -24.042 7.466 41.549 1.00 16.08 ? 105 TYR A CE1 1 ATOM 778 C CE2 . TYR A 1 100 ? -26.064 6.401 40.743 1.00 16.64 ? 105 TYR A CE2 1 ATOM 779 C CZ . TYR A 1 100 ? -24.678 6.363 41.012 1.00 15.24 ? 105 TYR A CZ 1 ATOM 780 O OH . TYR A 1 100 ? -23.995 5.208 40.730 1.00 17.43 ? 105 TYR A OH 1 ATOM 781 N N . GLU A 1 101 ? -27.363 11.685 39.411 1.00 15.62 ? 106 GLU A N 1 ATOM 782 C CA . GLU A 1 101 ? -27.361 11.853 37.974 1.00 16.65 ? 106 GLU A CA 1 ATOM 783 C C . GLU A 1 101 ? -26.525 13.041 37.542 1.00 15.79 ? 106 GLU A C 1 ATOM 784 O O . GLU A 1 101 ? -25.834 13.000 36.531 1.00 15.55 ? 106 GLU A O 1 ATOM 785 C CB . GLU A 1 101 ? -28.785 11.938 37.448 1.00 17.76 ? 106 GLU A CB 1 ATOM 786 C CG . GLU A 1 101 ? -29.545 10.612 37.606 1.00 20.30 ? 106 GLU A CG 1 ATOM 787 C CD . GLU A 1 101 ? -29.980 10.317 39.032 1.00 20.56 ? 106 GLU A CD 1 ATOM 788 O OE1 . GLU A 1 101 ? -30.219 11.260 39.827 1.00 20.83 ? 106 GLU A OE1 1 ATOM 789 O OE2 . GLU A 1 101 ? -30.039 9.108 39.330 1.00 28.79 ? 106 GLU A OE2 1 ATOM 790 N N . GLU A 1 102 ? -26.546 14.101 38.351 1.00 15.85 ? 107 GLU A N 1 ATOM 791 C CA . GLU A 1 102 ? -25.621 15.224 38.127 1.00 16.04 ? 107 GLU A CA 1 ATOM 792 C C . GLU A 1 102 ? -24.144 14.838 38.215 1.00 15.87 ? 107 GLU A C 1 ATOM 793 O O . GLU A 1 102 ? -23.325 15.257 37.395 1.00 16.02 ? 107 GLU A O 1 ATOM 794 C CB . GLU A 1 102 ? -25.930 16.349 39.092 1.00 16.07 ? 107 GLU A CB 1 ATOM 795 C CG . GLU A 1 102 ? -27.182 17.148 38.652 1.00 15.61 ? 107 GLU A CG 1 ATOM 796 C CD . GLU A 1 102 ? -26.954 18.083 37.460 1.00 17.64 ? 107 GLU A CD 1 ATOM 797 O OE1 . GLU A 1 102 ? -26.008 18.864 37.473 1.00 18.31 ? 107 GLU A OE1 1 ATOM 798 O OE2 . GLU A 1 102 ? -27.768 18.056 36.507 1.00 17.69 ? 107 GLU A OE2 1 ATOM 799 N N . LEU A 1 103 ? -23.832 13.995 39.193 1.00 15.83 ? 108 LEU A N 1 ATOM 800 C CA . LEU A 1 103 ? -22.465 13.450 39.322 1.00 16.71 ? 108 LEU A CA 1 ATOM 801 C C . LEU A 1 103 ? -22.065 12.624 38.089 1.00 17.54 ? 108 LEU A C 1 ATOM 802 O O . LEU A 1 103 ? -20.965 12.821 37.532 1.00 17.11 ? 108 LEU A O 1 ATOM 803 C CB . LEU A 1 103 ? -22.344 12.607 40.606 1.00 17.04 ? 108 LEU A CB 1 ATOM 804 C CG . LEU A 1 103 ? -20.916 12.099 40.828 1.00 18.44 ? 108 LEU A CG 1 ATOM 805 C CD1 . LEU A 1 103 ? -19.909 13.214 40.720 1.00 22.98 ? 108 LEU A CD1 1 ATOM 806 C CD2 . LEU A 1 103 ? -20.908 11.439 42.210 1.00 20.84 ? 108 LEU A CD2 1 ATOM 807 N N . LYS A 1 104 ? -22.962 11.751 37.622 1.00 17.77 ? 109 LYS A N 1 ATOM 808 C CA . LYS A 1 104 ? -22.669 10.959 36.426 1.00 18.72 ? 109 LYS A CA 1 ATOM 809 C C . LYS A 1 104 ? -22.466 11.860 35.205 1.00 17.77 ? 109 LYS A C 1 ATOM 810 O O . LYS A 1 104 ? -21.614 11.599 34.331 1.00 19.09 ? 109 LYS A O 1 ATOM 811 C CB . LYS A 1 104 ? -23.799 9.951 36.186 1.00 17.78 ? 109 LYS A CB 1 ATOM 812 C CG . LYS A 1 104 ? -23.933 8.923 37.347 1.00 17.87 ? 109 LYS A CG 1 ATOM 813 C CD . LYS A 1 104 ? -25.080 7.931 37.120 1.00 23.00 ? 109 LYS A CD 1 ATOM 814 C CE . LYS A 1 104 ? -24.538 6.575 36.772 1.00 26.99 ? 109 LYS A CE 1 ATOM 815 N NZ . LYS A 1 104 ? -25.683 5.594 36.638 1.00 26.02 ? 109 LYS A NZ 1 ATOM 816 N N . HIS A 1 105 ? -23.256 12.932 35.118 1.00 17.72 ? 110 HIS A N 1 ATOM 817 C CA . HIS A 1 105 ? -23.091 13.867 34.026 1.00 18.43 ? 110 HIS A CA 1 ATOM 818 C C . HIS A 1 105 ? -21.702 14.531 34.068 1.00 18.49 ? 110 HIS A C 1 ATOM 819 O O . HIS A 1 105 ? -21.060 14.710 33.024 1.00 18.70 ? 110 HIS A O 1 ATOM 820 C CB . HIS A 1 105 ? -24.206 14.921 34.026 1.00 19.91 ? 110 HIS A CB 1 ATOM 821 C CG . HIS A 1 105 ? -24.058 15.903 32.930 1.00 19.57 ? 110 HIS A CG 1 ATOM 822 N ND1 . HIS A 1 105 ? -24.253 15.570 31.604 1.00 21.06 ? 110 HIS A ND1 1 ATOM 823 C CD2 . HIS A 1 105 ? -23.634 17.182 32.949 1.00 20.62 ? 110 HIS A CD2 1 ATOM 824 C CE1 . HIS A 1 105 ? -24.032 16.643 30.863 1.00 22.83 ? 110 HIS A CE1 1 ATOM 825 N NE2 . HIS A 1 105 ? -23.642 17.627 31.653 1.00 23.46 ? 110 HIS A NE2 1 ATOM 826 N N . LEU A 1 106 ? -21.259 14.929 35.260 1.00 18.36 ? 111 LEU A N 1 ATOM 827 C CA . LEU A 1 106 ? -19.900 15.432 35.410 1.00 20.35 ? 111 LEU A CA 1 ATOM 828 C C . LEU A 1 106 ? -18.879 14.476 34.796 1.00 21.21 ? 111 LEU A C 1 ATOM 829 O O . LEU A 1 106 ? -17.957 14.899 34.089 1.00 20.53 ? 111 LEU A O 1 ATOM 830 C CB . LEU A 1 106 ? -19.579 15.742 36.876 1.00 20.28 ? 111 LEU A CB 1 ATOM 831 C CG . LEU A 1 106 ? -18.083 16.035 37.059 1.00 21.19 ? 111 LEU A CG 1 ATOM 832 C CD1 . LEU A 1 106 ? -17.707 17.347 36.381 1.00 22.80 ? 111 LEU A CD1 1 ATOM 833 C CD2 . LEU A 1 106 ? -17.711 16.057 38.501 1.00 23.81 ? 111 LEU A CD2 1 ATOM 834 N N . LEU A 1 107 ? -19.060 13.189 35.050 1.00 22.38 ? 112 LEU A N 1 ATOM 835 C CA . LEU A 1 107 ? -18.112 12.183 34.564 1.00 24.63 ? 112 LEU A CA 1 ATOM 836 C C . LEU A 1 107 ? -17.975 12.118 33.048 1.00 26.45 ? 112 LEU A C 1 ATOM 837 O O . LEU A 1 107 ? -16.918 11.706 32.553 1.00 27.73 ? 112 LEU A O 1 ATOM 838 C CB . LEU A 1 107 ? -18.440 10.809 35.149 1.00 25.96 ? 112 LEU A CB 1 ATOM 839 C CG . LEU A 1 107 ? -18.302 10.756 36.662 1.00 26.36 ? 112 LEU A CG 1 ATOM 840 C CD1 . LEU A 1 107 ? -18.679 9.385 37.157 1.00 27.60 ? 112 LEU A CD1 1 ATOM 841 C CD2 . LEU A 1 107 ? -16.889 11.115 37.122 1.00 31.85 ? 112 LEU A CD2 1 ATOM 842 N N . SER A 1 108 ? -18.992 12.569 32.301 1.00 25.79 ? 113 SER A N 1 ATOM 843 C CA . SER A 1 108 ? -18.882 12.707 30.821 1.00 27.49 ? 113 SER A CA 1 ATOM 844 C C . SER A 1 108 ? -17.775 13.586 30.322 1.00 26.96 ? 113 SER A C 1 ATOM 845 O O . SER A 1 108 ? -17.440 13.545 29.127 1.00 28.08 ? 113 SER A O 1 ATOM 846 C CB . SER A 1 108 ? -20.183 13.252 30.224 1.00 29.14 ? 113 SER A CB 1 ATOM 847 O OG . SER A 1 108 ? -21.150 12.256 30.347 1.00 30.37 ? 113 SER A OG 1 ATOM 848 N N . SER A 1 109 ? -17.224 14.424 31.199 1.00 25.05 ? 114 SER A N 1 ATOM 849 C CA . SER A 1 109 ? -16.188 15.371 30.787 1.00 24.38 ? 114 SER A CA 1 ATOM 850 C C . SER A 1 109 ? -14.914 15.163 31.616 1.00 23.26 ? 114 SER A C 1 ATOM 851 O O . SER A 1 109 ? -14.037 16.024 31.624 1.00 23.76 ? 114 SER A O 1 ATOM 852 C CB . SER A 1 109 ? -16.698 16.817 30.826 1.00 26.50 ? 114 SER A CB 1 ATOM 853 O OG . SER A 1 109 ? -17.170 17.208 32.111 1.00 27.76 ? 114 SER A OG 1 ATOM 854 N N . VAL A 1 110 ? -14.866 14.048 32.345 1.00 21.75 ? 115 VAL A N 1 ATOM 855 C CA . VAL A 1 110 ? -13.684 13.694 33.169 1.00 20.90 ? 115 VAL A CA 1 ATOM 856 C C . VAL A 1 110 ? -13.098 12.381 32.636 1.00 20.69 ? 115 VAL A C 1 ATOM 857 O O . VAL A 1 110 ? -13.831 11.405 32.394 1.00 20.49 ? 115 VAL A O 1 ATOM 858 C CB . VAL A 1 110 ? -14.045 13.536 34.674 1.00 21.44 ? 115 VAL A CB 1 ATOM 859 C CG1 . VAL A 1 110 ? -12.830 12.971 35.487 1.00 20.39 ? 115 VAL A CG1 1 ATOM 860 C CG2 . VAL A 1 110 ? -14.591 14.857 35.262 1.00 21.72 ? 115 VAL A CG2 1 ATOM 861 N N . LYS A 1 111 ? -11.773 12.368 32.473 1.00 19.52 ? 116 LYS A N 1 ATOM 862 C CA . LYS A 1 111 ? -11.062 11.230 31.906 1.00 19.86 ? 116 LYS A CA 1 ATOM 863 C C . LYS A 1 111 ? -10.082 10.650 32.913 1.00 18.68 ? 116 LYS A C 1 ATOM 864 O O . LYS A 1 111 ? -9.588 9.571 32.692 1.00 18.38 ? 116 LYS A O 1 ATOM 865 C CB . LYS A 1 111 ? -10.293 11.607 30.646 1.00 20.72 ? 116 LYS A CB 1 ATOM 866 C CG . LYS A 1 111 ? -11.200 11.862 29.451 1.00 25.27 ? 116 LYS A CG 1 ATOM 867 C CD . LYS A 1 111 ? -10.334 12.418 28.336 1.00 30.15 ? 116 LYS A CD 1 ATOM 868 C CE . LYS A 1 111 ? -11.012 12.184 26.997 1.00 34.36 ? 116 LYS A CE 1 ATOM 869 N NZ . LYS A 1 111 ? -10.262 12.872 25.939 1.00 36.26 ? 116 LYS A NZ 1 ATOM 870 N N . HIS A 1 112 A -9.831 11.352 34.019 1.00 17.34 ? 116 HIS A N 1 ATOM 871 C CA . HIS A 1 112 A -9.002 10.758 35.078 1.00 16.10 ? 116 HIS A CA 1 ATOM 872 C C . HIS A 1 112 A -9.178 11.490 36.391 1.00 15.76 ? 116 HIS A C 1 ATOM 873 O O . HIS A 1 112 A -9.461 12.697 36.409 1.00 17.29 ? 116 HIS A O 1 ATOM 874 C CB . HIS A 1 112 A -7.507 10.788 34.674 1.00 16.49 ? 116 HIS A CB 1 ATOM 875 C CG . HIS A 1 112 A -6.617 9.920 35.522 1.00 16.25 ? 116 HIS A CG 1 ATOM 876 N ND1 . HIS A 1 112 A -5.393 10.352 35.994 1.00 19.72 ? 116 HIS A ND1 1 ATOM 877 C CD2 . HIS A 1 112 A -6.760 8.645 35.963 1.00 18.73 ? 116 HIS A CD2 1 ATOM 878 C CE1 . HIS A 1 112 A -4.819 9.375 36.682 1.00 20.58 ? 116 HIS A CE1 1 ATOM 879 N NE2 . HIS A 1 112 A -5.632 8.330 36.691 1.00 19.75 ? 116 HIS A NE2 1 ATOM 880 N N . PHE A 1 113 B -9.043 10.730 37.480 1.00 16.63 ? 116 PHE A N 1 ATOM 881 C CA . PHE A 1 113 B -8.959 11.274 38.852 1.00 16.26 ? 116 PHE A CA 1 ATOM 882 C C . PHE A 1 113 B -7.623 10.895 39.454 1.00 17.33 ? 116 PHE A C 1 ATOM 883 O O . PHE A 1 113 B -7.051 9.850 39.134 1.00 17.90 ? 116 PHE A O 1 ATOM 884 C CB . PHE A 1 113 B -10.015 10.618 39.769 1.00 17.08 ? 116 PHE A CB 1 ATOM 885 C CG . PHE A 1 113 B -11.424 11.068 39.526 1.00 16.57 ? 116 PHE A CG 1 ATOM 886 C CD1 . PHE A 1 113 B -11.770 12.429 39.518 1.00 17.81 ? 116 PHE A CD1 1 ATOM 887 C CD2 . PHE A 1 113 B -12.430 10.115 39.353 1.00 17.27 ? 116 PHE A CD2 1 ATOM 888 C CE1 . PHE A 1 113 B -13.084 12.846 39.315 1.00 16.21 ? 116 PHE A CE1 1 ATOM 889 C CE2 . PHE A 1 113 B -13.769 10.513 39.128 1.00 18.58 ? 116 PHE A CE2 1 ATOM 890 C CZ . PHE A 1 113 B -14.100 11.888 39.132 1.00 19.40 ? 116 PHE A CZ 1 ATOM 891 N N . GLU A 1 114 C -7.136 11.725 40.371 1.00 17.04 ? 116 GLU A N 1 ATOM 892 C CA . GLU A 1 114 C -6.098 11.305 41.319 1.00 17.05 ? 116 GLU A CA 1 ATOM 893 C C . GLU A 1 114 C -6.771 11.305 42.679 1.00 18.15 ? 116 GLU A C 1 ATOM 894 O O . GLU A 1 114 C -7.268 12.340 43.132 1.00 16.62 ? 116 GLU A O 1 ATOM 895 C CB . GLU A 1 114 C -4.940 12.306 41.307 1.00 19.20 ? 116 GLU A CB 1 ATOM 896 C CG . GLU A 1 114 C -4.093 12.189 40.050 1.00 24.18 ? 116 GLU A CG 1 ATOM 897 C CD . GLU A 1 114 C -2.997 13.252 39.984 1.00 30.63 ? 116 GLU A CD 1 ATOM 898 O OE1 . GLU A 1 114 C -2.640 13.832 41.040 1.00 30.39 ? 116 GLU A OE1 1 ATOM 899 O OE2 . GLU A 1 114 C -2.467 13.495 38.871 1.00 35.94 ? 116 GLU A OE2 1 ATOM 900 N N . LYS A 1 115 ? -6.858 10.133 43.307 1.00 17.56 ? 117 LYS A N 1 ATOM 901 C CA . LYS A 1 115 ? -7.457 10.045 44.626 1.00 19.56 ? 117 LYS A CA 1 ATOM 902 C C . LYS A 1 115 ? -6.447 10.522 45.660 1.00 19.40 ? 117 LYS A C 1 ATOM 903 O O . LYS A 1 115 ? -5.311 10.026 45.717 1.00 20.59 ? 117 LYS A O 1 ATOM 904 C CB . LYS A 1 115 ? -8.003 8.613 44.877 1.00 19.82 ? 117 LYS A CB 1 ATOM 905 C CG . LYS A 1 115 ? -8.919 8.481 46.111 1.00 20.65 ? 117 LYS A CG 1 ATOM 906 C CD . LYS A 1 115 ? -9.567 7.075 46.224 1.00 21.05 ? 117 LYS A CD 1 ATOM 907 C CE . LYS A 1 115 ? -8.563 6.029 46.687 1.00 22.36 ? 117 LYS A CE 1 ATOM 908 N NZ . LYS A 1 115 ? -9.214 4.694 46.852 1.00 17.95 ? 117 LYS A NZ 1 ATOM 909 N N . VAL A 1 116 ? -6.836 11.515 46.444 1.00 17.95 ? 118 VAL A N 1 ATOM 910 C CA . VAL A 1 116 ? -5.945 12.222 47.379 1.00 18.45 ? 118 VAL A CA 1 ATOM 911 C C . VAL A 1 116 ? -6.452 11.960 48.791 1.00 18.44 ? 118 VAL A C 1 ATOM 912 O O . VAL A 1 116 ? -7.645 12.104 49.050 1.00 17.30 ? 118 VAL A O 1 ATOM 913 C CB . VAL A 1 116 ? -5.953 13.755 47.092 1.00 19.51 ? 118 VAL A CB 1 ATOM 914 C CG1 . VAL A 1 116 ? -5.245 14.574 48.180 1.00 21.70 ? 118 VAL A CG1 1 ATOM 915 C CG2 . VAL A 1 116 ? -5.368 14.051 45.732 1.00 21.75 ? 118 VAL A CG2 1 ATOM 916 N N . LYS A 1 117 ? -5.546 11.584 49.703 1.00 16.73 ? 119 LYS A N 1 ATOM 917 C CA . LYS A 1 117 ? -5.998 11.311 51.082 1.00 17.02 ? 119 LYS A CA 1 ATOM 918 C C . LYS A 1 117 ? -6.127 12.618 51.848 1.00 17.48 ? 119 LYS A C 1 ATOM 919 O O . LYS A 1 117 ? -5.192 13.068 52.572 1.00 20.83 ? 119 LYS A O 1 ATOM 920 C CB . LYS A 1 117 ? -5.074 10.276 51.790 1.00 16.18 ? 119 LYS A CB 1 ATOM 921 C CG . LYS A 1 117 ? -5.642 9.848 53.147 1.00 19.87 ? 119 LYS A CG 1 ATOM 922 C CD . LYS A 1 117 ? -4.701 8.981 53.975 1.00 19.09 ? 119 LYS A CD 1 ATOM 923 C CE . LYS A 1 117 ? -4.600 7.582 53.426 1.00 22.61 ? 119 LYS A CE 1 ATOM 924 N NZ . LYS A 1 117 ? -3.424 6.890 54.062 1.00 23.35 ? 119 LYS A NZ 1 ATOM 925 N N . ILE A 1 118 ? -7.303 13.229 51.738 1.00 17.49 ? 120 ILE A N 1 ATOM 926 C CA . ILE A 1 118 ? -7.525 14.571 52.237 1.00 18.19 ? 120 ILE A CA 1 ATOM 927 C C . ILE A 1 118 ? -7.736 14.645 53.740 1.00 18.53 ? 120 ILE A C 1 ATOM 928 O O . ILE A 1 118 ? -7.435 15.675 54.360 1.00 19.07 ? 120 ILE A O 1 ATOM 929 C CB . ILE A 1 118 ? -8.713 15.265 51.486 1.00 17.45 ? 120 ILE A CB 1 ATOM 930 C CG1 . ILE A 1 118 ? -10.006 14.485 51.721 1.00 18.35 ? 120 ILE A CG1 1 ATOM 931 C CG2 . ILE A 1 118 ? -8.380 15.393 49.997 1.00 20.06 ? 120 ILE A CG2 1 ATOM 932 C CD1 . ILE A 1 118 ? -11.324 15.232 51.305 1.00 20.01 ? 120 ILE A CD1 1 ATOM 933 N N . LEU A 1 119 ? -8.287 13.581 54.330 1.00 16.94 ? 121 LEU A N 1 ATOM 934 C CA . LEU A 1 119 ? -8.666 13.580 55.737 1.00 16.90 ? 121 LEU A CA 1 ATOM 935 C C . LEU A 1 119 ? -8.261 12.255 56.328 1.00 17.40 ? 121 LEU A C 1 ATOM 936 O O . LEU A 1 119 ? -9.072 11.393 56.583 1.00 16.53 ? 121 LEU A O 1 ATOM 937 C CB . LEU A 1 119 ? -10.168 13.832 55.943 1.00 17.47 ? 121 LEU A CB 1 ATOM 938 C CG . LEU A 1 119 ? -10.607 15.273 55.623 1.00 18.16 ? 121 LEU A CG 1 ATOM 939 C CD1 . LEU A 1 119 ? -12.121 15.236 55.526 1.00 20.88 ? 121 LEU A CD1 1 ATOM 940 C CD2 . LEU A 1 119 ? -10.170 16.248 56.702 1.00 20.64 ? 121 LEU A CD2 1 ATOM 941 N N . PRO A 1 120 ? -6.953 12.056 56.496 1.00 18.10 ? 122 PRO A N 1 ATOM 942 C CA . PRO A 1 120 ? -6.469 10.750 56.921 1.00 19.27 ? 122 PRO A CA 1 ATOM 943 C C . PRO A 1 120 ? -7.171 10.299 58.200 1.00 19.22 ? 122 PRO A C 1 ATOM 944 O O . PRO A 1 120 ? -7.323 11.082 59.141 1.00 20.71 ? 122 PRO A O 1 ATOM 945 C CB . PRO A 1 120 ? -4.987 10.981 57.192 1.00 19.18 ? 122 PRO A CB 1 ATOM 946 C CG . PRO A 1 120 ? -4.642 12.227 56.525 1.00 21.01 ? 122 PRO A CG 1 ATOM 947 C CD . PRO A 1 120 ? -5.883 13.032 56.261 1.00 18.97 ? 122 PRO A CD 1 ATOM 948 N N . LYS A 1 121 ? -7.618 9.049 58.186 1.00 20.27 ? 123 LYS A N 1 ATOM 949 C CA . LYS A 1 121 ? -8.435 8.430 59.233 1.00 24.05 ? 123 LYS A CA 1 ATOM 950 C C . LYS A 1 121 ? -7.798 8.497 60.616 1.00 24.74 ? 123 LYS A C 1 ATOM 951 O O . LYS A 1 121 ? -8.481 8.662 61.643 1.00 25.27 ? 123 LYS A O 1 ATOM 952 C CB . LYS A 1 121 ? -8.666 6.956 58.835 1.00 24.75 ? 123 LYS A CB 1 ATOM 953 C CG . LYS A 1 121 ? -9.723 6.212 59.604 1.00 28.31 ? 123 LYS A CG 1 ATOM 954 C CD . LYS A 1 121 ? -10.399 5.121 58.731 1.00 30.55 ? 123 LYS A CD 1 ATOM 955 C CE . LYS A 1 121 ? -9.427 4.166 58.058 1.00 30.64 ? 123 LYS A CE 1 ATOM 956 N NZ . LYS A 1 121 ? -10.159 3.121 57.262 1.00 28.54 ? 123 LYS A NZ 1 ATOM 957 N N . ASP A 1 122 ? -6.472 8.388 60.645 1.00 26.32 ? 125 ASP A N 1 ATOM 958 C CA . ASP A 1 122 ? -5.745 8.393 61.915 1.00 28.06 ? 125 ASP A CA 1 ATOM 959 C C . ASP A 1 122 ? -5.785 9.719 62.696 1.00 28.30 ? 125 ASP A C 1 ATOM 960 O O . ASP A 1 122 ? -5.411 9.746 63.875 1.00 29.34 ? 125 ASP A O 1 ATOM 961 C CB . ASP A 1 122 ? -4.304 7.857 61.704 1.00 28.46 ? 125 ASP A CB 1 ATOM 962 C CG . ASP A 1 122 ? -3.391 8.837 60.956 1.00 30.98 ? 125 ASP A CG 1 ATOM 963 O OD1 . ASP A 1 122 ? -3.843 9.897 60.505 1.00 34.15 ? 125 ASP A OD1 1 ATOM 964 O OD2 . ASP A 1 122 ? -2.175 8.559 60.834 1.00 33.28 ? 125 ASP A OD2 1 ATOM 965 N N . ARG A 1 123 ? -6.234 10.808 62.055 1.00 27.29 ? 126 ARG A N 1 ATOM 966 C CA . ARG A 1 123 ? -6.307 12.135 62.673 1.00 27.88 ? 126 ARG A CA 1 ATOM 967 C C . ARG A 1 123 ? -7.595 12.356 63.475 1.00 27.64 ? 126 ARG A C 1 ATOM 968 O O . ARG A 1 123 ? -7.740 13.398 64.144 1.00 27.90 ? 126 ARG A O 1 ATOM 969 C CB . ARG A 1 123 ? -6.122 13.252 61.623 1.00 27.93 ? 126 ARG A CB 1 ATOM 970 C CG . ARG A 1 123 ? -4.674 13.428 61.069 1.00 29.00 ? 126 ARG A CG 1 ATOM 971 C CD . ARG A 1 123 ? -3.841 14.358 61.973 1.00 32.28 ? 126 ARG A CD 1 ATOM 972 N NE . ARG A 1 123 ? -2.430 14.371 61.576 1.00 36.08 ? 126 ARG A NE 1 ATOM 973 C CZ . ARG A 1 123 ? -1.476 15.074 62.180 1.00 36.62 ? 126 ARG A CZ 1 ATOM 974 N NH1 . ARG A 1 123 ? -1.758 15.837 63.232 1.00 39.97 ? 126 ARG A NH1 1 ATOM 975 N NH2 . ARG A 1 123 ? -0.230 15.005 61.735 1.00 37.23 ? 126 ARG A NH2 1 ATOM 976 N N . TRP A 1 124 ? -8.528 11.391 63.388 1.00 26.55 ? 127 TRP A N 1 ATOM 977 C CA . TRP A 1 124 ? -9.756 11.395 64.191 1.00 26.52 ? 127 TRP A CA 1 ATOM 978 C C . TRP A 1 124 ? -9.421 10.730 65.520 1.00 28.04 ? 127 TRP A C 1 ATOM 979 O O . TRP A 1 124 ? -9.805 9.576 65.781 1.00 28.24 ? 127 TRP A O 1 ATOM 980 C CB . TRP A 1 124 ? -10.884 10.598 63.507 1.00 24.37 ? 127 TRP A CB 1 ATOM 981 C CG . TRP A 1 124 ? -11.408 11.183 62.210 1.00 22.11 ? 127 TRP A CG 1 ATOM 982 C CD1 . TRP A 1 124 ? -11.352 10.603 60.948 1.00 20.98 ? 127 TRP A CD1 1 ATOM 983 C CD2 . TRP A 1 124 ? -12.141 12.412 62.049 1.00 21.22 ? 127 TRP A CD2 1 ATOM 984 N NE1 . TRP A 1 124 ? -11.960 11.430 60.033 1.00 17.09 ? 127 TRP A NE1 1 ATOM 985 C CE2 . TRP A 1 124 ? -12.464 12.533 60.675 1.00 19.02 ? 127 TRP A CE2 1 ATOM 986 C CE3 . TRP A 1 124 ? -12.547 13.434 62.934 1.00 19.31 ? 127 TRP A CE3 1 ATOM 987 C CZ2 . TRP A 1 124 ? -13.165 13.643 60.161 1.00 20.24 ? 127 TRP A CZ2 1 ATOM 988 C CZ3 . TRP A 1 124 ? -13.254 14.522 62.428 1.00 21.02 ? 127 TRP A CZ3 1 ATOM 989 C CH2 . TRP A 1 124 ? -13.566 14.623 61.056 1.00 22.08 ? 127 TRP A CH2 1 ATOM 990 N N . THR A 1 125 ? -8.662 11.452 66.344 1.00 29.92 ? 128 THR A N 1 ATOM 991 C CA . THR A 1 125 ? -8.122 10.865 67.556 1.00 30.98 ? 128 THR A CA 1 ATOM 992 C C . THR A 1 125 ? -9.156 10.806 68.682 1.00 31.47 ? 128 THR A C 1 ATOM 993 O O . THR A 1 125 ? -8.969 10.048 69.636 1.00 33.20 ? 128 THR A O 1 ATOM 994 C CB . THR A 1 125 ? -6.833 11.585 68.034 1.00 30.49 ? 128 THR A CB 1 ATOM 995 O OG1 . THR A 1 125 ? -7.096 12.987 68.216 1.00 32.02 ? 128 THR A OG1 1 ATOM 996 C CG2 . THR A 1 125 ? -5.716 11.397 67.021 1.00 31.63 ? 128 THR A CG2 1 ATOM 997 N N . GLN A 1 126 ? -10.234 11.587 68.574 1.00 31.05 ? 129 GLN A N 1 ATOM 998 C CA . GLN A 1 126 ? -11.260 11.620 69.619 1.00 30.54 ? 129 GLN A CA 1 ATOM 999 C C . GLN A 1 126 ? -12.475 10.718 69.321 1.00 29.26 ? 129 GLN A C 1 ATOM 1000 O O . GLN A 1 126 ? -13.453 10.740 70.066 1.00 28.48 ? 129 GLN A O 1 ATOM 1001 C CB . GLN A 1 126 ? -11.738 13.060 69.880 1.00 30.45 ? 129 GLN A CB 1 ATOM 1002 C CG . GLN A 1 126 ? -10.741 13.995 70.571 1.00 32.67 ? 129 GLN A CG 1 ATOM 1003 C CD . GLN A 1 126 ? -11.389 15.329 70.952 1.00 33.58 ? 129 GLN A CD 1 ATOM 1004 O OE1 . GLN A 1 126 ? -11.552 16.228 70.108 1.00 37.63 ? 129 GLN A OE1 1 ATOM 1005 N NE2 . GLN A 1 126 ? -11.781 15.458 72.229 1.00 37.16 ? 129 GLN A NE2 1 ATOM 1006 N N . HIS A 1 127 ? -12.416 9.943 68.236 1.00 28.08 ? 130 HIS A N 1 ATOM 1007 C CA . HIS A 1 127 ? -13.539 9.115 67.788 1.00 27.53 ? 130 HIS A CA 1 ATOM 1008 C C . HIS A 1 127 ? -13.034 7.766 67.305 1.00 27.37 ? 130 HIS A C 1 ATOM 1009 O O . HIS A 1 127 ? -11.881 7.639 66.879 1.00 27.62 ? 130 HIS A O 1 ATOM 1010 C CB . HIS A 1 127 ? -14.293 9.788 66.611 1.00 26.93 ? 130 HIS A CB 1 ATOM 1011 C CG . HIS A 1 127 ? -14.909 11.110 66.950 1.00 26.65 ? 130 HIS A CG 1 ATOM 1012 N ND1 . HIS A 1 127 ? -14.192 12.288 66.960 1.00 25.08 ? 130 HIS A ND1 1 ATOM 1013 C CD2 . HIS A 1 127 ? -16.173 11.437 67.311 1.00 26.61 ? 130 HIS A CD2 1 ATOM 1014 C CE1 . HIS A 1 127 ? -14.994 13.287 67.285 1.00 25.27 ? 130 HIS A CE1 1 ATOM 1015 N NE2 . HIS A 1 127 ? -16.202 12.796 67.504 1.00 25.51 ? 130 HIS A NE2 1 ATOM 1016 N N . THR A 1 128 ? -13.900 6.755 67.354 1.00 26.95 ? 131 THR A N 1 ATOM 1017 C CA . THR A 1 128 ? -13.619 5.440 66.794 1.00 26.72 ? 131 THR A CA 1 ATOM 1018 C C . THR A 1 128 ? -13.864 5.495 65.275 1.00 26.64 ? 131 THR A C 1 ATOM 1019 O O . THR A 1 128 ? -14.818 6.137 64.828 1.00 26.20 ? 131 THR A O 1 ATOM 1020 C CB . THR A 1 128 ? -14.532 4.390 67.457 1.00 27.82 ? 131 THR A CB 1 ATOM 1021 O OG1 . THR A 1 128 ? -14.279 4.379 68.877 1.00 29.41 ? 131 THR A OG1 1 ATOM 1022 C CG2 . THR A 1 128 ? -14.319 2.987 66.883 1.00 26.54 ? 131 THR A CG2 1 ATOM 1023 N N . THR A 1 129 ? -13.002 4.849 64.502 1.00 26.39 ? 132 THR A N 1 ATOM 1024 C CA . THR A 1 129 ? -13.091 4.900 63.028 1.00 26.46 ? 132 THR A CA 1 ATOM 1025 C C . THR A 1 129 ? -13.139 3.525 62.399 1.00 26.69 ? 132 THR A C 1 ATOM 1026 O O . THR A 1 129 ? -13.122 3.391 61.172 1.00 25.77 ? 132 THR A O 1 ATOM 1027 C CB . THR A 1 129 ? -11.906 5.674 62.411 1.00 26.66 ? 132 THR A CB 1 ATOM 1028 O OG1 . THR A 1 129 ? -10.670 5.026 62.769 1.00 27.14 ? 132 THR A OG1 1 ATOM 1029 C CG2 . THR A 1 129 ? -11.881 7.133 62.886 1.00 28.04 ? 132 THR A CG2 1 ATOM 1030 N N . THR A 1 130 ? -13.161 2.486 63.229 1.00 27.25 ? 133 THR A N 1 ATOM 1031 C CA . THR A 1 130 ? -13.080 1.119 62.727 1.00 27.88 ? 133 THR A CA 1 ATOM 1032 C C . THR A 1 130 ? -14.460 0.546 62.381 1.00 27.88 ? 133 THR A C 1 ATOM 1033 O O . THR A 1 130 ? -14.561 -0.604 61.953 1.00 28.11 ? 133 THR A O 1 ATOM 1034 C CB . THR A 1 130 ? -12.315 0.202 63.718 1.00 28.69 ? 133 THR A CB 1 ATOM 1035 O OG1 . THR A 1 130 ? -12.855 0.378 65.032 1.00 30.20 ? 133 THR A OG1 1 ATOM 1036 C CG2 . THR A 1 130 ? -10.847 0.563 63.730 1.00 28.55 ? 133 THR A CG2 1 ATOM 1037 N N . GLY A 1 131 ? -15.493 1.383 62.537 1.00 27.43 ? 134 GLY A N 1 ATOM 1038 C CA . GLY A 1 131 ? -16.901 1.043 62.293 1.00 25.81 ? 134 GLY A CA 1 ATOM 1039 C C . GLY A 1 131 ? -17.171 0.470 60.927 1.00 24.71 ? 134 GLY A C 1 ATOM 1040 O O . GLY A 1 131 ? -16.718 1.008 59.899 1.00 23.26 ? 134 GLY A O 1 ATOM 1041 N N . GLY A 1 132 ? -17.934 -0.629 60.941 1.00 24.27 ? 135 GLY A N 1 ATOM 1042 C CA . GLY A 1 132 ? -18.343 -1.323 59.727 1.00 21.69 ? 135 GLY A CA 1 ATOM 1043 C C . GLY A 1 132 ? -19.652 -2.053 59.915 1.00 20.69 ? 135 GLY A C 1 ATOM 1044 O O . GLY A 1 132 ? -20.316 -1.938 60.970 1.00 22.52 ? 135 GLY A O 1 ATOM 1045 N N . SER A 1 133 ? -20.049 -2.776 58.873 1.00 18.47 ? 136 SER A N 1 ATOM 1046 C CA . SER A 1 133 ? -21.315 -3.441 58.834 1.00 18.11 ? 136 SER A CA 1 ATOM 1047 C C . SER A 1 133 ? -21.229 -4.789 58.109 1.00 17.26 ? 136 SER A C 1 ATOM 1048 O O . SER A 1 133 ? -20.490 -4.970 57.139 1.00 16.26 ? 136 SER A O 1 ATOM 1049 C CB . SER A 1 133 ? -22.328 -2.549 58.099 1.00 17.24 ? 136 SER A CB 1 ATOM 1050 O OG . SER A 1 133 ? -23.521 -3.254 57.901 1.00 17.82 ? 136 SER A OG 1 ATOM 1051 N N . ARG A 1 134 ? -22.028 -5.742 58.573 1.00 17.82 ? 137 ARG A N 1 ATOM 1052 C CA . ARG A 1 134 ? -22.169 -6.982 57.867 1.00 19.50 ? 137 ARG A CA 1 ATOM 1053 C C . ARG A 1 134 ? -22.696 -6.819 56.440 1.00 18.56 ? 137 ARG A C 1 ATOM 1054 O O . ARG A 1 134 ? -22.469 -7.690 55.601 1.00 19.12 ? 137 ARG A O 1 ATOM 1055 C CB . ARG A 1 134 ? -23.049 -7.947 58.676 1.00 20.79 ? 137 ARG A CB 1 ATOM 1056 C CG . ARG A 1 134 ? -22.346 -8.341 59.965 1.00 27.98 ? 137 ARG A CG 1 ATOM 1057 C CD . ARG A 1 134 ? -22.762 -9.727 60.486 1.00 35.87 ? 137 ARG A CD 1 ATOM 1058 N NE . ARG A 1 134 ? -22.526 -10.830 59.542 1.00 41.21 ? 137 ARG A NE 1 ATOM 1059 C CZ . ARG A 1 134 ? -21.474 -10.997 58.727 1.00 43.37 ? 137 ARG A CZ 1 ATOM 1060 N NH1 . ARG A 1 134 ? -20.440 -10.147 58.688 1.00 42.04 ? 137 ARG A NH1 1 ATOM 1061 N NH2 . ARG A 1 134 ? -21.461 -12.064 57.940 1.00 43.76 ? 137 ARG A NH2 1 ATOM 1062 N N . ALA A 1 135 ? -23.380 -5.702 56.166 1.00 17.52 ? 138 ALA A N 1 ATOM 1063 C CA . ALA A 1 135 ? -23.883 -5.432 54.820 1.00 17.71 ? 138 ALA A CA 1 ATOM 1064 C C . ALA A 1 135 ? -22.736 -5.145 53.835 1.00 17.42 ? 138 ALA A C 1 ATOM 1065 O O . ALA A 1 135 ? -22.941 -5.243 52.614 1.00 18.60 ? 138 ALA A O 1 ATOM 1066 C CB . ALA A 1 135 ? -24.857 -4.253 54.842 1.00 17.56 ? 138 ALA A CB 1 ATOM 1067 N N . CYS A 1 136 ? -21.564 -4.765 54.366 1.00 17.01 ? 139 CYS A N 1 ATOM 1068 C CA . CYS A 1 136 ? -20.373 -4.508 53.542 1.00 16.98 ? 139 CYS A CA 1 ATOM 1069 C C . CYS A 1 136 ? -19.267 -5.454 53.982 1.00 18.28 ? 139 CYS A C 1 ATOM 1070 O O . CYS A 1 136 ? -18.113 -5.025 54.125 1.00 18.17 ? 139 CYS A O 1 ATOM 1071 C CB . CYS A 1 136 ? -19.846 -3.103 53.750 1.00 17.54 ? 139 CYS A CB 1 ATOM 1072 S SG . CYS A 1 136 ? -21.137 -1.819 53.323 1.00 21.72 ? 139 CYS A SG 1 ATOM 1073 N N . ALA A 1 137 ? -19.618 -6.712 54.235 1.00 19.02 ? 140 ALA A N 1 ATOM 1074 C CA . ALA A 1 137 ? -18.633 -7.608 54.884 1.00 19.55 ? 140 ALA A CA 1 ATOM 1075 C C . ALA A 1 137 ? -17.538 -8.039 53.924 1.00 20.08 ? 140 ALA A C 1 ATOM 1076 O O . ALA A 1 137 ? -17.728 -8.049 52.704 1.00 20.94 ? 140 ALA A O 1 ATOM 1077 C CB . ALA A 1 137 ? -19.308 -8.830 55.495 1.00 20.54 ? 140 ALA A CB 1 ATOM 1078 N N . VAL A 1 138 ? -16.392 -8.393 54.493 1.00 20.27 ? 141 VAL A N 1 ATOM 1079 C CA . VAL A 1 138 ? -15.247 -8.864 53.725 1.00 20.69 ? 141 VAL A CA 1 ATOM 1080 C C . VAL A 1 138 ? -14.718 -10.051 54.523 1.00 20.87 ? 141 VAL A C 1 ATOM 1081 O O . VAL A 1 138 ? -14.371 -9.898 55.698 1.00 19.72 ? 141 VAL A O 1 ATOM 1082 C CB . VAL A 1 138 ? -14.182 -7.763 53.655 1.00 20.66 ? 141 VAL A CB 1 ATOM 1083 C CG1 . VAL A 1 138 ? -12.843 -8.277 53.105 1.00 24.01 ? 141 VAL A CG1 1 ATOM 1084 C CG2 . VAL A 1 138 ? -14.712 -6.575 52.816 1.00 20.74 ? 141 VAL A CG2 1 ATOM 1085 N N . SER A 1 139 ? -14.666 -11.217 53.872 1.00 22.56 ? 142 SER A N 1 ATOM 1086 C CA . SER A 1 139 ? -14.192 -12.444 54.518 1.00 23.50 ? 142 SER A CA 1 ATOM 1087 C C . SER A 1 139 ? -14.936 -12.744 55.807 1.00 24.07 ? 142 SER A C 1 ATOM 1088 O O . SER A 1 139 ? -14.327 -13.097 56.823 1.00 24.97 ? 142 SER A O 1 ATOM 1089 C CB . SER A 1 139 ? -12.692 -12.336 54.789 1.00 24.64 ? 142 SER A CB 1 ATOM 1090 O OG . SER A 1 139 ? -12.022 -12.191 53.566 1.00 24.28 ? 142 SER A OG 1 ATOM 1091 N N . GLY A 1 140 ? -16.253 -12.569 55.775 1.00 23.59 ? 143 GLY A N 1 ATOM 1092 C CA . GLY A 1 140 ? -17.060 -12.924 56.923 1.00 24.66 ? 143 GLY A CA 1 ATOM 1093 C C . GLY A 1 140 ? -17.076 -11.933 58.062 1.00 23.55 ? 143 GLY A C 1 ATOM 1094 O O . GLY A 1 140 ? -17.761 -12.179 59.076 1.00 25.09 ? 143 GLY A O 1 ATOM 1095 N N . ASN A 1 141 ? -16.346 -10.820 57.943 1.00 22.24 ? 144 ASN A N 1 ATOM 1096 C CA . ASN A 1 141 ? -16.401 -9.850 59.028 1.00 21.11 ? 144 ASN A CA 1 ATOM 1097 C C . ASN A 1 141 ? -16.936 -8.521 58.549 1.00 19.26 ? 144 ASN A C 1 ATOM 1098 O O . ASN A 1 141 ? -16.764 -8.196 57.386 1.00 18.14 ? 144 ASN A O 1 ATOM 1099 C CB . ASN A 1 141 ? -15.075 -9.646 59.702 1.00 21.74 ? 144 ASN A CB 1 ATOM 1100 C CG . ASN A 1 141 ? -14.661 -10.865 60.506 1.00 25.52 ? 144 ASN A CG 1 ATOM 1101 O OD1 . ASN A 1 141 ? -13.880 -11.661 60.016 1.00 29.37 ? 144 ASN A OD1 1 ATOM 1102 N ND2 . ASN A 1 141 ? -15.235 -11.043 61.708 1.00 28.89 ? 144 ASN A ND2 1 ATOM 1103 N N . PRO A 1 142 ? -17.592 -7.785 59.451 1.00 18.17 ? 145 PRO A N 1 ATOM 1104 C CA . PRO A 1 142 ? -18.069 -6.435 59.093 1.00 16.91 ? 145 PRO A CA 1 ATOM 1105 C C . PRO A 1 142 ? -16.947 -5.556 58.516 1.00 16.42 ? 145 PRO A C 1 ATOM 1106 O O . PRO A 1 142 ? -15.796 -5.589 58.994 1.00 18.10 ? 145 PRO A O 1 ATOM 1107 C CB . PRO A 1 142 ? -18.575 -5.887 60.423 1.00 17.15 ? 145 PRO A CB 1 ATOM 1108 C CG . PRO A 1 142 ? -18.997 -7.108 61.192 1.00 18.62 ? 145 PRO A CG 1 ATOM 1109 C CD . PRO A 1 142 ? -17.948 -8.129 60.839 1.00 17.91 ? 145 PRO A CD 1 ATOM 1110 N N . SER A 1 143 ? -17.278 -4.796 57.474 1.00 15.56 ? 146 SER A N 1 ATOM 1111 C CA . SER A 1 143 ? -16.327 -3.843 56.917 1.00 15.53 ? 146 SER A CA 1 ATOM 1112 C C . SER A 1 143 ? -17.129 -2.666 56.397 1.00 15.00 ? 146 SER A C 1 ATOM 1113 O O . SER A 1 143 ? -18.292 -2.457 56.788 1.00 14.76 ? 146 SER A O 1 ATOM 1114 C CB . SER A 1 143 ? -15.497 -4.474 55.794 1.00 16.57 ? 146 SER A CB 1 ATOM 1115 O OG . SER A 1 143 ? -14.307 -3.733 55.563 1.00 19.58 ? 146 SER A OG 1 ATOM 1116 N N . PHE A 1 144 ? -16.503 -1.889 55.532 1.00 15.53 ? 147 PHE A N 1 ATOM 1117 C CA . PHE A 1 144 ? -17.124 -0.609 55.146 1.00 15.24 ? 147 PHE A CA 1 ATOM 1118 C C . PHE A 1 144 ? -16.485 -0.067 53.880 1.00 14.86 ? 147 PHE A C 1 ATOM 1119 O O . PHE A 1 144 ? -15.392 -0.500 53.487 1.00 15.64 ? 147 PHE A O 1 ATOM 1120 C CB . PHE A 1 144 ? -16.993 0.416 56.286 1.00 16.60 ? 147 PHE A CB 1 ATOM 1121 C CG . PHE A 1 144 ? -17.980 1.565 56.212 1.00 15.74 ? 147 PHE A CG 1 ATOM 1122 C CD1 . PHE A 1 144 ? -19.342 1.348 56.311 1.00 16.80 ? 147 PHE A CD1 1 ATOM 1123 C CD2 . PHE A 1 144 ? -17.526 2.892 56.090 1.00 15.84 ? 147 PHE A CD2 1 ATOM 1124 C CE1 . PHE A 1 144 ? -20.260 2.414 56.238 1.00 16.48 ? 147 PHE A CE1 1 ATOM 1125 C CE2 . PHE A 1 144 ? -18.451 3.961 56.061 1.00 13.41 ? 147 PHE A CE2 1 ATOM 1126 C CZ . PHE A 1 144 ? -19.790 3.737 56.129 1.00 15.62 ? 147 PHE A CZ 1 ATOM 1127 N N . PHE A 1 145 ? -17.189 0.875 53.250 1.00 14.12 ? 148 PHE A N 1 ATOM 1128 C CA . PHE A 1 145 ? -16.699 1.582 52.090 1.00 13.25 ? 148 PHE A CA 1 ATOM 1129 C C . PHE A 1 145 ? -15.264 2.021 52.340 1.00 13.20 ? 148 PHE A C 1 ATOM 1130 O O . PHE A 1 145 ? -14.981 2.680 53.369 1.00 15.45 ? 148 PHE A O 1 ATOM 1131 C CB . PHE A 1 145 ? -17.569 2.852 51.865 1.00 13.80 ? 148 PHE A CB 1 ATOM 1132 C CG . PHE A 1 145 ? -19.030 2.565 51.589 1.00 14.33 ? 148 PHE A CG 1 ATOM 1133 C CD1 . PHE A 1 145 ? -19.435 2.063 50.354 1.00 16.43 ? 148 PHE A CD1 1 ATOM 1134 C CD2 . PHE A 1 145 ? -20.012 2.898 52.555 1.00 15.88 ? 148 PHE A CD2 1 ATOM 1135 C CE1 . PHE A 1 145 ? -20.821 1.838 50.072 1.00 16.14 ? 148 PHE A CE1 1 ATOM 1136 C CE2 . PHE A 1 145 ? -21.393 2.677 52.322 1.00 16.62 ? 148 PHE A CE2 1 ATOM 1137 C CZ . PHE A 1 145 ? -21.798 2.166 51.071 1.00 16.35 ? 148 PHE A CZ 1 ATOM 1138 N N . ARG A 1 146 ? -14.374 1.680 51.410 1.00 14.17 ? 149 ARG A N 1 ATOM 1139 C CA . ARG A 1 146 ? -12.940 1.884 51.618 1.00 14.73 ? 149 ARG A CA 1 ATOM 1140 C C . ARG A 1 146 ? -12.574 3.351 51.670 1.00 15.08 ? 149 ARG A C 1 ATOM 1141 O O . ARG A 1 146 ? -11.542 3.690 52.291 1.00 15.60 ? 149 ARG A O 1 ATOM 1142 C CB . ARG A 1 146 ? -12.134 1.261 50.483 1.00 16.73 ? 149 ARG A CB 1 ATOM 1143 C CG . ARG A 1 146 ? -12.447 -0.233 50.268 1.00 23.11 ? 149 ARG A CG 1 ATOM 1144 C CD . ARG A 1 146 ? -11.918 -1.045 51.349 1.00 27.78 ? 149 ARG A CD 1 ATOM 1145 N NE . ARG A 1 146 ? -11.956 -2.501 51.064 1.00 25.85 ? 149 ARG A NE 1 ATOM 1146 C CZ . ARG A 1 146 ? -11.755 -3.422 52.008 1.00 30.86 ? 149 ARG A CZ 1 ATOM 1147 N NH1 . ARG A 1 146 ? -11.525 -3.055 53.259 1.00 35.37 ? 149 ARG A NH1 1 ATOM 1148 N NH2 . ARG A 1 146 ? -11.760 -4.711 51.706 1.00 29.57 ? 149 ARG A NH2 1 ATOM 1149 N N . ASN A 1 147 ? -13.361 4.192 50.984 1.00 14.01 ? 150 ASN A N 1 ATOM 1150 C CA . ASN A 1 147 ? -12.977 5.622 50.881 1.00 14.48 ? 150 ASN A CA 1 ATOM 1151 C C . ASN A 1 147 ? -13.607 6.509 51.947 1.00 14.05 ? 150 ASN A C 1 ATOM 1152 O O . ASN A 1 147 ? -13.308 7.713 51.988 1.00 13.48 ? 150 ASN A O 1 ATOM 1153 C CB . ASN A 1 147 ? -13.282 6.166 49.486 1.00 14.08 ? 150 ASN A CB 1 ATOM 1154 C CG . ASN A 1 147 ? -12.489 5.434 48.418 1.00 13.24 ? 150 ASN A CG 1 ATOM 1155 O OD1 . ASN A 1 147 ? -11.353 5.016 48.671 1.00 15.81 ? 150 ASN A OD1 1 ATOM 1156 N ND2 . ASN A 1 147 ? -13.055 5.306 47.242 1.00 13.78 ? 150 ASN A ND2 1 ATOM 1157 N N . MET A 1 148 ? -14.379 5.891 52.839 1.00 13.98 ? 151 MET A N 1 ATOM 1158 C CA . MET A 1 148 ? -15.198 6.647 53.791 1.00 13.61 ? 151 MET A CA 1 ATOM 1159 C C . MET A 1 148 ? -14.845 6.184 55.188 1.00 14.53 ? 151 MET A C 1 ATOM 1160 O O . MET A 1 148 ? -14.260 5.107 55.366 1.00 15.73 ? 151 MET A O 1 ATOM 1161 C CB . MET A 1 148 ? -16.706 6.437 53.559 1.00 13.87 ? 151 MET A CB 1 ATOM 1162 C CG . MET A 1 148 ? -17.194 6.626 52.082 1.00 14.67 ? 151 MET A CG 1 ATOM 1163 S SD . MET A 1 148 ? -16.765 8.273 51.467 1.00 16.16 ? 151 MET A SD 1 ATOM 1164 C CE . MET A 1 148 ? -17.912 9.280 52.427 1.00 15.50 ? 151 MET A CE 1 ATOM 1165 N N . VAL A 1 149 ? -15.216 7.018 56.165 1.00 13.94 ? 152 VAL A N 1 ATOM 1166 C CA . VAL A 1 149 ? -14.914 6.747 57.552 1.00 14.88 ? 152 VAL A CA 1 ATOM 1167 C C . VAL A 1 149 ? -16.194 6.879 58.381 1.00 14.60 ? 152 VAL A C 1 ATOM 1168 O O . VAL A 1 149 ? -16.816 7.943 58.405 1.00 15.70 ? 152 VAL A O 1 ATOM 1169 C CB . VAL A 1 149 ? -13.876 7.737 58.070 1.00 14.65 ? 152 VAL A CB 1 ATOM 1170 C CG1 . VAL A 1 149 ? -13.487 7.367 59.482 1.00 15.60 ? 152 VAL A CG1 1 ATOM 1171 C CG2 . VAL A 1 149 ? -12.646 7.734 57.169 1.00 15.90 ? 152 VAL A CG2 1 ATOM 1172 N N . TRP A 1 150 ? -16.573 5.803 59.064 1.00 15.54 ? 153 TRP A N 1 ATOM 1173 C CA . TRP A 1 150 ? -17.742 5.807 59.916 1.00 15.78 ? 153 TRP A CA 1 ATOM 1174 C C . TRP A 1 150 ? -17.282 6.182 61.342 1.00 17.36 ? 153 TRP A C 1 ATOM 1175 O O . TRP A 1 150 ? -16.716 5.349 62.043 1.00 17.75 ? 153 TRP A O 1 ATOM 1176 C CB . TRP A 1 150 ? -18.389 4.423 59.913 1.00 15.61 ? 153 TRP A CB 1 ATOM 1177 C CG . TRP A 1 150 ? -19.748 4.361 60.521 1.00 16.89 ? 153 TRP A CG 1 ATOM 1178 C CD1 . TRP A 1 150 ? -20.381 5.308 61.283 1.00 16.49 ? 153 TRP A CD1 1 ATOM 1179 C CD2 . TRP A 1 150 ? -20.655 3.268 60.388 1.00 15.36 ? 153 TRP A CD2 1 ATOM 1180 N NE1 . TRP A 1 150 ? -21.669 4.853 61.633 1.00 16.98 ? 153 TRP A NE1 1 ATOM 1181 C CE2 . TRP A 1 150 ? -21.835 3.600 61.106 1.00 15.71 ? 153 TRP A CE2 1 ATOM 1182 C CE3 . TRP A 1 150 ? -20.575 2.016 59.736 1.00 18.13 ? 153 TRP A CE3 1 ATOM 1183 C CZ2 . TRP A 1 150 ? -22.914 2.733 61.203 1.00 16.84 ? 153 TRP A CZ2 1 ATOM 1184 C CZ3 . TRP A 1 150 ? -21.668 1.147 59.832 1.00 19.16 ? 153 TRP A CZ3 1 ATOM 1185 C CH2 . TRP A 1 150 ? -22.828 1.528 60.533 1.00 18.89 ? 153 TRP A CH2 1 ATOM 1186 N N . LEU A 1 151 ? -17.497 7.427 61.750 1.00 17.09 ? 154 LEU A N 1 ATOM 1187 C CA A LEU A 1 151 ? -17.089 7.863 63.091 0.50 18.26 ? 154 LEU A CA 1 ATOM 1188 C CA B LEU A 1 151 ? -17.095 7.867 63.091 0.50 18.28 ? 154 LEU A CA 1 ATOM 1189 C C . LEU A 1 151 ? -18.107 7.366 64.117 1.00 18.87 ? 154 LEU A C 1 ATOM 1190 O O . LEU A 1 151 ? -19.319 7.519 63.937 1.00 18.81 ? 154 LEU A O 1 ATOM 1191 C CB A LEU A 1 151 ? -16.981 9.396 63.140 0.50 18.09 ? 154 LEU A CB 1 ATOM 1192 C CB B LEU A 1 151 ? -16.999 9.401 63.125 0.50 18.01 ? 154 LEU A CB 1 ATOM 1193 C CG A LEU A 1 151 ? -15.730 10.061 62.516 0.50 18.04 ? 154 LEU A CG 1 ATOM 1194 C CG B LEU A 1 151 ? -15.956 9.990 62.142 0.50 18.34 ? 154 LEU A CG 1 ATOM 1195 C CD1 A LEU A 1 151 ? -15.741 10.023 60.991 0.50 20.27 ? 154 LEU A CD1 1 ATOM 1196 C CD1 B LEU A 1 151 ? -16.034 11.510 62.073 0.50 19.45 ? 154 LEU A CD1 1 ATOM 1197 C CD2 A LEU A 1 151 ? -15.677 11.505 62.996 0.50 18.26 ? 154 LEU A CD2 1 ATOM 1198 C CD2 B LEU A 1 151 ? -14.553 9.541 62.462 0.50 16.98 ? 154 LEU A CD2 1 ATOM 1199 N N . THR A 1 152 ? -17.617 6.751 65.190 1.00 20.93 ? 155 THR A N 1 ATOM 1200 C CA . THR A 1 152 ? -18.527 6.332 66.259 1.00 23.18 ? 155 THR A CA 1 ATOM 1201 C C . THR A 1 152 ? -17.935 6.730 67.618 1.00 24.25 ? 155 THR A C 1 ATOM 1202 O O . THR A 1 152 ? -16.825 7.245 67.683 1.00 24.98 ? 155 THR A O 1 ATOM 1203 C CB . THR A 1 152 ? -18.851 4.807 66.198 1.00 22.65 ? 155 THR A CB 1 ATOM 1204 O OG1 . THR A 1 152 ? -17.654 4.008 66.247 1.00 23.37 ? 155 THR A OG1 1 ATOM 1205 C CG2 . THR A 1 152 ? -19.669 4.468 64.909 1.00 21.08 ? 155 THR A CG2 1 ATOM 1206 N N . GLU A 1 153 ? -18.720 6.517 68.674 1.00 26.63 ? 156 GLU A N 1 ATOM 1207 C CA . GLU A 1 153 ? -18.306 6.738 70.056 1.00 28.90 ? 156 GLU A CA 1 ATOM 1208 C C . GLU A 1 153 ? -16.941 6.140 70.373 1.00 28.58 ? 156 GLU A C 1 ATOM 1209 O O . GLU A 1 153 ? -16.644 5.016 69.988 1.00 27.79 ? 156 GLU A O 1 ATOM 1210 C CB . GLU A 1 153 ? -19.380 6.143 70.995 1.00 29.22 ? 156 GLU A CB 1 ATOM 1211 C CG . GLU A 1 153 ? -18.886 5.800 72.396 1.00 34.40 ? 156 GLU A CG 1 ATOM 1212 C CD . GLU A 1 153 ? -18.285 4.424 72.493 1.00 36.18 ? 156 GLU A CD 1 ATOM 1213 O OE1 . GLU A 1 153 ? -18.930 3.441 72.062 1.00 39.04 ? 156 GLU A OE1 1 ATOM 1214 O OE2 . GLU A 1 153 ? -17.161 4.324 73.011 1.00 41.64 ? 156 GLU A OE2 1 ATOM 1215 N N . LYS A 1 154 ? -16.133 6.897 71.120 1.00 30.41 ? 157 LYS A N 1 ATOM 1216 C CA . LYS A 1 154 ? -14.877 6.397 71.650 1.00 31.83 ? 157 LYS A CA 1 ATOM 1217 C C . LYS A 1 154 ? -14.894 6.652 73.165 1.00 32.78 ? 157 LYS A C 1 ATOM 1218 O O . LYS A 1 154 ? -15.060 7.793 73.595 1.00 32.80 ? 157 LYS A O 1 ATOM 1219 C CB . LYS A 1 154 ? -13.705 7.126 70.993 1.00 32.13 ? 157 LYS A CB 1 ATOM 1220 C CG . LYS A 1 154 ? -12.335 6.598 71.381 1.00 33.78 ? 157 LYS A CG 1 ATOM 1221 C CD . LYS A 1 154 ? -11.238 7.551 70.934 1.00 35.44 ? 157 LYS A CD 1 ATOM 1222 C CE . LYS A 1 154 ? -9.877 6.931 71.133 1.00 38.38 ? 157 LYS A CE 1 ATOM 1223 N NZ . LYS A 1 154 ? -8.828 7.986 71.168 1.00 40.09 ? 157 LYS A NZ 1 ATOM 1224 N N . GLY A 1 155 ? -14.769 5.582 73.949 1.00 34.07 ? 158 GLY A N 1 ATOM 1225 C CA . GLY A 1 155 ? -14.724 5.682 75.419 1.00 35.82 ? 158 GLY A CA 1 ATOM 1226 C C . GLY A 1 155 ? -16.049 6.137 76.002 1.00 36.71 ? 158 GLY A C 1 ATOM 1227 O O . GLY A 1 155 ? -16.088 6.799 77.044 1.00 37.89 ? 158 GLY A O 1 ATOM 1228 N N . SER A 1 156 ? -17.124 5.766 75.310 1.00 36.73 ? 159 SER A N 1 ATOM 1229 C CA . SER A 1 156 ? -18.506 6.189 75.590 1.00 36.73 ? 159 SER A CA 1 ATOM 1230 C C . SER A 1 156 ? -18.818 7.679 75.350 1.00 36.00 ? 159 SER A C 1 ATOM 1231 O O . SER A 1 156 ? -19.842 8.192 75.816 1.00 36.64 ? 159 SER A O 1 ATOM 1232 C CB . SER A 1 156 ? -18.981 5.713 76.970 1.00 37.09 ? 159 SER A CB 1 ATOM 1233 O OG . SER A 1 156 ? -20.396 5.637 76.977 1.00 38.99 ? 159 SER A OG 1 ATOM 1234 N N . ASN A 1 157 ? -17.963 8.362 74.589 1.00 35.10 ? 160 ASN A N 1 ATOM 1235 C CA . ASN A 1 157 ? -18.203 9.762 74.243 1.00 34.32 ? 160 ASN A CA 1 ATOM 1236 C C . ASN A 1 157 ? -18.051 10.064 72.754 1.00 32.67 ? 160 ASN A C 1 ATOM 1237 O O . ASN A 1 157 ? -17.208 9.480 72.087 1.00 32.98 ? 160 ASN A O 1 ATOM 1238 C CB . ASN A 1 157 ? -17.280 10.686 75.054 1.00 35.18 ? 160 ASN A CB 1 ATOM 1239 C CG . ASN A 1 157 ? -17.650 10.724 76.529 1.00 36.59 ? 160 ASN A CG 1 ATOM 1240 O OD1 . ASN A 1 157 ? -18.727 11.201 76.905 1.00 40.09 ? 160 ASN A OD1 1 ATOM 1241 N ND2 . ASN A 1 157 ? -16.763 10.217 77.370 1.00 38.79 ? 160 ASN A ND2 1 ATOM 1242 N N . TYR A 1 158 ? -18.860 10.990 72.258 1.00 30.90 ? 161 TYR A N 1 ATOM 1243 C CA . TYR A 1 158 ? -18.716 11.491 70.892 1.00 29.53 ? 161 TYR A CA 1 ATOM 1244 C C . TYR A 1 158 ? -18.624 13.022 70.916 1.00 29.23 ? 161 TYR A C 1 ATOM 1245 O O . TYR A 1 158 ? -19.624 13.714 70.792 1.00 29.85 ? 161 TYR A O 1 ATOM 1246 C CB . TYR A 1 158 ? -19.872 10.977 70.009 1.00 28.17 ? 161 TYR A CB 1 ATOM 1247 C CG . TYR A 1 158 ? -19.734 11.190 68.502 1.00 26.36 ? 161 TYR A CG 1 ATOM 1248 C CD1 . TYR A 1 158 ? -19.708 10.102 67.623 1.00 25.04 ? 161 TYR A CD1 1 ATOM 1249 C CD2 . TYR A 1 158 ? -19.668 12.467 67.964 1.00 25.01 ? 161 TYR A CD2 1 ATOM 1250 C CE1 . TYR A 1 158 ? -19.611 10.295 66.238 1.00 23.22 ? 161 TYR A CE1 1 ATOM 1251 C CE2 . TYR A 1 158 ? -19.557 12.681 66.585 1.00 23.71 ? 161 TYR A CE2 1 ATOM 1252 C CZ . TYR A 1 158 ? -19.536 11.591 65.732 1.00 23.75 ? 161 TYR A CZ 1 ATOM 1253 O OH . TYR A 1 158 ? -19.457 11.844 64.375 1.00 24.13 ? 161 TYR A OH 1 ATOM 1254 N N . PRO A 1 159 ? -17.391 13.565 71.067 1.00 29.40 ? 162 PRO A N 1 ATOM 1255 C CA . PRO A 1 159 ? -17.165 15.017 71.002 1.00 29.55 ? 162 PRO A CA 1 ATOM 1256 C C . PRO A 1 159 ? -17.496 15.587 69.622 1.00 29.64 ? 162 PRO A C 1 ATOM 1257 O O . PRO A 1 159 ? -17.611 14.810 68.650 1.00 30.39 ? 162 PRO A O 1 ATOM 1258 C CB . PRO A 1 159 ? -15.663 15.166 71.301 1.00 29.81 ? 162 PRO A CB 1 ATOM 1259 C CG . PRO A 1 159 ? -15.074 13.839 71.160 1.00 28.88 ? 162 PRO A CG 1 ATOM 1260 C CD . PRO A 1 159 ? -16.151 12.800 71.292 1.00 29.47 ? 162 PRO A CD 1 ATOM 1261 N N . VAL A 1 160 ? -17.681 16.903 69.522 1.00 28.43 ? 163 VAL A N 1 ATOM 1262 C CA . VAL A 1 160 ? -17.928 17.530 68.217 1.00 28.78 ? 163 VAL A CA 1 ATOM 1263 C C . VAL A 1 160 ? -16.782 17.120 67.292 1.00 27.80 ? 163 VAL A C 1 ATOM 1264 O O . VAL A 1 160 ? -15.605 17.222 67.650 1.00 28.73 ? 163 VAL A O 1 ATOM 1265 C CB . VAL A 1 160 ? -18.071 19.083 68.290 1.00 28.51 ? 163 VAL A CB 1 ATOM 1266 C CG1 . VAL A 1 160 ? -18.552 19.662 66.944 1.00 28.63 ? 163 VAL A CG1 1 ATOM 1267 C CG2 . VAL A 1 160 ? -19.081 19.466 69.360 1.00 31.01 ? 163 VAL A CG2 1 ATOM 1268 N N . ALA A 1 161 ? -17.137 16.596 66.126 1.00 26.87 ? 164 ALA A N 1 ATOM 1269 C CA . ALA A 1 161 ? -16.137 16.129 65.171 1.00 25.17 ? 164 ALA A CA 1 ATOM 1270 C C . ALA A 1 161 ? -15.960 17.231 64.154 1.00 24.22 ? 164 ALA A C 1 ATOM 1271 O O . ALA A 1 161 ? -16.924 17.645 63.519 1.00 23.88 ? 164 ALA A O 1 ATOM 1272 C CB . ALA A 1 161 ? -16.600 14.816 64.500 1.00 25.16 ? 164 ALA A CB 1 ATOM 1273 N N . LYS A 1 162 ? -14.732 17.742 64.019 1.00 23.81 ? 165 LYS A N 1 ATOM 1274 C CA . LYS A 1 162 ? -14.469 18.785 63.036 1.00 23.93 ? 165 LYS A CA 1 ATOM 1275 C C . LYS A 1 162 ? -13.272 18.358 62.199 1.00 23.06 ? 165 LYS A C 1 ATOM 1276 O O . LYS A 1 162 ? -12.238 17.952 62.738 1.00 23.99 ? 165 LYS A O 1 ATOM 1277 C CB . LYS A 1 162 ? -14.210 20.161 63.691 1.00 24.52 ? 165 LYS A CB 1 ATOM 1278 C CG . LYS A 1 162 ? -15.495 20.828 64.232 1.00 25.21 ? 165 LYS A CG 1 ATOM 1279 C CD . LYS A 1 162 ? -15.259 22.317 64.603 1.00 27.87 ? 165 LYS A CD 1 ATOM 1280 C CE . LYS A 1 162 ? -15.456 23.242 63.396 1.00 32.59 ? 165 LYS A CE 1 ATOM 1281 N NZ . LYS A 1 162 ? -16.611 22.845 62.561 1.00 37.86 ? 165 LYS A NZ 1 ATOM 1282 N N . GLY A 1 163 ? -13.439 18.420 60.891 1.00 22.57 ? 166 GLY A N 1 ATOM 1283 C CA . GLY A 1 163 ? -12.355 18.164 59.947 1.00 21.27 ? 166 GLY A CA 1 ATOM 1284 C C . GLY A 1 163 ? -12.414 19.237 58.887 1.00 20.85 ? 166 GLY A C 1 ATOM 1285 O O . GLY A 1 163 ? -13.504 19.723 58.539 1.00 21.43 ? 166 GLY A O 1 ATOM 1286 N N . SER A 1 164 ? -11.250 19.633 58.364 1.00 19.32 ? 167 SER A N 1 ATOM 1287 C CA A SER A 1 164 ? -11.250 20.600 57.286 0.50 19.03 ? 167 SER A CA 1 ATOM 1288 C CA B SER A 1 164 ? -11.189 20.673 57.352 0.50 19.39 ? 167 SER A CA 1 ATOM 1289 C C . SER A 1 164 ? -10.121 20.312 56.320 1.00 19.00 ? 167 SER A C 1 ATOM 1290 O O . SER A 1 164 ? -9.095 19.719 56.695 1.00 17.92 ? 167 SER A O 1 ATOM 1291 C CB A SER A 1 164 ? -11.135 22.029 57.829 0.50 19.26 ? 167 SER A CB 1 ATOM 1292 C CB B SER A 1 164 ? -10.845 22.006 58.040 0.50 19.55 ? 167 SER A CB 1 ATOM 1293 O OG A SER A 1 164 ? -9.809 22.322 58.236 0.50 18.86 ? 167 SER A OG 1 ATOM 1294 O OG B SER A 1 164 ? -10.833 23.106 57.141 0.50 20.74 ? 167 SER A OG 1 ATOM 1295 N N . TYR A 1 165 ? -10.347 20.688 55.066 1.00 17.88 ? 168 TYR A N 1 ATOM 1296 C CA . TYR A 1 165 ? -9.373 20.464 54.003 1.00 17.16 ? 168 TYR A CA 1 ATOM 1297 C C . TYR A 1 165 ? -9.355 21.623 53.026 1.00 16.84 ? 168 TYR A C 1 ATOM 1298 O O . TYR A 1 165 ? -10.400 22.003 52.468 1.00 16.02 ? 168 TYR A O 1 ATOM 1299 C CB . TYR A 1 165 ? -9.668 19.153 53.222 1.00 17.29 ? 168 TYR A CB 1 ATOM 1300 C CG . TYR A 1 165 ? -8.765 19.000 52.027 1.00 16.04 ? 168 TYR A CG 1 ATOM 1301 C CD1 . TYR A 1 165 ? -7.401 18.670 52.197 1.00 15.91 ? 168 TYR A CD1 1 ATOM 1302 C CD2 . TYR A 1 165 ? -9.228 19.238 50.714 1.00 16.70 ? 168 TYR A CD2 1 ATOM 1303 C CE1 . TYR A 1 165 ? -6.553 18.558 51.094 1.00 16.56 ? 168 TYR A CE1 1 ATOM 1304 C CE2 . TYR A 1 165 ? -8.380 19.132 49.608 1.00 17.16 ? 168 TYR A CE2 1 ATOM 1305 C CZ . TYR A 1 165 ? -7.039 18.794 49.816 1.00 16.75 ? 168 TYR A CZ 1 ATOM 1306 O OH . TYR A 1 165 ? -6.193 18.696 48.722 1.00 19.10 ? 168 TYR A OH 1 ATOM 1307 N N . ASN A 1 166 ? -8.163 22.186 52.839 1.00 15.37 ? 169 ASN A N 1 ATOM 1308 C CA . ASN A 1 166 ? -7.962 23.226 51.839 1.00 15.70 ? 169 ASN A CA 1 ATOM 1309 C C . ASN A 1 166 ? -7.479 22.552 50.571 1.00 15.79 ? 169 ASN A C 1 ATOM 1310 O O . ASN A 1 166 ? -6.453 21.858 50.600 1.00 14.96 ? 169 ASN A O 1 ATOM 1311 C CB . ASN A 1 166 ? -6.917 24.225 52.379 1.00 16.37 ? 169 ASN A CB 1 ATOM 1312 C CG . ASN A 1 166 ? -6.652 25.401 51.445 1.00 18.89 ? 169 ASN A CG 1 ATOM 1313 O OD1 . ASN A 1 166 ? -6.986 25.389 50.245 1.00 17.49 ? 169 ASN A OD1 1 ATOM 1314 N ND2 . ASN A 1 166 ? -6.005 26.437 52.013 1.00 20.78 ? 169 ASN A ND2 1 ATOM 1315 N N . ASN A 1 167 ? -8.229 22.728 49.485 1.00 15.22 ? 170 ASN A N 1 ATOM 1316 C CA . ASN A 1 167 ? -7.859 22.161 48.188 1.00 15.59 ? 170 ASN A CA 1 ATOM 1317 C C . ASN A 1 167 ? -6.632 22.822 47.521 1.00 16.70 ? 170 ASN A C 1 ATOM 1318 O O . ASN A 1 167 ? -6.763 23.732 46.690 1.00 17.61 ? 170 ASN A O 1 ATOM 1319 C CB . ASN A 1 167 ? -9.068 22.111 47.222 1.00 16.65 ? 170 ASN A CB 1 ATOM 1320 C CG . ASN A 1 167 ? -8.703 21.480 45.887 1.00 13.64 ? 170 ASN A CG 1 ATOM 1321 O OD1 . ASN A 1 167 ? -7.642 20.866 45.783 1.00 17.22 ? 170 ASN A OD1 1 ATOM 1322 N ND2 . ASN A 1 167 ? -9.593 21.538 44.900 1.00 15.15 ? 170 ASN A ND2 1 ATOM 1323 N N . THR A 1 168 ? -5.460 22.307 47.882 1.00 16.76 ? 171 THR A N 1 ATOM 1324 C CA . THR A 1 168 ? -4.193 22.782 47.348 1.00 17.98 ? 171 THR A CA 1 ATOM 1325 C C . THR A 1 168 ? -3.720 21.868 46.214 1.00 18.59 ? 171 THR A C 1 ATOM 1326 O O . THR A 1 168 ? -2.570 21.967 45.743 1.00 17.97 ? 171 THR A O 1 ATOM 1327 C CB . THR A 1 168 ? -3.130 22.817 48.456 1.00 18.49 ? 171 THR A CB 1 ATOM 1328 O OG1 . THR A 1 168 ? -2.963 21.502 49.014 1.00 20.08 ? 171 THR A OG1 1 ATOM 1329 C CG2 . THR A 1 168 ? -3.550 23.802 49.566 1.00 20.34 ? 171 THR A CG2 1 ATOM 1330 N N . SER A 1 169 ? -4.622 20.983 45.778 1.00 18.53 ? 172 SER A N 1 ATOM 1331 C CA . SER A 1 169 ? -4.247 19.922 44.828 1.00 18.71 ? 172 SER A CA 1 ATOM 1332 C C . SER A 1 169 ? -3.922 20.363 43.407 1.00 20.09 ? 172 SER A C 1 ATOM 1333 O O . SER A 1 169 ? -3.341 19.573 42.643 1.00 20.93 ? 172 SER A O 1 ATOM 1334 C CB . SER A 1 169 ? -5.337 18.840 44.767 1.00 19.23 ? 172 SER A CB 1 ATOM 1335 O OG . SER A 1 169 ? -6.397 19.310 43.949 1.00 18.24 ? 172 SER A OG 1 ATOM 1336 N N . GLY A 1 170 ? -4.317 21.574 43.051 1.00 19.32 ? 173 GLY A N 1 ATOM 1337 C CA . GLY A 1 170 ? -4.111 22.122 41.717 1.00 21.44 ? 173 GLY A CA 1 ATOM 1338 C C . GLY A 1 170 ? -5.232 21.893 40.718 1.00 21.93 ? 173 GLY A C 1 ATOM 1339 O O . GLY A 1 170 ? -5.136 22.335 39.574 1.00 23.35 ? 173 GLY A O 1 ATOM 1340 N N . GLU A 1 171 ? -6.301 21.203 41.127 1.00 19.50 ? 174 GLU A N 1 ATOM 1341 C CA . GLU A 1 171 ? -7.497 21.108 40.305 1.00 19.57 ? 174 GLU A CA 1 ATOM 1342 C C . GLU A 1 171 ? -8.731 21.011 41.197 1.00 16.95 ? 174 GLU A C 1 ATOM 1343 O O . GLU A 1 171 ? -8.612 20.800 42.402 1.00 17.27 ? 174 GLU A O 1 ATOM 1344 C CB . GLU A 1 171 ? -7.447 19.891 39.361 1.00 20.46 ? 174 GLU A CB 1 ATOM 1345 C CG . GLU A 1 171 ? -7.188 20.231 37.874 1.00 27.21 ? 174 GLU A CG 1 ATOM 1346 C CD . GLU A 1 171 ? -8.482 20.666 37.123 1.00 32.58 ? 174 GLU A CD 1 ATOM 1347 O OE1 . GLU A 1 171 ? -9.469 21.116 37.782 1.00 35.06 ? 174 GLU A OE1 1 ATOM 1348 O OE2 . GLU A 1 171 ? -8.505 20.577 35.859 1.00 35.40 ? 174 GLU A OE2 1 ATOM 1349 N N . GLN A 1 172 ? -9.898 21.184 40.591 1.00 18.14 ? 175 GLN A N 1 ATOM 1350 C CA . GLN A 1 172 ? -11.169 20.977 41.288 1.00 17.95 ? 175 GLN A CA 1 ATOM 1351 C C . GLN A 1 172 ? -11.196 19.563 41.828 1.00 17.87 ? 175 GLN A C 1 ATOM 1352 O O . GLN A 1 172 ? -10.648 18.646 41.185 1.00 16.76 ? 175 GLN A O 1 ATOM 1353 C CB . GLN A 1 172 ? -12.328 21.139 40.319 1.00 19.67 ? 175 GLN A CB 1 ATOM 1354 C CG . GLN A 1 172 ? -12.663 22.537 39.946 1.00 25.00 ? 175 GLN A CG 1 ATOM 1355 C CD . GLN A 1 172 ? -14.058 22.592 39.332 1.00 29.27 ? 175 GLN A CD 1 ATOM 1356 O OE1 . GLN A 1 172 ? -14.336 21.876 38.357 1.00 30.64 ? 175 GLN A OE1 1 ATOM 1357 N NE2 . GLN A 1 172 ? -14.949 23.404 39.908 1.00 29.00 ? 175 GLN A NE2 1 ATOM 1358 N N . MET A 1 173 ? -11.797 19.385 43.005 1.00 16.89 ? 176 MET A N 1 ATOM 1359 C CA . MET A 1 173 ? -11.818 18.055 43.643 1.00 16.66 ? 176 MET A CA 1 ATOM 1360 C C . MET A 1 173 ? -13.232 17.619 44.025 1.00 16.48 ? 176 MET A C 1 ATOM 1361 O O . MET A 1 173 ? -13.967 18.347 44.703 1.00 16.60 ? 176 MET A O 1 ATOM 1362 C CB . MET A 1 173 ? -10.970 18.095 44.906 1.00 17.00 ? 176 MET A CB 1 ATOM 1363 C CG . MET A 1 173 ? -10.920 16.768 45.651 1.00 18.39 ? 176 MET A CG 1 ATOM 1364 S SD . MET A 1 173 ? -9.854 16.929 47.077 1.00 18.46 ? 176 MET A SD 1 ATOM 1365 C CE . MET A 1 173 ? -8.196 17.015 46.402 1.00 19.72 ? 176 MET A CE 1 ATOM 1366 N N . LEU A 1 174 ? -13.579 16.395 43.625 1.00 15.74 ? 177 LEU A N 1 ATOM 1367 C CA . LEU A 1 174 ? -14.874 15.794 43.988 1.00 15.63 ? 177 LEU A CA 1 ATOM 1368 C C . LEU A 1 174 ? -14.740 15.228 45.410 1.00 15.11 ? 177 LEU A C 1 ATOM 1369 O O . LEU A 1 174 ? -13.781 14.479 45.706 1.00 14.87 ? 177 LEU A O 1 ATOM 1370 C CB . LEU A 1 174 ? -15.187 14.693 42.993 1.00 15.70 ? 177 LEU A CB 1 ATOM 1371 C CG . LEU A 1 174 ? -16.365 13.798 43.377 1.00 18.95 ? 177 LEU A CG 1 ATOM 1372 C CD1 . LEU A 1 174 ? -17.659 14.613 43.445 1.00 19.59 ? 177 LEU A CD1 1 ATOM 1373 C CD2 . LEU A 1 174 ? -16.470 12.657 42.416 1.00 22.74 ? 177 LEU A CD2 1 ATOM 1374 N N . ILE A 1 175 ? -15.660 15.611 46.280 1.00 13.75 ? 178 ILE A N 1 ATOM 1375 C CA . ILE A 1 175 ? -15.677 15.116 47.692 1.00 14.25 ? 178 ILE A CA 1 ATOM 1376 C C . ILE A 1 175 ? -17.075 14.641 48.030 1.00 14.69 ? 178 ILE A C 1 ATOM 1377 O O . ILE A 1 175 ? -18.078 15.343 47.705 1.00 14.54 ? 178 ILE A O 1 ATOM 1378 C CB . ILE A 1 175 ? -15.190 16.185 48.722 1.00 12.87 ? 178 ILE A CB 1 ATOM 1379 C CG1 . ILE A 1 175 ? -13.761 16.663 48.343 1.00 16.58 ? 178 ILE A CG1 1 ATOM 1380 C CG2 . ILE A 1 175 ? -15.322 15.690 50.167 1.00 14.03 ? 178 ILE A CG2 1 ATOM 1381 C CD1 . ILE A 1 175 ? -13.281 17.821 49.177 1.00 15.64 ? 178 ILE A CD1 1 ATOM 1382 N N . ILE A 1 176 ? -17.147 13.420 48.607 1.00 14.11 ? 179 ILE A N 1 ATOM 1383 C CA . ILE A 1 176 ? -18.459 12.847 49.004 1.00 13.98 ? 179 ILE A CA 1 ATOM 1384 C C . ILE A 1 176 ? -18.522 12.706 50.542 1.00 14.70 ? 179 ILE A C 1 ATOM 1385 O O . ILE A 1 176 ? -17.485 12.469 51.204 1.00 14.77 ? 179 ILE A O 1 ATOM 1386 C CB . ILE A 1 176 ? -18.673 11.454 48.318 1.00 13.71 ? 179 ILE A CB 1 ATOM 1387 C CG1 . ILE A 1 176 ? -18.511 11.588 46.774 1.00 13.55 ? 179 ILE A CG1 1 ATOM 1388 C CG2 . ILE A 1 176 ? -19.951 10.798 48.786 1.00 16.18 ? 179 ILE A CG2 1 ATOM 1389 C CD1 . ILE A 1 176 ? -18.110 10.263 46.100 1.00 14.63 ? 179 ILE A CD1 1 ATOM 1390 N N . TRP A 1 177 ? -19.690 12.897 51.144 1.00 13.68 ? 180 TRP A N 1 ATOM 1391 C CA . TRP A 1 177 ? -19.841 12.615 52.574 1.00 15.53 ? 180 TRP A CA 1 ATOM 1392 C C . TRP A 1 177 ? -21.268 12.040 52.776 1.00 14.39 ? 180 TRP A C 1 ATOM 1393 O O . TRP A 1 177 ? -22.097 12.028 51.844 1.00 14.39 ? 180 TRP A O 1 ATOM 1394 C CB . TRP A 1 177 ? -19.658 13.863 53.426 1.00 16.39 ? 180 TRP A CB 1 ATOM 1395 C CG . TRP A 1 177 ? -20.721 14.891 53.131 1.00 18.52 ? 180 TRP A CG 1 ATOM 1396 C CD1 . TRP A 1 177 ? -21.921 15.056 53.772 1.00 20.42 ? 180 TRP A CD1 1 ATOM 1397 C CD2 . TRP A 1 177 ? -20.688 15.852 52.067 1.00 18.48 ? 180 TRP A CD2 1 ATOM 1398 N NE1 . TRP A 1 177 ? -22.634 16.099 53.183 1.00 18.22 ? 180 TRP A NE1 1 ATOM 1399 C CE2 . TRP A 1 177 ? -21.895 16.594 52.135 1.00 21.11 ? 180 TRP A CE2 1 ATOM 1400 C CE3 . TRP A 1 177 ? -19.736 16.180 51.078 1.00 21.68 ? 180 TRP A CE3 1 ATOM 1401 C CZ2 . TRP A 1 177 ? -22.198 17.615 51.209 1.00 20.53 ? 180 TRP A CZ2 1 ATOM 1402 C CZ3 . TRP A 1 177 ? -20.010 17.235 50.174 1.00 19.25 ? 180 TRP A CZ3 1 ATOM 1403 C CH2 . TRP A 1 177 ? -21.251 17.917 50.243 1.00 20.92 ? 180 TRP A CH2 1 ATOM 1404 N N . GLY A 1 178 ? -21.514 11.501 53.954 1.00 15.13 ? 181 GLY A N 1 ATOM 1405 C CA . GLY A 1 178 ? -22.860 10.953 54.198 1.00 15.04 ? 181 GLY A CA 1 ATOM 1406 C C . GLY A 1 178 ? -23.345 11.227 55.607 1.00 15.28 ? 181 GLY A C 1 ATOM 1407 O O . GLY A 1 178 ? -22.582 11.670 56.479 1.00 15.74 ? 181 GLY A O 1 ATOM 1408 N N . VAL A 1 179 ? -24.626 10.914 55.805 1.00 14.46 ? 182 VAL A N 1 ATOM 1409 C CA . VAL A 1 179 ? -25.274 10.979 57.098 1.00 14.46 ? 182 VAL A CA 1 ATOM 1410 C C . VAL A 1 179 ? -25.959 9.646 57.292 1.00 14.89 ? 182 VAL A C 1 ATOM 1411 O O . VAL A 1 179 ? -26.586 9.121 56.373 1.00 14.54 ? 182 VAL A O 1 ATOM 1412 C CB . VAL A 1 179 ? -26.325 12.123 57.154 1.00 16.33 ? 182 VAL A CB 1 ATOM 1413 C CG1 . VAL A 1 179 ? -27.390 11.944 56.112 1.00 18.97 ? 182 VAL A CG1 1 ATOM 1414 C CG2 . VAL A 1 179 ? -26.957 12.209 58.529 1.00 16.52 ? 182 VAL A CG2 1 ATOM 1415 N N . HIS A 1 180 ? -25.788 9.101 58.487 1.00 14.74 ? 183 HIS A N 1 ATOM 1416 C CA . HIS A 1 180 ? -26.372 7.819 58.829 1.00 14.50 ? 183 HIS A CA 1 ATOM 1417 C C . HIS A 1 180 ? -27.733 8.044 59.477 1.00 14.89 ? 183 HIS A C 1 ATOM 1418 O O . HIS A 1 180 ? -27.813 8.785 60.470 1.00 14.55 ? 183 HIS A O 1 ATOM 1419 C CB . HIS A 1 180 ? -25.444 7.132 59.829 1.00 15.79 ? 183 HIS A CB 1 ATOM 1420 C CG . HIS A 1 180 ? -25.933 5.789 60.264 1.00 14.98 ? 183 HIS A CG 1 ATOM 1421 N ND1 . HIS A 1 180 ? -25.889 5.370 61.583 1.00 17.50 ? 183 HIS A ND1 1 ATOM 1422 C CD2 . HIS A 1 180 ? -26.460 4.759 59.557 1.00 18.50 ? 183 HIS A CD2 1 ATOM 1423 C CE1 . HIS A 1 180 ? -26.388 4.147 61.665 1.00 18.42 ? 183 HIS A CE1 1 ATOM 1424 N NE2 . HIS A 1 180 ? -26.734 3.753 60.453 1.00 18.53 ? 183 HIS A NE2 1 ATOM 1425 N N . HIS A 1 181 ? -28.769 7.401 58.918 1.00 13.52 ? 184 HIS A N 1 ATOM 1426 C CA . HIS A 1 181 ? -30.154 7.449 59.427 1.00 13.98 ? 184 HIS A CA 1 ATOM 1427 C C . HIS A 1 181 ? -30.471 6.098 60.090 1.00 14.59 ? 184 HIS A C 1 ATOM 1428 O O . HIS A 1 181 ? -30.740 5.115 59.377 1.00 15.03 ? 184 HIS A O 1 ATOM 1429 C CB . HIS A 1 181 ? -31.117 7.643 58.268 1.00 15.11 ? 184 HIS A CB 1 ATOM 1430 C CG . HIS A 1 181 ? -30.941 8.942 57.543 1.00 16.65 ? 184 HIS A CG 1 ATOM 1431 N ND1 . HIS A 1 181 ? -31.131 10.161 58.154 1.00 18.62 ? 184 HIS A ND1 1 ATOM 1432 C CD2 . HIS A 1 181 ? -30.596 9.211 56.258 1.00 17.74 ? 184 HIS A CD2 1 ATOM 1433 C CE1 . HIS A 1 181 ? -30.921 11.133 57.279 1.00 19.30 ? 184 HIS A CE1 1 ATOM 1434 N NE2 . HIS A 1 181 ? -30.628 10.586 56.114 1.00 14.77 ? 184 HIS A NE2 1 ATOM 1435 N N . PRO A 1 182 ? -30.385 6.035 61.425 1.00 15.15 ? 185 PRO A N 1 ATOM 1436 C CA . PRO A 1 182 ? -30.616 4.734 62.106 1.00 16.15 ? 185 PRO A CA 1 ATOM 1437 C C . PRO A 1 182 ? -32.043 4.191 62.008 1.00 17.47 ? 185 PRO A C 1 ATOM 1438 O O . PRO A 1 182 ? -32.976 4.892 61.629 1.00 16.17 ? 185 PRO A O 1 ATOM 1439 C CB . PRO A 1 182 ? -30.268 5.019 63.578 1.00 15.98 ? 185 PRO A CB 1 ATOM 1440 C CG . PRO A 1 182 ? -29.369 6.253 63.552 1.00 16.69 ? 185 PRO A CG 1 ATOM 1441 C CD . PRO A 1 182 ? -29.961 7.088 62.370 1.00 15.90 ? 185 PRO A CD 1 ATOM 1442 N N . ASN A 1 183 ? -32.172 2.915 62.370 1.00 18.43 ? 186 ASN A N 1 ATOM 1443 C CA . ASN A 1 183 ? -33.464 2.246 62.417 1.00 20.60 ? 186 ASN A CA 1 ATOM 1444 C C . ASN A 1 183 ? -34.190 2.546 63.713 1.00 22.12 ? 186 ASN A C 1 ATOM 1445 O O . ASN A 1 183 ? -35.442 2.644 63.741 1.00 22.74 ? 186 ASN A O 1 ATOM 1446 C CB . ASN A 1 183 ? -33.225 0.736 62.252 1.00 20.49 ? 186 ASN A CB 1 ATOM 1447 C CG . ASN A 1 183 ? -34.516 -0.060 62.194 1.00 23.07 ? 186 ASN A CG 1 ATOM 1448 O OD1 . ASN A 1 183 ? -35.165 -0.155 61.159 1.00 24.47 ? 186 ASN A OD1 1 ATOM 1449 N ND2 . ASN A 1 183 ? -34.850 -0.690 63.305 1.00 28.05 ? 186 ASN A ND2 1 ATOM 1450 N N . ASP A 1 184 ? -33.414 2.707 64.791 1.00 22.94 ? 187 ASP A N 1 ATOM 1451 C CA . ASP A 1 184 ? -33.995 2.916 66.111 1.00 25.50 ? 187 ASP A CA 1 ATOM 1452 C C . ASP A 1 184 ? -33.056 3.665 67.059 1.00 25.57 ? 187 ASP A C 1 ATOM 1453 O O . ASP A 1 184 ? -31.878 3.876 66.763 1.00 24.50 ? 187 ASP A O 1 ATOM 1454 C CB . ASP A 1 184 ? -34.408 1.557 66.708 1.00 25.45 ? 187 ASP A CB 1 ATOM 1455 C CG . ASP A 1 184 ? -33.251 0.596 66.780 1.00 29.21 ? 187 ASP A CG 1 ATOM 1456 O OD1 . ASP A 1 184 ? -32.313 0.870 67.543 1.00 29.32 ? 187 ASP A OD1 1 ATOM 1457 O OD2 . ASP A 1 184 ? -33.269 -0.418 66.047 1.00 35.05 ? 187 ASP A OD2 1 ATOM 1458 N N . GLU A 1 185 ? -33.615 4.041 68.210 1.00 26.80 ? 188 GLU A N 1 ATOM 1459 C CA A GLU A 1 185 ? -32.946 4.810 69.256 0.50 27.41 ? 188 GLU A CA 1 ATOM 1460 C CA B GLU A 1 185 ? -32.883 4.842 69.189 0.50 27.42 ? 188 GLU A CA 1 ATOM 1461 C C . GLU A 1 185 ? -31.799 4.058 69.912 1.00 27.86 ? 188 GLU A C 1 ATOM 1462 O O . GLU A 1 185 ? -30.803 4.652 70.336 1.00 28.22 ? 188 GLU A O 1 ATOM 1463 C CB A GLU A 1 185 ? -33.971 5.166 70.341 0.50 27.97 ? 188 GLU A CB 1 ATOM 1464 C CB B GLU A 1 185 ? -33.825 5.514 70.203 0.50 28.15 ? 188 GLU A CB 1 ATOM 1465 C CG A GLU A 1 185 ? -35.388 5.402 69.830 0.50 29.36 ? 188 GLU A CG 1 ATOM 1466 C CG B GLU A 1 185 ? -34.850 6.480 69.604 0.50 29.50 ? 188 GLU A CG 1 ATOM 1467 C CD A GLU A 1 185 ? -36.163 4.116 69.570 0.50 30.50 ? 188 GLU A CD 1 ATOM 1468 C CD B GLU A 1 185 ? -34.343 7.901 69.383 0.50 31.52 ? 188 GLU A CD 1 ATOM 1469 O OE1 A GLU A 1 185 ? -36.536 3.434 70.554 0.50 32.54 ? 188 GLU A OE1 1 ATOM 1470 O OE1 B GLU A 1 185 ? -33.136 8.167 69.594 0.50 34.65 ? 188 GLU A OE1 1 ATOM 1471 O OE2 A GLU A 1 185 ? -36.410 3.797 68.385 0.50 28.65 ? 188 GLU A OE2 1 ATOM 1472 O OE2 B GLU A 1 185 ? -35.168 8.765 68.989 0.50 30.91 ? 188 GLU A OE2 1 ATOM 1473 N N . THR A 1 186 ? -31.950 2.740 70.048 1.00 27.85 ? 189 THR A N 1 ATOM 1474 C CA A THR A 1 186 ? -30.860 1.966 70.662 0.50 28.19 ? 189 THR A CA 1 ATOM 1475 C CA B THR A 1 186 ? -30.872 1.925 70.638 0.50 27.87 ? 189 THR A CA 1 ATOM 1476 C C . THR A 1 186 ? -29.624 2.001 69.761 1.00 27.80 ? 189 THR A C 1 ATOM 1477 O O . THR A 1 186 ? -28.515 2.164 70.256 1.00 28.13 ? 189 THR A O 1 ATOM 1478 C CB A THR A 1 186 ? -31.274 0.531 71.171 0.50 28.54 ? 189 THR A CB 1 ATOM 1479 C CB B THR A 1 186 ? -31.280 0.444 70.906 0.50 28.16 ? 189 THR A CB 1 ATOM 1480 O OG1 A THR A 1 186 ? -30.189 -0.400 70.999 0.50 28.78 ? 189 THR A OG1 1 ATOM 1481 O OG1 B THR A 1 186 ? -31.387 -0.288 69.672 0.50 27.81 ? 189 THR A OG1 1 ATOM 1482 C CG2 A THR A 1 186 ? -32.495 0.017 70.457 0.50 28.95 ? 189 THR A CG2 1 ATOM 1483 C CG2 B THR A 1 186 ? -32.578 0.369 71.709 0.50 27.25 ? 189 THR A CG2 1 ATOM 1484 N N . GLU A 1 187 ? -29.826 1.914 68.442 1.00 26.86 ? 190 GLU A N 1 ATOM 1485 C CA . GLU A 1 187 ? -28.733 2.046 67.470 1.00 27.03 ? 190 GLU A CA 1 ATOM 1486 C C . GLU A 1 187 ? -28.029 3.414 67.562 1.00 26.84 ? 190 GLU A C 1 ATOM 1487 O O . GLU A 1 187 ? -26.805 3.495 67.656 1.00 27.64 ? 190 GLU A O 1 ATOM 1488 C CB . GLU A 1 187 ? -29.268 1.790 66.051 1.00 26.30 ? 190 GLU A CB 1 ATOM 1489 C CG . GLU A 1 187 ? -28.314 2.061 64.921 1.00 28.04 ? 190 GLU A CG 1 ATOM 1490 C CD . GLU A 1 187 ? -28.898 1.675 63.550 1.00 27.85 ? 190 GLU A CD 1 ATOM 1491 O OE1 . GLU A 1 187 ? -30.108 1.340 63.473 1.00 27.28 ? 190 GLU A OE1 1 ATOM 1492 O OE2 . GLU A 1 187 ? -28.147 1.723 62.540 1.00 27.22 ? 190 GLU A OE2 1 ATOM 1493 N N . GLN A 1 188 ? -28.817 4.479 67.547 1.00 26.52 ? 191 GLN A N 1 ATOM 1494 C CA . GLN A 1 188 ? -28.300 5.816 67.775 1.00 26.73 ? 191 GLN A CA 1 ATOM 1495 C C . GLN A 1 188 ? -27.471 5.892 69.067 1.00 27.69 ? 191 GLN A C 1 ATOM 1496 O O . GLN A 1 188 ? -26.365 6.412 69.063 1.00 26.55 ? 191 GLN A O 1 ATOM 1497 C CB . GLN A 1 188 ? -29.443 6.838 67.775 1.00 26.25 ? 191 GLN A CB 1 ATOM 1498 C CG . GLN A 1 188 ? -29.008 8.300 68.019 1.00 25.86 ? 191 GLN A CG 1 ATOM 1499 C CD . GLN A 1 188 ? -28.272 8.898 66.825 1.00 25.00 ? 191 GLN A CD 1 ATOM 1500 O OE1 . GLN A 1 188 ? -28.472 8.450 65.698 1.00 22.53 ? 191 GLN A OE1 1 ATOM 1501 N NE2 . GLN A 1 188 ? -27.432 9.934 67.064 1.00 22.62 ? 191 GLN A NE2 1 ATOM 1502 N N . ARG A 1 189 ? -27.986 5.364 70.179 1.00 28.21 ? 192 ARG A N 1 ATOM 1503 C CA . ARG A 1 189 ? -27.242 5.465 71.439 1.00 29.88 ? 192 ARG A CA 1 ATOM 1504 C C . ARG A 1 189 ? -25.955 4.627 71.463 1.00 29.76 ? 192 ARG A C 1 ATOM 1505 O O . ARG A 1 189 ? -24.895 5.118 71.872 1.00 30.11 ? 192 ARG A O 1 ATOM 1506 C CB . ARG A 1 189 ? -28.145 5.146 72.643 1.00 29.76 ? 192 ARG A CB 1 ATOM 1507 C CG . ARG A 1 189 ? -27.426 5.262 73.995 1.00 32.87 ? 192 ARG A CG 1 ATOM 1508 C CD . ARG A 1 189 ? -28.188 4.547 75.127 1.00 33.57 ? 192 ARG A CD 1 ATOM 1509 N NE . ARG A 1 189 ? -28.043 3.094 74.991 1.00 40.74 ? 192 ARG A NE 1 ATOM 1510 C CZ . ARG A 1 189 ? -29.009 2.273 74.587 1.00 42.57 ? 192 ARG A CZ 1 ATOM 1511 N NH1 . ARG A 1 189 ? -30.224 2.743 74.320 1.00 44.33 ? 192 ARG A NH1 1 ATOM 1512 N NH2 . ARG A 1 189 ? -28.761 0.976 74.474 1.00 43.89 ? 192 ARG A NH2 1 ATOM 1513 N N . THR A 1 190 ? -26.033 3.380 71.001 1.00 29.13 ? 193 THR A N 1 ATOM 1514 C CA . THR A 1 190 ? -24.859 2.505 70.971 1.00 29.47 ? 193 THR A CA 1 ATOM 1515 C C . THR A 1 190 ? -23.728 3.090 70.089 1.00 28.91 ? 193 THR A C 1 ATOM 1516 O O . THR A 1 190 ? -22.555 3.010 70.446 1.00 28.87 ? 193 THR A O 1 ATOM 1517 C CB . THR A 1 190 ? -25.210 1.076 70.505 1.00 29.72 ? 193 THR A CB 1 ATOM 1518 O OG1 . THR A 1 190 ? -25.772 1.121 69.188 1.00 33.61 ? 193 THR A OG1 1 ATOM 1519 C CG2 . THR A 1 190 ? -26.218 0.429 71.441 1.00 29.81 ? 193 THR A CG2 1 ATOM 1520 N N . LEU A 1 191 ? -24.096 3.677 68.945 1.00 28.55 ? 194 LEU A N 1 ATOM 1521 C CA . LEU A 1 191 ? -23.121 4.222 67.984 1.00 27.91 ? 194 LEU A CA 1 ATOM 1522 C C . LEU A 1 191 ? -22.567 5.607 68.328 1.00 28.24 ? 194 LEU A C 1 ATOM 1523 O O . LEU A 1 191 ? -21.381 5.863 68.107 1.00 28.41 ? 194 LEU A O 1 ATOM 1524 C CB . LEU A 1 191 ? -23.737 4.279 66.572 1.00 27.54 ? 194 LEU A CB 1 ATOM 1525 C CG . LEU A 1 191 ? -23.978 2.929 65.892 1.00 25.06 ? 194 LEU A CG 1 ATOM 1526 C CD1 . LEU A 1 191 ? -24.675 3.134 64.541 1.00 26.04 ? 194 LEU A CD1 1 ATOM 1527 C CD2 . LEU A 1 191 ? -22.667 2.174 65.742 1.00 25.27 ? 194 LEU A CD2 1 ATOM 1528 N N . TYR A 1 192 ? -23.418 6.497 68.852 1.00 28.05 ? 195 TYR A N 1 ATOM 1529 C CA . TYR A 1 192 ? -23.074 7.930 68.971 1.00 28.59 ? 195 TYR A CA 1 ATOM 1530 C C . TYR A 1 192 ? -23.230 8.522 70.360 1.00 30.19 ? 195 TYR A C 1 ATOM 1531 O O . TYR A 1 192 ? -22.743 9.626 70.597 1.00 31.00 ? 195 TYR A O 1 ATOM 1532 C CB . TYR A 1 192 ? -23.876 8.783 67.968 1.00 26.82 ? 195 TYR A CB 1 ATOM 1533 C CG . TYR A 1 192 ? -23.873 8.171 66.580 1.00 24.98 ? 195 TYR A CG 1 ATOM 1534 C CD1 . TYR A 1 192 ? -22.701 8.137 65.824 1.00 23.74 ? 195 TYR A CD1 1 ATOM 1535 C CD2 . TYR A 1 192 ? -25.035 7.624 66.027 1.00 24.43 ? 195 TYR A CD2 1 ATOM 1536 C CE1 . TYR A 1 192 ? -22.665 7.547 64.571 1.00 19.57 ? 195 TYR A CE1 1 ATOM 1537 C CE2 . TYR A 1 192 ? -25.010 7.025 64.747 1.00 22.29 ? 195 TYR A CE2 1 ATOM 1538 C CZ . TYR A 1 192 ? -23.817 7.005 64.033 1.00 23.68 ? 195 TYR A CZ 1 ATOM 1539 O OH . TYR A 1 192 ? -23.754 6.433 62.787 1.00 19.58 ? 195 TYR A OH 1 ATOM 1540 N N . GLN A 1 193 ? -23.930 7.800 71.242 1.00 31.79 ? 196 GLN A N 1 ATOM 1541 C CA . GLN A 1 193 ? -24.249 8.266 72.611 1.00 34.30 ? 196 GLN A CA 1 ATOM 1542 C C . GLN A 1 193 ? -25.120 9.517 72.671 1.00 34.85 ? 196 GLN A C 1 ATOM 1543 O O . GLN A 1 193 ? -25.906 9.679 73.615 1.00 37.02 ? 196 GLN A O 1 ATOM 1544 C CB . GLN A 1 193 ? -22.972 8.462 73.442 1.00 34.48 ? 196 GLN A CB 1 ATOM 1545 C CG . GLN A 1 193 ? -22.136 7.189 73.621 1.00 37.16 ? 196 GLN A CG 1 ATOM 1546 C CD . GLN A 1 193 ? -22.895 6.054 74.296 1.00 40.73 ? 196 GLN A CD 1 ATOM 1547 O OE1 . GLN A 1 193 ? -23.754 6.279 75.154 1.00 43.56 ? 196 GLN A OE1 1 ATOM 1548 N NE2 . GLN A 1 193 ? -22.572 4.823 73.917 1.00 43.01 ? 196 GLN A NE2 1 ATOM 1549 N N . ASN A 1 194 ? -24.976 10.397 71.681 1.00 35.16 ? 197 ASN A N 1 ATOM 1550 C CA . ASN A 1 194 ? -25.711 11.657 71.586 1.00 35.14 ? 197 ASN A CA 1 ATOM 1551 C C . ASN A 1 194 ? -27.049 11.530 70.833 1.00 35.10 ? 197 ASN A C 1 ATOM 1552 O O . ASN A 1 194 ? -27.228 10.642 69.981 1.00 34.68 ? 197 ASN A O 1 ATOM 1553 C CB . ASN A 1 194 ? -24.859 12.738 70.882 1.00 35.29 ? 197 ASN A CB 1 ATOM 1554 C CG . ASN A 1 194 ? -23.474 12.938 71.509 1.00 36.65 ? 197 ASN A CG 1 ATOM 1555 O OD1 . ASN A 1 194 ? -23.261 12.726 72.713 1.00 37.23 ? 197 ASN A OD1 1 ATOM 1556 N ND2 . ASN A 1 194 ? -22.524 13.375 70.686 1.00 36.98 ? 197 ASN A ND2 1 ATOM 1557 N N . VAL A 1 195 ? -27.959 12.455 71.127 1.00 34.64 ? 198 VAL A N 1 ATOM 1558 C CA . VAL A 1 195 ? -29.249 12.567 70.444 1.00 34.05 ? 198 VAL A CA 1 ATOM 1559 C C . VAL A 1 195 ? -29.417 13.980 69.897 1.00 33.49 ? 198 VAL A C 1 ATOM 1560 O O . VAL A 1 195 ? -28.760 14.912 70.366 1.00 34.36 ? 198 VAL A O 1 ATOM 1561 C CB . VAL A 1 195 ? -30.419 12.224 71.390 1.00 34.92 ? 198 VAL A CB 1 ATOM 1562 C CG1 . VAL A 1 195 ? -30.493 10.724 71.609 1.00 35.22 ? 198 VAL A CG1 1 ATOM 1563 C CG2 . VAL A 1 195 ? -30.274 12.967 72.732 1.00 35.33 ? 198 VAL A CG2 1 ATOM 1564 N N . GLY A 1 196 ? -30.280 14.148 68.902 1.00 32.26 ? 199 GLY A N 1 ATOM 1565 C CA . GLY A 1 196 ? -30.502 15.467 68.310 1.00 30.73 ? 199 GLY A CA 1 ATOM 1566 C C . GLY A 1 196 ? -29.208 15.925 67.658 1.00 29.84 ? 199 GLY A C 1 ATOM 1567 O O . GLY A 1 196 ? -28.805 17.075 67.764 1.00 30.36 ? 199 GLY A O 1 ATOM 1568 N N . THR A 1 197 ? -28.569 14.992 66.968 1.00 27.14 ? 200 THR A N 1 ATOM 1569 C CA . THR A 1 197 ? -27.266 15.253 66.370 1.00 24.56 ? 200 THR A CA 1 ATOM 1570 C C . THR A 1 197 ? -27.438 15.935 65.017 1.00 23.06 ? 200 THR A C 1 ATOM 1571 O O . THR A 1 197 ? -28.546 16.060 64.494 1.00 21.74 ? 200 THR A O 1 ATOM 1572 C CB . THR A 1 197 ? -26.505 13.938 66.210 1.00 25.12 ? 200 THR A CB 1 ATOM 1573 O OG1 . THR A 1 197 ? -27.292 13.079 65.391 1.00 22.17 ? 200 THR A OG1 1 ATOM 1574 C CG2 . THR A 1 197 ? -26.271 13.255 67.547 1.00 24.82 ? 200 THR A CG2 1 ATOM 1575 N N . TYR A 1 198 ? -26.334 16.371 64.405 1.00 22.63 ? 201 TYR A N 1 ATOM 1576 C CA . TYR A 1 198 ? -26.385 16.998 63.106 1.00 23.05 ? 201 TYR A CA 1 ATOM 1577 C C . TYR A 1 198 ? -25.066 16.742 62.372 1.00 21.43 ? 201 TYR A C 1 ATOM 1578 O O . TYR A 1 198 ? -24.058 16.404 62.999 1.00 22.87 ? 201 TYR A O 1 ATOM 1579 C CB . TYR A 1 198 ? -26.561 18.544 63.223 1.00 25.25 ? 201 TYR A CB 1 ATOM 1580 C CG . TYR A 1 198 ? -25.391 19.181 63.959 1.00 29.63 ? 201 TYR A CG 1 ATOM 1581 C CD1 . TYR A 1 198 ? -24.297 19.708 63.267 1.00 29.73 ? 201 TYR A CD1 1 ATOM 1582 C CD2 . TYR A 1 198 ? -25.352 19.202 65.369 1.00 30.95 ? 201 TYR A CD2 1 ATOM 1583 C CE1 . TYR A 1 198 ? -23.194 20.254 63.962 1.00 31.48 ? 201 TYR A CE1 1 ATOM 1584 C CE2 . TYR A 1 198 ? -24.280 19.737 66.064 1.00 32.00 ? 201 TYR A CE2 1 ATOM 1585 C CZ . TYR A 1 198 ? -23.198 20.261 65.369 1.00 32.27 ? 201 TYR A CZ 1 ATOM 1586 O OH . TYR A 1 198 ? -22.152 20.783 66.108 1.00 32.78 ? 201 TYR A OH 1 ATOM 1587 N N . VAL A 1 199 ? -25.116 16.907 61.055 1.00 21.82 ? 202 VAL A N 1 ATOM 1588 C CA . VAL A 1 199 ? -23.930 16.913 60.206 1.00 21.65 ? 202 VAL A CA 1 ATOM 1589 C C . VAL A 1 199 ? -23.935 18.197 59.389 1.00 21.12 ? 202 VAL A C 1 ATOM 1590 O O . VAL A 1 199 ? -24.845 18.395 58.569 1.00 22.59 ? 202 VAL A O 1 ATOM 1591 C CB . VAL A 1 199 ? -23.909 15.708 59.250 1.00 22.09 ? 202 VAL A CB 1 ATOM 1592 C CG1 . VAL A 1 199 ? -22.683 15.805 58.354 1.00 21.06 ? 202 VAL A CG1 1 ATOM 1593 C CG2 . VAL A 1 199 ? -23.909 14.382 60.066 1.00 21.55 ? 202 VAL A CG2 1 ATOM 1594 N N . SER A 1 200 ? -22.917 19.055 59.584 1.00 20.47 ? 203 SER A N 1 ATOM 1595 C CA A SER A 1 200 ? -22.808 20.278 58.789 0.50 18.95 ? 203 SER A CA 1 ATOM 1596 C CA B SER A 1 200 ? -22.793 20.292 58.826 0.50 19.61 ? 203 SER A CA 1 ATOM 1597 C C . SER A 1 200 ? -21.586 20.265 57.875 1.00 19.22 ? 203 SER A C 1 ATOM 1598 O O . SER A 1 200 ? -20.496 19.812 58.268 1.00 19.48 ? 203 SER A O 1 ATOM 1599 C CB A SER A 1 200 ? -22.810 21.572 59.650 0.50 19.45 ? 203 SER A CB 1 ATOM 1600 C CB B SER A 1 200 ? -22.670 21.503 59.780 0.50 20.26 ? 203 SER A CB 1 ATOM 1601 O OG A SER A 1 200 ? -24.038 22.273 59.514 0.50 17.88 ? 203 SER A OG 1 ATOM 1602 O OG B SER A 1 200 ? -21.536 21.359 60.631 0.50 22.11 ? 203 SER A OG 1 ATOM 1603 N N . VAL A 1 201 ? -21.791 20.723 56.641 1.00 19.39 ? 204 VAL A N 1 ATOM 1604 C CA . VAL A 1 201 ? -20.726 20.834 55.650 1.00 19.89 ? 204 VAL A CA 1 ATOM 1605 C C . VAL A 1 201 ? -20.773 22.234 55.025 1.00 20.66 ? 204 VAL A C 1 ATOM 1606 O O . VAL A 1 201 ? -21.863 22.761 54.677 1.00 20.33 ? 204 VAL A O 1 ATOM 1607 C CB . VAL A 1 201 ? -20.853 19.771 54.560 1.00 20.74 ? 204 VAL A CB 1 ATOM 1608 C CG1 . VAL A 1 201 ? -19.639 19.794 53.618 1.00 21.32 ? 204 VAL A CG1 1 ATOM 1609 C CG2 . VAL A 1 201 ? -21.042 18.390 55.186 1.00 22.09 ? 204 VAL A CG2 1 ATOM 1610 N N . GLY A 1 202 ? -19.595 22.844 54.876 1.00 19.79 ? 205 GLY A N 1 ATOM 1611 C CA . GLY A 1 202 ? -19.526 24.235 54.416 1.00 19.07 ? 205 GLY A CA 1 ATOM 1612 C C . GLY A 1 202 ? -18.271 24.476 53.619 1.00 18.46 ? 205 GLY A C 1 ATOM 1613 O O . GLY A 1 202 ? -17.170 24.003 53.998 1.00 18.71 ? 205 GLY A O 1 ATOM 1614 N N . THR A 1 203 ? -18.454 25.126 52.484 1.00 18.02 ? 206 THR A N 1 ATOM 1615 C CA . THR A 1 203 ? -17.357 25.624 51.667 1.00 17.47 ? 206 THR A CA 1 ATOM 1616 C C . THR A 1 203 ? -17.640 27.121 51.500 1.00 17.75 ? 206 THR A C 1 ATOM 1617 O O . THR A 1 203 ? -18.488 27.634 52.238 1.00 17.03 ? 206 THR A O 1 ATOM 1618 C CB . THR A 1 203 ? -17.243 24.920 50.292 1.00 17.80 ? 206 THR A CB 1 ATOM 1619 O OG1 . THR A 1 203 ? -18.351 25.299 49.437 1.00 18.78 ? 206 THR A OG1 1 ATOM 1620 C CG2 . THR A 1 203 ? -17.132 23.329 50.452 1.00 18.39 ? 206 THR A CG2 1 ATOM 1621 N N . SER A 1 204 ? -16.951 27.789 50.575 1.00 17.01 ? 207 SER A N 1 ATOM 1622 C CA A SER A 1 204 ? -17.247 29.205 50.320 0.50 17.79 ? 207 SER A CA 1 ATOM 1623 C CA B SER A 1 204 ? -17.236 29.204 50.271 0.50 18.64 ? 207 SER A CA 1 ATOM 1624 C C . SER A 1 204 ? -18.644 29.359 49.704 1.00 19.25 ? 207 SER A C 1 ATOM 1625 O O . SER A 1 204 ? -19.294 30.384 49.912 1.00 19.61 ? 207 SER A O 1 ATOM 1626 C CB A SER A 1 204 ? -16.156 29.867 49.463 0.50 17.91 ? 207 SER A CB 1 ATOM 1627 C CB B SER A 1 204 ? -16.209 29.777 49.286 0.50 18.90 ? 207 SER A CB 1 ATOM 1628 O OG A SER A 1 204 ? -14.935 30.005 50.190 0.50 13.70 ? 207 SER A OG 1 ATOM 1629 O OG B SER A 1 204 ? -16.323 29.170 48.006 0.50 19.89 ? 207 SER A OG 1 ATOM 1630 N N . THR A 1 205 ? -19.118 28.321 49.001 1.00 20.36 ? 208 THR A N 1 ATOM 1631 C CA . THR A 1 205 ? -20.401 28.403 48.256 1.00 23.18 ? 208 THR A CA 1 ATOM 1632 C C . THR A 1 205 ? -21.474 27.432 48.735 1.00 23.42 ? 208 THR A C 1 ATOM 1633 O O . THR A 1 205 ? -22.678 27.668 48.529 1.00 25.54 ? 208 THR A O 1 ATOM 1634 C CB . THR A 1 205 ? -20.169 28.223 46.749 1.00 23.37 ? 208 THR A CB 1 ATOM 1635 O OG1 . THR A 1 205 ? -19.514 26.965 46.516 1.00 26.67 ? 208 THR A OG1 1 ATOM 1636 C CG2 . THR A 1 205 ? -19.282 29.321 46.201 1.00 26.60 ? 208 THR A CG2 1 ATOM 1637 N N . LEU A 1 206 ? -21.072 26.349 49.388 1.00 22.41 ? 209 LEU A N 1 ATOM 1638 C CA . LEU A 1 206 ? -22.020 25.351 49.863 1.00 23.13 ? 209 LEU A CA 1 ATOM 1639 C C . LEU A 1 206 ? -22.218 25.434 51.365 1.00 21.92 ? 209 LEU A C 1 ATOM 1640 O O . LEU A 1 206 ? -21.286 25.619 52.146 1.00 20.50 ? 209 LEU A O 1 ATOM 1641 C CB . LEU A 1 206 ? -21.582 23.949 49.413 1.00 23.50 ? 209 LEU A CB 1 ATOM 1642 C CG . LEU A 1 206 ? -22.492 22.783 49.745 1.00 25.48 ? 209 LEU A CG 1 ATOM 1643 C CD1 . LEU A 1 206 ? -23.866 22.953 49.056 1.00 27.50 ? 209 LEU A CD1 1 ATOM 1644 C CD2 . LEU A 1 206 ? -21.757 21.493 49.330 1.00 25.49 ? 209 LEU A CD2 1 ATOM 1645 N N . ASN A 1 207 ? -23.473 25.374 51.772 1.00 20.82 ? 210 ASN A N 1 ATOM 1646 C CA . ASN A 1 207 ? -23.789 25.286 53.162 1.00 22.27 ? 210 ASN A CA 1 ATOM 1647 C C . ASN A 1 207 ? -24.902 24.271 53.237 1.00 24.03 ? 210 ASN A C 1 ATOM 1648 O O . ASN A 1 207 ? -26.018 24.561 52.913 1.00 24.06 ? 210 ASN A O 1 ATOM 1649 C CB . ASN A 1 207 ? -24.247 26.645 53.728 1.00 22.77 ? 210 ASN A CB 1 ATOM 1650 C CG . ASN A 1 207 ? -24.817 26.504 55.136 1.00 25.80 ? 210 ASN A CG 1 ATOM 1651 O OD1 . ASN A 1 207 ? -24.139 26.004 56.038 1.00 25.83 ? 210 ASN A OD1 1 ATOM 1652 N ND2 . ASN A 1 207 ? -26.085 26.882 55.313 1.00 27.54 ? 210 ASN A ND2 1 ATOM 1653 N N . LYS A 1 208 ? -24.599 23.059 53.648 1.00 25.49 ? 211 LYS A N 1 ATOM 1654 C CA . LYS A 1 208 ? -25.636 22.038 53.564 1.00 27.86 ? 211 LYS A CA 1 ATOM 1655 C C . LYS A 1 208 ? -25.623 21.364 54.885 1.00 29.02 ? 211 LYS A C 1 ATOM 1656 O O . LYS A 1 208 ? -24.590 20.845 55.305 1.00 30.47 ? 211 LYS A O 1 ATOM 1657 C CB . LYS A 1 208 ? -25.298 21.030 52.461 1.00 28.24 ? 211 LYS A CB 1 ATOM 1658 C CG . LYS A 1 208 ? -26.437 20.059 52.087 1.00 29.96 ? 211 LYS A CG 1 ATOM 1659 C CD . LYS A 1 208 ? -25.990 19.134 50.912 1.00 28.72 ? 211 LYS A CD 1 ATOM 1660 C CE . LYS A 1 208 ? -27.157 18.249 50.437 1.00 35.21 ? 211 LYS A CE 1 ATOM 1661 N NZ . LYS A 1 208 ? -27.160 16.927 51.123 1.00 36.73 ? 211 LYS A NZ 1 ATOM 1662 N N . ARG A 1 209 ? -26.759 21.311 55.551 1.00 29.63 ? 212 ARG A N 1 ATOM 1663 C CA . ARG A 1 209 ? -26.774 20.509 56.748 1.00 30.09 ? 212 ARG A CA 1 ATOM 1664 C C . ARG A 1 209 ? -27.794 19.373 56.788 1.00 31.76 ? 212 ARG A C 1 ATOM 1665 O O . ARG A 1 209 ? -28.679 19.290 55.906 1.00 31.97 ? 212 ARG A O 1 ATOM 1666 C CB . ARG A 1 209 ? -26.916 21.381 57.967 1.00 29.23 ? 212 ARG A CB 1 ATOM 1667 C CG . ARG A 1 209 ? -27.535 20.596 59.089 1.00 29.51 ? 212 ARG A CG 1 ATOM 1668 C CD . ARG A 1 209 ? -27.728 21.414 60.281 1.00 29.06 ? 212 ARG A CD 1 ATOM 1669 N NE . ARG A 1 209 ? -26.529 22.155 60.569 1.00 28.81 ? 212 ARG A NE 1 ATOM 1670 C CZ . ARG A 1 209 ? -26.441 22.974 61.604 1.00 31.48 ? 212 ARG A CZ 1 ATOM 1671 N NH1 . ARG A 1 209 ? -27.505 23.096 62.381 1.00 31.56 ? 212 ARG A NH1 1 ATOM 1672 N NH2 . ARG A 1 209 ? -25.314 23.643 61.852 1.00 28.11 ? 212 ARG A NH2 1 ATOM 1673 N N . SER A 1 210 ? -27.683 18.556 57.856 1.00 32.03 ? 213 SER A N 1 ATOM 1674 C CA . SER A 1 210 ? -28.571 17.395 58.112 1.00 31.77 ? 213 SER A CA 1 ATOM 1675 C C . SER A 1 210 ? -28.772 16.978 59.570 1.00 31.29 ? 213 SER A C 1 ATOM 1676 O O . SER A 1 210 ? -27.856 17.013 60.390 1.00 30.67 ? 213 SER A O 1 ATOM 1677 C CB . SER A 1 210 ? -28.030 16.208 57.377 1.00 31.81 ? 213 SER A CB 1 ATOM 1678 O OG . SER A 1 210 ? -27.669 16.615 56.084 1.00 33.98 ? 213 SER A OG 1 ATOM 1679 N N . THR A 1 211 ? -29.997 16.542 59.872 1.00 29.87 ? 214 THR A N 1 ATOM 1680 C CA . THR A 1 211 ? -30.271 15.922 61.144 1.00 29.92 ? 214 THR A CA 1 ATOM 1681 C C . THR A 1 211 ? -30.660 14.498 60.710 1.00 27.67 ? 214 THR A C 1 ATOM 1682 O O . THR A 1 211 ? -31.436 14.314 59.767 1.00 28.63 ? 214 THR A O 1 ATOM 1683 C CB . THR A 1 211 ? -31.422 16.570 61.918 1.00 30.35 ? 214 THR A CB 1 ATOM 1684 O OG1 . THR A 1 211 ? -32.519 16.688 61.050 1.00 32.39 ? 214 THR A OG1 1 ATOM 1685 C CG2 . THR A 1 211 ? -31.042 18.003 62.460 1.00 32.01 ? 214 THR A CG2 1 ATOM 1686 N N . PRO A 1 212 ? -30.036 13.509 61.337 1.00 26.56 ? 215 PRO A N 1 ATOM 1687 C CA . PRO A 1 212 ? -30.335 12.110 61.081 1.00 24.18 ? 215 PRO A CA 1 ATOM 1688 C C . PRO A 1 212 ? -31.783 11.831 61.416 1.00 23.84 ? 215 PRO A C 1 ATOM 1689 O O . PRO A 1 212 ? -32.356 12.482 62.316 1.00 23.34 ? 215 PRO A O 1 ATOM 1690 C CB . PRO A 1 212 ? -29.408 11.365 62.037 1.00 24.66 ? 215 PRO A CB 1 ATOM 1691 C CG . PRO A 1 212 ? -28.368 12.352 62.454 1.00 25.92 ? 215 PRO A CG 1 ATOM 1692 C CD . PRO A 1 212 ? -28.989 13.697 62.356 1.00 26.27 ? 215 PRO A CD 1 ATOM 1693 N N . GLU A 1 213 ? -32.370 10.877 60.705 1.00 22.08 ? 216 GLU A N 1 ATOM 1694 C CA . GLU A 1 213 ? -33.758 10.518 60.923 1.00 22.51 ? 216 GLU A CA 1 ATOM 1695 C C . GLU A 1 213 ? -33.749 9.083 61.422 1.00 22.83 ? 216 GLU A C 1 ATOM 1696 O O . GLU A 1 213 ? -33.279 8.188 60.726 1.00 23.72 ? 216 GLU A O 1 ATOM 1697 C CB . GLU A 1 213 ? -34.527 10.602 59.610 1.00 22.22 ? 216 GLU A CB 1 ATOM 1698 C CG . GLU A 1 213 ? -34.476 11.986 59.000 1.00 25.03 ? 216 GLU A CG 1 ATOM 1699 C CD . GLU A 1 213 ? -34.987 12.069 57.591 1.00 28.68 ? 216 GLU A CD 1 ATOM 1700 O OE1 . GLU A 1 213 ? -35.538 11.074 57.068 1.00 33.23 ? 216 GLU A OE1 1 ATOM 1701 O OE2 . GLU A 1 213 ? -34.874 13.174 57.004 1.00 32.30 ? 216 GLU A OE2 1 ATOM 1702 N N . ILE A 1 214 ? -34.211 8.890 62.651 1.00 21.84 ? 217 ILE A N 1 ATOM 1703 C CA . ILE A 1 214 ? -34.436 7.548 63.175 1.00 21.18 ? 217 ILE A CA 1 ATOM 1704 C C . ILE A 1 214 ? -35.849 7.050 62.841 1.00 21.20 ? 217 ILE A C 1 ATOM 1705 O O . ILE A 1 214 ? -36.853 7.708 63.164 1.00 21.40 ? 217 ILE A O 1 ATOM 1706 C CB . ILE A 1 214 ? -34.230 7.554 64.690 1.00 21.54 ? 217 ILE A CB 1 ATOM 1707 C CG1 . ILE A 1 214 ? -32.786 7.972 65.013 1.00 20.96 ? 217 ILE A CG1 1 ATOM 1708 C CG2 . ILE A 1 214 ? -34.532 6.175 65.247 1.00 22.13 ? 217 ILE A CG2 1 ATOM 1709 C CD1 . ILE A 1 214 ? -32.585 8.475 66.443 1.00 26.12 ? 217 ILE A CD1 1 ATOM 1710 N N . ALA A 1 215 ? -35.949 5.892 62.204 1.00 20.53 ? 218 ALA A N 1 ATOM 1711 C CA . ALA A 1 215 ? -37.256 5.370 61.788 1.00 22.43 ? 218 ALA A CA 1 ATOM 1712 C C . ALA A 1 215 ? -37.104 3.936 61.317 1.00 22.78 ? 218 ALA A C 1 ATOM 1713 O O . ALA A 1 215 ? -36.149 3.625 60.638 1.00 23.55 ? 218 ALA A O 1 ATOM 1714 C CB . ALA A 1 215 ? -37.841 6.233 60.638 1.00 20.96 ? 218 ALA A CB 1 ATOM 1715 N N . THR A 1 216 ? -38.092 3.091 61.643 1.00 24.28 ? 219 THR A N 1 ATOM 1716 C CA . THR A 1 216 ? -38.153 1.714 61.134 1.00 25.21 ? 219 THR A CA 1 ATOM 1717 C C . THR A 1 216 ? -38.518 1.701 59.633 1.00 24.78 ? 219 THR A C 1 ATOM 1718 O O . THR A 1 216 ? -39.514 2.285 59.216 1.00 26.71 ? 219 THR A O 1 ATOM 1719 C CB . THR A 1 216 ? -39.177 0.900 61.992 1.00 26.20 ? 219 THR A CB 1 ATOM 1720 O OG1 . THR A 1 216 ? -38.584 0.659 63.268 1.00 30.42 ? 219 THR A OG1 1 ATOM 1721 C CG2 . THR A 1 216 ? -39.565 -0.411 61.313 1.00 28.34 ? 219 THR A CG2 1 ATOM 1722 N N . ARG A 1 217 ? -37.675 1.072 58.817 1.00 22.29 ? 220 ARG A N 1 ATOM 1723 C CA . ARG A 1 217 ? -37.882 0.980 57.366 1.00 20.57 ? 220 ARG A CA 1 ATOM 1724 C C . ARG A 1 217 ? -37.735 -0.465 56.948 1.00 20.23 ? 220 ARG A C 1 ATOM 1725 O O . ARG A 1 217 ? -37.142 -1.256 57.704 1.00 17.75 ? 220 ARG A O 1 ATOM 1726 C CB . ARG A 1 217 ? -36.828 1.803 56.611 1.00 20.59 ? 220 ARG A CB 1 ATOM 1727 C CG . ARG A 1 217 ? -36.698 3.236 57.105 1.00 19.26 ? 220 ARG A CG 1 ATOM 1728 C CD . ARG A 1 217 ? -35.482 3.975 56.521 1.00 20.14 ? 220 ARG A CD 1 ATOM 1729 N NE . ARG A 1 217 ? -35.340 5.310 57.138 1.00 18.79 ? 220 ARG A NE 1 ATOM 1730 C CZ . ARG A 1 217 ? -34.608 5.574 58.226 1.00 19.92 ? 220 ARG A CZ 1 ATOM 1731 N NH1 . ARG A 1 217 ? -33.899 4.623 58.790 1.00 21.11 ? 220 ARG A NH1 1 ATOM 1732 N NH2 . ARG A 1 217 ? -34.568 6.809 58.727 1.00 22.03 ? 220 ARG A NH2 1 ATOM 1733 N N . PRO A 1 218 ? -38.240 -0.815 55.751 1.00 20.68 ? 221 PRO A N 1 ATOM 1734 C CA . PRO A 1 218 ? -38.081 -2.159 55.235 1.00 20.41 ? 221 PRO A CA 1 ATOM 1735 C C . PRO A 1 218 ? -36.613 -2.508 55.140 1.00 20.12 ? 221 PRO A C 1 ATOM 1736 O O . PRO A 1 218 ? -35.772 -1.647 54.851 1.00 18.79 ? 221 PRO A O 1 ATOM 1737 C CB . PRO A 1 218 ? -38.737 -2.083 53.850 1.00 21.04 ? 221 PRO A CB 1 ATOM 1738 C CG . PRO A 1 218 ? -39.697 -0.944 53.994 1.00 22.12 ? 221 PRO A CG 1 ATOM 1739 C CD . PRO A 1 218 ? -39.041 0.030 54.835 1.00 21.55 ? 221 PRO A CD 1 ATOM 1740 N N . LYS A 1 219 ? -36.291 -3.766 55.413 1.00 20.42 ? 222 LYS A N 1 ATOM 1741 C CA . LYS A 1 219 ? -34.900 -4.181 55.326 1.00 20.19 ? 222 LYS A CA 1 ATOM 1742 C C . LYS A 1 219 ? -34.385 -4.266 53.903 1.00 20.03 ? 222 LYS A C 1 ATOM 1743 O O . LYS A 1 219 ? -35.041 -4.840 53.018 1.00 19.59 ? 222 LYS A O 1 ATOM 1744 C CB . LYS A 1 219 ? -34.694 -5.524 56.055 1.00 21.61 ? 222 LYS A CB 1 ATOM 1745 C CG . LYS A 1 219 ? -34.855 -5.389 57.533 1.00 23.87 ? 222 LYS A CG 1 ATOM 1746 C CD . LYS A 1 219 ? -34.554 -6.730 58.195 1.00 31.32 ? 222 LYS A CD 1 ATOM 1747 C CE . LYS A 1 219 ? -34.817 -6.653 59.680 1.00 35.39 ? 222 LYS A CE 1 ATOM 1748 N NZ . LYS A 1 219 ? -33.819 -5.778 60.353 1.00 37.49 ? 222 LYS A NZ 1 ATOM 1749 N N . VAL A 1 220 ? -33.198 -3.682 53.689 1.00 18.62 ? 223 VAL A N 1 ATOM 1750 C CA . VAL A 1 220 ? -32.470 -3.787 52.431 1.00 19.22 ? 223 VAL A CA 1 ATOM 1751 C C . VAL A 1 220 ? -31.053 -4.235 52.782 1.00 19.70 ? 223 VAL A C 1 ATOM 1752 O O . VAL A 1 220 ? -30.410 -3.651 53.670 1.00 19.45 ? 223 VAL A O 1 ATOM 1753 C CB . VAL A 1 220 ? -32.412 -2.427 51.714 1.00 19.56 ? 223 VAL A CB 1 ATOM 1754 C CG1 . VAL A 1 220 ? -31.622 -2.508 50.396 1.00 20.16 ? 223 VAL A CG1 1 ATOM 1755 C CG2 . VAL A 1 220 ? -33.870 -1.911 51.458 1.00 19.17 ? 223 VAL A CG2 1 ATOM 1756 N N . ASN A 1 221 ? -30.578 -5.290 52.112 1.00 19.63 ? 224 ASN A N 1 ATOM 1757 C CA . ASN A 1 221 ? -29.277 -5.882 52.494 1.00 21.16 ? 224 ASN A CA 1 ATOM 1758 C C . ASN A 1 221 ? -29.233 -6.123 53.983 1.00 20.62 ? 224 ASN A C 1 ATOM 1759 O O . ASN A 1 221 ? -28.171 -5.985 54.599 1.00 22.49 ? 224 ASN A O 1 ATOM 1760 C CB . ASN A 1 221 ? -28.125 -4.956 52.108 1.00 21.55 ? 224 ASN A CB 1 ATOM 1761 C CG . ASN A 1 221 ? -28.037 -4.725 50.626 1.00 24.39 ? 224 ASN A CG 1 ATOM 1762 O OD1 . ASN A 1 221 ? -28.549 -5.514 49.834 1.00 25.81 ? 224 ASN A OD1 1 ATOM 1763 N ND2 . ASN A 1 221 ? -27.413 -3.623 50.240 1.00 24.77 ? 224 ASN A ND2 1 ATOM 1764 N N . GLY A 1 222 ? -30.377 -6.481 54.560 1.00 20.10 ? 225 GLY A N 1 ATOM 1765 C CA . GLY A 1 222 ? -30.537 -6.766 56.003 1.00 20.31 ? 225 GLY A CA 1 ATOM 1766 C C . GLY A 1 222 ? -30.774 -5.619 56.977 1.00 19.90 ? 225 GLY A C 1 ATOM 1767 O O . GLY A 1 222 ? -30.950 -5.848 58.190 1.00 21.18 ? 225 GLY A O 1 ATOM 1768 N N . LEU A 1 223 ? -30.800 -4.379 56.477 1.00 18.54 ? 226 LEU A N 1 ATOM 1769 C CA . LEU A 1 223 ? -30.826 -3.222 57.373 1.00 17.30 ? 226 LEU A CA 1 ATOM 1770 C C . LEU A 1 223 ? -32.022 -2.336 57.109 1.00 16.01 ? 226 LEU A C 1 ATOM 1771 O O . LEU A 1 223 ? -32.292 -2.071 55.941 1.00 16.46 ? 226 LEU A O 1 ATOM 1772 C CB . LEU A 1 223 ? -29.590 -2.382 57.126 1.00 17.08 ? 226 LEU A CB 1 ATOM 1773 C CG . LEU A 1 223 ? -28.312 -3.108 57.527 1.00 18.27 ? 226 LEU A CG 1 ATOM 1774 C CD1 . LEU A 1 223 ? -27.124 -2.405 56.939 1.00 16.91 ? 226 LEU A CD1 1 ATOM 1775 C CD2 . LEU A 1 223 ? -28.204 -3.236 59.054 1.00 23.07 ? 226 LEU A CD2 1 ATOM 1776 N N . GLY A 1 224 ? -32.670 -1.887 58.175 1.00 16.01 ? 227 GLY A N 1 ATOM 1777 C CA . GLY A 1 224 ? -33.713 -0.815 58.115 1.00 16.29 ? 227 GLY A CA 1 ATOM 1778 C C . GLY A 1 224 ? -33.125 0.599 58.202 1.00 16.04 ? 227 GLY A C 1 ATOM 1779 O O . GLY A 1 224 ? -33.841 1.591 58.060 1.00 17.77 ? 227 GLY A O 1 ATOM 1780 N N . SER A 1 225 ? -31.838 0.679 58.543 1.00 15.44 ? 228 SER A N 1 ATOM 1781 C CA A SER A 1 225 ? -31.088 1.945 58.586 0.50 15.11 ? 228 SER A CA 1 ATOM 1782 C CA B SER A 1 225 ? -31.132 1.965 58.585 0.50 14.12 ? 228 SER A CA 1 ATOM 1783 C C . SER A 1 225 ? -30.680 2.349 57.177 1.00 14.15 ? 228 SER A C 1 ATOM 1784 O O . SER A 1 225 ? -30.791 1.548 56.245 1.00 13.77 ? 228 SER A O 1 ATOM 1785 C CB A SER A 1 225 ? -29.813 1.787 59.421 0.50 15.36 ? 228 SER A CB 1 ATOM 1786 C CB B SER A 1 225 ? -29.919 1.864 59.507 0.50 14.30 ? 228 SER A CB 1 ATOM 1787 O OG A SER A 1 225 ? -30.085 1.298 60.719 0.50 18.26 ? 228 SER A OG 1 ATOM 1788 O OG B SER A 1 225 ? -29.251 0.641 59.274 0.50 11.25 ? 228 SER A OG 1 ATOM 1789 N N . ARG A 1 226 ? -30.200 3.584 57.021 1.00 13.77 ? 229 ARG A N 1 ATOM 1790 C CA . ARG A 1 226 ? -29.787 4.059 55.714 1.00 13.74 ? 229 ARG A CA 1 ATOM 1791 C C . ARG A 1 226 ? -28.609 4.990 55.839 1.00 14.56 ? 229 ARG A C 1 ATOM 1792 O O . ARG A 1 226 ? -28.430 5.615 56.887 1.00 15.43 ? 229 ARG A O 1 ATOM 1793 C CB . ARG A 1 226 ? -30.945 4.869 55.044 1.00 13.99 ? 229 ARG A CB 1 ATOM 1794 C CG . ARG A 1 226 ? -32.272 4.094 54.862 1.00 14.76 ? 229 ARG A CG 1 ATOM 1795 C CD . ARG A 1 226 ? -32.194 3.069 53.760 1.00 14.41 ? 229 ARG A CD 1 ATOM 1796 N NE . ARG A 1 226 ? -33.515 2.443 53.497 1.00 14.80 ? 229 ARG A NE 1 ATOM 1797 C CZ . ARG A 1 226 ? -33.885 1.221 53.897 1.00 19.43 ? 229 ARG A CZ 1 ATOM 1798 N NH1 . ARG A 1 226 ? -33.075 0.456 54.640 1.00 18.36 ? 229 ARG A NH1 1 ATOM 1799 N NH2 . ARG A 1 226 ? -35.100 0.753 53.557 1.00 16.09 ? 229 ARG A NH2 1 ATOM 1800 N N . MET A 1 227 ? -27.845 5.097 54.754 1.00 13.65 ? 230 MET A N 1 ATOM 1801 C CA . MET A 1 227 ? -26.849 6.167 54.663 1.00 14.19 ? 230 MET A CA 1 ATOM 1802 C C . MET A 1 227 ? -27.156 7.011 53.441 1.00 14.46 ? 230 MET A C 1 ATOM 1803 O O . MET A 1 227 ? -27.359 6.505 52.346 1.00 15.31 ? 230 MET A O 1 ATOM 1804 C CB . MET A 1 227 ? -25.445 5.558 54.595 1.00 14.73 ? 230 MET A CB 1 ATOM 1805 C CG . MET A 1 227 ? -24.965 5.146 55.968 1.00 15.93 ? 230 MET A CG 1 ATOM 1806 S SD . MET A 1 227 ? -23.293 4.454 55.887 1.00 18.18 ? 230 MET A SD 1 ATOM 1807 C CE . MET A 1 227 ? -23.302 3.814 57.564 1.00 19.04 ? 230 MET A CE 1 ATOM 1808 N N . GLU A 1 228 ? -27.228 8.307 53.666 1.00 13.09 ? 231 GLU A N 1 ATOM 1809 C CA . GLU A 1 228 ? -27.574 9.263 52.622 1.00 14.85 ? 231 GLU A CA 1 ATOM 1810 C C . GLU A 1 228 ? -26.325 10.051 52.260 1.00 14.49 ? 231 GLU A C 1 ATOM 1811 O O . GLU A 1 228 ? -25.826 10.814 53.083 1.00 14.24 ? 231 GLU A O 1 ATOM 1812 C CB . GLU A 1 228 ? -28.681 10.227 53.130 1.00 15.79 ? 231 GLU A CB 1 ATOM 1813 C CG . GLU A 1 228 ? -28.996 11.342 52.137 1.00 16.30 ? 231 GLU A CG 1 ATOM 1814 C CD . GLU A 1 228 ? -29.992 12.376 52.661 1.00 19.26 ? 231 GLU A CD 1 ATOM 1815 O OE1 . GLU A 1 228 ? -30.697 12.078 53.661 1.00 21.32 ? 231 GLU A OE1 1 ATOM 1816 O OE2 . GLU A 1 228 ? -30.039 13.498 52.079 1.00 20.95 ? 231 GLU A OE2 1 ATOM 1817 N N . PHE A 1 229 ? -25.859 9.886 51.032 1.00 15.02 ? 232 PHE A N 1 ATOM 1818 C CA . PHE A 1 229 ? -24.614 10.533 50.567 1.00 14.26 ? 232 PHE A CA 1 ATOM 1819 C C . PHE A 1 229 ? -24.916 11.778 49.776 1.00 14.52 ? 232 PHE A C 1 ATOM 1820 O O . PHE A 1 229 ? -25.958 11.873 49.094 1.00 15.09 ? 232 PHE A O 1 ATOM 1821 C CB . PHE A 1 229 ? -23.760 9.563 49.759 1.00 15.17 ? 232 PHE A CB 1 ATOM 1822 C CG . PHE A 1 229 ? -23.273 8.423 50.580 1.00 14.23 ? 232 PHE A CG 1 ATOM 1823 C CD1 . PHE A 1 229 ? -22.178 8.585 51.458 1.00 15.03 ? 232 PHE A CD1 1 ATOM 1824 C CD2 . PHE A 1 229 ? -23.987 7.213 50.582 1.00 14.47 ? 232 PHE A CD2 1 ATOM 1825 C CE1 . PHE A 1 229 ? -21.711 7.486 52.303 1.00 15.56 ? 232 PHE A CE1 1 ATOM 1826 C CE2 . PHE A 1 229 ? -23.532 6.115 51.428 1.00 17.46 ? 232 PHE A CE2 1 ATOM 1827 C CZ . PHE A 1 229 ? -22.407 6.273 52.280 1.00 16.11 ? 232 PHE A CZ 1 ATOM 1828 N N . SER A 1 230 ? -24.019 12.746 49.895 1.00 15.01 ? 233 SER A N 1 ATOM 1829 C CA . SER A 1 230 ? -24.066 13.976 49.099 1.00 15.02 ? 233 SER A CA 1 ATOM 1830 C C . SER A 1 230 ? -22.655 14.267 48.573 1.00 15.39 ? 233 SER A C 1 ATOM 1831 O O . SER A 1 230 ? -21.689 13.682 49.029 1.00 15.26 ? 233 SER A O 1 ATOM 1832 C CB . SER A 1 230 ? -24.509 15.151 49.979 1.00 16.11 ? 233 SER A CB 1 ATOM 1833 O OG . SER A 1 230 ? -25.827 14.954 50.516 1.00 17.40 ? 233 SER A OG 1 ATOM 1834 N N . TRP A 1 231 ? -22.535 15.211 47.650 1.00 14.83 ? 234 TRP A N 1 ATOM 1835 C CA . TRP A 1 231 ? -21.192 15.502 47.104 1.00 15.87 ? 234 TRP A CA 1 ATOM 1836 C C . TRP A 1 231 ? -21.074 16.933 46.692 1.00 16.69 ? 234 TRP A C 1 ATOM 1837 O O . TRP A 1 231 ? -22.081 17.652 46.512 1.00 17.72 ? 234 TRP A O 1 ATOM 1838 C CB . TRP A 1 231 ? -20.941 14.606 45.905 1.00 16.80 ? 234 TRP A CB 1 ATOM 1839 C CG . TRP A 1 231 ? -21.827 14.872 44.725 1.00 17.05 ? 234 TRP A CG 1 ATOM 1840 C CD1 . TRP A 1 231 ? -23.130 14.413 44.508 1.00 20.04 ? 234 TRP A CD1 1 ATOM 1841 C CD2 . TRP A 1 231 ? -21.498 15.666 43.577 1.00 17.82 ? 234 TRP A CD2 1 ATOM 1842 N NE1 . TRP A 1 231 ? -23.587 14.895 43.310 1.00 19.88 ? 234 TRP A NE1 1 ATOM 1843 C CE2 . TRP A 1 231 ? -22.629 15.659 42.718 1.00 21.03 ? 234 TRP A CE2 1 ATOM 1844 C CE3 . TRP A 1 231 ? -20.368 16.387 43.196 1.00 22.61 ? 234 TRP A CE3 1 ATOM 1845 C CZ2 . TRP A 1 231 ? -22.642 16.346 41.514 1.00 20.84 ? 234 TRP A CZ2 1 ATOM 1846 C CZ3 . TRP A 1 231 ? -20.370 17.043 41.973 1.00 23.16 ? 234 TRP A CZ3 1 ATOM 1847 C CH2 . TRP A 1 231 ? -21.510 17.025 41.156 1.00 22.39 ? 234 TRP A CH2 1 ATOM 1848 N N . THR A 1 232 ? -19.840 17.369 46.528 1.00 17.39 ? 235 THR A N 1 ATOM 1849 C CA . THR A 1 232 ? -19.624 18.721 46.033 1.00 17.05 ? 235 THR A CA 1 ATOM 1850 C C . THR A 1 232 ? -18.339 18.700 45.247 1.00 17.85 ? 235 THR A C 1 ATOM 1851 O O . THR A 1 232 ? -17.534 17.765 45.383 1.00 16.40 ? 235 THR A O 1 ATOM 1852 C CB . THR A 1 232 ? -19.530 19.735 47.191 1.00 19.17 ? 235 THR A CB 1 ATOM 1853 O OG1 . THR A 1 232 ? -19.588 21.080 46.653 1.00 21.26 ? 235 THR A OG1 1 ATOM 1854 C CG2 . THR A 1 232 ? -18.183 19.573 47.982 1.00 19.60 ? 235 THR A CG2 1 ATOM 1855 N N . LEU A 1 233 ? -18.167 19.706 44.389 1.00 18.17 ? 236 LEU A N 1 ATOM 1856 C CA A LEU A 1 233 ? -16.882 19.925 43.753 0.50 19.08 ? 236 LEU A CA 1 ATOM 1857 C CA B LEU A 1 233 ? -16.869 19.961 43.767 0.50 18.70 ? 236 LEU A CA 1 ATOM 1858 C C . LEU A 1 233 ? -16.202 21.084 44.523 1.00 19.57 ? 236 LEU A C 1 ATOM 1859 O O . LEU A 1 233 ? -16.736 22.202 44.608 1.00 19.86 ? 236 LEU A O 1 ATOM 1860 C CB A LEU A 1 233 ? -17.097 20.195 42.252 0.50 19.93 ? 236 LEU A CB 1 ATOM 1861 C CB B LEU A 1 233 ? -17.021 20.388 42.317 0.50 19.89 ? 236 LEU A CB 1 ATOM 1862 C CG A LEU A 1 233 ? -16.009 20.119 41.171 0.50 20.29 ? 236 LEU A CG 1 ATOM 1863 C CG B LEU A 1 233 ? -17.519 19.338 41.349 0.50 17.76 ? 236 LEU A CG 1 ATOM 1864 C CD1 A LEU A 1 233 ? -15.290 18.785 41.197 0.50 17.60 ? 236 LEU A CD1 1 ATOM 1865 C CD1 B LEU A 1 233 ? -17.503 19.884 39.934 0.50 20.56 ? 236 LEU A CD1 1 ATOM 1866 C CD2 A LEU A 1 233 ? -16.610 20.332 39.794 0.50 19.66 ? 236 LEU A CD2 1 ATOM 1867 C CD2 B LEU A 1 233 ? -16.641 18.081 41.471 0.50 19.78 ? 236 LEU A CD2 1 ATOM 1868 N N . LEU A 1 234 ? -15.054 20.801 45.132 1.00 17.85 ? 237 LEU A N 1 ATOM 1869 C CA . LEU A 1 234 ? -14.360 21.815 45.918 1.00 17.35 ? 237 LEU A CA 1 ATOM 1870 C C . LEU A 1 234 ? -13.417 22.550 44.972 1.00 18.49 ? 237 LEU A C 1 ATOM 1871 O O . LEU A 1 234 ? -12.545 21.963 44.320 1.00 17.30 ? 237 LEU A O 1 ATOM 1872 C CB . LEU A 1 234 ? -13.582 21.190 47.079 1.00 18.29 ? 237 LEU A CB 1 ATOM 1873 C CG . LEU A 1 234 ? -12.851 22.108 48.057 1.00 17.67 ? 237 LEU A CG 1 ATOM 1874 C CD1 . LEU A 1 234 ? -13.874 23.023 48.758 1.00 17.94 ? 237 LEU A CD1 1 ATOM 1875 C CD2 . LEU A 1 234 ? -12.112 21.322 49.110 1.00 16.70 ? 237 LEU A CD2 1 ATOM 1876 N N . ASP A 1 235 ? -13.606 23.861 44.864 1.00 18.13 ? 238 ASP A N 1 ATOM 1877 C CA . ASP A 1 235 ? -12.755 24.637 43.979 1.00 19.58 ? 238 ASP A CA 1 ATOM 1878 C C . ASP A 1 235 ? -11.300 24.715 44.443 1.00 19.16 ? 238 ASP A C 1 ATOM 1879 O O . ASP A 1 235 ? -11.005 24.575 45.632 1.00 17.95 ? 238 ASP A O 1 ATOM 1880 C CB . ASP A 1 235 ? -13.320 26.058 43.870 1.00 20.45 ? 238 ASP A CB 1 ATOM 1881 C CG . ASP A 1 235 ? -14.527 26.152 42.967 1.00 25.55 ? 238 ASP A CG 1 ATOM 1882 O OD1 . ASP A 1 235 ? -14.920 25.170 42.290 1.00 25.82 ? 238 ASP A OD1 1 ATOM 1883 O OD2 . ASP A 1 235 ? -15.095 27.274 42.932 1.00 32.51 ? 238 ASP A OD2 1 ATOM 1884 N N . MET A 1 236 ? -10.390 24.941 43.502 1.00 19.49 ? 239 MET A N 1 ATOM 1885 C CA . MET A 1 236 ? -8.997 25.184 43.864 1.00 21.99 ? 239 MET A CA 1 ATOM 1886 C C . MET A 1 236 ? -8.917 26.276 44.895 1.00 21.04 ? 239 MET A C 1 ATOM 1887 O O . MET A 1 236 ? -9.549 27.326 44.750 1.00 20.73 ? 239 MET A O 1 ATOM 1888 C CB . MET A 1 236 ? -8.155 25.555 42.655 1.00 20.96 ? 239 MET A CB 1 ATOM 1889 C CG . MET A 1 236 ? -8.010 24.443 41.657 1.00 25.28 ? 239 MET A CG 1 ATOM 1890 S SD . MET A 1 236 ? -7.136 24.957 40.188 1.00 31.44 ? 239 MET A SD 1 ATOM 1891 C CE . MET A 1 236 ? -8.421 25.809 39.308 1.00 33.07 ? 239 MET A CE 1 ATOM 1892 N N . TRP A 1 237 ? -8.149 25.996 45.935 1.00 20.56 ? 240 TRP A N 1 ATOM 1893 C CA . TRP A 1 237 ? -7.791 26.919 47.006 1.00 20.67 ? 240 TRP A CA 1 ATOM 1894 C C . TRP A 1 237 ? -8.962 27.218 47.963 1.00 19.47 ? 240 TRP A C 1 ATOM 1895 O O . TRP A 1 237 ? -8.809 28.049 48.859 1.00 19.21 ? 240 TRP A O 1 ATOM 1896 C CB . TRP A 1 237 ? -7.141 28.239 46.476 1.00 21.33 ? 240 TRP A CB 1 ATOM 1897 C CG . TRP A 1 237 ? -6.256 28.050 45.264 1.00 22.07 ? 240 TRP A CG 1 ATOM 1898 C CD1 . TRP A 1 237 ? -6.480 28.510 43.993 1.00 23.49 ? 240 TRP A CD1 1 ATOM 1899 C CD2 . TRP A 1 237 ? -5.046 27.300 45.209 1.00 21.84 ? 240 TRP A CD2 1 ATOM 1900 N NE1 . TRP A 1 237 ? -5.460 28.107 43.157 1.00 23.61 ? 240 TRP A NE1 1 ATOM 1901 C CE2 . TRP A 1 237 ? -4.570 27.359 43.880 1.00 23.21 ? 240 TRP A CE2 1 ATOM 1902 C CE3 . TRP A 1 237 ? -4.316 26.578 46.159 1.00 22.95 ? 240 TRP A CE3 1 ATOM 1903 C CZ2 . TRP A 1 237 ? -3.377 26.734 43.477 1.00 23.60 ? 240 TRP A CZ2 1 ATOM 1904 C CZ3 . TRP A 1 237 ? -3.138 25.959 45.769 1.00 24.36 ? 240 TRP A CZ3 1 ATOM 1905 C CH2 . TRP A 1 237 ? -2.679 26.038 44.427 1.00 24.17 ? 240 TRP A CH2 1 ATOM 1906 N N . ASP A 1 238 ? -10.114 26.559 47.750 1.00 18.88 ? 241 ASP A N 1 ATOM 1907 C CA . ASP A 1 238 ? -11.243 26.642 48.694 1.00 19.63 ? 241 ASP A CA 1 ATOM 1908 C C . ASP A 1 238 ? -11.096 25.546 49.754 1.00 19.38 ? 241 ASP A C 1 ATOM 1909 O O . ASP A 1 238 ? -10.402 24.534 49.538 1.00 19.08 ? 241 ASP A O 1 ATOM 1910 C CB . ASP A 1 238 ? -12.610 26.518 47.997 1.00 19.01 ? 241 ASP A CB 1 ATOM 1911 C CG . ASP A 1 238 ? -13.766 27.085 48.855 1.00 19.55 ? 241 ASP A CG 1 ATOM 1912 O OD1 . ASP A 1 238 ? -13.488 27.825 49.837 1.00 19.08 ? 241 ASP A OD1 1 ATOM 1913 O OD2 . ASP A 1 238 ? -14.931 26.788 48.534 1.00 20.17 ? 241 ASP A OD2 1 ATOM 1914 N N . THR A 1 239 ? -11.766 25.749 50.879 1.00 18.29 ? 242 THR A N 1 ATOM 1915 C CA . THR A 1 239 ? -11.719 24.852 52.016 1.00 17.69 ? 242 THR A CA 1 ATOM 1916 C C . THR A 1 239 ? -13.102 24.247 52.215 1.00 18.63 ? 242 THR A C 1 ATOM 1917 O O . THR A 1 239 ? -14.110 24.923 51.968 1.00 17.72 ? 242 THR A O 1 ATOM 1918 C CB . THR A 1 239 ? -11.228 25.608 53.241 1.00 18.68 ? 242 THR A CB 1 ATOM 1919 O OG1 . THR A 1 239 ? -9.858 25.957 53.035 1.00 18.43 ? 242 THR A OG1 1 ATOM 1920 C CG2 . THR A 1 239 ? -11.374 24.775 54.518 1.00 20.43 ? 242 THR A CG2 1 ATOM 1921 N N . ILE A 1 240 ? -13.133 22.969 52.604 1.00 16.84 ? 243 ILE A N 1 ATOM 1922 C CA . ILE A 1 240 ? -14.357 22.309 53.057 1.00 16.77 ? 243 ILE A CA 1 ATOM 1923 C C . ILE A 1 240 ? -14.248 22.014 54.549 1.00 16.92 ? 243 ILE A C 1 ATOM 1924 O O . ILE A 1 240 ? -13.181 21.589 55.039 1.00 15.94 ? 243 ILE A O 1 ATOM 1925 C CB . ILE A 1 240 ? -14.668 21.019 52.246 1.00 16.20 ? 243 ILE A CB 1 ATOM 1926 C CG1 . ILE A 1 240 ? -16.026 20.447 52.678 1.00 16.21 ? 243 ILE A CG1 1 ATOM 1927 C CG2 . ILE A 1 240 ? -13.503 19.943 52.355 1.00 16.91 ? 243 ILE A CG2 1 ATOM 1928 C CD1 . ILE A 1 240 ? -16.567 19.447 51.673 1.00 18.55 ? 243 ILE A CD1 1 ATOM 1929 N N . ASN A 1 241 ? -15.302 22.351 55.297 1.00 16.24 ? 244 ASN A N 1 ATOM 1930 C CA . ASN A 1 241 ? -15.342 22.111 56.740 1.00 16.43 ? 244 ASN A CA 1 ATOM 1931 C C . ASN A 1 241 ? -16.456 21.126 57.079 1.00 17.98 ? 244 ASN A C 1 ATOM 1932 O O . ASN A 1 241 ? -17.611 21.353 56.676 1.00 17.95 ? 244 ASN A O 1 ATOM 1933 C CB . ASN A 1 241 ? -15.578 23.439 57.520 1.00 18.06 ? 244 ASN A CB 1 ATOM 1934 C CG . ASN A 1 241 ? -14.426 24.443 57.314 1.00 17.33 ? 244 ASN A CG 1 ATOM 1935 O OD1 . ASN A 1 241 ? -13.297 24.059 56.983 1.00 27.70 ? 244 ASN A OD1 1 ATOM 1936 N ND2 . ASN A 1 241 ? -14.693 25.690 57.491 1.00 25.43 ? 244 ASN A ND2 1 ATOM 1937 N N . PHE A 1 242 ? -16.128 20.060 57.806 1.00 17.25 ? 245 PHE A N 1 ATOM 1938 C CA . PHE A 1 242 ? -17.128 19.107 58.309 1.00 18.12 ? 245 PHE A CA 1 ATOM 1939 C C . PHE A 1 242 ? -17.269 19.338 59.799 1.00 18.91 ? 245 PHE A C 1 ATOM 1940 O O . PHE A 1 242 ? -16.260 19.514 60.495 1.00 19.29 ? 245 PHE A O 1 ATOM 1941 C CB . PHE A 1 242 ? -16.625 17.672 58.064 1.00 17.64 ? 245 PHE A CB 1 ATOM 1942 C CG . PHE A 1 242 ? -16.615 17.313 56.635 1.00 18.24 ? 245 PHE A CG 1 ATOM 1943 C CD1 . PHE A 1 242 ? -17.782 16.870 56.033 1.00 15.96 ? 245 PHE A CD1 1 ATOM 1944 C CD2 . PHE A 1 242 ? -15.460 17.430 55.870 1.00 18.74 ? 245 PHE A CD2 1 ATOM 1945 C CE1 . PHE A 1 242 ? -17.807 16.551 54.659 1.00 19.81 ? 245 PHE A CE1 1 ATOM 1946 C CE2 . PHE A 1 242 ? -15.467 17.094 54.506 1.00 18.57 ? 245 PHE A CE2 1 ATOM 1947 C CZ . PHE A 1 242 ? -16.658 16.636 53.911 1.00 18.78 ? 245 PHE A CZ 1 ATOM 1948 N N . GLU A 1 243 ? -18.498 19.329 60.304 1.00 19.93 ? 246 GLU A N 1 ATOM 1949 C CA . GLU A 1 243 ? -18.728 19.475 61.725 1.00 22.62 ? 246 GLU A CA 1 ATOM 1950 C C . GLU A 1 243 ? -19.892 18.553 62.097 1.00 22.65 ? 246 GLU A C 1 ATOM 1951 O O . GLU A 1 243 ? -20.929 18.601 61.437 1.00 23.30 ? 246 GLU A O 1 ATOM 1952 C CB . GLU A 1 243 ? -19.041 20.947 61.971 1.00 23.14 ? 246 GLU A CB 1 ATOM 1953 C CG . GLU A 1 243 ? -19.535 21.324 63.312 1.00 29.24 ? 246 GLU A CG 1 ATOM 1954 C CD . GLU A 1 243 ? -19.950 22.793 63.343 1.00 31.30 ? 246 GLU A CD 1 ATOM 1955 O OE1 . GLU A 1 243 ? -19.061 23.650 63.159 1.00 32.30 ? 246 GLU A OE1 1 ATOM 1956 O OE2 . GLU A 1 243 ? -21.165 23.085 63.542 1.00 34.04 ? 246 GLU A OE2 1 ATOM 1957 N N . SER A 1 244 ? -19.723 17.716 63.106 1.00 23.21 ? 247 SER A N 1 ATOM 1958 C CA . SER A 1 244 ? -20.842 16.819 63.512 1.00 23.63 ? 247 SER A CA 1 ATOM 1959 C C . SER A 1 244 ? -20.854 16.375 64.978 1.00 23.08 ? 247 SER A C 1 ATOM 1960 O O . SER A 1 244 ? -19.811 16.157 65.579 1.00 23.02 ? 247 SER A O 1 ATOM 1961 C CB . SER A 1 244 ? -20.839 15.556 62.619 1.00 23.87 ? 247 SER A CB 1 ATOM 1962 O OG . SER A 1 244 ? -21.834 14.630 63.045 1.00 25.32 ? 247 SER A OG 1 ATOM 1963 N N . THR A 1 245 ? -22.057 16.172 65.540 1.00 24.49 ? 248 THR A N 1 ATOM 1964 C CA . THR A 1 245 ? -22.168 15.592 66.888 1.00 24.83 ? 248 THR A CA 1 ATOM 1965 C C . THR A 1 245 ? -22.612 14.138 66.831 1.00 24.36 ? 248 THR A C 1 ATOM 1966 O O . THR A 1 245 ? -22.902 13.495 67.846 1.00 24.94 ? 248 THR A O 1 ATOM 1967 C CB . THR A 1 245 ? -23.168 16.361 67.778 1.00 25.09 ? 248 THR A CB 1 ATOM 1968 O OG1 . THR A 1 245 ? -24.352 16.644 67.027 1.00 24.50 ? 248 THR A OG1 1 ATOM 1969 C CG2 . THR A 1 245 ? -22.530 17.677 68.283 1.00 27.29 ? 248 THR A CG2 1 ATOM 1970 N N . GLY A 1 246 ? -22.632 13.598 65.615 1.00 23.23 ? 249 GLY A N 1 ATOM 1971 C CA . GLY A 1 246 ? -23.024 12.238 65.442 1.00 20.47 ? 249 GLY A CA 1 ATOM 1972 C C . GLY A 1 246 ? -23.540 12.062 64.032 1.00 17.86 ? 249 GLY A C 1 ATOM 1973 O O . GLY A 1 246 ? -24.058 13.002 63.424 1.00 18.14 ? 249 GLY A O 1 ATOM 1974 N N . ASN A 1 247 ? -23.374 10.840 63.545 1.00 17.96 ? 250 ASN A N 1 ATOM 1975 C CA . ASN A 1 247 ? -23.992 10.371 62.309 1.00 16.36 ? 250 ASN A CA 1 ATOM 1976 C C . ASN A 1 247 ? -23.256 10.755 61.024 1.00 16.71 ? 250 ASN A C 1 ATOM 1977 O O . ASN A 1 247 ? -23.750 10.498 59.923 1.00 16.95 ? 250 ASN A O 1 ATOM 1978 C CB . ASN A 1 247 ? -25.492 10.698 62.222 1.00 16.42 ? 250 ASN A CB 1 ATOM 1979 C CG . ASN A 1 247 ? -26.269 10.220 63.451 1.00 18.96 ? 250 ASN A CG 1 ATOM 1980 O OD1 . ASN A 1 247 ? -26.057 10.731 64.555 1.00 20.22 ? 250 ASN A OD1 1 ATOM 1981 N ND2 . ASN A 1 247 ? -27.183 9.255 63.265 1.00 17.44 ? 250 ASN A ND2 1 ATOM 1982 N N . LEU A 1 248 ? -22.115 11.420 61.168 1.00 16.28 ? 251 LEU A N 1 ATOM 1983 C CA . LEU A 1 248 ? -21.285 11.730 60.004 1.00 14.52 ? 251 LEU A CA 1 ATOM 1984 C C . LEU A 1 248 ? -20.543 10.511 59.452 1.00 14.83 ? 251 LEU A C 1 ATOM 1985 O O . LEU A 1 248 ? -19.857 9.788 60.184 1.00 15.97 ? 251 LEU A O 1 ATOM 1986 C CB . LEU A 1 248 ? -20.237 12.813 60.360 1.00 14.89 ? 251 LEU A CB 1 ATOM 1987 C CG . LEU A 1 248 ? -19.093 13.122 59.401 1.00 15.44 ? 251 LEU A CG 1 ATOM 1988 C CD1 . LEU A 1 248 ? -19.611 13.728 58.075 1.00 18.36 ? 251 LEU A CD1 1 ATOM 1989 C CD2 . LEU A 1 248 ? -18.098 14.009 60.155 1.00 17.16 ? 251 LEU A CD2 1 ATOM 1990 N N . ILE A 1 249 ? -20.649 10.366 58.133 1.00 13.37 ? 252 ILE A N 1 ATOM 1991 C CA . ILE A 1 249 ? -19.812 9.424 57.370 1.00 13.85 ? 252 ILE A CA 1 ATOM 1992 C C . ILE A 1 249 ? -18.854 10.301 56.590 1.00 14.51 ? 252 ILE A C 1 ATOM 1993 O O . ILE A 1 249 ? -19.245 10.971 55.603 1.00 14.89 ? 252 ILE A O 1 ATOM 1994 C CB . ILE A 1 249 ? -20.693 8.529 56.425 1.00 14.01 ? 252 ILE A CB 1 ATOM 1995 C CG1 . ILE A 1 249 ? -21.836 7.830 57.208 1.00 14.03 ? 252 ILE A CG1 1 ATOM 1996 C CG2 . ILE A 1 249 ? -19.783 7.505 55.778 1.00 14.55 ? 252 ILE A CG2 1 ATOM 1997 C CD1 . ILE A 1 249 ? -21.368 7.007 58.494 1.00 14.90 ? 252 ILE A CD1 1 ATOM 1998 N N . ALA A 1 250 ? -17.610 10.357 57.046 1.00 14.63 ? 253 ALA A N 1 ATOM 1999 C CA . ALA A 1 250 ? -16.676 11.315 56.522 1.00 13.58 ? 253 ALA A CA 1 ATOM 2000 C C . ALA A 1 250 ? -15.949 10.719 55.323 1.00 13.72 ? 253 ALA A C 1 ATOM 2001 O O . ALA A 1 250 ? -15.606 9.526 55.331 1.00 15.02 ? 253 ALA A O 1 ATOM 2002 C CB . ALA A 1 250 ? -15.617 11.695 57.596 1.00 13.50 ? 253 ALA A CB 1 ATOM 2003 N N . PRO A 1 251 ? -15.578 11.561 54.362 1.00 13.66 ? 254 PRO A N 1 ATOM 2004 C CA . PRO A 1 251 ? -14.641 11.054 53.359 1.00 13.92 ? 254 PRO A CA 1 ATOM 2005 C C . PRO A 1 251 ? -13.245 10.961 53.981 1.00 13.60 ? 254 PRO A C 1 ATOM 2006 O O . PRO A 1 251 ? -12.899 11.798 54.838 1.00 12.82 ? 254 PRO A O 1 ATOM 2007 C CB . PRO A 1 251 ? -14.660 12.141 52.279 1.00 14.28 ? 254 PRO A CB 1 ATOM 2008 C CG . PRO A 1 251 ? -14.999 13.441 53.043 1.00 14.23 ? 254 PRO A CG 1 ATOM 2009 C CD . PRO A 1 251 ? -15.925 12.991 54.163 1.00 14.65 ? 254 PRO A CD 1 ATOM 2010 N N . GLU A 1 252 ? -12.480 9.928 53.605 1.00 12.89 ? 255 GLU A N 1 ATOM 2011 C CA . GLU A 1 252 ? -11.029 9.967 53.856 1.00 14.35 ? 255 GLU A CA 1 ATOM 2012 C C . GLU A 1 252 ? -10.291 10.563 52.651 1.00 13.59 ? 255 GLU A C 1 ATOM 2013 O O . GLU A 1 252 ? -9.184 11.123 52.797 1.00 15.23 ? 255 GLU A O 1 ATOM 2014 C CB . GLU A 1 252 ? -10.490 8.543 54.129 1.00 14.38 ? 255 GLU A CB 1 ATOM 2015 C CG . GLU A 1 252 ? -9.019 8.604 54.583 1.00 17.19 ? 255 GLU A CG 1 ATOM 2016 C CD . GLU A 1 252 ? -8.414 7.297 55.074 1.00 19.10 ? 255 GLU A CD 1 ATOM 2017 O OE1 . GLU A 1 252 ? -8.907 6.208 54.705 1.00 21.29 ? 255 GLU A OE1 1 ATOM 2018 O OE2 . GLU A 1 252 ? -7.360 7.398 55.791 1.00 19.80 ? 255 GLU A OE2 1 ATOM 2019 N N . TYR A 1 253 ? -10.866 10.352 51.456 1.00 15.42 ? 256 TYR A N 1 ATOM 2020 C CA . TYR A 1 253 ? -10.249 10.772 50.193 1.00 14.44 ? 256 TYR A CA 1 ATOM 2021 C C . TYR A 1 253 ? -11.084 11.763 49.438 1.00 15.54 ? 256 TYR A C 1 ATOM 2022 O O . TYR A 1 253 ? -12.324 11.802 49.610 1.00 14.90 ? 256 TYR A O 1 ATOM 2023 C CB . TYR A 1 253 ? -10.059 9.553 49.255 1.00 15.08 ? 256 TYR A CB 1 ATOM 2024 C CG . TYR A 1 253 ? -9.183 8.505 49.812 1.00 15.07 ? 256 TYR A CG 1 ATOM 2025 C CD1 . TYR A 1 253 ? -7.818 8.509 49.531 1.00 16.33 ? 256 TYR A CD1 1 ATOM 2026 C CD2 . TYR A 1 253 ? -9.705 7.491 50.637 1.00 16.07 ? 256 TYR A CD2 1 ATOM 2027 C CE1 . TYR A 1 253 ? -6.975 7.529 50.074 1.00 17.45 ? 256 TYR A CE1 1 ATOM 2028 C CE2 . TYR A 1 253 ? -8.859 6.501 51.165 1.00 18.72 ? 256 TYR A CE2 1 ATOM 2029 C CZ . TYR A 1 253 ? -7.528 6.538 50.877 1.00 19.01 ? 256 TYR A CZ 1 ATOM 2030 O OH . TYR A 1 253 ? -6.721 5.538 51.359 1.00 21.96 ? 256 TYR A OH 1 ATOM 2031 N N . GLY A 1 254 ? -10.431 12.516 48.557 1.00 14.47 ? 257 GLY A N 1 ATOM 2032 C CA . GLY A 1 254 ? -11.110 13.342 47.526 1.00 15.43 ? 257 GLY A CA 1 ATOM 2033 C C . GLY A 1 254 ? -10.629 12.893 46.167 1.00 15.80 ? 257 GLY A C 1 ATOM 2034 O O . GLY A 1 254 ? -9.525 12.327 46.054 1.00 16.64 ? 257 GLY A O 1 ATOM 2035 N N . PHE A 1 255 ? -11.412 13.157 45.124 1.00 15.33 ? 258 PHE A N 1 ATOM 2036 C CA . PHE A 1 255 ? -10.976 12.787 43.786 1.00 14.65 ? 258 PHE A CA 1 ATOM 2037 C C . PHE A 1 255 ? -10.647 14.055 43.001 1.00 15.27 ? 258 PHE A C 1 ATOM 2038 O O . PHE A 1 255 ? -11.544 14.779 42.581 1.00 15.55 ? 258 PHE A O 1 ATOM 2039 C CB . PHE A 1 255 ? -12.076 11.992 43.082 1.00 14.51 ? 258 PHE A CB 1 ATOM 2040 C CG . PHE A 1 255 ? -12.307 10.640 43.667 1.00 14.48 ? 258 PHE A CG 1 ATOM 2041 C CD1 . PHE A 1 255 ? -11.686 9.511 43.108 1.00 14.41 ? 258 PHE A CD1 1 ATOM 2042 C CD2 . PHE A 1 255 ? -13.141 10.465 44.760 1.00 16.08 ? 258 PHE A CD2 1 ATOM 2043 C CE1 . PHE A 1 255 ? -11.903 8.232 43.659 1.00 15.91 ? 258 PHE A CE1 1 ATOM 2044 C CE2 . PHE A 1 255 ? -13.333 9.189 45.339 1.00 16.81 ? 258 PHE A CE2 1 ATOM 2045 C CZ . PHE A 1 255 ? -12.726 8.068 44.780 1.00 17.18 ? 258 PHE A CZ 1 ATOM 2046 N N . LYS A 1 256 ? -9.358 14.331 42.883 1.00 15.32 ? 259 LYS A N 1 ATOM 2047 C CA . LYS A 1 256 ? -8.874 15.471 42.111 1.00 15.40 ? 259 LYS A CA 1 ATOM 2048 C C . LYS A 1 256 ? -9.124 15.188 40.625 1.00 16.24 ? 259 LYS A C 1 ATOM 2049 O O . LYS A 1 256 ? -8.772 14.131 40.101 1.00 16.47 ? 259 LYS A O 1 ATOM 2050 C CB . LYS A 1 256 ? -7.361 15.647 42.348 1.00 15.77 ? 259 LYS A CB 1 ATOM 2051 C CG . LYS A 1 256 ? -6.797 16.771 41.528 1.00 17.50 ? 259 LYS A CG 1 ATOM 2052 C CD . LYS A 1 256 ? -5.270 16.752 41.637 1.00 20.13 ? 259 LYS A CD 1 ATOM 2053 C CE . LYS A 1 256 ? -4.600 17.544 40.553 1.00 27.19 ? 259 LYS A CE 1 ATOM 2054 N NZ . LYS A 1 256 ? -3.090 17.506 40.764 1.00 25.97 ? 259 LYS A NZ 1 ATOM 2055 N N . ILE A 1 257 ? -9.729 16.135 39.917 1.00 18.06 ? 260 ILE A N 1 ATOM 2056 C CA . ILE A 1 257 ? -9.964 15.929 38.495 1.00 20.16 ? 260 ILE A CA 1 ATOM 2057 C C . ILE A 1 257 ? -8.632 16.159 37.798 1.00 21.31 ? 260 ILE A C 1 ATOM 2058 O O . ILE A 1 257 ? -8.175 17.307 37.707 1.00 22.80 ? 260 ILE A O 1 ATOM 2059 C CB . ILE A 1 257 ? -11.049 16.897 37.964 1.00 20.19 ? 260 ILE A CB 1 ATOM 2060 C CG1 . ILE A 1 257 ? -12.412 16.537 38.548 1.00 19.62 ? 260 ILE A CG1 1 ATOM 2061 C CG2 . ILE A 1 257 ? -11.076 16.874 36.413 1.00 22.74 ? 260 ILE A CG2 1 ATOM 2062 C CD1 . ILE A 1 257 ? -13.504 17.576 38.256 1.00 22.98 ? 260 ILE A CD1 1 ATOM 2063 N N . SER A 1 258 ? -8.004 15.080 37.318 1.00 20.31 ? 261 SER A N 1 ATOM 2064 C CA . SER A 1 258 ? -6.628 15.181 36.796 1.00 21.92 ? 261 SER A CA 1 ATOM 2065 C C . SER A 1 258 ? -6.540 15.237 35.286 1.00 22.61 ? 261 SER A C 1 ATOM 2066 O O . SER A 1 258 ? -5.478 15.590 34.739 1.00 23.88 ? 261 SER A O 1 ATOM 2067 C CB . SER A 1 258 ? -5.747 14.060 37.336 1.00 20.34 ? 261 SER A CB 1 ATOM 2068 O OG . SER A 1 258 ? -6.374 12.820 37.150 1.00 23.91 ? 261 SER A OG 1 ATOM 2069 N N A LYS A 1 259 ? -7.605 14.816 34.600 0.50 22.63 ? 262 LYS A N 1 ATOM 2070 N N B LYS A 1 259 ? -7.634 14.877 34.623 0.50 22.59 ? 262 LYS A N 1 ATOM 2071 C CA A LYS A 1 259 ? -7.734 14.983 33.141 0.50 22.97 ? 262 LYS A CA 1 ATOM 2072 C CA B LYS A 1 259 ? -7.747 15.036 33.183 0.50 22.85 ? 262 LYS A CA 1 ATOM 2073 C C A LYS A 1 259 ? -9.191 15.246 32.767 0.50 23.19 ? 262 LYS A C 1 ATOM 2074 C C B LYS A 1 259 ? -9.196 15.245 32.765 0.50 23.11 ? 262 LYS A C 1 ATOM 2075 O O A LYS A 1 259 ? -10.096 14.553 33.241 0.50 22.51 ? 262 LYS A O 1 ATOM 2076 O O B LYS A 1 259 ? -10.092 14.519 33.203 0.50 22.41 ? 262 LYS A O 1 ATOM 2077 C CB A LYS A 1 259 ? -7.252 13.747 32.360 0.50 22.93 ? 262 LYS A CB 1 ATOM 2078 C CB B LYS A 1 259 ? -7.138 13.840 32.450 0.50 22.69 ? 262 LYS A CB 1 ATOM 2079 C CG A LYS A 1 259 ? -5.808 13.287 32.610 0.50 23.55 ? 262 LYS A CG 1 ATOM 2080 C CG B LYS A 1 259 ? -7.358 13.863 30.972 0.50 23.27 ? 262 LYS A CG 1 ATOM 2081 C CD A LYS A 1 259 ? -4.852 13.692 31.494 0.50 24.73 ? 262 LYS A CD 1 ATOM 2082 C CD B LYS A 1 259 ? -6.265 13.178 30.209 0.50 25.40 ? 262 LYS A CD 1 ATOM 2083 C CE A LYS A 1 259 ? -3.386 13.409 31.865 0.50 25.47 ? 262 LYS A CE 1 ATOM 2084 C CE B LYS A 1 259 ? -6.269 13.671 28.756 0.50 26.79 ? 262 LYS A CE 1 ATOM 2085 N NZ A LYS A 1 259 ? -2.954 14.214 33.055 0.50 24.17 ? 262 LYS A NZ 1 ATOM 2086 N NZ B LYS A 1 259 ? -6.864 15.058 28.658 0.50 28.14 ? 262 LYS A NZ 1 ATOM 2087 N N . ARG A 1 260 ? -9.400 16.242 31.904 1.00 23.81 ? 263 ARG A N 1 ATOM 2088 C CA . ARG A 1 260 ? -10.724 16.586 31.390 1.00 24.58 ? 263 ARG A CA 1 ATOM 2089 C C . ARG A 1 260 ? -10.825 16.325 29.879 1.00 25.10 ? 263 ARG A C 1 ATOM 2090 O O . ARG A 1 260 ? -9.820 16.347 29.165 1.00 25.24 ? 263 ARG A O 1 ATOM 2091 C CB . ARG A 1 260 ? -11.018 18.071 31.685 1.00 25.33 ? 263 ARG A CB 1 ATOM 2092 C CG . ARG A 1 260 ? -11.182 18.404 33.153 1.00 27.57 ? 263 ARG A CG 1 ATOM 2093 C CD . ARG A 1 260 ? -11.280 19.904 33.326 1.00 31.95 ? 263 ARG A CD 1 ATOM 2094 N NE . ARG A 1 260 ? -11.267 20.317 34.729 1.00 33.30 ? 263 ARG A NE 1 ATOM 2095 C CZ . ARG A 1 260 ? -12.338 20.413 35.511 1.00 32.51 ? 263 ARG A CZ 1 ATOM 2096 N NH1 . ARG A 1 260 ? -13.547 20.097 35.057 1.00 33.51 ? 263 ARG A NH1 1 ATOM 2097 N NH2 . ARG A 1 260 ? -12.197 20.827 36.768 1.00 33.15 ? 263 ARG A NH2 1 ATOM 2098 N N . GLY A 1 261 A -12.039 16.044 29.401 1.00 25.18 ? 263 GLY A N 1 ATOM 2099 C CA . GLY A 1 261 A -12.308 15.945 27.973 1.00 25.71 ? 263 GLY A CA 1 ATOM 2100 C C . GLY A 1 261 A -13.535 15.112 27.664 1.00 26.18 ? 263 GLY A C 1 ATOM 2101 O O . GLY A 1 261 A -14.146 14.568 28.571 1.00 26.41 ? 263 GLY A O 1 ATOM 2102 N N . SER A 1 262 ? -13.876 14.970 26.386 1.00 27.34 ? 264 SER A N 1 ATOM 2103 C CA . SER A 1 262 ? -15.134 14.315 26.043 1.00 28.32 ? 264 SER A CA 1 ATOM 2104 C C . SER A 1 262 ? -14.997 12.836 26.282 1.00 27.92 ? 264 SER A C 1 ATOM 2105 O O . SER A 1 262 ? -14.059 12.182 25.818 1.00 27.96 ? 264 SER A O 1 ATOM 2106 C CB . SER A 1 262 ? -15.620 14.640 24.622 1.00 30.02 ? 264 SER A CB 1 ATOM 2107 O OG . SER A 1 262 ? -14.548 14.553 23.709 1.00 32.99 ? 264 SER A OG 1 ATOM 2108 N N . SER A 1 263 ? -15.905 12.339 27.100 1.00 26.69 ? 265 SER A N 1 ATOM 2109 C CA A SER A 1 263 ? -15.936 10.943 27.472 0.50 26.62 ? 265 SER A CA 1 ATOM 2110 C CA B SER A 1 263 ? -15.945 10.911 27.389 0.50 26.99 ? 265 SER A CA 1 ATOM 2111 C C . SER A 1 263 ? -17.408 10.526 27.475 1.00 26.70 ? 265 SER A C 1 ATOM 2112 O O . SER A 1 263 ? -18.213 10.991 26.644 1.00 27.64 ? 265 SER A O 1 ATOM 2113 C CB A SER A 1 263 ? -15.297 10.783 28.849 0.50 26.56 ? 265 SER A CB 1 ATOM 2114 C CB B SER A 1 263 ? -15.157 10.552 28.650 0.50 26.92 ? 265 SER A CB 1 ATOM 2115 O OG A SER A 1 263 ? -15.007 9.432 29.146 0.50 25.85 ? 265 SER A OG 1 ATOM 2116 O OG B SER A 1 263 ? -15.537 11.346 29.756 0.50 28.12 ? 265 SER A OG 1 ATOM 2117 N N . GLY A 1 264 ? -17.772 9.707 28.443 1.00 26.46 ? 266 GLY A N 1 ATOM 2118 C CA . GLY A 1 264 ? -19.161 9.310 28.567 1.00 24.90 ? 266 GLY A CA 1 ATOM 2119 C C . GLY A 1 264 ? -19.268 8.005 29.309 1.00 24.45 ? 266 GLY A C 1 ATOM 2120 O O . GLY A 1 264 ? -18.287 7.268 29.453 1.00 23.99 ? 266 GLY A O 1 ATOM 2121 N N . ILE A 1 265 ? -20.473 7.731 29.795 1.00 24.45 ? 267 ILE A N 1 ATOM 2122 C CA . ILE A 1 265 ? -20.755 6.452 30.418 1.00 23.94 ? 267 ILE A CA 1 ATOM 2123 C C . ILE A 1 265 ? -21.583 5.670 29.434 1.00 24.36 ? 267 ILE A C 1 ATOM 2124 O O . ILE A 1 265 ? -22.690 6.086 29.073 1.00 25.16 ? 267 ILE A O 1 ATOM 2125 C CB . ILE A 1 265 ? -21.549 6.598 31.728 1.00 23.51 ? 267 ILE A CB 1 ATOM 2126 C CG1 . ILE A 1 265 ? -20.761 7.470 32.728 1.00 25.51 ? 267 ILE A CG1 1 ATOM 2127 C CG2 . ILE A 1 265 ? -21.936 5.199 32.273 1.00 27.47 ? 267 ILE A CG2 1 ATOM 2128 C CD1 . ILE A 1 265 ? -21.506 7.737 34.050 1.00 25.06 ? 267 ILE A CD1 1 ATOM 2129 N N . MET A 1 266 ? -21.055 4.544 29.004 1.00 23.00 ? 268 MET A N 1 ATOM 2130 C CA . MET A 1 266 ? -21.778 3.657 28.119 1.00 25.47 ? 268 MET A CA 1 ATOM 2131 C C . MET A 1 266 ? -22.475 2.589 28.925 1.00 23.87 ? 268 MET A C 1 ATOM 2132 O O . MET A 1 266 ? -21.827 1.872 29.702 1.00 21.95 ? 268 MET A O 1 ATOM 2133 C CB . MET A 1 266 ? -20.781 2.962 27.194 1.00 24.95 ? 268 MET A CB 1 ATOM 2134 C CG . MET A 1 266 ? -21.415 1.957 26.267 1.00 27.88 ? 268 MET A CG 1 ATOM 2135 S SD . MET A 1 266 ? -20.242 1.605 24.937 1.00 32.13 ? 268 MET A SD 1 ATOM 2136 C CE . MET A 1 266 ? -20.297 3.177 24.112 1.00 29.70 ? 268 MET A CE 1 ATOM 2137 N N . LYS A 1 267 ? -23.782 2.436 28.713 1.00 22.39 ? 269 LYS A N 1 ATOM 2138 C CA . LYS A 1 267 ? -24.500 1.354 29.366 1.00 23.00 ? 269 LYS A CA 1 ATOM 2139 C C . LYS A 1 267 ? -24.344 0.067 28.549 1.00 23.22 ? 269 LYS A C 1 ATOM 2140 O O . LYS A 1 267 ? -24.753 0.000 27.377 1.00 22.72 ? 269 LYS A O 1 ATOM 2141 C CB . LYS A 1 267 ? -25.991 1.716 29.583 1.00 23.29 ? 269 LYS A CB 1 ATOM 2142 C CG . LYS A 1 267 ? -26.262 2.830 30.650 1.00 26.73 ? 269 LYS A CG 1 ATOM 2143 C CD . LYS A 1 267 ? -25.758 2.411 32.079 1.00 28.78 ? 269 LYS A CD 1 ATOM 2144 C CE . LYS A 1 267 ? -26.775 2.703 33.226 1.00 31.74 ? 269 LYS A CE 1 ATOM 2145 N NZ . LYS A 1 267 ? -26.377 2.091 34.627 1.00 29.08 ? 269 LYS A NZ 1 ATOM 2146 N N . THR A 1 268 ? -23.733 -0.938 29.164 1.00 22.06 ? 270 THR A N 1 ATOM 2147 C CA . THR A 1 268 ? -23.430 -2.206 28.509 1.00 22.98 ? 270 THR A CA 1 ATOM 2148 C C . THR A 1 268 ? -23.214 -3.311 29.520 1.00 23.34 ? 270 THR A C 1 ATOM 2149 O O . THR A 1 268 ? -22.642 -3.074 30.598 1.00 23.01 ? 270 THR A O 1 ATOM 2150 C CB . THR A 1 268 ? -22.188 -2.108 27.562 1.00 22.92 ? 270 THR A CB 1 ATOM 2151 O OG1 . THR A 1 268 ? -21.916 -3.375 26.972 1.00 23.75 ? 270 THR A OG1 1 ATOM 2152 C CG2 . THR A 1 268 ? -20.929 -1.625 28.312 1.00 23.05 ? 270 THR A CG2 1 ATOM 2153 N N . GLU A 1 269 ? -23.645 -4.527 29.154 1.00 22.79 ? 271 GLU A N 1 ATOM 2154 C CA . GLU A 1 269 ? -23.420 -5.731 29.967 1.00 23.29 ? 271 GLU A CA 1 ATOM 2155 C C . GLU A 1 269 ? -22.117 -6.458 29.576 1.00 23.06 ? 271 GLU A C 1 ATOM 2156 O O . GLU A 1 269 ? -21.692 -7.458 30.198 1.00 23.55 ? 271 GLU A O 1 ATOM 2157 C CB . GLU A 1 269 ? -24.625 -6.681 29.854 1.00 22.88 ? 271 GLU A CB 1 ATOM 2158 C CG . GLU A 1 269 ? -25.978 -6.035 30.115 1.00 23.88 ? 271 GLU A CG 1 ATOM 2159 C CD . GLU A 1 269 ? -26.038 -5.284 31.436 1.00 24.48 ? 271 GLU A CD 1 ATOM 2160 O OE1 . GLU A 1 269 ? -25.754 -5.911 32.473 1.00 24.77 ? 271 GLU A OE1 1 ATOM 2161 O OE2 . GLU A 1 269 ? -26.396 -4.088 31.412 1.00 27.08 ? 271 GLU A OE2 1 ATOM 2162 N N . GLY A 1 270 ? -21.459 -5.934 28.549 1.00 22.69 ? 272 GLY A N 1 ATOM 2163 C CA . GLY A 1 270 ? -20.322 -6.620 27.959 1.00 22.46 ? 272 GLY A CA 1 ATOM 2164 C C . GLY A 1 270 ? -18.986 -6.263 28.573 1.00 21.97 ? 272 GLY A C 1 ATOM 2165 O O . GLY A 1 270 ? -18.900 -5.521 29.539 1.00 21.41 ? 272 GLY A O 1 ATOM 2166 N N . THR A 1 271 ? -17.934 -6.811 27.988 1.00 22.14 ? 273 THR A N 1 ATOM 2167 C CA . THR A 1 271 ? -16.614 -6.701 28.554 1.00 22.12 ? 273 THR A CA 1 ATOM 2168 C C . THR A 1 271 ? -15.647 -6.204 27.480 1.00 21.33 ? 273 THR A C 1 ATOM 2169 O O . THR A 1 271 ? -15.891 -6.353 26.270 1.00 21.58 ? 273 THR A O 1 ATOM 2170 C CB . THR A 1 271 ? -16.187 -8.050 29.232 1.00 22.95 ? 273 THR A CB 1 ATOM 2171 O OG1 . THR A 1 271 ? -15.044 -7.842 30.069 1.00 24.75 ? 273 THR A OG1 1 ATOM 2172 C CG2 . THR A 1 271 ? -15.896 -9.148 28.192 1.00 23.75 ? 273 THR A CG2 1 ATOM 2173 N N . LEU A 1 272 ? -14.562 -5.590 27.923 1.00 19.52 ? 274 LEU A N 1 ATOM 2174 C CA . LEU A 1 272 ? -13.570 -5.062 27.006 1.00 19.63 ? 274 LEU A CA 1 ATOM 2175 C C . LEU A 1 272 ? -12.786 -6.163 26.316 1.00 20.78 ? 274 LEU A C 1 ATOM 2176 O O . LEU A 1 272 ? -12.318 -7.116 26.955 1.00 21.13 ? 274 LEU A O 1 ATOM 2177 C CB . LEU A 1 272 ? -12.604 -4.145 27.757 1.00 20.61 ? 274 LEU A CB 1 ATOM 2178 C CG . LEU A 1 272 ? -11.426 -3.560 26.970 1.00 19.23 ? 274 LEU A CG 1 ATOM 2179 C CD1 . LEU A 1 272 ? -11.898 -2.637 25.845 1.00 21.30 ? 274 LEU A CD1 1 ATOM 2180 C CD2 . LEU A 1 272 ? -10.491 -2.816 27.942 1.00 20.52 ? 274 LEU A CD2 1 ATOM 2181 N N . GLU A 1 273 ? -12.660 -6.035 25.002 1.00 20.48 ? 275 GLU A N 1 ATOM 2182 C CA . GLU A 1 273 ? -11.863 -6.975 24.227 1.00 21.99 ? 275 GLU A CA 1 ATOM 2183 C C . GLU A 1 273 ? -10.590 -6.302 23.726 1.00 21.38 ? 275 GLU A C 1 ATOM 2184 O O . GLU A 1 273 ? -10.457 -5.076 23.776 1.00 21.87 ? 275 GLU A O 1 ATOM 2185 C CB . GLU A 1 273 ? -12.703 -7.557 23.084 1.00 22.44 ? 275 GLU A CB 1 ATOM 2186 C CG . GLU A 1 273 ? -13.870 -8.411 23.597 1.00 24.15 ? 275 GLU A CG 1 ATOM 2187 C CD . GLU A 1 273 ? -14.695 -9.048 22.497 1.00 25.61 ? 275 GLU A CD 1 ATOM 2188 O OE1 . GLU A 1 273 ? -14.107 -9.772 21.642 1.00 30.41 ? 275 GLU A OE1 1 ATOM 2189 O OE2 . GLU A 1 273 ? -15.934 -8.847 22.492 1.00 28.20 ? 275 GLU A OE2 1 ATOM 2190 N N . ASN A 1 274 ? -9.657 -7.113 23.248 1.00 21.40 ? 276 ASN A N 1 ATOM 2191 C CA . ASN A 1 274 ? -8.369 -6.622 22.785 1.00 21.48 ? 276 ASN A CA 1 ATOM 2192 C C . ASN A 1 274 ? -8.496 -6.140 21.335 1.00 21.88 ? 276 ASN A C 1 ATOM 2193 O O . ASN A 1 274 ? -8.145 -6.849 20.377 1.00 22.20 ? 276 ASN A O 1 ATOM 2194 C CB . ASN A 1 274 ? -7.316 -7.741 22.939 1.00 20.64 ? 276 ASN A CB 1 ATOM 2195 C CG . ASN A 1 274 ? -5.926 -7.293 22.553 1.00 22.43 ? 276 ASN A CG 1 ATOM 2196 O OD1 . ASN A 1 274 ? -5.667 -6.109 22.366 1.00 25.99 ? 276 ASN A OD1 1 ATOM 2197 N ND2 . ASN A 1 274 ? -5.016 -8.257 22.411 1.00 23.92 ? 276 ASN A ND2 1 ATOM 2198 N N . CYS A 1 275 ? -9.043 -4.936 21.188 1.00 21.66 ? 277 CYS A N 1 ATOM 2199 C CA . CYS A 1 275 ? -9.278 -4.326 19.896 1.00 23.30 ? 277 CYS A CA 1 ATOM 2200 C C . CYS A 1 275 ? -9.154 -2.822 20.050 1.00 23.70 ? 277 CYS A C 1 ATOM 2201 O O . CYS A 1 275 ? -9.178 -2.279 21.186 1.00 22.63 ? 277 CYS A O 1 ATOM 2202 C CB . CYS A 1 275 ? -10.655 -4.708 19.308 1.00 23.88 ? 277 CYS A CB 1 ATOM 2203 S SG . CYS A 1 275 ? -12.088 -4.496 20.430 1.00 28.23 ? 277 CYS A SG 1 ATOM 2204 N N . GLU A 1 276 ? -9.033 -2.165 18.898 1.00 23.77 ? 278 GLU A N 1 ATOM 2205 C CA . GLU A 1 276 ? -8.771 -0.736 18.805 1.00 24.77 ? 278 GLU A CA 1 ATOM 2206 C C . GLU A 1 276 ? -9.818 -0.100 17.876 1.00 24.46 ? 278 GLU A C 1 ATOM 2207 O O . GLU A 1 276 ? -10.153 -0.696 16.847 1.00 24.30 ? 278 GLU A O 1 ATOM 2208 C CB . GLU A 1 276 ? -7.332 -0.561 18.257 1.00 25.91 ? 278 GLU A CB 1 ATOM 2209 C CG . GLU A 1 276 ? -6.999 0.816 17.679 1.00 28.53 ? 278 GLU A CG 1 ATOM 2210 C CD . GLU A 1 276 ? -7.045 1.915 18.719 1.00 34.06 ? 278 GLU A CD 1 ATOM 2211 O OE1 . GLU A 1 276 ? -7.028 1.581 19.918 1.00 32.69 ? 278 GLU A OE1 1 ATOM 2212 O OE2 . GLU A 1 276 ? -7.097 3.103 18.325 1.00 35.16 ? 278 GLU A OE2 1 ATOM 2213 N N . THR A 1 277 ? -10.348 1.067 18.249 1.00 23.77 ? 279 THR A N 1 ATOM 2214 C CA . THR A 1 277 ? -11.271 1.835 17.391 1.00 23.69 ? 279 THR A CA 1 ATOM 2215 C C . THR A 1 277 ? -11.104 3.340 17.540 1.00 24.33 ? 279 THR A C 1 ATOM 2216 O O . THR A 1 277 ? -10.494 3.823 18.505 1.00 24.30 ? 279 THR A O 1 ATOM 2217 C CB . THR A 1 277 ? -12.773 1.443 17.603 1.00 23.65 ? 279 THR A CB 1 ATOM 2218 O OG1 . THR A 1 277 ? -13.583 1.960 16.531 1.00 23.81 ? 279 THR A OG1 1 ATOM 2219 C CG2 . THR A 1 277 ? -13.313 1.967 18.938 1.00 22.81 ? 279 THR A CG2 1 ATOM 2220 N N . LYS A 1 278 ? -11.635 4.073 16.562 1.00 24.80 ? 280 LYS A N 1 ATOM 2221 C CA . LYS A 1 278 ? -11.797 5.523 16.662 1.00 26.29 ? 280 LYS A CA 1 ATOM 2222 C C . LYS A 1 278 ? -13.254 5.894 17.006 1.00 25.79 ? 280 LYS A C 1 ATOM 2223 O O . LYS A 1 278 ? -13.536 7.027 17.391 1.00 26.77 ? 280 LYS A O 1 ATOM 2224 C CB . LYS A 1 278 ? -11.312 6.201 15.358 1.00 26.78 ? 280 LYS A CB 1 ATOM 2225 C CG . LYS A 1 278 ? -9.789 5.987 15.114 1.00 27.33 ? 280 LYS A CG 1 ATOM 2226 C CD . LYS A 1 278 ? -9.351 6.393 13.691 1.00 30.04 ? 280 LYS A CD 1 ATOM 2227 C CE . LYS A 1 278 ? -7.820 6.506 13.612 1.00 32.43 ? 280 LYS A CE 1 ATOM 2228 N NZ . LYS A 1 278 ? -7.247 5.880 12.369 1.00 36.86 ? 280 LYS A NZ 1 ATOM 2229 N N . CYS A 1 279 ? -14.169 4.930 16.868 1.00 25.41 ? 281 CYS A N 1 ATOM 2230 C CA . CYS A 1 279 ? -15.606 5.154 17.084 1.00 25.12 ? 281 CYS A CA 1 ATOM 2231 C C . CYS A 1 279 ? -16.245 3.961 17.797 1.00 23.98 ? 281 CYS A C 1 ATOM 2232 O O . CYS A 1 279 ? -16.295 2.866 17.246 1.00 23.78 ? 281 CYS A O 1 ATOM 2233 C CB . CYS A 1 279 ? -16.317 5.412 15.740 1.00 25.26 ? 281 CYS A CB 1 ATOM 2234 S SG . CYS A 1 279 ? -18.070 5.620 15.877 1.00 26.70 ? 281 CYS A SG 1 ATOM 2235 N N . GLN A 1 280 ? -16.708 4.164 19.029 1.00 22.99 ? 282 GLN A N 1 ATOM 2236 C CA . GLN A 1 280 ? -17.297 3.074 19.804 1.00 22.61 ? 282 GLN A CA 1 ATOM 2237 C C . GLN A 1 280 ? -18.794 3.297 19.984 1.00 22.63 ? 282 GLN A C 1 ATOM 2238 O O . GLN A 1 280 ? -19.212 4.385 20.353 1.00 24.10 ? 282 GLN A O 1 ATOM 2239 C CB . GLN A 1 280 ? -16.656 2.995 21.196 1.00 21.66 ? 282 GLN A CB 1 ATOM 2240 C CG . GLN A 1 280 ? -17.142 1.794 21.996 1.00 20.90 ? 282 GLN A CG 1 ATOM 2241 C CD . GLN A 1 280 ? -16.637 0.491 21.392 1.00 20.34 ? 282 GLN A CD 1 ATOM 2242 O OE1 . GLN A 1 280 ? -15.433 0.300 21.222 1.00 21.13 ? 282 GLN A OE1 1 ATOM 2243 N NE2 . GLN A 1 280 ? -17.561 -0.403 21.062 1.00 19.64 ? 282 GLN A NE2 1 ATOM 2244 N N . THR A 1 281 ? -19.584 2.254 19.740 1.00 23.62 ? 283 THR A N 1 ATOM 2245 C CA . THR A 1 281 ? -21.003 2.264 20.118 1.00 24.38 ? 283 THR A CA 1 ATOM 2246 C C . THR A 1 281 ? -21.269 1.160 21.148 1.00 24.62 ? 283 THR A C 1 ATOM 2247 O O . THR A 1 281 ? -20.473 0.238 21.285 1.00 23.36 ? 283 THR A O 1 ATOM 2248 C CB . THR A 1 281 ? -21.946 2.056 18.902 1.00 24.43 ? 283 THR A CB 1 ATOM 2249 O OG1 . THR A 1 281 ? -22.146 0.657 18.698 1.00 24.80 ? 283 THR A OG1 1 ATOM 2250 C CG2 . THR A 1 281 ? -21.375 2.694 17.625 1.00 26.32 ? 283 THR A CG2 1 ATOM 2251 N N . PRO A 1 282 ? -22.402 1.239 21.870 1.00 25.48 ? 284 PRO A N 1 ATOM 2252 C CA . PRO A 1 282 ? -22.729 0.171 22.826 1.00 26.75 ? 284 PRO A CA 1 ATOM 2253 C C . PRO A 1 282 ? -22.897 -1.196 22.190 1.00 27.71 ? 284 PRO A C 1 ATOM 2254 O O . PRO A 1 282 ? -22.754 -2.230 22.868 1.00 29.07 ? 284 PRO A O 1 ATOM 2255 C CB . PRO A 1 282 ? -24.069 0.641 23.443 1.00 26.19 ? 284 PRO A CB 1 ATOM 2256 C CG . PRO A 1 282 ? -24.070 2.116 23.248 1.00 25.82 ? 284 PRO A CG 1 ATOM 2257 C CD . PRO A 1 282 ? -23.406 2.309 21.889 1.00 25.18 ? 284 PRO A CD 1 ATOM 2258 N N . LEU A 1 283 ? -23.181 -1.225 20.893 1.00 27.82 ? 285 LEU A N 1 ATOM 2259 C CA . LEU A 1 283 ? -23.335 -2.484 20.187 1.00 28.18 ? 285 LEU A CA 1 ATOM 2260 C C . LEU A 1 283 ? -22.013 -3.037 19.660 1.00 27.16 ? 285 LEU A C 1 ATOM 2261 O O . LEU A 1 283 ? -21.890 -4.234 19.449 1.00 28.41 ? 285 LEU A O 1 ATOM 2262 C CB . LEU A 1 283 ? -24.349 -2.352 19.038 1.00 28.22 ? 285 LEU A CB 1 ATOM 2263 C CG . LEU A 1 283 ? -25.815 -2.192 19.454 1.00 30.35 ? 285 LEU A CG 1 ATOM 2264 C CD1 . LEU A 1 283 ? -26.699 -1.972 18.223 1.00 31.52 ? 285 LEU A CD1 1 ATOM 2265 C CD2 . LEU A 1 283 ? -26.265 -3.437 20.208 1.00 31.43 ? 285 LEU A CD2 1 ATOM 2266 N N . GLY A 1 284 ? -21.030 -2.156 19.460 1.00 26.29 ? 286 GLY A N 1 ATOM 2267 C CA . GLY A 1 284 ? -19.739 -2.525 18.860 1.00 24.77 ? 286 GLY A CA 1 ATOM 2268 C C . GLY A 1 284 ? -19.079 -1.337 18.193 1.00 23.91 ? 286 GLY A C 1 ATOM 2269 O O . GLY A 1 284 ? -19.687 -0.277 18.049 1.00 23.48 ? 286 GLY A O 1 ATOM 2270 N N . ALA A 1 285 ? -17.828 -1.518 17.800 1.00 23.81 ? 287 ALA A N 1 ATOM 2271 C CA . ALA A 1 285 ? -17.011 -0.448 17.237 1.00 23.76 ? 287 ALA A CA 1 ATOM 2272 C C . ALA A 1 285 ? -17.219 -0.303 15.727 1.00 24.02 ? 287 ALA A C 1 ATOM 2273 O O . ALA A 1 285 ? -17.411 -1.293 15.023 1.00 23.50 ? 287 ALA A O 1 ATOM 2274 C CB . ALA A 1 285 ? -15.561 -0.708 17.526 1.00 23.91 ? 287 ALA A CB 1 ATOM 2275 N N . ILE A 1 286 ? -17.153 0.940 15.255 1.00 24.11 ? 288 ILE A N 1 ATOM 2276 C CA . ILE A 1 286 ? -17.319 1.274 13.835 1.00 24.86 ? 288 ILE A CA 1 ATOM 2277 C C . ILE A 1 286 ? -15.977 1.658 13.221 1.00 25.70 ? 288 ILE A C 1 ATOM 2278 O O . ILE A 1 286 ? -15.234 2.454 13.785 1.00 25.63 ? 288 ILE A O 1 ATOM 2279 C CB . ILE A 1 286 ? -18.311 2.452 13.668 1.00 25.36 ? 288 ILE A CB 1 ATOM 2280 C CG1 . ILE A 1 286 ? -19.733 2.022 14.053 1.00 24.70 ? 288 ILE A CG1 1 ATOM 2281 C CG2 . ILE A 1 286 ? -18.264 3.012 12.251 1.00 24.48 ? 288 ILE A CG2 1 ATOM 2282 C CD1 . ILE A 1 286 ? -20.740 3.193 14.070 1.00 25.08 ? 288 ILE A CD1 1 ATOM 2283 N N . ASN A 1 287 ? -15.675 1.075 12.062 1.00 27.00 ? 289 ASN A N 1 ATOM 2284 C CA . ASN A 1 287 ? -14.505 1.430 11.258 1.00 28.05 ? 289 ASN A CA 1 ATOM 2285 C C . ASN A 1 287 ? -14.977 1.696 9.834 1.00 28.42 ? 289 ASN A C 1 ATOM 2286 O O . ASN A 1 287 ? -15.205 0.754 9.076 1.00 28.16 ? 289 ASN A O 1 ATOM 2287 C CB . ASN A 1 287 ? -13.495 0.275 11.239 1.00 28.87 ? 289 ASN A CB 1 ATOM 2288 C CG . ASN A 1 287 ? -12.160 0.661 10.611 1.00 30.90 ? 289 ASN A CG 1 ATOM 2289 O OD1 . ASN A 1 287 ? -11.952 1.802 10.195 1.00 35.11 ? 289 ASN A OD1 1 ATOM 2290 N ND2 . ASN A 1 287 ? -11.236 -0.295 10.559 1.00 35.47 ? 289 ASN A ND2 1 ATOM 2291 N N . THR A 1 288 ? -15.127 2.970 9.499 1.00 28.62 ? 290 THR A N 1 ATOM 2292 C CA . THR A 1 288 ? -15.660 3.396 8.194 1.00 28.63 ? 290 THR A CA 1 ATOM 2293 C C . THR A 1 288 ? -15.167 4.792 7.807 1.00 29.71 ? 290 THR A C 1 ATOM 2294 O O . THR A 1 288 ? -14.772 5.600 8.668 1.00 29.33 ? 290 THR A O 1 ATOM 2295 C CB . THR A 1 288 ? -17.211 3.391 8.202 1.00 28.44 ? 290 THR A CB 1 ATOM 2296 O OG1 . THR A 1 288 ? -17.719 3.472 6.861 1.00 28.58 ? 290 THR A OG1 1 ATOM 2297 C CG2 . THR A 1 288 ? -17.767 4.547 9.046 1.00 27.56 ? 290 THR A CG2 1 ATOM 2298 N N . THR A 1 289 ? -15.208 5.068 6.505 1.00 30.61 ? 291 THR A N 1 ATOM 2299 C CA . THR A 1 289 ? -15.026 6.425 5.989 1.00 31.95 ? 291 THR A CA 1 ATOM 2300 C C . THR A 1 289 ? -16.347 7.024 5.481 1.00 31.68 ? 291 THR A C 1 ATOM 2301 O O . THR A 1 289 ? -16.394 8.195 5.049 1.00 32.08 ? 291 THR A O 1 ATOM 2302 C CB . THR A 1 289 ? -13.982 6.449 4.856 1.00 32.12 ? 291 THR A CB 1 ATOM 2303 O OG1 . THR A 1 289 ? -14.358 5.499 3.851 1.00 33.97 ? 291 THR A OG1 1 ATOM 2304 C CG2 . THR A 1 289 ? -12.603 6.080 5.401 1.00 33.15 ? 291 THR A CG2 1 ATOM 2305 N N . LEU A 1 290 ? -17.417 6.226 5.546 1.00 30.91 ? 292 LEU A N 1 ATOM 2306 C CA . LEU A 1 290 ? -18.747 6.684 5.144 1.00 29.78 ? 292 LEU A CA 1 ATOM 2307 C C . LEU A 1 290 ? -19.259 7.774 6.085 1.00 29.65 ? 292 LEU A C 1 ATOM 2308 O O . LEU A 1 290 ? -18.996 7.727 7.288 1.00 29.46 ? 292 LEU A O 1 ATOM 2309 C CB . LEU A 1 290 ? -19.728 5.506 5.045 1.00 29.50 ? 292 LEU A CB 1 ATOM 2310 C CG . LEU A 1 290 ? -19.429 4.473 3.944 1.00 28.51 ? 292 LEU A CG 1 ATOM 2311 C CD1 . LEU A 1 290 ? -20.550 3.452 3.818 1.00 26.75 ? 292 LEU A CD1 1 ATOM 2312 C CD2 . LEU A 1 290 ? -19.165 5.140 2.591 1.00 29.60 ? 292 LEU A CD2 1 ATOM 2313 N N . PRO A 1 291 ? -19.960 8.780 5.536 1.00 29.13 ? 293 PRO A N 1 ATOM 2314 C CA . PRO A 1 291 ? -20.433 9.923 6.321 1.00 28.77 ? 293 PRO A CA 1 ATOM 2315 C C . PRO A 1 291 ? -21.598 9.677 7.292 1.00 28.54 ? 293 PRO A C 1 ATOM 2316 O O . PRO A 1 291 ? -21.756 10.461 8.235 1.00 29.19 ? 293 PRO A O 1 ATOM 2317 C CB . PRO A 1 291 ? -20.850 10.930 5.240 1.00 29.21 ? 293 PRO A CB 1 ATOM 2318 C CG . PRO A 1 291 ? -21.281 10.071 4.106 1.00 28.67 ? 293 PRO A CG 1 ATOM 2319 C CD . PRO A 1 291 ? -20.305 8.930 4.103 1.00 29.14 ? 293 PRO A CD 1 ATOM 2320 N N . PHE A 1 292 ? -22.397 8.629 7.066 1.00 27.63 ? 294 PHE A N 1 ATOM 2321 C CA . PHE A 1 292 ? -23.544 8.282 7.924 1.00 27.07 ? 294 PHE A CA 1 ATOM 2322 C C . PHE A 1 292 ? -23.420 6.847 8.441 1.00 25.97 ? 294 PHE A C 1 ATOM 2323 O O . PHE A 1 292 ? -22.758 6.020 7.821 1.00 24.38 ? 294 PHE A O 1 ATOM 2324 C CB . PHE A 1 292 ? -24.874 8.376 7.156 1.00 27.81 ? 294 PHE A CB 1 ATOM 2325 C CG . PHE A 1 292 ? -25.211 9.746 6.656 1.00 29.66 ? 294 PHE A CG 1 ATOM 2326 C CD1 . PHE A 1 292 ? -25.909 10.647 7.464 1.00 32.54 ? 294 PHE A CD1 1 ATOM 2327 C CD2 . PHE A 1 292 ? -24.878 10.124 5.359 1.00 30.68 ? 294 PHE A CD2 1 ATOM 2328 C CE1 . PHE A 1 292 ? -26.242 11.915 6.988 1.00 33.78 ? 294 PHE A CE1 1 ATOM 2329 C CE2 . PHE A 1 292 ? -25.202 11.385 4.873 1.00 32.14 ? 294 PHE A CE2 1 ATOM 2330 C CZ . PHE A 1 292 ? -25.884 12.283 5.687 1.00 32.17 ? 294 PHE A CZ 1 ATOM 2331 N N . HIS A 1 293 ? -24.060 6.550 9.576 1.00 24.92 ? 295 HIS A N 1 ATOM 2332 C CA . HIS A 1 293 ? -24.229 5.163 10.001 1.00 24.75 ? 295 HIS A CA 1 ATOM 2333 C C . HIS A 1 293 ? -25.600 5.014 10.650 1.00 24.65 ? 295 HIS A C 1 ATOM 2334 O O . HIS A 1 293 ? -26.223 6.017 11.031 1.00 25.03 ? 295 HIS A O 1 ATOM 2335 C CB . HIS A 1 293 ? -23.118 4.747 10.987 1.00 24.08 ? 295 HIS A CB 1 ATOM 2336 C CG . HIS A 1 293 ? -23.281 5.335 12.352 1.00 25.57 ? 295 HIS A CG 1 ATOM 2337 N ND1 . HIS A 1 293 ? -23.914 4.667 13.383 1.00 25.27 ? 295 HIS A ND1 1 ATOM 2338 C CD2 . HIS A 1 293 ? -22.906 6.536 12.855 1.00 27.00 ? 295 HIS A CD2 1 ATOM 2339 C CE1 . HIS A 1 293 ? -23.941 5.442 14.454 1.00 24.25 ? 295 HIS A CE1 1 ATOM 2340 N NE2 . HIS A 1 293 ? -23.336 6.581 14.161 1.00 25.26 ? 295 HIS A NE2 1 ATOM 2341 N N . ASN A 1 294 ? -26.070 3.780 10.796 1.00 23.59 ? 296 ASN A N 1 ATOM 2342 C CA . ASN A 1 294 ? -27.357 3.547 11.440 1.00 24.67 ? 296 ASN A CA 1 ATOM 2343 C C . ASN A 1 294 ? -27.233 2.567 12.607 1.00 24.92 ? 296 ASN A C 1 ATOM 2344 O O . ASN A 1 294 ? -28.191 1.894 12.972 1.00 25.44 ? 296 ASN A O 1 ATOM 2345 C CB . ASN A 1 294 ? -28.419 3.077 10.418 1.00 24.11 ? 296 ASN A CB 1 ATOM 2346 C CG . ASN A 1 294 ? -28.142 1.675 9.864 1.00 25.43 ? 296 ASN A CG 1 ATOM 2347 O OD1 . ASN A 1 294 ? -27.120 1.051 10.182 1.00 26.59 ? 296 ASN A OD1 1 ATOM 2348 N ND2 . ASN A 1 294 ? -29.055 1.179 9.019 1.00 25.01 ? 296 ASN A ND2 1 ATOM 2349 N N . VAL A 1 295 ? -26.043 2.504 13.200 1.00 25.66 ? 297 VAL A N 1 ATOM 2350 C CA . VAL A 1 295 ? -25.719 1.443 14.160 1.00 26.37 ? 297 VAL A CA 1 ATOM 2351 C C . VAL A 1 295 ? -26.387 1.660 15.523 1.00 26.86 ? 297 VAL A C 1 ATOM 2352 O O . VAL A 1 295 ? -27.091 0.782 16.000 1.00 27.29 ? 297 VAL A O 1 ATOM 2353 C CB . VAL A 1 295 ? -24.178 1.237 14.324 1.00 26.31 ? 297 VAL A CB 1 ATOM 2354 C CG1 . VAL A 1 295 ? -23.885 0.323 15.517 1.00 26.39 ? 297 VAL A CG1 1 ATOM 2355 C CG2 . VAL A 1 295 ? -23.581 0.629 13.044 1.00 26.80 ? 297 VAL A CG2 1 ATOM 2356 N N . HIS A 1 296 ? -26.176 2.840 16.104 1.00 27.38 ? 298 HIS A N 1 ATOM 2357 C CA . HIS A 1 296 ? -26.712 3.211 17.419 1.00 28.56 ? 298 HIS A CA 1 ATOM 2358 C C . HIS A 1 296 ? -26.569 4.724 17.588 1.00 28.48 ? 298 HIS A C 1 ATOM 2359 O O . HIS A 1 296 ? -25.584 5.295 17.133 1.00 29.17 ? 298 HIS A O 1 ATOM 2360 C CB . HIS A 1 296 ? -25.921 2.475 18.517 1.00 28.81 ? 298 HIS A CB 1 ATOM 2361 C CG . HIS A 1 296 ? -26.608 2.441 19.845 1.00 29.23 ? 298 HIS A CG 1 ATOM 2362 N ND1 . HIS A 1 296 ? -26.570 3.496 20.728 1.00 32.11 ? 298 HIS A ND1 1 ATOM 2363 C CD2 . HIS A 1 296 ? -27.345 1.475 20.443 1.00 31.63 ? 298 HIS A CD2 1 ATOM 2364 C CE1 . HIS A 1 296 ? -27.252 3.184 21.817 1.00 32.35 ? 298 HIS A CE1 1 ATOM 2365 N NE2 . HIS A 1 296 ? -27.733 1.963 21.669 1.00 30.80 ? 298 HIS A NE2 1 ATOM 2366 N N . PRO A 1 297 ? -27.549 5.406 18.228 1.00 29.15 ? 299 PRO A N 1 ATOM 2367 C CA . PRO A 1 297 ? -27.365 6.849 18.420 1.00 29.35 ? 299 PRO A CA 1 ATOM 2368 C C . PRO A 1 297 ? -26.300 7.282 19.443 1.00 29.76 ? 299 PRO A C 1 ATOM 2369 O O . PRO A 1 297 ? -25.829 8.417 19.386 1.00 29.62 ? 299 PRO A O 1 ATOM 2370 C CB . PRO A 1 297 ? -28.758 7.324 18.884 1.00 29.30 ? 299 PRO A CB 1 ATOM 2371 C CG . PRO A 1 297 ? -29.371 6.147 19.505 1.00 29.66 ? 299 PRO A CG 1 ATOM 2372 C CD . PRO A 1 297 ? -28.864 4.951 18.730 1.00 29.26 ? 299 PRO A CD 1 ATOM 2373 N N . LEU A 1 298 ? -25.932 6.394 20.367 1.00 30.44 ? 300 LEU A N 1 ATOM 2374 C CA . LEU A 1 298 ? -25.059 6.789 21.477 1.00 31.59 ? 300 LEU A CA 1 ATOM 2375 C C . LEU A 1 298 ? -23.640 6.334 21.217 1.00 31.72 ? 300 LEU A C 1 ATOM 2376 O O . LEU A 1 298 ? -23.232 5.260 21.659 1.00 33.86 ? 300 LEU A O 1 ATOM 2377 C CB . LEU A 1 298 ? -25.577 6.266 22.826 1.00 31.95 ? 300 LEU A CB 1 ATOM 2378 C CG . LEU A 1 298 ? -26.893 6.848 23.384 1.00 32.67 ? 300 LEU A CG 1 ATOM 2379 C CD1 . LEU A 1 298 ? -27.195 6.249 24.756 1.00 36.24 ? 300 LEU A CD1 1 ATOM 2380 C CD2 . LEU A 1 298 ? -26.886 8.374 23.451 1.00 34.26 ? 300 LEU A CD2 1 ATOM 2381 N N . THR A 1 299 ? -22.895 7.172 20.517 1.00 31.81 ? 301 THR A N 1 ATOM 2382 C CA . THR A 1 299 ? -21.530 6.842 20.146 1.00 31.64 ? 301 THR A CA 1 ATOM 2383 C C . THR A 1 299 ? -20.513 7.738 20.848 1.00 31.88 ? 301 THR A C 1 ATOM 2384 O O . THR A 1 299 ? -20.817 8.872 21.259 1.00 32.24 ? 301 THR A O 1 ATOM 2385 C CB . THR A 1 299 ? -21.300 6.877 18.615 1.00 31.48 ? 301 THR A CB 1 ATOM 2386 O OG1 . THR A 1 299 ? -21.259 8.237 18.162 1.00 31.39 ? 301 THR A OG1 1 ATOM 2387 C CG2 . THR A 1 299 ? -22.398 6.114 17.879 1.00 30.71 ? 301 THR A CG2 1 ATOM 2388 N N . ILE A 1 300 ? -19.308 7.206 21.003 1.00 31.66 ? 302 ILE A N 1 ATOM 2389 C CA . ILE A 1 300 ? -18.195 7.944 21.566 1.00 31.63 ? 302 ILE A CA 1 ATOM 2390 C C . ILE A 1 300 ? -17.014 7.907 20.604 1.00 31.44 ? 302 ILE A C 1 ATOM 2391 O O . ILE A 1 300 ? -16.681 6.853 20.062 1.00 30.14 ? 302 ILE A O 1 ATOM 2392 C CB . ILE A 1 300 ? -17.812 7.399 22.978 1.00 32.35 ? 302 ILE A CB 1 ATOM 2393 C CG1 . ILE A 1 300 ? -19.044 7.476 23.890 1.00 33.60 ? 302 ILE A CG1 1 ATOM 2394 C CG2 . ILE A 1 300 ? -16.663 8.214 23.577 1.00 32.53 ? 302 ILE A CG2 1 ATOM 2395 C CD1 . ILE A 1 300 ? -19.072 6.450 25.014 1.00 37.12 ? 302 ILE A CD1 1 ATOM 2396 N N . GLY A 1 301 ? -16.407 9.075 20.377 1.00 31.10 ? 303 GLY A N 1 ATOM 2397 C CA . GLY A 1 301 ? -15.203 9.198 19.566 1.00 32.13 ? 303 GLY A CA 1 ATOM 2398 C C . GLY A 1 301 ? -15.464 9.989 18.296 1.00 33.16 ? 303 GLY A C 1 ATOM 2399 O O . GLY A 1 301 ? -16.375 10.823 18.244 1.00 33.91 ? 303 GLY A O 1 ATOM 2400 N N . GLU A 1 302 ? -14.669 9.695 17.277 1.00 33.22 ? 304 GLU A N 1 ATOM 2401 C CA . GLU A 1 302 ? -14.710 10.370 15.980 1.00 34.23 ? 304 GLU A CA 1 ATOM 2402 C C . GLU A 1 302 ? -15.587 9.524 15.058 1.00 33.14 ? 304 GLU A C 1 ATOM 2403 O O . GLU A 1 302 ? -15.116 8.565 14.454 1.00 32.73 ? 304 GLU A O 1 ATOM 2404 C CB . GLU A 1 302 ? -13.282 10.508 15.444 1.00 33.92 ? 304 GLU A CB 1 ATOM 2405 C CG . GLU A 1 302 ? -12.320 11.205 16.444 1.00 37.06 ? 304 GLU A CG 1 ATOM 2406 C CD . GLU A 1 302 ? -10.821 11.083 16.093 1.00 37.44 ? 304 GLU A CD 1 ATOM 2407 O OE1 . GLU A 1 302 ? -10.232 9.970 16.146 1.00 41.26 ? 304 GLU A OE1 1 ATOM 2408 O OE2 . GLU A 1 302 ? -10.210 12.135 15.800 1.00 44.32 ? 304 GLU A OE2 1 ATOM 2409 N N . CYS A 1 303 ? -16.874 9.861 15.000 1.00 32.70 ? 305 CYS A N 1 ATOM 2410 C CA . CYS A 1 303 ? -17.874 8.982 14.382 1.00 32.51 ? 305 CYS A CA 1 ATOM 2411 C C . CYS A 1 303 ? -18.577 9.587 13.167 1.00 31.90 ? 305 CYS A C 1 ATOM 2412 O O . CYS A 1 303 ? -18.578 10.808 13.009 1.00 32.04 ? 305 CYS A O 1 ATOM 2413 C CB . CYS A 1 303 ? -18.928 8.569 15.412 1.00 32.16 ? 305 CYS A CB 1 ATOM 2414 S SG . CYS A 1 303 ? -18.286 7.484 16.741 1.00 34.81 ? 305 CYS A SG 1 ATOM 2415 N N . PRO A 1 304 ? -19.206 8.729 12.330 1.00 30.96 ? 306 PRO A N 1 ATOM 2416 C CA . PRO A 1 304 ? -20.080 9.271 11.294 1.00 30.25 ? 306 PRO A CA 1 ATOM 2417 C C . PRO A 1 304 ? -21.355 9.798 11.939 1.00 30.10 ? 306 PRO A C 1 ATOM 2418 O O . PRO A 1 304 ? -21.603 9.549 13.122 1.00 30.05 ? 306 PRO A O 1 ATOM 2419 C CB . PRO A 1 304 ? -20.400 8.047 10.418 1.00 29.85 ? 306 PRO A CB 1 ATOM 2420 C CG . PRO A 1 304 ? -19.470 6.949 10.854 1.00 30.30 ? 306 PRO A CG 1 ATOM 2421 C CD . PRO A 1 304 ? -19.194 7.251 12.303 1.00 30.58 ? 306 PRO A CD 1 ATOM 2422 N N . LYS A 1 305 ? -22.166 10.518 11.182 1.00 29.81 ? 307 LYS A N 1 ATOM 2423 C CA A LYS A 1 305 ? -23.429 11.007 11.725 0.50 29.98 ? 307 LYS A CA 1 ATOM 2424 C CA B LYS A 1 305 ? -23.440 11.026 11.685 0.50 29.94 ? 307 LYS A CA 1 ATOM 2425 C C . LYS A 1 305 ? -24.490 9.913 11.680 1.00 30.04 ? 307 LYS A C 1 ATOM 2426 O O . LYS A 1 305 ? -24.654 9.216 10.673 1.00 29.56 ? 307 LYS A O 1 ATOM 2427 C CB A LYS A 1 305 ? -23.900 12.278 11.007 0.50 30.62 ? 307 LYS A CB 1 ATOM 2428 C CB B LYS A 1 305 ? -23.917 12.213 10.834 0.50 30.50 ? 307 LYS A CB 1 ATOM 2429 C CG A LYS A 1 305 ? -22.952 13.486 11.147 0.50 31.21 ? 307 LYS A CG 1 ATOM 2430 C CG B LYS A 1 305 ? -22.818 13.232 10.450 0.50 30.99 ? 307 LYS A CG 1 ATOM 2431 C CD A LYS A 1 305 ? -22.636 13.846 12.608 0.50 32.39 ? 307 LYS A CD 1 ATOM 2432 C CD B LYS A 1 305 ? -22.005 13.741 11.665 0.50 31.87 ? 307 LYS A CD 1 ATOM 2433 C CE A LYS A 1 305 ? -21.250 14.484 12.746 0.50 31.50 ? 307 LYS A CE 1 ATOM 2434 C CE B LYS A 1 305 ? -22.680 14.916 12.380 0.50 32.05 ? 307 LYS A CE 1 ATOM 2435 N NZ A LYS A 1 305 ? -20.160 13.455 12.780 0.50 31.63 ? 307 LYS A NZ 1 ATOM 2436 N NZ B LYS A 1 305 ? -22.458 14.879 13.855 0.50 32.52 ? 307 LYS A NZ 1 ATOM 2437 N N . TYR A 1 306 ? -25.208 9.754 12.790 1.00 29.44 ? 308 TYR A N 1 ATOM 2438 C CA . TYR A 1 306 ? -26.233 8.720 12.887 1.00 29.19 ? 308 TYR A CA 1 ATOM 2439 C C . TYR A 1 306 ? -27.583 9.143 12.296 1.00 29.55 ? 308 TYR A C 1 ATOM 2440 O O . TYR A 1 306 ? -28.080 10.238 12.581 1.00 29.34 ? 308 TYR A O 1 ATOM 2441 C CB . TYR A 1 306 ? -26.435 8.298 14.344 1.00 29.28 ? 308 TYR A CB 1 ATOM 2442 C CG . TYR A 1 306 ? -27.591 7.348 14.579 1.00 27.91 ? 308 TYR A CG 1 ATOM 2443 C CD1 . TYR A 1 306 ? -27.451 5.977 14.352 1.00 25.94 ? 308 TYR A CD1 1 ATOM 2444 C CD2 . TYR A 1 306 ? -28.815 7.807 15.073 1.00 28.56 ? 308 TYR A CD2 1 ATOM 2445 C CE1 . TYR A 1 306 ? -28.482 5.105 14.570 1.00 26.69 ? 308 TYR A CE1 1 ATOM 2446 C CE2 . TYR A 1 306 ? -29.864 6.926 15.313 1.00 27.79 ? 308 TYR A CE2 1 ATOM 2447 C CZ . TYR A 1 306 ? -29.698 5.580 15.046 1.00 28.65 ? 308 TYR A CZ 1 ATOM 2448 O OH . TYR A 1 306 ? -30.727 4.693 15.268 1.00 29.87 ? 308 TYR A OH 1 ATOM 2449 N N . VAL A 1 307 ? -28.172 8.248 11.504 1.00 29.32 ? 309 VAL A N 1 ATOM 2450 C CA . VAL A 1 307 ? -29.560 8.381 11.022 1.00 29.50 ? 309 VAL A CA 1 ATOM 2451 C C . VAL A 1 307 ? -30.289 7.050 11.183 1.00 30.00 ? 309 VAL A C 1 ATOM 2452 O O . VAL A 1 307 ? -29.653 5.986 11.212 1.00 29.56 ? 309 VAL A O 1 ATOM 2453 C CB . VAL A 1 307 ? -29.637 8.812 9.525 1.00 29.48 ? 309 VAL A CB 1 ATOM 2454 C CG1 . VAL A 1 307 ? -29.239 10.272 9.357 1.00 30.35 ? 309 VAL A CG1 1 ATOM 2455 C CG2 . VAL A 1 307 ? -28.790 7.870 8.623 1.00 29.71 ? 309 VAL A CG2 1 ATOM 2456 N N . LYS A 1 308 ? -31.616 7.113 11.268 1.00 30.19 ? 310 LYS A N 1 ATOM 2457 C CA . LYS A 1 308 ? -32.478 5.932 11.369 1.00 31.87 ? 310 LYS A CA 1 ATOM 2458 C C . LYS A 1 308 ? -32.631 5.130 10.058 1.00 32.02 ? 310 LYS A C 1 ATOM 2459 O O . LYS A 1 308 ? -33.267 4.071 10.044 1.00 33.02 ? 310 LYS A O 1 ATOM 2460 C CB . LYS A 1 308 ? -33.886 6.332 11.847 1.00 32.38 ? 310 LYS A CB 1 ATOM 2461 C CG . LYS A 1 308 ? -34.031 6.688 13.314 1.00 34.76 ? 310 LYS A CG 1 ATOM 2462 C CD . LYS A 1 308 ? -35.508 6.619 13.708 1.00 38.93 ? 310 LYS A CD 1 ATOM 2463 C CE . LYS A 1 308 ? -35.748 6.867 15.196 1.00 41.59 ? 310 LYS A CE 1 ATOM 2464 N NZ . LYS A 1 308 ? -36.137 8.288 15.499 1.00 41.72 ? 310 LYS A NZ 1 ATOM 2465 N N . SER A 1 309 ? -32.038 5.615 8.976 1.00 32.29 ? 311 SER A N 1 ATOM 2466 C CA . SER A 1 309 ? -32.294 5.064 7.637 1.00 32.31 ? 311 SER A CA 1 ATOM 2467 C C . SER A 1 309 ? -31.882 3.606 7.501 1.00 32.23 ? 311 SER A C 1 ATOM 2468 O O . SER A 1 309 ? -30.903 3.185 8.105 1.00 31.68 ? 311 SER A O 1 ATOM 2469 C CB . SER A 1 309 ? -31.574 5.895 6.578 1.00 32.32 ? 311 SER A CB 1 ATOM 2470 O OG . SER A 1 309 ? -31.781 7.278 6.802 1.00 32.67 ? 311 SER A OG 1 ATOM 2471 N N . GLU A 1 310 ? -32.638 2.844 6.708 1.00 32.14 ? 312 GLU A N 1 ATOM 2472 C CA . GLU A 1 310 ? -32.235 1.487 6.352 1.00 32.77 ? 312 GLU A CA 1 ATOM 2473 C C . GLU A 1 310 ? -31.277 1.521 5.155 1.00 31.58 ? 312 GLU A C 1 ATOM 2474 O O . GLU A 1 310 ? -30.467 0.610 4.974 1.00 31.18 ? 312 GLU A O 1 ATOM 2475 C CB . GLU A 1 310 ? -33.448 0.607 6.042 1.00 33.18 ? 312 GLU A CB 1 ATOM 2476 C CG . GLU A 1 310 ? -34.389 0.375 7.236 1.00 35.89 ? 312 GLU A CG 1 ATOM 2477 C CD . GLU A 1 310 ? -35.451 -0.696 6.952 1.00 36.33 ? 312 GLU A CD 1 ATOM 2478 O OE1 . GLU A 1 310 ? -35.067 -1.867 6.707 1.00 41.47 ? 312 GLU A OE1 1 ATOM 2479 O OE2 . GLU A 1 310 ? -36.669 -0.375 6.982 1.00 41.25 ? 312 GLU A OE2 1 ATOM 2480 N N . LYS A 1 311 ? -31.377 2.577 4.350 1.00 30.39 ? 313 LYS A N 1 ATOM 2481 C CA . LYS A 1 311 ? -30.525 2.739 3.179 1.00 29.75 ? 313 LYS A CA 1 ATOM 2482 C C . LYS A 1 311 ? -30.364 4.202 2.771 1.00 28.01 ? 313 LYS A C 1 ATOM 2483 O O . LYS A 1 311 ? -31.300 5.000 2.848 1.00 27.40 ? 313 LYS A O 1 ATOM 2484 C CB . LYS A 1 311 ? -31.048 1.916 1.984 1.00 29.93 ? 313 LYS A CB 1 ATOM 2485 C CG . LYS A 1 311 ? -32.489 2.206 1.619 1.00 31.39 ? 313 LYS A CG 1 ATOM 2486 C CD . LYS A 1 311 ? -32.924 1.538 0.326 1.00 31.57 ? 313 LYS A CD 1 ATOM 2487 C CE . LYS A 1 311 ? -34.393 1.870 0.075 1.00 34.41 ? 313 LYS A CE 1 ATOM 2488 N NZ . LYS A 1 311 ? -34.927 1.274 -1.176 1.00 37.54 ? 313 LYS A NZ 1 ATOM 2489 N N . LEU A 1 312 ? -29.155 4.527 2.331 1.00 27.13 ? 314 LEU A N 1 ATOM 2490 C CA . LEU A 1 312 ? -28.853 5.810 1.728 1.00 26.16 ? 314 LEU A CA 1 ATOM 2491 C C . LEU A 1 312 ? -27.910 5.555 0.556 1.00 25.54 ? 314 LEU A C 1 ATOM 2492 O O . LEU A 1 312 ? -26.703 5.392 0.731 1.00 25.14 ? 314 LEU A O 1 ATOM 2493 C CB . LEU A 1 312 ? -28.230 6.773 2.740 1.00 26.56 ? 314 LEU A CB 1 ATOM 2494 C CG . LEU A 1 312 ? -29.139 7.352 3.826 1.00 27.46 ? 314 LEU A CG 1 ATOM 2495 C CD1 . LEU A 1 312 ? -28.297 8.123 4.823 1.00 28.17 ? 314 LEU A CD1 1 ATOM 2496 C CD2 . LEU A 1 312 ? -30.245 8.237 3.225 1.00 27.75 ? 314 LEU A CD2 1 ATOM 2497 N N . VAL A 1 313 ? -28.481 5.496 -0.645 1.00 24.57 ? 315 VAL A N 1 ATOM 2498 C CA . VAL A 1 313 ? -27.692 5.229 -1.835 1.00 23.80 ? 315 VAL A CA 1 ATOM 2499 C C . VAL A 1 313 ? -27.896 6.365 -2.823 1.00 23.43 ? 315 VAL A C 1 ATOM 2500 O O . VAL A 1 313 ? -29.021 6.642 -3.235 1.00 22.89 ? 315 VAL A O 1 ATOM 2501 C CB . VAL A 1 313 ? -28.070 3.888 -2.503 1.00 23.70 ? 315 VAL A CB 1 ATOM 2502 C CG1 . VAL A 1 313 ? -27.183 3.632 -3.724 1.00 22.68 ? 315 VAL A CG1 1 ATOM 2503 C CG2 . VAL A 1 313 ? -27.956 2.743 -1.531 1.00 24.20 ? 315 VAL A CG2 1 ATOM 2504 N N . LEU A 1 314 ? -26.796 7.027 -3.175 1.00 23.18 ? 316 LEU A N 1 ATOM 2505 C CA . LEU A 1 314 ? -26.812 8.102 -4.148 1.00 23.23 ? 316 LEU A CA 1 ATOM 2506 C C . LEU A 1 314 ? -26.511 7.553 -5.537 1.00 22.46 ? 316 LEU A C 1 ATOM 2507 O O . LEU A 1 314 ? -25.509 6.864 -5.722 1.00 22.96 ? 316 LEU A O 1 ATOM 2508 C CB . LEU A 1 314 ? -25.737 9.130 -3.799 1.00 23.48 ? 316 LEU A CB 1 ATOM 2509 C CG . LEU A 1 314 ? -26.069 10.286 -2.863 1.00 24.71 ? 316 LEU A CG 1 ATOM 2510 C CD1 . LEU A 1 314 ? -24.737 10.947 -2.515 1.00 26.69 ? 316 LEU A CD1 1 ATOM 2511 C CD2 . LEU A 1 314 ? -27.050 11.302 -3.469 1.00 23.41 ? 316 LEU A CD2 1 ATOM 2512 N N . ALA A 1 315 ? -27.360 7.863 -6.514 1.00 22.14 ? 317 ALA A N 1 ATOM 2513 C CA . ALA A 1 315 ? -27.027 7.566 -7.900 1.00 21.27 ? 317 ALA A CA 1 ATOM 2514 C C . ALA A 1 315 ? -25.862 8.463 -8.286 1.00 20.66 ? 317 ALA A C 1 ATOM 2515 O O . ALA A 1 315 ? -25.859 9.656 -7.964 1.00 20.89 ? 317 ALA A O 1 ATOM 2516 C CB . ALA A 1 315 ? -28.222 7.836 -8.812 1.00 20.98 ? 317 ALA A CB 1 ATOM 2517 N N . THR A 1 316 ? -24.877 7.893 -8.967 1.00 19.65 ? 318 THR A N 1 ATOM 2518 C CA . THR A 1 316 ? -23.819 8.696 -9.562 1.00 19.10 ? 318 THR A CA 1 ATOM 2519 C C . THR A 1 316 ? -23.831 8.535 -11.099 1.00 18.65 ? 318 THR A C 1 ATOM 2520 O O . THR A 1 316 ? -23.713 9.513 -11.844 1.00 19.10 ? 318 THR A O 1 ATOM 2521 C CB . THR A 1 316 ? -22.431 8.374 -8.980 1.00 19.52 ? 318 THR A CB 1 ATOM 2522 O OG1 . THR A 1 316 ? -22.092 7.001 -9.226 1.00 20.03 ? 318 THR A OG1 1 ATOM 2523 C CG2 . THR A 1 316 ? -22.396 8.669 -7.464 1.00 19.14 ? 318 THR A CG2 1 ATOM 2524 N N . GLY A 1 317 ? -23.997 7.297 -11.550 1.00 17.57 ? 319 GLY A N 1 ATOM 2525 C CA . GLY A 1 317 ? -24.154 7.025 -12.988 1.00 17.65 ? 319 GLY A CA 1 ATOM 2526 C C . GLY A 1 317 ? -25.572 7.261 -13.478 1.00 17.61 ? 319 GLY A C 1 ATOM 2527 O O . GLY A 1 317 ? -26.398 7.861 -12.790 1.00 17.17 ? 319 GLY A O 1 ATOM 2528 N N . LEU A 1 318 ? -25.852 6.810 -14.698 1.00 17.00 ? 320 LEU A N 1 ATOM 2529 C CA . LEU A 1 318 ? -27.162 7.021 -15.311 1.00 17.39 ? 320 LEU A CA 1 ATOM 2530 C C . LEU A 1 318 ? -28.000 5.756 -15.188 1.00 17.55 ? 320 LEU A C 1 ATOM 2531 O O . LEU A 1 318 ? -27.511 4.714 -14.724 1.00 17.45 ? 320 LEU A O 1 ATOM 2532 C CB . LEU A 1 318 ? -27.021 7.444 -16.779 1.00 17.43 ? 320 LEU A CB 1 ATOM 2533 C CG . LEU A 1 318 ? -26.200 6.500 -17.657 1.00 17.44 ? 320 LEU A CG 1 ATOM 2534 C CD1 . LEU A 1 318 ? -26.801 6.415 -19.059 1.00 17.92 ? 320 LEU A CD1 1 ATOM 2535 C CD2 . LEU A 1 318 ? -24.760 6.961 -17.709 1.00 20.40 ? 320 LEU A CD2 1 ATOM 2536 N N . ARG A 1 319 ? -29.266 5.879 -15.570 1.00 18.06 ? 321 ARG A N 1 ATOM 2537 C CA . ARG A 1 319 ? -30.199 4.767 -15.663 1.00 19.50 ? 321 ARG A CA 1 ATOM 2538 C C . ARG A 1 319 ? -29.573 3.692 -16.556 1.00 20.08 ? 321 ARG A C 1 ATOM 2539 O O . ARG A 1 319 ? -29.134 3.989 -17.679 1.00 19.50 ? 321 ARG A O 1 ATOM 2540 C CB . ARG A 1 319 ? -31.529 5.279 -16.233 1.00 19.84 ? 321 ARG A CB 1 ATOM 2541 C CG . ARG A 1 319 ? -32.648 4.243 -16.379 1.00 20.59 ? 321 ARG A CG 1 ATOM 2542 C CD . ARG A 1 319 ? -33.882 4.847 -17.019 1.00 21.03 ? 321 ARG A CD 1 ATOM 2543 N NE . ARG A 1 319 ? -34.316 6.056 -16.327 1.00 23.02 ? 321 ARG A NE 1 ATOM 2544 C CZ . ARG A 1 319 ? -35.267 6.087 -15.394 1.00 25.81 ? 321 ARG A CZ 1 ATOM 2545 N NH1 . ARG A 1 319 ? -35.915 4.976 -15.069 1.00 24.75 ? 321 ARG A NH1 1 ATOM 2546 N NH2 . ARG A 1 319 ? -35.578 7.235 -14.797 1.00 25.44 ? 321 ARG A NH2 1 ATOM 2547 N N . ASN A 1 320 ? -29.498 2.471 -16.028 1.00 20.70 ? 322 ASN A N 1 ATOM 2548 C CA . ASN A 1 320 ? -28.892 1.329 -16.717 1.00 22.36 ? 322 ASN A CA 1 ATOM 2549 C C . ASN A 1 320 ? -29.956 0.698 -17.595 1.00 23.88 ? 322 ASN A C 1 ATOM 2550 O O . ASN A 1 320 ? -30.872 0.042 -17.094 1.00 24.14 ? 322 ASN A O 1 ATOM 2551 C CB . ASN A 1 320 ? -28.336 0.304 -15.717 1.00 22.59 ? 322 ASN A CB 1 ATOM 2552 C CG . ASN A 1 320 ? -27.251 -0.595 -16.315 1.00 22.77 ? 322 ASN A CG 1 ATOM 2553 O OD1 . ASN A 1 320 ? -26.790 -0.381 -17.436 1.00 20.74 ? 322 ASN A OD1 1 ATOM 2554 N ND2 . ASN A 1 320 ? -26.818 -1.598 -15.539 1.00 23.71 ? 322 ASN A ND2 1 ATOM 2555 N N . VAL A 1 321 ? -29.835 0.929 -18.899 1.00 25.07 ? 323 VAL A N 1 ATOM 2556 C CA . VAL A 1 321 ? -30.840 0.512 -19.874 1.00 26.70 ? 323 VAL A CA 1 ATOM 2557 C C . VAL A 1 321 ? -30.323 -0.619 -20.780 1.00 28.19 ? 323 VAL A C 1 ATOM 2558 O O . VAL A 1 321 ? -29.444 -0.394 -21.633 1.00 28.66 ? 323 VAL A O 1 ATOM 2559 C CB . VAL A 1 321 ? -31.341 1.695 -20.763 1.00 26.23 ? 323 VAL A CB 1 ATOM 2560 C CG1 . VAL A 1 321 ? -32.497 1.246 -21.645 1.00 26.20 ? 323 VAL A CG1 1 ATOM 2561 C CG2 . VAL A 1 321 ? -31.772 2.883 -19.925 1.00 26.73 ? 323 VAL A CG2 1 ATOM 2562 N N . PRO A 1 322 ? -30.905 -1.826 -20.625 1.00 29.31 ? 324 PRO A N 1 ATOM 2563 C CA . PRO A 1 322 ? -30.706 -2.996 -21.495 1.00 29.88 ? 324 PRO A CA 1 ATOM 2564 C C . PRO A 1 322 ? -30.468 -2.632 -22.973 1.00 30.25 ? 324 PRO A C 1 ATOM 2565 O O . PRO A 1 322 ? -31.291 -1.944 -23.599 1.00 31.23 ? 324 PRO A O 1 ATOM 2566 C CB . PRO A 1 322 ? -32.036 -3.762 -21.357 1.00 29.83 ? 324 PRO A CB 1 ATOM 2567 C CG . PRO A 1 322 ? -32.868 -2.987 -20.286 1.00 30.10 ? 324 PRO A CG 1 ATOM 2568 C CD . PRO A 1 322 ? -31.885 -2.124 -19.567 1.00 29.36 ? 324 PRO A CD 1 ATOM 2569 N N . GLY B 2 1 ? -37.400 9.966 -19.558 1.00 29.00 ? 1 GLY B N 1 ATOM 2570 C CA . GLY B 2 1 ? -36.908 10.993 -18.607 1.00 28.97 ? 1 GLY B CA 1 ATOM 2571 C C . GLY B 2 1 ? -37.168 12.400 -19.104 1.00 28.73 ? 1 GLY B C 1 ATOM 2572 O O . GLY B 2 1 ? -37.693 12.602 -20.202 1.00 28.73 ? 1 GLY B O 1 ATOM 2573 N N . LEU B 2 2 ? -36.753 13.377 -18.309 1.00 28.65 ? 2 LEU B N 1 ATOM 2574 C CA . LEU B 2 2 ? -37.141 14.769 -18.539 1.00 28.38 ? 2 LEU B CA 1 ATOM 2575 C C . LEU B 2 2 ? -36.710 15.299 -19.913 1.00 27.96 ? 2 LEU B C 1 ATOM 2576 O O . LEU B 2 2 ? -37.405 16.113 -20.525 1.00 26.84 ? 2 LEU B O 1 ATOM 2577 C CB . LEU B 2 2 ? -36.587 15.639 -17.412 1.00 29.48 ? 2 LEU B CB 1 ATOM 2578 C CG . LEU B 2 2 ? -37.491 16.669 -16.731 1.00 29.79 ? 2 LEU B CG 1 ATOM 2579 C CD1 . LEU B 2 2 ? -38.916 16.170 -16.445 1.00 30.62 ? 2 LEU B CD1 1 ATOM 2580 C CD2 . LEU B 2 2 ? -36.821 17.154 -15.466 1.00 29.80 ? 2 LEU B CD2 1 ATOM 2581 N N . PHE B 2 3 ? -35.577 14.803 -20.400 1.00 26.89 ? 3 PHE B N 1 ATOM 2582 C CA . PHE B 2 3 ? -35.001 15.323 -21.638 1.00 26.47 ? 3 PHE B CA 1 ATOM 2583 C C . PHE B 2 3 ? -35.220 14.440 -22.862 1.00 26.04 ? 3 PHE B C 1 ATOM 2584 O O . PHE B 2 3 ? -34.875 14.829 -23.987 1.00 25.08 ? 3 PHE B O 1 ATOM 2585 C CB . PHE B 2 3 ? -33.545 15.730 -21.381 1.00 26.66 ? 3 PHE B CB 1 ATOM 2586 C CG . PHE B 2 3 ? -33.447 16.845 -20.395 1.00 27.49 ? 3 PHE B CG 1 ATOM 2587 C CD1 . PHE B 2 3 ? -33.602 18.163 -20.805 1.00 29.84 ? 3 PHE B CD1 1 ATOM 2588 C CD2 . PHE B 2 3 ? -33.300 16.575 -19.034 1.00 28.83 ? 3 PHE B CD2 1 ATOM 2589 C CE1 . PHE B 2 3 ? -33.572 19.205 -19.883 1.00 30.20 ? 3 PHE B CE1 1 ATOM 2590 C CE2 . PHE B 2 3 ? -33.274 17.611 -18.106 1.00 29.59 ? 3 PHE B CE2 1 ATOM 2591 C CZ . PHE B 2 3 ? -33.405 18.921 -18.530 1.00 29.60 ? 3 PHE B CZ 1 ATOM 2592 N N . GLY B 2 4 ? -35.838 13.282 -22.630 1.00 24.76 ? 4 GLY B N 1 ATOM 2593 C CA . GLY B 2 4 ? -36.363 12.407 -23.686 1.00 24.43 ? 4 GLY B CA 1 ATOM 2594 C C . GLY B 2 4 ? -35.369 11.562 -24.470 1.00 24.03 ? 4 GLY B C 1 ATOM 2595 O O . GLY B 2 4 ? -35.757 10.927 -25.445 1.00 24.15 ? 4 GLY B O 1 ATOM 2596 N N . ALA B 2 5 ? -34.099 11.568 -24.058 1.00 23.34 ? 5 ALA B N 1 ATOM 2597 C CA . ALA B 2 5 ? -33.039 10.835 -24.774 1.00 23.60 ? 5 ALA B CA 1 ATOM 2598 C C . ALA B 2 5 ? -32.812 9.448 -24.196 1.00 23.29 ? 5 ALA B C 1 ATOM 2599 O O . ALA B 2 5 ? -33.021 8.457 -24.876 1.00 23.51 ? 5 ALA B O 1 ATOM 2600 C CB . ALA B 2 5 ? -31.741 11.623 -24.762 1.00 23.63 ? 5 ALA B CB 1 ATOM 2601 N N . ILE B 2 6 ? -32.369 9.392 -22.942 1.00 23.09 ? 6 ILE B N 1 ATOM 2602 C CA . ILE B 2 6 ? -32.112 8.112 -22.277 1.00 23.34 ? 6 ILE B CA 1 ATOM 2603 C C . ILE B 2 6 ? -33.400 7.312 -22.096 1.00 23.88 ? 6 ILE B C 1 ATOM 2604 O O . ILE B 2 6 ? -34.395 7.824 -21.584 1.00 24.18 ? 6 ILE B O 1 ATOM 2605 C CB . ILE B 2 6 ? -31.390 8.311 -20.924 1.00 22.72 ? 6 ILE B CB 1 ATOM 2606 C CG1 . ILE B 2 6 ? -29.964 8.797 -21.170 1.00 21.62 ? 6 ILE B CG1 1 ATOM 2607 C CG2 . ILE B 2 6 ? -31.366 7.009 -20.132 1.00 22.92 ? 6 ILE B CG2 1 ATOM 2608 C CD1 . ILE B 2 6 ? -29.226 9.262 -19.881 1.00 22.95 ? 6 ILE B CD1 1 ATOM 2609 N N . ALA B 2 7 ? -33.371 6.056 -22.533 1.00 24.98 ? 7 ALA B N 1 ATOM 2610 C CA . ALA B 2 7 ? -34.577 5.220 -22.614 1.00 25.78 ? 7 ALA B CA 1 ATOM 2611 C C . ALA B 2 7 ? -35.722 6.020 -23.262 1.00 26.15 ? 7 ALA B C 1 ATOM 2612 O O . ALA B 2 7 ? -36.887 5.950 -22.853 1.00 26.67 ? 7 ALA B O 1 ATOM 2613 C CB . ALA B 2 7 ? -34.966 4.674 -21.242 1.00 26.14 ? 7 ALA B CB 1 ATOM 2614 N N . GLY B 2 8 ? -35.350 6.814 -24.262 1.00 25.90 ? 8 GLY B N 1 ATOM 2615 C CA . GLY B 2 8 ? -36.297 7.645 -24.984 1.00 25.56 ? 8 GLY B CA 1 ATOM 2616 C C . GLY B 2 8 ? -36.089 7.410 -26.460 1.00 25.68 ? 8 GLY B C 1 ATOM 2617 O O . GLY B 2 8 ? -36.202 6.275 -26.936 1.00 25.73 ? 8 GLY B O 1 ATOM 2618 N N . PHE B 2 9 ? -35.748 8.467 -27.196 1.00 25.62 ? 9 PHE B N 1 ATOM 2619 C CA . PHE B 2 9 ? -35.511 8.278 -28.630 1.00 25.28 ? 9 PHE B CA 1 ATOM 2620 C C . PHE B 2 9 ? -34.245 7.472 -28.880 1.00 24.80 ? 9 PHE B C 1 ATOM 2621 O O . PHE B 2 9 ? -34.143 6.777 -29.890 1.00 24.62 ? 9 PHE B O 1 ATOM 2622 C CB . PHE B 2 9 ? -35.550 9.583 -29.430 1.00 25.62 ? 9 PHE B CB 1 ATOM 2623 C CG . PHE B 2 9 ? -34.360 10.480 -29.234 1.00 25.46 ? 9 PHE B CG 1 ATOM 2624 C CD1 . PHE B 2 9 ? -33.217 10.332 -30.025 1.00 27.33 ? 9 PHE B CD1 1 ATOM 2625 C CD2 . PHE B 2 9 ? -34.397 11.522 -28.306 1.00 24.53 ? 9 PHE B CD2 1 ATOM 2626 C CE1 . PHE B 2 9 ? -32.114 11.191 -29.864 1.00 26.57 ? 9 PHE B CE1 1 ATOM 2627 C CE2 . PHE B 2 9 ? -33.297 12.378 -28.153 1.00 26.15 ? 9 PHE B CE2 1 ATOM 2628 C CZ . PHE B 2 9 ? -32.161 12.208 -28.933 1.00 26.51 ? 9 PHE B CZ 1 ATOM 2629 N N . ILE B 2 10 ? -33.286 7.562 -27.955 1.00 24.34 ? 10 ILE B N 1 ATOM 2630 C CA . ILE B 2 10 ? -32.167 6.622 -27.935 1.00 24.54 ? 10 ILE B CA 1 ATOM 2631 C C . ILE B 2 10 ? -32.598 5.487 -26.995 1.00 25.40 ? 10 ILE B C 1 ATOM 2632 O O . ILE B 2 10 ? -32.499 5.604 -25.777 1.00 25.16 ? 10 ILE B O 1 ATOM 2633 C CB . ILE B 2 10 ? -30.840 7.283 -27.495 1.00 24.20 ? 10 ILE B CB 1 ATOM 2634 C CG1 . ILE B 2 10 ? -30.517 8.470 -28.417 1.00 24.37 ? 10 ILE B CG1 1 ATOM 2635 C CG2 . ILE B 2 10 ? -29.694 6.245 -27.525 1.00 24.03 ? 10 ILE B CG2 1 ATOM 2636 C CD1 . ILE B 2 10 ? -29.323 9.293 -27.970 1.00 24.65 ? 10 ILE B CD1 1 ATOM 2637 N N . GLU B 2 11 ? -33.100 4.402 -27.589 1.00 26.42 ? 11 GLU B N 1 ATOM 2638 C CA . GLU B 2 11 ? -33.899 3.421 -26.848 1.00 27.55 ? 11 GLU B CA 1 ATOM 2639 C C . GLU B 2 11 ? -33.144 2.601 -25.806 1.00 27.25 ? 11 GLU B C 1 ATOM 2640 O O . GLU B 2 11 ? -33.726 2.200 -24.789 1.00 28.52 ? 11 GLU B O 1 ATOM 2641 C CB . GLU B 2 11 ? -34.636 2.508 -27.820 1.00 28.39 ? 11 GLU B CB 1 ATOM 2642 C CG . GLU B 2 11 ? -35.752 3.214 -28.570 1.00 31.93 ? 11 GLU B CG 1 ATOM 2643 C CD . GLU B 2 11 ? -36.374 2.363 -29.651 1.00 36.41 ? 11 GLU B CD 1 ATOM 2644 O OE1 . GLU B 2 11 ? -37.109 2.942 -30.492 1.00 38.85 ? 11 GLU B OE1 1 ATOM 2645 O OE2 . GLU B 2 11 ? -36.114 1.133 -29.689 1.00 38.26 ? 11 GLU B OE2 1 ATOM 2646 N N . GLY B 2 12 ? -31.857 2.366 -26.030 1.00 26.61 ? 12 GLY B N 1 ATOM 2647 C CA . GLY B 2 12 ? -31.084 1.571 -25.078 1.00 26.38 ? 12 GLY B CA 1 ATOM 2648 C C . GLY B 2 12 ? -29.639 1.994 -24.953 1.00 26.26 ? 12 GLY B C 1 ATOM 2649 O O . GLY B 2 12 ? -29.147 2.817 -25.739 1.00 25.93 ? 12 GLY B O 1 ATOM 2650 N N . GLY B 2 13 ? -28.955 1.425 -23.961 1.00 25.87 ? 13 GLY B N 1 ATOM 2651 C CA . GLY B 2 13 ? -27.544 1.692 -23.751 1.00 25.61 ? 13 GLY B CA 1 ATOM 2652 C C . GLY B 2 13 ? -26.598 0.761 -24.478 1.00 26.47 ? 13 GLY B C 1 ATOM 2653 O O . GLY B 2 13 ? -27.009 -0.242 -25.075 1.00 25.99 ? 13 GLY B O 1 ATOM 2654 N N . TRP B 2 14 ? -25.316 1.100 -24.411 1.00 26.60 ? 14 TRP B N 1 ATOM 2655 C CA . TRP B 2 14 ? -24.271 0.338 -25.062 1.00 27.25 ? 14 TRP B CA 1 ATOM 2656 C C . TRP B 2 14 ? -23.321 -0.335 -24.080 1.00 27.83 ? 14 TRP B C 1 ATOM 2657 O O . TRP B 2 14 ? -22.500 0.336 -23.445 1.00 27.50 ? 14 TRP B O 1 ATOM 2658 C CB . TRP B 2 14 ? -23.463 1.255 -25.975 1.00 26.46 ? 14 TRP B CB 1 ATOM 2659 C CG . TRP B 2 14 ? -24.199 1.784 -27.138 1.00 26.87 ? 14 TRP B CG 1 ATOM 2660 C CD1 . TRP B 2 14 ? -25.270 1.217 -27.771 1.00 26.06 ? 14 TRP B CD1 1 ATOM 2661 C CD2 . TRP B 2 14 ? -23.886 2.978 -27.859 1.00 25.10 ? 14 TRP B CD2 1 ATOM 2662 N NE1 . TRP B 2 14 ? -25.653 1.997 -28.831 1.00 27.25 ? 14 TRP B NE1 1 ATOM 2663 C CE2 . TRP B 2 14 ? -24.826 3.088 -28.909 1.00 26.04 ? 14 TRP B CE2 1 ATOM 2664 C CE3 . TRP B 2 14 ? -22.907 3.973 -27.715 1.00 26.17 ? 14 TRP B CE3 1 ATOM 2665 C CZ2 . TRP B 2 14 ? -24.813 4.146 -29.828 1.00 25.73 ? 14 TRP B CZ2 1 ATOM 2666 C CZ3 . TRP B 2 14 ? -22.892 5.038 -28.646 1.00 26.35 ? 14 TRP B CZ3 1 ATOM 2667 C CH2 . TRP B 2 14 ? -23.848 5.110 -29.673 1.00 26.99 ? 14 TRP B CH2 1 ATOM 2668 N N . GLN B 2 15 ? -23.422 -1.662 -23.979 1.00 29.23 ? 15 GLN B N 1 ATOM 2669 C CA . GLN B 2 15 ? -22.471 -2.458 -23.193 1.00 30.89 ? 15 GLN B CA 1 ATOM 2670 C C . GLN B 2 15 ? -21.077 -2.296 -23.793 1.00 31.42 ? 15 GLN B C 1 ATOM 2671 O O . GLN B 2 15 ? -20.074 -2.314 -23.075 1.00 31.58 ? 15 GLN B O 1 ATOM 2672 C CB . GLN B 2 15 ? -22.853 -3.947 -23.180 1.00 31.03 ? 15 GLN B CB 1 ATOM 2673 C CG . GLN B 2 15 ? -24.285 -4.272 -22.712 1.00 32.77 ? 15 GLN B CG 1 ATOM 2674 C CD . GLN B 2 15 ? -24.478 -4.236 -21.203 1.00 34.41 ? 15 GLN B CD 1 ATOM 2675 O OE1 . GLN B 2 15 ? -23.635 -4.709 -20.438 1.00 34.84 ? 15 GLN B OE1 1 ATOM 2676 N NE2 . GLN B 2 15 ? -25.617 -3.706 -20.772 1.00 34.68 ? 15 GLN B NE2 1 ATOM 2677 N N . GLY B 2 16 ? -21.033 -2.123 -25.114 1.00 32.17 ? 16 GLY B N 1 ATOM 2678 C CA . GLY B 2 16 ? -19.790 -2.003 -25.859 1.00 33.10 ? 16 GLY B CA 1 ATOM 2679 C C . GLY B 2 16 ? -19.042 -0.692 -25.732 1.00 34.02 ? 16 GLY B C 1 ATOM 2680 O O . GLY B 2 16 ? -17.945 -0.559 -26.279 1.00 34.09 ? 16 GLY B O 1 ATOM 2681 N N . MET B 2 17 ? -19.629 0.284 -25.040 1.00 34.79 ? 17 MET B N 1 ATOM 2682 C CA . MET B 2 17 ? -18.931 1.534 -24.745 1.00 35.51 ? 17 MET B CA 1 ATOM 2683 C C . MET B 2 17 ? -18.520 1.592 -23.276 1.00 35.83 ? 17 MET B C 1 ATOM 2684 O O . MET B 2 17 ? -19.264 2.077 -22.419 1.00 35.57 ? 17 MET B O 1 ATOM 2685 C CB . MET B 2 17 ? -19.782 2.743 -25.119 1.00 35.40 ? 17 MET B CB 1 ATOM 2686 C CG . MET B 2 17 ? -18.997 4.047 -25.118 1.00 36.25 ? 17 MET B CG 1 ATOM 2687 S SD . MET B 2 17 ? -19.990 5.471 -25.555 1.00 35.97 ? 17 MET B SD 1 ATOM 2688 C CE . MET B 2 17 ? -21.075 5.548 -24.128 1.00 36.22 ? 17 MET B CE 1 ATOM 2689 N N . VAL B 2 18 ? -17.319 1.095 -22.999 1.00 36.58 ? 18 VAL B N 1 ATOM 2690 C CA . VAL B 2 18 ? -16.872 0.870 -21.625 1.00 37.07 ? 18 VAL B CA 1 ATOM 2691 C C . VAL B 2 18 ? -16.052 2.013 -21.010 1.00 37.34 ? 18 VAL B C 1 ATOM 2692 O O . VAL B 2 18 ? -15.787 2.000 -19.805 1.00 37.56 ? 18 VAL B O 1 ATOM 2693 C CB . VAL B 2 18 ? -16.064 -0.454 -21.508 1.00 37.26 ? 18 VAL B CB 1 ATOM 2694 C CG1 . VAL B 2 18 ? -16.948 -1.653 -21.816 1.00 37.82 ? 18 VAL B CG1 1 ATOM 2695 C CG2 . VAL B 2 18 ? -14.862 -0.424 -22.431 1.00 36.93 ? 18 VAL B CG2 1 ATOM 2696 N N . ASP B 2 19 ? -15.662 2.996 -21.826 1.00 37.57 ? 19 ASP B N 1 ATOM 2697 C CA . ASP B 2 19 ? -14.710 4.025 -21.381 1.00 37.69 ? 19 ASP B CA 1 ATOM 2698 C C . ASP B 2 19 ? -15.310 5.402 -21.065 1.00 36.96 ? 19 ASP B C 1 ATOM 2699 O O . ASP B 2 19 ? -14.572 6.368 -20.848 1.00 37.11 ? 19 ASP B O 1 ATOM 2700 C CB . ASP B 2 19 ? -13.533 4.142 -22.367 1.00 38.40 ? 19 ASP B CB 1 ATOM 2701 C CG . ASP B 2 19 ? -13.869 4.966 -23.604 1.00 41.31 ? 19 ASP B CG 1 ATOM 2702 O OD1 . ASP B 2 19 ? -14.751 4.554 -24.404 1.00 43.67 ? 19 ASP B OD1 1 ATOM 2703 O OD2 . ASP B 2 19 ? -13.223 6.024 -23.790 1.00 44.39 ? 19 ASP B OD2 1 ATOM 2704 N N . GLY B 2 20 ? -16.638 5.486 -21.023 1.00 35.49 ? 20 GLY B N 1 ATOM 2705 C CA . GLY B 2 20 ? -17.305 6.743 -20.713 1.00 34.17 ? 20 GLY B CA 1 ATOM 2706 C C . GLY B 2 20 ? -18.807 6.617 -20.592 1.00 32.82 ? 20 GLY B C 1 ATOM 2707 O O . GLY B 2 20 ? -19.384 5.593 -20.947 1.00 32.91 ? 20 GLY B O 1 ATOM 2708 N N . TRP B 2 21 ? -19.438 7.679 -20.104 1.00 31.82 ? 21 TRP B N 1 ATOM 2709 C CA . TRP B 2 21 ? -20.878 7.701 -19.905 1.00 30.17 ? 21 TRP B CA 1 ATOM 2710 C C . TRP B 2 21 ? -21.654 7.956 -21.187 1.00 29.36 ? 21 TRP B C 1 ATOM 2711 O O . TRP B 2 21 ? -22.748 7.428 -21.359 1.00 28.59 ? 21 TRP B O 1 ATOM 2712 C CB . TRP B 2 21 ? -21.260 8.765 -18.864 1.00 30.42 ? 21 TRP B CB 1 ATOM 2713 C CG . TRP B 2 21 ? -21.213 8.287 -17.420 1.00 30.48 ? 21 TRP B CG 1 ATOM 2714 C CD1 . TRP B 2 21 ? -21.435 7.017 -16.961 1.00 30.90 ? 21 TRP B CD1 1 ATOM 2715 C CD2 . TRP B 2 21 ? -20.977 9.096 -16.262 1.00 31.26 ? 21 TRP B CD2 1 ATOM 2716 N NE1 . TRP B 2 21 ? -21.338 6.983 -15.578 1.00 30.10 ? 21 TRP B NE1 1 ATOM 2717 C CE2 . TRP B 2 21 ? -21.055 8.248 -15.129 1.00 31.02 ? 21 TRP B CE2 1 ATOM 2718 C CE3 . TRP B 2 21 ? -20.710 10.460 -16.069 1.00 31.70 ? 21 TRP B CE3 1 ATOM 2719 C CZ2 . TRP B 2 21 ? -20.854 8.719 -13.828 1.00 30.43 ? 21 TRP B CZ2 1 ATOM 2720 C CZ3 . TRP B 2 21 ? -20.512 10.928 -14.773 1.00 30.37 ? 21 TRP B CZ3 1 ATOM 2721 C CH2 . TRP B 2 21 ? -20.590 10.059 -13.670 1.00 30.90 ? 21 TRP B CH2 1 ATOM 2722 N N . TYR B 2 22 ? -21.102 8.807 -22.050 1.00 28.74 ? 22 TYR B N 1 ATOM 2723 C CA . TYR B 2 22 ? -21.747 9.191 -23.307 1.00 28.36 ? 22 TYR B CA 1 ATOM 2724 C C . TYR B 2 22 ? -20.738 9.112 -24.444 1.00 28.31 ? 22 TYR B C 1 ATOM 2725 O O . TYR B 2 22 ? -19.538 9.252 -24.218 1.00 28.39 ? 22 TYR B O 1 ATOM 2726 C CB . TYR B 2 22 ? -22.283 10.629 -23.257 1.00 28.67 ? 22 TYR B CB 1 ATOM 2727 C CG . TYR B 2 22 ? -22.655 11.151 -21.895 1.00 28.58 ? 22 TYR B CG 1 ATOM 2728 C CD1 . TYR B 2 22 ? -23.660 10.539 -21.132 1.00 27.69 ? 22 TYR B CD1 1 ATOM 2729 C CD2 . TYR B 2 22 ? -22.001 12.256 -21.354 1.00 29.28 ? 22 TYR B CD2 1 ATOM 2730 C CE1 . TYR B 2 22 ? -24.000 11.014 -19.890 1.00 30.14 ? 22 TYR B CE1 1 ATOM 2731 C CE2 . TYR B 2 22 ? -22.334 12.738 -20.089 1.00 28.88 ? 22 TYR B CE2 1 ATOM 2732 C CZ . TYR B 2 22 ? -23.340 12.114 -19.374 1.00 29.71 ? 22 TYR B CZ 1 ATOM 2733 O OH . TYR B 2 22 ? -23.699 12.559 -18.133 1.00 30.16 ? 22 TYR B OH 1 ATOM 2734 N N . GLY B 2 23 ? -21.224 8.901 -25.664 1.00 28.07 ? 23 GLY B N 1 ATOM 2735 C CA . GLY B 2 23 ? -20.322 8.855 -26.810 1.00 27.79 ? 23 GLY B CA 1 ATOM 2736 C C . GLY B 2 23 ? -20.924 8.410 -28.131 1.00 28.26 ? 23 GLY B C 1 ATOM 2737 O O . GLY B 2 23 ? -22.112 8.607 -28.392 1.00 27.90 ? 23 GLY B O 1 ATOM 2738 N N . TYR B 2 24 ? -20.083 7.781 -28.942 1.00 28.19 ? 24 TYR B N 1 ATOM 2739 C CA . TYR B 2 24 ? -20.396 7.499 -30.335 1.00 28.86 ? 24 TYR B CA 1 ATOM 2740 C C . TYR B 2 24 ? -20.272 6.025 -30.708 1.00 28.91 ? 24 TYR B C 1 ATOM 2741 O O . TYR B 2 24 ? -19.541 5.251 -30.061 1.00 29.02 ? 24 TYR B O 1 ATOM 2742 C CB . TYR B 2 24 ? -19.485 8.337 -31.247 1.00 29.00 ? 24 TYR B CB 1 ATOM 2743 C CG . TYR B 2 24 ? -19.354 9.788 -30.831 1.00 29.42 ? 24 TYR B CG 1 ATOM 2744 C CD1 . TYR B 2 24 ? -20.224 10.754 -31.328 1.00 30.75 ? 24 TYR B CD1 1 ATOM 2745 C CD2 . TYR B 2 24 ? -18.365 10.192 -29.943 1.00 29.05 ? 24 TYR B CD2 1 ATOM 2746 C CE1 . TYR B 2 24 ? -20.109 12.094 -30.951 1.00 31.07 ? 24 TYR B CE1 1 ATOM 2747 C CE2 . TYR B 2 24 ? -18.251 11.523 -29.550 1.00 29.95 ? 24 TYR B CE2 1 ATOM 2748 C CZ . TYR B 2 24 ? -19.125 12.467 -30.063 1.00 30.32 ? 24 TYR B CZ 1 ATOM 2749 O OH . TYR B 2 24 ? -19.007 13.786 -29.681 1.00 32.14 ? 24 TYR B OH 1 ATOM 2750 N N . HIS B 2 25 ? -21.044 5.650 -31.724 1.00 28.94 ? 25 HIS B N 1 ATOM 2751 C CA . HIS B 2 25 ? -20.815 4.446 -32.507 1.00 29.21 ? 25 HIS B CA 1 ATOM 2752 C C . HIS B 2 25 ? -20.904 4.855 -33.973 1.00 29.14 ? 25 HIS B C 1 ATOM 2753 O O . HIS B 2 25 ? -21.916 5.413 -34.407 1.00 29.36 ? 25 HIS B O 1 ATOM 2754 C CB . HIS B 2 25 ? -21.850 3.358 -32.219 1.00 28.79 ? 25 HIS B CB 1 ATOM 2755 C CG . HIS B 2 25 ? -21.561 2.061 -32.910 1.00 29.79 ? 25 HIS B CG 1 ATOM 2756 N ND1 . HIS B 2 25 ? -22.023 1.770 -34.176 1.00 30.04 ? 25 HIS B ND1 1 ATOM 2757 C CD2 . HIS B 2 25 ? -20.841 0.983 -32.517 1.00 29.73 ? 25 HIS B CD2 1 ATOM 2758 C CE1 . HIS B 2 25 ? -21.609 0.566 -34.530 1.00 29.85 ? 25 HIS B CE1 1 ATOM 2759 N NE2 . HIS B 2 25 ? -20.885 0.069 -33.545 1.00 29.98 ? 25 HIS B NE2 1 ATOM 2760 N N . HIS B 2 26 ? -19.854 4.569 -34.732 1.00 29.67 ? 26 HIS B N 1 ATOM 2761 C CA . HIS B 2 26 ? -19.813 4.922 -36.154 1.00 30.01 ? 26 HIS B CA 1 ATOM 2762 C C . HIS B 2 26 ? -19.839 3.668 -37.044 1.00 30.42 ? 26 HIS B C 1 ATOM 2763 O O . HIS B 2 26 ? -19.426 2.580 -36.627 1.00 29.79 ? 26 HIS B O 1 ATOM 2764 C CB . HIS B 2 26 ? -18.534 5.694 -36.452 1.00 30.60 ? 26 HIS B CB 1 ATOM 2765 C CG . HIS B 2 26 ? -17.332 4.810 -36.552 1.00 29.95 ? 26 HIS B CG 1 ATOM 2766 N ND1 . HIS B 2 26 ? -16.655 4.353 -35.444 1.00 30.58 ? 26 HIS B ND1 1 ATOM 2767 C CD2 . HIS B 2 26 ? -16.723 4.249 -37.625 1.00 29.26 ? 26 HIS B CD2 1 ATOM 2768 C CE1 . HIS B 2 26 ? -15.660 3.573 -35.829 1.00 30.49 ? 26 HIS B CE1 1 ATOM 2769 N NE2 . HIS B 2 26 ? -15.687 3.486 -37.147 1.00 29.37 ? 26 HIS B NE2 1 ATOM 2770 N N . SER B 2 27 ? -20.280 3.833 -38.285 1.00 30.78 ? 27 SER B N 1 ATOM 2771 C CA . SER B 2 27 ? -20.317 2.724 -39.214 1.00 31.30 ? 27 SER B CA 1 ATOM 2772 C C . SER B 2 27 ? -20.014 3.229 -40.614 1.00 30.81 ? 27 SER B C 1 ATOM 2773 O O . SER B 2 27 ? -20.701 4.113 -41.134 1.00 30.41 ? 27 SER B O 1 ATOM 2774 C CB . SER B 2 27 ? -21.680 2.029 -39.162 1.00 31.57 ? 27 SER B CB 1 ATOM 2775 O OG . SER B 2 27 ? -21.650 0.821 -39.891 1.00 34.30 ? 27 SER B OG 1 ATOM 2776 N N . ASN B 2 28 ? -18.964 2.682 -41.215 1.00 31.00 ? 28 ASN B N 1 ATOM 2777 C CA . ASN B 2 28 ? -18.590 3.080 -42.569 1.00 30.82 ? 28 ASN B CA 1 ATOM 2778 C C . ASN B 2 28 ? -18.005 1.913 -43.380 1.00 31.35 ? 28 ASN B C 1 ATOM 2779 O O . ASN B 2 28 ? -18.143 0.751 -42.985 1.00 31.07 ? 28 ASN B O 1 ATOM 2780 C CB . ASN B 2 28 ? -17.684 4.334 -42.546 1.00 30.61 ? 28 ASN B CB 1 ATOM 2781 C CG . ASN B 2 28 ? -16.351 4.104 -41.852 1.00 29.97 ? 28 ASN B CG 1 ATOM 2782 O OD1 . ASN B 2 28 ? -15.894 2.971 -41.710 1.00 32.55 ? 28 ASN B OD1 1 ATOM 2783 N ND2 . ASN B 2 28 ? -15.706 5.190 -41.440 1.00 29.22 ? 28 ASN B ND2 1 ATOM 2784 N N . ASP B 2 29 ? -17.381 2.218 -44.520 1.00 32.14 ? 29 ASP B N 1 ATOM 2785 C CA . ASP B 2 29 ? -16.775 1.182 -45.353 1.00 33.17 ? 29 ASP B CA 1 ATOM 2786 C C . ASP B 2 29 ? -15.586 0.519 -44.659 1.00 33.52 ? 29 ASP B C 1 ATOM 2787 O O . ASP B 2 29 ? -15.331 -0.670 -44.860 1.00 34.27 ? 29 ASP B O 1 ATOM 2788 C CB . ASP B 2 29 ? -16.349 1.751 -46.711 1.00 32.88 ? 29 ASP B CB 1 ATOM 2789 C CG . ASP B 2 29 ? -17.487 1.766 -47.737 1.00 34.37 ? 29 ASP B CG 1 ATOM 2790 O OD1 . ASP B 2 29 ? -18.624 1.346 -47.426 1.00 34.31 ? 29 ASP B OD1 1 ATOM 2791 O OD2 . ASP B 2 29 ? -17.232 2.188 -48.883 1.00 35.49 ? 29 ASP B OD2 1 ATOM 2792 N N . GLN B 2 30 ? -14.878 1.291 -43.836 1.00 34.00 ? 30 GLN B N 1 ATOM 2793 C CA . GLN B 2 30 ? -13.677 0.824 -43.144 1.00 34.23 ? 30 GLN B CA 1 ATOM 2794 C C . GLN B 2 30 ? -14.001 -0.029 -41.917 1.00 34.22 ? 30 GLN B C 1 ATOM 2795 O O . GLN B 2 30 ? -13.138 -0.755 -41.422 1.00 34.30 ? 30 GLN B O 1 ATOM 2796 C CB . GLN B 2 30 ? -12.810 2.012 -42.713 1.00 34.63 ? 30 GLN B CB 1 ATOM 2797 C CG . GLN B 2 30 ? -12.336 2.900 -43.846 1.00 35.14 ? 30 GLN B CG 1 ATOM 2798 C CD . GLN B 2 30 ? -11.777 4.217 -43.344 1.00 37.14 ? 30 GLN B CD 1 ATOM 2799 O OE1 . GLN B 2 30 ? -12.476 5.225 -43.329 1.00 36.99 ? 30 GLN B OE1 1 ATOM 2800 N NE2 . GLN B 2 30 ? -10.516 4.209 -42.915 1.00 37.63 ? 30 GLN B NE2 1 ATOM 2801 N N . GLY B 2 31 ? -15.236 0.077 -41.424 1.00 33.82 ? 31 GLY B N 1 ATOM 2802 C CA . GLY B 2 31 ? -15.673 -0.701 -40.273 1.00 33.47 ? 31 GLY B CA 1 ATOM 2803 C C . GLY B 2 31 ? -16.564 0.071 -39.316 1.00 33.12 ? 31 GLY B C 1 ATOM 2804 O O . GLY B 2 31 ? -17.183 1.072 -39.686 1.00 33.14 ? 31 GLY B O 1 ATOM 2805 N N . SER B 2 32 ? -16.617 -0.406 -38.078 1.00 33.14 ? 32 SER B N 1 ATOM 2806 C CA . SER B 2 32 ? -17.519 0.130 -37.071 1.00 32.80 ? 32 SER B CA 1 ATOM 2807 C C . SER B 2 32 ? -16.919 0.002 -35.664 1.00 32.83 ? 32 SER B C 1 ATOM 2808 O O . SER B 2 32 ? -15.991 -0.778 -35.459 1.00 32.62 ? 32 SER B O 1 ATOM 2809 C CB . SER B 2 32 ? -18.884 -0.575 -37.164 1.00 33.09 ? 32 SER B CB 1 ATOM 2810 O OG . SER B 2 32 ? -18.855 -1.882 -36.552 1.00 32.35 ? 32 SER B OG 1 ATOM 2811 N N . GLY B 2 33 ? -17.439 0.770 -34.702 1.00 32.53 ? 33 GLY B N 1 ATOM 2812 C CA . GLY B 2 33 ? -16.968 0.676 -33.309 1.00 32.43 ? 33 GLY B CA 1 ATOM 2813 C C . GLY B 2 33 ? -17.456 1.768 -32.369 1.00 32.52 ? 33 GLY B C 1 ATOM 2814 O O . GLY B 2 33 ? -18.085 2.730 -32.803 1.00 32.44 ? 33 GLY B O 1 ATOM 2815 N N . TYR B 2 34 ? -17.152 1.610 -31.079 1.00 32.59 ? 34 TYR B N 1 ATOM 2816 C CA . TYR B 2 34 ? -17.565 2.559 -30.038 1.00 32.76 ? 34 TYR B CA 1 ATOM 2817 C C . TYR B 2 34 ? -16.421 3.465 -29.583 1.00 33.29 ? 34 TYR B C 1 ATOM 2818 O O . TYR B 2 34 ? -15.247 3.077 -29.630 1.00 33.25 ? 34 TYR B O 1 ATOM 2819 C CB . TYR B 2 34 ? -18.114 1.812 -28.820 1.00 32.40 ? 34 TYR B CB 1 ATOM 2820 C CG . TYR B 2 34 ? -19.295 0.910 -29.110 1.00 32.37 ? 34 TYR B CG 1 ATOM 2821 C CD1 . TYR B 2 34 ? -20.605 1.392 -29.013 1.00 30.64 ? 34 TYR B CD1 1 ATOM 2822 C CD2 . TYR B 2 34 ? -19.104 -0.432 -29.464 1.00 31.45 ? 34 TYR B CD2 1 ATOM 2823 C CE1 . TYR B 2 34 ? -21.697 0.561 -29.267 1.00 30.64 ? 34 TYR B CE1 1 ATOM 2824 C CE2 . TYR B 2 34 ? -20.188 -1.270 -29.719 1.00 31.05 ? 34 TYR B CE2 1 ATOM 2825 C CZ . TYR B 2 34 ? -21.481 -0.764 -29.619 1.00 31.16 ? 34 TYR B CZ 1 ATOM 2826 O OH . TYR B 2 34 ? -22.559 -1.586 -29.867 1.00 31.23 ? 34 TYR B OH 1 ATOM 2827 N N . ALA B 2 35 ? -16.778 4.670 -29.147 1.00 33.68 ? 35 ALA B N 1 ATOM 2828 C CA . ALA B 2 35 ? -15.831 5.636 -28.597 1.00 34.42 ? 35 ALA B CA 1 ATOM 2829 C C . ALA B 2 35 ? -16.575 6.579 -27.661 1.00 34.85 ? 35 ALA B C 1 ATOM 2830 O O . ALA B 2 35 ? -17.587 7.166 -28.050 1.00 34.98 ? 35 ALA B O 1 ATOM 2831 C CB . ALA B 2 35 ? -15.164 6.422 -29.715 1.00 34.43 ? 35 ALA B CB 1 ATOM 2832 N N . ALA B 2 36 ? -16.087 6.723 -26.430 1.00 35.64 ? 36 ALA B N 1 ATOM 2833 C CA . ALA B 2 36 ? -16.682 7.673 -25.485 1.00 36.36 ? 36 ALA B CA 1 ATOM 2834 C C . ALA B 2 36 ? -16.348 9.097 -25.894 1.00 36.88 ? 36 ALA B C 1 ATOM 2835 O O . ALA B 2 36 ? -15.275 9.352 -26.456 1.00 36.92 ? 36 ALA B O 1 ATOM 2836 C CB . ALA B 2 36 ? -16.206 7.412 -24.078 1.00 36.63 ? 36 ALA B CB 1 ATOM 2837 N N . ASP B 2 37 ? -17.279 10.012 -25.632 1.00 37.10 ? 37 ASP B N 1 ATOM 2838 C CA . ASP B 2 37 ? -17.022 11.439 -25.759 1.00 37.60 ? 37 ASP B CA 1 ATOM 2839 C C . ASP B 2 37 ? -16.409 11.883 -24.431 1.00 38.11 ? 37 ASP B C 1 ATOM 2840 O O . ASP B 2 37 ? -17.087 11.905 -23.403 1.00 38.15 ? 37 ASP B O 1 ATOM 2841 C CB . ASP B 2 37 ? -18.318 12.201 -26.070 1.00 37.20 ? 37 ASP B CB 1 ATOM 2842 C CG . ASP B 2 37 ? -18.096 13.693 -26.258 1.00 37.00 ? 37 ASP B CG 1 ATOM 2843 O OD1 . ASP B 2 37 ? -17.553 14.101 -27.308 1.00 35.95 ? 37 ASP B OD1 1 ATOM 2844 O OD2 . ASP B 2 37 ? -18.472 14.464 -25.356 1.00 37.83 ? 37 ASP B OD2 1 ATOM 2845 N N . LYS B 2 38 ? -15.113 12.200 -24.457 1.00 38.79 ? 38 LYS B N 1 ATOM 2846 C CA . LYS B 2 38 ? -14.349 12.485 -23.235 1.00 39.57 ? 38 LYS B CA 1 ATOM 2847 C C . LYS B 2 38 ? -14.736 13.810 -22.574 1.00 39.47 ? 38 LYS B C 1 ATOM 2848 O O . LYS B 2 38 ? -14.824 13.894 -21.349 1.00 39.80 ? 38 LYS B O 1 ATOM 2849 C CB . LYS B 2 38 ? -12.836 12.443 -23.515 1.00 39.97 ? 38 LYS B CB 1 ATOM 2850 C CG . LYS B 2 38 ? -12.268 11.052 -23.856 1.00 40.47 ? 38 LYS B CG 1 ATOM 2851 C CD . LYS B 2 38 ? -12.021 10.210 -22.599 1.00 41.95 ? 38 LYS B CD 1 ATOM 2852 C CE . LYS B 2 38 ? -11.499 8.812 -22.939 1.00 41.12 ? 38 LYS B CE 1 ATOM 2853 N NZ . LYS B 2 38 ? -10.056 8.812 -23.342 1.00 42.76 ? 38 LYS B NZ 1 ATOM 2854 N N . GLU B 2 39 ? -14.976 14.834 -23.387 1.00 39.51 ? 39 GLU B N 1 ATOM 2855 C CA . GLU B 2 39 ? -15.322 16.170 -22.890 1.00 39.65 ? 39 GLU B CA 1 ATOM 2856 C C . GLU B 2 39 ? -16.600 16.196 -22.049 1.00 39.00 ? 39 GLU B C 1 ATOM 2857 O O . GLU B 2 39 ? -16.589 16.699 -20.917 1.00 39.20 ? 39 GLU B O 1 ATOM 2858 C CB . GLU B 2 39 ? -15.439 17.175 -24.045 1.00 40.21 ? 39 GLU B CB 1 ATOM 2859 C CG . GLU B 2 39 ? -14.171 17.353 -24.886 1.00 42.14 ? 39 GLU B CG 1 ATOM 2860 C CD . GLU B 2 39 ? -14.007 16.303 -25.998 1.00 44.68 ? 39 GLU B CD 1 ATOM 2861 O OE1 . GLU B 2 39 ? -15.014 15.691 -26.435 1.00 45.73 ? 39 GLU B OE1 1 ATOM 2862 O OE2 . GLU B 2 39 ? -12.856 16.104 -26.447 1.00 45.31 ? 39 GLU B OE2 1 ATOM 2863 N N . SER B 2 40 ? -17.693 15.662 -22.598 1.00 37.75 ? 40 SER B N 1 ATOM 2864 C CA . SER B 2 40 ? -18.986 15.662 -21.906 1.00 37.13 ? 40 SER B CA 1 ATOM 2865 C C . SER B 2 40 ? -19.003 14.707 -20.718 1.00 36.39 ? 40 SER B C 1 ATOM 2866 O O . SER B 2 40 ? -19.672 14.965 -19.718 1.00 36.17 ? 40 SER B O 1 ATOM 2867 C CB . SER B 2 40 ? -20.132 15.311 -22.856 1.00 36.99 ? 40 SER B CB 1 ATOM 2868 O OG . SER B 2 40 ? -19.942 14.038 -23.460 1.00 37.18 ? 40 SER B OG 1 ATOM 2869 N N . THR B 2 41 ? -18.282 13.597 -20.847 1.00 36.20 ? 41 THR B N 1 ATOM 2870 C CA . THR B 2 41 ? -18.135 12.634 -19.754 1.00 36.02 ? 41 THR B CA 1 ATOM 2871 C C . THR B 2 41 ? -17.444 13.291 -18.557 1.00 36.14 ? 41 THR B C 1 ATOM 2872 O O . THR B 2 41 ? -17.929 13.182 -17.430 1.00 36.06 ? 41 THR B O 1 ATOM 2873 C CB . THR B 2 41 ? -17.377 11.362 -20.200 1.00 35.91 ? 41 THR B CB 1 ATOM 2874 O OG1 . THR B 2 41 ? -18.117 10.698 -21.229 1.00 36.17 ? 41 THR B OG1 1 ATOM 2875 C CG2 . THR B 2 41 ? -17.186 10.386 -19.039 1.00 35.98 ? 41 THR B CG2 1 ATOM 2876 N N . GLN B 2 42 ? -16.331 13.982 -18.817 1.00 36.51 ? 42 GLN B N 1 ATOM 2877 C CA . GLN B 2 42 ? -15.560 14.657 -17.763 1.00 36.97 ? 42 GLN B CA 1 ATOM 2878 C C . GLN B 2 42 ? -16.350 15.761 -17.065 1.00 36.82 ? 42 GLN B C 1 ATOM 2879 O O . GLN B 2 42 ? -16.307 15.870 -15.844 1.00 36.35 ? 42 GLN B O 1 ATOM 2880 C CB . GLN B 2 42 ? -14.238 15.212 -18.306 1.00 37.37 ? 42 GLN B CB 1 ATOM 2881 C CG . GLN B 2 42 ? -13.328 15.817 -17.235 1.00 38.72 ? 42 GLN B CG 1 ATOM 2882 C CD . GLN B 2 42 ? -12.738 14.772 -16.292 1.00 40.58 ? 42 GLN B CD 1 ATOM 2883 O OE1 . GLN B 2 42 ? -12.003 13.881 -16.723 1.00 41.82 ? 42 GLN B OE1 1 ATOM 2884 N NE2 . GLN B 2 42 ? -13.053 14.884 -14.998 1.00 39.99 ? 42 GLN B NE2 1 ATOM 2885 N N . LYS B 2 43 ? -17.071 16.567 -17.844 1.00 37.08 ? 43 LYS B N 1 ATOM 2886 C CA . LYS B 2 43 ? -17.921 17.633 -17.301 1.00 37.41 ? 43 LYS B CA 1 ATOM 2887 C C . LYS B 2 43 ? -19.024 17.097 -16.382 1.00 37.32 ? 43 LYS B C 1 ATOM 2888 O O . LYS B 2 43 ? -19.315 17.700 -15.344 1.00 37.37 ? 43 LYS B O 1 ATOM 2889 C CB . LYS B 2 43 ? -18.475 18.530 -18.434 1.00 37.87 ? 43 LYS B CB 1 ATOM 2890 C CG . LYS B 2 43 ? -19.720 19.349 -18.074 1.00 39.50 ? 43 LYS B CG 1 ATOM 2891 C CD . LYS B 2 43 ? -20.939 18.875 -18.881 1.00 42.32 ? 43 LYS B CD 1 ATOM 2892 C CE . LYS B 2 43 ? -22.147 18.494 -18.002 1.00 42.04 ? 43 LYS B CE 1 ATOM 2893 N NZ . LYS B 2 43 ? -22.811 19.668 -17.364 1.00 45.93 ? 43 LYS B NZ 1 ATOM 2894 N N . ALA B 2 44 ? -19.616 15.959 -16.747 1.00 36.77 ? 44 ALA B N 1 ATOM 2895 C CA . ALA B 2 44 ? -20.636 15.318 -15.914 1.00 36.35 ? 44 ALA B CA 1 ATOM 2896 C C . ALA B 2 44 ? -20.009 14.706 -14.664 1.00 36.35 ? 44 ALA B C 1 ATOM 2897 O O . ALA B 2 44 ? -20.576 14.788 -13.575 1.00 35.88 ? 44 ALA B O 1 ATOM 2898 C CB . ALA B 2 44 ? -21.384 14.253 -16.704 1.00 36.39 ? 44 ALA B CB 1 ATOM 2899 N N . PHE B 2 45 ? -18.846 14.087 -14.835 1.00 36.40 ? 45 PHE B N 1 ATOM 2900 C CA . PHE B 2 45 ? -18.100 13.514 -13.716 1.00 37.09 ? 45 PHE B CA 1 ATOM 2901 C C . PHE B 2 45 ? -17.781 14.572 -12.657 1.00 36.94 ? 45 PHE B C 1 ATOM 2902 O O . PHE B 2 45 ? -17.898 14.317 -11.446 1.00 37.08 ? 45 PHE B O 1 ATOM 2903 C CB . PHE B 2 45 ? -16.810 12.852 -14.222 1.00 37.31 ? 45 PHE B CB 1 ATOM 2904 C CG . PHE B 2 45 ? -16.071 12.083 -13.159 1.00 38.48 ? 45 PHE B CG 1 ATOM 2905 C CD1 . PHE B 2 45 ? -16.532 10.838 -12.735 1.00 38.79 ? 45 PHE B CD1 1 ATOM 2906 C CD2 . PHE B 2 45 ? -14.922 12.609 -12.575 1.00 39.18 ? 45 PHE B CD2 1 ATOM 2907 C CE1 . PHE B 2 45 ? -15.858 10.125 -11.745 1.00 39.70 ? 45 PHE B CE1 1 ATOM 2908 C CE2 . PHE B 2 45 ? -14.238 11.900 -11.585 1.00 39.20 ? 45 PHE B CE2 1 ATOM 2909 C CZ . PHE B 2 45 ? -14.713 10.659 -11.170 1.00 39.24 ? 45 PHE B CZ 1 ATOM 2910 N N . ASP B 2 46 ? -17.382 15.755 -13.122 1.00 36.96 ? 46 ASP B N 1 ATOM 2911 C CA . ASP B 2 46 ? -17.028 16.872 -12.239 1.00 37.11 ? 46 ASP B CA 1 ATOM 2912 C C . ASP B 2 46 ? -18.229 17.375 -11.444 1.00 36.67 ? 46 ASP B C 1 ATOM 2913 O O . ASP B 2 46 ? -18.131 17.607 -10.224 1.00 37.10 ? 46 ASP B O 1 ATOM 2914 C CB . ASP B 2 46 ? -16.385 18.006 -13.046 1.00 37.39 ? 46 ASP B CB 1 ATOM 2915 C CG . ASP B 2 46 ? -15.011 17.640 -13.571 1.00 38.71 ? 46 ASP B CG 1 ATOM 2916 O OD1 . ASP B 2 46 ? -14.462 16.591 -13.159 1.00 40.87 ? 46 ASP B OD1 1 ATOM 2917 O OD2 . ASP B 2 46 ? -14.472 18.406 -14.393 1.00 39.89 ? 46 ASP B OD2 1 ATOM 2918 N N . GLY B 2 47 ? -19.355 17.531 -12.134 1.00 35.90 ? 47 GLY B N 1 ATOM 2919 C CA . GLY B 2 47 ? -20.627 17.876 -11.505 1.00 35.16 ? 47 GLY B CA 1 ATOM 2920 C C . GLY B 2 47 ? -21.098 16.842 -10.494 1.00 35.03 ? 47 GLY B C 1 ATOM 2921 O O . GLY B 2 47 ? -21.498 17.187 -9.373 1.00 34.44 ? 47 GLY B O 1 ATOM 2922 N N . ILE B 2 48 ? -21.040 15.568 -10.876 1.00 34.66 ? 48 ILE B N 1 ATOM 2923 C CA . ILE B 2 48 ? -21.500 14.494 -9.989 1.00 34.80 ? 48 ILE B CA 1 ATOM 2924 C C . ILE B 2 48 ? -20.621 14.417 -8.735 1.00 35.33 ? 48 ILE B C 1 ATOM 2925 O O . ILE B 2 48 ? -21.135 14.250 -7.620 1.00 35.32 ? 48 ILE B O 1 ATOM 2926 C CB . ILE B 2 48 ? -21.563 13.115 -10.717 1.00 34.89 ? 48 ILE B CB 1 ATOM 2927 C CG1 . ILE B 2 48 ? -22.644 13.122 -11.816 1.00 33.96 ? 48 ILE B CG1 1 ATOM 2928 C CG2 . ILE B 2 48 ? -21.807 11.977 -9.726 1.00 34.33 ? 48 ILE B CG2 1 ATOM 2929 C CD1 . ILE B 2 48 ? -24.078 13.299 -11.302 1.00 34.16 ? 48 ILE B CD1 1 ATOM 2930 N N . THR B 2 49 ? -19.307 14.549 -8.922 1.00 35.69 ? 49 THR B N 1 ATOM 2931 C CA . THR B 2 49 ? -18.374 14.569 -7.786 1.00 36.26 ? 49 THR B CA 1 ATOM 2932 C C . THR B 2 49 ? -18.668 15.746 -6.853 1.00 36.70 ? 49 THR B C 1 ATOM 2933 O O . THR B 2 49 ? -18.637 15.595 -5.633 1.00 36.78 ? 49 THR B O 1 ATOM 2934 C CB . THR B 2 49 ? -16.918 14.587 -8.240 1.00 36.17 ? 49 THR B CB 1 ATOM 2935 O OG1 . THR B 2 49 ? -16.665 13.432 -9.047 1.00 36.95 ? 49 THR B OG1 1 ATOM 2936 C CG2 . THR B 2 49 ? -15.952 14.591 -7.035 1.00 35.77 ? 49 THR B CG2 1 ATOM 2937 N N . ASN B 2 50 ? -18.969 16.907 -7.435 1.00 37.12 ? 50 ASN B N 1 ATOM 2938 C CA . ASN B 2 50 ? -19.414 18.067 -6.661 1.00 37.55 ? 50 ASN B CA 1 ATOM 2939 C C . ASN B 2 50 ? -20.728 17.818 -5.902 1.00 37.31 ? 50 ASN B C 1 ATOM 2940 O O . ASN B 2 50 ? -20.854 18.172 -4.715 1.00 37.18 ? 50 ASN B O 1 ATOM 2941 C CB . ASN B 2 50 ? -19.526 19.306 -7.561 1.00 37.79 ? 50 ASN B CB 1 ATOM 2942 C CG . ASN B 2 50 ? -19.680 20.586 -6.764 1.00 40.13 ? 50 ASN B CG 1 ATOM 2943 O OD1 . ASN B 2 50 ? -20.784 21.118 -6.632 1.00 44.50 ? 50 ASN B OD1 1 ATOM 2944 N ND2 . ASN B 2 50 ? -18.580 21.069 -6.194 1.00 41.09 ? 50 ASN B ND2 1 ATOM 2945 N N . LYS B 2 51 ? -21.693 17.182 -6.569 1.00 36.69 ? 51 LYS B N 1 ATOM 2946 C CA . LYS B 2 51 ? -22.989 16.868 -5.956 1.00 36.77 ? 51 LYS B CA 1 ATOM 2947 C C . LYS B 2 51 ? -22.866 16.038 -4.669 1.00 37.04 ? 51 LYS B C 1 ATOM 2948 O O . LYS B 2 51 ? -23.447 16.383 -3.627 1.00 37.12 ? 51 LYS B O 1 ATOM 2949 C CB . LYS B 2 51 ? -23.915 16.150 -6.957 1.00 36.52 ? 51 LYS B CB 1 ATOM 2950 C CG . LYS B 2 51 ? -25.227 15.684 -6.329 1.00 36.44 ? 51 LYS B CG 1 ATOM 2951 C CD . LYS B 2 51 ? -26.178 15.047 -7.315 1.00 36.49 ? 51 LYS B CD 1 ATOM 2952 C CE . LYS B 2 51 ? -26.602 16.040 -8.370 1.00 34.30 ? 51 LYS B CE 1 ATOM 2953 N NZ . LYS B 2 51 ? -27.982 15.776 -8.819 1.00 31.31 ? 51 LYS B NZ 1 ATOM 2954 N N . VAL B 2 52 ? -22.115 14.942 -4.751 1.00 37.32 ? 52 VAL B N 1 ATOM 2955 C CA . VAL B 2 52 ? -22.003 14.018 -3.629 1.00 37.97 ? 52 VAL B CA 1 ATOM 2956 C C . VAL B 2 52 ? -21.341 14.706 -2.436 1.00 38.26 ? 52 VAL B C 1 ATOM 2957 O O . VAL B 2 52 ? -21.822 14.579 -1.311 1.00 38.80 ? 52 VAL B O 1 ATOM 2958 C CB . VAL B 2 52 ? -21.294 12.683 -3.988 1.00 38.02 ? 52 VAL B CB 1 ATOM 2959 C CG1 . VAL B 2 52 ? -22.161 11.850 -4.922 1.00 37.83 ? 52 VAL B CG1 1 ATOM 2960 C CG2 . VAL B 2 52 ? -19.915 12.911 -4.598 1.00 38.65 ? 52 VAL B CG2 1 ATOM 2961 N N . ASN B 2 53 ? -20.277 15.465 -2.702 1.00 38.67 ? 53 ASN B N 1 ATOM 2962 C CA . ASN B 2 53 ? -19.623 16.262 -1.668 1.00 39.22 ? 53 ASN B CA 1 ATOM 2963 C C . ASN B 2 53 ? -20.587 17.245 -1.024 1.00 39.89 ? 53 ASN B C 1 ATOM 2964 O O . ASN B 2 53 ? -20.662 17.331 0.202 1.00 39.70 ? 53 ASN B O 1 ATOM 2965 C CB . ASN B 2 53 ? -18.393 16.976 -2.218 1.00 39.28 ? 53 ASN B CB 1 ATOM 2966 C CG . ASN B 2 53 ? -17.270 16.011 -2.556 1.00 40.25 ? 53 ASN B CG 1 ATOM 2967 O OD1 . ASN B 2 53 ? -17.283 14.856 -2.126 1.00 42.06 ? 53 ASN B OD1 1 ATOM 2968 N ND2 . ASN B 2 53 ? -16.292 16.479 -3.321 1.00 39.14 ? 53 ASN B ND2 1 ATOM 2969 N N . SER B 2 54 ? -21.352 17.957 -1.845 1.00 40.08 ? 54 SER B N 1 ATOM 2970 C CA . SER B 2 54 ? -22.359 18.881 -1.324 1.00 40.91 ? 54 SER B CA 1 ATOM 2971 C C . SER B 2 54 ? -23.374 18.222 -0.380 1.00 41.92 ? 54 SER B C 1 ATOM 2972 O O . SER B 2 54 ? -23.657 18.750 0.702 1.00 41.91 ? 54 SER B O 1 ATOM 2973 C CB . SER B 2 54 ? -23.074 19.607 -2.469 1.00 40.50 ? 54 SER B CB 1 ATOM 2974 O OG . SER B 2 54 ? -22.173 20.497 -3.107 1.00 39.69 ? 54 SER B OG 1 ATOM 2975 N N . VAL B 2 55 ? -23.917 17.074 -0.784 1.00 42.90 ? 55 VAL B N 1 ATOM 2976 C CA . VAL B 2 55 ? -24.967 16.422 -0.007 1.00 44.23 ? 55 VAL B CA 1 ATOM 2977 C C . VAL B 2 55 ? -24.406 15.963 1.346 1.00 45.16 ? 55 VAL B C 1 ATOM 2978 O O . VAL B 2 55 ? -25.020 16.184 2.390 1.00 44.96 ? 55 VAL B O 1 ATOM 2979 C CB . VAL B 2 55 ? -25.707 15.271 -0.786 1.00 44.55 ? 55 VAL B CB 1 ATOM 2980 C CG1 . VAL B 2 55 ? -26.431 15.827 -2.017 1.00 44.27 ? 55 VAL B CG1 1 ATOM 2981 C CG2 . VAL B 2 55 ? -24.760 14.164 -1.198 1.00 44.42 ? 55 VAL B CG2 1 ATOM 2982 N N . ILE B 2 56 ? -23.216 15.373 1.313 1.00 45.97 ? 56 ILE B N 1 ATOM 2983 C CA . ILE B 2 56 ? -22.503 14.994 2.528 1.00 47.34 ? 56 ILE B CA 1 ATOM 2984 C C . ILE B 2 56 ? -22.196 16.206 3.419 1.00 48.50 ? 56 ILE B C 1 ATOM 2985 O O . ILE B 2 56 ? -22.550 16.212 4.606 1.00 48.64 ? 56 ILE B O 1 ATOM 2986 C CB . ILE B 2 56 ? -21.203 14.218 2.188 1.00 47.14 ? 56 ILE B CB 1 ATOM 2987 C CG1 . ILE B 2 56 ? -21.554 12.840 1.618 1.00 47.08 ? 56 ILE B CG1 1 ATOM 2988 C CG2 . ILE B 2 56 ? -20.276 14.099 3.413 1.00 46.69 ? 56 ILE B CG2 1 ATOM 2989 C CD1 . ILE B 2 56 ? -20.402 12.147 0.901 1.00 46.82 ? 56 ILE B CD1 1 ATOM 2990 N N . GLU B 2 57 ? -21.556 17.223 2.842 1.00 49.89 ? 57 GLU B N 1 ATOM 2991 C CA . GLU B 2 57 ? -21.051 18.378 3.601 1.00 51.53 ? 57 GLU B CA 1 ATOM 2992 C C . GLU B 2 57 ? -22.140 19.202 4.298 1.00 52.68 ? 57 GLU B C 1 ATOM 2993 O O . GLU B 2 57 ? -21.917 19.741 5.388 1.00 52.66 ? 57 GLU B O 1 ATOM 2994 C CB . GLU B 2 57 ? -20.188 19.277 2.710 1.00 51.51 ? 57 GLU B CB 1 ATOM 2995 C CG . GLU B 2 57 ? -18.847 18.654 2.320 1.00 51.79 ? 57 GLU B CG 1 ATOM 2996 C CD . GLU B 2 57 ? -18.149 19.373 1.168 1.00 51.89 ? 57 GLU B CD 1 ATOM 2997 O OE1 . GLU B 2 57 ? -18.755 20.270 0.537 1.00 52.31 ? 57 GLU B OE1 1 ATOM 2998 O OE2 . GLU B 2 57 ? -16.979 19.031 0.892 1.00 52.47 ? 57 GLU B OE2 1 ATOM 2999 N N . LYS B 2 58 ? -23.315 19.283 3.680 1.00 54.06 ? 58 LYS B N 1 ATOM 3000 C CA . LYS B 2 58 ? -24.425 20.041 4.253 1.00 55.59 ? 58 LYS B CA 1 ATOM 3001 C C . LYS B 2 58 ? -25.051 19.333 5.453 1.00 56.60 ? 58 LYS B C 1 ATOM 3002 O O . LYS B 2 58 ? -25.722 19.965 6.275 1.00 56.41 ? 58 LYS B O 1 ATOM 3003 C CB . LYS B 2 58 ? -25.477 20.373 3.184 1.00 55.74 ? 58 LYS B CB 1 ATOM 3004 C CG . LYS B 2 58 ? -25.241 21.705 2.442 1.00 56.22 ? 58 LYS B CG 1 ATOM 3005 C CD . LYS B 2 58 ? -24.283 21.582 1.243 1.00 57.70 ? 58 LYS B CD 1 ATOM 3006 C CE . LYS B 2 58 ? -22.811 21.833 1.610 1.00 57.89 ? 58 LYS B CE 1 ATOM 3007 N NZ . LYS B 2 58 ? -21.897 21.806 0.429 1.00 57.03 ? 58 LYS B NZ 1 ATOM 3008 N N . MET B 2 59 ? -24.813 18.026 5.556 1.00 57.91 ? 59 MET B N 1 ATOM 3009 C CA . MET B 2 59 ? -25.304 17.227 6.683 1.00 59.44 ? 59 MET B CA 1 ATOM 3010 C C . MET B 2 59 ? -24.177 16.783 7.613 1.00 59.66 ? 59 MET B C 1 ATOM 3011 O O . MET B 2 59 ? -24.237 15.708 8.214 1.00 60.12 ? 59 MET B O 1 ATOM 3012 C CB . MET B 2 59 ? -26.129 16.037 6.190 1.00 59.39 ? 59 MET B CB 1 ATOM 3013 C CG . MET B 2 59 ? -27.270 16.460 5.290 1.00 60.11 ? 59 MET B CG 1 ATOM 3014 S SD . MET B 2 59 ? -28.343 15.133 4.742 1.00 60.95 ? 59 MET B SD 1 ATOM 3015 C CE . MET B 2 59 ? -27.312 14.292 3.530 1.00 61.95 ? 59 MET B CE 1 ATOM 3016 N N . ASN B 2 60 ? -23.153 17.627 7.719 1.00 60.21 ? 60 ASN B N 1 ATOM 3017 C CA . ASN B 2 60 ? -22.099 17.476 8.722 1.00 60.57 ? 60 ASN B CA 1 ATOM 3018 C C . ASN B 2 60 ? -22.406 18.346 9.945 1.00 60.66 ? 60 ASN B C 1 ATOM 3019 O O . ASN B 2 60 ? -21.783 18.204 11.008 1.00 60.62 ? 60 ASN B O 1 ATOM 3020 C CB . ASN B 2 60 ? -20.730 17.828 8.126 1.00 60.73 ? 60 ASN B CB 1 ATOM 3021 C CG . ASN B 2 60 ? -20.221 16.775 7.136 1.00 61.14 ? 60 ASN B CG 1 ATOM 3022 O OD1 . ASN B 2 60 ? -20.819 15.706 6.966 1.00 61.49 ? 60 ASN B OD1 1 ATOM 3023 N ND2 . ASN B 2 60 ? -19.101 17.078 6.485 1.00 61.77 ? 60 ASN B ND2 1 ATOM 3024 N N . THR B 2 61 ? -23.383 19.240 9.776 1.00 60.66 ? 61 THR B N 1 ATOM 3025 C CA . THR B 2 61 ? -23.906 20.083 10.854 1.00 60.44 ? 61 THR B CA 1 ATOM 3026 C C . THR B 2 61 ? -25.109 19.384 11.502 1.00 59.92 ? 61 THR B C 1 ATOM 3027 O O . THR B 2 61 ? -26.200 19.955 11.591 1.00 59.91 ? 61 THR B O 1 ATOM 3028 C CB . THR B 2 61 ? -24.338 21.479 10.326 1.00 60.68 ? 61 THR B CB 1 ATOM 3029 O OG1 . THR B 2 61 ? -25.481 21.341 9.468 1.00 61.00 ? 61 THR B OG1 1 ATOM 3030 C CG2 . THR B 2 61 ? -23.197 22.158 9.558 1.00 60.81 ? 61 THR B CG2 1 ATOM 3031 N N . GLN B 2 62 ? -24.893 18.152 11.961 1.00 59.08 ? 62 GLN B N 1 ATOM 3032 C CA . GLN B 2 62 ? -25.974 17.270 12.400 1.00 58.26 ? 62 GLN B CA 1 ATOM 3033 C C . GLN B 2 62 ? -25.959 17.028 13.918 1.00 57.08 ? 62 GLN B C 1 ATOM 3034 O O . GLN B 2 62 ? -24.894 16.996 14.545 1.00 57.26 ? 62 GLN B O 1 ATOM 3035 C CB . GLN B 2 62 ? -25.901 15.954 11.609 1.00 58.35 ? 62 GLN B CB 1 ATOM 3036 C CG . GLN B 2 62 ? -26.944 14.900 11.965 1.00 59.02 ? 62 GLN B CG 1 ATOM 3037 C CD . GLN B 2 62 ? -27.170 13.889 10.853 1.00 59.00 ? 62 GLN B CD 1 ATOM 3038 O OE1 . GLN B 2 62 ? -26.967 14.183 9.671 1.00 61.07 ? 62 GLN B OE1 1 ATOM 3039 N NE2 . GLN B 2 62 ? -27.599 12.689 11.228 1.00 59.95 ? 62 GLN B NE2 1 ATOM 3040 N N . PHE B 2 63 ? -27.153 16.873 14.493 1.00 55.61 ? 63 PHE B N 1 ATOM 3041 C CA . PHE B 2 63 ? -27.345 16.656 15.929 1.00 54.00 ? 63 PHE B CA 1 ATOM 3042 C C . PHE B 2 63 ? -26.706 15.350 16.413 1.00 53.07 ? 63 PHE B C 1 ATOM 3043 O O . PHE B 2 63 ? -26.700 14.345 15.696 1.00 53.03 ? 63 PHE B O 1 ATOM 3044 C CB . PHE B 2 63 ? -28.845 16.670 16.253 1.00 54.06 ? 63 PHE B CB 1 ATOM 3045 C CG . PHE B 2 63 ? -29.172 16.447 17.711 1.00 54.09 ? 63 PHE B CG 1 ATOM 3046 C CD1 . PHE B 2 63 ? -29.160 17.512 18.618 1.00 54.16 ? 63 PHE B CD1 1 ATOM 3047 C CD2 . PHE B 2 63 ? -29.517 15.172 18.175 1.00 53.86 ? 63 PHE B CD2 1 ATOM 3048 C CE1 . PHE B 2 63 ? -29.470 17.303 19.965 1.00 53.55 ? 63 PHE B CE1 1 ATOM 3049 C CE2 . PHE B 2 63 ? -29.830 14.958 19.517 1.00 53.18 ? 63 PHE B CE2 1 ATOM 3050 C CZ . PHE B 2 63 ? -29.806 16.027 20.413 1.00 52.90 ? 63 PHE B CZ 1 ATOM 3051 N N . GLU B 2 64 ? -26.163 15.381 17.627 1.00 51.51 ? 64 GLU B N 1 ATOM 3052 C CA . GLU B 2 64 ? -25.611 14.189 18.263 1.00 50.12 ? 64 GLU B CA 1 ATOM 3053 C C . GLU B 2 64 ? -26.290 13.983 19.607 1.00 48.69 ? 64 GLU B C 1 ATOM 3054 O O . GLU B 2 64 ? -26.434 14.927 20.384 1.00 48.50 ? 64 GLU B O 1 ATOM 3055 C CB . GLU B 2 64 ? -24.108 14.338 18.482 1.00 50.47 ? 64 GLU B CB 1 ATOM 3056 C CG . GLU B 2 64 ? -23.296 14.562 17.216 1.00 51.82 ? 64 GLU B CG 1 ATOM 3057 C CD . GLU B 2 64 ? -21.981 15.274 17.491 1.00 53.47 ? 64 GLU B CD 1 ATOM 3058 O OE1 . GLU B 2 64 ? -21.629 15.458 18.679 1.00 53.36 ? 64 GLU B OE1 1 ATOM 3059 O OE2 . GLU B 2 64 ? -21.300 15.655 16.515 1.00 54.33 ? 64 GLU B OE2 1 ATOM 3060 N N . ALA B 2 65 ? -26.710 12.753 19.876 1.00 46.70 ? 65 ALA B N 1 ATOM 3061 C CA . ALA B 2 65 ? -27.283 12.415 21.171 1.00 45.02 ? 65 ALA B CA 1 ATOM 3062 C C . ALA B 2 65 ? -26.173 12.273 22.221 1.00 43.85 ? 65 ALA B C 1 ATOM 3063 O O . ALA B 2 65 ? -25.140 11.645 21.958 1.00 43.79 ? 65 ALA B O 1 ATOM 3064 C CB . ALA B 2 65 ? -28.108 11.138 21.070 1.00 44.98 ? 65 ALA B CB 1 ATOM 3065 N N . VAL B 2 66 ? -26.390 12.876 23.393 1.00 42.03 ? 66 VAL B N 1 ATOM 3066 C CA . VAL B 2 66 ? -25.463 12.792 24.537 1.00 40.13 ? 66 VAL B CA 1 ATOM 3067 C C . VAL B 2 66 ? -26.132 11.988 25.655 1.00 38.25 ? 66 VAL B C 1 ATOM 3068 O O . VAL B 2 66 ? -27.280 12.281 26.027 1.00 38.96 ? 66 VAL B O 1 ATOM 3069 C CB . VAL B 2 66 ? -25.030 14.220 25.042 1.00 40.34 ? 66 VAL B CB 1 ATOM 3070 C CG1 . VAL B 2 66 ? -24.679 14.242 26.551 1.00 40.63 ? 66 VAL B CG1 1 ATOM 3071 C CG2 . VAL B 2 66 ? -23.879 14.758 24.207 1.00 40.79 ? 66 VAL B CG2 1 ATOM 3072 N N . GLY B 2 67 ? -25.436 10.978 26.176 1.00 35.40 ? 67 GLY B N 1 ATOM 3073 C CA . GLY B 2 67 ? -25.976 10.137 27.252 1.00 31.86 ? 67 GLY B CA 1 ATOM 3074 C C . GLY B 2 67 ? -26.096 10.808 28.623 1.00 29.93 ? 67 GLY B C 1 ATOM 3075 O O . GLY B 2 67 ? -25.090 11.154 29.242 1.00 30.26 ? 67 GLY B O 1 ATOM 3076 N N . LYS B 2 68 ? -27.335 10.964 29.093 1.00 26.76 ? 68 LYS B N 1 ATOM 3077 C CA . LYS B 2 68 ? -27.684 11.589 30.383 1.00 24.36 ? 68 LYS B CA 1 ATOM 3078 C C . LYS B 2 68 ? -28.639 10.656 31.102 1.00 22.38 ? 68 LYS B C 1 ATOM 3079 O O . LYS B 2 68 ? -29.374 9.923 30.451 1.00 22.88 ? 68 LYS B O 1 ATOM 3080 C CB . LYS B 2 68 ? -28.450 12.902 30.155 1.00 24.95 ? 68 LYS B CB 1 ATOM 3081 C CG . LYS B 2 68 ? -27.609 14.068 29.711 1.00 28.57 ? 68 LYS B CG 1 ATOM 3082 C CD . LYS B 2 68 ? -28.486 15.307 29.703 1.00 30.75 ? 68 LYS B CD 1 ATOM 3083 C CE . LYS B 2 68 ? -27.784 16.429 29.027 1.00 31.62 ? 68 LYS B CE 1 ATOM 3084 N NZ . LYS B 2 68 ? -27.475 16.096 27.607 1.00 32.88 ? 68 LYS B NZ 1 ATOM 3085 N N . GLU B 2 69 ? -28.681 10.734 32.422 1.00 19.38 ? 69 GLU B N 1 ATOM 3086 C CA . GLU B 2 69 ? -29.573 9.921 33.242 1.00 18.98 ? 69 GLU B CA 1 ATOM 3087 C C . GLU B 2 69 ? -30.442 10.796 34.105 1.00 18.74 ? 69 GLU B C 1 ATOM 3088 O O . GLU B 2 69 ? -30.069 11.919 34.408 1.00 15.67 ? 69 GLU B O 1 ATOM 3089 C CB . GLU B 2 69 ? -28.765 8.928 34.084 1.00 21.28 ? 69 GLU B CB 1 ATOM 3090 C CG . GLU B 2 69 ? -27.973 8.028 33.112 1.00 23.41 ? 69 GLU B CG 1 ATOM 3091 C CD . GLU B 2 69 ? -27.110 7.012 33.798 1.00 26.03 ? 69 GLU B CD 1 ATOM 3092 O OE1 . GLU B 2 69 ? -27.661 6.191 34.536 1.00 31.00 ? 69 GLU B OE1 1 ATOM 3093 O OE2 . GLU B 2 69 ? -25.886 7.017 33.528 1.00 32.31 ? 69 GLU B OE2 1 ATOM 3094 N N . PHE B 2 70 ? -31.604 10.265 34.503 1.00 17.66 ? 70 PHE B N 1 ATOM 3095 C CA . PHE B 2 70 ? -32.607 11.006 35.266 1.00 18.05 ? 70 PHE B CA 1 ATOM 3096 C C . PHE B 2 70 ? -33.206 10.143 36.358 1.00 18.26 ? 70 PHE B C 1 ATOM 3097 O O . PHE B 2 70 ? -33.308 8.906 36.163 1.00 20.24 ? 70 PHE B O 1 ATOM 3098 C CB . PHE B 2 70 ? -33.724 11.401 34.276 1.00 18.01 ? 70 PHE B CB 1 ATOM 3099 C CG . PHE B 2 70 ? -33.227 12.215 33.136 1.00 18.04 ? 70 PHE B CG 1 ATOM 3100 C CD1 . PHE B 2 70 ? -33.062 13.599 33.298 1.00 17.81 ? 70 PHE B CD1 1 ATOM 3101 C CD2 . PHE B 2 70 ? -32.843 11.616 31.943 1.00 17.14 ? 70 PHE B CD2 1 ATOM 3102 C CE1 . PHE B 2 70 ? -32.563 14.356 32.230 1.00 16.91 ? 70 PHE B CE1 1 ATOM 3103 C CE2 . PHE B 2 70 ? -32.341 12.351 30.899 1.00 18.81 ? 70 PHE B CE2 1 ATOM 3104 C CZ . PHE B 2 70 ? -32.210 13.734 31.035 1.00 20.52 ? 70 PHE B CZ 1 ATOM 3105 N N . SER B 2 71 ? -33.599 10.760 37.477 1.00 17.57 ? 71 SER B N 1 ATOM 3106 C CA . SER B 2 71 ? -34.162 10.041 38.631 1.00 19.02 ? 71 SER B CA 1 ATOM 3107 C C . SER B 2 71 ? -35.609 9.654 38.346 1.00 19.51 ? 71 SER B C 1 ATOM 3108 O O . SER B 2 71 ? -36.192 10.070 37.347 1.00 18.20 ? 71 SER B O 1 ATOM 3109 C CB . SER B 2 71 ? -34.114 10.873 39.914 1.00 18.37 ? 71 SER B CB 1 ATOM 3110 O OG . SER B 2 71 ? -35.185 11.795 39.890 1.00 20.95 ? 71 SER B OG 1 ATOM 3111 N N . ASN B 2 72 ? -36.167 8.826 39.225 1.00 21.31 ? 72 ASN B N 1 ATOM 3112 C CA . ASN B 2 72 ? -37.580 8.466 39.105 1.00 22.96 ? 72 ASN B CA 1 ATOM 3113 C C . ASN B 2 72 ? -38.501 9.628 39.434 1.00 22.94 ? 72 ASN B C 1 ATOM 3114 O O . ASN B 2 72 ? -39.724 9.524 39.247 1.00 23.07 ? 72 ASN B O 1 ATOM 3115 C CB . ASN B 2 72 ? -37.905 7.233 39.976 1.00 24.37 ? 72 ASN B CB 1 ATOM 3116 C CG . ASN B 2 72 ? -37.608 7.453 41.436 1.00 29.21 ? 72 ASN B CG 1 ATOM 3117 O OD1 . ASN B 2 72 ? -36.711 8.226 41.807 1.00 34.15 ? 72 ASN B OD1 1 ATOM 3118 N ND2 . ASN B 2 72 ? -38.349 6.751 42.300 1.00 34.73 ? 72 ASN B ND2 1 ATOM 3119 N N . LEU B 2 73 ? -37.932 10.732 39.938 1.00 20.91 ? 73 LEU B N 1 ATOM 3120 C CA . LEU B 2 73 ? -38.711 11.960 40.144 1.00 21.82 ? 73 LEU B CA 1 ATOM 3121 C C . LEU B 2 73 ? -38.434 13.046 39.089 1.00 19.21 ? 73 LEU B C 1 ATOM 3122 O O . LEU B 2 73 ? -38.788 14.218 39.292 1.00 19.51 ? 73 LEU B O 1 ATOM 3123 C CB . LEU B 2 73 ? -38.453 12.514 41.535 1.00 23.02 ? 73 LEU B CB 1 ATOM 3124 C CG . LEU B 2 73 ? -39.242 11.947 42.747 1.00 26.63 ? 73 LEU B CG 1 ATOM 3125 C CD1 . LEU B 2 73 ? -38.863 10.503 43.124 1.00 30.82 ? 73 LEU B CD1 1 ATOM 3126 C CD2 . LEU B 2 73 ? -39.089 12.856 43.942 1.00 25.57 ? 73 LEU B CD2 1 ATOM 3127 N N . GLU B 2 74 ? -37.782 12.652 38.006 1.00 16.21 ? 74 GLU B N 1 ATOM 3128 C CA . GLU B 2 74 ? -37.488 13.553 36.891 1.00 15.86 ? 74 GLU B CA 1 ATOM 3129 C C . GLU B 2 74 ? -38.018 12.976 35.610 1.00 15.40 ? 74 GLU B C 1 ATOM 3130 O O . GLU B 2 74 ? -37.392 13.059 34.555 1.00 14.28 ? 74 GLU B O 1 ATOM 3131 C CB . GLU B 2 74 ? -35.967 13.764 36.795 1.00 15.87 ? 74 GLU B CB 1 ATOM 3132 C CG . GLU B 2 74 ? -35.397 14.438 37.997 1.00 16.97 ? 74 GLU B CG 1 ATOM 3133 C CD . GLU B 2 74 ? -33.888 14.576 37.891 1.00 20.67 ? 74 GLU B CD 1 ATOM 3134 O OE1 . GLU B 2 74 ? -33.215 13.577 37.535 1.00 18.49 ? 74 GLU B OE1 1 ATOM 3135 O OE2 . GLU B 2 74 ? -33.394 15.672 38.198 1.00 21.90 ? 74 GLU B OE2 1 ATOM 3136 N N . ARG B 2 75 ? -39.217 12.371 35.676 1.00 14.58 ? 75 ARG B N 1 ATOM 3137 C CA . ARG B 2 75 ? -39.755 11.793 34.457 1.00 15.21 ? 75 ARG B CA 1 ATOM 3138 C C . ARG B 2 75 ? -40.118 12.821 33.385 1.00 13.64 ? 75 ARG B C 1 ATOM 3139 O O . ARG B 2 75 ? -39.993 12.541 32.226 1.00 14.11 ? 75 ARG B O 1 ATOM 3140 C CB . ARG B 2 75 ? -40.975 10.935 34.821 1.00 16.69 ? 75 ARG B CB 1 ATOM 3141 C CG . ARG B 2 75 ? -40.626 9.865 35.835 1.00 18.56 ? 75 ARG B CG 1 ATOM 3142 C CD . ARG B 2 75 ? -39.687 8.854 35.231 1.00 29.42 ? 75 ARG B CD 1 ATOM 3143 N NE . ARG B 2 75 ? -39.496 7.714 36.121 1.00 35.21 ? 75 ARG B NE 1 ATOM 3144 C CZ . ARG B 2 75 ? -38.705 6.683 35.838 1.00 38.88 ? 75 ARG B CZ 1 ATOM 3145 N NH1 . ARG B 2 75 ? -38.037 6.661 34.690 1.00 42.22 ? 75 ARG B NH1 1 ATOM 3146 N NH2 . ARG B 2 75 ? -38.573 5.684 36.706 1.00 39.80 ? 75 ARG B NH2 1 ATOM 3147 N N . ARG B 2 76 ? -40.583 14.010 33.770 1.00 13.36 ? 76 ARG B N 1 ATOM 3148 C CA . ARG B 2 76 ? -40.901 14.963 32.692 1.00 12.67 ? 76 ARG B CA 1 ATOM 3149 C C . ARG B 2 76 ? -39.610 15.379 32.014 1.00 12.69 ? 76 ARG B C 1 ATOM 3150 O O . ARG B 2 76 ? -39.566 15.494 30.809 1.00 14.09 ? 76 ARG B O 1 ATOM 3151 C CB . ARG B 2 76 ? -41.545 16.231 33.267 1.00 12.32 ? 76 ARG B CB 1 ATOM 3152 C CG . ARG B 2 76 ? -42.957 16.011 33.859 1.00 11.82 ? 76 ARG B CG 1 ATOM 3153 C CD . ARG B 2 76 ? -43.441 17.206 34.653 1.00 10.11 ? 76 ARG B CD 1 ATOM 3154 N NE . ARG B 2 76 ? -42.572 17.357 35.814 1.00 9.28 ? 76 ARG B NE 1 ATOM 3155 C CZ . ARG B 2 76 ? -42.277 18.491 36.422 1.00 11.44 ? 76 ARG B CZ 1 ATOM 3156 N NH1 . ARG B 2 76 ? -42.831 19.630 35.997 1.00 13.11 ? 76 ARG B NH1 1 ATOM 3157 N NH2 . ARG B 2 76 ? -41.438 18.482 37.451 1.00 11.64 ? 76 ARG B NH2 1 ATOM 3158 N N . LEU B 2 77 ? -38.596 15.654 32.830 1.00 13.66 ? 77 LEU B N 1 ATOM 3159 C CA . LEU B 2 77 ? -37.308 16.073 32.251 1.00 14.62 ? 77 LEU B CA 1 ATOM 3160 C C . LEU B 2 77 ? -36.739 14.969 31.340 1.00 14.76 ? 77 LEU B C 1 ATOM 3161 O O . LEU B 2 77 ? -36.262 15.222 30.256 1.00 14.56 ? 77 LEU B O 1 ATOM 3162 C CB . LEU B 2 77 ? -36.355 16.483 33.375 1.00 14.68 ? 77 LEU B CB 1 ATOM 3163 C CG . LEU B 2 77 ? -34.961 16.943 32.907 1.00 17.18 ? 77 LEU B CG 1 ATOM 3164 C CD1 . LEU B 2 77 ? -35.047 18.197 32.066 1.00 18.31 ? 77 LEU B CD1 1 ATOM 3165 C CD2 . LEU B 2 77 ? -34.092 17.167 34.119 1.00 17.45 ? 77 LEU B CD2 1 ATOM 3166 N N . GLU B 2 78 ? -36.818 13.728 31.790 1.00 15.49 ? 78 GLU B N 1 ATOM 3167 C CA . GLU B 2 78 ? -36.373 12.588 30.987 1.00 16.63 ? 78 GLU B CA 1 ATOM 3168 C C . GLU B 2 78 ? -37.119 12.518 29.673 1.00 16.84 ? 78 GLU B C 1 ATOM 3169 O O . GLU B 2 78 ? -36.536 12.328 28.606 1.00 16.69 ? 78 GLU B O 1 ATOM 3170 C CB . GLU B 2 78 ? -36.536 11.304 31.783 1.00 18.50 ? 78 GLU B CB 1 ATOM 3171 C CG . GLU B 2 78 ? -36.007 10.054 31.068 1.00 22.80 ? 78 GLU B CG 1 ATOM 3172 C CD . GLU B 2 78 ? -36.271 8.840 31.907 1.00 29.98 ? 78 GLU B CD 1 ATOM 3173 O OE1 . GLU B 2 78 ? -37.406 8.717 32.432 1.00 34.09 ? 78 GLU B OE1 1 ATOM 3174 O OE2 . GLU B 2 78 ? -35.350 8.022 32.092 1.00 35.91 ? 78 GLU B OE2 1 ATOM 3175 N N . ASN B 2 79 ? -38.433 12.724 29.729 1.00 16.45 ? 79 ASN B N 1 ATOM 3176 C CA . ASN B 2 79 ? -39.240 12.693 28.519 1.00 17.29 ? 79 ASN B CA 1 ATOM 3177 C C . ASN B 2 79 ? -38.916 13.840 27.549 1.00 17.73 ? 79 ASN B C 1 ATOM 3178 O O . ASN B 2 79 ? -38.872 13.662 26.343 1.00 17.59 ? 79 ASN B O 1 ATOM 3179 C CB . ASN B 2 79 ? -40.723 12.657 28.888 1.00 16.87 ? 79 ASN B CB 1 ATOM 3180 C CG . ASN B 2 79 ? -41.608 12.395 27.677 1.00 22.15 ? 79 ASN B CG 1 ATOM 3181 O OD1 . ASN B 2 79 ? -42.274 13.307 27.159 1.00 24.78 ? 79 ASN B OD1 1 ATOM 3182 N ND2 . ASN B 2 79 ? -41.550 11.168 27.169 1.00 25.90 ? 79 ASN B ND2 1 ATOM 3183 N N . LEU B 2 80 ? -38.646 15.011 28.111 1.00 17.54 ? 80 LEU B N 1 ATOM 3184 C CA . LEU B 2 80 ? -38.239 16.153 27.327 1.00 17.30 ? 80 LEU B CA 1 ATOM 3185 C C . LEU B 2 80 ? -36.934 15.855 26.604 1.00 17.22 ? 80 LEU B C 1 ATOM 3186 O O . LEU B 2 80 ? -36.810 16.118 25.407 1.00 17.39 ? 80 LEU B O 1 ATOM 3187 C CB . LEU B 2 80 ? -38.050 17.347 28.251 1.00 17.94 ? 80 LEU B CB 1 ATOM 3188 C CG . LEU B 2 80 ? -37.922 18.670 27.518 1.00 22.92 ? 80 LEU B CG 1 ATOM 3189 C CD1 . LEU B 2 80 ? -38.206 19.778 28.497 1.00 26.00 ? 80 LEU B CD1 1 ATOM 3190 C CD2 . LEU B 2 80 ? -36.555 18.786 26.919 1.00 28.01 ? 80 LEU B CD2 1 ATOM 3191 N N . ASN B 2 81 ? -35.985 15.286 27.326 1.00 18.03 ? 81 ASN B N 1 ATOM 3192 C CA . ASN B 2 81 ? -34.711 14.916 26.735 1.00 21.16 ? 81 ASN B CA 1 ATOM 3193 C C . ASN B 2 81 ? -34.876 13.916 25.606 1.00 21.56 ? 81 ASN B C 1 ATOM 3194 O O . ASN B 2 81 ? -34.268 14.076 24.526 1.00 22.80 ? 81 ASN B O 1 ATOM 3195 C CB . ASN B 2 81 ? -33.776 14.379 27.816 1.00 20.92 ? 81 ASN B CB 1 ATOM 3196 C CG . ASN B 2 81 ? -32.343 14.270 27.326 1.00 24.27 ? 81 ASN B CG 1 ATOM 3197 O OD1 . ASN B 2 81 ? -31.802 13.173 27.216 1.00 26.76 ? 81 ASN B OD1 1 ATOM 3198 N ND2 . ASN B 2 81 ? -31.726 15.417 27.045 1.00 25.91 ? 81 ASN B ND2 1 ATOM 3199 N N . LYS B 2 82 ? -35.680 12.884 25.861 1.00 22.08 ? 82 LYS B N 1 ATOM 3200 C CA . LYS B 2 82 ? -35.962 11.854 24.870 1.00 24.17 ? 82 LYS B CA 1 ATOM 3201 C C . LYS B 2 82 ? -36.691 12.424 23.645 1.00 23.98 ? 82 LYS B C 1 ATOM 3202 O O . LYS B 2 82 ? -36.336 12.114 22.492 1.00 24.11 ? 82 LYS B O 1 ATOM 3203 C CB . LYS B 2 82 ? -36.811 10.757 25.499 1.00 24.77 ? 82 LYS B CB 1 ATOM 3204 C CG . LYS B 2 82 ? -37.146 9.608 24.532 1.00 28.64 ? 82 LYS B CG 1 ATOM 3205 C CD . LYS B 2 82 ? -38.507 9.020 24.883 1.00 33.52 ? 82 LYS B CD 1 ATOM 3206 C CE . LYS B 2 82 ? -38.608 7.573 24.472 1.00 36.35 ? 82 LYS B CE 1 ATOM 3207 N NZ . LYS B 2 82 ? -39.855 7.316 23.699 1.00 39.25 ? 82 LYS B NZ 1 ATOM 3208 N N . LYS B 2 83 ? -37.708 13.243 23.871 1.00 24.14 ? 83 LYS B N 1 ATOM 3209 C CA . LYS B 2 83 ? -38.431 13.878 22.745 1.00 25.07 ? 83 LYS B CA 1 ATOM 3210 C C . LYS B 2 83 ? -37.520 14.758 21.906 1.00 25.03 ? 83 LYS B C 1 ATOM 3211 O O . LYS B 2 83 ? -37.651 14.844 20.672 1.00 23.98 ? 83 LYS B O 1 ATOM 3212 C CB . LYS B 2 83 ? -39.631 14.679 23.254 1.00 25.27 ? 83 LYS B CB 1 ATOM 3213 C CG . LYS B 2 83 ? -40.839 13.792 23.595 1.00 28.48 ? 83 LYS B CG 1 ATOM 3214 C CD . LYS B 2 83 ? -41.808 13.690 22.420 1.00 35.15 ? 83 LYS B CD 1 ATOM 3215 C CE . LYS B 2 83 ? -43.077 14.500 22.647 1.00 37.41 ? 83 LYS B CE 1 ATOM 3216 N NZ . LYS B 2 83 ? -42.880 15.970 22.863 1.00 40.70 ? 83 LYS B NZ 1 ATOM 3217 N N . MET B 2 84 ? -36.578 15.412 22.571 1.00 24.81 ? 84 MET B N 1 ATOM 3218 C CA . MET B 2 84 ? -35.652 16.273 21.871 1.00 27.60 ? 84 MET B CA 1 ATOM 3219 C C . MET B 2 84 ? -34.697 15.469 21.007 1.00 27.39 ? 84 MET B C 1 ATOM 3220 O O . MET B 2 84 ? -34.514 15.769 19.825 1.00 26.82 ? 84 MET B O 1 ATOM 3221 C CB . MET B 2 84 ? -34.844 17.099 22.871 1.00 25.87 ? 84 MET B CB 1 ATOM 3222 C CG . MET B 2 84 ? -34.093 18.182 22.171 1.00 28.71 ? 84 MET B CG 1 ATOM 3223 S SD . MET B 2 84 ? -32.852 18.935 23.187 1.00 33.80 ? 84 MET B SD 1 ATOM 3224 C CE . MET B 2 84 ? -31.817 17.565 23.659 1.00 32.47 ? 84 MET B CE 1 ATOM 3225 N N . GLU B 2 85 ? -34.075 14.453 21.596 1.00 28.68 ? 85 GLU B N 1 ATOM 3226 C CA . GLU B 2 85 ? -33.062 13.678 20.871 1.00 30.96 ? 85 GLU B CA 1 ATOM 3227 C C . GLU B 2 85 ? -33.674 12.891 19.715 1.00 31.85 ? 85 GLU B C 1 ATOM 3228 O O . GLU B 2 85 ? -33.127 12.908 18.584 1.00 32.88 ? 85 GLU B O 1 ATOM 3229 C CB . GLU B 2 85 ? -32.223 12.822 21.838 1.00 31.77 ? 85 GLU B CB 1 ATOM 3230 C CG . GLU B 2 85 ? -31.328 13.692 22.712 1.00 33.05 ? 85 GLU B CG 1 ATOM 3231 C CD . GLU B 2 85 ? -30.263 12.924 23.461 1.00 36.89 ? 85 GLU B CD 1 ATOM 3232 O OE1 . GLU B 2 85 ? -30.520 11.746 23.822 1.00 38.68 ? 85 GLU B OE1 1 ATOM 3233 O OE2 . GLU B 2 85 ? -29.179 13.514 23.708 1.00 35.82 ? 85 GLU B OE2 1 ATOM 3234 N N . ASP B 2 86 ? -34.829 12.278 19.971 1.00 32.65 ? 86 ASP B N 1 ATOM 3235 C CA . ASP B 2 86 ? -35.630 11.621 18.941 1.00 33.69 ? 86 ASP B CA 1 ATOM 3236 C C . ASP B 2 86 ? -36.086 12.620 17.867 1.00 33.16 ? 86 ASP B C 1 ATOM 3237 O O . ASP B 2 86 ? -36.037 12.314 16.666 1.00 33.10 ? 86 ASP B O 1 ATOM 3238 C CB . ASP B 2 86 ? -36.890 10.992 19.544 1.00 34.85 ? 86 ASP B CB 1 ATOM 3239 C CG . ASP B 2 86 ? -36.612 9.755 20.401 1.00 37.18 ? 86 ASP B CG 1 ATOM 3240 O OD1 . ASP B 2 86 ? -35.435 9.398 20.647 1.00 39.41 ? 86 ASP B OD1 1 ATOM 3241 O OD2 . ASP B 2 86 ? -37.617 9.153 20.848 1.00 40.55 ? 86 ASP B OD2 1 ATOM 3242 N N . GLY B 2 87 ? -36.555 13.794 18.299 1.00 31.44 ? 87 GLY B N 1 ATOM 3243 C CA . GLY B 2 87 ? -37.031 14.840 17.378 1.00 31.84 ? 87 GLY B CA 1 ATOM 3244 C C . GLY B 2 87 ? -35.992 15.274 16.370 1.00 31.65 ? 87 GLY B C 1 ATOM 3245 O O . GLY B 2 87 ? -36.269 15.373 15.164 1.00 31.94 ? 87 GLY B O 1 ATOM 3246 N N . PHE B 2 88 ? -34.787 15.548 16.858 1.00 31.50 ? 88 PHE B N 1 ATOM 3247 C CA . PHE B 2 88 ? -33.682 15.902 15.963 1.00 31.28 ? 88 PHE B CA 1 ATOM 3248 C C . PHE B 2 88 ? -33.286 14.739 15.068 1.00 32.11 ? 88 PHE B C 1 ATOM 3249 O O . PHE B 2 88 ? -33.036 14.931 13.860 1.00 30.91 ? 88 PHE B O 1 ATOM 3250 C CB . PHE B 2 88 ? -32.481 16.433 16.743 1.00 31.41 ? 88 PHE B CB 1 ATOM 3251 C CG . PHE B 2 88 ? -32.659 17.847 17.225 1.00 31.17 ? 88 PHE B CG 1 ATOM 3252 C CD1 . PHE B 2 88 ? -32.863 18.883 16.312 1.00 30.51 ? 88 PHE B CD1 1 ATOM 3253 C CD2 . PHE B 2 88 ? -32.641 18.151 18.591 1.00 30.80 ? 88 PHE B CD2 1 ATOM 3254 C CE1 . PHE B 2 88 ? -33.040 20.201 16.734 1.00 30.43 ? 88 PHE B CE1 1 ATOM 3255 C CE2 . PHE B 2 88 ? -32.812 19.478 19.023 1.00 30.50 ? 88 PHE B CE2 1 ATOM 3256 C CZ . PHE B 2 88 ? -33.026 20.492 18.101 1.00 30.24 ? 88 PHE B CZ 1 ATOM 3257 N N . LEU B 2 89 ? -33.266 13.539 15.650 1.00 32.15 ? 89 LEU B N 1 ATOM 3258 C CA . LEU B 2 89 ? -32.996 12.312 14.896 1.00 33.42 ? 89 LEU B CA 1 ATOM 3259 C C . LEU B 2 89 ? -33.970 12.167 13.725 1.00 33.91 ? 89 LEU B C 1 ATOM 3260 O O . LEU B 2 89 ? -33.555 11.879 12.582 1.00 34.40 ? 89 LEU B O 1 ATOM 3261 C CB . LEU B 2 89 ? -33.074 11.084 15.808 1.00 33.90 ? 89 LEU B CB 1 ATOM 3262 C CG . LEU B 2 89 ? -32.834 9.721 15.156 1.00 34.84 ? 89 LEU B CG 1 ATOM 3263 C CD1 . LEU B 2 89 ? -31.570 9.755 14.281 1.00 34.84 ? 89 LEU B CD1 1 ATOM 3264 C CD2 . LEU B 2 89 ? -32.754 8.662 16.243 1.00 37.69 ? 89 LEU B CD2 1 ATOM 3265 N N . ASP B 2 90 ? -35.253 12.374 13.995 1.00 33.80 ? 90 ASP B N 1 ATOM 3266 C CA . ASP B 2 90 ? -36.243 12.334 12.917 1.00 34.63 ? 90 ASP B CA 1 ATOM 3267 C C . ASP B 2 90 ? -36.020 13.418 11.857 1.00 34.33 ? 90 ASP B C 1 ATOM 3268 O O . ASP B 2 90 ? -36.119 13.146 10.631 1.00 34.03 ? 90 ASP B O 1 ATOM 3269 C CB . ASP B 2 90 ? -37.650 12.406 13.489 1.00 34.68 ? 90 ASP B CB 1 ATOM 3270 C CG . ASP B 2 90 ? -38.030 11.149 14.235 1.00 38.09 ? 90 ASP B CG 1 ATOM 3271 O OD1 . ASP B 2 90 ? -37.489 10.067 13.898 1.00 42.32 ? 90 ASP B OD1 1 ATOM 3272 O OD2 . ASP B 2 90 ? -38.868 11.234 15.157 1.00 39.12 ? 90 ASP B OD2 1 ATOM 3273 N N . VAL B 2 91 ? -35.694 14.632 12.310 1.00 33.08 ? 91 VAL B N 1 ATOM 3274 C CA . VAL B 2 91 ? -35.424 15.753 11.384 1.00 33.06 ? 91 VAL B CA 1 ATOM 3275 C C . VAL B 2 91 ? -34.235 15.418 10.476 1.00 33.47 ? 91 VAL B C 1 ATOM 3276 O O . VAL B 2 91 ? -34.296 15.598 9.257 1.00 33.07 ? 91 VAL B O 1 ATOM 3277 C CB . VAL B 2 91 ? -35.215 17.104 12.136 1.00 32.98 ? 91 VAL B CB 1 ATOM 3278 C CG1 . VAL B 2 91 ? -34.591 18.171 11.226 1.00 30.78 ? 91 VAL B CG1 1 ATOM 3279 C CG2 . VAL B 2 91 ? -36.536 17.607 12.698 1.00 32.52 ? 91 VAL B CG2 1 ATOM 3280 N N . TRP B 2 92 ? -33.155 14.913 11.059 1.00 33.76 ? 92 TRP B N 1 ATOM 3281 C CA . TRP B 2 92 ? -31.965 14.623 10.258 1.00 34.54 ? 92 TRP B CA 1 ATOM 3282 C C . TRP B 2 92 ? -32.115 13.413 9.338 1.00 34.44 ? 92 TRP B C 1 ATOM 3283 O O . TRP B 2 92 ? -31.596 13.420 8.205 1.00 35.03 ? 92 TRP B O 1 ATOM 3284 C CB . TRP B 2 92 ? -30.718 14.527 11.126 1.00 34.74 ? 92 TRP B CB 1 ATOM 3285 C CG . TRP B 2 92 ? -30.341 15.863 11.670 1.00 35.02 ? 92 TRP B CG 1 ATOM 3286 C CD1 . TRP B 2 92 ? -30.403 16.259 12.977 1.00 35.17 ? 92 TRP B CD1 1 ATOM 3287 C CD2 . TRP B 2 92 ? -29.876 16.999 10.927 1.00 34.62 ? 92 TRP B CD2 1 ATOM 3288 N NE1 . TRP B 2 92 ? -30.002 17.565 13.092 1.00 34.79 ? 92 TRP B NE1 1 ATOM 3289 C CE2 . TRP B 2 92 ? -29.665 18.043 11.852 1.00 34.97 ? 92 TRP B CE2 1 ATOM 3290 C CE3 . TRP B 2 92 ? -29.616 17.237 9.566 1.00 35.11 ? 92 TRP B CE3 1 ATOM 3291 C CZ2 . TRP B 2 92 ? -29.209 19.314 11.464 1.00 34.79 ? 92 TRP B CZ2 1 ATOM 3292 C CZ3 . TRP B 2 92 ? -29.151 18.495 9.185 1.00 35.25 ? 92 TRP B CZ3 1 ATOM 3293 C CH2 . TRP B 2 92 ? -28.954 19.515 10.127 1.00 35.43 ? 92 TRP B CH2 1 ATOM 3294 N N . THR B 2 93 ? -32.848 12.401 9.792 1.00 34.14 ? 93 THR B N 1 ATOM 3295 C CA . THR B 2 93 ? -33.161 11.262 8.928 1.00 34.49 ? 93 THR B CA 1 ATOM 3296 C C . THR B 2 93 ? -33.951 11.796 7.724 1.00 35.11 ? 93 THR B C 1 ATOM 3297 O O . THR B 2 93 ? -33.584 11.521 6.565 1.00 34.88 ? 93 THR B O 1 ATOM 3298 C CB . THR B 2 93 ? -33.891 10.130 9.700 1.00 34.93 ? 93 THR B CB 1 ATOM 3299 O OG1 . THR B 2 93 ? -33.049 9.661 10.770 1.00 31.89 ? 93 THR B OG1 1 ATOM 3300 C CG2 . THR B 2 93 ? -34.208 8.953 8.778 1.00 34.43 ? 93 THR B CG2 1 ATOM 3301 N N . TYR B 2 94 ? -34.986 12.596 7.995 1.00 34.96 ? 94 TYR B N 1 ATOM 3302 C CA . TYR B 2 94 ? -35.788 13.244 6.944 1.00 36.09 ? 94 TYR B CA 1 ATOM 3303 C C . TYR B 2 94 ? -34.927 14.036 5.950 1.00 35.98 ? 94 TYR B C 1 ATOM 3304 O O . TYR B 2 94 ? -35.079 13.877 4.731 1.00 36.59 ? 94 TYR B O 1 ATOM 3305 C CB . TYR B 2 94 ? -36.869 14.151 7.548 1.00 36.10 ? 94 TYR B CB 1 ATOM 3306 C CG . TYR B 2 94 ? -37.617 14.986 6.516 1.00 36.81 ? 94 TYR B CG 1 ATOM 3307 C CD1 . TYR B 2 94 ? -38.789 14.525 5.949 1.00 37.13 ? 94 TYR B CD1 1 ATOM 3308 C CD2 . TYR B 2 94 ? -37.144 16.240 6.122 1.00 37.00 ? 94 TYR B CD2 1 ATOM 3309 C CE1 . TYR B 2 94 ? -39.481 15.286 4.996 1.00 36.52 ? 94 TYR B CE1 1 ATOM 3310 C CE2 . TYR B 2 94 ? -37.826 17.015 5.180 1.00 37.51 ? 94 TYR B CE2 1 ATOM 3311 C CZ . TYR B 2 94 ? -38.996 16.530 4.621 1.00 37.35 ? 94 TYR B CZ 1 ATOM 3312 O OH . TYR B 2 94 ? -39.677 17.298 3.681 1.00 38.90 ? 94 TYR B OH 1 ATOM 3313 N N . ASN B 2 95 ? -34.044 14.896 6.473 1.00 36.05 ? 95 ASN B N 1 ATOM 3314 C CA . ASN B 2 95 ? -33.144 15.700 5.637 1.00 35.98 ? 95 ASN B CA 1 ATOM 3315 C C . ASN B 2 95 ? -32.264 14.820 4.739 1.00 35.70 ? 95 ASN B C 1 ATOM 3316 O O . ASN B 2 95 ? -32.131 15.092 3.533 1.00 35.38 ? 95 ASN B O 1 ATOM 3317 C CB . ASN B 2 95 ? -32.266 16.626 6.496 1.00 36.02 ? 95 ASN B CB 1 ATOM 3318 C CG . ASN B 2 95 ? -33.042 17.811 7.091 1.00 36.71 ? 95 ASN B CG 1 ATOM 3319 O OD1 . ASN B 2 95 ? -34.219 18.030 6.786 1.00 37.85 ? 95 ASN B OD1 1 ATOM 3320 N ND2 . ASN B 2 95 ? -32.367 18.587 7.947 1.00 36.94 ? 95 ASN B ND2 1 ATOM 3321 N N . ALA B 2 96 ? -31.680 13.770 5.321 1.00 34.51 ? 96 ALA B N 1 ATOM 3322 C CA . ALA B 2 96 ? -30.819 12.853 4.569 1.00 34.71 ? 96 ALA B CA 1 ATOM 3323 C C . ALA B 2 96 ? -31.593 12.094 3.491 1.00 34.29 ? 96 ALA B C 1 ATOM 3324 O O . ALA B 2 96 ? -31.160 12.039 2.324 1.00 34.62 ? 96 ALA B O 1 ATOM 3325 C CB . ALA B 2 96 ? -30.098 11.886 5.490 1.00 33.97 ? 96 ALA B CB 1 ATOM 3326 N N . GLU B 2 97 ? -32.728 11.514 3.871 1.00 33.96 ? 97 GLU B N 1 ATOM 3327 C CA . GLU B 2 97 ? -33.499 10.690 2.933 1.00 34.09 ? 97 GLU B CA 1 ATOM 3328 C C . GLU B 2 97 ? -34.067 11.518 1.784 1.00 34.09 ? 97 GLU B C 1 ATOM 3329 O O . GLU B 2 97 ? -33.969 11.117 0.611 1.00 33.85 ? 97 GLU B O 1 ATOM 3330 C CB . GLU B 2 97 ? -34.569 9.884 3.658 1.00 33.84 ? 97 GLU B CB 1 ATOM 3331 C CG . GLU B 2 97 ? -33.951 8.830 4.579 1.00 33.09 ? 97 GLU B CG 1 ATOM 3332 C CD . GLU B 2 97 ? -34.962 7.942 5.255 1.00 35.30 ? 97 GLU B CD 1 ATOM 3333 O OE1 . GLU B 2 97 ? -36.175 8.221 5.154 1.00 36.69 ? 97 GLU B OE1 1 ATOM 3334 O OE2 . GLU B 2 97 ? -34.546 6.944 5.889 1.00 33.35 ? 97 GLU B OE2 1 ATOM 3335 N N . LEU B 2 98 ? -34.616 12.682 2.119 1.00 34.18 ? 98 LEU B N 1 ATOM 3336 C CA . LEU B 2 98 ? -35.178 13.599 1.123 1.00 34.77 ? 98 LEU B CA 1 ATOM 3337 C C . LEU B 2 98 ? -34.122 14.112 0.158 1.00 35.30 ? 98 LEU B C 1 ATOM 3338 O O . LEU B 2 98 ? -34.360 14.189 -1.069 1.00 34.59 ? 98 LEU B O 1 ATOM 3339 C CB . LEU B 2 98 ? -35.887 14.788 1.794 1.00 34.34 ? 98 LEU B CB 1 ATOM 3340 C CG . LEU B 2 98 ? -36.583 15.712 0.782 1.00 34.32 ? 98 LEU B CG 1 ATOM 3341 C CD1 . LEU B 2 98 ? -37.648 14.947 -0.028 1.00 33.51 ? 98 LEU B CD1 1 ATOM 3342 C CD2 . LEU B 2 98 ? -37.171 16.964 1.423 1.00 34.49 ? 98 LEU B CD2 1 ATOM 3343 N N . LEU B 2 99 ? -32.966 14.481 0.704 1.00 35.84 ? 99 LEU B N 1 ATOM 3344 C CA . LEU B 2 99 ? -31.893 15.047 -0.096 1.00 36.65 ? 99 LEU B CA 1 ATOM 3345 C C . LEU B 2 99 ? -31.409 14.031 -1.119 1.00 36.63 ? 99 LEU B C 1 ATOM 3346 O O . LEU B 2 99 ? -31.252 14.363 -2.300 1.00 36.31 ? 99 LEU B O 1 ATOM 3347 C CB . LEU B 2 99 ? -30.731 15.501 0.792 1.00 36.75 ? 99 LEU B CB 1 ATOM 3348 C CG . LEU B 2 99 ? -29.514 16.172 0.137 1.00 37.94 ? 99 LEU B CG 1 ATOM 3349 C CD1 . LEU B 2 99 ? -29.905 17.209 -0.913 1.00 38.72 ? 99 LEU B CD1 1 ATOM 3350 C CD2 . LEU B 2 99 ? -28.636 16.820 1.210 1.00 37.52 ? 99 LEU B CD2 1 ATOM 3351 N N . VAL B 2 100 ? -31.188 12.800 -0.658 1.00 36.26 ? 100 VAL B N 1 ATOM 3352 C CA . VAL B 2 100 ? -30.803 11.695 -1.539 1.00 35.95 ? 100 VAL B CA 1 ATOM 3353 C C . VAL B 2 100 ? -31.877 11.428 -2.609 1.00 35.45 ? 100 VAL B C 1 ATOM 3354 O O . VAL B 2 100 ? -31.535 11.260 -3.789 1.00 35.18 ? 100 VAL B O 1 ATOM 3355 C CB . VAL B 2 100 ? -30.475 10.418 -0.734 1.00 35.86 ? 100 VAL B CB 1 ATOM 3356 C CG1 . VAL B 2 100 ? -30.209 9.236 -1.660 1.00 35.22 ? 100 VAL B CG1 1 ATOM 3357 C CG2 . VAL B 2 100 ? -29.257 10.649 0.174 1.00 36.60 ? 100 VAL B CG2 1 ATOM 3358 N N . LEU B 2 101 ? -33.156 11.407 -2.227 1.00 34.78 ? 101 LEU B N 1 ATOM 3359 C CA . LEU B 2 101 ? -34.234 11.179 -3.223 1.00 34.71 ? 101 LEU B CA 1 ATOM 3360 C C . LEU B 2 101 ? -34.319 12.267 -4.287 1.00 34.95 ? 101 LEU B C 1 ATOM 3361 O O . LEU B 2 101 ? -34.375 11.969 -5.486 1.00 33.54 ? 101 LEU B O 1 ATOM 3362 C CB . LEU B 2 101 ? -35.610 11.029 -2.574 1.00 34.69 ? 101 LEU B CB 1 ATOM 3363 C CG . LEU B 2 101 ? -35.934 9.761 -1.795 1.00 35.97 ? 101 LEU B CG 1 ATOM 3364 C CD1 . LEU B 2 101 ? -37.385 9.771 -1.329 1.00 37.38 ? 101 LEU B CD1 1 ATOM 3365 C CD2 . LEU B 2 101 ? -35.644 8.534 -2.604 1.00 33.89 ? 101 LEU B CD2 1 ATOM 3366 N N . MET B 2 102 ? -34.346 13.521 -3.842 1.00 34.33 ? 102 MET B N 1 ATOM 3367 C CA . MET B 2 102 ? -34.455 14.672 -4.740 1.00 35.05 ? 102 MET B CA 1 ATOM 3368 C C . MET B 2 102 ? -33.253 14.768 -5.652 1.00 34.67 ? 102 MET B C 1 ATOM 3369 O O . MET B 2 102 ? -33.388 15.006 -6.873 1.00 34.87 ? 102 MET B O 1 ATOM 3370 C CB . MET B 2 102 ? -34.584 15.951 -3.918 1.00 35.33 ? 102 MET B CB 1 ATOM 3371 C CG . MET B 2 102 ? -35.952 16.138 -3.337 1.00 35.65 ? 102 MET B CG 1 ATOM 3372 S SD . MET B 2 102 ? -35.995 17.689 -2.442 1.00 36.29 ? 102 MET B SD 1 ATOM 3373 C CE . MET B 2 102 ? -37.751 17.989 -2.340 1.00 37.58 ? 102 MET B CE 1 ATOM 3374 N N . GLU B 2 103 ? -32.075 14.555 -5.075 1.00 34.25 ? 103 GLU B N 1 ATOM 3375 C CA . GLU B 2 103 ? -30.854 14.632 -5.860 1.00 33.93 ? 103 GLU B CA 1 ATOM 3376 C C . GLU B 2 103 ? -30.650 13.430 -6.784 1.00 32.94 ? 103 GLU B C 1 ATOM 3377 O O . GLU B 2 103 ? -30.121 13.602 -7.880 1.00 32.79 ? 103 GLU B O 1 ATOM 3378 C CB . GLU B 2 103 ? -29.639 14.884 -4.976 1.00 34.10 ? 103 GLU B CB 1 ATOM 3379 C CG . GLU B 2 103 ? -29.551 16.347 -4.476 1.00 36.20 ? 103 GLU B CG 1 ATOM 3380 C CD . GLU B 2 103 ? -29.710 17.378 -5.606 1.00 38.71 ? 103 GLU B CD 1 ATOM 3381 O OE1 . GLU B 2 103 ? -29.098 17.179 -6.680 1.00 40.35 ? 103 GLU B OE1 1 ATOM 3382 O OE2 . GLU B 2 103 ? -30.444 18.380 -5.433 1.00 39.23 ? 103 GLU B OE2 1 ATOM 3383 N N . ASN B 2 104 ? -31.076 12.234 -6.369 1.00 31.44 ? 104 ASN B N 1 ATOM 3384 C CA . ASN B 2 104 ? -31.106 11.085 -7.298 1.00 30.81 ? 104 ASN B CA 1 ATOM 3385 C C . ASN B 2 104 ? -31.955 11.393 -8.546 1.00 31.15 ? 104 ASN B C 1 ATOM 3386 O O . ASN B 2 104 ? -31.539 11.106 -9.688 1.00 30.18 ? 104 ASN B O 1 ATOM 3387 C CB . ASN B 2 104 ? -31.627 9.832 -6.608 1.00 30.78 ? 104 ASN B CB 1 ATOM 3388 C CG . ASN B 2 104 ? -30.579 9.181 -5.709 1.00 29.79 ? 104 ASN B CG 1 ATOM 3389 O OD1 . ASN B 2 104 ? -29.408 9.547 -5.760 1.00 29.27 ? 104 ASN B OD1 1 ATOM 3390 N ND2 . ASN B 2 104 ? -30.995 8.204 -4.910 1.00 27.77 ? 104 ASN B ND2 1 ATOM 3391 N N . GLU B 2 105 ? -33.146 11.958 -8.321 1.00 31.00 ? 105 GLU B N 1 ATOM 3392 C CA . GLU B 2 105 ? -34.017 12.421 -9.429 1.00 32.20 ? 105 GLU B CA 1 ATOM 3393 C C . GLU B 2 105 ? -33.266 13.333 -10.373 1.00 31.84 ? 105 GLU B C 1 ATOM 3394 O O . GLU B 2 105 ? -33.299 13.161 -11.607 1.00 32.32 ? 105 GLU B O 1 ATOM 3395 C CB . GLU B 2 105 ? -35.220 13.173 -8.851 1.00 32.12 ? 105 GLU B CB 1 ATOM 3396 C CG . GLU B 2 105 ? -36.332 13.520 -9.836 1.00 37.12 ? 105 GLU B CG 1 ATOM 3397 C CD . GLU B 2 105 ? -37.698 13.369 -9.185 1.00 41.89 ? 105 GLU B CD 1 ATOM 3398 O OE1 . GLU B 2 105 ? -38.055 12.211 -8.872 1.00 43.09 ? 105 GLU B OE1 1 ATOM 3399 O OE2 . GLU B 2 105 ? -38.401 14.392 -8.976 1.00 46.35 ? 105 GLU B OE2 1 ATOM 3400 N N . ARG B 2 106 ? -32.590 14.317 -9.800 1.00 31.51 ? 106 ARG B N 1 ATOM 3401 C CA . ARG B 2 106 ? -31.854 15.283 -10.599 1.00 32.01 ? 106 ARG B CA 1 ATOM 3402 C C . ARG B 2 106 ? -30.626 14.693 -11.311 1.00 32.01 ? 106 ARG B C 1 ATOM 3403 O O . ARG B 2 106 ? -30.283 15.117 -12.431 1.00 31.54 ? 106 ARG B O 1 ATOM 3404 C CB . ARG B 2 106 ? -31.531 16.527 -9.756 1.00 32.68 ? 106 ARG B CB 1 ATOM 3405 C CG . ARG B 2 106 ? -32.804 17.372 -9.544 1.00 36.35 ? 106 ARG B CG 1 ATOM 3406 C CD . ARG B 2 106 ? -32.542 18.779 -9.063 1.00 42.19 ? 106 ARG B CD 1 ATOM 3407 N NE . ARG B 2 106 ? -32.429 18.775 -7.611 1.00 46.90 ? 106 ARG B NE 1 ATOM 3408 C CZ . ARG B 2 106 ? -33.461 18.721 -6.765 1.00 49.82 ? 106 ARG B CZ 1 ATOM 3409 N NH1 . ARG B 2 106 ? -34.713 18.684 -7.216 1.00 49.37 ? 106 ARG B NH1 1 ATOM 3410 N NH2 . ARG B 2 106 ? -33.235 18.714 -5.454 1.00 49.12 ? 106 ARG B NH2 1 ATOM 3411 N N . THR B 2 107 ? -29.992 13.699 -10.686 1.00 31.16 ? 107 THR B N 1 ATOM 3412 C CA . THR B 2 107 ? -28.822 13.043 -11.284 1.00 30.36 ? 107 THR B CA 1 ATOM 3413 C C . THR B 2 107 ? -29.179 12.285 -12.564 1.00 29.77 ? 107 THR B C 1 ATOM 3414 O O . THR B 2 107 ? -28.438 12.343 -13.544 1.00 28.85 ? 107 THR B O 1 ATOM 3415 C CB . THR B 2 107 ? -28.130 12.101 -10.287 1.00 30.87 ? 107 THR B CB 1 ATOM 3416 O OG1 . THR B 2 107 ? -27.429 12.904 -9.335 1.00 30.50 ? 107 THR B OG1 1 ATOM 3417 C CG2 . THR B 2 107 ? -27.128 11.179 -10.983 1.00 30.50 ? 107 THR B CG2 1 ATOM 3418 N N . LEU B 2 108 ? -30.293 11.564 -12.533 1.00 28.73 ? 108 LEU B N 1 ATOM 3419 C CA . LEU B 2 108 ? -30.729 10.808 -13.710 1.00 29.65 ? 108 LEU B CA 1 ATOM 3420 C C . LEU B 2 108 ? -31.098 11.755 -14.850 1.00 29.67 ? 108 LEU B C 1 ATOM 3421 O O . LEU B 2 108 ? -30.805 11.493 -16.030 1.00 28.61 ? 108 LEU B O 1 ATOM 3422 C CB . LEU B 2 108 ? -31.882 9.870 -13.338 1.00 29.63 ? 108 LEU B CB 1 ATOM 3423 C CG . LEU B 2 108 ? -31.603 8.817 -12.243 1.00 30.73 ? 108 LEU B CG 1 ATOM 3424 C CD1 . LEU B 2 108 ? -32.826 7.948 -12.100 1.00 30.97 ? 108 LEU B CD1 1 ATOM 3425 C CD2 . LEU B 2 108 ? -30.354 7.964 -12.522 1.00 29.67 ? 108 LEU B CD2 1 ATOM 3426 N N . ASP B 2 109 ? -31.713 12.878 -14.492 1.00 29.67 ? 109 ASP B N 1 ATOM 3427 C CA . ASP B 2 109 ? -32.140 13.871 -15.473 1.00 29.82 ? 109 ASP B CA 1 ATOM 3428 C C . ASP B 2 109 ? -30.949 14.670 -16.024 1.00 28.79 ? 109 ASP B C 1 ATOM 3429 O O . ASP B 2 109 ? -30.941 15.073 -17.191 1.00 27.73 ? 109 ASP B O 1 ATOM 3430 C CB . ASP B 2 109 ? -33.196 14.814 -14.869 1.00 30.97 ? 109 ASP B CB 1 ATOM 3431 C CG . ASP B 2 109 ? -34.568 14.151 -14.726 1.00 34.48 ? 109 ASP B CG 1 ATOM 3432 O OD1 . ASP B 2 109 ? -34.892 13.229 -15.514 1.00 39.58 ? 109 ASP B OD1 1 ATOM 3433 O OD2 . ASP B 2 109 ? -35.341 14.561 -13.827 1.00 37.74 ? 109 ASP B OD2 1 ATOM 3434 N N . PHE B 2 110 ? -29.942 14.880 -15.185 1.00 27.28 ? 110 PHE B N 1 ATOM 3435 C CA . PHE B 2 110 ? -28.692 15.511 -15.603 1.00 26.86 ? 110 PHE B CA 1 ATOM 3436 C C . PHE B 2 110 ? -28.020 14.699 -16.724 1.00 26.28 ? 110 PHE B C 1 ATOM 3437 O O . PHE B 2 110 ? -27.606 15.252 -17.754 1.00 26.81 ? 110 PHE B O 1 ATOM 3438 C CB . PHE B 2 110 ? -27.785 15.604 -14.385 1.00 27.42 ? 110 PHE B CB 1 ATOM 3439 C CG . PHE B 2 110 ? -26.429 16.174 -14.651 1.00 26.82 ? 110 PHE B CG 1 ATOM 3440 C CD1 . PHE B 2 110 ? -26.268 17.467 -15.127 1.00 28.58 ? 110 PHE B CD1 1 ATOM 3441 C CD2 . PHE B 2 110 ? -25.296 15.428 -14.349 1.00 26.61 ? 110 PHE B CD2 1 ATOM 3442 C CE1 . PHE B 2 110 ? -24.982 17.984 -15.351 1.00 28.41 ? 110 PHE B CE1 1 ATOM 3443 C CE2 . PHE B 2 110 ? -24.029 15.946 -14.543 1.00 28.08 ? 110 PHE B CE2 1 ATOM 3444 C CZ . PHE B 2 110 ? -23.873 17.226 -15.036 1.00 28.41 ? 110 PHE B CZ 1 ATOM 3445 N N . HIS B 2 111 ? -27.934 13.387 -16.527 1.00 25.54 ? 111 HIS B N 1 ATOM 3446 C CA . HIS B 2 111 ? -27.341 12.484 -17.520 1.00 24.91 ? 111 HIS B CA 1 ATOM 3447 C C . HIS B 2 111 ? -28.167 12.511 -18.815 1.00 24.61 ? 111 HIS B C 1 ATOM 3448 O O . HIS B 2 111 ? -27.610 12.517 -19.926 1.00 25.17 ? 111 HIS B O 1 ATOM 3449 C CB . HIS B 2 111 ? -27.281 11.064 -16.971 1.00 24.96 ? 111 HIS B CB 1 ATOM 3450 C CG . HIS B 2 111 ? -26.202 10.852 -15.959 1.00 26.00 ? 111 HIS B CG 1 ATOM 3451 N ND1 . HIS B 2 111 ? -24.867 10.998 -16.260 1.00 27.58 ? 111 HIS B ND1 1 ATOM 3452 C CD2 . HIS B 2 111 ? -26.257 10.482 -14.657 1.00 28.42 ? 111 HIS B CD2 1 ATOM 3453 C CE1 . HIS B 2 111 ? -24.143 10.735 -15.184 1.00 28.14 ? 111 HIS B CE1 1 ATOM 3454 N NE2 . HIS B 2 111 ? -24.963 10.419 -14.200 1.00 27.97 ? 111 HIS B NE2 1 ATOM 3455 N N . ASP B 2 112 ? -29.489 12.545 -18.662 1.00 24.73 ? 112 ASP B N 1 ATOM 3456 C CA . ASP B 2 112 ? -30.413 12.623 -19.819 1.00 24.51 ? 112 ASP B CA 1 ATOM 3457 C C . ASP B 2 112 ? -30.179 13.912 -20.631 1.00 24.87 ? 112 ASP B C 1 ATOM 3458 O O . ASP B 2 112 ? -30.062 13.879 -21.880 1.00 23.86 ? 112 ASP B O 1 ATOM 3459 C CB . ASP B 2 112 ? -31.853 12.548 -19.301 1.00 25.19 ? 112 ASP B CB 1 ATOM 3460 C CG . ASP B 2 112 ? -32.870 12.192 -20.372 1.00 26.11 ? 112 ASP B CG 1 ATOM 3461 O OD1 . ASP B 2 112 ? -32.499 11.759 -21.499 1.00 25.19 ? 112 ASP B OD1 1 ATOM 3462 O OD2 . ASP B 2 112 ? -34.079 12.367 -20.071 1.00 28.04 ? 112 ASP B OD2 1 ATOM 3463 N N . SER B 2 113 ? -30.109 15.037 -19.915 1.00 23.87 ? 113 SER B N 1 ATOM 3464 C CA . SER B 2 113 ? -29.763 16.332 -20.498 1.00 24.52 ? 113 SER B CA 1 ATOM 3465 C C . SER B 2 113 ? -28.413 16.294 -21.221 1.00 24.06 ? 113 SER B C 1 ATOM 3466 O O . SER B 2 113 ? -28.290 16.826 -22.303 1.00 23.81 ? 113 SER B O 1 ATOM 3467 C CB . SER B 2 113 ? -29.764 17.440 -19.426 1.00 23.60 ? 113 SER B CB 1 ATOM 3468 O OG . SER B 2 113 ? -29.150 18.623 -19.925 1.00 25.64 ? 113 SER B OG 1 ATOM 3469 N N . ASN B 2 114 ? -27.411 15.655 -20.617 1.00 24.02 ? 114 ASN B N 1 ATOM 3470 C CA . ASN B 2 114 ? -26.069 15.609 -21.203 1.00 24.07 ? 114 ASN B CA 1 ATOM 3471 C C . ASN B 2 114 ? -26.059 14.828 -22.517 1.00 24.29 ? 114 ASN B C 1 ATOM 3472 O O . ASN B 2 114 ? -25.367 15.207 -23.480 1.00 24.47 ? 114 ASN B O 1 ATOM 3473 C CB . ASN B 2 114 ? -25.067 15.021 -20.213 1.00 24.65 ? 114 ASN B CB 1 ATOM 3474 C CG . ASN B 2 114 ? -24.804 15.944 -19.041 1.00 25.26 ? 114 ASN B CG 1 ATOM 3475 O OD1 . ASN B 2 114 ? -25.024 17.154 -19.131 1.00 26.97 ? 114 ASN B OD1 1 ATOM 3476 N ND2 . ASN B 2 114 ? -24.341 15.379 -17.939 1.00 27.55 ? 114 ASN B ND2 1 ATOM 3477 N N . VAL B 2 115 ? -26.838 13.750 -22.551 1.00 24.36 ? 115 VAL B N 1 ATOM 3478 C CA . VAL B 2 115 ? -26.984 12.943 -23.784 1.00 24.23 ? 115 VAL B CA 1 ATOM 3479 C C . VAL B 2 115 ? -27.709 13.765 -24.850 1.00 24.16 ? 115 VAL B C 1 ATOM 3480 O O . VAL B 2 115 ? -27.249 13.852 -25.997 1.00 24.02 ? 115 VAL B O 1 ATOM 3481 C CB . VAL B 2 115 ? -27.717 11.576 -23.525 1.00 23.94 ? 115 VAL B CB 1 ATOM 3482 C CG1 . VAL B 2 115 ? -28.049 10.853 -24.861 1.00 23.94 ? 115 VAL B CG1 1 ATOM 3483 C CG2 . VAL B 2 115 ? -26.862 10.656 -22.676 1.00 24.77 ? 115 VAL B CG2 1 ATOM 3484 N N . LYS B 2 116 ? -28.843 14.368 -24.485 1.00 23.76 ? 116 LYS B N 1 ATOM 3485 C CA . LYS B 2 116 ? -29.593 15.215 -25.429 1.00 24.24 ? 116 LYS B CA 1 ATOM 3486 C C . LYS B 2 116 ? -28.736 16.360 -25.987 1.00 24.29 ? 116 LYS B C 1 ATOM 3487 O O . LYS B 2 116 ? -28.743 16.611 -27.181 1.00 22.60 ? 116 LYS B O 1 ATOM 3488 C CB . LYS B 2 116 ? -30.900 15.723 -24.796 1.00 24.29 ? 116 LYS B CB 1 ATOM 3489 C CG . LYS B 2 116 ? -31.720 16.680 -25.674 1.00 26.80 ? 116 LYS B CG 1 ATOM 3490 C CD . LYS B 2 116 ? -32.484 15.962 -26.795 1.00 30.43 ? 116 LYS B CD 1 ATOM 3491 C CE . LYS B 2 116 ? -33.663 16.836 -27.278 1.00 30.91 ? 116 LYS B CE 1 ATOM 3492 N NZ . LYS B 2 116 ? -34.506 17.251 -26.095 1.00 33.98 ? 116 LYS B NZ 1 ATOM 3493 N N . ASN B 2 117 ? -27.972 17.028 -25.130 1.00 24.45 ? 117 ASN B N 1 ATOM 3494 C CA . ASN B 2 117 ? -27.146 18.150 -25.566 1.00 25.60 ? 117 ASN B CA 1 ATOM 3495 C C . ASN B 2 117 ? -26.008 17.746 -26.495 1.00 25.37 ? 117 ASN B C 1 ATOM 3496 O O . ASN B 2 117 ? -25.656 18.494 -27.413 1.00 25.76 ? 117 ASN B O 1 ATOM 3497 C CB . ASN B 2 117 ? -26.608 18.908 -24.354 1.00 25.86 ? 117 ASN B CB 1 ATOM 3498 C CG . ASN B 2 117 ? -27.683 19.714 -23.644 1.00 26.17 ? 117 ASN B CG 1 ATOM 3499 O OD1 . ASN B 2 117 ? -28.777 19.920 -24.157 1.00 25.21 ? 117 ASN B OD1 1 ATOM 3500 N ND2 . ASN B 2 117 ? -27.362 20.178 -22.432 1.00 26.47 ? 117 ASN B ND2 1 ATOM 3501 N N . LEU B 2 118 ? -25.456 16.555 -26.269 1.00 25.72 ? 118 LEU B N 1 ATOM 3502 C CA . LEU B 2 118 ? -24.406 16.014 -27.129 1.00 26.18 ? 118 LEU B CA 1 ATOM 3503 C C . LEU B 2 118 ? -24.965 15.681 -28.509 1.00 25.52 ? 118 LEU B C 1 ATOM 3504 O O . LEU B 2 118 ? -24.359 15.984 -29.548 1.00 24.81 ? 118 LEU B O 1 ATOM 3505 C CB . LEU B 2 118 ? -23.775 14.767 -26.502 1.00 26.55 ? 118 LEU B CB 1 ATOM 3506 C CG . LEU B 2 118 ? -22.697 14.090 -27.362 1.00 27.12 ? 118 LEU B CG 1 ATOM 3507 C CD1 . LEU B 2 118 ? -21.564 15.055 -27.675 1.00 27.44 ? 118 LEU B CD1 1 ATOM 3508 C CD2 . LEU B 2 118 ? -22.161 12.858 -26.645 1.00 27.91 ? 118 LEU B CD2 1 ATOM 3509 N N . TYR B 2 119 ? -26.126 15.040 -28.498 1.00 25.57 ? 119 TYR B N 1 ATOM 3510 C CA . TYR B 2 119 ? -26.859 14.744 -29.720 1.00 25.20 ? 119 TYR B CA 1 ATOM 3511 C C . TYR B 2 119 ? -27.134 16.001 -30.527 1.00 26.08 ? 119 TYR B C 1 ATOM 3512 O O . TYR B 2 119 ? -26.881 16.040 -31.730 1.00 25.92 ? 119 TYR B O 1 ATOM 3513 C CB . TYR B 2 119 ? -28.164 14.019 -29.400 1.00 24.90 ? 119 TYR B CB 1 ATOM 3514 C CG . TYR B 2 119 ? -28.996 13.710 -30.628 1.00 23.59 ? 119 TYR B CG 1 ATOM 3515 C CD1 . TYR B 2 119 ? -28.730 12.579 -31.404 1.00 23.61 ? 119 TYR B CD1 1 ATOM 3516 C CD2 . TYR B 2 119 ? -30.053 14.533 -31.002 1.00 22.61 ? 119 TYR B CD2 1 ATOM 3517 C CE1 . TYR B 2 119 ? -29.481 12.298 -32.546 1.00 24.21 ? 119 TYR B CE1 1 ATOM 3518 C CE2 . TYR B 2 119 ? -30.818 14.259 -32.147 1.00 24.08 ? 119 TYR B CE2 1 ATOM 3519 C CZ . TYR B 2 119 ? -30.520 13.136 -32.905 1.00 24.02 ? 119 TYR B CZ 1 ATOM 3520 O OH . TYR B 2 119 ? -31.252 12.828 -34.013 1.00 24.64 ? 119 TYR B OH 1 ATOM 3521 N N . ASP B 2 120 ? -27.664 17.017 -29.853 1.00 27.16 ? 120 ASP B N 1 ATOM 3522 C CA . ASP B 2 120 ? -27.997 18.289 -30.493 1.00 27.69 ? 120 ASP B CA 1 ATOM 3523 C C . ASP B 2 120 ? -26.775 19.005 -31.062 1.00 28.03 ? 120 ASP B C 1 ATOM 3524 O O . ASP B 2 120 ? -26.850 19.620 -32.132 1.00 27.40 ? 120 ASP B O 1 ATOM 3525 C CB . ASP B 2 120 ? -28.754 19.169 -29.496 1.00 28.36 ? 120 ASP B CB 1 ATOM 3526 C CG . ASP B 2 120 ? -30.229 18.820 -29.423 1.00 28.84 ? 120 ASP B CG 1 ATOM 3527 O OD1 . ASP B 2 120 ? -30.788 18.316 -30.432 1.00 29.95 ? 120 ASP B OD1 1 ATOM 3528 O OD2 . ASP B 2 120 ? -30.843 19.077 -28.378 1.00 29.81 ? 120 ASP B OD2 1 ATOM 3529 N N . LYS B 2 121 ? -25.652 18.897 -30.356 1.00 28.54 ? 121 LYS B N 1 ATOM 3530 C CA . LYS B 2 121 ? -24.384 19.473 -30.793 1.00 29.48 ? 121 LYS B CA 1 ATOM 3531 C C . LYS B 2 121 ? -23.934 18.875 -32.119 1.00 29.07 ? 121 LYS B C 1 ATOM 3532 O O . LYS B 2 121 ? -23.536 19.590 -33.045 1.00 29.69 ? 121 LYS B O 1 ATOM 3533 C CB . LYS B 2 121 ? -23.329 19.229 -29.709 1.00 30.15 ? 121 LYS B CB 1 ATOM 3534 C CG . LYS B 2 121 ? -22.254 20.292 -29.622 1.00 33.08 ? 121 LYS B CG 1 ATOM 3535 C CD . LYS B 2 121 ? -21.424 20.094 -28.347 1.00 34.26 ? 121 LYS B CD 1 ATOM 3536 C CE . LYS B 2 121 ? -20.342 21.178 -28.195 1.00 35.86 ? 121 LYS B CE 1 ATOM 3537 N NZ . LYS B 2 121 ? -19.411 21.239 -29.371 1.00 37.06 ? 121 LYS B NZ 1 ATOM 3538 N N . VAL B 2 122 ? -23.997 17.554 -32.215 1.00 28.46 ? 122 VAL B N 1 ATOM 3539 C CA . VAL B 2 122 ? -23.644 16.859 -33.443 1.00 27.62 ? 122 VAL B CA 1 ATOM 3540 C C . VAL B 2 122 ? -24.656 17.188 -34.553 1.00 27.98 ? 122 VAL B C 1 ATOM 3541 O O . VAL B 2 122 ? -24.273 17.495 -35.692 1.00 27.11 ? 122 VAL B O 1 ATOM 3542 C CB . VAL B 2 122 ? -23.560 15.333 -33.193 1.00 27.88 ? 122 VAL B CB 1 ATOM 3543 C CG1 . VAL B 2 122 ? -23.431 14.562 -34.509 1.00 26.62 ? 122 VAL B CG1 1 ATOM 3544 C CG2 . VAL B 2 122 ? -22.421 15.012 -32.223 1.00 26.40 ? 122 VAL B CG2 1 ATOM 3545 N N . ARG B 2 123 ? -25.945 17.137 -34.216 1.00 27.61 ? 123 ARG B N 1 ATOM 3546 C CA . ARG B 2 123 ? -27.013 17.470 -35.165 1.00 28.48 ? 123 ARG B CA 1 ATOM 3547 C C . ARG B 2 123 ? -26.800 18.845 -35.818 1.00 30.03 ? 123 ARG B C 1 ATOM 3548 O O . ARG B 2 123 ? -26.829 18.979 -37.055 1.00 30.14 ? 123 ARG B O 1 ATOM 3549 C CB . ARG B 2 123 ? -28.372 17.429 -34.449 1.00 27.49 ? 123 ARG B CB 1 ATOM 3550 C CG . ARG B 2 123 ? -29.553 17.808 -35.332 1.00 25.54 ? 123 ARG B CG 1 ATOM 3551 C CD . ARG B 2 123 ? -30.872 17.773 -34.562 1.00 28.74 ? 123 ARG B CD 1 ATOM 3552 N NE . ARG B 2 123 ? -30.939 18.689 -33.414 1.00 26.85 ? 123 ARG B NE 1 ATOM 3553 C CZ . ARG B 2 123 ? -31.234 19.990 -33.498 1.00 29.19 ? 123 ARG B CZ 1 ATOM 3554 N NH1 . ARG B 2 123 ? -31.450 20.563 -34.680 1.00 26.19 ? 123 ARG B NH1 1 ATOM 3555 N NH2 . ARG B 2 123 ? -31.292 20.727 -32.397 1.00 27.88 ? 123 ARG B NH2 1 ATOM 3556 N N . MET B 2 124 ? -26.567 19.845 -34.970 1.00 32.60 ? 124 MET B N 1 ATOM 3557 C CA . MET B 2 124 ? -26.465 21.243 -35.393 1.00 35.77 ? 124 MET B CA 1 ATOM 3558 C C . MET B 2 124 ? -25.209 21.492 -36.228 1.00 35.78 ? 124 MET B C 1 ATOM 3559 O O . MET B 2 124 ? -25.118 22.506 -36.927 1.00 36.15 ? 124 MET B O 1 ATOM 3560 C CB . MET B 2 124 ? -26.557 22.192 -34.182 1.00 34.97 ? 124 MET B CB 1 ATOM 3561 C CG . MET B 2 124 ? -27.925 22.125 -33.440 1.00 37.59 ? 124 MET B CG 1 ATOM 3562 S SD . MET B 2 124 ? -28.276 23.259 -32.056 1.00 40.40 ? 124 MET B SD 1 ATOM 3563 C CE . MET B 2 124 ? -28.542 24.784 -32.943 1.00 39.44 ? 124 MET B CE 1 ATOM 3564 N N . GLN B 2 125 ? -24.272 20.541 -36.175 1.00 36.30 ? 125 GLN B N 1 ATOM 3565 C CA . GLN B 2 125 ? -23.014 20.581 -36.925 1.00 36.71 ? 125 GLN B CA 1 ATOM 3566 C C . GLN B 2 125 ? -23.115 19.904 -38.308 1.00 36.02 ? 125 GLN B C 1 ATOM 3567 O O . GLN B 2 125 ? -22.627 20.438 -39.312 1.00 36.09 ? 125 GLN B O 1 ATOM 3568 C CB . GLN B 2 125 ? -21.878 19.981 -36.068 1.00 37.16 ? 125 GLN B CB 1 ATOM 3569 C CG . GLN B 2 125 ? -20.475 20.034 -36.701 1.00 39.02 ? 125 GLN B CG 1 ATOM 3570 C CD . GLN B 2 125 ? -19.338 19.747 -35.714 1.00 38.34 ? 125 GLN B CD 1 ATOM 3571 O OE1 . GLN B 2 125 ? -18.564 18.802 -35.898 1.00 39.71 ? 125 GLN B OE1 1 ATOM 3572 N NE2 . GLN B 2 125 ? -19.214 20.583 -34.686 1.00 40.90 ? 125 GLN B NE2 1 ATOM 3573 N N . LEU B 2 126 ? -23.762 18.741 -38.354 1.00 34.37 ? 126 LEU B N 1 ATOM 3574 C CA . LEU B 2 126 ? -23.910 17.961 -39.576 1.00 34.02 ? 126 LEU B CA 1 ATOM 3575 C C . LEU B 2 126 ? -24.936 18.584 -40.514 1.00 33.30 ? 126 LEU B C 1 ATOM 3576 O O . LEU B 2 126 ? -24.821 18.447 -41.725 1.00 33.92 ? 126 LEU B O 1 ATOM 3577 C CB . LEU B 2 126 ? -24.298 16.514 -39.243 1.00 33.63 ? 126 LEU B CB 1 ATOM 3578 C CG . LEU B 2 126 ? -23.414 15.791 -38.212 1.00 33.24 ? 126 LEU B CG 1 ATOM 3579 C CD1 . LEU B 2 126 ? -23.876 14.344 -38.014 1.00 32.39 ? 126 LEU B CD1 1 ATOM 3580 C CD2 . LEU B 2 126 ? -21.928 15.855 -38.569 1.00 34.17 ? 126 LEU B CD2 1 ATOM 3581 N N . ARG B 2 127 ? -25.936 19.251 -39.930 1.00 33.03 ? 127 ARG B N 1 ATOM 3582 C CA A ARG B 2 127 ? -27.013 19.908 -40.684 0.50 32.95 ? 127 ARG B CA 1 ATOM 3583 C CA B ARG B 2 127 ? -27.011 19.904 -40.683 0.50 32.97 ? 127 ARG B CA 1 ATOM 3584 C C . ARG B 2 127 ? -27.650 18.952 -41.691 1.00 33.01 ? 127 ARG B C 1 ATOM 3585 O O . ARG B 2 127 ? -27.995 17.826 -41.335 1.00 32.38 ? 127 ARG B O 1 ATOM 3586 C CB A ARG B 2 127 ? -26.525 21.208 -41.351 0.50 33.04 ? 127 ARG B CB 1 ATOM 3587 C CB B ARG B 2 127 ? -26.507 21.190 -41.349 0.50 33.03 ? 127 ARG B CB 1 ATOM 3588 C CG A ARG B 2 127 ? -26.055 22.269 -40.357 0.50 32.51 ? 127 ARG B CG 1 ATOM 3589 C CG B ARG B 2 127 ? -25.828 22.142 -40.372 0.50 32.47 ? 127 ARG B CG 1 ATOM 3590 C CD A ARG B 2 127 ? -25.429 23.490 -41.042 0.50 32.81 ? 127 ARG B CD 1 ATOM 3591 C CD B ARG B 2 127 ? -25.340 23.407 -41.058 0.50 32.52 ? 127 ARG B CD 1 ATOM 3592 N NE A ARG B 2 127 ? -24.431 24.131 -40.181 0.50 32.75 ? 127 ARG B NE 1 ATOM 3593 N NE B ARG B 2 127 ? -26.458 24.190 -41.573 0.50 32.43 ? 127 ARG B NE 1 ATOM 3594 C CZ A ARG B 2 127 ? -23.844 25.307 -40.412 0.50 32.03 ? 127 ARG B CZ 1 ATOM 3595 C CZ B ARG B 2 127 ? -26.367 25.416 -42.074 0.50 32.51 ? 127 ARG B CZ 1 ATOM 3596 N NH1 A ARG B 2 127 ? -24.147 26.030 -41.490 0.50 31.46 ? 127 ARG B NH1 1 ATOM 3597 N NH1 B ARG B 2 127 ? -25.198 26.045 -42.143 0.50 32.07 ? 127 ARG B NH1 1 ATOM 3598 N NH2 A ARG B 2 127 ? -22.948 25.770 -39.548 0.50 30.16 ? 127 ARG B NH2 1 ATOM 3599 N NH2 B ARG B 2 127 ? -27.464 26.015 -42.509 0.50 33.47 ? 127 ARG B NH2 1 ATOM 3600 N N . ASP B 2 128 ? -27.797 19.386 -42.953 1.00 33.09 ? 128 ASP B N 1 ATOM 3601 C CA . ASP B 2 128 ? -28.472 18.570 -43.952 1.00 33.78 ? 128 ASP B CA 1 ATOM 3602 C C . ASP B 2 128 ? -27.534 17.689 -44.780 1.00 33.50 ? 128 ASP B C 1 ATOM 3603 O O . ASP B 2 128 ? -27.933 17.129 -45.800 1.00 33.83 ? 128 ASP B O 1 ATOM 3604 C CB . ASP B 2 128 ? -29.359 19.428 -44.867 1.00 33.75 ? 128 ASP B CB 1 ATOM 3605 C CG . ASP B 2 128 ? -28.578 20.476 -45.634 1.00 35.56 ? 128 ASP B CG 1 ATOM 3606 O OD1 . ASP B 2 128 ? -27.349 20.574 -45.451 1.00 37.81 ? 128 ASP B OD1 1 ATOM 3607 O OD2 . ASP B 2 128 ? -29.206 21.206 -46.435 1.00 36.58 ? 128 ASP B OD2 1 ATOM 3608 N N . ASN B 2 129 ? -26.296 17.554 -44.324 1.00 33.35 ? 129 ASN B N 1 ATOM 3609 C CA . ASN B 2 129 ? -25.400 16.562 -44.892 1.00 33.30 ? 129 ASN B CA 1 ATOM 3610 C C . ASN B 2 129 ? -25.692 15.146 -44.398 1.00 32.90 ? 129 ASN B C 1 ATOM 3611 O O . ASN B 2 129 ? -25.075 14.175 -44.856 1.00 32.82 ? 129 ASN B O 1 ATOM 3612 C CB . ASN B 2 129 ? -23.953 16.959 -44.639 1.00 33.48 ? 129 ASN B CB 1 ATOM 3613 C CG . ASN B 2 129 ? -23.468 18.005 -45.627 1.00 34.71 ? 129 ASN B CG 1 ATOM 3614 O OD1 . ASN B 2 129 ? -24.209 18.404 -46.536 1.00 34.05 ? 129 ASN B OD1 1 ATOM 3615 N ND2 . ASN B 2 129 ? -22.222 18.455 -45.458 1.00 35.73 ? 129 ASN B ND2 1 ATOM 3616 N N . VAL B 2 130 ? -26.650 15.038 -43.470 1.00 32.44 ? 130 VAL B N 1 ATOM 3617 C CA . VAL B 2 130 ? -27.080 13.753 -42.901 1.00 31.71 ? 130 VAL B CA 1 ATOM 3618 C C . VAL B 2 130 ? -28.610 13.694 -42.815 1.00 31.57 ? 130 VAL B C 1 ATOM 3619 O O . VAL B 2 130 ? -29.267 14.738 -42.877 1.00 31.88 ? 130 VAL B O 1 ATOM 3620 C CB . VAL B 2 130 ? -26.462 13.503 -41.482 1.00 31.92 ? 130 VAL B CB 1 ATOM 3621 C CG1 . VAL B 2 130 ? -24.947 13.486 -41.547 1.00 32.49 ? 130 VAL B CG1 1 ATOM 3622 C CG2 . VAL B 2 130 ? -26.953 14.547 -40.462 1.00 30.82 ? 130 VAL B CG2 1 ATOM 3623 N N . LYS B 2 131 ? -29.169 12.486 -42.696 1.00 31.03 ? 131 LYS B N 1 ATOM 3624 C CA . LYS B 2 131 ? -30.582 12.302 -42.345 1.00 30.28 ? 131 LYS B CA 1 ATOM 3625 C C . LYS B 2 131 ? -30.616 11.960 -40.867 1.00 29.63 ? 131 LYS B C 1 ATOM 3626 O O . LYS B 2 131 ? -29.834 11.134 -40.423 1.00 28.78 ? 131 LYS B O 1 ATOM 3627 C CB . LYS B 2 131 ? -31.227 11.110 -43.061 1.00 30.74 ? 131 LYS B CB 1 ATOM 3628 C CG . LYS B 2 131 ? -31.178 11.102 -44.563 1.00 32.83 ? 131 LYS B CG 1 ATOM 3629 C CD . LYS B 2 131 ? -32.374 10.337 -45.136 1.00 36.62 ? 131 LYS B CD 1 ATOM 3630 C CE . LYS B 2 131 ? -32.536 8.948 -44.519 1.00 39.13 ? 131 LYS B CE 1 ATOM 3631 N NZ . LYS B 2 131 ? -31.705 7.945 -45.224 1.00 42.13 ? 131 LYS B NZ 1 ATOM 3632 N N . GLU B 2 132 ? -31.536 12.577 -40.135 1.00 29.40 ? 132 GLU B N 1 ATOM 3633 C CA . GLU B 2 132 ? -31.824 12.186 -38.758 1.00 29.34 ? 132 GLU B CA 1 ATOM 3634 C C . GLU B 2 132 ? -32.751 10.983 -38.773 1.00 28.82 ? 132 GLU B C 1 ATOM 3635 O O . GLU B 2 132 ? -33.919 11.115 -39.133 1.00 28.32 ? 132 GLU B O 1 ATOM 3636 C CB . GLU B 2 132 ? -32.550 13.320 -38.036 1.00 29.94 ? 132 GLU B CB 1 ATOM 3637 C CG . GLU B 2 132 ? -31.727 14.086 -37.056 1.00 32.37 ? 132 GLU B CG 1 ATOM 3638 C CD . GLU B 2 132 ? -32.565 15.071 -36.285 1.00 34.17 ? 132 GLU B CD 1 ATOM 3639 O OE1 . GLU B 2 132 ? -32.835 14.823 -35.078 1.00 32.28 ? 132 GLU B OE1 1 ATOM 3640 O OE2 . GLU B 2 132 ? -32.953 16.084 -36.908 1.00 36.16 ? 132 GLU B OE2 1 ATOM 3641 N N . LEU B 2 133 ? -32.260 9.821 -38.354 1.00 28.39 ? 133 LEU B N 1 ATOM 3642 C CA . LEU B 2 133 ? -33.089 8.612 -38.385 1.00 28.32 ? 133 LEU B CA 1 ATOM 3643 C C . LEU B 2 133 ? -34.178 8.540 -37.314 1.00 27.95 ? 133 LEU B C 1 ATOM 3644 O O . LEU B 2 133 ? -35.215 7.900 -37.524 1.00 27.64 ? 133 LEU B O 1 ATOM 3645 C CB . LEU B 2 133 ? -32.222 7.353 -38.379 1.00 28.79 ? 133 LEU B CB 1 ATOM 3646 C CG . LEU B 2 133 ? -31.251 7.234 -39.555 1.00 29.89 ? 133 LEU B CG 1 ATOM 3647 C CD1 . LEU B 2 133 ? -30.429 5.967 -39.387 1.00 31.63 ? 133 LEU B CD1 1 ATOM 3648 C CD2 . LEU B 2 133 ? -31.965 7.249 -40.922 1.00 32.80 ? 133 LEU B CD2 1 ATOM 3649 N N . GLY B 2 134 ? -33.934 9.190 -36.175 1.00 27.33 ? 134 GLY B N 1 ATOM 3650 C CA . GLY B 2 134 ? -34.901 9.280 -35.087 1.00 27.03 ? 134 GLY B CA 1 ATOM 3651 C C . GLY B 2 134 ? -34.558 8.390 -33.910 1.00 26.90 ? 134 GLY B C 1 ATOM 3652 O O . GLY B 2 134 ? -35.316 8.322 -32.945 1.00 27.52 ? 134 GLY B O 1 ATOM 3653 N N . ASN B 2 135 ? -33.407 7.727 -34.000 1.00 26.18 ? 135 ASN B N 1 ATOM 3654 C CA . ASN B 2 135 ? -32.973 6.713 -33.037 1.00 26.37 ? 135 ASN B CA 1 ATOM 3655 C C . ASN B 2 135 ? -31.618 7.050 -32.396 1.00 26.02 ? 135 ASN B C 1 ATOM 3656 O O . ASN B 2 135 ? -30.990 6.180 -31.776 1.00 25.69 ? 135 ASN B O 1 ATOM 3657 C CB . ASN B 2 135 ? -32.892 5.343 -33.742 1.00 26.86 ? 135 ASN B CB 1 ATOM 3658 C CG . ASN B 2 135 ? -31.819 5.300 -34.823 1.00 27.79 ? 135 ASN B CG 1 ATOM 3659 O OD1 . ASN B 2 135 ? -31.328 6.339 -35.283 1.00 25.90 ? 135 ASN B OD1 1 ATOM 3660 N ND2 . ASN B 2 135 ? -31.457 4.091 -35.249 1.00 29.25 ? 135 ASN B ND2 1 ATOM 3661 N N . GLY B 2 136 ? -31.166 8.298 -32.562 1.00 25.07 ? 136 GLY B N 1 ATOM 3662 C CA . GLY B 2 136 ? -29.833 8.703 -32.103 1.00 25.14 ? 136 GLY B CA 1 ATOM 3663 C C . GLY B 2 136 ? -28.760 8.682 -33.185 1.00 25.56 ? 136 GLY B C 1 ATOM 3664 O O . GLY B 2 136 ? -27.637 9.149 -32.973 1.00 24.97 ? 136 GLY B O 1 ATOM 3665 N N . CYS B 2 137 ? -29.106 8.119 -34.341 1.00 25.65 ? 137 CYS B N 1 ATOM 3666 C CA . CYS B 2 137 ? -28.178 8.022 -35.465 1.00 25.92 ? 137 CYS B CA 1 ATOM 3667 C C . CYS B 2 137 ? -28.432 9.041 -36.563 1.00 25.88 ? 137 CYS B C 1 ATOM 3668 O O . CYS B 2 137 ? -29.571 9.462 -36.807 1.00 24.98 ? 137 CYS B O 1 ATOM 3669 C CB . CYS B 2 137 ? -28.224 6.626 -36.090 1.00 26.53 ? 137 CYS B CB 1 ATOM 3670 S SG . CYS B 2 137 ? -27.950 5.300 -34.919 1.00 28.49 ? 137 CYS B SG 1 ATOM 3671 N N . PHE B 2 138 ? -27.339 9.380 -37.246 1.00 26.40 ? 138 PHE B N 1 ATOM 3672 C CA . PHE B 2 138 ? -27.349 10.226 -38.429 1.00 27.22 ? 138 PHE B CA 1 ATOM 3673 C C . PHE B 2 138 ? -26.741 9.412 -39.542 1.00 28.56 ? 138 PHE B C 1 ATOM 3674 O O . PHE B 2 138 ? -25.670 8.826 -39.370 1.00 28.08 ? 138 PHE B O 1 ATOM 3675 C CB . PHE B 2 138 ? -26.479 11.466 -38.219 1.00 27.38 ? 138 PHE B CB 1 ATOM 3676 C CG . PHE B 2 138 ? -26.874 12.282 -37.023 1.00 25.81 ? 138 PHE B CG 1 ATOM 3677 C CD1 . PHE B 2 138 ? -27.893 13.213 -37.122 1.00 26.95 ? 138 PHE B CD1 1 ATOM 3678 C CD2 . PHE B 2 138 ? -26.230 12.108 -35.807 1.00 28.70 ? 138 PHE B CD2 1 ATOM 3679 C CE1 . PHE B 2 138 ? -28.267 13.964 -36.020 1.00 25.93 ? 138 PHE B CE1 1 ATOM 3680 C CE2 . PHE B 2 138 ? -26.603 12.858 -34.696 1.00 27.15 ? 138 PHE B CE2 1 ATOM 3681 C CZ . PHE B 2 138 ? -27.617 13.789 -34.816 1.00 26.52 ? 138 PHE B CZ 1 ATOM 3682 N N . GLU B 2 139 ? -27.435 9.390 -40.676 1.00 30.06 ? 139 GLU B N 1 ATOM 3683 C CA . GLU B 2 139 ? -26.977 8.663 -41.848 1.00 31.72 ? 139 GLU B CA 1 ATOM 3684 C C . GLU B 2 139 ? -26.496 9.699 -42.849 1.00 32.68 ? 139 GLU B C 1 ATOM 3685 O O . GLU B 2 139 ? -27.243 10.611 -43.222 1.00 33.13 ? 139 GLU B O 1 ATOM 3686 C CB . GLU B 2 139 ? -28.136 7.848 -42.402 1.00 31.91 ? 139 GLU B CB 1 ATOM 3687 C CG . GLU B 2 139 ? -27.779 6.815 -43.453 1.00 34.45 ? 139 GLU B CG 1 ATOM 3688 C CD . GLU B 2 139 ? -28.927 6.624 -44.400 1.00 38.48 ? 139 GLU B CD 1 ATOM 3689 O OE1 . GLU B 2 139 ? -29.579 5.554 -44.379 1.00 41.20 ? 139 GLU B OE1 1 ATOM 3690 O OE2 . GLU B 2 139 ? -29.205 7.578 -45.155 1.00 42.05 ? 139 GLU B OE2 1 ATOM 3691 N N . PHE B 2 140 ? -25.244 9.550 -43.273 1.00 33.65 ? 140 PHE B N 1 ATOM 3692 C CA . PHE B 2 140 ? -24.551 10.512 -44.124 1.00 34.34 ? 140 PHE B CA 1 ATOM 3693 C C . PHE B 2 140 ? -24.983 10.452 -45.584 1.00 34.66 ? 140 PHE B C 1 ATOM 3694 O O . PHE B 2 140 ? -25.212 9.376 -46.130 1.00 34.71 ? 140 PHE B O 1 ATOM 3695 C CB . PHE B 2 140 ? -23.041 10.276 -44.034 1.00 34.59 ? 140 PHE B CB 1 ATOM 3696 C CG . PHE B 2 140 ? -22.440 10.694 -42.726 1.00 34.23 ? 140 PHE B CG 1 ATOM 3697 C CD1 . PHE B 2 140 ? -21.822 11.931 -42.603 1.00 33.10 ? 140 PHE B CD1 1 ATOM 3698 C CD2 . PHE B 2 140 ? -22.491 9.856 -41.611 1.00 34.96 ? 140 PHE B CD2 1 ATOM 3699 C CE1 . PHE B 2 140 ? -21.267 12.335 -41.409 1.00 34.35 ? 140 PHE B CE1 1 ATOM 3700 C CE2 . PHE B 2 140 ? -21.935 10.258 -40.402 1.00 34.41 ? 140 PHE B CE2 1 ATOM 3701 C CZ . PHE B 2 140 ? -21.325 11.499 -40.300 1.00 33.93 ? 140 PHE B CZ 1 ATOM 3702 N N . TYR B 2 141 ? -25.112 11.632 -46.184 1.00 35.10 ? 141 TYR B N 1 ATOM 3703 C CA . TYR B 2 141 ? -25.357 11.799 -47.619 1.00 36.11 ? 141 TYR B CA 1 ATOM 3704 C C . TYR B 2 141 ? -24.035 11.835 -48.389 1.00 36.60 ? 141 TYR B C 1 ATOM 3705 O O . TYR B 2 141 ? -23.912 12.488 -49.448 1.00 36.83 ? 141 TYR B O 1 ATOM 3706 C CB . TYR B 2 141 ? -26.103 13.100 -47.854 1.00 35.84 ? 141 TYR B CB 1 ATOM 3707 C CG . TYR B 2 141 ? -27.579 13.026 -47.601 1.00 35.95 ? 141 TYR B CG 1 ATOM 3708 C CD1 . TYR B 2 141 ? -28.384 12.139 -48.317 1.00 37.07 ? 141 TYR B CD1 1 ATOM 3709 C CD2 . TYR B 2 141 ? -28.182 13.876 -46.678 1.00 37.19 ? 141 TYR B CD2 1 ATOM 3710 C CE1 . TYR B 2 141 ? -29.748 12.082 -48.098 1.00 37.74 ? 141 TYR B CE1 1 ATOM 3711 C CE2 . TYR B 2 141 ? -29.544 13.829 -46.447 1.00 36.14 ? 141 TYR B CE2 1 ATOM 3712 C CZ . TYR B 2 141 ? -30.318 12.932 -47.149 1.00 36.56 ? 141 TYR B CZ 1 ATOM 3713 O OH . TYR B 2 141 ? -31.668 12.896 -46.934 1.00 35.92 ? 141 TYR B OH 1 ATOM 3714 N N . HIS B 2 142 ? -23.051 11.126 -47.848 1.00 36.90 ? 142 HIS B N 1 ATOM 3715 C CA . HIS B 2 142 ? -21.723 11.030 -48.432 1.00 37.26 ? 142 HIS B CA 1 ATOM 3716 C C . HIS B 2 142 ? -20.952 9.929 -47.706 1.00 37.61 ? 142 HIS B C 1 ATOM 3717 O O . HIS B 2 142 ? -21.361 9.484 -46.633 1.00 37.32 ? 142 HIS B O 1 ATOM 3718 C CB . HIS B 2 142 ? -20.992 12.387 -48.362 1.00 37.12 ? 142 HIS B CB 1 ATOM 3719 C CG . HIS B 2 142 ? -20.640 12.840 -46.975 1.00 36.76 ? 142 HIS B CG 1 ATOM 3720 N ND1 . HIS B 2 142 ? -19.488 12.439 -46.335 1.00 37.31 ? 142 HIS B ND1 1 ATOM 3721 C CD2 . HIS B 2 142 ? -21.262 13.694 -46.126 1.00 37.51 ? 142 HIS B CD2 1 ATOM 3722 C CE1 . HIS B 2 142 ? -19.421 13.013 -45.144 1.00 37.70 ? 142 HIS B CE1 1 ATOM 3723 N NE2 . HIS B 2 142 ? -20.486 13.779 -44.991 1.00 36.99 ? 142 HIS B NE2 1 ATOM 3724 N N . LYS B 2 143 ? -19.864 9.460 -48.308 1.00 38.10 ? 143 LYS B N 1 ATOM 3725 C CA . LYS B 2 143 ? -18.965 8.543 -47.608 1.00 38.67 ? 143 LYS B CA 1 ATOM 3726 C C . LYS B 2 143 ? -18.204 9.335 -46.549 1.00 38.79 ? 143 LYS B C 1 ATOM 3727 O O . LYS B 2 143 ? -17.705 10.427 -46.822 1.00 38.98 ? 143 LYS B O 1 ATOM 3728 C CB . LYS B 2 143 ? -18.023 7.840 -48.592 1.00 38.68 ? 143 LYS B CB 1 ATOM 3729 C CG . LYS B 2 143 ? -18.784 7.076 -49.668 1.00 39.10 ? 143 LYS B CG 1 ATOM 3730 C CD . LYS B 2 143 ? -17.973 5.946 -50.260 1.00 40.23 ? 143 LYS B CD 1 ATOM 3731 C CE . LYS B 2 143 ? -18.876 4.764 -50.616 1.00 40.76 ? 143 LYS B CE 1 ATOM 3732 N NZ . LYS B 2 143 ? -19.388 4.065 -49.384 1.00 41.27 ? 143 LYS B NZ 1 ATOM 3733 N N . CYS B 2 144 ? -18.162 8.800 -45.331 1.00 39.26 ? 144 CYS B N 1 ATOM 3734 C CA . CYS B 2 144 ? -17.509 9.474 -44.209 1.00 39.80 ? 144 CYS B CA 1 ATOM 3735 C C . CYS B 2 144 ? -16.486 8.533 -43.586 1.00 40.42 ? 144 CYS B C 1 ATOM 3736 O O . CYS B 2 144 ? -16.837 7.668 -42.774 1.00 40.40 ? 144 CYS B O 1 ATOM 3737 C CB . CYS B 2 144 ? -18.549 9.933 -43.167 1.00 39.67 ? 144 CYS B CB 1 ATOM 3738 S SG . CYS B 2 144 ? -17.905 10.916 -41.757 1.00 39.18 ? 144 CYS B SG 1 ATOM 3739 N N . ASP B 2 145 ? -15.221 8.703 -43.972 1.00 40.88 ? 145 ASP B N 1 ATOM 3740 C CA . ASP B 2 145 ? -14.138 7.823 -43.512 1.00 41.53 ? 145 ASP B CA 1 ATOM 3741 C C . ASP B 2 145 ? -13.797 7.953 -42.011 1.00 41.63 ? 145 ASP B C 1 ATOM 3742 O O . ASP B 2 145 ? -14.507 8.627 -41.264 1.00 41.77 ? 145 ASP B O 1 ATOM 3743 C CB . ASP B 2 145 ? -12.900 7.923 -44.436 1.00 41.65 ? 145 ASP B CB 1 ATOM 3744 C CG . ASP B 2 145 ? -12.038 9.168 -44.196 1.00 42.01 ? 145 ASP B CG 1 ATOM 3745 O OD1 . ASP B 2 145 ? -12.327 9.993 -43.312 1.00 42.46 ? 145 ASP B OD1 1 ATOM 3746 O OD2 . ASP B 2 145 ? -11.031 9.312 -44.923 1.00 42.88 ? 145 ASP B OD2 1 ATOM 3747 N N . ASP B 2 146 ? -12.732 7.290 -41.571 1.00 41.79 ? 146 ASP B N 1 ATOM 3748 C CA . ASP B 2 146 ? -12.336 7.352 -40.166 1.00 41.84 ? 146 ASP B CA 1 ATOM 3749 C C . ASP B 2 146 ? -11.925 8.756 -39.740 1.00 41.80 ? 146 ASP B C 1 ATOM 3750 O O . ASP B 2 146 ? -12.316 9.219 -38.677 1.00 41.54 ? 146 ASP B O 1 ATOM 3751 C CB . ASP B 2 146 ? -11.243 6.325 -39.853 1.00 42.05 ? 146 ASP B CB 1 ATOM 3752 C CG . ASP B 2 146 ? -11.797 4.918 -39.680 1.00 42.27 ? 146 ASP B CG 1 ATOM 3753 O OD1 . ASP B 2 146 ? -13.035 4.739 -39.714 1.00 42.60 ? 146 ASP B OD1 1 ATOM 3754 O OD2 . ASP B 2 146 ? -10.991 3.983 -39.504 1.00 42.90 ? 146 ASP B OD2 1 ATOM 3755 N N . GLU B 2 147 ? -11.173 9.446 -40.591 1.00 41.74 ? 147 GLU B N 1 ATOM 3756 C CA . GLU B 2 147 ? -10.779 10.834 -40.331 1.00 42.01 ? 147 GLU B CA 1 ATOM 3757 C C . GLU B 2 147 ? -11.996 11.756 -40.315 1.00 41.77 ? 147 GLU B C 1 ATOM 3758 O O . GLU B 2 147 ? -12.032 12.740 -39.568 1.00 41.87 ? 147 GLU B O 1 ATOM 3759 C CB . GLU B 2 147 ? -9.770 11.318 -41.384 1.00 42.45 ? 147 GLU B CB 1 ATOM 3760 C CG . GLU B 2 147 ? -8.603 10.356 -41.654 1.00 43.60 ? 147 GLU B CG 1 ATOM 3761 C CD . GLU B 2 147 ? -7.674 10.154 -40.462 1.00 45.56 ? 147 GLU B CD 1 ATOM 3762 O OE1 . GLU B 2 147 ? -7.808 10.866 -39.435 1.00 47.39 ? 147 GLU B OE1 1 ATOM 3763 O OE2 . GLU B 2 147 ? -6.795 9.269 -40.554 1.00 46.56 ? 147 GLU B OE2 1 ATOM 3764 N N . CYS B 2 148 ? -12.982 11.419 -41.148 1.00 41.54 ? 148 CYS B N 1 ATOM 3765 C CA . CYS B 2 148 ? -14.251 12.138 -41.230 1.00 40.96 ? 148 CYS B CA 1 ATOM 3766 C C . CYS B 2 148 ? -15.076 11.923 -39.959 1.00 40.43 ? 148 CYS B C 1 ATOM 3767 O O . CYS B 2 148 ? -15.641 12.873 -39.417 1.00 40.63 ? 148 CYS B O 1 ATOM 3768 C CB . CYS B 2 148 ? -15.039 11.697 -42.474 1.00 40.65 ? 148 CYS B CB 1 ATOM 3769 S SG . CYS B 2 148 ? -16.739 12.347 -42.653 1.00 42.45 ? 148 CYS B SG 1 ATOM 3770 N N . MET B 2 149 ? -15.144 10.680 -39.488 1.00 39.63 ? 149 MET B N 1 ATOM 3771 C CA . MET B 2 149 ? -15.853 10.379 -38.237 1.00 38.98 ? 149 MET B CA 1 ATOM 3772 C C . MET B 2 149 ? -15.158 11.068 -37.063 1.00 38.67 ? 149 MET B C 1 ATOM 3773 O O . MET B 2 149 ? -15.806 11.651 -36.200 1.00 38.36 ? 149 MET B O 1 ATOM 3774 C CB . MET B 2 149 ? -15.966 8.867 -38.010 1.00 38.76 ? 149 MET B CB 1 ATOM 3775 C CG . MET B 2 149 ? -16.834 8.123 -39.038 1.00 37.76 ? 149 MET B CG 1 ATOM 3776 S SD . MET B 2 149 ? -18.584 8.575 -38.996 1.00 35.43 ? 149 MET B SD 1 ATOM 3777 C CE . MET B 2 149 ? -19.279 7.410 -40.174 1.00 37.62 ? 149 MET B CE 1 ATOM 3778 N N . ASN B 2 150 ? -13.829 11.031 -37.066 1.00 38.40 ? 150 ASN B N 1 ATOM 3779 C CA . ASN B 2 150 ? -13.033 11.686 -36.035 1.00 38.75 ? 150 ASN B CA 1 ATOM 3780 C C . ASN B 2 150 ? -13.243 13.194 -35.945 1.00 38.66 ? 150 ASN B C 1 ATOM 3781 O O . ASN B 2 150 ? -13.168 13.757 -34.858 1.00 38.41 ? 150 ASN B O 1 ATOM 3782 C CB . ASN B 2 150 ? -11.544 11.355 -36.203 1.00 38.90 ? 150 ASN B CB 1 ATOM 3783 C CG . ASN B 2 150 ? -11.218 9.910 -35.844 1.00 39.61 ? 150 ASN B CG 1 ATOM 3784 O OD1 . ASN B 2 150 ? -11.905 9.282 -35.029 1.00 38.98 ? 150 ASN B OD1 1 ATOM 3785 N ND2 . ASN B 2 150 ? -10.157 9.375 -36.453 1.00 40.26 ? 150 ASN B ND2 1 ATOM 3786 N N . SER B 2 151 ? -13.513 13.841 -37.077 1.00 38.96 ? 151 SER B N 1 ATOM 3787 C CA . SER B 2 151 ? -13.817 15.276 -37.086 1.00 39.05 ? 151 SER B CA 1 ATOM 3788 C C . SER B 2 151 ? -15.146 15.601 -36.398 1.00 39.12 ? 151 SER B C 1 ATOM 3789 O O . SER B 2 151 ? -15.250 16.590 -35.670 1.00 38.94 ? 151 SER B O 1 ATOM 3790 C CB . SER B 2 151 ? -13.800 15.831 -38.514 1.00 39.01 ? 151 SER B CB 1 ATOM 3791 O OG . SER B 2 151 ? -14.881 15.337 -39.278 1.00 39.32 ? 151 SER B OG 1 ATOM 3792 N N . VAL B 2 152 ? -16.150 14.758 -36.621 1.00 39.57 ? 152 VAL B N 1 ATOM 3793 C CA . VAL B 2 152 ? -17.463 14.933 -35.994 1.00 40.22 ? 152 VAL B CA 1 ATOM 3794 C C . VAL B 2 152 ? -17.347 14.795 -34.470 1.00 40.93 ? 152 VAL B C 1 ATOM 3795 O O . VAL B 2 152 ? -17.845 15.643 -33.728 1.00 40.62 ? 152 VAL B O 1 ATOM 3796 C CB . VAL B 2 152 ? -18.520 13.927 -36.547 1.00 40.09 ? 152 VAL B CB 1 ATOM 3797 C CG1 . VAL B 2 152 ? -19.892 14.154 -35.895 1.00 39.97 ? 152 VAL B CG1 1 ATOM 3798 C CG2 . VAL B 2 152 ? -18.627 14.014 -38.056 1.00 39.68 ? 152 VAL B CG2 1 ATOM 3799 N N . LYS B 2 153 ? -16.653 13.743 -34.023 1.00 42.05 ? 153 LYS B N 1 ATOM 3800 C CA . LYS B 2 153 ? -16.524 13.415 -32.599 1.00 43.41 ? 153 LYS B CA 1 ATOM 3801 C C . LYS B 2 153 ? -15.821 14.484 -31.762 1.00 44.52 ? 153 LYS B C 1 ATOM 3802 O O . LYS B 2 153 ? -15.961 14.499 -30.541 1.00 44.60 ? 153 LYS B O 1 ATOM 3803 C CB . LYS B 2 153 ? -15.797 12.079 -32.412 1.00 43.29 ? 153 LYS B CB 1 ATOM 3804 C CG . LYS B 2 153 ? -16.481 10.868 -33.022 1.00 43.37 ? 153 LYS B CG 1 ATOM 3805 C CD . LYS B 2 153 ? -15.815 9.608 -32.500 1.00 44.37 ? 153 LYS B CD 1 ATOM 3806 C CE . LYS B 2 153 ? -15.824 8.495 -33.522 1.00 45.37 ? 153 LYS B CE 1 ATOM 3807 N NZ . LYS B 2 153 ? -15.055 7.316 -33.020 1.00 44.90 ? 153 LYS B NZ 1 ATOM 3808 N N . ASN B 2 154 ? -15.058 15.360 -32.418 1.00 46.08 ? 154 ASN B N 1 ATOM 3809 C CA . ASN B 2 154 ? -14.391 16.474 -31.730 1.00 47.63 ? 154 ASN B CA 1 ATOM 3810 C C . ASN B 2 154 ? -14.798 17.845 -32.282 1.00 47.38 ? 154 ASN B C 1 ATOM 3811 O O . ASN B 2 154 ? -14.123 18.852 -32.042 1.00 47.76 ? 154 ASN B O 1 ATOM 3812 C CB . ASN B 2 154 ? -12.858 16.293 -31.712 1.00 48.30 ? 154 ASN B CB 1 ATOM 3813 C CG . ASN B 2 154 ? -12.204 16.558 -33.062 1.00 51.75 ? 154 ASN B CG 1 ATOM 3814 O OD1 . ASN B 2 154 ? -12.819 16.393 -34.120 1.00 52.16 ? 154 ASN B OD1 1 ATOM 3815 N ND2 . ASN B 2 154 ? -10.933 16.968 -33.022 1.00 57.37 ? 154 ASN B ND2 1 ATOM 3816 N N . GLY B 2 155 ? -15.902 17.862 -33.024 1.00 46.98 ? 155 GLY B N 1 ATOM 3817 C CA . GLY B 2 155 ? -16.476 19.092 -33.569 1.00 46.25 ? 155 GLY B CA 1 ATOM 3818 C C . GLY B 2 155 ? -15.635 19.855 -34.576 1.00 45.43 ? 155 GLY B C 1 ATOM 3819 O O . GLY B 2 155 ? -15.465 21.062 -34.443 1.00 45.63 ? 155 GLY B O 1 ATOM 3820 N N . THR B 2 156 ? -15.110 19.157 -35.583 1.00 44.66 ? 156 THR B N 1 ATOM 3821 C CA . THR B 2 156 ? -14.322 19.786 -36.654 1.00 43.89 ? 156 THR B CA 1 ATOM 3822 C C . THR B 2 156 ? -14.780 19.304 -38.037 1.00 43.39 ? 156 THR B C 1 ATOM 3823 O O . THR B 2 156 ? -14.057 19.431 -39.040 1.00 42.93 ? 156 THR B O 1 ATOM 3824 C CB . THR B 2 156 ? -12.806 19.532 -36.490 1.00 44.06 ? 156 THR B CB 1 ATOM 3825 O OG1 . THR B 2 156 ? -12.538 18.133 -36.623 1.00 44.36 ? 156 THR B OG1 1 ATOM 3826 C CG2 . THR B 2 156 ? -12.302 20.018 -35.130 1.00 43.65 ? 156 THR B CG2 1 ATOM 3827 N N . TYR B 2 157 ? -15.989 18.751 -38.078 1.00 42.66 ? 157 TYR B N 1 ATOM 3828 C CA . TYR B 2 157 ? -16.618 18.336 -39.325 1.00 42.37 ? 157 TYR B CA 1 ATOM 3829 C C . TYR B 2 157 ? -16.647 19.530 -40.271 1.00 43.27 ? 157 TYR B C 1 ATOM 3830 O O . TYR B 2 157 ? -17.031 20.630 -39.874 1.00 43.18 ? 157 TYR B O 1 ATOM 3831 C CB . TYR B 2 157 ? -18.042 17.841 -39.062 1.00 40.61 ? 157 TYR B CB 1 ATOM 3832 C CG . TYR B 2 157 ? -18.807 17.425 -40.302 1.00 38.82 ? 157 TYR B CG 1 ATOM 3833 C CD1 . TYR B 2 157 ? -18.577 16.197 -40.896 1.00 37.51 ? 157 TYR B CD1 1 ATOM 3834 C CD2 . TYR B 2 157 ? -19.783 18.251 -40.859 1.00 37.32 ? 157 TYR B CD2 1 ATOM 3835 C CE1 . TYR B 2 157 ? -19.276 15.800 -42.011 1.00 37.00 ? 157 TYR B CE1 1 ATOM 3836 C CE2 . TYR B 2 157 ? -20.494 17.864 -41.994 1.00 36.57 ? 157 TYR B CE2 1 ATOM 3837 C CZ . TYR B 2 157 ? -20.230 16.639 -42.561 1.00 37.11 ? 157 TYR B CZ 1 ATOM 3838 O OH . TYR B 2 157 ? -20.918 16.217 -43.658 1.00 36.40 ? 157 TYR B OH 1 ATOM 3839 N N . ASP B 2 158 ? -16.218 19.329 -41.512 1.00 44.77 ? 158 ASP B N 1 ATOM 3840 C CA . ASP B 2 158 ? -16.304 20.431 -42.448 1.00 46.11 ? 158 ASP B CA 1 ATOM 3841 C C . ASP B 2 158 ? -17.521 20.289 -43.345 1.00 46.67 ? 158 ASP B C 1 ATOM 3842 O O . ASP B 2 158 ? -17.517 19.550 -44.335 1.00 46.96 ? 158 ASP B O 1 ATOM 3843 C CB . ASP B 2 158 ? -14.994 20.664 -43.198 1.00 46.46 ? 158 ASP B CB 1 ATOM 3844 C CG . ASP B 2 158 ? -14.504 22.115 -43.078 1.00 48.21 ? 158 ASP B CG 1 ATOM 3845 O OD1 . ASP B 2 158 ? -15.341 23.052 -43.130 1.00 49.36 ? 158 ASP B OD1 1 ATOM 3846 O OD2 . ASP B 2 158 ? -13.278 22.321 -42.920 1.00 49.45 ? 158 ASP B OD2 1 ATOM 3847 N N . TYR B 2 159 ? -18.582 20.969 -42.923 1.00 47.85 ? 159 TYR B N 1 ATOM 3848 C CA . TYR B 2 159 ? -19.846 21.046 -43.639 1.00 49.12 ? 159 TYR B CA 1 ATOM 3849 C C . TYR B 2 159 ? -19.668 21.875 -44.907 1.00 49.73 ? 159 TYR B C 1 ATOM 3850 O O . TYR B 2 159 ? -20.011 21.394 -45.988 1.00 49.99 ? 159 TYR B O 1 ATOM 3851 C CB . TYR B 2 159 ? -20.939 21.638 -42.736 1.00 49.54 ? 159 TYR B CB 1 ATOM 3852 C CG . TYR B 2 159 ? -22.219 22.023 -43.443 1.00 50.13 ? 159 TYR B CG 1 ATOM 3853 C CD1 . TYR B 2 159 ? -23.127 21.049 -43.859 1.00 50.68 ? 159 TYR B CD1 1 ATOM 3854 C CD2 . TYR B 2 159 ? -22.533 23.363 -43.674 1.00 50.70 ? 159 TYR B CD2 1 ATOM 3855 C CE1 . TYR B 2 159 ? -24.310 21.394 -44.505 1.00 51.31 ? 159 TYR B CE1 1 ATOM 3856 C CE2 . TYR B 2 159 ? -23.714 23.724 -44.322 1.00 51.22 ? 159 TYR B CE2 1 ATOM 3857 C CZ . TYR B 2 159 ? -24.596 22.733 -44.733 1.00 50.99 ? 159 TYR B CZ 1 ATOM 3858 O OH . TYR B 2 159 ? -25.764 23.075 -45.365 1.00 50.29 ? 159 TYR B OH 1 ATOM 3859 N N . PRO B 2 160 ? -19.115 23.108 -44.786 1.00 50.32 ? 160 PRO B N 1 ATOM 3860 C CA . PRO B 2 160 ? -18.801 23.867 -45.997 1.00 50.81 ? 160 PRO B CA 1 ATOM 3861 C C . PRO B 2 160 ? -18.014 23.029 -46.993 1.00 51.20 ? 160 PRO B C 1 ATOM 3862 O O . PRO B 2 160 ? -18.091 23.279 -48.189 1.00 51.40 ? 160 PRO B O 1 ATOM 3863 C CB . PRO B 2 160 ? -17.933 25.011 -45.473 1.00 50.80 ? 160 PRO B CB 1 ATOM 3864 C CG . PRO B 2 160 ? -18.420 25.244 -44.100 1.00 50.71 ? 160 PRO B CG 1 ATOM 3865 C CD . PRO B 2 160 ? -18.760 23.872 -43.572 1.00 50.49 ? 160 PRO B CD 1 ATOM 3866 N N . LYS B 2 161 ? -17.289 22.032 -46.482 1.00 51.91 ? 161 LYS B N 1 ATOM 3867 C CA . LYS B 2 161 ? -16.491 21.103 -47.291 1.00 52.34 ? 161 LYS B CA 1 ATOM 3868 C C . LYS B 2 161 ? -17.331 20.050 -48.027 1.00 52.67 ? 161 LYS B C 1 ATOM 3869 O O . LYS B 2 161 ? -17.176 19.881 -49.238 1.00 52.73 ? 161 LYS B O 1 ATOM 3870 C CB . LYS B 2 161 ? -15.406 20.450 -46.422 1.00 52.37 ? 161 LYS B CB 1 ATOM 3871 C CG . LYS B 2 161 ? -14.561 19.380 -47.091 1.00 52.41 ? 161 LYS B CG 1 ATOM 3872 C CD . LYS B 2 161 ? -13.387 19.000 -46.192 1.00 52.33 ? 161 LYS B CD 1 ATOM 3873 C CE . LYS B 2 161 ? -12.467 17.978 -46.846 1.00 52.37 ? 161 LYS B CE 1 ATOM 3874 N NZ . LYS B 2 161 ? -13.089 16.626 -46.974 1.00 51.88 ? 161 LYS B NZ 1 ATOM 3875 N N . TYR B 2 162 ? -18.219 19.355 -47.308 1.00 53.19 ? 162 TYR B N 1 ATOM 3876 C CA . TYR B 2 162 ? -19.062 18.305 -47.916 1.00 53.24 ? 162 TYR B CA 1 ATOM 3877 C C . TYR B 2 162 ? -20.393 18.811 -48.488 1.00 53.17 ? 162 TYR B C 1 ATOM 3878 O O . TYR B 2 162 ? -21.184 18.021 -49.003 1.00 53.01 ? 162 TYR B O 1 ATOM 3879 C CB . TYR B 2 162 ? -19.327 17.164 -46.919 1.00 53.53 ? 162 TYR B CB 1 ATOM 3880 C CG . TYR B 2 162 ? -18.117 16.320 -46.570 1.00 53.59 ? 162 TYR B CG 1 ATOM 3881 C CD1 . TYR B 2 162 ? -17.786 15.189 -47.322 1.00 53.88 ? 162 TYR B CD1 1 ATOM 3882 C CD2 . TYR B 2 162 ? -17.310 16.646 -45.483 1.00 53.57 ? 162 TYR B CD2 1 ATOM 3883 C CE1 . TYR B 2 162 ? -16.669 14.407 -46.998 1.00 53.90 ? 162 TYR B CE1 1 ATOM 3884 C CE2 . TYR B 2 162 ? -16.200 15.878 -45.146 1.00 53.67 ? 162 TYR B CE2 1 ATOM 3885 C CZ . TYR B 2 162 ? -15.883 14.761 -45.903 1.00 54.01 ? 162 TYR B CZ 1 ATOM 3886 O OH . TYR B 2 162 ? -14.781 14.006 -45.558 1.00 53.83 ? 162 TYR B OH 1 ATOM 3887 N N . GLU B 2 163 ? -20.621 20.122 -48.402 1.00 53.55 ? 163 GLU B N 1 ATOM 3888 C CA . GLU B 2 163 ? -21.883 20.765 -48.809 1.00 53.93 ? 163 GLU B CA 1 ATOM 3889 C C . GLU B 2 163 ? -22.421 20.336 -50.186 1.00 54.26 ? 163 GLU B C 1 ATOM 3890 O O . GLU B 2 163 ? -23.589 19.950 -50.303 1.00 54.23 ? 163 GLU B O 1 ATOM 3891 C CB . GLU B 2 163 ? -21.738 22.292 -48.725 1.00 54.01 ? 163 GLU B CB 1 ATOM 3892 C CG . GLU B 2 163 ? -23.042 23.085 -48.831 1.00 54.14 ? 163 GLU B CG 1 ATOM 3893 C CD . GLU B 2 163 ? -22.914 24.528 -48.329 1.00 54.19 ? 163 GLU B CD 1 ATOM 3894 O OE1 . GLU B 2 163 ? -21.785 24.988 -48.033 1.00 54.08 ? 163 GLU B OE1 1 ATOM 3895 O OE2 . GLU B 2 163 ? -23.957 25.207 -48.227 1.00 54.17 ? 163 GLU B OE2 1 ATOM 3896 N N . GLU B 2 164 ? -21.566 20.386 -51.212 1.00 54.61 ? 164 GLU B N 1 ATOM 3897 C CA . GLU B 2 164 ? -21.967 20.076 -52.591 1.00 54.92 ? 164 GLU B CA 1 ATOM 3898 C C . GLU B 2 164 ? -22.105 18.578 -52.866 1.00 54.85 ? 164 GLU B C 1 ATOM 3899 O O . GLU B 2 164 ? -23.027 18.152 -53.570 1.00 54.67 ? 164 GLU B O 1 ATOM 3900 C CB . GLU B 2 164 ? -21.007 20.716 -53.613 1.00 55.24 ? 164 GLU B CB 1 ATOM 3901 C CG . GLU B 2 164 ? -21.100 22.244 -53.727 1.00 55.97 ? 164 GLU B CG 1 ATOM 3902 C CD . GLU B 2 164 ? -20.565 22.976 -52.499 1.00 57.06 ? 164 GLU B CD 1 ATOM 3903 O OE1 . GLU B 2 164 ? -21.096 24.061 -52.173 1.00 57.34 ? 164 GLU B OE1 1 ATOM 3904 O OE2 . GLU B 2 164 ? -19.620 22.468 -51.853 1.00 57.88 ? 164 GLU B OE2 1 ATOM 3905 N N . GLU B 2 165 ? -21.181 17.792 -52.315 1.00 54.91 ? 165 GLU B N 1 ATOM 3906 C CA . GLU B 2 165 ? -21.199 16.331 -52.442 1.00 54.86 ? 165 GLU B CA 1 ATOM 3907 C C . GLU B 2 165 ? -22.513 15.719 -51.943 1.00 55.26 ? 165 GLU B C 1 ATOM 3908 O O . GLU B 2 165 ? -23.044 14.778 -52.550 1.00 55.63 ? 165 GLU B O 1 ATOM 3909 C CB . GLU B 2 165 ? -20.011 15.731 -51.676 1.00 55.01 ? 165 GLU B CB 1 ATOM 3910 C CG . GLU B 2 165 ? -19.992 14.199 -51.606 1.00 54.30 ? 165 GLU B CG 1 ATOM 3911 C CD . GLU B 2 165 ? -18.730 13.638 -50.959 1.00 54.32 ? 165 GLU B CD 1 ATOM 3912 O OE1 . GLU B 2 165 ? -17.852 14.423 -50.520 1.00 52.89 ? 165 GLU B OE1 1 ATOM 3913 O OE2 . GLU B 2 165 ? -18.619 12.396 -50.894 1.00 52.84 ? 165 GLU B OE2 1 ATOM 3914 N N . SER B 2 166 ? -23.033 16.268 -50.845 1.00 55.17 ? 166 SER B N 1 ATOM 3915 C CA . SER B 2 166 ? -24.222 15.729 -50.188 1.00 55.08 ? 166 SER B CA 1 ATOM 3916 C C . SER B 2 166 ? -25.539 16.115 -50.859 1.00 55.20 ? 166 SER B C 1 ATOM 3917 O O . SER B 2 166 ? -26.429 15.273 -50.981 1.00 55.00 ? 166 SER B O 1 ATOM 3918 C CB . SER B 2 166 ? -24.238 16.116 -48.711 1.00 54.92 ? 166 SER B CB 1 ATOM 3919 O OG . SER B 2 166 ? -23.265 15.379 -47.995 1.00 54.57 ? 166 SER B OG 1 ATOM 3920 N N . LYS B 2 167 ? -25.657 17.372 -51.293 1.00 55.39 ? 167 LYS B N 1 ATOM 3921 C CA . LYS B 2 167 ? -26.860 17.843 -51.999 1.00 55.69 ? 167 LYS B CA 1 ATOM 3922 C C . LYS B 2 167 ? -27.158 17.037 -53.265 1.00 55.87 ? 167 LYS B C 1 ATOM 3923 O O . LYS B 2 167 ? -28.317 16.757 -53.567 1.00 55.58 ? 167 LYS B O 1 ATOM 3924 C CB . LYS B 2 167 ? -26.800 19.347 -52.309 1.00 55.62 ? 167 LYS B CB 1 ATOM 3925 C CG . LYS B 2 167 ? -25.589 19.795 -53.105 1.00 56.22 ? 167 LYS B CG 1 ATOM 3926 C CD . LYS B 2 167 ? -25.916 20.977 -54.019 1.00 56.69 ? 167 LYS B CD 1 ATOM 3927 C CE . LYS B 2 167 ? -24.649 21.595 -54.630 1.00 56.94 ? 167 LYS B CE 1 ATOM 3928 N NZ . LYS B 2 167 ? -23.855 20.652 -55.478 1.00 56.53 ? 167 LYS B NZ 1 ATOM 3929 N N . LEU B 2 168 ? -26.110 16.656 -53.993 1.00 56.22 ? 168 LEU B N 1 ATOM 3930 C CA . LEU B 2 168 ? -26.272 15.810 -55.170 1.00 56.68 ? 168 LEU B CA 1 ATOM 3931 C C . LEU B 2 168 ? -26.782 14.427 -54.767 1.00 56.88 ? 168 LEU B C 1 ATOM 3932 O O . LEU B 2 168 ? -27.743 13.923 -55.351 1.00 56.78 ? 168 LEU B O 1 ATOM 3933 C CB . LEU B 2 168 ? -24.966 15.732 -55.974 1.00 56.78 ? 168 LEU B CB 1 ATOM 3934 C CG . LEU B 2 168 ? -24.483 17.074 -56.555 1.00 57.10 ? 168 LEU B CG 1 ATOM 3935 C CD1 . LEU B 2 168 ? -22.983 17.059 -56.881 1.00 57.30 ? 168 LEU B CD1 1 ATOM 3936 C CD2 . LEU B 2 168 ? -25.315 17.505 -57.777 1.00 56.85 ? 168 LEU B CD2 1 ATOM 3937 N N . ASN B 2 169 ? -26.152 13.837 -53.751 1.00 57.19 ? 169 ASN B N 1 ATOM 3938 C CA . ASN B 2 169 ? -26.618 12.587 -53.146 1.00 57.37 ? 169 ASN B CA 1 ATOM 3939 C C . ASN B 2 169 ? -28.060 12.687 -52.646 1.00 57.49 ? 169 ASN B C 1 ATOM 3940 O O . ASN B 2 169 ? -28.878 11.789 -52.883 1.00 57.40 ? 169 ASN B O 1 ATOM 3941 C CB . ASN B 2 169 ? -25.710 12.201 -51.974 1.00 57.53 ? 169 ASN B CB 1 ATOM 3942 C CG . ASN B 2 169 ? -24.520 11.367 -52.400 1.00 57.81 ? 169 ASN B CG 1 ATOM 3943 O OD1 . ASN B 2 169 ? -24.673 10.215 -52.803 1.00 58.18 ? 169 ASN B OD1 1 ATOM 3944 N ND2 . ASN B 2 169 ? -23.322 11.937 -52.286 1.00 57.99 ? 169 ASN B ND2 1 ATOM 3945 N N . ARG B 2 170 ? -28.351 13.791 -51.957 1.00 57.57 ? 170 ARG B N 1 ATOM 3946 C CA . ARG B 2 170 ? -29.640 14.021 -51.317 1.00 57.66 ? 170 ARG B CA 1 ATOM 3947 C C . ARG B 2 170 ? -30.756 14.184 -52.342 1.00 58.20 ? 170 ARG B C 1 ATOM 3948 O O . ARG B 2 170 ? -31.895 13.801 -52.083 1.00 58.35 ? 170 ARG B O 1 ATOM 3949 C CB . ARG B 2 170 ? -29.560 15.246 -50.395 1.00 57.53 ? 170 ARG B CB 1 ATOM 3950 C CG . ARG B 2 170 ? -30.753 15.440 -49.466 1.00 57.07 ? 170 ARG B CG 1 ATOM 3951 C CD . ARG B 2 170 ? -30.515 16.555 -48.459 1.00 56.56 ? 170 ARG B CD 1 ATOM 3952 N NE . ARG B 2 170 ? -30.321 17.851 -49.106 1.00 54.65 ? 170 ARG B NE 1 ATOM 3953 C CZ . ARG B 2 170 ? -29.180 18.538 -49.118 1.00 53.51 ? 170 ARG B CZ 1 ATOM 3954 N NH1 . ARG B 2 170 ? -28.095 18.079 -48.502 1.00 52.12 ? 170 ARG B NH1 1 ATOM 3955 N NH2 . ARG B 2 170 ? -29.130 19.701 -49.747 1.00 53.44 ? 170 ARG B NH2 1 ATOM 3956 N N . ASN B 2 171 ? -30.421 14.731 -53.509 1.00 58.95 ? 171 ASN B N 1 ATOM 3957 C CA . ASN B 2 171 ? -31.415 14.986 -54.557 1.00 59.61 ? 171 ASN B CA 1 ATOM 3958 C C . ASN B 2 171 ? -31.544 13.900 -55.638 1.00 59.98 ? 171 ASN B C 1 ATOM 3959 O O . ASN B 2 171 ? -32.662 13.553 -56.021 1.00 60.08 ? 171 ASN B O 1 ATOM 3960 C CB . ASN B 2 171 ? -31.178 16.358 -55.204 1.00 59.67 ? 171 ASN B CB 1 ATOM 3961 C CG . ASN B 2 171 ? -31.175 17.494 -54.189 1.00 59.95 ? 171 ASN B CG 1 ATOM 3962 O OD1 . ASN B 2 171 ? -31.982 17.521 -53.256 1.00 60.83 ? 171 ASN B OD1 1 ATOM 3963 N ND2 . ASN B 2 171 ? -30.260 18.437 -54.368 1.00 59.92 ? 171 ASN B ND2 1 ATOM 3964 N N . GLU B 2 172 ? -30.412 13.374 -56.115 1.00 60.44 ? 172 GLU B N 1 ATOM 3965 C CA . GLU B 2 172 ? -30.376 12.445 -57.266 1.00 60.95 ? 172 GLU B CA 1 ATOM 3966 C C . GLU B 2 172 ? -31.390 11.300 -57.198 1.00 60.95 ? 172 GLU B C 1 ATOM 3967 O O . GLU B 2 172 ? -31.563 10.665 -56.158 1.00 61.15 ? 172 GLU B O 1 ATOM 3968 C CB . GLU B 2 172 ? -28.958 11.891 -57.499 1.00 60.92 ? 172 GLU B CB 1 ATOM 3969 C CG . GLU B 2 172 ? -28.397 11.042 -56.344 1.00 61.42 ? 172 GLU B CG 1 ATOM 3970 C CD . GLU B 2 172 ? -26.966 10.567 -56.568 1.00 61.43 ? 172 GLU B CD 1 ATOM 3971 O OE1 . GLU B 2 172 ? -26.336 10.965 -57.578 1.00 61.93 ? 172 GLU B OE1 1 ATOM 3972 O OE2 . GLU B 2 172 ? -26.471 9.787 -55.722 1.00 62.13 ? 172 GLU B OE2 1 HETATM 3973 C C1 . NAG C 3 . ? -5.617 27.509 51.133 1.00 26.36 ? 330 NAG A C1 1 HETATM 3974 C C2 . NAG C 3 . ? -5.592 28.777 52.024 1.00 28.94 ? 330 NAG A C2 1 HETATM 3975 C C3 . NAG C 3 . ? -5.184 29.992 51.202 1.00 32.05 ? 330 NAG A C3 1 HETATM 3976 C C4 . NAG C 3 . ? -3.928 29.657 50.398 1.00 34.39 ? 330 NAG A C4 1 HETATM 3977 C C5 . NAG C 3 . ? -3.980 28.311 49.635 1.00 30.24 ? 330 NAG A C5 1 HETATM 3978 C C6 . NAG C 3 . ? -2.655 27.901 48.988 1.00 32.19 ? 330 NAG A C6 1 HETATM 3979 C C7 . NAG C 3 . ? -6.949 29.389 53.969 1.00 28.93 ? 330 NAG A C7 1 HETATM 3980 C C8 . NAG C 3 . ? -8.343 29.553 54.505 1.00 29.00 ? 330 NAG A C8 1 HETATM 3981 N N2 . NAG C 3 . ? -6.855 29.062 52.684 1.00 27.08 ? 330 NAG A N2 1 HETATM 3982 O O3 . NAG C 3 . ? -4.880 31.089 52.067 1.00 31.10 ? 330 NAG A O3 1 HETATM 3983 O O4 . NAG C 3 . ? -3.506 30.815 49.690 1.00 41.86 ? 330 NAG A O4 1 HETATM 3984 O O5 . NAG C 3 . ? -4.312 27.305 50.568 1.00 28.46 ? 330 NAG A O5 1 HETATM 3985 O O6 . NAG C 3 . ? -1.683 27.712 49.996 1.00 31.46 ? 330 NAG A O6 1 HETATM 3986 O O7 . NAG C 3 . ? -5.972 29.592 54.714 1.00 30.85 ? 330 NAG A O7 1 HETATM 3987 C C1 . NAG D 3 . ? -4.038 31.379 48.458 1.00 48.51 ? 331 NAG A C1 1 HETATM 3988 C C2 . NAG D 3 . ? -3.061 31.014 47.326 1.00 51.41 ? 331 NAG A C2 1 HETATM 3989 C C3 . NAG D 3 . ? -3.499 31.488 45.945 1.00 51.62 ? 331 NAG A C3 1 HETATM 3990 C C4 . NAG D 3 . ? -5.017 31.500 45.744 1.00 53.05 ? 331 NAG A C4 1 HETATM 3991 C C5 . NAG D 3 . ? -5.763 32.028 46.982 1.00 53.02 ? 331 NAG A C5 1 HETATM 3992 C C6 . NAG D 3 . ? -7.286 32.042 46.794 1.00 53.83 ? 331 NAG A C6 1 HETATM 3993 C C7 . NAG D 3 . ? -1.216 31.964 48.751 1.00 53.98 ? 331 NAG A C7 1 HETATM 3994 C C8 . NAG D 3 . ? -0.604 33.333 48.627 1.00 53.59 ? 331 NAG A C8 1 HETATM 3995 N N2 . NAG D 3 . ? -1.682 31.415 47.611 1.00 52.21 ? 331 NAG A N2 1 HETATM 3996 O O3 . NAG D 3 . ? -2.923 30.593 45.025 1.00 52.47 ? 331 NAG A O3 1 HETATM 3997 O O4 . NAG D 3 . ? -5.338 32.273 44.601 1.00 53.48 ? 331 NAG A O4 1 HETATM 3998 O O5 . NAG D 3 . ? -5.416 31.232 48.111 1.00 52.10 ? 331 NAG A O5 1 HETATM 3999 O O6 . NAG D 3 . ? -7.663 32.592 45.545 1.00 54.91 ? 331 NAG A O6 1 HETATM 4000 O O7 . NAG D 3 . ? -1.254 31.410 49.861 1.00 53.69 ? 331 NAG A O7 1 HETATM 4001 C C1 . NAG E 3 . ? -36.990 -4.056 -7.888 1.00 56.03 ? 332 NAG A C1 1 HETATM 4002 C C2 . NAG E 3 . ? -37.951 -4.871 -7.003 1.00 61.36 ? 332 NAG A C2 1 HETATM 4003 C C3 . NAG E 3 . ? -38.462 -6.174 -7.635 1.00 61.87 ? 332 NAG A C3 1 HETATM 4004 C C4 . NAG E 3 . ? -37.443 -6.902 -8.527 1.00 62.26 ? 332 NAG A C4 1 HETATM 4005 C C5 . NAG E 3 . ? -36.447 -5.969 -9.227 1.00 61.70 ? 332 NAG A C5 1 HETATM 4006 C C6 . NAG E 3 . ? -36.254 -6.375 -10.689 1.00 62.38 ? 332 NAG A C6 1 HETATM 4007 C C7 . NAG E 3 . ? -37.689 -4.599 -4.578 1.00 64.10 ? 332 NAG A C7 1 HETATM 4008 C C8 . NAG E 3 . ? -36.849 -4.923 -3.374 1.00 64.46 ? 332 NAG A C8 1 HETATM 4009 N N2 . NAG E 3 . ? -37.329 -5.183 -5.723 1.00 63.05 ? 332 NAG A N2 1 HETATM 4010 O O3 . NAG E 3 . ? -39.628 -5.905 -8.384 1.00 62.94 ? 332 NAG A O3 1 HETATM 4011 O O4 . NAG E 3 . ? -36.732 -7.840 -7.749 1.00 63.31 ? 332 NAG A O4 1 HETATM 4012 O O5 . NAG E 3 . ? -36.888 -4.622 -9.180 1.00 59.79 ? 332 NAG A O5 1 HETATM 4013 O O6 . NAG E 3 . ? -35.759 -5.289 -11.449 1.00 62.26 ? 332 NAG A O6 1 HETATM 4014 O O7 . NAG E 3 . ? -38.647 -3.830 -4.478 1.00 65.39 ? 332 NAG A O7 1 HETATM 4015 C C1 . EDO F 4 . ? -9.236 13.641 59.936 1.00 27.13 ? 1 EDO A C1 1 HETATM 4016 O O1 . EDO F 4 . ? -8.278 13.923 58.891 1.00 24.69 ? 1 EDO A O1 1 HETATM 4017 C C2 . EDO F 4 . ? -9.904 14.930 60.431 1.00 29.11 ? 1 EDO A C2 1 HETATM 4018 O O2 . EDO F 4 . ? -8.970 15.953 60.811 1.00 29.25 ? 1 EDO A O2 1 HETATM 4019 C C1 . NAG G 3 . ? -10.228 16.820 -34.282 1.00 63.45 ? 175 NAG B C1 1 HETATM 4020 C C2 . NAG G 3 . ? -8.944 17.538 -33.848 1.00 66.96 ? 175 NAG B C2 1 HETATM 4021 C C3 . NAG G 3 . ? -7.851 17.396 -34.904 1.00 67.51 ? 175 NAG B C3 1 HETATM 4022 C C4 . NAG G 3 . ? -7.640 15.930 -35.280 1.00 67.61 ? 175 NAG B C4 1 HETATM 4023 C C5 . NAG G 3 . ? -8.969 15.237 -35.602 1.00 67.12 ? 175 NAG B C5 1 HETATM 4024 C C6 . NAG G 3 . ? -8.753 13.732 -35.729 1.00 67.83 ? 175 NAG B C6 1 HETATM 4025 C C7 . NAG G 3 . ? -9.022 19.429 -32.329 1.00 68.41 ? 175 NAG B C7 1 HETATM 4026 C C8 . NAG G 3 . ? -9.830 20.647 -31.979 1.00 68.33 ? 175 NAG B C8 1 HETATM 4027 N N2 . NAG G 3 . ? -9.182 18.945 -33.560 1.00 67.76 ? 175 NAG B N2 1 HETATM 4028 O O3 . NAG G 3 . ? -6.652 17.960 -34.412 1.00 68.53 ? 175 NAG B O3 1 HETATM 4029 O O4 . NAG G 3 . ? -6.764 15.846 -36.387 1.00 67.97 ? 175 NAG B O4 1 HETATM 4030 O O5 . NAG G 3 . ? -9.935 15.463 -34.581 1.00 65.48 ? 175 NAG B O5 1 HETATM 4031 O O6 . NAG G 3 . ? -8.879 13.322 -37.075 1.00 68.98 ? 175 NAG B O6 1 HETATM 4032 O O7 . NAG G 3 . ? -8.263 18.916 -31.505 1.00 68.86 ? 175 NAG B O7 1 HETATM 4033 C C1 . PEG H 5 . ? -28.950 1.352 -33.090 1.00 38.96 ? 176 PEG B C1 1 HETATM 4034 O O1 . PEG H 5 . ? -30.246 1.740 -32.637 1.00 40.18 ? 176 PEG B O1 1 HETATM 4035 C C2 . PEG H 5 . ? -27.818 2.263 -32.616 1.00 37.91 ? 176 PEG B C2 1 HETATM 4036 O O2 . PEG H 5 . ? -26.766 1.372 -32.250 1.00 39.45 ? 176 PEG B O2 1 HETATM 4037 C C3 . PEG H 5 . ? -25.424 1.761 -32.522 1.00 39.22 ? 176 PEG B C3 1 HETATM 4038 C C4 . PEG H 5 . ? -24.505 0.610 -32.112 1.00 42.47 ? 176 PEG B C4 1 HETATM 4039 O O4 . PEG H 5 . ? -25.131 -0.660 -32.360 1.00 44.29 ? 176 PEG B O4 1 HETATM 4040 O O . HOH I 6 . ? -9.305 3.181 33.905 1.00 16.71 ? 2 HOH A O 1 HETATM 4041 O O . HOH I 6 . ? -11.675 11.026 57.375 1.00 15.94 ? 4 HOH A O 1 HETATM 4042 O O . HOH I 6 . ? -28.932 14.543 39.879 1.00 17.72 ? 5 HOH A O 1 HETATM 4043 O O . HOH I 6 . ? -22.272 -4.849 47.212 1.00 21.29 ? 6 HOH A O 1 HETATM 4044 O O . HOH I 6 . ? -10.469 4.951 42.271 1.00 16.25 ? 8 HOH A O 1 HETATM 4045 O O . HOH I 6 . ? -8.768 9.584 27.904 1.00 37.22 ? 124 HOH A O 1 HETATM 4046 O O . HOH I 6 . ? -6.984 -3.218 33.029 1.00 33.15 ? 333 HOH A O 1 HETATM 4047 O O . HOH I 6 . ? -21.365 -1.779 36.145 1.00 18.31 ? 334 HOH A O 1 HETATM 4048 O O . HOH I 6 . ? -25.725 22.743 64.652 1.00 41.66 ? 335 HOH A O 1 HETATM 4049 O O . HOH I 6 . ? -23.846 -6.345 38.244 1.00 20.84 ? 336 HOH A O 1 HETATM 4050 O O . HOH I 6 . ? -7.592 -0.965 36.344 1.00 35.60 ? 337 HOH A O 1 HETATM 4051 O O . HOH I 6 . ? -4.694 0.121 20.582 1.00 40.37 ? 338 HOH A O 1 HETATM 4052 O O . HOH I 6 . ? -25.755 13.703 52.899 1.00 19.36 ? 339 HOH A O 1 HETATM 4053 O O . HOH I 6 . ? -1.355 8.374 54.779 1.00 43.65 ? 340 HOH A O 1 HETATM 4054 O O . HOH I 6 . ? -15.130 3.223 59.321 1.00 15.92 ? 341 HOH A O 1 HETATM 4055 O O . HOH I 6 . ? -31.134 19.654 57.619 1.00 39.05 ? 342 HOH A O 1 HETATM 4056 O O . HOH I 6 . ? -13.428 29.455 43.194 1.00 43.00 ? 343 HOH A O 1 HETATM 4057 O O . HOH I 6 . ? -25.262 3.861 38.793 1.00 17.54 ? 344 HOH A O 1 HETATM 4058 O O . HOH I 6 . ? -13.451 -0.498 46.706 1.00 19.90 ? 345 HOH A O 1 HETATM 4059 O O . HOH I 6 . ? -31.395 7.696 52.414 1.00 17.75 ? 346 HOH A O 1 HETATM 4060 O O . HOH I 6 . ? -26.434 11.883 33.913 1.00 19.98 ? 347 HOH A O 1 HETATM 4061 O O . HOH I 6 . ? -31.497 1.601 -3.031 1.00 44.81 ? 348 HOH A O 1 HETATM 4062 O O . HOH I 6 . ? -18.425 -2.648 32.953 1.00 20.28 ? 349 HOH A O 1 HETATM 4063 O O . HOH I 6 . ? -28.010 -1.494 15.026 1.00 44.80 ? 350 HOH A O 1 HETATM 4064 O O . HOH I 6 . ? -25.334 2.648 43.143 1.00 20.37 ? 351 HOH A O 1 HETATM 4065 O O . HOH I 6 . ? -20.237 22.112 65.624 1.00 37.21 ? 352 HOH A O 1 HETATM 4066 O O . HOH I 6 . ? -18.877 -8.149 34.130 1.00 50.57 ? 353 HOH A O 1 HETATM 4067 O O . HOH I 6 . ? -3.973 16.491 32.158 1.00 43.31 ? 354 HOH A O 1 HETATM 4068 O O . HOH I 6 . ? -8.010 24.992 36.168 1.00 54.87 ? 355 HOH A O 1 HETATM 4069 O O . HOH I 6 . ? -25.222 15.986 46.665 1.00 19.31 ? 356 HOH A O 1 HETATM 4070 O O . HOH I 6 . ? -16.869 -6.762 23.866 1.00 23.99 ? 357 HOH A O 1 HETATM 4071 O O . HOH I 6 . ? -22.631 -1.856 62.559 1.00 54.58 ? 358 HOH A O 1 HETATM 4072 O O . HOH I 6 . ? -7.140 32.986 52.915 1.00 43.99 ? 359 HOH A O 1 HETATM 4073 O O . HOH I 6 . ? -21.157 0.237 -10.994 1.00 42.52 ? 360 HOH A O 1 HETATM 4074 O O . HOH I 6 . ? -25.403 4.814 76.555 1.00 58.23 ? 361 HOH A O 1 HETATM 4075 O O . HOH I 6 . ? -17.495 24.142 38.874 1.00 38.45 ? 362 HOH A O 1 HETATM 4076 O O . HOH I 6 . ? -30.076 22.097 62.782 1.00 41.08 ? 363 HOH A O 1 HETATM 4077 O O . HOH I 6 . ? -0.249 21.374 49.534 1.00 47.89 ? 364 HOH A O 1 HETATM 4078 O O . HOH I 6 . ? -2.489 16.650 43.662 1.00 42.62 ? 365 HOH A O 1 HETATM 4079 O O . HOH I 6 . ? -18.221 -3.051 63.502 1.00 42.35 ? 366 HOH A O 1 HETATM 4080 O O . HOH I 6 . ? -20.955 -4.735 62.776 1.00 52.44 ? 367 HOH A O 1 HETATM 4081 O O . HOH I 6 . ? -22.392 0.587 3.485 1.00 50.48 ? 368 HOH A O 1 HETATM 4082 O O . HOH I 6 . ? -6.157 15.476 64.859 1.00 45.60 ? 369 HOH A O 1 HETATM 4083 O O . HOH I 6 . ? -34.014 15.402 58.836 1.00 47.07 ? 370 HOH A O 1 HETATM 4084 O O . HOH I 6 . ? -16.076 11.468 22.090 1.00 49.77 ? 371 HOH A O 1 HETATM 4085 O O . HOH I 6 . ? -24.042 -4.123 -9.222 1.00 54.90 ? 372 HOH A O 1 HETATM 4086 O O . HOH I 6 . ? -21.276 -8.310 52.226 1.00 41.37 ? 373 HOH A O 1 HETATM 4087 O O . HOH I 6 . ? -29.973 1.326 48.798 1.00 18.72 ? 374 HOH A O 1 HETATM 4088 O O . HOH I 6 . ? -8.492 2.939 31.341 1.00 18.99 ? 375 HOH A O 1 HETATM 4089 O O . HOH I 6 . ? -3.281 2.917 26.735 1.00 45.23 ? 376 HOH A O 1 HETATM 4090 O O . HOH I 6 . ? 2.191 15.863 61.654 1.00 40.16 ? 377 HOH A O 1 HETATM 4091 O O . HOH I 6 . ? -13.467 10.481 22.476 1.00 37.17 ? 378 HOH A O 1 HETATM 4092 O O . HOH I 6 . ? -20.850 12.330 73.712 1.00 37.44 ? 379 HOH A O 1 HETATM 4093 O O . HOH I 6 . ? -8.976 31.417 43.699 1.00 51.14 ? 380 HOH A O 1 HETATM 4094 O O . HOH I 6 . ? -12.131 13.271 24.197 1.00 50.30 ? 381 HOH A O 1 HETATM 4095 O O . HOH I 6 . ? -42.723 5.931 -11.154 1.00 48.04 ? 382 HOH A O 1 HETATM 4096 O O . HOH I 6 . ? -26.036 15.823 70.294 1.00 40.90 ? 383 HOH A O 1 HETATM 4097 O O . HOH I 6 . ? -35.368 4.297 52.506 1.00 20.66 ? 384 HOH A O 1 HETATM 4098 O O . HOH I 6 . ? -32.398 14.951 51.480 1.00 51.29 ? 385 HOH A O 1 HETATM 4099 O O . HOH I 6 . ? -20.349 1.684 69.231 1.00 48.17 ? 386 HOH A O 1 HETATM 4100 O O . HOH I 6 . ? -29.793 -5.955 34.652 1.00 40.69 ? 387 HOH A O 1 HETATM 4101 O O . HOH I 6 . ? -5.516 23.917 44.249 1.00 23.97 ? 388 HOH A O 1 HETATM 4102 O O . HOH I 6 . ? -28.610 20.889 64.693 1.00 47.23 ? 389 HOH A O 1 HETATM 4103 O O . HOH I 6 . ? -30.301 -1.336 39.594 1.00 54.44 ? 390 HOH A O 1 HETATM 4104 O O . HOH I 6 . ? -12.141 2.936 7.639 1.00 47.85 ? 391 HOH A O 1 HETATM 4105 O O . HOH I 6 . ? -11.080 -0.954 33.893 1.00 18.46 ? 392 HOH A O 1 HETATM 4106 O O . HOH I 6 . ? -15.670 25.256 46.237 1.00 21.20 ? 393 HOH A O 1 HETATM 4107 O O . HOH I 6 . ? -8.511 7.628 38.587 1.00 17.01 ? 394 HOH A O 1 HETATM 4108 O O . HOH I 6 . ? -20.400 9.790 62.882 1.00 17.74 ? 395 HOH A O 1 HETATM 4109 O O . HOH I 6 . ? -5.486 18.504 33.012 1.00 40.13 ? 396 HOH A O 1 HETATM 4110 O O . HOH I 6 . ? -19.065 -10.938 28.576 1.00 49.03 ? 397 HOH A O 1 HETATM 4111 O O . HOH I 6 . ? -11.329 29.142 45.799 1.00 45.91 ? 398 HOH A O 1 HETATM 4112 O O . HOH I 6 . ? -24.887 11.398 15.524 1.00 43.70 ? 399 HOH A O 1 HETATM 4113 O O . HOH I 6 . ? -4.330 21.166 52.159 1.00 24.20 ? 400 HOH A O 1 HETATM 4114 O O . HOH I 6 . ? -23.232 7.471 26.380 1.00 45.11 ? 401 HOH A O 1 HETATM 4115 O O . HOH I 6 . ? -11.171 4.748 55.083 1.00 23.69 ? 402 HOH A O 1 HETATM 4116 O O . HOH I 6 . ? -13.015 1.907 44.627 1.00 21.21 ? 403 HOH A O 1 HETATM 4117 O O . HOH I 6 . ? -30.177 7.555 45.489 1.00 22.34 ? 404 HOH A O 1 HETATM 4118 O O . HOH I 6 . ? -28.310 -2.852 -19.066 1.00 41.38 ? 405 HOH A O 1 HETATM 4119 O O . HOH I 6 . ? -13.645 -7.869 49.210 1.00 38.05 ? 406 HOH A O 1 HETATM 4120 O O . HOH I 6 . ? -11.483 4.249 44.910 1.00 19.29 ? 407 HOH A O 1 HETATM 4121 O O . HOH I 6 . ? -23.877 29.116 51.105 1.00 20.40 ? 408 HOH A O 1 HETATM 4122 O O . HOH I 6 . ? -17.464 18.352 72.006 1.00 38.24 ? 409 HOH A O 1 HETATM 4123 O O . HOH I 6 . ? -9.198 3.526 49.949 1.00 37.34 ? 410 HOH A O 1 HETATM 4124 O O . HOH I 6 . ? -22.115 31.068 50.364 1.00 21.18 ? 411 HOH A O 1 HETATM 4125 O O . HOH I 6 . ? -0.730 19.089 40.243 1.00 49.69 ? 412 HOH A O 1 HETATM 4126 O O . HOH I 6 . ? -29.749 -2.638 47.109 1.00 39.44 ? 413 HOH A O 1 HETATM 4127 O O . HOH I 6 . ? -12.280 3.256 70.223 1.00 46.37 ? 414 HOH A O 1 HETATM 4128 O O . HOH I 6 . ? -4.868 -0.014 44.180 1.00 51.35 ? 415 HOH A O 1 HETATM 4129 O O . HOH I 6 . ? -20.123 5.764 -7.968 1.00 48.16 ? 416 HOH A O 1 HETATM 4130 O O . HOH I 6 . ? -15.552 -8.129 38.394 1.00 47.32 ? 417 HOH A O 1 HETATM 4131 O O . HOH I 6 . ? -22.354 -8.039 63.414 1.00 50.68 ? 418 HOH A O 1 HETATM 4132 O O . HOH I 6 . ? -21.896 24.717 57.012 1.00 21.76 ? 419 HOH A O 1 HETATM 4133 O O . HOH I 6 . ? -21.589 21.339 68.999 1.00 50.73 ? 420 HOH A O 1 HETATM 4134 O O . HOH I 6 . ? -2.253 17.117 47.012 1.00 37.84 ? 421 HOH A O 1 HETATM 4135 O O . HOH I 6 . ? -17.964 12.242 16.175 1.00 44.22 ? 422 HOH A O 1 HETATM 4136 O O . HOH I 6 . ? -20.404 -11.930 55.755 1.00 49.19 ? 423 HOH A O 1 HETATM 4137 O O . HOH I 6 . ? -31.504 11.148 49.144 1.00 20.40 ? 424 HOH A O 1 HETATM 4138 O O . HOH I 6 . ? -9.294 -1.659 12.358 1.00 53.34 ? 425 HOH A O 1 HETATM 4139 O O . HOH I 6 . ? -12.018 -3.638 56.981 1.00 51.71 ? 426 HOH A O 1 HETATM 4140 O O . HOH I 6 . ? -31.969 13.077 64.867 1.00 45.06 ? 427 HOH A O 1 HETATM 4141 O O . HOH I 6 . ? -19.984 -4.916 49.901 1.00 22.76 ? 428 HOH A O 1 HETATM 4142 O O . HOH I 6 . ? -20.313 -4.205 31.615 1.00 21.29 ? 429 HOH A O 1 HETATM 4143 O O . HOH I 6 . ? -30.035 11.479 42.533 1.00 21.97 ? 430 HOH A O 1 HETATM 4144 O O . HOH I 6 . ? -29.624 -5.558 -23.376 1.00 67.58 ? 431 HOH A O 1 HETATM 4145 O O . HOH I 6 . ? -18.220 23.667 47.105 1.00 20.96 ? 432 HOH A O 1 HETATM 4146 O O . HOH I 6 . ? -3.313 7.417 33.791 1.00 21.81 ? 433 HOH A O 1 HETATM 4147 O O . HOH I 6 . ? -27.915 2.715 -19.858 1.00 30.59 ? 434 HOH A O 1 HETATM 4148 O O . HOH I 6 . ? -13.429 32.164 50.546 1.00 41.20 ? 435 HOH A O 1 HETATM 4149 O O . HOH I 6 . ? -19.926 24.711 66.054 1.00 43.51 ? 436 HOH A O 1 HETATM 4150 O O . HOH I 6 . ? -37.303 3.100 65.484 1.00 43.92 ? 437 HOH A O 1 HETATM 4151 O O . HOH I 6 . ? -9.353 28.175 51.558 1.00 24.14 ? 438 HOH A O 1 HETATM 4152 O O . HOH I 6 . ? -5.913 21.254 54.463 1.00 25.68 ? 439 HOH A O 1 HETATM 4153 O O . HOH I 6 . ? -5.435 -10.800 22.572 1.00 46.85 ? 440 HOH A O 1 HETATM 4154 O O . HOH I 6 . ? -9.364 2.358 52.935 1.00 23.88 ? 441 HOH A O 1 HETATM 4155 O O . HOH I 6 . ? -7.555 4.204 53.699 1.00 27.47 ? 442 HOH A O 1 HETATM 4156 O O . HOH I 6 . ? -10.185 15.164 65.243 1.00 48.50 ? 443 HOH A O 1 HETATM 4157 O O . HOH I 6 . ? -5.597 -0.200 38.088 1.00 39.23 ? 444 HOH A O 1 HETATM 4158 O O . HOH I 6 . ? -30.157 19.721 43.702 1.00 49.65 ? 445 HOH A O 1 HETATM 4159 O O . HOH I 6 . ? -5.042 1.919 45.936 1.00 40.35 ? 446 HOH A O 1 HETATM 4160 O O . HOH I 6 . ? -0.261 23.215 46.409 1.00 38.77 ? 447 HOH A O 1 HETATM 4161 O O . HOH I 6 . ? -17.503 26.523 44.692 1.00 46.05 ? 448 HOH A O 1 HETATM 4162 O O . HOH I 6 . ? -6.056 29.656 57.547 1.00 50.97 ? 449 HOH A O 1 HETATM 4163 O O . HOH I 6 . ? -17.384 9.494 9.023 1.00 51.46 ? 450 HOH A O 1 HETATM 4164 O O . HOH I 6 . ? -6.145 7.569 42.180 1.00 19.64 ? 451 HOH A O 1 HETATM 4165 O O . HOH I 6 . ? -23.511 -6.507 19.898 1.00 44.04 ? 452 HOH A O 1 HETATM 4166 O O . HOH I 6 . ? -32.410 10.470 46.385 1.00 51.28 ? 453 HOH A O 1 HETATM 4167 O O . HOH I 6 . ? -8.109 1.092 56.865 1.00 50.41 ? 454 HOH A O 1 HETATM 4168 O O . HOH I 6 . ? -11.509 -4.271 31.078 1.00 23.06 ? 455 HOH A O 1 HETATM 4169 O O . HOH I 6 . ? -22.632 -10.819 54.962 1.00 57.33 ? 456 HOH A O 1 HETATM 4170 O O . HOH I 6 . ? -23.474 -3.630 5.038 1.00 50.12 ? 457 HOH A O 1 HETATM 4171 O O . HOH I 6 . ? -1.598 9.644 56.848 1.00 53.75 ? 458 HOH A O 1 HETATM 4172 O O . HOH I 6 . ? -23.667 2.204 -42.121 1.00 54.07 ? 459 HOH A O 1 HETATM 4173 O O . HOH I 6 . ? -34.621 3.867 4.914 1.00 53.83 ? 460 HOH A O 1 HETATM 4174 O O . HOH I 6 . ? -32.055 -6.477 49.939 1.00 26.03 ? 461 HOH A O 1 HETATM 4175 O O . HOH I 6 . ? -6.096 11.320 24.823 1.00 53.44 ? 462 HOH A O 1 HETATM 4176 O O . HOH I 6 . ? -31.914 -6.781 -22.837 1.00 74.34 ? 463 HOH A O 1 HETATM 4177 O O . HOH I 6 . ? -6.294 4.862 61.920 1.00 47.45 ? 464 HOH A O 1 HETATM 4178 O O . HOH I 6 . ? -20.547 -14.306 57.353 1.00 43.84 ? 465 HOH A O 1 HETATM 4179 O O . HOH I 6 . ? -30.604 2.755 13.651 1.00 45.07 ? 466 HOH A O 1 HETATM 4180 O O . HOH I 6 . ? -20.716 -8.911 42.576 1.00 30.13 ? 467 HOH A O 1 HETATM 4181 O O . HOH I 6 . ? -2.781 7.956 27.197 1.00 42.73 ? 468 HOH A O 1 HETATM 4182 O O . HOH I 6 . ? -17.747 -6.310 41.953 1.00 20.41 ? 469 HOH A O 1 HETATM 4183 O O . HOH I 6 . ? -7.974 20.333 30.351 1.00 48.68 ? 470 HOH A O 1 HETATM 4184 O O . HOH I 6 . ? -8.517 14.710 26.551 1.00 51.09 ? 471 HOH A O 1 HETATM 4185 O O . HOH I 6 . ? -9.608 -5.962 30.082 1.00 43.99 ? 472 HOH A O 1 HETATM 4186 O O . HOH I 6 . ? -21.313 11.912 26.856 1.00 48.94 ? 473 HOH A O 1 HETATM 4187 O O . HOH I 6 . ? -19.527 23.553 58.037 1.00 28.50 ? 474 HOH A O 1 HETATM 4188 O O . HOH I 6 . ? -17.779 11.995 24.165 1.00 41.56 ? 475 HOH A O 1 HETATM 4189 O O . HOH I 6 . ? -18.783 23.299 67.991 1.00 55.52 ? 476 HOH A O 1 HETATM 4190 O O . HOH I 6 . ? -8.295 6.254 40.968 1.00 19.05 ? 477 HOH A O 1 HETATM 4191 O O . HOH I 6 . ? -19.956 16.958 31.913 1.00 26.99 ? 478 HOH A O 1 HETATM 4192 O O . HOH I 6 . ? -29.210 -2.346 -5.181 1.00 45.58 ? 479 HOH A O 1 HETATM 4193 O O . HOH I 6 . ? -22.192 -6.279 49.450 1.00 38.76 ? 480 HOH A O 1 HETATM 4194 O O . HOH I 6 . ? -10.345 1.793 13.543 1.00 47.87 ? 481 HOH A O 1 HETATM 4195 O O . HOH I 6 . ? -14.975 -6.904 34.355 1.00 40.67 ? 482 HOH A O 1 HETATM 4196 O O . HOH I 6 . ? -33.620 -3.023 34.428 1.00 61.81 ? 483 HOH A O 1 HETATM 4197 O O . HOH I 6 . ? -29.846 0.727 17.526 1.00 52.05 ? 484 HOH A O 1 HETATM 4198 O O . HOH I 6 . ? -29.960 16.874 40.869 1.00 24.97 ? 485 HOH A O 1 HETATM 4199 O O . HOH I 6 . ? -31.117 13.992 44.140 1.00 21.55 ? 486 HOH A O 1 HETATM 4200 O O . HOH I 6 . ? -4.862 4.621 30.555 1.00 25.31 ? 487 HOH A O 1 HETATM 4201 O O . HOH I 6 . ? -12.089 -13.764 61.367 1.00 46.66 ? 488 HOH A O 1 HETATM 4202 O O . HOH I 6 . ? -2.631 19.952 38.971 1.00 41.55 ? 489 HOH A O 1 HETATM 4203 O O . HOH I 6 . ? -8.274 26.131 55.325 1.00 25.96 ? 490 HOH A O 1 HETATM 4204 O O . HOH I 6 . ? -2.841 1.068 23.499 1.00 49.19 ? 491 HOH A O 1 HETATM 4205 O O . HOH I 6 . ? -20.457 17.337 29.025 1.00 47.72 ? 492 HOH A O 1 HETATM 4206 O O . HOH I 6 . ? -30.273 -5.129 47.846 1.00 38.67 ? 493 HOH A O 1 HETATM 4207 O O . HOH I 6 . ? -28.433 -0.811 48.180 1.00 26.56 ? 494 HOH A O 1 HETATM 4208 O O . HOH I 6 . ? -15.661 8.950 48.353 1.00 20.83 ? 495 HOH A O 1 HETATM 4209 O O . HOH I 6 . ? -26.218 -6.124 45.971 1.00 48.09 ? 496 HOH A O 1 HETATM 4210 O O . HOH I 6 . ? -25.981 -0.512 42.121 1.00 41.27 ? 497 HOH A O 1 HETATM 4211 O O . HOH I 6 . ? -8.972 0.654 34.678 1.00 19.46 ? 498 HOH A O 1 HETATM 4212 O O . HOH I 6 . ? -27.217 -5.218 34.659 1.00 23.64 ? 499 HOH A O 1 HETATM 4213 O O . HOH I 6 . ? -20.434 11.178 22.474 1.00 42.23 ? 500 HOH A O 1 HETATM 4214 O O . HOH I 6 . ? -31.380 13.580 39.702 1.00 23.67 ? 501 HOH A O 1 HETATM 4215 O O . HOH I 6 . ? -4.132 17.558 36.566 1.00 45.37 ? 502 HOH A O 1 HETATM 4216 O O . HOH I 6 . ? -15.026 3.047 4.550 1.00 58.81 ? 503 HOH A O 1 HETATM 4217 O O . HOH I 6 . ? -20.204 -4.355 -16.772 1.00 57.51 ? 504 HOH A O 1 HETATM 4218 O O . HOH I 6 . ? -18.267 14.151 26.878 1.00 52.92 ? 505 HOH A O 1 HETATM 4219 O O . HOH I 6 . ? -3.846 6.526 38.044 1.00 22.98 ? 506 HOH A O 1 HETATM 4220 O O . HOH I 6 . ? -18.278 -6.023 32.553 1.00 26.34 ? 507 HOH A O 1 HETATM 4221 O O . HOH I 6 . ? -16.756 -5.909 64.002 1.00 53.94 ? 508 HOH A O 1 HETATM 4222 O O . HOH I 6 . ? -37.944 1.206 -11.471 1.00 50.59 ? 509 HOH A O 1 HETATM 4223 O O . HOH I 6 . ? -28.314 2.671 36.277 1.00 53.38 ? 510 HOH A O 1 HETATM 4224 O O . HOH I 6 . ? -13.399 3.162 57.031 1.00 28.73 ? 511 HOH A O 1 HETATM 4225 O O . HOH I 6 . ? -8.504 2.541 14.912 1.00 48.26 ? 512 HOH A O 1 HETATM 4226 O O . HOH I 6 . ? -4.071 3.726 38.681 1.00 26.62 ? 513 HOH A O 1 HETATM 4227 O O . HOH I 6 . ? -27.636 27.915 53.198 1.00 21.99 ? 515 HOH A O 1 HETATM 4228 O O . HOH I 6 . ? -18.346 -11.947 53.952 1.00 31.76 ? 516 HOH A O 1 HETATM 4229 O O . HOH I 6 . ? -27.995 5.830 -31.020 1.00 28.07 ? 517 HOH A O 1 HETATM 4230 O O . HOH I 6 . ? -8.645 6.197 63.388 1.00 48.21 ? 518 HOH A O 1 HETATM 4231 O O . HOH I 6 . ? -11.627 25.091 60.024 1.00 42.87 ? 519 HOH A O 1 HETATM 4232 O O . HOH I 6 . ? -19.938 -11.164 60.969 1.00 49.47 ? 520 HOH A O 1 HETATM 4233 O O . HOH I 6 . ? -4.736 29.044 40.616 1.00 54.18 ? 522 HOH A O 1 HETATM 4234 O O . HOH I 6 . ? -3.639 17.909 49.181 1.00 24.98 ? 523 HOH A O 1 HETATM 4235 O O . HOH I 6 . ? -3.363 -4.835 22.981 1.00 60.02 ? 524 HOH A O 1 HETATM 4236 O O . HOH I 6 . ? -28.845 -0.689 29.432 1.00 52.14 ? 525 HOH A O 1 HETATM 4237 O O . HOH I 6 . ? -12.821 9.838 25.016 1.00 25.41 ? 526 HOH A O 1 HETATM 4238 O O . HOH I 6 . ? -5.603 26.378 54.968 1.00 27.32 ? 527 HOH A O 1 HETATM 4239 O O . HOH I 6 . ? -15.916 -8.741 49.876 1.00 51.75 ? 528 HOH A O 1 HETATM 4240 O O . HOH I 6 . ? -32.316 2.907 45.529 1.00 51.26 ? 529 HOH A O 1 HETATM 4241 O O . HOH I 6 . ? 0.033 9.690 33.821 1.00 36.24 ? 531 HOH A O 1 HETATM 4242 O O . HOH I 6 . ? -24.841 -5.100 6.823 1.00 56.85 ? 532 HOH A O 1 HETATM 4243 O O . HOH I 6 . ? -17.676 28.480 42.758 1.00 51.79 ? 533 HOH A O 1 HETATM 4244 O O . HOH I 6 . ? -27.318 2.342 2.134 1.00 28.04 ? 534 HOH A O 1 HETATM 4245 O O . HOH I 6 . ? -24.764 -3.134 60.218 1.00 25.31 ? 535 HOH A O 1 HETATM 4246 O O . HOH I 6 . ? -1.393 25.440 40.985 1.00 59.29 ? 536 HOH A O 1 HETATM 4247 O O . HOH I 6 . ? -35.211 10.995 64.420 1.00 26.57 ? 537 HOH A O 1 HETATM 4248 O O . HOH I 6 . ? -1.024 10.891 54.135 1.00 36.05 ? 538 HOH A O 1 HETATM 4249 O O . HOH I 6 . ? -11.561 -10.386 21.381 1.00 62.04 ? 539 HOH A O 1 HETATM 4250 O O . HOH I 6 . ? -7.012 0.690 31.809 1.00 23.54 ? 540 HOH A O 1 HETATM 4251 O O . HOH I 6 . ? -9.270 -6.923 27.555 1.00 46.80 ? 541 HOH A O 1 HETATM 4252 O O . HOH I 6 . ? -2.078 11.966 37.022 1.00 43.83 ? 542 HOH A O 1 HETATM 4253 O O . HOH I 6 . ? -30.935 9.584 44.285 1.00 46.94 ? 543 HOH A O 1 HETATM 4254 O O . HOH I 6 . ? -22.530 -10.173 36.884 1.00 65.15 ? 544 HOH A O 1 HETATM 4255 O O . HOH I 6 . ? -17.667 -9.031 64.044 1.00 55.36 ? 545 HOH A O 1 HETATM 4256 O O . HOH I 6 . ? 0.788 17.083 63.414 1.00 58.78 ? 546 HOH A O 1 HETATM 4257 O O . HOH I 6 . ? -11.629 -11.057 51.128 1.00 26.49 ? 547 HOH A O 1 HETATM 4258 O O . HOH I 6 . ? -38.687 -3.719 61.518 1.00 52.19 ? 549 HOH A O 1 HETATM 4259 O O . HOH I 6 . ? -32.212 1.635 11.056 1.00 59.44 ? 550 HOH A O 1 HETATM 4260 O O . HOH I 6 . ? -1.523 14.254 46.370 1.00 44.87 ? 551 HOH A O 1 HETATM 4261 O O . HOH I 6 . ? -25.352 26.979 49.867 1.00 26.38 ? 552 HOH A O 1 HETATM 4262 O O . HOH I 6 . ? -6.527 11.113 71.372 1.00 58.02 ? 553 HOH A O 1 HETATM 4263 O O . HOH I 6 . ? -8.167 28.759 58.766 1.00 46.54 ? 554 HOH A O 1 HETATM 4264 O O . HOH I 6 . ? -16.256 23.561 35.492 1.00 48.89 ? 555 HOH A O 1 HETATM 4265 O O . HOH I 6 . ? -5.948 5.489 44.193 1.00 27.10 ? 556 HOH A O 1 HETATM 4266 O O . HOH I 6 . ? -6.358 15.996 58.436 1.00 29.29 ? 557 HOH A O 1 HETATM 4267 O O . HOH I 6 . ? -27.603 11.440 -6.985 1.00 27.84 ? 558 HOH A O 1 HETATM 4268 O O . HOH I 6 . ? -11.571 12.718 66.364 1.00 29.27 ? 560 HOH A O 1 HETATM 4269 O O . HOH I 6 . ? -6.575 20.459 57.313 1.00 45.45 ? 561 HOH A O 1 HETATM 4270 O O . HOH I 6 . ? -3.233 23.540 53.233 1.00 28.80 ? 562 HOH A O 1 HETATM 4271 O O . HOH I 6 . ? -2.817 8.010 49.253 1.00 53.31 ? 563 HOH A O 1 HETATM 4272 O O . HOH I 6 . ? -24.565 12.733 75.126 1.00 40.79 ? 564 HOH A O 1 HETATM 4273 O O . HOH I 6 . ? -2.354 -3.908 20.466 1.00 46.60 ? 565 HOH A O 1 HETATM 4274 O O . HOH I 6 . ? -24.036 -2.939 25.123 1.00 43.18 ? 566 HOH A O 1 HETATM 4275 O O . HOH I 6 . ? -19.715 32.676 48.413 1.00 25.72 ? 567 HOH A O 1 HETATM 4276 O O . HOH I 6 . ? -2.980 27.920 54.694 1.00 43.13 ? 568 HOH A O 1 HETATM 4277 O O . HOH I 6 . ? -26.051 -8.984 55.007 1.00 54.39 ? 569 HOH A O 1 HETATM 4278 O O . HOH I 6 . ? -11.497 25.613 40.876 1.00 27.51 ? 570 HOH A O 1 HETATM 4279 O O . HOH I 6 . ? -3.189 10.660 64.827 1.00 64.33 ? 571 HOH A O 1 HETATM 4280 O O . HOH I 6 . ? -32.755 5.077 16.960 1.00 55.60 ? 572 HOH A O 1 HETATM 4281 O O . HOH I 6 . ? -26.701 14.817 73.089 1.00 61.26 ? 573 HOH A O 1 HETATM 4282 O O . HOH I 6 . ? -27.272 12.372 74.606 1.00 51.36 ? 574 HOH A O 1 HETATM 4283 O O . HOH I 6 . ? -4.534 -2.755 39.588 1.00 51.29 ? 575 HOH A O 1 HETATM 4284 O O . HOH I 6 . ? -24.964 3.882 26.697 1.00 29.28 ? 576 HOH A O 1 HETATM 4285 O O . HOH I 6 . ? -22.303 -8.494 45.768 1.00 28.63 ? 577 HOH A O 1 HETATM 4286 O O . HOH I 6 . ? -37.284 -2.516 63.815 1.00 49.29 ? 578 HOH A O 1 HETATM 4287 O O . HOH I 6 . ? -26.093 -7.010 36.699 1.00 28.34 ? 579 HOH A O 1 HETATM 4288 O O . HOH I 6 . ? -26.099 -1.375 25.585 1.00 50.17 ? 580 HOH A O 1 HETATM 4289 O O . HOH I 6 . ? -34.941 1.369 69.848 1.00 42.49 ? 582 HOH A O 1 HETATM 4290 O O . HOH I 6 . ? -3.747 12.132 34.807 1.00 34.68 ? 584 HOH A O 1 HETATM 4291 O O . HOH I 6 . ? -2.880 11.176 49.288 1.00 28.54 ? 585 HOH A O 1 HETATM 4292 O O . HOH I 6 . ? -15.466 -11.772 51.444 1.00 25.15 ? 587 HOH A O 1 HETATM 4293 O O . HOH I 6 . ? -26.779 0.918 45.070 1.00 21.82 ? 588 HOH A O 1 HETATM 4294 O O . HOH I 6 . ? -34.386 14.826 61.398 1.00 45.59 ? 589 HOH A O 1 HETATM 4295 O O . HOH I 6 . ? -33.265 8.922 -17.177 1.00 27.98 ? 590 HOH A O 1 HETATM 4296 O O . HOH I 6 . ? -5.283 6.039 56.303 1.00 30.31 ? 591 HOH A O 1 HETATM 4297 O O . HOH I 6 . ? -20.520 21.152 43.197 1.00 28.51 ? 592 HOH A O 1 HETATM 4298 O O . HOH I 6 . ? -26.157 -0.496 61.080 1.00 31.38 ? 593 HOH A O 1 HETATM 4299 O O . HOH I 6 . ? -32.190 14.612 57.113 1.00 53.66 ? 594 HOH A O 1 HETATM 4300 O O . HOH I 6 . ? -22.709 8.884 15.843 1.00 31.28 ? 595 HOH A O 1 HETATM 4301 O O . HOH I 6 . ? -18.721 -8.890 26.170 1.00 31.31 ? 596 HOH A O 1 HETATM 4302 O O . HOH I 6 . ? -4.004 -5.758 19.870 1.00 66.01 ? 597 HOH A O 1 HETATM 4303 O O . HOH I 6 . ? -29.632 13.962 75.924 1.00 62.39 ? 598 HOH A O 1 HETATM 4304 O O . HOH I 6 . ? -7.934 -4.792 27.176 1.00 49.19 ? 599 HOH A O 1 HETATM 4305 O O . HOH I 6 . ? -20.721 14.268 25.950 1.00 65.92 ? 600 HOH A O 1 HETATM 4306 O O . HOH I 6 . ? -41.880 -4.839 -8.648 1.00 59.96 ? 601 HOH A O 1 HETATM 4307 O O . HOH I 6 . ? -1.871 9.203 39.852 1.00 46.25 ? 602 HOH A O 1 HETATM 4308 O O . HOH I 6 . ? -26.493 1.908 25.630 1.00 52.27 ? 603 HOH A O 1 HETATM 4309 O O . HOH I 6 . ? -17.759 -11.567 62.472 1.00 57.48 ? 604 HOH A O 1 HETATM 4310 O O . HOH I 6 . ? -16.447 -16.416 56.859 1.00 36.45 ? 605 HOH A O 1 HETATM 4311 O O . HOH I 6 . ? -20.819 -8.393 24.629 1.00 54.57 ? 606 HOH A O 1 HETATM 4312 O O . HOH I 6 . ? -6.560 -3.839 47.524 1.00 48.04 ? 607 HOH A O 1 HETATM 4313 O O . HOH I 6 . ? -27.834 -0.519 40.512 1.00 48.56 ? 608 HOH A O 1 HETATM 4314 O O . HOH I 6 . ? -13.846 18.869 29.459 1.00 55.68 ? 609 HOH A O 1 HETATM 4315 O O . HOH I 6 . ? -24.485 20.713 46.507 1.00 44.03 ? 610 HOH A O 1 HETATM 4316 O O . HOH I 6 . ? -3.001 30.470 53.921 1.00 48.48 ? 611 HOH A O 1 HETATM 4317 O O . HOH I 6 . ? -7.297 35.570 45.003 1.00 57.75 ? 612 HOH A O 1 HETATM 4318 O O . HOH I 6 . ? 0.001 -0.002 36.261 0.33 26.04 ? 613 HOH A O 1 HETATM 4319 O O . HOH I 6 . ? -26.175 18.158 68.309 1.00 35.98 ? 614 HOH A O 1 HETATM 4320 O O . HOH I 6 . ? -22.801 17.914 36.740 1.00 32.56 ? 615 HOH A O 1 HETATM 4321 O O . HOH I 6 . ? -8.323 -3.784 49.542 1.00 28.20 ? 616 HOH A O 1 HETATM 4322 O O . HOH I 6 . ? -28.680 5.352 44.504 1.00 37.67 ? 617 HOH A O 1 HETATM 4323 O O . HOH I 6 . ? -4.328 1.719 30.970 1.00 29.94 ? 618 HOH A O 1 HETATM 4324 O O . HOH I 6 . ? -38.379 -5.650 55.701 1.00 30.01 ? 619 HOH A O 1 HETATM 4325 O O . HOH I 6 . ? -32.840 -7.554 53.469 1.00 32.17 ? 620 HOH A O 1 HETATM 4326 O O . HOH I 6 . ? -24.454 -2.807 46.938 1.00 26.65 ? 621 HOH A O 1 HETATM 4327 O O . HOH I 6 . ? -32.444 5.329 47.238 1.00 36.36 ? 622 HOH A O 1 HETATM 4328 O O . HOH I 6 . ? -29.902 -1.021 61.320 1.00 30.86 ? 623 HOH A O 1 HETATM 4329 O O . HOH I 6 . ? -11.439 -3.045 35.743 1.00 28.82 ? 624 HOH A O 1 HETATM 4330 O O . HOH I 6 . ? -12.595 3.234 13.895 1.00 30.64 ? 625 HOH A O 1 HETATM 4331 O O . HOH I 6 . ? -6.653 -0.519 41.993 1.00 32.86 ? 626 HOH A O 1 HETATM 4332 O O . HOH I 6 . ? -37.144 9.742 -11.520 1.00 32.03 ? 627 HOH A O 1 HETATM 4333 O O . HOH I 6 . ? -15.246 -2.017 13.410 1.00 34.54 ? 628 HOH A O 1 HETATM 4334 O O . HOH I 6 . ? -13.517 15.531 68.654 1.00 41.50 ? 629 HOH A O 1 HETATM 4335 O O . HOH I 6 . ? -21.977 21.760 45.601 1.00 29.80 ? 630 HOH A O 1 HETATM 4336 O O . HOH I 6 . ? -8.490 -4.019 16.727 1.00 41.31 ? 631 HOH A O 1 HETATM 4337 O O . HOH I 6 . ? -7.806 -1.693 30.600 1.00 25.05 ? 632 HOH A O 1 HETATM 4338 O O . HOH I 6 . ? -36.560 -2.336 59.989 1.00 33.31 ? 633 HOH A O 1 HETATM 4339 O O . HOH I 6 . ? -26.609 -7.089 56.678 1.00 30.35 ? 634 HOH A O 1 HETATM 4340 O O . HOH I 6 . ? -23.041 4.996 25.093 1.00 37.48 ? 635 HOH A O 1 HETATM 4341 O O . HOH I 6 . ? -10.446 -1.644 31.232 1.00 25.30 ? 636 HOH A O 1 HETATM 4342 O O . HOH I 6 . ? -22.998 -5.380 61.255 1.00 35.41 ? 637 HOH A O 1 HETATM 4343 O O . HOH I 6 . ? -18.720 -15.735 55.655 1.00 31.86 ? 638 HOH A O 1 HETATM 4344 O O . HOH I 6 . ? -28.995 22.736 55.071 1.00 34.57 ? 639 HOH A O 1 HETATM 4345 O O . HOH I 6 . ? -29.955 12.343 66.152 1.00 36.51 ? 640 HOH A O 1 HETATM 4346 O O . HOH I 6 . ? -12.374 -6.012 43.227 1.00 28.98 ? 641 HOH A O 1 HETATM 4347 O O . HOH I 6 . ? -17.898 -0.272 10.831 1.00 31.29 ? 642 HOH A O 1 HETATM 4348 O O . HOH I 6 . ? -8.384 -3.692 24.856 1.00 34.59 ? 643 HOH A O 1 HETATM 4349 O O . HOH I 6 . ? -17.838 2.880 68.682 1.00 33.46 ? 644 HOH A O 1 HETATM 4350 O O . HOH I 6 . ? -13.173 -6.689 45.713 1.00 26.09 ? 645 HOH A O 1 HETATM 4351 O O . HOH I 6 . ? -16.332 3.592 63.966 1.00 28.97 ? 646 HOH A O 1 HETATM 4352 O O . HOH I 6 . ? -13.726 9.620 49.795 1.00 33.85 ? 647 HOH A O 1 HETATM 4353 O O . HOH I 6 . ? -8.941 8.288 22.937 1.00 30.63 ? 648 HOH A O 1 HETATM 4354 O O . HOH I 6 . ? -10.129 -9.978 23.479 1.00 36.63 ? 649 HOH A O 1 HETATM 4355 O O . HOH I 6 . ? -22.710 -1.097 5.544 1.00 40.62 ? 650 HOH A O 1 HETATM 4356 O O . HOH I 6 . ? -32.077 -2.583 60.917 1.00 25.78 ? 651 HOH A O 1 HETATM 4357 O O . HOH I 6 . ? -11.517 29.503 51.132 1.00 36.48 ? 652 HOH A O 1 HETATM 4358 O O . HOH I 6 . ? -26.074 5.373 43.979 1.00 31.80 ? 653 HOH A O 1 HETATM 4359 O O . HOH I 6 . ? -12.458 -8.082 29.408 1.00 36.76 ? 654 HOH A O 1 HETATM 4360 O O . HOH I 6 . ? -24.160 18.772 48.255 1.00 27.98 ? 655 HOH A O 1 HETATM 4361 O O . HOH I 6 . ? -12.402 27.317 57.679 1.00 34.51 ? 656 HOH A O 1 HETATM 4362 O O . HOH I 6 . ? -8.950 18.482 59.779 1.00 31.31 ? 657 HOH A O 1 HETATM 4363 O O . HOH I 6 . ? -16.057 21.051 36.566 1.00 38.55 ? 658 HOH A O 1 HETATM 4364 O O . HOH I 6 . ? -11.479 8.615 18.215 1.00 37.64 ? 659 HOH A O 1 HETATM 4365 O O . HOH I 6 . ? -7.207 17.859 31.015 1.00 35.65 ? 660 HOH A O 1 HETATM 4366 O O . HOH I 6 . ? -7.875 30.499 49.223 1.00 31.79 ? 661 HOH A O 1 HETATM 4367 O O . HOH I 6 . ? -8.028 1.242 50.689 1.00 31.15 ? 662 HOH A O 1 HETATM 4368 O O . HOH I 6 . ? -7.119 3.340 48.301 1.00 31.13 ? 663 HOH A O 1 HETATM 4369 O O . HOH I 6 . ? -9.905 9.274 25.002 1.00 35.43 ? 664 HOH A O 1 HETATM 4370 O O . HOH I 6 . ? -11.413 21.725 61.420 1.00 42.47 ? 665 HOH A O 1 HETATM 4371 O O . HOH I 6 . ? -2.000 6.822 36.160 1.00 29.19 ? 666 HOH A O 1 HETATM 4372 O O . HOH I 6 . ? -27.798 26.508 50.682 1.00 33.37 ? 667 HOH A O 1 HETATM 4373 O O . HOH I 6 . ? -13.985 10.434 72.635 1.00 36.17 ? 668 HOH A O 1 HETATM 4374 O O . HOH I 6 . ? -37.721 -8.189 56.521 1.00 40.34 ? 669 HOH A O 1 HETATM 4375 O O . HOH I 6 . ? -9.837 -7.258 47.580 1.00 41.04 ? 670 HOH A O 1 HETATM 4376 O O . HOH I 6 . ? -2.660 9.958 33.238 1.00 31.59 ? 671 HOH A O 1 HETATM 4377 O O . HOH I 6 . ? -2.327 1.305 32.693 1.00 32.32 ? 672 HOH A O 1 HETATM 4378 O O . HOH I 6 . ? -16.041 9.404 31.556 1.00 30.66 ? 673 HOH A O 1 HETATM 4379 O O . HOH I 6 . ? -15.095 -1.242 58.944 1.00 34.32 ? 674 HOH A O 1 HETATM 4380 O O . HOH I 6 . ? -14.532 18.674 32.707 1.00 32.00 ? 675 HOH A O 1 HETATM 4381 O O . HOH I 6 . ? -2.288 25.849 52.618 1.00 36.61 ? 676 HOH A O 1 HETATM 4382 O O . HOH I 6 . ? -4.503 8.210 40.051 1.00 30.65 ? 677 HOH A O 1 HETATM 4383 O O . HOH I 6 . ? -16.111 -10.953 47.594 1.00 27.79 ? 678 HOH A O 1 HETATM 4384 O O . HOH I 6 . ? -22.547 20.007 30.736 1.00 32.51 ? 679 HOH A O 1 HETATM 4385 O O . HOH I 6 . ? -13.196 1.463 55.348 1.00 32.52 ? 680 HOH A O 1 HETATM 4386 O O . HOH I 6 . ? -2.160 1.267 35.404 1.00 35.25 ? 681 HOH A O 1 HETATM 4387 O O . HOH I 6 . ? -24.943 -5.105 26.748 1.00 33.74 ? 682 HOH A O 1 HETATM 4388 O O . HOH I 6 . ? -8.156 -1.457 50.894 1.00 39.11 ? 683 HOH A O 1 HETATM 4389 O O . HOH I 6 . ? -37.545 -5.705 53.131 1.00 37.21 ? 684 HOH A O 1 HETATM 4390 O O . HOH I 6 . ? -31.585 6.191 -0.441 1.00 36.76 ? 685 HOH A O 1 HETATM 4391 O O . HOH I 6 . ? -23.944 19.271 39.150 1.00 27.88 ? 686 HOH A O 1 HETATM 4392 O O . HOH I 6 . ? -10.987 -4.966 33.764 1.00 30.96 ? 687 HOH A O 1 HETATM 4393 O O . HOH I 6 . ? -23.981 18.463 44.603 1.00 33.20 ? 688 HOH A O 1 HETATM 4394 O O . HOH I 6 . ? -29.091 15.951 53.192 1.00 35.46 ? 689 HOH A O 1 HETATM 4395 O O . HOH I 6 . ? -27.343 -1.222 68.950 1.00 44.23 ? 690 HOH A O 1 HETATM 4396 O O . HOH I 6 . ? -7.091 17.710 56.529 1.00 32.97 ? 691 HOH A O 1 HETATM 4397 O O . HOH I 6 . ? -11.641 1.345 59.141 1.00 38.72 ? 692 HOH A O 1 HETATM 4398 O O . HOH I 6 . ? -13.030 -0.153 14.775 1.00 35.70 ? 693 HOH A O 1 HETATM 4399 O O . HOH I 6 . ? -18.427 -9.290 41.434 1.00 32.00 ? 694 HOH A O 1 HETATM 4400 O O . HOH I 6 . ? -0.633 9.059 37.364 1.00 39.76 ? 695 HOH A O 1 HETATM 4401 O O . HOH I 6 . ? -0.725 4.487 35.805 1.00 31.94 ? 696 HOH A O 1 HETATM 4402 O O . HOH I 6 . ? -29.019 2.565 46.314 1.00 39.69 ? 697 HOH A O 1 HETATM 4403 O O . HOH I 6 . ? -31.512 5.519 -3.256 1.00 36.46 ? 698 HOH A O 1 HETATM 4404 O O . HOH I 6 . ? -10.514 3.659 65.876 1.00 29.49 ? 699 HOH A O 1 HETATM 4405 O O . HOH I 6 . ? -24.539 24.173 57.979 1.00 35.14 ? 700 HOH A O 1 HETATM 4406 O O . HOH I 6 . ? -31.365 8.247 41.395 1.00 41.34 ? 701 HOH A O 1 HETATM 4407 O O . HOH I 6 . ? -41.198 3.555 60.288 1.00 33.81 ? 702 HOH A O 1 HETATM 4408 O O . HOH I 6 . ? -8.293 23.760 56.157 1.00 39.49 ? 703 HOH A O 1 HETATM 4409 O O . HOH I 6 . ? -4.607 7.325 58.573 1.00 37.19 ? 704 HOH A O 1 HETATM 4410 O O . HOH I 6 . ? -1.567 12.642 43.095 1.00 35.70 ? 705 HOH A O 1 HETATM 4411 O O . HOH I 6 . ? -20.449 0.610 63.209 1.00 41.84 ? 706 HOH A O 1 HETATM 4412 O O . HOH I 6 . ? -14.304 2.801 72.992 1.00 44.56 ? 707 HOH A O 1 HETATM 4413 O O . HOH I 6 . ? -19.487 -8.512 31.369 1.00 38.09 ? 708 HOH A O 1 HETATM 4414 O O . HOH I 6 . ? -11.977 -10.932 58.131 1.00 36.76 ? 709 HOH A O 1 HETATM 4415 O O . HOH I 6 . ? -32.518 13.603 54.792 1.00 33.09 ? 710 HOH A O 1 HETATM 4416 O O . HOH I 6 . ? -24.844 -5.669 50.888 1.00 38.14 ? 711 HOH A O 1 HETATM 4417 O O . HOH I 6 . ? -10.975 24.801 38.101 1.00 40.18 ? 713 HOH A O 1 HETATM 4418 O O . HOH I 6 . ? -17.377 24.142 42.797 1.00 40.71 ? 714 HOH A O 1 HETATM 4419 O O . HOH I 6 . ? -26.357 15.801 54.434 1.00 37.65 ? 715 HOH A O 1 HETATM 4420 O O . HOH I 6 . ? -14.277 -5.193 36.232 1.00 52.36 ? 716 HOH A O 1 HETATM 4421 O O . HOH I 6 . ? -19.800 12.351 8.574 1.00 42.19 ? 717 HOH A O 1 HETATM 4422 O O . HOH I 6 . ? -16.875 -9.412 43.811 1.00 37.39 ? 718 HOH A O 1 HETATM 4423 O O . HOH I 6 . ? -6.711 -0.495 34.205 1.00 37.25 ? 720 HOH A O 1 HETATM 4424 O O . HOH I 6 . ? -9.207 2.950 61.566 1.00 44.55 ? 721 HOH A O 1 HETATM 4425 O O . HOH I 6 . ? -5.735 -3.691 20.262 1.00 43.73 ? 722 HOH A O 1 HETATM 4426 O O . HOH I 6 . ? -2.079 11.791 59.297 1.00 43.29 ? 723 HOH A O 1 HETATM 4427 O O . HOH I 6 . ? -14.619 4.686 11.760 1.00 42.76 ? 724 HOH A O 1 HETATM 4428 O O . HOH I 6 . ? -12.460 -8.731 56.987 1.00 39.96 ? 725 HOH A O 1 HETATM 4429 O O . HOH I 6 . ? -11.111 -0.148 54.681 1.00 45.15 ? 726 HOH A O 1 HETATM 4430 O O . HOH I 6 . ? -10.539 -8.783 19.535 1.00 41.32 ? 727 HOH A O 1 HETATM 4431 O O . HOH I 6 . ? -21.815 -8.703 48.484 1.00 39.42 ? 728 HOH A O 1 HETATM 4432 O O . HOH I 6 . ? -27.690 23.623 50.450 1.00 32.96 ? 729 HOH A O 1 HETATM 4433 O O . HOH I 6 . ? -6.646 -2.469 28.405 1.00 38.76 ? 730 HOH A O 1 HETATM 4434 O O . HOH I 6 . ? -15.832 6.799 12.248 1.00 41.56 ? 731 HOH A O 1 HETATM 4435 O O . HOH I 6 . ? -9.468 -6.943 52.100 1.00 38.91 ? 732 HOH A O 1 HETATM 4436 O O . HOH I 6 . ? -2.350 5.985 31.655 1.00 41.73 ? 733 HOH A O 1 HETATM 4437 O O . HOH I 6 . ? -25.067 -9.221 35.465 1.00 42.32 ? 734 HOH A O 1 HETATM 4438 O O . HOH I 6 . ? -4.602 -0.513 35.941 1.00 33.90 ? 735 HOH A O 1 HETATM 4439 O O . HOH I 6 . ? -9.435 6.695 66.242 1.00 39.55 ? 736 HOH A O 1 HETATM 4440 O O . HOH I 6 . ? -0.616 22.242 41.272 1.00 44.73 ? 737 HOH A O 1 HETATM 4441 O O . HOH I 6 . ? -18.399 -6.906 50.621 1.00 36.63 ? 738 HOH A O 1 HETATM 4442 O O . HOH I 6 . ? -21.062 2.074 -2.715 1.00 43.39 ? 739 HOH A O 1 HETATM 4443 O O . HOH I 6 . ? -26.754 1.908 40.616 1.00 32.26 ? 740 HOH A O 1 HETATM 4444 O O . HOH I 6 . ? -33.357 10.112 43.238 1.00 38.36 ? 741 HOH A O 1 HETATM 4445 O O . HOH I 6 . ? -22.379 9.719 29.344 1.00 36.30 ? 742 HOH A O 1 HETATM 4446 O O . HOH I 6 . ? -31.119 16.056 65.003 1.00 45.36 ? 743 HOH A O 1 HETATM 4447 O O . HOH I 6 . ? -19.214 10.409 18.551 1.00 41.79 ? 744 HOH A O 1 HETATM 4448 O O . HOH I 6 . ? -28.371 8.551 71.826 1.00 43.11 ? 745 HOH A O 1 HETATM 4449 O O . HOH I 6 . ? -10.995 -8.432 50.507 1.00 36.17 ? 746 HOH A O 1 HETATM 4450 O O . HOH I 6 . ? -32.326 14.491 42.020 1.00 35.11 ? 747 HOH A O 1 HETATM 4451 O O . HOH I 6 . ? -30.581 16.799 46.186 1.00 41.74 ? 748 HOH A O 1 HETATM 4452 O O . HOH I 6 . ? -20.615 19.244 33.437 1.00 38.65 ? 749 HOH A O 1 HETATM 4453 O O . HOH I 6 . ? -27.032 -2.668 28.983 1.00 42.81 ? 750 HOH A O 1 HETATM 4454 O O . HOH I 6 . ? -7.816 18.215 34.881 1.00 37.33 ? 751 HOH A O 1 HETATM 4455 O O . HOH I 6 . ? -34.523 0.693 -14.031 1.00 46.56 ? 752 HOH A O 1 HETATM 4456 O O . HOH I 6 . ? -9.926 16.672 63.170 1.00 38.42 ? 753 HOH A O 1 HETATM 4457 O O . HOH I 6 . ? -12.560 16.583 65.846 1.00 38.26 ? 755 HOH A O 1 HETATM 4458 O O . HOH I 6 . ? -1.285 9.323 51.046 1.00 31.54 ? 756 HOH A O 1 HETATM 4459 O O . HOH I 6 . ? -31.955 17.212 57.778 1.00 37.16 ? 757 HOH A O 1 HETATM 4460 O O . HOH I 6 . ? -31.466 11.407 68.065 1.00 32.76 ? 758 HOH A O 1 HETATM 4461 O O . HOH I 6 . ? -21.282 1.713 -8.457 1.00 47.17 ? 759 HOH A O 1 HETATM 4462 O O . HOH I 6 . ? -10.785 28.251 55.999 1.00 41.83 ? 760 HOH A O 1 HETATM 4463 O O . HOH I 6 . ? -24.905 17.703 54.291 1.00 35.26 ? 762 HOH A O 1 HETATM 4464 O O . HOH I 6 . ? -6.917 -2.978 44.366 1.00 36.28 ? 763 HOH A O 1 HETATM 4465 O O . HOH I 6 . ? -37.017 7.175 67.664 1.00 52.16 ? 764 HOH A O 1 HETATM 4466 O O . HOH I 6 . ? -9.200 -2.840 37.357 1.00 40.63 ? 765 HOH A O 1 HETATM 4467 O O . HOH I 6 . ? -22.484 -5.550 11.751 1.00 42.41 ? 766 HOH A O 1 HETATM 4468 O O . HOH I 6 . ? -13.290 -6.490 58.460 1.00 38.66 ? 767 HOH A O 1 HETATM 4469 O O . HOH I 6 . ? -28.423 0.147 0.813 1.00 48.57 ? 768 HOH A O 1 HETATM 4470 O O . HOH I 6 . ? -25.384 -8.526 32.740 1.00 40.59 ? 769 HOH A O 1 HETATM 4471 O O . HOH I 6 . ? -25.035 7.348 30.139 1.00 49.97 ? 770 HOH A O 1 HETATM 4472 O O . HOH I 6 . ? -16.211 6.696 1.101 1.00 54.43 ? 771 HOH A O 1 HETATM 4473 O O . HOH I 6 . ? -33.280 -2.988 70.040 1.00 57.68 ? 772 HOH A O 1 HETATM 4474 O O . HOH I 6 . ? -18.013 16.602 27.351 1.00 41.36 ? 773 HOH A O 1 HETATM 4475 O O . HOH I 6 . ? -1.244 3.784 32.755 1.00 52.92 ? 774 HOH A O 1 HETATM 4476 O O . HOH I 6 . ? -26.131 20.779 69.056 1.00 42.46 ? 775 HOH A O 1 HETATM 4477 O O . HOH I 6 . ? -2.877 12.500 53.714 1.00 32.43 ? 776 HOH A O 1 HETATM 4478 O O . HOH I 6 . ? -17.983 -9.682 21.289 1.00 49.79 ? 777 HOH A O 1 HETATM 4479 O O . HOH I 6 . ? -0.487 15.448 41.014 1.00 34.85 ? 778 HOH A O 1 HETATM 4480 O O . HOH I 6 . ? -24.358 25.254 47.217 1.00 60.65 ? 779 HOH A O 1 HETATM 4481 O O . HOH I 6 . ? -29.907 17.057 48.994 1.00 43.15 ? 780 HOH A O 1 HETATM 4482 O O . HOH J 6 . ? -38.835 16.399 35.616 1.00 16.64 ? 178 HOH B O 1 HETATM 4483 O O . HOH J 6 . ? -34.638 18.003 37.898 1.00 19.47 ? 179 HOH B O 1 HETATM 4484 O O . HOH J 6 . ? -39.268 16.909 38.831 1.00 20.25 ? 180 HOH B O 1 HETATM 4485 O O . HOH J 6 . ? -22.878 -2.142 -27.011 1.00 50.50 ? 181 HOH B O 1 HETATM 4486 O O . HOH J 6 . ? -14.431 8.969 -21.266 1.00 58.57 ? 182 HOH B O 1 HETATM 4487 O O . HOH J 6 . ? -31.467 10.268 -34.893 1.00 27.55 ? 183 HOH B O 1 HETATM 4488 O O . HOH J 6 . ? -35.487 10.323 -21.441 1.00 28.30 ? 184 HOH B O 1 HETATM 4489 O O . HOH J 6 . ? -32.193 3.929 -30.443 1.00 26.78 ? 185 HOH B O 1 HETATM 4490 O O . HOH J 6 . ? -26.342 21.082 -27.777 1.00 39.24 ? 186 HOH B O 1 HETATM 4491 O O . HOH J 6 . ? -30.465 8.558 -16.455 1.00 28.35 ? 187 HOH B O 1 HETATM 4492 O O . HOH J 6 . ? -38.230 6.649 45.499 1.00 42.12 ? 188 HOH B O 1 HETATM 4493 O O . HOH J 6 . ? -37.235 18.229 36.994 1.00 19.45 ? 189 HOH B O 1 HETATM 4494 O O . HOH J 6 . ? -29.530 19.556 14.961 1.00 38.61 ? 190 HOH B O 1 HETATM 4495 O O . HOH J 6 . ? -26.888 4.000 -26.477 1.00 29.67 ? 191 HOH B O 1 HETATM 4496 O O . HOH J 6 . ? -28.319 17.260 -38.745 1.00 30.08 ? 192 HOH B O 1 HETATM 4497 O O . HOH J 6 . ? -32.085 7.763 33.366 1.00 30.53 ? 193 HOH B O 1 HETATM 4498 O O . HOH J 6 . ? -23.297 3.340 -36.501 1.00 41.34 ? 194 HOH B O 1 HETATM 4499 O O . HOH J 6 . ? -39.706 13.587 19.437 1.00 34.27 ? 195 HOH B O 1 HETATM 4500 O O . HOH J 6 . ? -28.048 3.808 -29.190 1.00 32.79 ? 196 HOH B O 1 HETATM 4501 O O . HOH J 6 . ? -30.663 2.509 -28.609 1.00 31.04 ? 197 HOH B O 1 HETATM 4502 O O . HOH J 6 . ? -38.381 10.493 -25.999 1.00 35.29 ? 199 HOH B O 1 HETATM 4503 O O . HOH J 6 . ? -23.811 24.489 2.727 1.00 50.57 ? 200 HOH B O 1 HETATM 4504 O O . HOH J 6 . ? -33.312 8.195 0.435 1.00 41.58 ? 201 HOH B O 1 HETATM 4505 O O . HOH J 6 . ? -27.558 24.099 -36.936 1.00 33.47 ? 202 HOH B O 1 HETATM 4506 O O . HOH J 6 . ? -23.264 17.114 -23.063 1.00 36.32 ? 203 HOH B O 1 HETATM 4507 O O . HOH J 6 . ? -23.668 13.079 30.193 1.00 36.60 ? 204 HOH B O 1 HETATM 4508 O O . HOH J 6 . ? -38.248 17.122 -22.846 1.00 35.99 ? 205 HOH B O 1 HETATM 4509 O O . HOH J 6 . ? -34.874 14.007 41.867 1.00 32.03 ? 206 HOH B O 1 HETATM 4510 O O . HOH J 6 . ? -39.823 9.803 31.449 1.00 28.61 ? 207 HOH B O 1 HETATM 4511 O O . HOH J 6 . ? -29.787 3.384 -37.466 1.00 41.64 ? 208 HOH B O 1 HETATM 4512 O O . HOH J 6 . ? -19.820 10.248 -51.086 1.00 40.91 ? 209 HOH B O 1 HETATM 4513 O O . HOH J 6 . ? -35.065 11.356 -12.646 1.00 40.50 ? 210 HOH B O 1 HETATM 4514 O O . HOH J 6 . ? -36.857 15.870 41.362 1.00 30.93 ? 211 HOH B O 1 HETATM 4515 O O . HOH J 6 . ? -24.426 10.632 32.541 1.00 37.01 ? 212 HOH B O 1 HETATM 4516 O O . HOH J 6 . ? -16.678 17.514 -49.697 1.00 43.32 ? 217 HOH B O 1 HETATM 4517 O O . HOH J 6 . ? -38.632 19.898 2.695 1.00 40.52 ? 230 HOH B O 1 HETATM 4518 O O . HOH J 6 . ? -34.145 7.161 40.878 1.00 34.71 ? 231 HOH B O 1 HETATM 4519 O O . HOH J 6 . ? -28.146 0.959 -36.100 1.00 51.33 ? 234 HOH B O 1 HETATM 4520 O O . HOH J 6 . ? -26.891 19.083 -18.526 1.00 37.41 ? 242 HOH B O 1 HETATM 4521 O O . HOH J 6 . ? -32.053 9.097 20.294 1.00 43.80 ? 249 HOH B O 1 HETATM 4522 O O . HOH J 6 . ? -17.178 5.607 -32.887 1.00 49.91 ? 252 HOH B O 1 HETATM 4523 O O . HOH J 6 . ? -15.991 14.570 -41.485 1.00 48.99 ? 258 HOH B O 1 HETATM 4524 O O . HOH J 6 . ? -41.871 12.410 41.986 1.00 35.21 ? 265 HOH B O 1 HETATM 4525 O O . HOH J 6 . ? -39.698 9.245 28.131 1.00 37.29 ? 267 HOH B O 1 HETATM 4526 O O . HOH J 6 . ? -41.755 7.861 40.225 1.00 38.55 ? 268 HOH B O 1 HETATM 4527 O O . HOH J 6 . ? -18.409 -2.347 -33.042 1.00 51.25 ? 272 HOH B O 1 HETATM 4528 O O . HOH J 6 . ? -24.924 18.979 -21.277 1.00 42.75 ? 274 HOH B O 1 HETATM 4529 O O . HOH J 6 . ? -29.444 20.920 -26.620 1.00 44.59 ? 282 HOH B O 1 HETATM 4530 O O . HOH J 6 . ? -34.242 10.661 28.208 1.00 36.50 ? 283 HOH B O 1 HETATM 4531 O O . HOH J 6 . ? -21.829 16.595 -20.462 1.00 49.62 ? 291 HOH B O 1 HETATM 4532 O O . HOH J 6 . ? -22.717 22.029 -33.390 1.00 41.25 ? 293 HOH B O 1 HETATM 4533 O O . HOH J 6 . ? -13.119 8.873 -31.048 1.00 53.19 ? 294 HOH B O 1 HETATM 4534 O O . HOH J 6 . ? -31.290 17.820 -13.233 1.00 34.92 ? 297 HOH B O 1 HETATM 4535 O O . HOH J 6 . ? -33.197 14.593 -41.359 1.00 34.44 ? 302 HOH B O 1 HETATM 4536 O O . HOH J 6 . ? -34.126 16.546 -33.482 1.00 35.63 ? 307 HOH B O 1 HETATM 4537 O O . HOH J 6 . ? -35.657 12.044 44.000 1.00 46.47 ? 308 HOH B O 1 HETATM 4538 O O . HOH J 6 . ? -23.252 10.809 24.328 1.00 44.72 ? 310 HOH B O 1 HETATM 4539 O O . HOH J 6 . ? -40.299 14.565 41.662 1.00 42.24 ? 311 HOH B O 1 HETATM 4540 O O . HOH J 6 . ? -36.890 9.107 11.320 1.00 57.63 ? 312 HOH B O 1 HETATM 4541 O O . HOH J 6 . ? -35.094 7.755 -18.942 1.00 40.87 ? 322 HOH B O 1 HETATM 4542 O O . HOH J 6 . ? -31.311 19.967 -37.633 1.00 41.09 ? 329 HOH B O 1 HETATM 4543 O O . HOH J 6 . ? -13.424 6.769 -36.166 1.00 46.27 ? 331 HOH B O 1 HETATM 4544 O O . HOH J 6 . ? -25.955 17.820 19.017 1.00 45.08 ? 334 HOH B O 1 HETATM 4545 O O . HOH J 6 . ? -34.136 2.284 -34.524 1.00 52.78 ? 336 HOH B O 1 HETATM 4546 O O . HOH J 6 . ? -37.939 13.390 -13.871 1.00 45.80 ? 341 HOH B O 1 HETATM 4547 O O . HOH J 6 . ? -16.654 11.122 -49.232 1.00 43.96 ? 344 HOH B O 1 HETATM 4548 O O . HOH J 6 . ? -14.334 2.439 -39.233 1.00 54.76 ? 345 HOH B O 1 HETATM 4549 O O . HOH J 6 . ? -35.187 18.270 40.402 1.00 43.90 ? 346 HOH B O 1 HETATM 4550 O O . HOH J 6 . ? -36.138 5.639 -31.202 1.00 46.00 ? 347 HOH B O 1 HETATM 4551 O O . HOH J 6 . ? -29.468 16.494 25.834 1.00 40.80 ? 349 HOH B O 1 HETATM 4552 O O . HOH J 6 . ? -40.168 11.308 20.580 1.00 50.26 ? 351 HOH B O 1 HETATM 4553 O O . HOH J 6 . ? -36.382 2.431 -24.240 1.00 48.26 ? 356 HOH B O 1 HETATM 4554 O O . HOH J 6 . ? -34.510 2.757 -31.694 1.00 40.26 ? 357 HOH B O 1 HETATM 4555 O O . HOH J 6 . ? -34.520 19.109 -33.753 1.00 45.30 ? 374 HOH B O 1 HETATM 4556 O O . HOH J 6 . ? -29.763 22.406 -37.652 1.00 46.19 ? 375 HOH B O 1 HETATM 4557 O O . HOH J 6 . ? -39.839 13.413 16.147 1.00 48.93 ? 384 HOH B O 1 HETATM 4558 O O . HOH J 6 . ? -31.686 20.276 -47.103 1.00 54.60 ? 388 HOH B O 1 HETATM 4559 O O . HOH J 6 . ? -13.646 12.000 -19.715 1.00 53.42 ? 393 HOH B O 1 HETATM 4560 O O . HOH J 6 . ? -30.925 17.653 -38.701 1.00 53.99 ? 394 HOH B O 1 HETATM 4561 O O . HOH J 6 . ? -35.173 5.568 42.944 1.00 55.64 ? 395 HOH B O 1 HETATM 4562 O O . HOH J 6 . ? -35.848 16.306 -7.676 1.00 49.21 ? 400 HOH B O 1 HETATM 4563 O O . HOH J 6 . ? -14.837 10.340 -29.132 1.00 51.63 ? 402 HOH B O 1 HETATM 4564 O O . HOH J 6 . ? -38.587 6.910 -29.867 1.00 38.68 ? 403 HOH B O 1 HETATM 4565 O O . HOH J 6 . ? -33.816 18.278 -13.493 1.00 44.26 ? 404 HOH B O 1 HETATM 4566 O O . HOH J 6 . ? -34.941 16.370 -12.260 1.00 44.08 ? 407 HOH B O 1 HETATM 4567 O O . HOH J 6 . ? -30.230 8.425 22.141 1.00 50.53 ? 408 HOH B O 1 HETATM 4568 O O . HOH J 6 . ? -34.678 19.034 4.249 1.00 44.61 ? 411 HOH B O 1 HETATM 4569 O O . HOH J 6 . ? -25.401 20.872 -17.182 1.00 50.02 ? 419 HOH B O 1 HETATM 4570 O O . HOH J 6 . ? -26.293 22.326 -30.142 1.00 37.19 ? 424 HOH B O 1 HETATM 4571 O O . HOH J 6 . ? -28.316 17.679 -10.845 1.00 45.59 ? 428 HOH B O 1 HETATM 4572 O O . HOH J 6 . ? -29.309 -1.169 -26.476 1.00 45.45 ? 429 HOH B O 1 HETATM 4573 O O . HOH J 6 . ? -35.305 20.427 7.995 0.33 34.51 ? 430 HOH B O 1 HETATM 4574 O O . HOH J 6 . ? -32.506 10.360 24.082 1.00 52.82 ? 432 HOH B O 1 HETATM 4575 O O . HOH J 6 . ? -20.158 20.273 -14.348 1.00 51.31 ? 434 HOH B O 1 HETATM 4576 O O . HOH J 6 . ? -35.404 14.218 -26.508 1.00 48.77 ? 438 HOH B O 1 HETATM 4577 O O . HOH J 6 . ? -42.596 10.365 24.472 1.00 51.88 ? 439 HOH B O 1 HETATM 4578 O O . HOH J 6 . ? -36.412 17.898 -24.166 1.00 59.23 ? 441 HOH B O 1 HETATM 4579 O O . HOH J 6 . ? -37.442 4.327 -25.686 1.00 54.72 ? 442 HOH B O 1 HETATM 4580 O O . HOH J 6 . ? -21.470 3.328 -47.819 1.00 51.09 ? 451 HOH B O 1 HETATM 4581 O O . HOH J 6 . ? -22.277 18.135 -25.449 1.00 46.87 ? 455 HOH B O 1 HETATM 4582 O O . HOH J 6 . ? -38.419 9.201 -31.555 1.00 48.66 ? 461 HOH B O 1 HETATM 4583 O O . HOH J 6 . ? -20.176 -1.846 -20.428 1.00 42.28 ? 467 HOH B O 1 HETATM 4584 O O . HOH J 6 . ? -35.314 6.923 1.091 1.00 40.89 ? 469 HOH B O 1 HETATM 4585 O O . HOH J 6 . ? -41.134 5.706 38.311 1.00 50.22 ? 478 HOH B O 1 HETATM 4586 O O . HOH J 6 . ? -35.353 20.402 -27.960 0.33 51.59 ? 485 HOH B O 1 HETATM 4587 O O . HOH J 6 . ? -18.761 19.969 -51.306 1.00 47.09 ? 486 HOH B O 1 HETATM 4588 O O . HOH J 6 . ? -19.229 17.547 -25.733 1.00 47.91 ? 487 HOH B O 1 HETATM 4589 O O . HOH J 6 . ? -17.806 6.592 -53.714 1.00 53.16 ? 490 HOH B O 1 HETATM 4590 O O . HOH J 6 . ? -21.873 23.066 -3.646 1.00 58.60 ? 494 HOH B O 1 HETATM 4591 O O . HOH J 6 . ? -22.421 13.071 21.906 1.00 50.65 ? 495 HOH B O 1 HETATM 4592 O O . HOH J 6 . ? -28.860 7.120 36.970 1.00 51.41 ? 498 HOH B O 1 HETATM 4593 O O . HOH J 6 . ? -36.911 7.952 28.189 1.00 55.30 ? 499 HOH B O 1 HETATM 4594 O O . HOH J 6 . ? -26.677 10.887 17.583 1.00 40.46 ? 501 HOH B O 1 HETATM 4595 O O . HOH J 6 . ? -18.271 0.395 -51.107 1.00 58.07 ? 506 HOH B O 1 HETATM 4596 O O . HOH J 6 . ? -15.458 18.399 -9.440 1.00 64.47 ? 507 HOH B O 1 HETATM 4597 O O . HOH J 6 . ? -18.146 -1.852 -18.629 1.00 59.06 ? 513 HOH B O 1 HETATM 4598 O O . HOH J 6 . ? -25.168 20.353 -47.955 1.00 44.18 ? 515 HOH B O 1 HETATM 4599 O O . HOH J 6 . ? -21.641 15.747 21.446 1.00 62.32 ? 516 HOH B O 1 HETATM 4600 O O . HOH J 6 . ? -22.497 24.123 -35.583 1.00 56.35 ? 523 HOH B O 1 HETATM 4601 O O . HOH J 6 . ? -29.682 0.000 -28.892 1.00 43.04 ? 526 HOH B O 1 HETATM 4602 O O . HOH J 6 . ? -21.496 22.780 -39.771 1.00 48.29 ? 527 HOH B O 1 HETATM 4603 O O . HOH J 6 . ? -14.585 16.752 -42.081 1.00 48.06 ? 534 HOH B O 1 HETATM 4604 O O . HOH J 6 . ? -27.979 21.800 -48.672 1.00 48.70 ? 535 HOH B O 1 HETATM 4605 O O . HOH J 6 . ? -17.649 21.677 -37.789 1.00 59.05 ? 537 HOH B O 1 HETATM 4606 O O . HOH J 6 . ? -29.463 15.732 -58.104 1.00 60.49 ? 547 HOH B O 1 HETATM 4607 O O . HOH J 6 . ? -20.989 -5.079 -19.717 1.00 52.84 ? 552 HOH B O 1 HETATM 4608 O O . HOH J 6 . ? -36.514 6.035 7.587 1.00 48.93 ? 556 HOH B O 1 HETATM 4609 O O . HOH J 6 . ? -27.964 3.391 -43.374 1.00 48.90 ? 559 HOH B O 1 HETATM 4610 O O . HOH J 6 . ? -18.542 22.469 -40.879 1.00 47.91 ? 560 HOH B O 1 HETATM 4611 O O . HOH J 6 . ? -40.917 5.674 41.106 1.00 56.88 ? 562 HOH B O 1 HETATM 4612 O O . HOH J 6 . ? -39.030 8.043 -27.249 1.00 44.84 ? 570 HOH B O 1 HETATM 4613 O O . HOH J 6 . ? -36.658 1.438 -21.414 1.00 58.23 ? 576 HOH B O 1 HETATM 4614 O O . HOH J 6 . ? -23.619 10.523 20.228 1.00 49.67 ? 577 HOH B O 1 HETATM 4615 O O . HOH J 6 . ? -37.308 14.837 45.739 1.00 46.34 ? 579 HOH B O 1 HETATM 4616 O O . HOH J 6 . ? -33.961 11.437 -17.212 1.00 61.96 ? 588 HOH B O 1 HETATM 4617 O O . HOH J 6 . ? -36.542 8.884 34.921 1.00 50.76 ? 590 HOH B O 1 HETATM 4618 O O . HOH J 6 . ? -24.158 17.824 17.237 1.00 62.21 ? 591 HOH B O 1 HETATM 4619 O O . HOH J 6 . ? -22.714 20.578 -14.344 1.00 58.49 ? 595 HOH B O 1 HETATM 4620 O O . HOH J 6 . ? -33.771 -0.558 -24.329 1.00 61.57 ? 605 HOH B O 1 HETATM 4621 O O . HOH J 6 . ? -29.331 11.213 16.875 1.00 35.41 ? 614 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 PRO 1 9 9 PRO PRO A . n A 1 2 GLY 2 10 10 GLY GLY A . n A 1 3 ASP 3 11 11 ASP ASP A . n A 1 4 GLN 4 12 12 GLN GLN A . n A 1 5 ILE 5 13 13 ILE ILE A . n A 1 6 CYS 6 14 14 CYS CYS A . n A 1 7 ILE 7 15 15 ILE ILE A . n A 1 8 GLY 8 16 16 GLY GLY A . n A 1 9 TYR 9 17 17 TYR TYR A . n A 1 10 HIS 10 18 18 HIS HIS A . n A 1 11 ALA 11 19 19 ALA ALA A . n A 1 12 ASN 12 20 20 ASN ASN A . n A 1 13 ASN 13 21 21 ASN ASN A . n A 1 14 SER 14 22 22 SER SER A . n A 1 15 THR 15 23 23 THR THR A . n A 1 16 GLU 16 24 24 GLU GLU A . n A 1 17 LYS 17 25 25 LYS LYS A . n A 1 18 VAL 18 26 26 VAL VAL A . n A 1 19 ASP 19 27 27 ASP ASP A . n A 1 20 THR 20 28 28 THR THR A . n A 1 21 ILE 21 29 29 ILE ILE A . n A 1 22 LEU 22 30 30 LEU LEU A . n A 1 23 GLU 23 31 31 GLU GLU A . n A 1 24 ARG 24 32 32 ARG ARG A . n A 1 25 ASN 25 33 33 ASN ASN A . n A 1 26 VAL 26 34 34 VAL VAL A . n A 1 27 THR 27 35 35 THR THR A . n A 1 28 VAL 28 36 36 VAL VAL A . n A 1 29 THR 29 37 37 THR THR A . n A 1 30 HIS 30 38 38 HIS HIS A . n A 1 31 ALA 31 39 39 ALA ALA A . n A 1 32 LYS 32 40 40 LYS LYS A . n A 1 33 ASP 33 41 41 ASP ASP A . n A 1 34 ILE 34 42 42 ILE ILE A . n A 1 35 LEU 35 43 43 LEU LEU A . n A 1 36 GLU 36 44 44 GLU GLU A . n A 1 37 LYS 37 45 45 LYS LYS A . n A 1 38 THR 38 46 46 THR THR A . n A 1 39 HIS 39 47 47 HIS HIS A . n A 1 40 ASN 40 48 48 ASN ASN A . n A 1 41 GLY 41 49 49 GLY GLY A . n A 1 42 LYS 42 50 50 LYS LYS A . n A 1 43 LEU 43 51 51 LEU LEU A . n A 1 44 CYS 44 52 52 CYS CYS A . n A 1 45 LYS 45 53 53 LYS LYS A . n A 1 46 LEU 46 53 53 LEU LEU A A n A 1 47 ASN 47 54 54 ASN ASN A . n A 1 48 GLY 48 55 55 GLY GLY A . n A 1 49 ILE 49 56 56 ILE ILE A . n A 1 50 PRO 50 57 57 PRO PRO A . n A 1 51 PRO 51 58 58 PRO PRO A . n A 1 52 LEU 52 59 59 LEU LEU A . n A 1 53 GLU 53 60 60 GLU GLU A . n A 1 54 LEU 54 61 61 LEU LEU A . n A 1 55 GLY 55 62 62 GLY GLY A . n A 1 56 ASP 56 63 63 ASP ASP A . n A 1 57 CYS 57 64 64 CYS CYS A . n A 1 58 SER 58 65 65 SER SER A . n A 1 59 ILE 59 66 66 ILE ILE A . n A 1 60 ALA 60 67 67 ALA ALA A . n A 1 61 GLY 61 68 68 GLY GLY A . n A 1 62 TRP 62 69 69 TRP TRP A . n A 1 63 LEU 63 70 70 LEU LEU A . n A 1 64 LEU 64 71 71 LEU LEU A . n A 1 65 GLY 65 72 72 GLY GLY A . n A 1 66 ASN 66 73 73 ASN ASN A . n A 1 67 PRO 67 74 74 PRO PRO A . n A 1 68 GLU 68 75 75 GLU GLU A . n A 1 69 CYS 69 76 76 CYS CYS A . n A 1 70 ASP 70 77 77 ASP ASP A . n A 1 71 ARG 71 78 78 ARG ARG A . n A 1 72 LEU 72 79 79 LEU LEU A . n A 1 73 LEU 73 80 80 LEU LEU A . n A 1 74 SER 74 81 81 SER SER A . n A 1 75 VAL 75 81 81 VAL VAL A A n A 1 76 PRO 76 82 82 PRO PRO A . n A 1 77 GLU 77 83 83 GLU GLU A . n A 1 78 TRP 78 84 84 TRP TRP A . n A 1 79 SER 79 85 85 SER SER A . n A 1 80 TYR 80 86 86 TYR TYR A . n A 1 81 ILE 81 87 87 ILE ILE A . n A 1 82 MET 82 88 88 MET MET A . n A 1 83 GLU 83 89 89 GLU GLU A . n A 1 84 LYS 84 90 90 LYS LYS A . n A 1 85 GLU 85 91 91 GLU GLU A . n A 1 86 ASN 86 92 92 ASN ASN A . n A 1 87 PRO 87 93 93 PRO PRO A . n A 1 88 ARG 88 94 94 ARG ARG A . n A 1 89 ASP 89 95 95 ASP ASP A . n A 1 90 GLY 90 95 95 GLY GLY A A n A 1 91 LEU 91 96 96 LEU LEU A . n A 1 92 CYS 92 97 97 CYS CYS A . n A 1 93 TYR 93 98 98 TYR TYR A . n A 1 94 PRO 94 99 99 PRO PRO A . n A 1 95 GLY 95 100 100 GLY GLY A . n A 1 96 SER 96 101 101 SER SER A . n A 1 97 PHE 97 102 102 PHE PHE A . n A 1 98 ASN 98 103 103 ASN ASN A . n A 1 99 ASP 99 104 104 ASP ASP A . n A 1 100 TYR 100 105 105 TYR TYR A . n A 1 101 GLU 101 106 106 GLU GLU A . n A 1 102 GLU 102 107 107 GLU GLU A . n A 1 103 LEU 103 108 108 LEU LEU A . n A 1 104 LYS 104 109 109 LYS LYS A . n A 1 105 HIS 105 110 110 HIS HIS A . n A 1 106 LEU 106 111 111 LEU LEU A . n A 1 107 LEU 107 112 112 LEU LEU A . n A 1 108 SER 108 113 113 SER SER A . n A 1 109 SER 109 114 114 SER SER A . n A 1 110 VAL 110 115 115 VAL VAL A . n A 1 111 LYS 111 116 116 LYS LYS A . n A 1 112 HIS 112 116 116 HIS HIS A A n A 1 113 PHE 113 116 116 PHE PHE A B n A 1 114 GLU 114 116 116 GLU GLU A C n A 1 115 LYS 115 117 117 LYS LYS A . n A 1 116 VAL 116 118 118 VAL VAL A . n A 1 117 LYS 117 119 119 LYS LYS A . n A 1 118 ILE 118 120 120 ILE ILE A . n A 1 119 LEU 119 121 121 LEU LEU A . n A 1 120 PRO 120 122 122 PRO PRO A . n A 1 121 LYS 121 123 123 LYS LYS A . n A 1 122 ASP 122 125 125 ASP ASP A . n A 1 123 ARG 123 126 126 ARG ARG A . n A 1 124 TRP 124 127 127 TRP TRP A . n A 1 125 THR 125 128 128 THR THR A . n A 1 126 GLN 126 129 129 GLN GLN A . n A 1 127 HIS 127 130 130 HIS HIS A . n A 1 128 THR 128 131 131 THR THR A . n A 1 129 THR 129 132 132 THR THR A . n A 1 130 THR 130 133 133 THR THR A . n A 1 131 GLY 131 134 134 GLY GLY A . n A 1 132 GLY 132 135 135 GLY GLY A . n A 1 133 SER 133 136 136 SER SER A . n A 1 134 ARG 134 137 137 ARG ARG A . n A 1 135 ALA 135 138 138 ALA ALA A . n A 1 136 CYS 136 139 139 CYS CYS A . n A 1 137 ALA 137 140 140 ALA ALA A . n A 1 138 VAL 138 141 141 VAL VAL A . n A 1 139 SER 139 142 142 SER SER A . n A 1 140 GLY 140 143 143 GLY GLY A . n A 1 141 ASN 141 144 144 ASN ASN A . n A 1 142 PRO 142 145 145 PRO PRO A . n A 1 143 SER 143 146 146 SER SER A . n A 1 144 PHE 144 147 147 PHE PHE A . n A 1 145 PHE 145 148 148 PHE PHE A . n A 1 146 ARG 146 149 149 ARG ARG A . n A 1 147 ASN 147 150 150 ASN ASN A . n A 1 148 MET 148 151 151 MET MET A . n A 1 149 VAL 149 152 152 VAL VAL A . n A 1 150 TRP 150 153 153 TRP TRP A . n A 1 151 LEU 151 154 154 LEU LEU A . n A 1 152 THR 152 155 155 THR THR A . n A 1 153 GLU 153 156 156 GLU GLU A . n A 1 154 LYS 154 157 157 LYS LYS A . n A 1 155 GLY 155 158 158 GLY GLY A . n A 1 156 SER 156 159 159 SER SER A . n A 1 157 ASN 157 160 160 ASN ASN A . n A 1 158 TYR 158 161 161 TYR TYR A . n A 1 159 PRO 159 162 162 PRO PRO A . n A 1 160 VAL 160 163 163 VAL VAL A . n A 1 161 ALA 161 164 164 ALA ALA A . n A 1 162 LYS 162 165 165 LYS LYS A . n A 1 163 GLY 163 166 166 GLY GLY A . n A 1 164 SER 164 167 167 SER SER A . n A 1 165 TYR 165 168 168 TYR TYR A . n A 1 166 ASN 166 169 169 ASN ASN A . n A 1 167 ASN 167 170 170 ASN ASN A . n A 1 168 THR 168 171 171 THR THR A . n A 1 169 SER 169 172 172 SER SER A . n A 1 170 GLY 170 173 173 GLY GLY A . n A 1 171 GLU 171 174 174 GLU GLU A . n A 1 172 GLN 172 175 175 GLN GLN A . n A 1 173 MET 173 176 176 MET MET A . n A 1 174 LEU 174 177 177 LEU LEU A . n A 1 175 ILE 175 178 178 ILE ILE A . n A 1 176 ILE 176 179 179 ILE ILE A . n A 1 177 TRP 177 180 180 TRP TRP A . n A 1 178 GLY 178 181 181 GLY GLY A . n A 1 179 VAL 179 182 182 VAL VAL A . n A 1 180 HIS 180 183 183 HIS HIS A . n A 1 181 HIS 181 184 184 HIS HIS A . n A 1 182 PRO 182 185 185 PRO PRO A . n A 1 183 ASN 183 186 186 ASN ASN A . n A 1 184 ASP 184 187 187 ASP ASP A . n A 1 185 GLU 185 188 188 GLU GLU A . n A 1 186 THR 186 189 189 THR THR A . n A 1 187 GLU 187 190 190 GLU GLU A . n A 1 188 GLN 188 191 191 GLN GLN A . n A 1 189 ARG 189 192 192 ARG ARG A . n A 1 190 THR 190 193 193 THR THR A . n A 1 191 LEU 191 194 194 LEU LEU A . n A 1 192 TYR 192 195 195 TYR TYR A . n A 1 193 GLN 193 196 196 GLN GLN A . n A 1 194 ASN 194 197 197 ASN ASN A . n A 1 195 VAL 195 198 198 VAL VAL A . n A 1 196 GLY 196 199 199 GLY GLY A . n A 1 197 THR 197 200 200 THR THR A . n A 1 198 TYR 198 201 201 TYR TYR A . n A 1 199 VAL 199 202 202 VAL VAL A . n A 1 200 SER 200 203 203 SER SER A . n A 1 201 VAL 201 204 204 VAL VAL A . n A 1 202 GLY 202 205 205 GLY GLY A . n A 1 203 THR 203 206 206 THR THR A . n A 1 204 SER 204 207 207 SER SER A . n A 1 205 THR 205 208 208 THR THR A . n A 1 206 LEU 206 209 209 LEU LEU A . n A 1 207 ASN 207 210 210 ASN ASN A . n A 1 208 LYS 208 211 211 LYS LYS A . n A 1 209 ARG 209 212 212 ARG ARG A . n A 1 210 SER 210 213 213 SER SER A . n A 1 211 THR 211 214 214 THR THR A . n A 1 212 PRO 212 215 215 PRO PRO A . n A 1 213 GLU 213 216 216 GLU GLU A . n A 1 214 ILE 214 217 217 ILE ILE A . n A 1 215 ALA 215 218 218 ALA ALA A . n A 1 216 THR 216 219 219 THR THR A . n A 1 217 ARG 217 220 220 ARG ARG A . n A 1 218 PRO 218 221 221 PRO PRO A . n A 1 219 LYS 219 222 222 LYS LYS A . n A 1 220 VAL 220 223 223 VAL VAL A . n A 1 221 ASN 221 224 224 ASN ASN A . n A 1 222 GLY 222 225 225 GLY GLY A . n A 1 223 LEU 223 226 226 LEU LEU A . n A 1 224 GLY 224 227 227 GLY GLY A . n A 1 225 SER 225 228 228 SER SER A . n A 1 226 ARG 226 229 229 ARG ARG A . n A 1 227 MET 227 230 230 MET MET A . n A 1 228 GLU 228 231 231 GLU GLU A . n A 1 229 PHE 229 232 232 PHE PHE A . n A 1 230 SER 230 233 233 SER SER A . n A 1 231 TRP 231 234 234 TRP TRP A . n A 1 232 THR 232 235 235 THR THR A . n A 1 233 LEU 233 236 236 LEU LEU A . n A 1 234 LEU 234 237 237 LEU LEU A . n A 1 235 ASP 235 238 238 ASP ASP A . n A 1 236 MET 236 239 239 MET MET A . n A 1 237 TRP 237 240 240 TRP TRP A . n A 1 238 ASP 238 241 241 ASP ASP A . n A 1 239 THR 239 242 242 THR THR A . n A 1 240 ILE 240 243 243 ILE ILE A . n A 1 241 ASN 241 244 244 ASN ASN A . n A 1 242 PHE 242 245 245 PHE PHE A . n A 1 243 GLU 243 246 246 GLU GLU A . n A 1 244 SER 244 247 247 SER SER A . n A 1 245 THR 245 248 248 THR THR A . n A 1 246 GLY 246 249 249 GLY GLY A . n A 1 247 ASN 247 250 250 ASN ASN A . n A 1 248 LEU 248 251 251 LEU LEU A . n A 1 249 ILE 249 252 252 ILE ILE A . n A 1 250 ALA 250 253 253 ALA ALA A . n A 1 251 PRO 251 254 254 PRO PRO A . n A 1 252 GLU 252 255 255 GLU GLU A . n A 1 253 TYR 253 256 256 TYR TYR A . n A 1 254 GLY 254 257 257 GLY GLY A . n A 1 255 PHE 255 258 258 PHE PHE A . n A 1 256 LYS 256 259 259 LYS LYS A . n A 1 257 ILE 257 260 260 ILE ILE A . n A 1 258 SER 258 261 261 SER SER A . n A 1 259 LYS 259 262 262 LYS LYS A . n A 1 260 ARG 260 263 263 ARG ARG A . n A 1 261 GLY 261 263 263 GLY GLY A A n A 1 262 SER 262 264 264 SER SER A . n A 1 263 SER 263 265 265 SER SER A . n A 1 264 GLY 264 266 266 GLY GLY A . n A 1 265 ILE 265 267 267 ILE ILE A . n A 1 266 MET 266 268 268 MET MET A . n A 1 267 LYS 267 269 269 LYS LYS A . n A 1 268 THR 268 270 270 THR THR A . n A 1 269 GLU 269 271 271 GLU GLU A . n A 1 270 GLY 270 272 272 GLY GLY A . n A 1 271 THR 271 273 273 THR THR A . n A 1 272 LEU 272 274 274 LEU LEU A . n A 1 273 GLU 273 275 275 GLU GLU A . n A 1 274 ASN 274 276 276 ASN ASN A . n A 1 275 CYS 275 277 277 CYS CYS A . n A 1 276 GLU 276 278 278 GLU GLU A . n A 1 277 THR 277 279 279 THR THR A . n A 1 278 LYS 278 280 280 LYS LYS A . n A 1 279 CYS 279 281 281 CYS CYS A . n A 1 280 GLN 280 282 282 GLN GLN A . n A 1 281 THR 281 283 283 THR THR A . n A 1 282 PRO 282 284 284 PRO PRO A . n A 1 283 LEU 283 285 285 LEU LEU A . n A 1 284 GLY 284 286 286 GLY GLY A . n A 1 285 ALA 285 287 287 ALA ALA A . n A 1 286 ILE 286 288 288 ILE ILE A . n A 1 287 ASN 287 289 289 ASN ASN A . n A 1 288 THR 288 290 290 THR THR A . n A 1 289 THR 289 291 291 THR THR A . n A 1 290 LEU 290 292 292 LEU LEU A . n A 1 291 PRO 291 293 293 PRO PRO A . n A 1 292 PHE 292 294 294 PHE PHE A . n A 1 293 HIS 293 295 295 HIS HIS A . n A 1 294 ASN 294 296 296 ASN ASN A . n A 1 295 VAL 295 297 297 VAL VAL A . n A 1 296 HIS 296 298 298 HIS HIS A . n A 1 297 PRO 297 299 299 PRO PRO A . n A 1 298 LEU 298 300 300 LEU LEU A . n A 1 299 THR 299 301 301 THR THR A . n A 1 300 ILE 300 302 302 ILE ILE A . n A 1 301 GLY 301 303 303 GLY GLY A . n A 1 302 GLU 302 304 304 GLU GLU A . n A 1 303 CYS 303 305 305 CYS CYS A . n A 1 304 PRO 304 306 306 PRO PRO A . n A 1 305 LYS 305 307 307 LYS LYS A . n A 1 306 TYR 306 308 308 TYR TYR A . n A 1 307 VAL 307 309 309 VAL VAL A . n A 1 308 LYS 308 310 310 LYS LYS A . n A 1 309 SER 309 311 311 SER SER A . n A 1 310 GLU 310 312 312 GLU GLU A . n A 1 311 LYS 311 313 313 LYS LYS A . n A 1 312 LEU 312 314 314 LEU LEU A . n A 1 313 VAL 313 315 315 VAL VAL A . n A 1 314 LEU 314 316 316 LEU LEU A . n A 1 315 ALA 315 317 317 ALA ALA A . n A 1 316 THR 316 318 318 THR THR A . n A 1 317 GLY 317 319 319 GLY GLY A . n A 1 318 LEU 318 320 320 LEU LEU A . n A 1 319 ARG 319 321 321 ARG ARG A . n A 1 320 ASN 320 322 322 ASN ASN A . n A 1 321 VAL 321 323 323 VAL VAL A . n A 1 322 PRO 322 324 324 PRO PRO A . n A 1 323 GLN 323 325 ? ? ? A . n A 1 324 ILE 324 326 ? ? ? A . n A 1 325 GLU 325 327 ? ? ? A . n A 1 326 SER 326 328 ? ? ? A . n A 1 327 ARG 327 329 ? ? ? A . n B 2 1 GLY 1 1 1 GLY GLY B . n B 2 2 LEU 2 2 2 LEU LEU B . n B 2 3 PHE 3 3 3 PHE PHE B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 ALA 5 5 5 ALA ALA B . n B 2 6 ILE 6 6 6 ILE ILE B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLY 8 8 8 GLY GLY B . n B 2 9 PHE 9 9 9 PHE PHE B . n B 2 10 ILE 10 10 10 ILE ILE B . n B 2 11 GLU 11 11 11 GLU GLU B . n B 2 12 GLY 12 12 12 GLY GLY B . n B 2 13 GLY 13 13 13 GLY GLY B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 VAL 18 18 18 VAL VAL B . n B 2 19 ASP 19 19 19 ASP ASP B . n B 2 20 GLY 20 20 20 GLY GLY B . n B 2 21 TRP 21 21 21 TRP TRP B . n B 2 22 TYR 22 22 22 TYR TYR B . n B 2 23 GLY 23 23 23 GLY GLY B . n B 2 24 TYR 24 24 24 TYR TYR B . n B 2 25 HIS 25 25 25 HIS HIS B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 SER 27 27 27 SER SER B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 ASP 29 29 29 ASP ASP B . n B 2 30 GLN 30 30 30 GLN GLN B . n B 2 31 GLY 31 31 31 GLY GLY B . n B 2 32 SER 32 32 32 SER SER B . n B 2 33 GLY 33 33 33 GLY GLY B . n B 2 34 TYR 34 34 34 TYR TYR B . n B 2 35 ALA 35 35 35 ALA ALA B . n B 2 36 ALA 36 36 36 ALA ALA B . n B 2 37 ASP 37 37 37 ASP ASP B . n B 2 38 LYS 38 38 38 LYS LYS B . n B 2 39 GLU 39 39 39 GLU GLU B . n B 2 40 SER 40 40 40 SER SER B . n B 2 41 THR 41 41 41 THR THR B . n B 2 42 GLN 42 42 42 GLN GLN B . n B 2 43 LYS 43 43 43 LYS LYS B . n B 2 44 ALA 44 44 44 ALA ALA B . n B 2 45 PHE 45 45 45 PHE PHE B . n B 2 46 ASP 46 46 46 ASP ASP B . n B 2 47 GLY 47 47 47 GLY GLY B . n B 2 48 ILE 48 48 48 ILE ILE B . n B 2 49 THR 49 49 49 THR THR B . n B 2 50 ASN 50 50 50 ASN ASN B . n B 2 51 LYS 51 51 51 LYS LYS B . n B 2 52 VAL 52 52 52 VAL VAL B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 SER 54 54 54 SER SER B . n B 2 55 VAL 55 55 55 VAL VAL B . n B 2 56 ILE 56 56 56 ILE ILE B . n B 2 57 GLU 57 57 57 GLU GLU B . n B 2 58 LYS 58 58 58 LYS LYS B . n B 2 59 MET 59 59 59 MET MET B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 THR 61 61 61 THR THR B . n B 2 62 GLN 62 62 62 GLN GLN B . n B 2 63 PHE 63 63 63 PHE PHE B . n B 2 64 GLU 64 64 64 GLU GLU B . n B 2 65 ALA 65 65 65 ALA ALA B . n B 2 66 VAL 66 66 66 VAL VAL B . n B 2 67 GLY 67 67 67 GLY GLY B . n B 2 68 LYS 68 68 68 LYS LYS B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 SER 71 71 71 SER SER B . n B 2 72 ASN 72 72 72 ASN ASN B . n B 2 73 LEU 73 73 73 LEU LEU B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 ARG 75 75 75 ARG ARG B . n B 2 76 ARG 76 76 76 ARG ARG B . n B 2 77 LEU 77 77 77 LEU LEU B . n B 2 78 GLU 78 78 78 GLU GLU B . n B 2 79 ASN 79 79 79 ASN ASN B . n B 2 80 LEU 80 80 80 LEU LEU B . n B 2 81 ASN 81 81 81 ASN ASN B . n B 2 82 LYS 82 82 82 LYS LYS B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 MET 84 84 84 MET MET B . n B 2 85 GLU 85 85 85 GLU GLU B . n B 2 86 ASP 86 86 86 ASP ASP B . n B 2 87 GLY 87 87 87 GLY GLY B . n B 2 88 PHE 88 88 88 PHE PHE B . n B 2 89 LEU 89 89 89 LEU LEU B . n B 2 90 ASP 90 90 90 ASP ASP B . n B 2 91 VAL 91 91 91 VAL VAL B . n B 2 92 TRP 92 92 92 TRP TRP B . n B 2 93 THR 93 93 93 THR THR B . n B 2 94 TYR 94 94 94 TYR TYR B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 ALA 96 96 96 ALA ALA B . n B 2 97 GLU 97 97 97 GLU GLU B . n B 2 98 LEU 98 98 98 LEU LEU B . n B 2 99 LEU 99 99 99 LEU LEU B . n B 2 100 VAL 100 100 100 VAL VAL B . n B 2 101 LEU 101 101 101 LEU LEU B . n B 2 102 MET 102 102 102 MET MET B . n B 2 103 GLU 103 103 103 GLU GLU B . n B 2 104 ASN 104 104 104 ASN ASN B . n B 2 105 GLU 105 105 105 GLU GLU B . n B 2 106 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 MET 124 124 124 MET MET B . n B 2 125 GLN 125 125 125 GLN GLN B . n B 2 126 LEU 126 126 126 LEU LEU B . n B 2 127 ARG 127 127 127 ARG ARG B . n B 2 128 ASP 128 128 128 ASP ASP B . n B 2 129 ASN 129 129 129 ASN ASN B . n B 2 130 VAL 130 130 130 VAL VAL B . n B 2 131 LYS 131 131 131 LYS LYS B . n B 2 132 GLU 132 132 132 GLU GLU B . n B 2 133 LEU 133 133 133 LEU LEU B . n B 2 134 GLY 134 134 134 GLY GLY B . n B 2 135 ASN 135 135 135 ASN ASN B . n B 2 136 GLY 136 136 136 GLY GLY B . n B 2 137 CYS 137 137 137 CYS CYS B . n B 2 138 PHE 138 138 138 PHE PHE B . n B 2 139 GLU 139 139 139 GLU GLU B . n B 2 140 PHE 140 140 140 PHE PHE B . n B 2 141 TYR 141 141 141 TYR TYR B . n B 2 142 HIS 142 142 142 HIS HIS B . n B 2 143 LYS 143 143 143 LYS LYS B . n B 2 144 CYS 144 144 144 CYS CYS B . n B 2 145 ASP 145 145 145 ASP ASP B . n B 2 146 ASP 146 146 146 ASP ASP B . n B 2 147 GLU 147 147 147 GLU GLU B . n B 2 148 CYS 148 148 148 CYS CYS B . n B 2 149 MET 149 149 149 MET MET B . n B 2 150 ASN 150 150 150 ASN ASN B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 LYS 153 153 153 LYS LYS B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 GLY 155 155 155 GLY GLY B . n B 2 156 THR 156 156 156 THR THR B . n B 2 157 TYR 157 157 157 TYR TYR B . n B 2 158 ASP 158 158 158 ASP ASP B . n B 2 159 TYR 159 159 159 TYR TYR B . n B 2 160 PRO 160 160 160 PRO PRO B . n B 2 161 LYS 161 161 161 LYS LYS B . n B 2 162 TYR 162 162 162 TYR TYR B . n B 2 163 GLU 163 163 163 GLU GLU B . n B 2 164 GLU 164 164 164 GLU GLU B . n B 2 165 GLU 165 165 165 GLU GLU B . n B 2 166 SER 166 166 166 SER SER B . n B 2 167 LYS 167 167 167 LYS LYS B . n B 2 168 LEU 168 168 168 LEU LEU B . n B 2 169 ASN 169 169 169 ASN ASN B . n B 2 170 ARG 170 170 170 ARG ARG B . n B 2 171 ASN 171 171 171 ASN ASN B . n B 2 172 GLU 172 172 172 GLU GLU B . n B 2 173 ILE 173 173 ? ? ? B . n B 2 174 LYS 174 174 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 NAG 1 330 330 NAG NAG A . D 3 NAG 2 331 331 NAG NAG A . E 3 NAG 1 332 332 NAG NAG A . F 4 EDO 1 1 1 EDO EDO A . G 3 NAG 1 175 175 NAG NAG B . H 5 PEG 1 176 176 PEG PEG B . I 6 HOH 1 2 2 HOH HOH A . I 6 HOH 2 4 4 HOH HOH A . I 6 HOH 3 5 5 HOH HOH A . I 6 HOH 4 6 6 HOH HOH A . I 6 HOH 5 8 8 HOH HOH A . I 6 HOH 6 124 124 HOH HOH A . I 6 HOH 7 333 333 HOH HOH A . I 6 HOH 8 334 334 HOH HOH A . I 6 HOH 9 335 335 HOH HOH A . I 6 HOH 10 336 336 HOH HOH A . I 6 HOH 11 337 337 HOH HOH A . I 6 HOH 12 338 338 HOH HOH A . I 6 HOH 13 339 339 HOH HOH A . I 6 HOH 14 340 340 HOH HOH A . I 6 HOH 15 341 341 HOH HOH A . I 6 HOH 16 342 342 HOH HOH A . I 6 HOH 17 343 343 HOH HOH A . I 6 HOH 18 344 344 HOH HOH A . I 6 HOH 19 345 345 HOH HOH A . I 6 HOH 20 346 346 HOH HOH A . I 6 HOH 21 347 347 HOH HOH A . I 6 HOH 22 348 348 HOH HOH A . I 6 HOH 23 349 349 HOH HOH A . I 6 HOH 24 350 350 HOH HOH A . I 6 HOH 25 351 351 HOH HOH A . I 6 HOH 26 352 352 HOH HOH A . I 6 HOH 27 353 353 HOH HOH A . I 6 HOH 28 354 354 HOH HOH A . I 6 HOH 29 355 355 HOH HOH A . I 6 HOH 30 356 356 HOH HOH A . I 6 HOH 31 357 357 HOH HOH A . I 6 HOH 32 358 358 HOH HOH A . I 6 HOH 33 359 359 HOH HOH A . I 6 HOH 34 360 360 HOH HOH A . I 6 HOH 35 361 361 HOH HOH A . I 6 HOH 36 362 362 HOH HOH A . I 6 HOH 37 363 363 HOH HOH A . I 6 HOH 38 364 364 HOH HOH A . I 6 HOH 39 365 365 HOH HOH A . I 6 HOH 40 366 366 HOH HOH A . I 6 HOH 41 367 367 HOH HOH A . I 6 HOH 42 368 368 HOH HOH A . I 6 HOH 43 369 369 HOH HOH A . I 6 HOH 44 370 370 HOH HOH A . I 6 HOH 45 371 371 HOH HOH A . I 6 HOH 46 372 372 HOH HOH A . I 6 HOH 47 373 373 HOH HOH A . I 6 HOH 48 374 374 HOH HOH A . I 6 HOH 49 375 375 HOH HOH A . I 6 HOH 50 376 376 HOH HOH A . I 6 HOH 51 377 377 HOH HOH A . I 6 HOH 52 378 378 HOH HOH A . I 6 HOH 53 379 379 HOH HOH A . I 6 HOH 54 380 380 HOH HOH A . I 6 HOH 55 381 381 HOH HOH A . I 6 HOH 56 382 382 HOH HOH A . I 6 HOH 57 383 383 HOH HOH A . I 6 HOH 58 384 384 HOH HOH A . I 6 HOH 59 385 385 HOH HOH A . I 6 HOH 60 386 386 HOH HOH A . I 6 HOH 61 387 387 HOH HOH A . I 6 HOH 62 388 388 HOH HOH A . I 6 HOH 63 389 389 HOH HOH A . I 6 HOH 64 390 390 HOH HOH A . I 6 HOH 65 391 391 HOH HOH A . I 6 HOH 66 392 392 HOH HOH A . I 6 HOH 67 393 393 HOH HOH A . I 6 HOH 68 394 394 HOH HOH A . I 6 HOH 69 395 395 HOH HOH A . I 6 HOH 70 396 396 HOH HOH A . I 6 HOH 71 397 397 HOH HOH A . I 6 HOH 72 398 398 HOH HOH A . I 6 HOH 73 399 399 HOH HOH A . I 6 HOH 74 400 400 HOH HOH A . I 6 HOH 75 401 401 HOH HOH A . I 6 HOH 76 402 402 HOH HOH A . I 6 HOH 77 403 403 HOH HOH A . I 6 HOH 78 404 404 HOH HOH A . I 6 HOH 79 405 177 HOH HOH A . I 6 HOH 80 406 406 HOH HOH A . I 6 HOH 81 407 407 HOH HOH A . I 6 HOH 82 408 408 HOH HOH A . I 6 HOH 83 409 409 HOH HOH A . I 6 HOH 84 410 410 HOH HOH A . I 6 HOH 85 411 411 HOH HOH A . I 6 HOH 86 412 412 HOH HOH A . I 6 HOH 87 413 413 HOH HOH A . I 6 HOH 88 414 414 HOH HOH A . I 6 HOH 89 415 415 HOH HOH A . I 6 HOH 90 416 416 HOH HOH A . I 6 HOH 91 417 417 HOH HOH A . I 6 HOH 92 418 418 HOH HOH A . I 6 HOH 93 419 419 HOH HOH A . I 6 HOH 94 420 420 HOH HOH A . I 6 HOH 95 421 421 HOH HOH A . I 6 HOH 96 422 422 HOH HOH A . I 6 HOH 97 423 423 HOH HOH A . I 6 HOH 98 424 424 HOH HOH A . I 6 HOH 99 425 425 HOH HOH A . I 6 HOH 100 426 426 HOH HOH A . I 6 HOH 101 427 427 HOH HOH A . I 6 HOH 102 428 428 HOH HOH A . I 6 HOH 103 429 429 HOH HOH A . I 6 HOH 104 430 430 HOH HOH A . I 6 HOH 105 431 511 HOH HOH A . I 6 HOH 106 432 432 HOH HOH A . I 6 HOH 107 433 433 HOH HOH A . I 6 HOH 108 434 434 HOH HOH A . I 6 HOH 109 435 435 HOH HOH A . I 6 HOH 110 436 436 HOH HOH A . I 6 HOH 111 437 437 HOH HOH A . I 6 HOH 112 438 438 HOH HOH A . I 6 HOH 113 439 439 HOH HOH A . I 6 HOH 114 440 440 HOH HOH A . I 6 HOH 115 441 441 HOH HOH A . I 6 HOH 116 442 442 HOH HOH A . I 6 HOH 117 443 443 HOH HOH A . I 6 HOH 118 444 444 HOH HOH A . I 6 HOH 119 445 445 HOH HOH A . I 6 HOH 120 446 446 HOH HOH A . I 6 HOH 121 447 447 HOH HOH A . I 6 HOH 122 448 448 HOH HOH A . I 6 HOH 123 449 449 HOH HOH A . I 6 HOH 124 450 450 HOH HOH A . I 6 HOH 125 451 451 HOH HOH A . I 6 HOH 126 452 452 HOH HOH A . I 6 HOH 127 453 453 HOH HOH A . I 6 HOH 128 454 454 HOH HOH A . I 6 HOH 129 455 455 HOH HOH A . I 6 HOH 130 456 456 HOH HOH A . I 6 HOH 131 457 457 HOH HOH A . I 6 HOH 132 458 458 HOH HOH A . I 6 HOH 133 459 459 HOH HOH A . I 6 HOH 134 460 460 HOH HOH A . I 6 HOH 135 461 461 HOH HOH A . I 6 HOH 136 462 462 HOH HOH A . I 6 HOH 137 463 567 HOH HOH A . I 6 HOH 138 464 464 HOH HOH A . I 6 HOH 139 465 465 HOH HOH A . I 6 HOH 140 466 466 HOH HOH A . I 6 HOH 141 467 467 HOH HOH A . I 6 HOH 142 468 468 HOH HOH A . I 6 HOH 143 469 469 HOH HOH A . I 6 HOH 144 470 470 HOH HOH A . I 6 HOH 145 471 471 HOH HOH A . I 6 HOH 146 472 472 HOH HOH A . I 6 HOH 147 473 473 HOH HOH A . I 6 HOH 148 474 474 HOH HOH A . I 6 HOH 149 475 475 HOH HOH A . I 6 HOH 150 476 476 HOH HOH A . I 6 HOH 151 477 477 HOH HOH A . I 6 HOH 152 478 478 HOH HOH A . I 6 HOH 153 479 479 HOH HOH A . I 6 HOH 154 480 480 HOH HOH A . I 6 HOH 155 481 481 HOH HOH A . I 6 HOH 156 482 482 HOH HOH A . I 6 HOH 157 483 483 HOH HOH A . I 6 HOH 158 484 484 HOH HOH A . I 6 HOH 159 485 485 HOH HOH A . I 6 HOH 160 486 486 HOH HOH A . I 6 HOH 161 487 487 HOH HOH A . I 6 HOH 162 488 488 HOH HOH A . I 6 HOH 163 489 489 HOH HOH A . I 6 HOH 164 490 490 HOH HOH A . I 6 HOH 165 491 491 HOH HOH A . I 6 HOH 166 492 492 HOH HOH A . I 6 HOH 167 493 493 HOH HOH A . I 6 HOH 168 494 494 HOH HOH A . I 6 HOH 169 495 495 HOH HOH A . I 6 HOH 170 496 496 HOH HOH A . I 6 HOH 171 497 497 HOH HOH A . I 6 HOH 172 498 498 HOH HOH A . I 6 HOH 173 499 499 HOH HOH A . I 6 HOH 174 500 500 HOH HOH A . I 6 HOH 175 501 501 HOH HOH A . I 6 HOH 176 502 502 HOH HOH A . I 6 HOH 177 503 503 HOH HOH A . I 6 HOH 178 504 504 HOH HOH A . I 6 HOH 179 505 505 HOH HOH A . I 6 HOH 180 506 506 HOH HOH A . I 6 HOH 181 507 507 HOH HOH A . I 6 HOH 182 508 508 HOH HOH A . I 6 HOH 183 509 509 HOH HOH A . I 6 HOH 184 510 510 HOH HOH A . I 6 HOH 185 511 511 HOH HOH A . I 6 HOH 186 512 512 HOH HOH A . I 6 HOH 187 513 513 HOH HOH A . I 6 HOH 188 515 515 HOH HOH A . I 6 HOH 189 516 516 HOH HOH A . I 6 HOH 190 517 517 HOH HOH A . I 6 HOH 191 518 518 HOH HOH A . I 6 HOH 192 519 519 HOH HOH A . I 6 HOH 193 520 520 HOH HOH A . I 6 HOH 194 522 522 HOH HOH A . I 6 HOH 195 523 523 HOH HOH A . I 6 HOH 196 524 524 HOH HOH A . I 6 HOH 197 525 525 HOH HOH A . I 6 HOH 198 526 526 HOH HOH A . I 6 HOH 199 527 527 HOH HOH A . I 6 HOH 200 528 528 HOH HOH A . I 6 HOH 201 529 529 HOH HOH A . I 6 HOH 202 531 531 HOH HOH A . I 6 HOH 203 532 532 HOH HOH A . I 6 HOH 204 533 533 HOH HOH A . I 6 HOH 205 534 534 HOH HOH A . I 6 HOH 206 535 535 HOH HOH A . I 6 HOH 207 536 536 HOH HOH A . I 6 HOH 208 537 537 HOH HOH A . I 6 HOH 209 538 538 HOH HOH A . I 6 HOH 210 539 539 HOH HOH A . I 6 HOH 211 540 540 HOH HOH A . I 6 HOH 212 541 541 HOH HOH A . I 6 HOH 213 542 542 HOH HOH A . I 6 HOH 214 543 543 HOH HOH A . I 6 HOH 215 544 544 HOH HOH A . I 6 HOH 216 545 545 HOH HOH A . I 6 HOH 217 546 546 HOH HOH A . I 6 HOH 218 547 547 HOH HOH A . I 6 HOH 219 549 549 HOH HOH A . I 6 HOH 220 550 550 HOH HOH A . I 6 HOH 221 551 551 HOH HOH A . I 6 HOH 222 552 552 HOH HOH A . I 6 HOH 223 553 553 HOH HOH A . I 6 HOH 224 554 554 HOH HOH A . I 6 HOH 225 555 555 HOH HOH A . I 6 HOH 226 556 556 HOH HOH A . I 6 HOH 227 557 557 HOH HOH A . I 6 HOH 228 558 558 HOH HOH A . I 6 HOH 229 560 560 HOH HOH A . I 6 HOH 230 561 561 HOH HOH A . I 6 HOH 231 562 562 HOH HOH A . I 6 HOH 232 563 563 HOH HOH A . I 6 HOH 233 564 564 HOH HOH A . I 6 HOH 234 565 565 HOH HOH A . I 6 HOH 235 566 566 HOH HOH A . I 6 HOH 236 567 567 HOH HOH A . I 6 HOH 237 568 568 HOH HOH A . I 6 HOH 238 569 569 HOH HOH A . I 6 HOH 239 570 570 HOH HOH A . I 6 HOH 240 571 571 HOH HOH A . I 6 HOH 241 572 572 HOH HOH A . I 6 HOH 242 573 573 HOH HOH A . I 6 HOH 243 574 574 HOH HOH A . I 6 HOH 244 575 575 HOH HOH A . I 6 HOH 245 576 576 HOH HOH A . I 6 HOH 246 577 577 HOH HOH A . I 6 HOH 247 578 578 HOH HOH A . I 6 HOH 248 579 579 HOH HOH A . I 6 HOH 249 580 580 HOH HOH A . I 6 HOH 250 582 582 HOH HOH A . I 6 HOH 251 584 584 HOH HOH A . I 6 HOH 252 585 585 HOH HOH A . I 6 HOH 253 587 587 HOH HOH A . I 6 HOH 254 588 588 HOH HOH A . I 6 HOH 255 589 589 HOH HOH A . I 6 HOH 256 590 590 HOH HOH A . I 6 HOH 257 591 591 HOH HOH A . I 6 HOH 258 592 592 HOH HOH A . I 6 HOH 259 593 593 HOH HOH A . I 6 HOH 260 594 594 HOH HOH A . I 6 HOH 261 595 595 HOH HOH A . I 6 HOH 262 596 596 HOH HOH A . I 6 HOH 263 597 597 HOH HOH A . I 6 HOH 264 598 598 HOH HOH A . I 6 HOH 265 599 599 HOH HOH A . I 6 HOH 266 600 600 HOH HOH A . I 6 HOH 267 601 601 HOH HOH A . I 6 HOH 268 602 602 HOH HOH A . I 6 HOH 269 603 603 HOH HOH A . I 6 HOH 270 604 604 HOH HOH A . I 6 HOH 271 605 605 HOH HOH A . I 6 HOH 272 606 606 HOH HOH A . I 6 HOH 273 607 607 HOH HOH A . I 6 HOH 274 608 608 HOH HOH A . I 6 HOH 275 609 609 HOH HOH A . I 6 HOH 276 610 610 HOH HOH A . I 6 HOH 277 611 611 HOH HOH A . I 6 HOH 278 612 612 HOH HOH A . I 6 HOH 279 613 613 HOH HOH A . I 6 HOH 280 614 614 HOH HOH A . I 6 HOH 281 615 615 HOH HOH A . I 6 HOH 282 616 616 HOH HOH A . I 6 HOH 283 617 617 HOH HOH A . I 6 HOH 284 618 618 HOH HOH A . I 6 HOH 285 619 619 HOH HOH A . I 6 HOH 286 620 620 HOH HOH A . I 6 HOH 287 621 621 HOH HOH A . I 6 HOH 288 622 622 HOH HOH A . I 6 HOH 289 623 623 HOH HOH A . I 6 HOH 290 624 624 HOH HOH A . I 6 HOH 291 625 625 HOH HOH A . I 6 HOH 292 626 626 HOH HOH A . I 6 HOH 293 627 627 HOH HOH A . I 6 HOH 294 628 628 HOH HOH A . I 6 HOH 295 629 629 HOH HOH A . I 6 HOH 296 630 630 HOH HOH A . I 6 HOH 297 631 631 HOH HOH A . I 6 HOH 298 632 632 HOH HOH A . I 6 HOH 299 633 633 HOH HOH A . I 6 HOH 300 634 634 HOH HOH A . I 6 HOH 301 635 635 HOH HOH A . I 6 HOH 302 636 636 HOH HOH A . I 6 HOH 303 637 637 HOH HOH A . I 6 HOH 304 638 638 HOH HOH A . I 6 HOH 305 639 639 HOH HOH A . I 6 HOH 306 640 640 HOH HOH A . I 6 HOH 307 641 641 HOH HOH A . I 6 HOH 308 642 642 HOH HOH A . I 6 HOH 309 643 643 HOH HOH A . I 6 HOH 310 644 644 HOH HOH A . I 6 HOH 311 645 645 HOH HOH A . I 6 HOH 312 646 646 HOH HOH A . I 6 HOH 313 647 647 HOH HOH A . I 6 HOH 314 648 648 HOH HOH A . I 6 HOH 315 649 649 HOH HOH A . I 6 HOH 316 650 650 HOH HOH A . I 6 HOH 317 651 651 HOH HOH A . I 6 HOH 318 652 652 HOH HOH A . I 6 HOH 319 653 653 HOH HOH A . I 6 HOH 320 654 654 HOH HOH A . I 6 HOH 321 655 655 HOH HOH A . I 6 HOH 322 656 656 HOH HOH A . I 6 HOH 323 657 657 HOH HOH A . I 6 HOH 324 658 658 HOH HOH A . I 6 HOH 325 659 659 HOH HOH A . I 6 HOH 326 660 660 HOH HOH A . I 6 HOH 327 661 661 HOH HOH A . I 6 HOH 328 662 662 HOH HOH A . I 6 HOH 329 663 663 HOH HOH A . I 6 HOH 330 664 664 HOH HOH A . I 6 HOH 331 665 665 HOH HOH A . I 6 HOH 332 666 666 HOH HOH A . I 6 HOH 333 667 667 HOH HOH A . I 6 HOH 334 668 668 HOH HOH A . I 6 HOH 335 669 669 HOH HOH A . I 6 HOH 336 670 670 HOH HOH A . I 6 HOH 337 671 671 HOH HOH A . I 6 HOH 338 672 672 HOH HOH A . I 6 HOH 339 673 673 HOH HOH A . I 6 HOH 340 674 674 HOH HOH A . I 6 HOH 341 675 675 HOH HOH A . I 6 HOH 342 676 676 HOH HOH A . I 6 HOH 343 677 677 HOH HOH A . I 6 HOH 344 678 678 HOH HOH A . I 6 HOH 345 679 679 HOH HOH A . I 6 HOH 346 680 680 HOH HOH A . I 6 HOH 347 681 681 HOH HOH A . I 6 HOH 348 682 682 HOH HOH A . I 6 HOH 349 683 683 HOH HOH A . I 6 HOH 350 684 684 HOH HOH A . I 6 HOH 351 685 685 HOH HOH A . I 6 HOH 352 686 686 HOH HOH A . I 6 HOH 353 687 687 HOH HOH A . I 6 HOH 354 688 688 HOH HOH A . I 6 HOH 355 689 689 HOH HOH A . I 6 HOH 356 690 690 HOH HOH A . I 6 HOH 357 691 691 HOH HOH A . I 6 HOH 358 692 692 HOH HOH A . I 6 HOH 359 693 693 HOH HOH A . I 6 HOH 360 694 694 HOH HOH A . I 6 HOH 361 695 695 HOH HOH A . I 6 HOH 362 696 696 HOH HOH A . I 6 HOH 363 697 697 HOH HOH A . I 6 HOH 364 698 698 HOH HOH A . I 6 HOH 365 699 699 HOH HOH A . I 6 HOH 366 700 700 HOH HOH A . I 6 HOH 367 701 701 HOH HOH A . I 6 HOH 368 702 702 HOH HOH A . I 6 HOH 369 703 703 HOH HOH A . I 6 HOH 370 704 704 HOH HOH A . I 6 HOH 371 705 705 HOH HOH A . I 6 HOH 372 706 706 HOH HOH A . I 6 HOH 373 707 707 HOH HOH A . I 6 HOH 374 708 708 HOH HOH A . I 6 HOH 375 709 709 HOH HOH A . I 6 HOH 376 710 710 HOH HOH A . I 6 HOH 377 711 711 HOH HOH A . I 6 HOH 378 713 713 HOH HOH A . I 6 HOH 379 714 714 HOH HOH A . I 6 HOH 380 715 715 HOH HOH A . I 6 HOH 381 716 716 HOH HOH A . I 6 HOH 382 717 717 HOH HOH A . I 6 HOH 383 718 718 HOH HOH A . I 6 HOH 384 720 720 HOH HOH A . I 6 HOH 385 721 721 HOH HOH A . I 6 HOH 386 722 722 HOH HOH A . I 6 HOH 387 723 723 HOH HOH A . I 6 HOH 388 724 724 HOH HOH A . I 6 HOH 389 725 725 HOH HOH A . I 6 HOH 390 726 726 HOH HOH A . I 6 HOH 391 727 727 HOH HOH A . I 6 HOH 392 728 728 HOH HOH A . I 6 HOH 393 729 729 HOH HOH A . I 6 HOH 394 730 730 HOH HOH A . I 6 HOH 395 731 731 HOH HOH A . I 6 HOH 396 732 732 HOH HOH A . I 6 HOH 397 733 733 HOH HOH A . I 6 HOH 398 734 734 HOH HOH A . I 6 HOH 399 735 735 HOH HOH A . I 6 HOH 400 736 736 HOH HOH A . I 6 HOH 401 737 737 HOH HOH A . I 6 HOH 402 738 738 HOH HOH A . I 6 HOH 403 739 739 HOH HOH A . I 6 HOH 404 740 740 HOH HOH A . I 6 HOH 405 741 741 HOH HOH A . I 6 HOH 406 742 742 HOH HOH A . I 6 HOH 407 743 743 HOH HOH A . I 6 HOH 408 744 744 HOH HOH A . I 6 HOH 409 745 745 HOH HOH A . I 6 HOH 410 746 746 HOH HOH A . I 6 HOH 411 747 747 HOH HOH A . I 6 HOH 412 748 748 HOH HOH A . I 6 HOH 413 749 749 HOH HOH A . I 6 HOH 414 750 750 HOH HOH A . I 6 HOH 415 751 751 HOH HOH A . I 6 HOH 416 752 752 HOH HOH A . I 6 HOH 417 753 753 HOH HOH A . I 6 HOH 418 755 755 HOH HOH A . I 6 HOH 419 756 756 HOH HOH A . I 6 HOH 420 757 757 HOH HOH A . I 6 HOH 421 758 758 HOH HOH A . I 6 HOH 422 759 759 HOH HOH A . I 6 HOH 423 760 760 HOH HOH A . I 6 HOH 424 762 762 HOH HOH A . I 6 HOH 425 763 763 HOH HOH A . I 6 HOH 426 764 764 HOH HOH A . I 6 HOH 427 765 765 HOH HOH A . I 6 HOH 428 766 766 HOH HOH A . I 6 HOH 429 767 767 HOH HOH A . I 6 HOH 430 768 768 HOH HOH A . I 6 HOH 431 769 769 HOH HOH A . I 6 HOH 432 770 770 HOH HOH A . I 6 HOH 433 771 771 HOH HOH A . I 6 HOH 434 772 772 HOH HOH A . I 6 HOH 435 773 773 HOH HOH A . I 6 HOH 436 774 774 HOH HOH A . I 6 HOH 437 775 775 HOH HOH A . I 6 HOH 438 776 776 HOH HOH A . I 6 HOH 439 777 777 HOH HOH A . I 6 HOH 440 778 778 HOH HOH A . I 6 HOH 441 779 779 HOH HOH A . I 6 HOH 442 780 780 HOH HOH A . J 6 HOH 1 178 178 HOH HOH B . J 6 HOH 2 179 179 HOH HOH B . J 6 HOH 3 180 180 HOH HOH B . J 6 HOH 4 181 181 HOH HOH B . J 6 HOH 5 182 182 HOH HOH B . J 6 HOH 6 183 183 HOH HOH B . J 6 HOH 7 184 184 HOH HOH B . J 6 HOH 8 185 185 HOH HOH B . J 6 HOH 9 186 186 HOH HOH B . J 6 HOH 10 187 187 HOH HOH B . J 6 HOH 11 188 188 HOH HOH B . J 6 HOH 12 189 189 HOH HOH B . J 6 HOH 13 190 190 HOH HOH B . J 6 HOH 14 191 191 HOH HOH B . J 6 HOH 15 192 192 HOH HOH B . J 6 HOH 16 193 193 HOH HOH B . J 6 HOH 17 194 194 HOH HOH B . J 6 HOH 18 195 195 HOH HOH B . J 6 HOH 19 196 196 HOH HOH B . J 6 HOH 20 197 197 HOH HOH B . J 6 HOH 21 199 199 HOH HOH B . J 6 HOH 22 200 200 HOH HOH B . J 6 HOH 23 201 201 HOH HOH B . J 6 HOH 24 202 202 HOH HOH B . J 6 HOH 25 203 203 HOH HOH B . J 6 HOH 26 204 204 HOH HOH B . J 6 HOH 27 205 205 HOH HOH B . J 6 HOH 28 206 206 HOH HOH B . J 6 HOH 29 207 207 HOH HOH B . J 6 HOH 30 208 208 HOH HOH B . J 6 HOH 31 209 209 HOH HOH B . J 6 HOH 32 210 210 HOH HOH B . J 6 HOH 33 211 211 HOH HOH B . J 6 HOH 34 212 212 HOH HOH B . J 6 HOH 35 217 217 HOH HOH B . J 6 HOH 36 230 230 HOH HOH B . J 6 HOH 37 231 231 HOH HOH B . J 6 HOH 38 234 234 HOH HOH B . J 6 HOH 39 242 242 HOH HOH B . J 6 HOH 40 249 249 HOH HOH B . J 6 HOH 41 252 252 HOH HOH B . J 6 HOH 42 258 258 HOH HOH B . J 6 HOH 43 265 265 HOH HOH B . J 6 HOH 44 267 267 HOH HOH B . J 6 HOH 45 268 268 HOH HOH B . J 6 HOH 46 272 272 HOH HOH B . J 6 HOH 47 274 274 HOH HOH B . J 6 HOH 48 282 282 HOH HOH B . J 6 HOH 49 283 283 HOH HOH B . J 6 HOH 50 291 291 HOH HOH B . J 6 HOH 51 293 293 HOH HOH B . J 6 HOH 52 294 294 HOH HOH B . J 6 HOH 53 297 297 HOH HOH B . J 6 HOH 54 302 302 HOH HOH B . J 6 HOH 55 307 307 HOH HOH B . J 6 HOH 56 308 308 HOH HOH B . J 6 HOH 57 310 310 HOH HOH B . J 6 HOH 58 311 311 HOH HOH B . J 6 HOH 59 312 312 HOH HOH B . J 6 HOH 60 322 322 HOH HOH B . J 6 HOH 61 329 329 HOH HOH B . J 6 HOH 62 331 331 HOH HOH B . J 6 HOH 63 334 334 HOH HOH B . J 6 HOH 64 336 336 HOH HOH B . J 6 HOH 65 341 341 HOH HOH B . J 6 HOH 66 344 344 HOH HOH B . J 6 HOH 67 345 345 HOH HOH B . J 6 HOH 68 346 346 HOH HOH B . J 6 HOH 69 347 347 HOH HOH B . J 6 HOH 70 349 349 HOH HOH B . J 6 HOH 71 351 351 HOH HOH B . J 6 HOH 72 356 356 HOH HOH B . J 6 HOH 73 357 357 HOH HOH B . J 6 HOH 74 374 374 HOH HOH B . J 6 HOH 75 375 375 HOH HOH B . J 6 HOH 76 384 384 HOH HOH B . J 6 HOH 77 388 388 HOH HOH B . J 6 HOH 78 393 393 HOH HOH B . J 6 HOH 79 394 394 HOH HOH B . J 6 HOH 80 395 395 HOH HOH B . J 6 HOH 81 400 400 HOH HOH B . J 6 HOH 82 402 402 HOH HOH B . J 6 HOH 83 403 403 HOH HOH B . J 6 HOH 84 404 404 HOH HOH B . J 6 HOH 85 407 407 HOH HOH B . J 6 HOH 86 408 408 HOH HOH B . J 6 HOH 87 411 411 HOH HOH B . J 6 HOH 88 419 419 HOH HOH B . J 6 HOH 89 424 424 HOH HOH B . J 6 HOH 90 428 428 HOH HOH B . J 6 HOH 91 429 429 HOH HOH B . J 6 HOH 92 430 430 HOH HOH B . J 6 HOH 93 432 432 HOH HOH B . J 6 HOH 94 434 434 HOH HOH B . J 6 HOH 95 438 438 HOH HOH B . J 6 HOH 96 439 439 HOH HOH B . J 6 HOH 97 441 441 HOH HOH B . J 6 HOH 98 442 442 HOH HOH B . J 6 HOH 99 451 451 HOH HOH B . J 6 HOH 100 455 455 HOH HOH B . J 6 HOH 101 461 461 HOH HOH B . J 6 HOH 102 467 467 HOH HOH B . J 6 HOH 103 469 469 HOH HOH B . J 6 HOH 104 478 478 HOH HOH B . J 6 HOH 105 485 485 HOH HOH B . J 6 HOH 106 486 486 HOH HOH B . J 6 HOH 107 487 487 HOH HOH B . J 6 HOH 108 490 490 HOH HOH B . J 6 HOH 109 494 494 HOH HOH B . J 6 HOH 110 495 495 HOH HOH B . J 6 HOH 111 498 498 HOH HOH B . J 6 HOH 112 499 499 HOH HOH B . J 6 HOH 113 501 501 HOH HOH B . J 6 HOH 114 506 506 HOH HOH B . J 6 HOH 115 507 507 HOH HOH B . J 6 HOH 116 513 513 HOH HOH B . J 6 HOH 117 515 515 HOH HOH B . J 6 HOH 118 516 516 HOH HOH B . J 6 HOH 119 523 523 HOH HOH B . J 6 HOH 120 526 526 HOH HOH B . J 6 HOH 121 527 527 HOH HOH B . J 6 HOH 122 534 534 HOH HOH B . J 6 HOH 123 535 535 HOH HOH B . J 6 HOH 124 537 537 HOH HOH B . J 6 HOH 125 547 547 HOH HOH B . J 6 HOH 126 552 552 HOH HOH B . J 6 HOH 127 556 556 HOH HOH B . J 6 HOH 128 559 559 HOH HOH B . J 6 HOH 129 560 560 HOH HOH B . J 6 HOH 130 562 562 HOH HOH B . J 6 HOH 131 570 570 HOH HOH B . J 6 HOH 132 576 576 HOH HOH B . J 6 HOH 133 577 577 HOH HOH B . J 6 HOH 134 579 579 HOH HOH B . J 6 HOH 135 588 588 HOH HOH B . J 6 HOH 136 590 590 HOH HOH B . J 6 HOH 137 591 591 HOH HOH B . J 6 HOH 138 595 595 HOH HOH B . J 6 HOH 139 605 605 HOH HOH B . J 6 HOH 140 614 614 HOH HOH B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 166 A ASN 169 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 25 A ASN 33 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 154 B ASN 154 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 31920 ? 1 MORE -104 ? 1 'SSA (A^2)' 61030 ? # 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 -35.3470000000 0.8660254038 -0.5000000000 0.0000000000 61.2227998951 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 -70.6940000000 -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 A HOH 613 ? I HOH . 2 1 B HOH 430 ? J HOH . 3 1 B HOH 485 ? J HOH . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2010-01-19 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2017-11-01 # _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' Advisory 2 2 'Structure model' 'Version format compliance' 3 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined -20.1590 6.9530 35.6230 -0.0554 -0.0397 0.0212 0.0151 -0.0069 -0.0072 0.3448 0.2721 0.5048 -0.0724 -0.0886 0.0730 0.0359 0.0240 0.0313 -0.0392 0.0012 -0.0106 0.0637 0.0593 -0.0370 'X-RAY DIFFRACTION' 2 ? refined -25.9580 12.8600 -16.9540 0.0722 0.0655 -0.0927 0.0596 0.0102 0.0206 0.3212 0.0501 6.2406 0.1225 -0.7731 -0.1726 -0.0915 0.0170 -0.0294 -0.0413 -0.0425 -0.0043 0.0839 0.4341 0.1340 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 326 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 B 1 ? ? B 172 ? ? ? ? # _pdbx_phasing_MR.entry_id 3KU5 _pdbx_phasing_MR.method_rotation ? _pdbx_phasing_MR.method_translation ? _pdbx_phasing_MR.model_details 'Phaser MODE: MR_AUTO' _pdbx_phasing_MR.R_factor ? _pdbx_phasing_MR.R_rigid_body ? _pdbx_phasing_MR.correlation_coeff_Fo_to_Fc ? _pdbx_phasing_MR.correlation_coeff_Io_to_Ic ? _pdbx_phasing_MR.d_res_high_rotation 2.500 _pdbx_phasing_MR.d_res_low_rotation 33.170 _pdbx_phasing_MR.d_res_high_translation 2.500 _pdbx_phasing_MR.d_res_low_translation 33.170 _pdbx_phasing_MR.packing ? _pdbx_phasing_MR.reflns_percent_rotation ? _pdbx_phasing_MR.reflns_percent_translation ? _pdbx_phasing_MR.sigma_F_rotation ? _pdbx_phasing_MR.sigma_F_translation ? _pdbx_phasing_MR.sigma_I_rotation ? _pdbx_phasing_MR.sigma_I_translation ? # _phasing.method MR # loop_ _software.pdbx_ordinal _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id 1 DENZO . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data reduction' http://www.hkl-xray.com/ ? ? 2 SCALEPACK . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data scaling' http://www.hkl-xray.com/ ? ? 3 PHASER 1.3.3 'Fri Oct 20 12:51:01 2006' program 'Randy J. Read' cimr-phaser@lists.cam.ac.uk phasing http://www-structmed.cimr.cam.ac.uk/phaser/ ? ? 4 REFMAC . ? program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 5 PDB_EXTRACT 3.005 'June 11, 2008' package PDB help@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 6 Blu-Ice . ? ? ? ? 'data collection' ? ? ? 7 HKL-2000 . ? ? ? ? 'data reduction' ? ? ? 8 HKL-2000 . ? ? ? ? 'data scaling' ? ? ? # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 561 ? ? 1_555 O A HOH 605 ? ? 3_555 2.12 2 1 O A HOH 538 ? ? 1_555 O A HOH 732 ? ? 3_555 2.19 # 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 GLN A 196 ? ? 62.61 -31.66 2 1 THR A 206 ? ? -124.62 -166.62 3 1 ASN A 250 ? ? 82.42 2.67 4 1 SER A 265 ? ? -139.35 -141.01 5 1 SER A 265 ? ? -142.00 -137.78 6 1 ALA B 5 ? ? -94.03 -63.85 7 1 THR B 61 ? ? -92.43 55.48 8 1 ARG B 127 ? ? 51.28 -130.71 9 1 ARG B 127 ? ? 51.20 -130.62 10 1 TYR B 141 ? ? -87.62 30.40 11 1 ASP B 145 ? ? -68.44 -172.88 # 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 325 ? A GLN 323 2 1 Y 1 A ILE 326 ? A ILE 324 3 1 Y 1 A GLU 327 ? A GLU 325 4 1 Y 1 A SER 328 ? A SER 326 5 1 Y 1 A ARG 329 ? A ARG 327 6 1 Y 1 B ILE 173 ? B ILE 173 7 1 Y 1 B LYS 174 ? B LYS 174 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 1,2-ETHANEDIOL EDO 5 'DI(HYDROXYETHYL)ETHER' PEG 6 water HOH #