data_4BSB # _entry.id 4BSB # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4BSB PDBE EBI-57235 WWPDB D_1290057235 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4BSA unspecified 'CRYSTAL STRUCTURE OF THE HAEMAGGLUTININ (WITH ASN-133 GLYCOSYLATION) FROM AN H7N9 INFLUENZA VIRUS ISOLATED FROM HUMANS' PDB 4BSC unspecified ;HUMAN H7N9 INFLUENZA VIRUS HAEMAGGLUTININ (WITH ASN-133 GLYCOSYLATION) IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'-SLN ; PDB 4BSD unspecified ;HUMAN H7N9 INFLUENZA VIRUS HAEMAGGLUTININ (WITH ASN-133 GLYCOSYLATION) IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'-SLN ; PDB 4BSE unspecified 'HUMAN H7N9 INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE LSTC' PDB 4BSF unspecified ;HUMAN H7N9 INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'-SLN ; PDB 4BSG unspecified 'CRYSTAL STRUCTURE OF AN H7N3 AVIAN INFLUENZA VIRUS HAEMAGGLUTININ' PDB 4BSH unspecified ;H7N3 AVIAN INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE 6'-SLN ; PDB 4BSI unspecified ;H7N3 AVIAN INFLUENZA VIRUS HAEMAGGLUTININ IN COMPLEX WITH AVIAN RECEPTOR ANALOGUE 3'-SLN ; # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4BSB _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2013-06-10 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Xiong, X.' 1 'Haire, L.F.' 2 'Martin, S.R.' 3 'Wharton, S.A.' 4 'Daniels, R.S.' 5 'Bennett, M.S.' 6 'McCauley, J.W.' 7 'Collins, P.J.' 8 'Walker, P.A.' 9 'Skehel, J.J.' 10 'Gamblin, S.J.' 11 # _citation.id primary _citation.title 'Receptor Binding by an H7N9 Influenza Virus from Humans' _citation.journal_abbrev Nature _citation.journal_volume 499 _citation.page_first 496 _citation.page_last ? _citation.year 2013 _citation.journal_id_ASTM NATUAS _citation.country UK _citation.journal_id_ISSN 0028-0836 _citation.journal_id_CSD 0006 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 23787694 _citation.pdbx_database_id_DOI 10.1038/NATURE12372 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Xiong, X.' 1 primary 'Martin, S.R.' 2 primary 'Haire, L.F.' 3 primary 'Wharton, S.A.' 4 primary 'Daniels, R.S.' 5 primary 'Bennett, M.S.' 6 primary 'Mccauley, J.W.' 7 primary 'Collins, P.J.' 8 primary 'Walker, P.A.' 9 primary 'Skehel, J.J.' 10 primary 'Gamblin, S.J.' 11 # _cell.entry_id 4BSB _cell.length_a 116.348 _cell.length_b 116.348 _cell.length_c 296.516 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 18 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4BSB _symmetry.space_group_name_H-M 'H 3 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 155 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man HEMAGGLUTININ 35037.613 1 ? ? 'HA1 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 19-339' ? 2 polymer man HEMAGGLUTININ 20442.463 1 ? ? 'HA2 OF TRYPSIN RELEASED ECTODOMAIN, RESIDUES 340-516' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 7 ? ? ? ? 4 non-polymer man 'O-SIALIC ACID' 309.270 1 ? ? ? ? 5 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 6 non-polymer syn 'SULFATE ION' 96.063 14 ? ? ? ? 7 water nat water 18.015 111 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'HAEMAGGLUTININ HA1' 2 'HAEMAGGLUTININ HA2' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;DKICLGHHALSNGTKVNTLTERGVEVVNATETVERTNIPRICSKGKRTVDLGQCGLLGTITGPPQCDQFLEFSADLIIER REGSDVCYPGKFVNEEALRQILRESGGIDKEAMGFTYSGIRTNGTTSACRRSGSSFYAEMKWLLSNTDNAAFPQMTKSYK NTRKSPALIVWGIHHSVSTAEQTKLYGSGNKLVTVGSSNYQQSFVPSPGARPQVNGLSGRIDFHWLMLNPNDTVTFSFNG AFIAPDRASFLRGKSMGIQSGVQVDANCEGDCYHSGGTIISNLPFQNIDSRAVGKCPRYVKQRSLLLATGMKNVPEIPKG R ; ;DKICLGHHALSNGTKVNTLTERGVEVVNATETVERTNIPRICSKGKRTVDLGQCGLLGTITGPPQCDQFLEFSADLIIER REGSDVCYPGKFVNEEALRQILRESGGIDKEAMGFTYSGIRTNGTTSACRRSGSSFYAEMKWLLSNTDNAAFPQMTKSYK NTRKSPALIVWGIHHSVSTAEQTKLYGSGNKLVTVGSSNYQQSFVPSPGARPQVNGLSGRIDFHWLMLNPNDTVTFSFNG AFIAPDRASFLRGKSMGIQSGVQVDANCEGDCYHSGGTIISNLPFQNIDSRAVGKCPRYVKQRSLLLATGMKNVPEIPKG R ; A ? 2 'polypeptide(L)' no no ;GLFGAIAGFIENGWEGLIDGWYGFRHQNAQGEGTAADYKSTQSAIDQITGKLNRLIEKTNQQFELIDNEFNEVEKQIGNV INWTRDSITEVWSYNAELLVAMENQHTIDLADSEMDKLYERVKRQLRENAEEDGTGCFEIFHKCDDDCMASIRNNTYDHS KYREEAMQNRIQIDPVK ; ;GLFGAIAGFIENGWEGLIDGWYGFRHQNAQGEGTAADYKSTQSAIDQITGKLNRLIEKTNQQFELIDNEFNEVEKQIGNV INWTRDSITEVWSYNAELLVAMENQHTIDLADSEMDKLYERVKRQLRENAEEDGTGCFEIFHKCDDDCMASIRNNTYDHS KYREEAMQNRIQIDPVK ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ASP n 1 2 LYS n 1 3 ILE n 1 4 CYS n 1 5 LEU n 1 6 GLY n 1 7 HIS n 1 8 HIS n 1 9 ALA n 1 10 LEU n 1 11 SER n 1 12 ASN n 1 13 GLY n 1 14 THR n 1 15 LYS n 1 16 VAL n 1 17 ASN n 1 18 THR n 1 19 LEU n 1 20 THR n 1 21 GLU n 1 22 ARG n 1 23 GLY n 1 24 VAL n 1 25 GLU n 1 26 VAL n 1 27 VAL n 1 28 ASN n 1 29 ALA n 1 30 THR n 1 31 GLU n 1 32 THR n 1 33 VAL n 1 34 GLU n 1 35 ARG n 1 36 THR n 1 37 ASN n 1 38 ILE n 1 39 PRO n 1 40 ARG n 1 41 ILE n 1 42 CYS n 1 43 SER n 1 44 LYS n 1 45 GLY n 1 46 LYS n 1 47 ARG n 1 48 THR n 1 49 VAL n 1 50 ASP n 1 51 LEU n 1 52 GLY n 1 53 GLN n 1 54 CYS n 1 55 GLY n 1 56 LEU n 1 57 LEU n 1 58 GLY n 1 59 THR n 1 60 ILE n 1 61 THR n 1 62 GLY n 1 63 PRO n 1 64 PRO n 1 65 GLN n 1 66 CYS n 1 67 ASP n 1 68 GLN n 1 69 PHE n 1 70 LEU n 1 71 GLU n 1 72 PHE n 1 73 SER n 1 74 ALA n 1 75 ASP n 1 76 LEU n 1 77 ILE n 1 78 ILE n 1 79 GLU n 1 80 ARG n 1 81 ARG n 1 82 GLU n 1 83 GLY n 1 84 SER n 1 85 ASP n 1 86 VAL n 1 87 CYS n 1 88 TYR n 1 89 PRO n 1 90 GLY n 1 91 LYS n 1 92 PHE n 1 93 VAL n 1 94 ASN n 1 95 GLU n 1 96 GLU n 1 97 ALA n 1 98 LEU n 1 99 ARG n 1 100 GLN n 1 101 ILE n 1 102 LEU n 1 103 ARG n 1 104 GLU n 1 105 SER n 1 106 GLY n 1 107 GLY n 1 108 ILE n 1 109 ASP n 1 110 LYS n 1 111 GLU n 1 112 ALA n 1 113 MET n 1 114 GLY n 1 115 PHE n 1 116 THR n 1 117 TYR n 1 118 SER n 1 119 GLY n 1 120 ILE n 1 121 ARG n 1 122 THR n 1 123 ASN n 1 124 GLY n 1 125 THR n 1 126 THR n 1 127 SER n 1 128 ALA n 1 129 CYS n 1 130 ARG n 1 131 ARG n 1 132 SER n 1 133 GLY n 1 134 SER n 1 135 SER n 1 136 PHE n 1 137 TYR n 1 138 ALA n 1 139 GLU n 1 140 MET n 1 141 LYS n 1 142 TRP n 1 143 LEU n 1 144 LEU n 1 145 SER n 1 146 ASN n 1 147 THR n 1 148 ASP n 1 149 ASN n 1 150 ALA n 1 151 ALA n 1 152 PHE n 1 153 PRO n 1 154 GLN n 1 155 MET n 1 156 THR n 1 157 LYS n 1 158 SER n 1 159 TYR n 1 160 LYS n 1 161 ASN n 1 162 THR n 1 163 ARG n 1 164 LYS n 1 165 SER n 1 166 PRO n 1 167 ALA n 1 168 LEU n 1 169 ILE n 1 170 VAL n 1 171 TRP n 1 172 GLY n 1 173 ILE n 1 174 HIS n 1 175 HIS n 1 176 SER n 1 177 VAL n 1 178 SER n 1 179 THR n 1 180 ALA n 1 181 GLU n 1 182 GLN n 1 183 THR n 1 184 LYS n 1 185 LEU n 1 186 TYR n 1 187 GLY n 1 188 SER n 1 189 GLY n 1 190 ASN n 1 191 LYS n 1 192 LEU n 1 193 VAL n 1 194 THR n 1 195 VAL n 1 196 GLY n 1 197 SER n 1 198 SER n 1 199 ASN n 1 200 TYR n 1 201 GLN n 1 202 GLN n 1 203 SER n 1 204 PHE n 1 205 VAL n 1 206 PRO n 1 207 SER n 1 208 PRO n 1 209 GLY n 1 210 ALA n 1 211 ARG n 1 212 PRO n 1 213 GLN n 1 214 VAL n 1 215 ASN n 1 216 GLY n 1 217 LEU n 1 218 SER n 1 219 GLY n 1 220 ARG n 1 221 ILE n 1 222 ASP n 1 223 PHE n 1 224 HIS n 1 225 TRP n 1 226 LEU n 1 227 MET n 1 228 LEU n 1 229 ASN n 1 230 PRO n 1 231 ASN n 1 232 ASP n 1 233 THR n 1 234 VAL n 1 235 THR n 1 236 PHE n 1 237 SER n 1 238 PHE n 1 239 ASN n 1 240 GLY n 1 241 ALA n 1 242 PHE n 1 243 ILE n 1 244 ALA n 1 245 PRO n 1 246 ASP n 1 247 ARG n 1 248 ALA n 1 249 SER n 1 250 PHE n 1 251 LEU n 1 252 ARG n 1 253 GLY n 1 254 LYS n 1 255 SER n 1 256 MET n 1 257 GLY n 1 258 ILE n 1 259 GLN n 1 260 SER n 1 261 GLY n 1 262 VAL n 1 263 GLN n 1 264 VAL n 1 265 ASP n 1 266 ALA n 1 267 ASN n 1 268 CYS n 1 269 GLU n 1 270 GLY n 1 271 ASP n 1 272 CYS n 1 273 TYR n 1 274 HIS n 1 275 SER n 1 276 GLY n 1 277 GLY n 1 278 THR n 1 279 ILE n 1 280 ILE n 1 281 SER n 1 282 ASN n 1 283 LEU n 1 284 PRO n 1 285 PHE n 1 286 GLN n 1 287 ASN n 1 288 ILE n 1 289 ASP n 1 290 SER n 1 291 ARG n 1 292 ALA n 1 293 VAL n 1 294 GLY n 1 295 LYS n 1 296 CYS n 1 297 PRO n 1 298 ARG n 1 299 TYR n 1 300 VAL n 1 301 LYS n 1 302 GLN n 1 303 ARG n 1 304 SER n 1 305 LEU n 1 306 LEU n 1 307 LEU n 1 308 ALA n 1 309 THR n 1 310 GLY n 1 311 MET n 1 312 LYS n 1 313 ASN n 1 314 VAL n 1 315 PRO n 1 316 GLU n 1 317 ILE n 1 318 PRO n 1 319 LYS n 1 320 GLY n 1 321 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 ASN n 2 13 GLY n 2 14 TRP n 2 15 GLU n 2 16 GLY n 2 17 LEU n 2 18 ILE n 2 19 ASP n 2 20 GLY n 2 21 TRP n 2 22 TYR n 2 23 GLY n 2 24 PHE n 2 25 ARG n 2 26 HIS n 2 27 GLN n 2 28 ASN n 2 29 ALA n 2 30 GLN n 2 31 GLY n 2 32 GLU n 2 33 GLY n 2 34 THR n 2 35 ALA n 2 36 ALA n 2 37 ASP n 2 38 TYR n 2 39 LYS n 2 40 SER n 2 41 THR n 2 42 GLN n 2 43 SER n 2 44 ALA n 2 45 ILE n 2 46 ASP n 2 47 GLN n 2 48 ILE n 2 49 THR n 2 50 GLY n 2 51 LYS n 2 52 LEU n 2 53 ASN n 2 54 ARG n 2 55 LEU n 2 56 ILE n 2 57 GLU n 2 58 LYS n 2 59 THR n 2 60 ASN n 2 61 GLN n 2 62 GLN n 2 63 PHE n 2 64 GLU n 2 65 LEU n 2 66 ILE n 2 67 ASP n 2 68 ASN n 2 69 GLU n 2 70 PHE n 2 71 ASN n 2 72 GLU n 2 73 VAL n 2 74 GLU n 2 75 LYS n 2 76 GLN n 2 77 ILE n 2 78 GLY n 2 79 ASN n 2 80 VAL n 2 81 ILE n 2 82 ASN n 2 83 TRP n 2 84 THR n 2 85 ARG n 2 86 ASP n 2 87 SER n 2 88 ILE n 2 89 THR n 2 90 GLU n 2 91 VAL n 2 92 TRP n 2 93 SER 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 ALA n 2 102 MET n 2 103 GLU n 2 104 ASN n 2 105 GLN n 2 106 HIS n 2 107 THR n 2 108 ILE n 2 109 ASP n 2 110 LEU n 2 111 ALA n 2 112 ASP n 2 113 SER n 2 114 GLU n 2 115 MET n 2 116 ASP n 2 117 LYS n 2 118 LEU n 2 119 TYR n 2 120 GLU n 2 121 ARG n 2 122 VAL n 2 123 LYS n 2 124 ARG n 2 125 GLN n 2 126 LEU n 2 127 ARG n 2 128 GLU n 2 129 ASN n 2 130 ALA n 2 131 GLU n 2 132 GLU n 2 133 ASP n 2 134 GLY n 2 135 THR n 2 136 GLY n 2 137 CYS n 2 138 PHE n 2 139 GLU n 2 140 ILE n 2 141 PHE n 2 142 HIS n 2 143 LYS n 2 144 CYS n 2 145 ASP n 2 146 ASP n 2 147 ASP n 2 148 CYS n 2 149 MET n 2 150 ALA n 2 151 SER n 2 152 ILE n 2 153 ARG n 2 154 ASN n 2 155 ASN n 2 156 THR n 2 157 TYR n 2 158 ASP n 2 159 HIS n 2 160 SER n 2 161 LYS n 2 162 TYR n 2 163 ARG n 2 164 GLU n 2 165 GLU n 2 166 ALA n 2 167 MET n 2 168 GLN n 2 169 ASN n 2 170 ARG n 2 171 ILE n 2 172 GLN n 2 173 ILE n 2 174 ASP n 2 175 PRO n 2 176 VAL n 2 177 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 ? ? ? ? ? ? ? ? ? ? ? ? 'INFLUENZA VIRUS A/ANHUI/1/2013 (H7N9)' 11320 ? ? ? ? ? ? ? 'FALL ARMYWORM' 'SPODOPTERA FRUGIPERDA' 7108 ? ? ? ? ? ? ? ? SF9 ? ? ? ? ? BACULOVIRUS ? ? ? PACGP67A ? 'WHO CHINESE NATIONAL INFLUENZA CENTER' 2 1 sample ? ? ? ? ? ? ? ? ? ? ? ? 'INFLUENZA VIRUS A/ANHUI/1/2013 (H7N9)' 11320 ? ? ? ? ? ? ? 'FALL ARMYWORM' 'SPODOPTERA FRUGIPERDA' 7108 ? ? ? ? ? ? ? ? SF9 ? ? ? ? ? BACULOVIRUS ? ? ? PACGP67A ? 'WHO CHINESE NATIONAL INFLUENZA CENTER' # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP M4YV75_9INFA 1 ? ? M4YV75 ? 2 UNP M4YV75_9INFA 2 ? ? M4YV75 ? # 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 4BSB A 1 ? 321 ? M4YV75 19 ? 339 ? 1 321 2 2 4BSB B 1 ? 177 ? M4YV75 340 ? 516 ? 1 177 # 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 4BSB LEU A 10 ? UNP M4YV75 VAL 28 'SEE REMARK 999' 10 1 1 4BSB THR A 125 ? UNP M4YV75 ALA 143 'SEE REMARK 999' 125 2 1 4BSB LEU A 217 ? UNP M4YV75 ILE 235 'SEE REMARK 999' 217 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 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SIA non-polymer . 'O-SIALIC ACID' ? 'C11 H19 N O9' 309.270 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 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 4BSB _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.55 _exptl_crystal.density_percent_sol 65 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH ? _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '291 K, 0.1 M PIPES PH 7.0, 2.2 M AMMONIUM SULFATE, 1% PEG 400' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'DECTRIS PILATUS 2M' _diffrn_detector.pdbx_collection_date ? _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.920 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04-1' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04-1 _diffrn_source.pdbx_wavelength 0.920 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4BSB _reflns.observed_criterion_sigma_I 2.43 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 41.67 _reflns.d_resolution_high 2.35 _reflns.number_obs 32536 _reflns.number_all ? _reflns.percent_possible_obs 99.8 _reflns.pdbx_Rmerge_I_obs 0.08 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 14.52 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 6.2 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.35 _reflns_shell.d_res_low 2.48 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.68 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.43 _reflns_shell.pdbx_redundancy 6.2 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4BSB _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 30884 _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 41.70 _refine.ls_d_res_high 2.35 _refine.ls_percent_reflns_obs 99.77 _refine.ls_R_factor_obs 0.23022 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.22839 _refine.ls_R_factor_R_free 0.26499 _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 1647 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.941 _refine.correlation_coeff_Fo_to_Fc_free 0.917 _refine.B_iso_mean 66.129 _refine.aniso_B[1][1] 0.59 _refine.aniso_B[2][2] 0.59 _refine.aniso_B[3][3] -1.91 _refine.aniso_B[1][2] 0.59 _refine.aniso_B[1][3] 0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED' _refine.pdbx_starting_model 'PDB ENTRY 1TI8' _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 0.291 _refine.pdbx_overall_ESU_R_Free 0.231 _refine.overall_SU_ML 0.185 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 15.348 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3795 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 200 _refine_hist.number_atoms_solvent 111 _refine_hist.number_atoms_total 4106 _refine_hist.d_res_high 2.35 _refine_hist.d_res_low 41.70 # 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 0.005 0.019 ? 4065 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3689 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.028 1.992 ? 5512 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.699 3.003 ? 8451 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.767 5.000 ? 484 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 35.612 24.513 ? 195 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 15.772 15.000 ? 665 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 13.844 15.000 ? 28 'X-RAY DIFFRACTION' ? r_chiral_restr 0.057 0.200 ? 616 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4563 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.001 0.020 ? 933 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.670 2.468 ? 1942 'X-RAY DIFFRACTION' ? r_mcbond_other 0.670 2.468 ? 1941 'X-RAY DIFFRACTION' ? r_mcangle_it 1.143 3.700 ? 2424 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 1.612 3.128 ? 2121 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.350 _refine_ls_shell.d_res_low 2.411 _refine_ls_shell.number_reflns_R_work 2251 _refine_ls_shell.R_factor_R_work 0.303 _refine_ls_shell.percent_reflns_obs 99.96 _refine_ls_shell.R_factor_R_free 0.350 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 111 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4BSB _struct.title 'Human H7N9 Influenza Virus Haemagglutinin (with Asn-133 Glycosylation) in Complex with Human Receptor Analogue LSTc' _struct.pdbx_descriptor HEMAGGLUTININ _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4BSB _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text 'VIRAL PROTEIN, FOWL PLAGUE VIRUS, SIALYLLACTOSAMINE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 3 ? E N N 3 ? F N N 3 ? G N N 4 ? H N N 5 ? I N N 3 ? J N N 6 ? K N N 6 ? L N N 6 ? M N N 6 ? N N N 6 ? O N N 6 ? P N N 6 ? Q N N 6 ? R N N 6 ? S N N 6 ? T N N 3 ? U N N 3 ? V N N 6 ? W N N 6 ? X N N 6 ? Y N N 6 ? Z N N 7 ? AA N N 7 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 LEU A 57 ? GLY A 62 ? LEU A 57 GLY A 62 1 ? 6 HELX_P HELX_P2 2 PRO A 63 ? LEU A 70 ? PRO A 63 LEU A 70 5 ? 8 HELX_P HELX_P3 3 ASN A 94 ? GLU A 104 ? ASN A 94 GLU A 104 1 ? 11 HELX_P HELX_P4 4 SER A 178 ? GLY A 187 ? SER A 178 GLY A 187 1 ? 10 HELX_P HELX_P5 5 GLY B 4 ? ILE B 10 ? GLY B 4 ILE B 10 1 ? 7 HELX_P HELX_P6 6 ASP B 37 ? ILE B 56 ? ASP B 37 ILE B 56 1 ? 20 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 ? ASN B 169 ? ASP B 158 ASN B 169 1 ? 12 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 4 SG ? ? ? 1_555 B CYS 137 SG ? ? A CYS 4 B CYS 137 1_555 ? ? ? ? ? ? ? 2.034 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 268 SG ? ? A CYS 42 A CYS 268 1_555 ? ? ? ? ? ? ? 2.059 ? disulf3 disulf ? ? A CYS 54 SG ? ? ? 1_555 A CYS 66 SG ? ? A CYS 54 A CYS 66 1_555 ? ? ? ? ? ? ? 2.048 ? disulf4 disulf ? ? A CYS 87 SG ? ? ? 1_555 A CYS 129 SG ? ? A CYS 87 A CYS 129 1_555 ? ? ? ? ? ? ? 2.049 ? disulf5 disulf ? ? A CYS 272 SG ? ? ? 1_555 A CYS 296 SG ? ? A CYS 272 A CYS 296 1_555 ? ? ? ? ? ? ? 2.067 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.040 ? covale1 covale ? ? A ASN 12 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 12 A NAG 1319 1_555 ? ? ? ? ? ? ? 1.456 ? covale2 covale ? ? A ASN 28 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 28 A NAG 1317 1_555 ? ? ? ? ? ? ? 1.454 ? covale3 covale ? ? A ASN 123 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 123 A NAG 1320 1_555 ? ? ? ? ? ? ? 1.459 ? covale4 covale ? ? A ASN 231 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 231 A NAG 1318 1_555 ? ? ? ? ? ? ? 1.447 ? covale5 covale ? ? H GAL . O6 ? ? ? 1_555 G SIA . C2 ? ? A GAL 1322 A SIA 1321 1_555 ? ? ? ? ? ? ? 1.427 ? covale6 covale ? ? H GAL . C1 ? ? ? 1_555 I NAG . O4 ? ? A GAL 1322 A NAG 1323 1_555 ? ? ? ? ? ? ? 1.434 ? covale7 covale ? ? B ASN 82 ND2 ? ? ? 1_555 T NAG . C1 ? ? B ASN 82 B NAG 1171 1_555 ? ? ? ? ? ? ? 1.452 ? covale8 covale ? ? T NAG . O4 ? ? ? 1_555 U NAG . C1 ? ? B NAG 1171 B NAG 1172 1_555 ? ? ? ? ? ? ? 1.445 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details BA ? 5 ? AA ? 2 ? AB ? 2 ? AC ? 3 ? AD ? 2 ? AE ? 3 ? AF ? 5 ? AG ? 5 ? AH ? 2 ? AI ? 2 ? AJ ? 4 ? AK ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel AA 1 2 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? parallel AC 2 3 ? parallel AD 1 2 ? parallel AE 1 2 ? parallel AE 2 3 ? parallel AF 1 2 ? parallel AF 2 3 ? anti-parallel AF 3 4 ? anti-parallel AF 4 5 ? parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? anti-parallel AI 1 2 ? anti-parallel AJ 1 2 ? anti-parallel AJ 2 3 ? anti-parallel AJ 3 4 ? anti-parallel AK 1 2 ? anti-parallel AK 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id BA 1 GLY B 31 ? ALA B 36 ? GLY B 31 ALA B 36 BA 2 TYR B 22 ? ASN B 28 ? TYR B 22 ASN B 28 BA 3 LYS A 2 ? HIS A 7 ? LYS A 2 HIS A 7 BA 4 CYS B 137 ? ILE B 140 ? CYS B 137 ILE B 140 BA 5 ALA B 130 ? GLU B 132 ? ALA B 130 GLU B 132 AA 1 THR A 14 ? VAL A 16 ? THR A 14 VAL A 16 AA 2 VAL A 24 ? VAL A 26 ? VAL A 24 VAL A 26 AB 1 ALA A 29 ? GLU A 31 ? ALA A 29 GLU A 31 AB 2 LEU A 306 ? ALA A 308 ? LEU A 306 ALA A 308 AC 1 VAL A 33 ? GLU A 34 ? VAL A 33 GLU A 34 AC 2 PHE A 285 ? GLN A 286 ? PHE A 285 GLN A 286 AC 3 ARG A 298 ? TYR A 299 ? ARG A 298 TYR A 299 AD 1 ILE A 41 ? CYS A 42 ? ILE A 41 CYS A 42 AD 2 VAL A 264 ? ASP A 265 ? VAL A 264 ASP A 265 AE 1 THR A 48 ? ASP A 50 ? THR A 48 ASP A 50 AE 2 LEU A 76 ? GLU A 79 ? LEU A 76 GLU A 79 AE 3 MET A 256 ? GLN A 259 ? MET A 256 GLN A 259 AF 1 GLY A 90 ? PHE A 92 ? GLY A 90 PHE A 92 AF 2 ARG A 220 ? LEU A 228 ? ARG A 220 LEU A 228 AF 3 ALA A 167 ? HIS A 175 ? ALA A 167 HIS A 175 AF 4 PHE A 242 ? PRO A 245 ? PHE A 242 PRO A 245 AF 5 MET A 140 ? TRP A 142 ? MET A 140 TRP A 142 AG 1 GLY A 90 ? PHE A 92 ? GLY A 90 PHE A 92 AG 2 ARG A 220 ? LEU A 228 ? ARG A 220 LEU A 228 AG 3 ALA A 167 ? HIS A 175 ? ALA A 167 HIS A 175 AG 4 ARG A 247 ? LEU A 251 ? ARG A 247 LEU A 251 AG 5 ILE A 108 ? ALA A 112 ? ILE A 108 ALA A 112 AH 1 ILE A 120 ? ARG A 121 ? ILE A 120 ARG A 121 AH 2 LEU A 144 ? SER A 145 ? LEU A 144 SER A 145 AI 1 THR A 126 ? ARG A 130 ? THR A 126 ARG A 130 AI 2 SER A 134 ? SER A 135 ? SER A 134 SER A 135 AJ 1 MET A 155 ? LYS A 160 ? MET A 155 LYS A 160 AJ 2 THR A 233 ? PHE A 238 ? THR A 233 PHE A 238 AJ 3 VAL A 193 ? SER A 197 ? VAL A 193 SER A 197 AJ 4 TYR A 200 ? PHE A 204 ? TYR A 200 PHE A 204 AK 1 GLY A 277 ? THR A 278 ? GLY A 277 THR A 278 AK 2 CYS A 272 ? HIS A 274 ? CYS A 272 HIS A 274 AK 3 VAL A 293 ? GLY A 294 ? VAL A 293 GLY A 294 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id BA 1 2 N ALA B 35 ? N ALA B 35 O PHE B 24 ? O PHE B 24 BA 2 3 N GLN B 27 ? N GLN B 27 O LYS A 2 ? O LYS A 2 BA 3 4 N ILE A 3 ? N ILE A 3 O PHE B 138 ? O PHE B 138 BA 4 5 N GLU B 139 ? N GLU B 139 O GLU B 131 ? O GLU B 131 AA 1 2 N VAL A 16 ? N VAL A 16 O VAL A 24 ? O VAL A 24 AB 1 2 N THR A 30 ? N THR A 30 O LEU A 307 ? O LEU A 307 AC 1 2 N GLU A 34 ? N GLU A 34 O PHE A 285 ? O PHE A 285 AC 2 3 N GLN A 286 ? N GLN A 286 O ARG A 298 ? O ARG A 298 AD 1 2 O ILE A 41 ? O ILE A 41 N ASP A 265 ? N ASP A 265 AE 1 2 N VAL A 49 ? N VAL A 49 O LEU A 76 ? O LEU A 76 AE 2 3 N ILE A 77 ? N ILE A 77 O MET A 256 ? O MET A 256 AF 1 2 N LYS A 91 ? N LYS A 91 O ILE A 221 ? O ILE A 221 AF 2 3 N LEU A 228 ? N LEU A 228 O ALA A 167 ? O ALA A 167 AF 3 4 N GLY A 172 ? N GLY A 172 O ILE A 243 ? O ILE A 243 AF 4 5 N ALA A 244 ? N ALA A 244 O LYS A 141 ? O LYS A 141 AG 1 2 N LYS A 91 ? N LYS A 91 O ILE A 221 ? O ILE A 221 AG 2 3 N LEU A 228 ? N LEU A 228 O ALA A 167 ? O ALA A 167 AG 3 4 N LEU A 168 ? N LEU A 168 O SER A 249 ? O SER A 249 AG 4 5 N PHE A 250 ? N PHE A 250 O ASP A 109 ? O ASP A 109 AH 1 2 N ARG A 121 ? N ARG A 121 O LEU A 144 ? O LEU A 144 AI 1 2 N THR A 126 ? N THR A 126 O SER A 135 ? O SER A 135 AJ 1 2 N TYR A 159 ? N TYR A 159 O VAL A 234 ? O VAL A 234 AJ 2 3 N SER A 237 ? N SER A 237 O THR A 194 ? O THR A 194 AJ 3 4 N SER A 197 ? N SER A 197 O TYR A 200 ? O TYR A 200 AK 1 2 N GLY A 277 ? N GLY A 277 O HIS A 274 ? O HIS A 274 AK 2 3 N TYR A 273 ? N TYR A 273 O VAL A 293 ? O VAL A 293 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1324' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 A 1325' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 A 1326' AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 1327' AC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 1328' AC6 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 1329' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1330' AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 1331' AC9 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 1332' BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1333' BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 1173' BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 1174' BC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 1175' BC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 B 1176' BC6 Software ? ? ? ? 2 'Binding site for Mono-Saccharide NAG A1319 bound to ASN A 12' BC7 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A1317 bound to ASN A 28' BC8 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1320 bound to ASN A 123' BC9 Software ? ? ? ? 1 'Binding site for Mono-Saccharide NAG A1318 bound to ASN A 231' CC1 Software ? ? ? ? 6 'Binding site for Poly-Saccharide residues NAG B1171 through NAG B1172 bound to ASN B 82' CC2 Software ? ? ? ? 7 'Binding site for Poly-Saccharide residues SIA A1321 through NAG A1323' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 4 TYR A 117 ? TYR A 117 . ? 1_555 ? 2 AC1 4 SER A 118 ? SER A 118 . ? 1_555 ? 3 AC1 4 GLY A 119 ? GLY A 119 . ? 1_555 ? 4 AC1 4 ILE A 120 ? ILE A 120 . ? 1_555 ? 5 AC2 2 ASN A 37 ? ASN A 37 . ? 1_555 ? 6 AC2 2 HOH Z . ? HOH A 2011 . ? 1_555 ? 7 AC3 2 ARG A 35 ? ARG A 35 . ? 1_555 ? 8 AC3 2 ARG A 303 ? ARG A 303 . ? 1_555 ? 9 AC4 3 PRO A 39 ? PRO A 39 . ? 1_555 ? 10 AC4 3 ARG A 40 ? ARG A 40 . ? 1_555 ? 11 AC4 3 HOH Z . ? HOH A 2080 . ? 1_555 ? 12 AC5 3 SER A 84 ? SER A 84 . ? 1_555 ? 13 AC5 3 ASP A 85 ? ASP A 85 . ? 1_555 ? 14 AC5 3 VAL A 86 ? VAL A 86 . ? 1_555 ? 15 AC6 3 ARG A 163 ? ARG A 163 . ? 1_555 ? 16 AC6 3 LYS A 164 ? LYS A 164 . ? 1_555 ? 17 AC6 3 SER A 165 ? SER A 165 . ? 1_555 ? 18 AC7 4 LYS A 110 ? LYS A 110 . ? 1_555 ? 19 AC7 4 GLU A 111 ? GLU A 111 . ? 1_555 ? 20 AC7 4 ALA A 112 ? ALA A 112 . ? 1_555 ? 21 AC7 4 ARG A 247 ? ARG A 247 . ? 1_555 ? 22 AC8 5 PHE A 92 ? PHE A 92 . ? 1_555 ? 23 AC8 5 ASN A 94 ? ASN A 94 . ? 1_555 ? 24 AC8 5 GLU A 95 ? GLU A 95 . ? 1_555 ? 25 AC8 5 HOH Z . ? HOH A 2029 . ? 1_555 ? 26 AC8 5 HOH Z . ? HOH A 2030 . ? 1_555 ? 27 AC9 3 THR A 20 ? THR A 20 . ? 1_555 ? 28 AC9 3 GLU A 21 ? GLU A 21 . ? 1_555 ? 29 AC9 3 ARG A 22 ? ARG A 22 . ? 1_555 ? 30 BC1 4 GLN A 302 ? GLN A 302 . ? 1_555 ? 31 BC1 4 ARG A 303 ? ARG A 303 . ? 1_555 ? 32 BC1 4 SER A 304 ? SER A 304 . ? 1_555 ? 33 BC1 4 HOH Z . ? HOH A 2081 . ? 1_555 ? 34 BC2 4 TRP B 14 ? TRP B 14 . ? 1_555 ? 35 BC2 4 GLU B 15 ? GLU B 15 . ? 1_555 ? 36 BC2 4 GLY B 16 ? GLY B 16 . ? 1_555 ? 37 BC2 4 ARG B 25 ? ARG B 25 . ? 1_555 ? 38 BC3 4 ASN A 199 ? ASN A 199 . ? 3_655 ? 39 BC3 4 ASN A 229 ? ASN A 229 . ? 3_655 ? 40 BC3 4 ASN B 71 ? ASN B 71 . ? 1_555 ? 41 BC3 4 GLU B 72 ? GLU B 72 . ? 1_555 ? 42 BC4 4 THR B 59 ? THR B 59 . ? 3_655 ? 43 BC4 4 SER B 93 ? SER B 93 . ? 1_555 ? 44 BC4 4 TYR B 94 ? TYR B 94 . ? 1_555 ? 45 BC4 4 GLU B 97 ? GLU B 97 . ? 1_555 ? 46 BC5 2 LYS B 123 ? LYS B 123 . ? 3_655 ? 47 BC5 2 LYS B 123 ? LYS B 123 . ? 2_545 ? 48 BC6 2 ASN A 12 ? ASN A 12 . ? 1_555 ? 49 BC6 2 GLY A 13 ? GLY A 13 . ? 1_555 ? 50 BC7 3 ASN A 28 ? ASN A 28 . ? 1_555 ? 51 BC7 3 THR A 30 ? THR A 30 . ? 1_555 ? 52 BC7 3 HOH Z . ? HOH A 2078 . ? 1_555 ? 53 BC8 1 ASN A 123 ? ASN A 123 . ? 1_555 ? 54 BC9 1 ASN A 231 ? ASN A 231 . ? 1_555 ? 55 CC1 6 HOH Z . ? HOH A 2066 . ? 1_555 ? 56 CC1 6 GLU B 72 ? GLU B 72 . ? 1_555 ? 57 CC1 6 LYS B 75 ? LYS B 75 . ? 1_555 ? 58 CC1 6 ASN B 79 ? ASN B 79 . ? 1_555 ? 59 CC1 6 ASN B 82 ? ASN B 82 . ? 1_555 ? 60 CC1 6 HOH AA . ? HOH B 2013 . ? 1_555 ? 61 CC2 7 TYR A 88 ? TYR A 88 . ? 1_555 ? 62 CC2 7 THR A 125 ? THR A 125 . ? 1_555 ? 63 CC2 7 THR A 126 ? THR A 126 . ? 1_555 ? 64 CC2 7 SER A 127 ? SER A 127 . ? 1_555 ? 65 CC2 7 HIS A 174 ? HIS A 174 . ? 1_555 ? 66 CC2 7 LEU A 185 ? LEU A 185 . ? 1_555 ? 67 CC2 7 HOH Z . ? HOH A 2044 . ? 1_555 ? # _database_PDB_matrix.entry_id 4BSB _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 4BSB _atom_sites.fract_transf_matrix[1][1] 0.008595 _atom_sites.fract_transf_matrix[1][2] 0.004962 _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] 0.009925 _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] 0.003372 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ASP A 1 1 ? 38.893 -29.429 -68.889 1.00 105.12 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 40.317 -29.008 -69.018 1.00 103.86 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 41.154 -29.267 -67.744 1.00 101.12 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 42.375 -29.386 -67.842 1.00 100.61 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 40.392 -27.524 -69.409 1.00 104.33 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 41.567 -27.211 -70.327 1.00 104.94 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 42.664 -27.762 -70.122 1.00 103.04 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 41.390 -26.410 -71.267 1.00 107.12 ? 1 ASP A OD2 1 ATOM 9 N N . LYS A 1 2 ? 40.529 -29.362 -66.565 1.00 99.62 ? 2 LYS A N 1 ATOM 10 C CA . LYS A 1 2 ? 41.306 -29.497 -65.316 1.00 96.88 ? 2 LYS A CA 1 ATOM 11 C C . LYS A 1 2 ? 40.623 -30.226 -64.151 1.00 94.75 ? 2 LYS A C 1 ATOM 12 O O . LYS A 1 2 ? 39.415 -30.462 -64.164 1.00 95.62 ? 2 LYS A O 1 ATOM 13 C CB . LYS A 1 2 ? 41.756 -28.111 -64.832 1.00 96.48 ? 2 LYS A CB 1 ATOM 14 C CG . LYS A 1 2 ? 40.654 -27.280 -64.189 1.00 96.95 ? 2 LYS A CG 1 ATOM 15 C CD . LYS A 1 2 ? 41.094 -25.847 -63.933 1.00 97.05 ? 2 LYS A CD 1 ATOM 16 C CE . LYS A 1 2 ? 40.056 -25.094 -63.111 1.00 97.07 ? 2 LYS A CE 1 ATOM 17 N NZ . LYS A 1 2 ? 40.293 -23.624 -63.105 1.00 97.77 ? 2 LYS A NZ 1 ATOM 18 N N . ILE A 1 3 ? 41.434 -30.567 -63.145 1.00 92.10 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 40.964 -31.151 -61.876 1.00 89.82 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 41.784 -30.606 -60.697 1.00 87.33 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 43.013 -30.724 -60.679 1.00 86.12 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 41.016 -32.699 -61.892 1.00 89.40 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 40.342 -33.273 -60.642 1.00 87.35 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 42.447 -33.215 -62.016 1.00 88.39 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 40.222 -34.781 -60.653 1.00 87.46 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 41.100 -30.007 -59.721 1.00 86.68 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 41.760 -29.341 -58.593 1.00 84.65 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 41.646 -30.152 -57.302 1.00 82.13 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 40.634 -30.813 -57.062 1.00 82.57 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 41.161 -27.948 -58.358 1.00 85.48 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 41.513 -26.656 -59.584 1.00 88.98 ? 4 CYS A SG 1 ATOM 32 N N . LEU A 1 5 ? 42.693 -30.078 -56.479 1.00 79.63 ? 5 LEU A N 1 ATOM 33 C CA . LEU A 1 5 ? 42.717 -30.697 -55.147 1.00 77.06 ? 5 LEU A CA 1 ATOM 34 C C . LEU A 1 5 ? 42.503 -29.631 -54.071 1.00 75.31 ? 5 LEU A C 1 ATOM 35 O O . LEU A 1 5 ? 43.043 -28.527 -54.160 1.00 75.58 ? 5 LEU A O 1 ATOM 36 C CB . LEU A 1 5 ? 44.059 -31.394 -54.893 1.00 75.59 ? 5 LEU A CB 1 ATOM 37 C CG . LEU A 1 5 ? 44.281 -32.787 -55.483 1.00 76.27 ? 5 LEU A CG 1 ATOM 38 C CD1 . LEU A 1 5 ? 43.348 -33.805 -54.845 1.00 75.65 ? 5 LEU A CD1 1 ATOM 39 C CD2 . LEU A 1 5 ? 44.119 -32.773 -56.993 1.00 78.60 ? 5 LEU A CD2 1 ATOM 40 N N . GLY A 1 6 ? 41.724 -29.971 -53.051 1.00 73.67 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 41.479 -29.060 -51.940 1.00 71.94 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 41.192 -29.797 -50.652 1.00 69.61 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 41.241 -31.026 -50.597 1.00 69.13 ? 6 GLY A O 1 ATOM 44 N N . HIS A 1 7 ? 40.891 -29.025 -49.615 1.00 68.22 ? 7 HIS A N 1 ATOM 45 C CA . HIS A 1 7 ? 40.600 -29.550 -48.289 1.00 65.89 ? 7 HIS A CA 1 ATOM 46 C C . HIS A 1 7 ? 39.435 -28.761 -47.715 1.00 66.05 ? 7 HIS A C 1 ATOM 47 O O . HIS A 1 7 ? 39.102 -27.694 -48.225 1.00 67.53 ? 7 HIS A O 1 ATOM 48 C CB . HIS A 1 7 ? 41.823 -29.405 -47.384 1.00 63.82 ? 7 HIS A CB 1 ATOM 49 C CG . HIS A 1 7 ? 42.325 -27.999 -47.282 1.00 63.67 ? 7 HIS A CG 1 ATOM 50 N ND1 . HIS A 1 7 ? 41.828 -27.093 -46.369 1.00 63.10 ? 7 HIS A ND1 1 ATOM 51 C CD2 . HIS A 1 7 ? 43.262 -27.335 -47.997 1.00 64.34 ? 7 HIS A CD2 1 ATOM 52 C CE1 . HIS A 1 7 ? 42.449 -25.937 -46.517 1.00 63.51 ? 7 HIS A CE1 1 ATOM 53 N NE2 . HIS A 1 7 ? 43.323 -26.056 -47.499 1.00 64.38 ? 7 HIS A NE2 1 ATOM 54 N N . HIS A 1 8 ? 38.822 -29.279 -46.656 1.00 64.77 ? 8 HIS A N 1 ATOM 55 C CA . HIS A 1 8 ? 37.646 -28.631 -46.074 1.00 65.53 ? 8 HIS A CA 1 ATOM 56 C C . HIS A 1 8 ? 38.029 -27.430 -45.206 1.00 65.30 ? 8 HIS A C 1 ATOM 57 O O . HIS A 1 8 ? 39.199 -27.254 -44.843 1.00 63.80 ? 8 HIS A O 1 ATOM 58 C CB . HIS A 1 8 ? 36.772 -29.646 -45.313 1.00 64.65 ? 8 HIS A CB 1 ATOM 59 C CG . HIS A 1 8 ? 37.351 -30.119 -44.014 1.00 61.90 ? 8 HIS A CG 1 ATOM 60 N ND1 . HIS A 1 8 ? 36.587 -30.740 -43.051 1.00 60.98 ? 8 HIS A ND1 1 ATOM 61 C CD2 . HIS A 1 8 ? 38.609 -30.063 -43.515 1.00 60.48 ? 8 HIS A CD2 1 ATOM 62 C CE1 . HIS A 1 8 ? 37.347 -31.047 -42.015 1.00 58.94 ? 8 HIS A CE1 1 ATOM 63 N NE2 . HIS A 1 8 ? 38.579 -30.645 -42.270 1.00 58.52 ? 8 HIS A NE2 1 ATOM 64 N N . ALA A 1 9 ? 37.036 -26.602 -44.895 1.00 66.84 ? 9 ALA A N 1 ATOM 65 C CA . ALA A 1 9 ? 37.257 -25.385 -44.122 1.00 67.14 ? 9 ALA A CA 1 ATOM 66 C C . ALA A 1 9 ? 35.946 -24.837 -43.573 1.00 69.18 ? 9 ALA A C 1 ATOM 67 O O . ALA A 1 9 ? 34.864 -25.228 -44.010 1.00 70.75 ? 9 ALA A O 1 ATOM 68 C CB . ALA A 1 9 ? 37.951 -24.335 -44.978 1.00 68.18 ? 9 ALA A CB 1 ATOM 69 N N . LEU A 1 10 ? 36.059 -23.934 -42.605 1.00 69.70 ? 10 LEU A N 1 ATOM 70 C CA . LEU A 1 10 ? 34.905 -23.271 -42.012 1.00 71.43 ? 10 LEU A CA 1 ATOM 71 C C . LEU A 1 10 ? 35.131 -21.775 -42.060 1.00 73.48 ? 10 LEU A C 1 ATOM 72 O O . LEU A 1 10 ? 36.259 -21.321 -42.218 1.00 72.48 ? 10 LEU A O 1 ATOM 73 C CB . LEU A 1 10 ? 34.727 -23.706 -40.559 1.00 69.68 ? 10 LEU A CB 1 ATOM 74 C CG . LEU A 1 10 ? 34.681 -25.209 -40.287 1.00 68.40 ? 10 LEU A CG 1 ATOM 75 C CD1 . LEU A 1 10 ? 34.810 -25.481 -38.795 1.00 66.41 ? 10 LEU A CD1 1 ATOM 76 C CD2 . LEU A 1 10 ? 33.404 -25.817 -40.844 1.00 69.96 ? 10 LEU A CD2 1 ATOM 77 N N . SER A 1 11 ? 34.052 -21.014 -41.932 1.00 77.83 ? 11 SER A N 1 ATOM 78 C CA . SER A 1 11 ? 34.141 -19.565 -41.782 1.00 81.26 ? 11 SER A CA 1 ATOM 79 C C . SER A 1 11 ? 34.951 -19.226 -40.533 1.00 82.30 ? 11 SER A C 1 ATOM 80 O O . SER A 1 11 ? 35.836 -18.370 -40.571 1.00 83.26 ? 11 SER A O 1 ATOM 81 C CB . SER A 1 11 ? 32.742 -18.957 -41.669 1.00 83.07 ? 11 SER A CB 1 ATOM 82 O OG . SER A 1 11 ? 32.800 -17.613 -41.226 1.00 84.40 ? 11 SER A OG 1 ATOM 83 N N . ASN A 1 12 ? 34.633 -19.917 -39.437 1.00 83.25 ? 12 ASN A N 1 ATOM 84 C CA . ASN A 1 12 ? 35.269 -19.714 -38.142 1.00 84.08 ? 12 ASN A CA 1 ATOM 85 C C . ASN A 1 12 ? 35.835 -21.022 -37.597 1.00 78.61 ? 12 ASN A C 1 ATOM 86 O O . ASN A 1 12 ? 35.139 -22.042 -37.573 1.00 77.70 ? 12 ASN A O 1 ATOM 87 C CB . ASN A 1 12 ? 34.241 -19.174 -37.139 1.00 90.31 ? 12 ASN A CB 1 ATOM 88 C CG . ASN A 1 12 ? 34.405 -17.695 -36.851 1.00 97.66 ? 12 ASN A CG 1 ATOM 89 O OD1 . ASN A 1 12 ? 35.365 -17.072 -37.308 1.00 97.96 ? 12 ASN A OD1 1 ATOM 90 N ND2 . ASN A 1 12 ? 33.478 -17.116 -36.078 1.00 107.01 ? 12 ASN A ND2 1 ATOM 91 N N . GLY A 1 13 ? 37.087 -20.980 -37.143 1.00 73.71 ? 13 GLY A N 1 ATOM 92 C CA . GLY A 1 13 ? 37.737 -22.143 -36.537 1.00 69.90 ? 13 GLY A CA 1 ATOM 93 C C . GLY A 1 13 ? 37.793 -22.046 -35.022 1.00 66.63 ? 13 GLY A C 1 ATOM 94 O O . GLY A 1 13 ? 37.143 -21.191 -34.417 1.00 66.67 ? 13 GLY A O 1 ATOM 95 N N . THR A 1 14 ? 38.572 -22.930 -34.408 1.00 62.61 ? 14 THR A N 1 ATOM 96 C CA . THR A 1 14 ? 38.802 -22.884 -32.971 1.00 59.13 ? 14 THR A CA 1 ATOM 97 C C . THR A 1 14 ? 40.282 -22.588 -32.729 1.00 56.75 ? 14 THR A C 1 ATOM 98 O O . THR A 1 14 ? 41.155 -23.318 -33.211 1.00 55.27 ? 14 THR A O 1 ATOM 99 C CB . THR A 1 14 ? 38.396 -24.206 -32.300 1.00 58.12 ? 14 THR A CB 1 ATOM 100 O OG1 . THR A 1 14 ? 37.101 -24.604 -32.766 1.00 59.92 ? 14 THR A OG1 1 ATOM 101 C CG2 . THR A 1 14 ? 38.352 -24.054 -30.786 1.00 57.18 ? 14 THR A CG2 1 ATOM 102 N N . LYS A 1 15 ? 40.559 -21.512 -31.995 1.00 55.21 ? 15 LYS A N 1 ATOM 103 C CA . LYS A 1 15 ? 41.937 -21.121 -31.696 1.00 54.41 ? 15 LYS A CA 1 ATOM 104 C C . LYS A 1 15 ? 42.616 -22.130 -30.766 1.00 51.29 ? 15 LYS A C 1 ATOM 105 O O . LYS A 1 15 ? 42.019 -22.591 -29.794 1.00 49.68 ? 15 LYS A O 1 ATOM 106 C CB . LYS A 1 15 ? 41.993 -19.726 -31.069 1.00 56.27 ? 15 LYS A CB 1 ATOM 107 C CG . LYS A 1 15 ? 41.801 -18.599 -32.065 1.00 59.51 ? 15 LYS A CG 1 ATOM 108 C CD . LYS A 1 15 ? 41.769 -17.233 -31.399 1.00 61.74 ? 15 LYS A CD 1 ATOM 109 C CE . LYS A 1 15 ? 40.522 -17.053 -30.543 1.00 63.07 ? 15 LYS A CE 1 ATOM 110 N NZ . LYS A 1 15 ? 40.037 -15.641 -30.551 1.00 65.73 ? 15 LYS A NZ 1 ATOM 111 N N . VAL A 1 16 ? 43.860 -22.471 -31.099 1.00 49.23 ? 16 VAL A N 1 ATOM 112 C CA . VAL A 1 16 ? 44.711 -23.327 -30.276 1.00 46.64 ? 16 VAL A CA 1 ATOM 113 C C . VAL A 1 16 ? 46.148 -22.817 -30.359 1.00 46.85 ? 16 VAL A C 1 ATOM 114 O O . VAL A 1 16 ? 46.490 -22.020 -31.243 1.00 47.11 ? 16 VAL A O 1 ATOM 115 C CB . VAL A 1 16 ? 44.678 -24.806 -30.727 1.00 45.49 ? 16 VAL A CB 1 ATOM 116 C CG1 . VAL A 1 16 ? 43.293 -25.399 -30.546 1.00 45.29 ? 16 VAL A CG1 1 ATOM 117 C CG2 . VAL A 1 16 ? 45.112 -24.952 -32.176 1.00 46.53 ? 16 VAL A CG2 1 ATOM 118 N N . ASN A 1 17 ? 46.986 -23.296 -29.443 1.00 45.56 ? 17 ASN A N 1 ATOM 119 C CA . ASN A 1 17 ? 48.395 -22.922 -29.400 1.00 45.71 ? 17 ASN A CA 1 ATOM 120 C C . ASN A 1 17 ? 49.283 -24.049 -29.914 1.00 44.10 ? 17 ASN A C 1 ATOM 121 O O . ASN A 1 17 ? 48.920 -25.214 -29.827 1.00 43.77 ? 17 ASN A O 1 ATOM 122 C CB . ASN A 1 17 ? 48.784 -22.547 -27.968 1.00 46.11 ? 17 ASN A CB 1 ATOM 123 C CG . ASN A 1 17 ? 47.959 -21.393 -27.422 1.00 47.65 ? 17 ASN A CG 1 ATOM 124 O OD1 . ASN A 1 17 ? 47.625 -20.446 -28.141 1.00 49.77 ? 17 ASN A OD1 1 ATOM 125 N ND2 . ASN A 1 17 ? 47.626 -21.465 -26.145 1.00 47.14 ? 17 ASN A ND2 1 ATOM 126 N N . THR A 1 18 ? 50.438 -23.692 -30.462 1.00 43.86 ? 18 THR A N 1 ATOM 127 C CA . THR A 1 18 ? 51.413 -24.664 -30.952 1.00 43.26 ? 18 THR A CA 1 ATOM 128 C C . THR A 1 18 ? 52.776 -24.284 -30.403 1.00 43.87 ? 18 THR A C 1 ATOM 129 O O . THR A 1 18 ? 52.865 -23.402 -29.562 1.00 44.26 ? 18 THR A O 1 ATOM 130 C CB . THR A 1 18 ? 51.462 -24.695 -32.495 1.00 44.01 ? 18 THR A CB 1 ATOM 131 O OG1 . THR A 1 18 ? 52.074 -23.498 -32.994 1.00 44.54 ? 18 THR A OG1 1 ATOM 132 C CG2 . THR A 1 18 ? 50.063 -24.831 -33.067 1.00 44.22 ? 18 THR A CG2 1 ATOM 133 N N . LEU A 1 19 ? 53.834 -24.947 -30.863 1.00 45.05 ? 19 LEU A N 1 ATOM 134 C CA . LEU A 1 19 ? 55.189 -24.595 -30.448 1.00 46.44 ? 19 LEU A CA 1 ATOM 135 C C . LEU A 1 19 ? 55.576 -23.246 -31.011 1.00 49.29 ? 19 LEU A C 1 ATOM 136 O O . LEU A 1 19 ? 56.306 -22.478 -30.386 1.00 50.35 ? 19 LEU A O 1 ATOM 137 C CB . LEU A 1 19 ? 56.197 -25.634 -30.938 1.00 46.66 ? 19 LEU A CB 1 ATOM 138 C CG . LEU A 1 19 ? 56.068 -27.059 -30.404 1.00 45.62 ? 19 LEU A CG 1 ATOM 139 C CD1 . LEU A 1 19 ? 57.109 -27.928 -31.087 1.00 46.24 ? 19 LEU A CD1 1 ATOM 140 C CD2 . LEU A 1 19 ? 56.219 -27.119 -28.887 1.00 44.69 ? 19 LEU A CD2 1 ATOM 141 N N . THR A 1 20 ? 55.081 -22.985 -32.211 1.00 51.47 ? 20 THR A N 1 ATOM 142 C CA . THR A 1 20 ? 55.430 -21.806 -32.972 1.00 54.68 ? 20 THR A CA 1 ATOM 143 C C . THR A 1 20 ? 54.508 -20.631 -32.674 1.00 56.77 ? 20 THR A C 1 ATOM 144 O O . THR A 1 20 ? 54.956 -19.484 -32.681 1.00 57.76 ? 20 THR A O 1 ATOM 145 C CB . THR A 1 20 ? 55.353 -22.127 -34.477 1.00 55.61 ? 20 THR A CB 1 ATOM 146 O OG1 . THR A 1 20 ? 56.534 -22.840 -34.860 1.00 56.30 ? 20 THR A OG1 1 ATOM 147 C CG2 . THR A 1 20 ? 55.253 -20.873 -35.307 1.00 58.22 ? 20 THR A CG2 1 ATOM 148 N N . GLU A 1 21 ? 53.231 -20.912 -32.409 1.00 56.90 ? 21 GLU A N 1 ATOM 149 C CA . GLU A 1 21 ? 52.198 -19.893 -32.553 1.00 59.03 ? 21 GLU A CA 1 ATOM 150 C C . GLU A 1 21 ? 51.146 -19.910 -31.451 1.00 58.00 ? 21 GLU A C 1 ATOM 151 O O . GLU A 1 21 ? 50.734 -20.971 -30.986 1.00 56.22 ? 21 GLU A O 1 ATOM 152 C CB . GLU A 1 21 ? 51.521 -20.080 -33.910 1.00 61.04 ? 21 GLU A CB 1 ATOM 153 C CG . GLU A 1 21 ? 50.777 -18.860 -34.424 1.00 64.04 ? 21 GLU A CG 1 ATOM 154 C CD . GLU A 1 21 ? 50.434 -18.952 -35.907 1.00 66.34 ? 21 GLU A CD 1 ATOM 155 O OE1 . GLU A 1 21 ? 51.105 -19.709 -36.648 1.00 66.96 ? 21 GLU A OE1 1 ATOM 156 O OE2 . GLU A 1 21 ? 49.492 -18.253 -36.337 1.00 68.65 ? 21 GLU A OE2 1 ATOM 157 N N . ARG A 1 22 ? 50.726 -18.719 -31.039 1.00 58.97 ? 22 ARG A N 1 ATOM 158 C CA . ARG A 1 22 ? 49.571 -18.561 -30.166 1.00 59.67 ? 22 ARG A CA 1 ATOM 159 C C . ARG A 1 22 ? 48.334 -18.319 -31.014 1.00 59.04 ? 22 ARG A C 1 ATOM 160 O O . ARG A 1 22 ? 48.341 -17.460 -31.888 1.00 59.41 ? 22 ARG A O 1 ATOM 161 C CB . ARG A 1 22 ? 49.753 -17.375 -29.211 1.00 62.84 ? 22 ARG A CB 1 ATOM 162 C CG . ARG A 1 22 ? 50.473 -17.709 -27.915 1.00 64.25 ? 22 ARG A CG 1 ATOM 163 C CD . ARG A 1 22 ? 49.863 -16.981 -26.724 1.00 67.57 ? 22 ARG A CD 1 ATOM 164 N NE . ARG A 1 22 ? 49.799 -17.864 -25.558 1.00 69.38 ? 22 ARG A NE 1 ATOM 165 C CZ . ARG A 1 22 ? 48.939 -17.745 -24.546 1.00 71.81 ? 22 ARG A CZ 1 ATOM 166 N NH1 . ARG A 1 22 ? 48.034 -16.765 -24.513 1.00 73.76 ? 22 ARG A NH1 1 ATOM 167 N NH2 . ARG A 1 22 ? 48.983 -18.626 -23.551 1.00 71.70 ? 22 ARG A NH2 1 ATOM 168 N N . GLY A 1 23 ? 47.277 -19.077 -30.756 1.00 57.00 ? 23 GLY A N 1 ATOM 169 C CA . GLY A 1 23 ? 45.966 -18.790 -31.329 1.00 56.82 ? 23 GLY A CA 1 ATOM 170 C C . GLY A 1 23 ? 45.790 -19.052 -32.812 1.00 56.69 ? 23 GLY A C 1 ATOM 171 O O . GLY A 1 23 ? 45.091 -18.305 -33.487 1.00 58.27 ? 23 GLY A O 1 ATOM 172 N N . VAL A 1 24 ? 46.415 -20.104 -33.333 1.00 55.22 ? 24 VAL A N 1 ATOM 173 C CA . VAL A 1 24 ? 46.123 -20.534 -34.700 1.00 55.50 ? 24 VAL A CA 1 ATOM 174 C C . VAL A 1 24 ? 44.759 -21.225 -34.713 1.00 54.81 ? 24 VAL A C 1 ATOM 175 O O . VAL A 1 24 ? 44.441 -22.004 -33.808 1.00 52.68 ? 24 VAL A O 1 ATOM 176 C CB . VAL A 1 24 ? 47.220 -21.443 -35.314 1.00 55.04 ? 24 VAL A CB 1 ATOM 177 C CG1 . VAL A 1 24 ? 47.461 -22.696 -34.489 1.00 53.36 ? 24 VAL A CG1 1 ATOM 178 C CG2 . VAL A 1 24 ? 46.855 -21.822 -36.743 1.00 56.06 ? 24 VAL A CG2 1 ATOM 179 N N . GLU A 1 25 ? 43.946 -20.923 -35.722 1.00 55.65 ? 25 GLU A N 1 ATOM 180 C CA . GLU A 1 25 ? 42.610 -21.506 -35.810 1.00 55.83 ? 25 GLU A CA 1 ATOM 181 C C . GLU A 1 25 ? 42.640 -22.826 -36.564 1.00 54.84 ? 25 GLU A C 1 ATOM 182 O O . GLU A 1 25 ? 43.283 -22.946 -37.610 1.00 55.87 ? 25 GLU A O 1 ATOM 183 C CB . GLU A 1 25 ? 41.619 -20.538 -36.461 1.00 58.21 ? 25 GLU A CB 1 ATOM 184 C CG . GLU A 1 25 ? 41.190 -19.409 -35.536 1.00 59.32 ? 25 GLU A CG 1 ATOM 185 C CD . GLU A 1 25 ? 40.043 -18.583 -36.095 1.00 61.98 ? 25 GLU A CD 1 ATOM 186 O OE1 . GLU A 1 25 ? 39.217 -19.134 -36.860 1.00 62.99 ? 25 GLU A OE1 1 ATOM 187 O OE2 . GLU A 1 25 ? 39.965 -17.380 -35.760 1.00 62.72 ? 25 GLU A OE2 1 ATOM 188 N N . VAL A 1 26 ? 41.936 -23.809 -36.018 1.00 53.69 ? 26 VAL A N 1 ATOM 189 C CA . VAL A 1 26 ? 41.844 -25.137 -36.614 1.00 53.70 ? 26 VAL A CA 1 ATOM 190 C C . VAL A 1 26 ? 40.382 -25.524 -36.790 1.00 55.03 ? 26 VAL A C 1 ATOM 191 O O . VAL A 1 26 ? 39.491 -24.881 -36.236 1.00 55.21 ? 26 VAL A O 1 ATOM 192 C CB . VAL A 1 26 ? 42.566 -26.197 -35.759 1.00 51.73 ? 26 VAL A CB 1 ATOM 193 C CG1 . VAL A 1 26 ? 44.074 -26.013 -35.846 1.00 51.11 ? 26 VAL A CG1 1 ATOM 194 C CG2 . VAL A 1 26 ? 42.098 -26.146 -34.308 1.00 50.57 ? 26 VAL A CG2 1 ATOM 195 N N . VAL A 1 27 ? 40.144 -26.582 -37.553 1.00 56.20 ? 27 VAL A N 1 ATOM 196 C CA . VAL A 1 27 ? 38.789 -26.965 -37.922 1.00 58.20 ? 27 VAL A CA 1 ATOM 197 C C . VAL A 1 27 ? 38.003 -27.471 -36.715 1.00 57.94 ? 27 VAL A C 1 ATOM 198 O O . VAL A 1 27 ? 36.846 -27.102 -36.533 1.00 58.04 ? 27 VAL A O 1 ATOM 199 C CB . VAL A 1 27 ? 38.789 -28.009 -39.057 1.00 59.01 ? 27 VAL A CB 1 ATOM 200 C CG1 . VAL A 1 27 ? 37.375 -28.503 -39.343 1.00 60.08 ? 27 VAL A CG1 1 ATOM 201 C CG2 . VAL A 1 27 ? 39.395 -27.407 -40.316 1.00 60.36 ? 27 VAL A CG2 1 ATOM 202 N N . ASN A 1 28 ? 38.631 -28.310 -35.898 1.00 58.48 ? 28 ASN A N 1 ATOM 203 C CA . ASN A 1 28 ? 38.016 -28.785 -34.661 1.00 59.38 ? 28 ASN A CA 1 ATOM 204 C C . ASN A 1 28 ? 39.060 -28.981 -33.552 1.00 55.32 ? 28 ASN A C 1 ATOM 205 O O . ASN A 1 28 ? 40.221 -29.272 -33.830 1.00 53.78 ? 28 ASN A O 1 ATOM 206 C CB . ASN A 1 28 ? 37.245 -30.087 -34.927 1.00 63.85 ? 28 ASN A CB 1 ATOM 207 C CG . ASN A 1 28 ? 36.258 -30.427 -33.818 1.00 70.11 ? 28 ASN A CG 1 ATOM 208 O OD1 . ASN A 1 28 ? 36.007 -29.615 -32.921 1.00 67.32 ? 28 ASN A OD1 1 ATOM 209 N ND2 . ASN A 1 28 ? 35.687 -31.636 -33.878 1.00 79.65 ? 28 ASN A ND2 1 ATOM 210 N N . ALA A 1 29 ? 38.640 -28.804 -32.301 1.00 52.81 ? 29 ALA A N 1 ATOM 211 C CA . ALA A 1 29 ? 39.511 -29.019 -31.141 1.00 50.58 ? 29 ALA A CA 1 ATOM 212 C C . ALA A 1 29 ? 38.723 -29.487 -29.920 1.00 49.18 ? 29 ALA A C 1 ATOM 213 O O . ALA A 1 29 ? 37.496 -29.407 -29.891 1.00 50.23 ? 29 ALA A O 1 ATOM 214 C CB . ALA A 1 29 ? 40.292 -27.756 -30.809 1.00 50.36 ? 29 ALA A CB 1 ATOM 215 N N . THR A 1 30 ? 39.442 -29.967 -28.911 1.00 46.75 ? 30 THR A N 1 ATOM 216 C CA . THR A 1 30 ? 38.813 -30.498 -27.710 1.00 45.79 ? 30 THR A CA 1 ATOM 217 C C . THR A 1 30 ? 39.593 -30.162 -26.435 1.00 43.49 ? 30 THR A C 1 ATOM 218 O O . THR A 1 30 ? 40.808 -30.011 -26.462 1.00 42.78 ? 30 THR A O 1 ATOM 219 C CB . THR A 1 30 ? 38.614 -32.024 -27.824 1.00 45.71 ? 30 THR A CB 1 ATOM 220 O OG1 . THR A 1 30 ? 37.539 -32.425 -26.970 1.00 46.82 ? 30 THR A OG1 1 ATOM 221 C CG2 . THR A 1 30 ? 39.878 -32.794 -27.452 1.00 44.99 ? 30 THR A CG2 1 ATOM 222 N N . GLU A 1 31 ? 38.872 -30.072 -25.323 1.00 42.31 ? 31 GLU A N 1 ATOM 223 C CA . GLU A 1 31 ? 39.437 -29.645 -24.050 1.00 40.96 ? 31 GLU A CA 1 ATOM 224 C C . GLU A 1 31 ? 40.228 -30.766 -23.363 1.00 39.16 ? 31 GLU A C 1 ATOM 225 O O . GLU A 1 31 ? 39.797 -31.915 -23.359 1.00 38.28 ? 31 GLU A O 1 ATOM 226 C CB . GLU A 1 31 ? 38.296 -29.171 -23.145 1.00 41.14 ? 31 GLU A CB 1 ATOM 227 C CG . GLU A 1 31 ? 38.734 -28.619 -21.805 1.00 40.88 ? 31 GLU A CG 1 ATOM 228 C CD . GLU A 1 31 ? 39.773 -27.519 -21.935 1.00 41.04 ? 31 GLU A CD 1 ATOM 229 O OE1 . GLU A 1 31 ? 39.390 -26.366 -22.202 1.00 42.12 ? 31 GLU A OE1 1 ATOM 230 O OE2 . GLU A 1 31 ? 40.970 -27.812 -21.757 1.00 39.99 ? 31 GLU A OE2 1 ATOM 231 N N . THR A 1 32 ? 41.386 -30.434 -22.791 1.00 38.58 ? 32 THR A N 1 ATOM 232 C CA . THR A 1 32 ? 42.175 -31.403 -22.012 1.00 36.87 ? 32 THR A CA 1 ATOM 233 C C . THR A 1 32 ? 42.127 -31.161 -20.500 1.00 36.00 ? 32 THR A C 1 ATOM 234 O O . THR A 1 32 ? 42.610 -31.987 -19.737 1.00 35.59 ? 32 THR A O 1 ATOM 235 C CB . THR A 1 32 ? 43.653 -31.403 -22.429 1.00 37.55 ? 32 THR A CB 1 ATOM 236 O OG1 . THR A 1 32 ? 44.260 -30.156 -22.067 1.00 37.58 ? 32 THR A OG1 1 ATOM 237 C CG2 . THR A 1 32 ? 43.792 -31.645 -23.930 1.00 38.68 ? 32 THR A CG2 1 ATOM 238 N N . VAL A 1 33 ? 41.567 -30.031 -20.073 1.00 36.24 ? 33 VAL A N 1 ATOM 239 C CA . VAL A 1 33 ? 41.504 -29.666 -18.659 1.00 36.09 ? 33 VAL A CA 1 ATOM 240 C C . VAL A 1 33 ? 40.059 -29.645 -18.157 1.00 37.10 ? 33 VAL A C 1 ATOM 241 O O . VAL A 1 33 ? 39.238 -28.869 -18.645 1.00 36.96 ? 33 VAL A O 1 ATOM 242 C CB . VAL A 1 33 ? 42.113 -28.278 -18.422 1.00 36.78 ? 33 VAL A CB 1 ATOM 243 C CG1 . VAL A 1 33 ? 42.033 -27.903 -16.944 1.00 36.68 ? 33 VAL A CG1 1 ATOM 244 C CG2 . VAL A 1 33 ? 43.550 -28.248 -18.920 1.00 37.28 ? 33 VAL A CG2 1 ATOM 245 N N . GLU A 1 34 ? 39.766 -30.484 -17.166 1.00 37.39 ? 34 GLU A N 1 ATOM 246 C CA . GLU A 1 34 ? 38.418 -30.594 -16.632 1.00 38.29 ? 34 GLU A CA 1 ATOM 247 C C . GLU A 1 34 ? 38.075 -29.433 -15.712 1.00 39.36 ? 34 GLU A C 1 ATOM 248 O O . GLU A 1 34 ? 38.819 -29.142 -14.771 1.00 39.00 ? 34 GLU A O 1 ATOM 249 C CB . GLU A 1 34 ? 38.259 -31.905 -15.864 1.00 37.72 ? 34 GLU A CB 1 ATOM 250 C CG . GLU A 1 34 ? 36.853 -32.146 -15.361 1.00 38.14 ? 34 GLU A CG 1 ATOM 251 C CD . GLU A 1 34 ? 35.853 -32.218 -16.495 1.00 38.78 ? 34 GLU A CD 1 ATOM 252 O OE1 . GLU A 1 34 ? 35.945 -33.151 -17.302 1.00 38.73 ? 34 GLU A OE1 1 ATOM 253 O OE2 . GLU A 1 34 ? 34.986 -31.333 -16.584 1.00 40.79 ? 34 GLU A OE2 1 ATOM 254 N N . ARG A 1 35 ? 36.948 -28.777 -15.993 1.00 41.35 ? 35 ARG A N 1 ATOM 255 C CA . ARG A 1 35 ? 36.408 -27.731 -15.122 1.00 42.96 ? 35 ARG A CA 1 ATOM 256 C C . ARG A 1 35 ? 35.055 -28.082 -14.503 1.00 43.11 ? 35 ARG A C 1 ATOM 257 O O . ARG A 1 35 ? 34.594 -27.386 -13.591 1.00 44.50 ? 35 ARG A O 1 ATOM 258 C CB . ARG A 1 35 ? 36.278 -26.412 -15.885 1.00 45.29 ? 35 ARG A CB 1 ATOM 259 C CG . ARG A 1 35 ? 37.606 -25.813 -16.320 1.00 46.16 ? 35 ARG A CG 1 ATOM 260 C CD . ARG A 1 35 ? 37.412 -24.446 -16.963 1.00 48.66 ? 35 ARG A CD 1 ATOM 261 N NE . ARG A 1 35 ? 36.596 -24.514 -18.177 1.00 50.27 ? 35 ARG A NE 1 ATOM 262 C CZ . ARG A 1 35 ? 37.019 -24.951 -19.366 1.00 51.16 ? 35 ARG A CZ 1 ATOM 263 N NH1 . ARG A 1 35 ? 38.272 -25.376 -19.552 1.00 50.77 ? 35 ARG A NH1 1 ATOM 264 N NH2 . ARG A 1 35 ? 36.175 -24.965 -20.389 1.00 51.75 ? 35 ARG A NH2 1 ATOM 265 N N . THR A 1 36 ? 34.414 -29.148 -14.974 1.00 42.67 ? 36 THR A N 1 ATOM 266 C CA . THR A 1 36 ? 33.068 -29.477 -14.502 1.00 43.52 ? 36 THR A CA 1 ATOM 267 C C . THR A 1 36 ? 33.129 -30.252 -13.195 1.00 42.19 ? 36 THR A C 1 ATOM 268 O O . THR A 1 36 ? 33.698 -31.335 -13.144 1.00 41.43 ? 36 THR A O 1 ATOM 269 C CB . THR A 1 36 ? 32.279 -30.301 -15.539 1.00 44.12 ? 36 THR A CB 1 ATOM 270 O OG1 . THR A 1 36 ? 32.291 -29.616 -16.792 1.00 44.94 ? 36 THR A OG1 1 ATOM 271 C CG2 . THR A 1 36 ? 30.823 -30.505 -15.091 1.00 45.43 ? 36 THR A CG2 1 ATOM 272 N N . ASN A 1 37 ? 32.546 -29.677 -12.147 1.00 42.67 ? 37 ASN A N 1 ATOM 273 C CA . ASN A 1 37 ? 32.403 -30.340 -10.862 1.00 42.41 ? 37 ASN A CA 1 ATOM 274 C C . ASN A 1 37 ? 31.009 -30.931 -10.733 1.00 43.27 ? 37 ASN A C 1 ATOM 275 O O . ASN A 1 37 ? 30.059 -30.413 -11.303 1.00 44.47 ? 37 ASN A O 1 ATOM 276 C CB . ASN A 1 37 ? 32.626 -29.350 -9.722 1.00 42.72 ? 37 ASN A CB 1 ATOM 277 C CG . ASN A 1 37 ? 32.583 -30.017 -8.357 1.00 42.87 ? 37 ASN A CG 1 ATOM 278 O OD1 . ASN A 1 37 ? 33.246 -31.027 -8.131 1.00 42.88 ? 37 ASN A OD1 1 ATOM 279 N ND2 . ASN A 1 37 ? 31.801 -29.463 -7.446 1.00 43.70 ? 37 ASN A ND2 1 ATOM 280 N N . ILE A 1 38 ? 30.892 -32.021 -9.986 1.00 43.04 ? 38 ILE A N 1 ATOM 281 C CA . ILE A 1 38 ? 29.588 -32.507 -9.559 1.00 43.94 ? 38 ILE A CA 1 ATOM 282 C C . ILE A 1 38 ? 29.495 -32.258 -8.065 1.00 42.80 ? 38 ILE A C 1 ATOM 283 O O . ILE A 1 38 ? 30.305 -32.789 -7.314 1.00 41.24 ? 38 ILE A O 1 ATOM 284 C CB . ILE A 1 38 ? 29.401 -33.991 -9.904 1.00 44.94 ? 38 ILE A CB 1 ATOM 285 C CG1 . ILE A 1 38 ? 29.324 -34.119 -11.428 1.00 47.04 ? 38 ILE A CG1 1 ATOM 286 C CG2 . ILE A 1 38 ? 28.147 -34.544 -9.231 1.00 45.61 ? 38 ILE A CG2 1 ATOM 287 C CD1 . ILE A 1 38 ? 29.129 -35.527 -11.935 1.00 48.49 ? 38 ILE A CD1 1 ATOM 288 N N . PRO A 1 39 ? 28.522 -31.438 -7.626 1.00 43.69 ? 39 PRO A N 1 ATOM 289 C CA . PRO A 1 39 ? 28.497 -30.996 -6.225 1.00 44.49 ? 39 PRO A CA 1 ATOM 290 C C . PRO A 1 39 ? 27.881 -32.003 -5.248 1.00 44.98 ? 39 PRO A C 1 ATOM 291 O O . PRO A 1 39 ? 27.115 -31.622 -4.367 1.00 45.74 ? 39 PRO A O 1 ATOM 292 C CB . PRO A 1 39 ? 27.665 -29.705 -6.290 1.00 45.66 ? 39 PRO A CB 1 ATOM 293 C CG . PRO A 1 39 ? 26.708 -29.949 -7.412 1.00 46.60 ? 39 PRO A CG 1 ATOM 294 C CD . PRO A 1 39 ? 27.438 -30.816 -8.414 1.00 45.22 ? 39 PRO A CD 1 ATOM 295 N N . ARG A 1 40 ? 28.237 -33.277 -5.398 1.00 45.42 ? 40 ARG A N 1 ATOM 296 C CA . ARG A 1 40 ? 27.823 -34.336 -4.481 1.00 45.74 ? 40 ARG A CA 1 ATOM 297 C C . ARG A 1 40 ? 28.988 -35.309 -4.319 1.00 43.45 ? 40 ARG A C 1 ATOM 298 O O . ARG A 1 40 ? 29.927 -35.284 -5.113 1.00 42.08 ? 40 ARG A O 1 ATOM 299 C CB . ARG A 1 40 ? 26.581 -35.050 -5.019 1.00 47.98 ? 40 ARG A CB 1 ATOM 300 C CG . ARG A 1 40 ? 25.346 -34.165 -5.040 1.00 51.65 ? 40 ARG A CG 1 ATOM 301 C CD . ARG A 1 40 ? 24.159 -34.803 -5.735 1.00 55.85 ? 40 ARG A CD 1 ATOM 302 N NE . ARG A 1 40 ? 24.402 -35.086 -7.156 1.00 58.30 ? 40 ARG A NE 1 ATOM 303 C CZ . ARG A 1 40 ? 24.264 -34.213 -8.159 1.00 60.31 ? 40 ARG A CZ 1 ATOM 304 N NH1 . ARG A 1 40 ? 23.897 -32.948 -7.938 1.00 61.59 ? 40 ARG A NH1 1 ATOM 305 N NH2 . ARG A 1 40 ? 24.509 -34.610 -9.404 1.00 60.42 ? 40 ARG A NH2 1 ATOM 306 N N . ILE A 1 41 ? 28.950 -36.129 -3.273 1.00 42.71 ? 41 ILE A N 1 ATOM 307 C CA . ILE A 1 41 ? 29.918 -37.211 -3.119 1.00 41.97 ? 41 ILE A CA 1 ATOM 308 C C . ILE A 1 41 ? 29.330 -38.434 -3.805 1.00 41.73 ? 41 ILE A C 1 ATOM 309 O O . ILE A 1 41 ? 28.392 -39.046 -3.297 1.00 41.68 ? 41 ILE A O 1 ATOM 310 C CB . ILE A 1 41 ? 30.220 -37.521 -1.643 1.00 42.91 ? 41 ILE A CB 1 ATOM 311 C CG1 . ILE A 1 41 ? 30.765 -36.271 -0.936 1.00 43.93 ? 41 ILE A CG1 1 ATOM 312 C CG2 . ILE A 1 41 ? 31.219 -38.670 -1.530 1.00 42.20 ? 41 ILE A CG2 1 ATOM 313 C CD1 . ILE A 1 41 ? 31.979 -35.652 -1.610 1.00 44.13 ? 41 ILE A CD1 1 ATOM 314 N N . CYS A 1 42 ? 29.868 -38.751 -4.981 1.00 40.74 ? 42 CYS A N 1 ATOM 315 C CA . CYS A 1 42 ? 29.377 -39.855 -5.802 1.00 41.09 ? 42 CYS A CA 1 ATOM 316 C C . CYS A 1 42 ? 29.877 -41.176 -5.230 1.00 40.50 ? 42 CYS A C 1 ATOM 317 O O . CYS A 1 42 ? 31.054 -41.504 -5.350 1.00 38.82 ? 42 CYS A O 1 ATOM 318 C CB . CYS A 1 42 ? 29.856 -39.698 -7.247 1.00 40.26 ? 42 CYS A CB 1 ATOM 319 S SG . CYS A 1 42 ? 29.085 -38.329 -8.133 1.00 41.44 ? 42 CYS A SG 1 ATOM 320 N N . SER A 1 43 ? 28.971 -41.925 -4.611 1.00 41.24 ? 43 SER A N 1 ATOM 321 C CA . SER A 1 43 ? 29.354 -43.088 -3.814 1.00 41.11 ? 43 SER A CA 1 ATOM 322 C C . SER A 1 43 ? 28.705 -44.387 -4.290 1.00 40.49 ? 43 SER A C 1 ATOM 323 O O . SER A 1 43 ? 28.745 -45.377 -3.577 1.00 39.94 ? 43 SER A O 1 ATOM 324 C CB . SER A 1 43 ? 28.986 -42.834 -2.354 1.00 41.34 ? 43 SER A CB 1 ATOM 325 O OG . SER A 1 43 ? 27.585 -42.706 -2.229 1.00 44.34 ? 43 SER A OG 1 ATOM 326 N N . LYS A 1 44 ? 28.124 -44.385 -5.490 1.00 40.72 ? 44 LYS A N 1 ATOM 327 C CA . LYS A 1 44 ? 27.530 -45.588 -6.057 1.00 41.74 ? 44 LYS A CA 1 ATOM 328 C C . LYS A 1 44 ? 28.471 -46.779 -5.997 1.00 40.37 ? 44 LYS A C 1 ATOM 329 O O . LYS A 1 44 ? 29.568 -46.714 -6.513 1.00 38.14 ? 44 LYS A O 1 ATOM 330 C CB . LYS A 1 44 ? 27.139 -45.388 -7.522 1.00 43.42 ? 44 LYS A CB 1 ATOM 331 C CG . LYS A 1 44 ? 26.602 -46.677 -8.148 1.00 45.45 ? 44 LYS A CG 1 ATOM 332 C CD . LYS A 1 44 ? 25.891 -46.438 -9.462 1.00 47.89 ? 44 LYS A CD 1 ATOM 333 C CE . LYS A 1 44 ? 26.872 -46.248 -10.606 1.00 47.83 ? 44 LYS A CE 1 ATOM 334 N NZ . LYS A 1 44 ? 26.257 -45.451 -11.706 1.00 49.76 ? 44 LYS A NZ 1 ATOM 335 N N . GLY A 1 45 ? 28.014 -47.874 -5.394 1.00 40.77 ? 45 GLY A N 1 ATOM 336 C CA . GLY A 1 45 ? 28.773 -49.120 -5.370 1.00 40.49 ? 45 GLY A CA 1 ATOM 337 C C . GLY A 1 45 ? 29.772 -49.213 -4.232 1.00 39.58 ? 45 GLY A C 1 ATOM 338 O O . GLY A 1 45 ? 30.477 -50.212 -4.113 1.00 39.69 ? 45 GLY A O 1 ATOM 339 N N . LYS A 1 46 ? 29.821 -48.192 -3.379 1.00 38.32 ? 46 LYS A N 1 ATOM 340 C CA . LYS A 1 46 ? 30.819 -48.137 -2.313 1.00 38.16 ? 46 LYS A CA 1 ATOM 341 C C . LYS A 1 46 ? 30.229 -48.176 -0.912 1.00 37.91 ? 46 LYS A C 1 ATOM 342 O O . LYS A 1 46 ? 29.335 -47.404 -0.590 1.00 38.09 ? 46 LYS A O 1 ATOM 343 C CB . LYS A 1 46 ? 31.655 -46.862 -2.454 1.00 37.79 ? 46 LYS A CB 1 ATOM 344 C CG . LYS A 1 46 ? 32.575 -46.890 -3.657 1.00 37.44 ? 46 LYS A CG 1 ATOM 345 C CD . LYS A 1 46 ? 33.400 -45.627 -3.764 1.00 36.52 ? 46 LYS A CD 1 ATOM 346 C CE . LYS A 1 46 ? 34.166 -45.628 -5.071 1.00 36.07 ? 46 LYS A CE 1 ATOM 347 N NZ . LYS A 1 46 ? 34.720 -44.285 -5.324 1.00 35.34 ? 46 LYS A NZ 1 ATOM 348 N N . ARG A 1 47 ? 30.772 -49.044 -0.069 1.00 38.39 ? 47 ARG A N 1 ATOM 349 C CA . ARG A 1 47 ? 30.431 -49.028 1.345 1.00 39.18 ? 47 ARG A CA 1 ATOM 350 C C . ARG A 1 47 ? 30.897 -47.701 1.924 1.00 36.49 ? 47 ARG A C 1 ATOM 351 O O . ARG A 1 47 ? 32.098 -47.438 2.031 1.00 34.05 ? 47 ARG A O 1 ATOM 352 C CB . ARG A 1 47 ? 31.047 -50.217 2.090 1.00 41.72 ? 47 ARG A CB 1 ATOM 353 C CG . ARG A 1 47 ? 30.385 -51.535 1.735 1.00 45.72 ? 47 ARG A CG 1 ATOM 354 C CD . ARG A 1 47 ? 30.910 -52.708 2.551 1.00 49.17 ? 47 ARG A CD 1 ATOM 355 N NE . ARG A 1 47 ? 32.118 -53.248 1.938 1.00 52.99 ? 47 ARG A NE 1 ATOM 356 C CZ . ARG A 1 47 ? 33.352 -53.189 2.443 1.00 56.55 ? 47 ARG A CZ 1 ATOM 357 N NH1 . ARG A 1 47 ? 33.600 -52.634 3.627 1.00 57.87 ? 47 ARG A NH1 1 ATOM 358 N NH2 . ARG A 1 47 ? 34.361 -53.718 1.751 1.00 59.01 ? 47 ARG A NH2 1 ATOM 359 N N . THR A 1 48 ? 29.928 -46.868 2.282 1.00 35.95 ? 48 THR A N 1 ATOM 360 C CA . THR A 1 48 ? 30.186 -45.494 2.680 1.00 35.84 ? 48 THR A CA 1 ATOM 361 C C . THR A 1 48 ? 29.704 -45.234 4.099 1.00 36.64 ? 48 THR A C 1 ATOM 362 O O . THR A 1 48 ? 28.584 -45.602 4.474 1.00 38.28 ? 48 THR A O 1 ATOM 363 C CB . THR A 1 48 ? 29.485 -44.513 1.727 1.00 36.24 ? 48 THR A CB 1 ATOM 364 O OG1 . THR A 1 48 ? 29.757 -44.898 0.374 1.00 36.69 ? 48 THR A OG1 1 ATOM 365 C CG2 . THR A 1 48 ? 29.950 -43.081 1.971 1.00 35.70 ? 48 THR A CG2 1 ATOM 366 N N . VAL A 1 49 ? 30.559 -44.578 4.871 1.00 36.38 ? 49 VAL A N 1 ATOM 367 C CA . VAL A 1 49 ? 30.265 -44.196 6.237 1.00 36.55 ? 49 VAL A CA 1 ATOM 368 C C . VAL A 1 49 ? 30.415 -42.683 6.331 1.00 36.66 ? 49 VAL A C 1 ATOM 369 O O . VAL A 1 49 ? 31.526 -42.151 6.254 1.00 35.17 ? 49 VAL A O 1 ATOM 370 C CB . VAL A 1 49 ? 31.244 -44.883 7.201 1.00 36.82 ? 49 VAL A CB 1 ATOM 371 C CG1 . VAL A 1 49 ? 31.140 -44.285 8.597 1.00 37.70 ? 49 VAL A CG1 1 ATOM 372 C CG2 . VAL A 1 49 ? 30.986 -46.383 7.215 1.00 37.06 ? 49 VAL A CG2 1 ATOM 373 N N . ASP A 1 50 ? 29.289 -41.992 6.470 1.00 37.55 ? 50 ASP A N 1 ATOM 374 C CA . ASP A 1 50 ? 29.295 -40.554 6.651 1.00 37.19 ? 50 ASP A CA 1 ATOM 375 C C . ASP A 1 50 ? 29.260 -40.286 8.155 1.00 37.71 ? 50 ASP A C 1 ATOM 376 O O . ASP A 1 50 ? 28.261 -40.558 8.816 1.00 38.05 ? 50 ASP A O 1 ATOM 377 C CB . ASP A 1 50 ? 28.101 -39.927 5.927 1.00 38.05 ? 50 ASP A CB 1 ATOM 378 C CG . ASP A 1 50 ? 27.994 -38.430 6.155 1.00 38.76 ? 50 ASP A CG 1 ATOM 379 O OD1 . ASP A 1 50 ? 28.865 -37.873 6.851 1.00 38.80 ? 50 ASP A OD1 1 ATOM 380 O OD2 . ASP A 1 50 ? 27.034 -37.811 5.641 1.00 39.77 ? 50 ASP A OD2 1 ATOM 381 N N . LEU A 1 51 ? 30.356 -39.749 8.683 1.00 37.69 ? 51 LEU A N 1 ATOM 382 C CA . LEU A 1 51 ? 30.552 -39.629 10.132 1.00 38.84 ? 51 LEU A CA 1 ATOM 383 C C . LEU A 1 51 ? 29.660 -38.581 10.803 1.00 40.63 ? 51 LEU A C 1 ATOM 384 O O . LEU A 1 51 ? 29.320 -38.714 11.981 1.00 42.32 ? 51 LEU A O 1 ATOM 385 C CB . LEU A 1 51 ? 32.023 -39.336 10.443 1.00 38.05 ? 51 LEU A CB 1 ATOM 386 C CG . LEU A 1 51 ? 33.000 -40.459 10.104 1.00 37.10 ? 51 LEU A CG 1 ATOM 387 C CD1 . LEU A 1 51 ? 34.440 -39.999 10.270 1.00 36.60 ? 51 LEU A CD1 1 ATOM 388 C CD2 . LEU A 1 51 ? 32.730 -41.675 10.973 1.00 37.60 ? 51 LEU A CD2 1 ATOM 389 N N . GLY A 1 52 ? 29.278 -37.550 10.063 1.00 41.55 ? 52 GLY A N 1 ATOM 390 C CA . GLY A 1 52 ? 28.367 -36.537 10.585 1.00 43.37 ? 52 GLY A CA 1 ATOM 391 C C . GLY A 1 52 ? 28.952 -35.860 11.809 1.00 44.66 ? 52 GLY A C 1 ATOM 392 O O . GLY A 1 52 ? 30.042 -35.273 11.743 1.00 44.40 ? 52 GLY A O 1 ATOM 393 N N . GLN A 1 53 ? 28.241 -35.957 12.932 1.00 45.41 ? 53 GLN A N 1 ATOM 394 C CA . GLN A 1 53 ? 28.677 -35.312 14.174 1.00 46.56 ? 53 GLN A CA 1 ATOM 395 C C . GLN A 1 53 ? 29.774 -36.079 14.922 1.00 44.51 ? 53 GLN A C 1 ATOM 396 O O . GLN A 1 53 ? 30.371 -35.554 15.861 1.00 43.31 ? 53 GLN A O 1 ATOM 397 C CB . GLN A 1 53 ? 27.483 -35.085 15.095 1.00 49.63 ? 53 GLN A CB 1 ATOM 398 C CG . GLN A 1 53 ? 26.608 -33.925 14.666 1.00 52.86 ? 53 GLN A CG 1 ATOM 399 C CD . GLN A 1 53 ? 25.441 -33.733 15.605 1.00 56.85 ? 53 GLN A CD 1 ATOM 400 O OE1 . GLN A 1 53 ? 24.364 -34.275 15.382 1.00 59.90 ? 53 GLN A OE1 1 ATOM 401 N NE2 . GLN A 1 53 ? 25.657 -32.986 16.682 1.00 58.69 ? 53 GLN A NE2 1 ATOM 402 N N . CYS A 1 54 ? 30.017 -37.321 14.521 1.00 42.93 ? 54 CYS A N 1 ATOM 403 C CA . CYS A 1 54 ? 31.119 -38.107 15.069 1.00 42.58 ? 54 CYS A CA 1 ATOM 404 C C . CYS A 1 54 ? 32.453 -37.683 14.457 1.00 41.87 ? 54 CYS A C 1 ATOM 405 O O . CYS A 1 54 ? 32.609 -37.681 13.236 1.00 41.45 ? 54 CYS A O 1 ATOM 406 C CB . CYS A 1 54 ? 30.898 -39.586 14.772 1.00 42.08 ? 54 CYS A CB 1 ATOM 407 S SG . CYS A 1 54 ? 32.208 -40.673 15.363 1.00 41.65 ? 54 CYS A SG 1 ATOM 408 N N . GLY A 1 55 ? 33.416 -37.334 15.302 1.00 41.71 ? 55 GLY A N 1 ATOM 409 C CA . GLY A 1 55 ? 34.788 -37.135 14.845 1.00 40.72 ? 55 GLY A CA 1 ATOM 410 C C . GLY A 1 55 ? 35.436 -38.486 14.604 1.00 40.13 ? 55 GLY A C 1 ATOM 411 O O . GLY A 1 55 ? 35.153 -39.449 15.324 1.00 40.53 ? 55 GLY A O 1 ATOM 412 N N . LEU A 1 56 ? 36.308 -38.565 13.601 1.00 38.47 ? 56 LEU A N 1 ATOM 413 C CA . LEU A 1 56 ? 36.931 -39.835 13.231 1.00 38.30 ? 56 LEU A CA 1 ATOM 414 C C . LEU A 1 56 ? 37.691 -40.487 14.392 1.00 38.36 ? 56 LEU A C 1 ATOM 415 O O . LEU A 1 56 ? 37.623 -41.698 14.573 1.00 37.90 ? 56 LEU A O 1 ATOM 416 C CB . LEU A 1 56 ? 37.875 -39.647 12.035 1.00 37.94 ? 56 LEU A CB 1 ATOM 417 C CG . LEU A 1 56 ? 38.668 -40.863 11.566 1.00 37.34 ? 56 LEU A CG 1 ATOM 418 C CD1 . LEU A 1 56 ? 37.750 -42.030 11.245 1.00 37.29 ? 56 LEU A CD1 1 ATOM 419 C CD2 . LEU A 1 56 ? 39.505 -40.492 10.349 1.00 37.24 ? 56 LEU A CD2 1 ATOM 420 N N . LEU A 1 57 ? 38.408 -39.685 15.172 1.00 38.93 ? 57 LEU A N 1 ATOM 421 C CA . LEU A 1 57 ? 39.159 -40.211 16.311 1.00 39.65 ? 57 LEU A CA 1 ATOM 422 C C . LEU A 1 57 ? 38.228 -40.666 17.438 1.00 40.09 ? 57 LEU A C 1 ATOM 423 O O . LEU A 1 57 ? 38.588 -41.539 18.229 1.00 40.45 ? 57 LEU A O 1 ATOM 424 C CB . LEU A 1 57 ? 40.165 -39.190 16.826 1.00 40.57 ? 57 LEU A CB 1 ATOM 425 C CG . LEU A 1 57 ? 41.145 -38.633 15.790 1.00 40.80 ? 57 LEU A CG 1 ATOM 426 C CD1 . LEU A 1 57 ? 42.170 -37.746 16.478 1.00 41.86 ? 57 LEU A CD1 1 ATOM 427 C CD2 . LEU A 1 57 ? 41.835 -39.753 15.023 1.00 40.66 ? 57 LEU A CD2 1 ATOM 428 N N . GLY A 1 58 ? 37.029 -40.091 17.491 1.00 39.75 ? 58 GLY A N 1 ATOM 429 C CA . GLY A 1 58 ? 36.004 -40.511 18.447 1.00 40.27 ? 58 GLY A CA 1 ATOM 430 C C . GLY A 1 58 ? 35.459 -41.919 18.226 1.00 39.70 ? 58 GLY A C 1 ATOM 431 O O . GLY A 1 58 ? 34.869 -42.499 19.132 1.00 39.94 ? 58 GLY A O 1 ATOM 432 N N . THR A 1 59 ? 35.661 -42.487 17.034 1.00 38.63 ? 59 THR A N 1 ATOM 433 C CA . THR A 1 59 ? 35.237 -43.859 16.780 1.00 38.23 ? 59 THR A CA 1 ATOM 434 C C . THR A 1 59 ? 36.028 -44.841 17.649 1.00 39.68 ? 59 THR A C 1 ATOM 435 O O . THR A 1 59 ? 35.538 -45.922 17.969 1.00 39.88 ? 59 THR A O 1 ATOM 436 C CB . THR A 1 59 ? 35.346 -44.278 15.290 1.00 37.26 ? 59 THR A CB 1 ATOM 437 O OG1 . THR A 1 59 ? 36.713 -44.328 14.868 1.00 36.12 ? 59 THR A OG1 1 ATOM 438 C CG2 . THR A 1 59 ? 34.559 -43.332 14.393 1.00 36.81 ? 59 THR A CG2 1 ATOM 439 N N . ILE A 1 60 ? 37.231 -44.442 18.049 1.00 40.55 ? 60 ILE A N 1 ATOM 440 C CA . ILE A 1 60 ? 38.099 -45.276 18.869 1.00 41.96 ? 60 ILE A CA 1 ATOM 441 C C . ILE A 1 60 ? 37.808 -45.171 20.370 1.00 43.34 ? 60 ILE A C 1 ATOM 442 O O . ILE A 1 60 ? 37.989 -46.153 21.092 1.00 44.94 ? 60 ILE A O 1 ATOM 443 C CB . ILE A 1 60 ? 39.581 -44.916 18.627 1.00 42.64 ? 60 ILE A CB 1 ATOM 444 C CG1 . ILE A 1 60 ? 39.914 -44.971 17.135 1.00 41.97 ? 60 ILE A CG1 1 ATOM 445 C CG2 . ILE A 1 60 ? 40.500 -45.848 19.407 1.00 44.14 ? 60 ILE A CG2 1 ATOM 446 C CD1 . ILE A 1 60 ? 39.618 -46.301 16.479 1.00 41.90 ? 60 ILE A CD1 1 ATOM 447 N N . THR A 1 61 ? 37.377 -43.994 20.840 1.00 43.17 ? 61 THR A N 1 ATOM 448 C CA . THR A 1 61 ? 37.175 -43.748 22.281 1.00 44.03 ? 61 THR A CA 1 ATOM 449 C C . THR A 1 61 ? 35.709 -43.834 22.695 1.00 44.34 ? 61 THR A C 1 ATOM 450 O O . THR A 1 61 ? 35.391 -44.339 23.777 1.00 45.05 ? 61 THR A O 1 ATOM 451 C CB . THR A 1 61 ? 37.742 -42.377 22.712 1.00 44.71 ? 61 THR A CB 1 ATOM 452 O OG1 . THR A 1 61 ? 37.123 -41.323 21.961 1.00 44.32 ? 61 THR A OG1 1 ATOM 453 C CG2 . THR A 1 61 ? 39.249 -42.334 22.488 1.00 44.75 ? 61 THR A CG2 1 ATOM 454 N N . GLY A 1 62 ? 34.829 -43.316 21.842 1.00 43.42 ? 62 GLY A N 1 ATOM 455 C CA . GLY A 1 62 ? 33.392 -43.502 21.987 1.00 43.90 ? 62 GLY A CA 1 ATOM 456 C C . GLY A 1 62 ? 32.613 -42.461 22.773 1.00 44.81 ? 62 GLY A C 1 ATOM 457 O O . GLY A 1 62 ? 31.925 -42.803 23.743 1.00 46.62 ? 62 GLY A O 1 ATOM 458 N N . PRO A 1 63 ? 32.682 -41.187 22.353 1.00 44.58 ? 63 PRO A N 1 ATOM 459 C CA . PRO A 1 63 ? 31.763 -40.203 22.919 1.00 45.43 ? 63 PRO A CA 1 ATOM 460 C C . PRO A 1 63 ? 30.369 -40.459 22.352 1.00 45.47 ? 63 PRO A C 1 ATOM 461 O O . PRO A 1 63 ? 30.251 -41.099 21.310 1.00 44.72 ? 63 PRO A O 1 ATOM 462 C CB . PRO A 1 63 ? 32.325 -38.879 22.412 1.00 44.99 ? 63 PRO A CB 1 ATOM 463 C CG . PRO A 1 63 ? 32.937 -39.223 21.104 1.00 43.35 ? 63 PRO A CG 1 ATOM 464 C CD . PRO A 1 63 ? 33.505 -40.606 21.278 1.00 43.34 ? 63 PRO A CD 1 ATOM 465 N N . PRO A 1 64 ? 29.318 -39.958 23.012 1.00 47.39 ? 64 PRO A N 1 ATOM 466 C CA . PRO A 1 64 ? 27.951 -40.393 22.654 1.00 47.82 ? 64 PRO A CA 1 ATOM 467 C C . PRO A 1 64 ? 27.604 -40.231 21.167 1.00 46.65 ? 64 PRO A C 1 ATOM 468 O O . PRO A 1 64 ? 26.938 -41.093 20.588 1.00 45.68 ? 64 PRO A O 1 ATOM 469 C CB . PRO A 1 64 ? 27.050 -39.508 23.520 1.00 49.56 ? 64 PRO A CB 1 ATOM 470 C CG . PRO A 1 64 ? 27.936 -38.944 24.585 1.00 50.47 ? 64 PRO A CG 1 ATOM 471 C CD . PRO A 1 64 ? 29.315 -38.870 24.005 1.00 49.05 ? 64 PRO A CD 1 ATOM 472 N N . GLN A 1 65 ? 28.082 -39.147 20.556 1.00 46.21 ? 65 GLN A N 1 ATOM 473 C CA . GLN A 1 65 ? 27.851 -38.896 19.130 1.00 45.39 ? 65 GLN A CA 1 ATOM 474 C C . GLN A 1 65 ? 28.509 -39.934 18.199 1.00 43.99 ? 65 GLN A C 1 ATOM 475 O O . GLN A 1 65 ? 28.215 -39.962 17.004 1.00 43.08 ? 65 GLN A O 1 ATOM 476 C CB . GLN A 1 65 ? 28.310 -37.473 18.750 1.00 45.33 ? 65 GLN A CB 1 ATOM 477 C CG . GLN A 1 65 ? 29.822 -37.253 18.768 1.00 44.60 ? 65 GLN A CG 1 ATOM 478 C CD . GLN A 1 65 ? 30.347 -36.707 20.084 1.00 45.99 ? 65 GLN A CD 1 ATOM 479 O OE1 . GLN A 1 65 ? 29.691 -36.802 21.119 1.00 47.31 ? 65 GLN A OE1 1 ATOM 480 N NE2 . GLN A 1 65 ? 31.546 -36.132 20.047 1.00 46.44 ? 65 GLN A NE2 1 ATOM 481 N N . CYS A 1 66 ? 29.409 -40.759 18.735 1.00 43.94 ? 66 CYS A N 1 ATOM 482 C CA . CYS A 1 66 ? 30.052 -41.828 17.958 1.00 43.40 ? 66 CYS A CA 1 ATOM 483 C C . CYS A 1 66 ? 29.557 -43.245 18.323 1.00 43.49 ? 66 CYS A C 1 ATOM 484 O O . CYS A 1 66 ? 30.146 -44.238 17.896 1.00 42.38 ? 66 CYS A O 1 ATOM 485 C CB . CYS A 1 66 ? 31.578 -41.748 18.123 1.00 42.87 ? 66 CYS A CB 1 ATOM 486 S SG . CYS A 1 66 ? 32.346 -40.293 17.371 1.00 42.78 ? 66 CYS A SG 1 ATOM 487 N N . ASP A 1 67 ? 28.469 -43.340 19.081 1.00 45.23 ? 67 ASP A N 1 ATOM 488 C CA . ASP A 1 67 ? 27.977 -44.645 19.561 1.00 46.33 ? 67 ASP A CA 1 ATOM 489 C C . ASP A 1 67 ? 27.633 -45.608 18.425 1.00 45.55 ? 67 ASP A C 1 ATOM 490 O O . ASP A 1 67 ? 27.811 -46.818 18.567 1.00 46.11 ? 67 ASP A O 1 ATOM 491 C CB . ASP A 1 67 ? 26.766 -44.469 20.498 1.00 47.72 ? 67 ASP A CB 1 ATOM 492 C CG . ASP A 1 67 ? 27.171 -44.106 21.922 1.00 48.99 ? 67 ASP A CG 1 ATOM 493 O OD1 . ASP A 1 67 ? 28.335 -44.370 22.295 1.00 48.71 ? 67 ASP A OD1 1 ATOM 494 O OD2 . ASP A 1 67 ? 26.325 -43.566 22.679 1.00 49.43 ? 67 ASP A OD2 1 ATOM 495 N N . GLN A 1 68 ? 27.178 -45.070 17.297 1.00 45.42 ? 68 GLN A N 1 ATOM 496 C CA . GLN A 1 68 ? 26.823 -45.889 16.134 1.00 45.74 ? 68 GLN A CA 1 ATOM 497 C C . GLN A 1 68 ? 27.991 -46.120 15.164 1.00 44.16 ? 68 GLN A C 1 ATOM 498 O O . GLN A 1 68 ? 27.796 -46.703 14.098 1.00 43.14 ? 68 GLN A O 1 ATOM 499 C CB . GLN A 1 68 ? 25.627 -45.263 15.391 1.00 47.01 ? 68 GLN A CB 1 ATOM 500 C CG . GLN A 1 68 ? 24.381 -45.067 16.256 1.00 48.80 ? 68 GLN A CG 1 ATOM 501 C CD . GLN A 1 68 ? 23.847 -46.374 16.833 1.00 51.33 ? 68 GLN A CD 1 ATOM 502 O OE1 . GLN A 1 68 ? 23.774 -46.547 18.050 1.00 52.92 ? 68 GLN A OE1 1 ATOM 503 N NE2 . GLN A 1 68 ? 23.481 -47.306 15.957 1.00 52.16 ? 68 GLN A NE2 1 ATOM 504 N N . PHE A 1 69 ? 29.199 -45.695 15.541 1.00 43.75 ? 69 PHE A N 1 ATOM 505 C CA . PHE A 1 69 ? 30.392 -45.858 14.692 1.00 42.44 ? 69 PHE A CA 1 ATOM 506 C C . PHE A 1 69 ? 31.534 -46.621 15.371 1.00 42.51 ? 69 PHE A C 1 ATOM 507 O O . PHE A 1 69 ? 32.676 -46.559 14.927 1.00 43.05 ? 69 PHE A O 1 ATOM 508 C CB . PHE A 1 69 ? 30.892 -44.477 14.254 1.00 41.38 ? 69 PHE A CB 1 ATOM 509 C CG . PHE A 1 69 ? 29.870 -43.683 13.486 1.00 41.59 ? 69 PHE A CG 1 ATOM 510 C CD1 . PHE A 1 69 ? 28.930 -42.912 14.149 1.00 42.33 ? 69 PHE A CD1 1 ATOM 511 C CD2 . PHE A 1 69 ? 29.833 -43.733 12.102 1.00 40.93 ? 69 PHE A CD2 1 ATOM 512 C CE1 . PHE A 1 69 ? 27.978 -42.192 13.445 1.00 42.82 ? 69 PHE A CE1 1 ATOM 513 C CE2 . PHE A 1 69 ? 28.888 -43.016 11.391 1.00 41.45 ? 69 PHE A CE2 1 ATOM 514 C CZ . PHE A 1 69 ? 27.958 -42.245 12.060 1.00 42.15 ? 69 PHE A CZ 1 ATOM 515 N N . LEU A 1 70 ? 31.239 -47.344 16.439 1.00 43.19 ? 70 LEU A N 1 ATOM 516 C CA . LEU A 1 70 ? 32.292 -47.980 17.227 1.00 43.68 ? 70 LEU A CA 1 ATOM 517 C C . LEU A 1 70 ? 32.972 -49.140 16.488 1.00 43.78 ? 70 LEU A C 1 ATOM 518 O O . LEU A 1 70 ? 34.118 -49.461 16.785 1.00 43.54 ? 70 LEU A O 1 ATOM 519 C CB . LEU A 1 70 ? 31.748 -48.458 18.582 1.00 44.14 ? 70 LEU A CB 1 ATOM 520 C CG . LEU A 1 70 ? 31.133 -47.383 19.485 1.00 44.85 ? 70 LEU A CG 1 ATOM 521 C CD1 . LEU A 1 70 ? 30.585 -47.996 20.767 1.00 46.09 ? 70 LEU A CD1 1 ATOM 522 C CD2 . LEU A 1 70 ? 32.115 -46.267 19.815 1.00 44.37 ? 70 LEU A CD2 1 ATOM 523 N N . GLU A 1 71 ? 32.273 -49.755 15.534 1.00 44.33 ? 71 GLU A N 1 ATOM 524 C CA . GLU A 1 71 ? 32.819 -50.882 14.782 1.00 45.48 ? 71 GLU A CA 1 ATOM 525 C C . GLU A 1 71 ? 32.505 -50.793 13.286 1.00 45.84 ? 71 GLU A C 1 ATOM 526 O O . GLU A 1 71 ? 32.267 -51.798 12.626 1.00 47.17 ? 71 GLU A O 1 ATOM 527 C CB . GLU A 1 71 ? 32.304 -52.204 15.360 1.00 46.17 ? 71 GLU A CB 1 ATOM 528 C CG . GLU A 1 71 ? 32.917 -52.562 16.703 1.00 47.43 ? 71 GLU A CG 1 ATOM 529 C CD . GLU A 1 71 ? 32.676 -54.013 17.073 1.00 49.13 ? 71 GLU A CD 1 ATOM 530 O OE1 . GLU A 1 71 ? 31.496 -54.383 17.254 1.00 50.27 ? 71 GLU A OE1 1 ATOM 531 O OE2 . GLU A 1 71 ? 33.660 -54.787 17.147 1.00 49.14 ? 71 GLU A OE2 1 ATOM 532 N N . PHE A 1 72 ? 32.544 -49.586 12.744 1.00 46.35 ? 72 PHE A N 1 ATOM 533 C CA . PHE A 1 72 ? 32.136 -49.370 11.361 1.00 45.91 ? 72 PHE A CA 1 ATOM 534 C C . PHE A 1 72 ? 33.013 -50.122 10.353 1.00 46.04 ? 72 PHE A C 1 ATOM 535 O O . PHE A 1 72 ? 34.124 -50.570 10.663 1.00 46.99 ? 72 PHE A O 1 ATOM 536 C CB . PHE A 1 72 ? 32.070 -47.873 11.037 1.00 44.14 ? 72 PHE A CB 1 ATOM 537 C CG . PHE A 1 72 ? 33.406 -47.221 10.862 1.00 43.52 ? 72 PHE A CG 1 ATOM 538 C CD1 . PHE A 1 72 ? 34.114 -46.744 11.956 1.00 43.55 ? 72 PHE A CD1 1 ATOM 539 C CD2 . PHE A 1 72 ? 33.944 -47.053 9.600 1.00 42.15 ? 72 PHE A CD2 1 ATOM 540 C CE1 . PHE A 1 72 ? 35.343 -46.135 11.795 1.00 43.03 ? 72 PHE A CE1 1 ATOM 541 C CE2 . PHE A 1 72 ? 35.168 -46.444 9.430 1.00 41.77 ? 72 PHE A CE2 1 ATOM 542 C CZ . PHE A 1 72 ? 35.873 -45.985 10.527 1.00 42.78 ? 72 PHE A CZ 1 ATOM 543 N N . SER A 1 73 ? 32.478 -50.260 9.148 1.00 44.91 ? 73 SER A N 1 ATOM 544 C CA . SER A 1 73 ? 33.143 -50.940 8.057 1.00 44.15 ? 73 SER A CA 1 ATOM 545 C C . SER A 1 73 ? 32.903 -50.113 6.800 1.00 42.04 ? 73 SER A C 1 ATOM 546 O O . SER A 1 73 ? 31.784 -49.648 6.587 1.00 42.20 ? 73 SER A O 1 ATOM 547 C CB . SER A 1 73 ? 32.565 -52.341 7.912 1.00 45.86 ? 73 SER A CB 1 ATOM 548 O OG . SER A 1 73 ? 33.367 -53.127 7.057 1.00 47.43 ? 73 SER A OG 1 ATOM 549 N N . ALA A 1 74 ? 33.941 -49.904 5.984 1.00 40.15 ? 74 ALA A N 1 ATOM 550 C CA . ALA A 1 74 ? 33.859 -48.921 4.896 1.00 39.37 ? 74 ALA A CA 1 ATOM 551 C C . ALA A 1 74 ? 34.896 -49.049 3.771 1.00 38.70 ? 74 ALA A C 1 ATOM 552 O O . ALA A 1 74 ? 36.022 -49.501 3.995 1.00 39.25 ? 74 ALA A O 1 ATOM 553 C CB . ALA A 1 74 ? 33.946 -47.523 5.485 1.00 38.94 ? 74 ALA A CB 1 ATOM 554 N N . ASP A 1 75 ? 34.487 -48.637 2.569 1.00 37.08 ? 75 ASP A N 1 ATOM 555 C CA . ASP A 1 75 ? 35.394 -48.340 1.462 1.00 36.61 ? 75 ASP A CA 1 ATOM 556 C C . ASP A 1 75 ? 35.710 -46.840 1.436 1.00 35.46 ? 75 ASP A C 1 ATOM 557 O O . ASP A 1 75 ? 36.827 -46.427 1.103 1.00 35.05 ? 75 ASP A O 1 ATOM 558 C CB . ASP A 1 75 ? 34.766 -48.715 0.113 1.00 36.83 ? 75 ASP A CB 1 ATOM 559 C CG . ASP A 1 75 ? 34.380 -50.175 0.028 1.00 38.69 ? 75 ASP A CG 1 ATOM 560 O OD1 . ASP A 1 75 ? 35.166 -51.038 0.473 1.00 39.70 ? 75 ASP A OD1 1 ATOM 561 O OD2 . ASP A 1 75 ? 33.285 -50.467 -0.497 1.00 40.56 ? 75 ASP A OD2 1 ATOM 562 N N . LEU A 1 76 ? 34.708 -46.031 1.756 1.00 35.14 ? 76 LEU A N 1 ATOM 563 C CA . LEU A 1 76 ? 34.837 -44.586 1.728 1.00 35.19 ? 76 LEU A CA 1 ATOM 564 C C . LEU A 1 76 ? 34.376 -44.022 3.073 1.00 35.78 ? 76 LEU A C 1 ATOM 565 O O . LEU A 1 76 ? 33.306 -44.378 3.568 1.00 37.27 ? 76 LEU A O 1 ATOM 566 C CB . LEU A 1 76 ? 34.007 -44.023 0.578 1.00 35.04 ? 76 LEU A CB 1 ATOM 567 C CG . LEU A 1 76 ? 33.963 -42.510 0.382 1.00 35.21 ? 76 LEU A CG 1 ATOM 568 C CD1 . LEU A 1 76 ? 35.327 -41.976 -0.024 1.00 35.10 ? 76 LEU A CD1 1 ATOM 569 C CD2 . LEU A 1 76 ? 32.922 -42.163 -0.667 1.00 35.44 ? 76 LEU A CD2 1 ATOM 570 N N . ILE A 1 77 ? 35.196 -43.159 3.664 1.00 34.94 ? 77 ILE A N 1 ATOM 571 C CA . ILE A 1 77 ? 34.892 -42.533 4.947 1.00 35.25 ? 77 ILE A CA 1 ATOM 572 C C . ILE A 1 77 ? 34.830 -41.021 4.745 1.00 35.39 ? 77 ILE A C 1 ATOM 573 O O . ILE A 1 77 ? 35.780 -40.439 4.210 1.00 35.98 ? 77 ILE A O 1 ATOM 574 C CB . ILE A 1 77 ? 35.992 -42.846 5.984 1.00 35.47 ? 77 ILE A CB 1 ATOM 575 C CG1 . ILE A 1 77 ? 36.063 -44.353 6.251 1.00 35.69 ? 77 ILE A CG1 1 ATOM 576 C CG2 . ILE A 1 77 ? 35.742 -42.089 7.280 1.00 36.28 ? 77 ILE A CG2 1 ATOM 577 C CD1 . ILE A 1 77 ? 37.318 -44.796 6.971 1.00 35.84 ? 77 ILE A CD1 1 ATOM 578 N N . ILE A 1 78 ? 33.734 -40.394 5.180 1.00 35.31 ? 78 ILE A N 1 ATOM 579 C CA . ILE A 1 78 ? 33.527 -38.958 5.007 1.00 35.66 ? 78 ILE A CA 1 ATOM 580 C C . ILE A 1 78 ? 33.521 -38.226 6.353 1.00 36.47 ? 78 ILE A C 1 ATOM 581 O O . ILE A 1 78 ? 32.677 -38.487 7.201 1.00 36.43 ? 78 ILE A O 1 ATOM 582 C CB . ILE A 1 78 ? 32.195 -38.648 4.290 1.00 36.66 ? 78 ILE A CB 1 ATOM 583 C CG1 . ILE A 1 78 ? 32.059 -39.446 2.989 1.00 36.60 ? 78 ILE A CG1 1 ATOM 584 C CG2 . ILE A 1 78 ? 32.101 -37.164 3.972 1.00 36.87 ? 78 ILE A CG2 1 ATOM 585 C CD1 . ILE A 1 78 ? 30.679 -39.341 2.375 1.00 37.65 ? 78 ILE A CD1 1 ATOM 586 N N . GLU A 1 79 ? 34.472 -37.309 6.531 1.00 36.84 ? 79 GLU A N 1 ATOM 587 C CA . GLU A 1 79 ? 34.529 -36.444 7.705 1.00 37.58 ? 79 GLU A CA 1 ATOM 588 C C . GLU A 1 79 ? 33.755 -35.155 7.426 1.00 38.18 ? 79 GLU A C 1 ATOM 589 O O . GLU A 1 79 ? 33.819 -34.617 6.312 1.00 37.32 ? 79 GLU A O 1 ATOM 590 C CB . GLU A 1 79 ? 35.976 -36.076 8.032 1.00 37.88 ? 79 GLU A CB 1 ATOM 591 C CG . GLU A 1 79 ? 36.876 -37.227 8.438 1.00 37.72 ? 79 GLU A CG 1 ATOM 592 C CD . GLU A 1 79 ? 38.266 -36.746 8.828 1.00 37.88 ? 79 GLU A CD 1 ATOM 593 O OE1 . GLU A 1 79 ? 39.102 -36.513 7.932 1.00 36.46 ? 79 GLU A OE1 1 ATOM 594 O OE2 . GLU A 1 79 ? 38.514 -36.577 10.040 1.00 40.03 ? 79 GLU A OE2 1 ATOM 595 N N . ARG A 1 80 ? 33.045 -34.661 8.437 1.00 38.89 ? 80 ARG A N 1 ATOM 596 C CA . ARG A 1 80 ? 32.255 -33.432 8.314 1.00 40.65 ? 80 ARG A CA 1 ATOM 597 C C . ARG A 1 80 ? 32.765 -32.349 9.259 1.00 42.30 ? 80 ARG A C 1 ATOM 598 O O . ARG A 1 80 ? 33.317 -32.654 10.309 1.00 42.25 ? 80 ARG A O 1 ATOM 599 C CB . ARG A 1 80 ? 30.782 -33.708 8.626 1.00 40.86 ? 80 ARG A CB 1 ATOM 600 C CG . ARG A 1 80 ? 30.147 -34.803 7.784 1.00 40.21 ? 80 ARG A CG 1 ATOM 601 C CD . ARG A 1 80 ? 30.134 -34.413 6.322 1.00 39.85 ? 80 ARG A CD 1 ATOM 602 N NE . ARG A 1 80 ? 29.226 -35.224 5.526 1.00 39.83 ? 80 ARG A NE 1 ATOM 603 C CZ . ARG A 1 80 ? 29.023 -35.049 4.223 1.00 40.44 ? 80 ARG A CZ 1 ATOM 604 N NH1 . ARG A 1 80 ? 29.652 -34.084 3.566 1.00 41.18 ? 80 ARG A NH1 1 ATOM 605 N NH2 . ARG A 1 80 ? 28.180 -35.834 3.573 1.00 41.07 ? 80 ARG A NH2 1 ATOM 606 N N . ARG A 1 81 ? 32.552 -31.087 8.893 1.00 44.08 ? 81 ARG A N 1 ATOM 607 C CA . ARG A 1 81 ? 32.985 -29.966 9.727 1.00 46.99 ? 81 ARG A CA 1 ATOM 608 C C . ARG A 1 81 ? 32.405 -30.030 11.149 1.00 47.89 ? 81 ARG A C 1 ATOM 609 O O . ARG A 1 81 ? 33.089 -29.687 12.115 1.00 47.52 ? 81 ARG A O 1 ATOM 610 C CB . ARG A 1 81 ? 32.616 -28.626 9.075 1.00 50.52 ? 81 ARG A CB 1 ATOM 611 C CG . ARG A 1 81 ? 33.584 -27.504 9.417 1.00 53.86 ? 81 ARG A CG 1 ATOM 612 C CD . ARG A 1 81 ? 33.281 -26.217 8.669 1.00 57.11 ? 81 ARG A CD 1 ATOM 613 N NE . ARG A 1 81 ? 34.504 -25.637 8.105 1.00 60.66 ? 81 ARG A NE 1 ATOM 614 C CZ . ARG A 1 81 ? 34.982 -25.889 6.884 1.00 61.45 ? 81 ARG A CZ 1 ATOM 615 N NH1 . ARG A 1 81 ? 34.343 -26.709 6.052 1.00 62.95 ? 81 ARG A NH1 1 ATOM 616 N NH2 . ARG A 1 81 ? 36.110 -25.313 6.481 1.00 62.73 ? 81 ARG A NH2 1 ATOM 617 N N . GLU A 1 82 ? 31.156 -30.485 11.271 1.00 47.58 ? 82 GLU A N 1 ATOM 618 C CA . GLU A 1 82 ? 30.487 -30.566 12.571 1.00 48.77 ? 82 GLU A CA 1 ATOM 619 C C . GLU A 1 82 ? 30.985 -31.730 13.447 1.00 48.06 ? 82 GLU A C 1 ATOM 620 O O . GLU A 1 82 ? 30.549 -31.876 14.585 1.00 48.74 ? 82 GLU A O 1 ATOM 621 C CB . GLU A 1 82 ? 28.947 -30.620 12.406 1.00 50.13 ? 82 GLU A CB 1 ATOM 622 C CG . GLU A 1 82 ? 28.348 -31.905 11.804 1.00 49.77 ? 82 GLU A CG 1 ATOM 623 C CD . GLU A 1 82 ? 28.236 -31.889 10.277 1.00 50.16 ? 82 GLU A CD 1 ATOM 624 O OE1 . GLU A 1 82 ? 28.885 -31.025 9.630 1.00 50.61 ? 82 GLU A OE1 1 ATOM 625 O OE2 . GLU A 1 82 ? 27.505 -32.749 9.717 1.00 49.73 ? 82 GLU A OE2 1 ATOM 626 N N . GLY A 1 83 ? 31.885 -32.558 12.924 1.00 46.60 ? 83 GLY A N 1 ATOM 627 C CA . GLY A 1 83 ? 32.400 -33.695 13.680 1.00 46.21 ? 83 GLY A CA 1 ATOM 628 C C . GLY A 1 83 ? 33.153 -33.282 14.933 1.00 47.16 ? 83 GLY A C 1 ATOM 629 O O . GLY A 1 83 ? 33.868 -32.283 14.925 1.00 49.00 ? 83 GLY A O 1 ATOM 630 N N . SER A 1 84 ? 32.987 -34.042 16.014 1.00 46.55 ? 84 SER A N 1 ATOM 631 C CA . SER A 1 84 ? 33.764 -33.834 17.231 1.00 46.47 ? 84 SER A CA 1 ATOM 632 C C . SER A 1 84 ? 34.306 -35.162 17.742 1.00 45.34 ? 84 SER A C 1 ATOM 633 O O . SER A 1 84 ? 33.571 -36.147 17.832 1.00 45.59 ? 84 SER A O 1 ATOM 634 C CB . SER A 1 84 ? 32.919 -33.164 18.310 1.00 48.63 ? 84 SER A CB 1 ATOM 635 O OG . SER A 1 84 ? 33.675 -32.978 19.494 1.00 49.43 ? 84 SER A OG 1 ATOM 636 N N . ASP A 1 85 ? 35.600 -35.172 18.055 1.00 44.45 ? 85 ASP A N 1 ATOM 637 C CA . ASP A 1 85 ? 36.311 -36.346 18.579 1.00 43.73 ? 85 ASP A CA 1 ATOM 638 C C . ASP A 1 85 ? 36.073 -36.560 20.076 1.00 44.89 ? 85 ASP A C 1 ATOM 639 O O . ASP A 1 85 ? 36.409 -37.623 20.613 1.00 45.22 ? 85 ASP A O 1 ATOM 640 C CB . ASP A 1 85 ? 37.831 -36.179 18.373 1.00 43.06 ? 85 ASP A CB 1 ATOM 641 C CG . ASP A 1 85 ? 38.254 -36.263 16.918 1.00 42.03 ? 85 ASP A CG 1 ATOM 642 O OD1 . ASP A 1 85 ? 37.704 -37.102 16.187 1.00 41.37 ? 85 ASP A OD1 1 ATOM 643 O OD2 . ASP A 1 85 ? 39.172 -35.517 16.504 1.00 42.54 ? 85 ASP A OD2 1 ATOM 644 N N . VAL A 1 86 ? 35.523 -35.552 20.752 1.00 45.56 ? 86 VAL A N 1 ATOM 645 C CA . VAL A 1 86 ? 35.433 -35.575 22.213 1.00 47.10 ? 86 VAL A CA 1 ATOM 646 C C . VAL A 1 86 ? 34.048 -35.225 22.730 1.00 48.34 ? 86 VAL A C 1 ATOM 647 O O . VAL A 1 86 ? 33.236 -34.616 22.036 1.00 48.15 ? 86 VAL A O 1 ATOM 648 C CB . VAL A 1 86 ? 36.439 -34.594 22.868 1.00 48.11 ? 86 VAL A CB 1 ATOM 649 C CG1 . VAL A 1 86 ? 37.868 -35.080 22.695 1.00 47.53 ? 86 VAL A CG1 1 ATOM 650 C CG2 . VAL A 1 86 ? 36.284 -33.179 22.312 1.00 48.55 ? 86 VAL A CG2 1 ATOM 651 N N . CYS A 1 87 ? 33.793 -35.628 23.963 1.00 50.53 ? 87 CYS A N 1 ATOM 652 C CA . CYS A 1 87 ? 32.667 -35.124 24.714 1.00 52.50 ? 87 CYS A CA 1 ATOM 653 C C . CYS A 1 87 ? 33.256 -34.323 25.860 1.00 54.56 ? 87 CYS A C 1 ATOM 654 O O . CYS A 1 87 ? 33.060 -33.103 25.929 1.00 55.95 ? 87 CYS A O 1 ATOM 655 C CB . CYS A 1 87 ? 31.744 -36.260 25.187 1.00 53.28 ? 87 CYS A CB 1 ATOM 656 S SG . CYS A 1 87 ? 32.505 -37.651 26.070 1.00 53.60 ? 87 CYS A SG 1 ATOM 657 N N . TYR A 1 88 ? 34.009 -34.987 26.737 1.00 54.75 ? 88 TYR A N 1 ATOM 658 C CA . TYR A 1 88 ? 34.778 -34.272 27.750 1.00 56.12 ? 88 TYR A CA 1 ATOM 659 C C . TYR A 1 88 ? 35.955 -33.568 27.065 1.00 56.27 ? 88 TYR A C 1 ATOM 660 O O . TYR A 1 88 ? 36.682 -34.202 26.293 1.00 55.63 ? 88 TYR A O 1 ATOM 661 C CB . TYR A 1 88 ? 35.291 -35.214 28.839 1.00 56.45 ? 88 TYR A CB 1 ATOM 662 C CG . TYR A 1 88 ? 35.828 -34.487 30.063 1.00 57.93 ? 88 TYR A CG 1 ATOM 663 C CD1 . TYR A 1 88 ? 34.989 -34.143 31.115 1.00 59.84 ? 88 TYR A CD1 1 ATOM 664 C CD2 . TYR A 1 88 ? 37.173 -34.136 30.158 1.00 58.16 ? 88 TYR A CD2 1 ATOM 665 C CE1 . TYR A 1 88 ? 35.472 -33.474 32.234 1.00 61.64 ? 88 TYR A CE1 1 ATOM 666 C CE2 . TYR A 1 88 ? 37.668 -33.467 31.264 1.00 59.84 ? 88 TYR A CE2 1 ATOM 667 C CZ . TYR A 1 88 ? 36.813 -33.139 32.302 1.00 61.69 ? 88 TYR A CZ 1 ATOM 668 O OH . TYR A 1 88 ? 37.295 -32.481 33.403 1.00 62.63 ? 88 TYR A OH 1 ATOM 669 N N . PRO A 1 89 ? 36.153 -32.262 27.344 1.00 58.06 ? 89 PRO A N 1 ATOM 670 C CA . PRO A 1 89 ? 37.212 -31.509 26.657 1.00 58.44 ? 89 PRO A CA 1 ATOM 671 C C . PRO A 1 89 ? 38.567 -32.206 26.706 1.00 58.57 ? 89 PRO A C 1 ATOM 672 O O . PRO A 1 89 ? 38.942 -32.775 27.735 1.00 59.42 ? 89 PRO A O 1 ATOM 673 C CB . PRO A 1 89 ? 37.267 -30.189 27.426 1.00 60.16 ? 89 PRO A CB 1 ATOM 674 C CG . PRO A 1 89 ? 35.903 -30.028 27.989 1.00 61.16 ? 89 PRO A CG 1 ATOM 675 C CD . PRO A 1 89 ? 35.431 -31.418 28.314 1.00 60.07 ? 89 PRO A CD 1 ATOM 676 N N . GLY A 1 90 ? 39.282 -32.156 25.590 1.00 58.24 ? 90 GLY A N 1 ATOM 677 C CA . GLY A 1 90 ? 40.562 -32.844 25.444 1.00 58.46 ? 90 GLY A CA 1 ATOM 678 C C . GLY A 1 90 ? 40.969 -32.944 23.984 1.00 57.56 ? 90 GLY A C 1 ATOM 679 O O . GLY A 1 90 ? 40.217 -32.549 23.095 1.00 57.15 ? 90 GLY A O 1 ATOM 680 N N . LYS A 1 91 ? 42.162 -33.469 23.735 1.00 58.09 ? 91 LYS A N 1 ATOM 681 C CA . LYS A 1 91 ? 42.623 -33.697 22.376 1.00 58.65 ? 91 LYS A CA 1 ATOM 682 C C . LYS A 1 91 ? 43.519 -34.931 22.320 1.00 58.05 ? 91 LYS A C 1 ATOM 683 O O . LYS A 1 91 ? 43.847 -35.509 23.356 1.00 59.46 ? 91 LYS A O 1 ATOM 684 C CB . LYS A 1 91 ? 43.379 -32.467 21.855 1.00 61.00 ? 91 LYS A CB 1 ATOM 685 C CG . LYS A 1 91 ? 44.616 -32.113 22.662 1.00 63.95 ? 91 LYS A CG 1 ATOM 686 C CD . LYS A 1 91 ? 45.733 -31.527 21.805 1.00 66.28 ? 91 LYS A CD 1 ATOM 687 C CE . LYS A 1 91 ? 45.391 -30.148 21.254 1.00 67.17 ? 91 LYS A CE 1 ATOM 688 N NZ . LYS A 1 91 ? 44.673 -30.201 19.946 1.00 66.10 ? 91 LYS A NZ 1 ATOM 689 N N . PHE A 1 92 ? 43.907 -35.316 21.106 1.00 56.46 ? 92 PHE A N 1 ATOM 690 C CA . PHE A 1 92 ? 44.849 -36.419 20.875 1.00 55.96 ? 92 PHE A CA 1 ATOM 691 C C . PHE A 1 92 ? 46.257 -35.911 20.597 1.00 56.05 ? 92 PHE A C 1 ATOM 692 O O . PHE A 1 92 ? 46.429 -34.942 19.867 1.00 56.51 ? 92 PHE A O 1 ATOM 693 C CB . PHE A 1 92 ? 44.421 -37.249 19.659 1.00 54.13 ? 92 PHE A CB 1 ATOM 694 C CG . PHE A 1 92 ? 43.402 -38.302 19.959 1.00 53.14 ? 92 PHE A CG 1 ATOM 695 C CD1 . PHE A 1 92 ? 42.058 -37.980 20.054 1.00 53.30 ? 92 PHE A CD1 1 ATOM 696 C CD2 . PHE A 1 92 ? 43.786 -39.627 20.102 1.00 52.79 ? 92 PHE A CD2 1 ATOM 697 C CE1 . PHE A 1 92 ? 41.112 -38.960 20.308 1.00 52.49 ? 92 PHE A CE1 1 ATOM 698 C CE2 . PHE A 1 92 ? 42.851 -40.607 20.362 1.00 52.83 ? 92 PHE A CE2 1 ATOM 699 C CZ . PHE A 1 92 ? 41.510 -40.274 20.461 1.00 52.11 ? 92 PHE A CZ 1 ATOM 700 N N . VAL A 1 93 ? 47.254 -36.591 21.159 1.00 57.28 ? 93 VAL A N 1 ATOM 701 C CA . VAL A 1 93 ? 48.653 -36.401 20.788 1.00 57.47 ? 93 VAL A CA 1 ATOM 702 C C . VAL A 1 93 ? 48.908 -37.188 19.501 1.00 56.60 ? 93 VAL A C 1 ATOM 703 O O . VAL A 1 93 ? 48.444 -38.323 19.365 1.00 55.82 ? 93 VAL A O 1 ATOM 704 C CB . VAL A 1 93 ? 49.591 -36.910 21.902 1.00 60.35 ? 93 VAL A CB 1 ATOM 705 C CG1 . VAL A 1 93 ? 51.053 -36.811 21.481 1.00 60.71 ? 93 VAL A CG1 1 ATOM 706 C CG2 . VAL A 1 93 ? 49.346 -36.144 23.202 1.00 61.59 ? 93 VAL A CG2 1 ATOM 707 N N . ASN A 1 94 ? 49.644 -36.591 18.561 1.00 56.61 ? 94 ASN A N 1 ATOM 708 C CA . ASN A 1 94 ? 49.863 -37.189 17.241 1.00 55.23 ? 94 ASN A CA 1 ATOM 709 C C . ASN A 1 94 ? 48.528 -37.447 16.532 1.00 52.04 ? 94 ASN A C 1 ATOM 710 O O . ASN A 1 94 ? 48.263 -38.553 16.049 1.00 50.22 ? 94 ASN A O 1 ATOM 711 C CB . ASN A 1 94 ? 50.680 -38.494 17.359 1.00 56.85 ? 94 ASN A CB 1 ATOM 712 C CG . ASN A 1 94 ? 52.134 -38.311 16.986 1.00 59.53 ? 94 ASN A CG 1 ATOM 713 O OD1 . ASN A 1 94 ? 52.892 -37.633 17.687 1.00 60.71 ? 94 ASN A OD1 1 ATOM 714 N ND2 . ASN A 1 94 ? 52.540 -38.931 15.878 1.00 59.80 ? 94 ASN A ND2 1 ATOM 715 N N . GLU A 1 95 ? 47.692 -36.416 16.469 1.00 50.39 ? 95 GLU A N 1 ATOM 716 C CA . GLU A 1 95 ? 46.314 -36.595 16.023 1.00 48.80 ? 95 GLU A CA 1 ATOM 717 C C . GLU A 1 95 ? 46.170 -36.856 14.528 1.00 46.43 ? 95 GLU A C 1 ATOM 718 O O . GLU A 1 95 ? 45.356 -37.684 14.125 1.00 45.27 ? 95 GLU A O 1 ATOM 719 C CB . GLU A 1 95 ? 45.425 -35.426 16.455 1.00 49.98 ? 95 GLU A CB 1 ATOM 720 C CG . GLU A 1 95 ? 45.711 -34.077 15.823 1.00 51.22 ? 95 GLU A CG 1 ATOM 721 C CD . GLU A 1 95 ? 44.711 -33.026 16.278 1.00 53.23 ? 95 GLU A CD 1 ATOM 722 O OE1 . GLU A 1 95 ? 44.850 -32.501 17.407 1.00 55.07 ? 95 GLU A OE1 1 ATOM 723 O OE2 . GLU A 1 95 ? 43.765 -32.740 15.512 1.00 54.03 ? 95 GLU A OE2 1 ATOM 724 N N . GLU A 1 96 ? 46.944 -36.159 13.707 1.00 44.76 ? 96 GLU A N 1 ATOM 725 C CA . GLU A 1 96 ? 46.764 -36.263 12.261 1.00 43.53 ? 96 GLU A CA 1 ATOM 726 C C . GLU A 1 96 ? 47.278 -37.588 11.699 1.00 42.11 ? 96 GLU A C 1 ATOM 727 O O . GLU A 1 96 ? 46.680 -38.133 10.781 1.00 39.69 ? 96 GLU A O 1 ATOM 728 C CB . GLU A 1 96 ? 47.417 -35.092 11.522 1.00 43.33 ? 96 GLU A CB 1 ATOM 729 C CG . GLU A 1 96 ? 46.903 -34.930 10.096 1.00 42.39 ? 96 GLU A CG 1 ATOM 730 C CD . GLU A 1 96 ? 45.397 -34.723 10.011 1.00 41.60 ? 96 GLU A CD 1 ATOM 731 O OE1 . GLU A 1 96 ? 44.799 -34.213 10.979 1.00 41.90 ? 96 GLU A OE1 1 ATOM 732 O OE2 . GLU A 1 96 ? 44.803 -35.054 8.963 1.00 41.26 ? 96 GLU A OE2 1 ATOM 733 N N . ALA A 1 97 ? 48.386 -38.085 12.245 1.00 42.77 ? 97 ALA A N 1 ATOM 734 C CA . ALA A 1 97 ? 48.877 -39.416 11.908 1.00 42.89 ? 97 ALA A CA 1 ATOM 735 C C . ALA A 1 97 ? 47.784 -40.468 12.130 1.00 42.27 ? 97 ALA A C 1 ATOM 736 O O . ALA A 1 97 ? 47.512 -41.289 11.250 1.00 41.24 ? 97 ALA A O 1 ATOM 737 C CB . ALA A 1 97 ? 50.109 -39.748 12.735 1.00 44.89 ? 97 ALA A CB 1 ATOM 738 N N . LEU A 1 98 ? 47.143 -40.419 13.295 1.00 42.38 ? 98 LEU A N 1 ATOM 739 C CA . LEU A 1 98 ? 46.081 -41.361 13.620 1.00 41.78 ? 98 LEU A CA 1 ATOM 740 C C . LEU A 1 98 ? 44.910 -41.243 12.645 1.00 40.79 ? 98 LEU A C 1 ATOM 741 O O . LEU A 1 98 ? 44.342 -42.261 12.232 1.00 40.01 ? 98 LEU A O 1 ATOM 742 C CB . LEU A 1 98 ? 45.593 -41.163 15.056 1.00 42.63 ? 98 LEU A CB 1 ATOM 743 C CG . LEU A 1 98 ? 44.519 -42.137 15.570 1.00 42.10 ? 98 LEU A CG 1 ATOM 744 C CD1 . LEU A 1 98 ? 44.950 -43.581 15.375 1.00 42.19 ? 98 LEU A CD1 1 ATOM 745 C CD2 . LEU A 1 98 ? 44.228 -41.868 17.041 1.00 43.06 ? 98 LEU A CD2 1 ATOM 746 N N . ARG A 1 99 ? 44.558 -40.016 12.268 1.00 39.94 ? 99 ARG A N 1 ATOM 747 C CA . ARG A 1 99 ? 43.504 -39.819 11.285 1.00 39.23 ? 99 ARG A CA 1 ATOM 748 C C . ARG A 1 99 ? 43.875 -40.503 9.986 1.00 39.08 ? 99 ARG A C 1 ATOM 749 O O . ARG A 1 99 ? 43.039 -41.161 9.366 1.00 39.97 ? 99 ARG A O 1 ATOM 750 C CB . ARG A 1 99 ? 43.231 -38.336 11.032 1.00 39.02 ? 99 ARG A CB 1 ATOM 751 C CG . ARG A 1 99 ? 42.514 -37.641 12.175 1.00 39.44 ? 99 ARG A CG 1 ATOM 752 C CD . ARG A 1 99 ? 41.753 -36.409 11.717 1.00 39.30 ? 99 ARG A CD 1 ATOM 753 N NE . ARG A 1 99 ? 41.163 -35.716 12.866 1.00 39.81 ? 99 ARG A NE 1 ATOM 754 C CZ . ARG A 1 99 ? 41.800 -34.852 13.653 1.00 41.03 ? 99 ARG A CZ 1 ATOM 755 N NH1 . ARG A 1 99 ? 43.075 -34.519 13.432 1.00 41.36 ? 99 ARG A NH1 1 ATOM 756 N NH2 . ARG A 1 99 ? 41.151 -34.312 14.679 1.00 41.96 ? 99 ARG A NH2 1 ATOM 757 N N . GLN A 1 100 ? 45.133 -40.365 9.581 1.00 38.94 ? 100 GLN A N 1 ATOM 758 C CA . GLN A 1 100 ? 45.577 -40.947 8.324 1.00 38.22 ? 100 GLN A CA 1 ATOM 759 C C . GLN A 1 100 ? 45.490 -42.472 8.370 1.00 38.09 ? 100 GLN A C 1 ATOM 760 O O . GLN A 1 100 ? 45.093 -43.091 7.390 1.00 36.94 ? 100 GLN A O 1 ATOM 761 C CB . GLN A 1 100 ? 46.979 -40.448 7.952 1.00 38.40 ? 100 GLN A CB 1 ATOM 762 C CG . GLN A 1 100 ? 46.952 -38.988 7.509 1.00 38.20 ? 100 GLN A CG 1 ATOM 763 C CD . GLN A 1 100 ? 48.313 -38.316 7.454 1.00 38.21 ? 100 GLN A CD 1 ATOM 764 O OE1 . GLN A 1 100 ? 49.342 -38.911 7.775 1.00 38.54 ? 100 GLN A OE1 1 ATOM 765 N NE2 . GLN A 1 100 ? 48.319 -37.057 7.034 1.00 38.34 ? 100 GLN A NE2 1 ATOM 766 N N . ILE A 1 101 ? 45.831 -43.062 9.513 1.00 38.94 ? 101 ILE A N 1 ATOM 767 C CA . ILE A 1 101 ? 45.705 -44.504 9.717 1.00 39.72 ? 101 ILE A CA 1 ATOM 768 C C . ILE A 1 101 ? 44.245 -44.948 9.584 1.00 39.71 ? 101 ILE A C 1 ATOM 769 O O . ILE A 1 101 ? 43.947 -45.916 8.890 1.00 40.86 ? 101 ILE A O 1 ATOM 770 C CB . ILE A 1 101 ? 46.266 -44.928 11.097 1.00 41.04 ? 101 ILE A CB 1 ATOM 771 C CG1 . ILE A 1 101 ? 47.796 -44.838 11.098 1.00 41.97 ? 101 ILE A CG1 1 ATOM 772 C CG2 . ILE A 1 101 ? 45.843 -46.347 11.462 1.00 41.51 ? 101 ILE A CG2 1 ATOM 773 C CD1 . ILE A 1 101 ? 48.411 -44.928 12.481 1.00 43.33 ? 101 ILE A CD1 1 ATOM 774 N N . LEU A 1 102 ? 43.338 -44.229 10.234 1.00 39.61 ? 102 LEU A N 1 ATOM 775 C CA . LEU A 1 102 ? 41.926 -44.607 10.247 1.00 38.63 ? 102 LEU A CA 1 ATOM 776 C C . LEU A 1 102 ? 41.220 -44.337 8.917 1.00 37.74 ? 102 LEU A C 1 ATOM 777 O O . LEU A 1 102 ? 40.299 -45.064 8.548 1.00 36.92 ? 102 LEU A O 1 ATOM 778 C CB . LEU A 1 102 ? 41.196 -43.923 11.404 1.00 38.86 ? 102 LEU A CB 1 ATOM 779 C CG . LEU A 1 102 ? 41.700 -44.324 12.790 1.00 39.88 ? 102 LEU A CG 1 ATOM 780 C CD1 . LEU A 1 102 ? 41.025 -43.494 13.876 1.00 39.99 ? 102 LEU A CD1 1 ATOM 781 C CD2 . LEU A 1 102 ? 41.483 -45.822 13.034 1.00 40.71 ? 102 LEU A CD2 1 ATOM 782 N N . ARG A 1 103 ? 41.659 -43.323 8.179 1.00 37.66 ? 103 ARG A N 1 ATOM 783 C CA . ARG A 1 103 ? 41.056 -43.046 6.873 1.00 37.36 ? 103 ARG A CA 1 ATOM 784 C C . ARG A 1 103 ? 41.198 -44.215 5.895 1.00 37.56 ? 103 ARG A C 1 ATOM 785 O O . ARG A 1 103 ? 40.279 -44.490 5.121 1.00 37.74 ? 103 ARG A O 1 ATOM 786 C CB . ARG A 1 103 ? 41.615 -41.760 6.255 1.00 37.07 ? 103 ARG A CB 1 ATOM 787 C CG . ARG A 1 103 ? 41.066 -40.485 6.886 1.00 37.66 ? 103 ARG A CG 1 ATOM 788 C CD . ARG A 1 103 ? 41.348 -39.248 6.038 1.00 37.19 ? 103 ARG A CD 1 ATOM 789 N NE . ARG A 1 103 ? 41.246 -38.016 6.820 1.00 37.31 ? 103 ARG A NE 1 ATOM 790 C CZ . ARG A 1 103 ? 42.269 -37.282 7.257 1.00 38.42 ? 103 ARG A CZ 1 ATOM 791 N NH1 . ARG A 1 103 ? 43.537 -37.610 6.994 1.00 38.38 ? 103 ARG A NH1 1 ATOM 792 N NH2 . ARG A 1 103 ? 42.017 -36.185 7.964 1.00 39.76 ? 103 ARG A NH2 1 ATOM 793 N N . GLU A 1 104 ? 42.330 -44.909 5.933 1.00 38.62 ? 104 GLU A N 1 ATOM 794 C CA . GLU A 1 104 ? 42.555 -46.032 5.010 1.00 39.90 ? 104 GLU A CA 1 ATOM 795 C C . GLU A 1 104 ? 42.402 -47.403 5.664 1.00 38.24 ? 104 GLU A C 1 ATOM 796 O O . GLU A 1 104 ? 42.722 -48.413 5.059 1.00 38.05 ? 104 GLU A O 1 ATOM 797 C CB . GLU A 1 104 ? 43.933 -45.917 4.343 1.00 42.52 ? 104 GLU A CB 1 ATOM 798 C CG . GLU A 1 104 ? 45.102 -45.962 5.303 1.00 46.36 ? 104 GLU A CG 1 ATOM 799 C CD . GLU A 1 104 ? 46.440 -46.126 4.601 1.00 50.65 ? 104 GLU A CD 1 ATOM 800 O OE1 . GLU A 1 104 ? 46.527 -45.841 3.375 1.00 51.76 ? 104 GLU A OE1 1 ATOM 801 O OE2 . GLU A 1 104 ? 47.403 -46.545 5.290 1.00 51.57 ? 104 GLU A OE2 1 ATOM 802 N N . SER A 1 105 ? 41.887 -47.428 6.888 1.00 37.38 ? 105 SER A N 1 ATOM 803 C CA . SER A 1 105 ? 41.743 -48.660 7.663 1.00 37.48 ? 105 SER A CA 1 ATOM 804 C C . SER A 1 105 ? 40.737 -49.659 7.095 1.00 37.38 ? 105 SER A C 1 ATOM 805 O O . SER A 1 105 ? 40.824 -50.845 7.387 1.00 38.74 ? 105 SER A O 1 ATOM 806 C CB . SER A 1 105 ? 41.293 -48.320 9.089 1.00 37.48 ? 105 SER A CB 1 ATOM 807 O OG . SER A 1 105 ? 39.988 -47.748 9.092 1.00 35.30 ? 105 SER A OG 1 ATOM 808 N N . GLY A 1 106 ? 39.773 -49.183 6.317 1.00 36.44 ? 106 GLY A N 1 ATOM 809 C CA . GLY A 1 106 ? 38.606 -49.995 5.979 1.00 37.35 ? 106 GLY A CA 1 ATOM 810 C C . GLY A 1 106 ? 37.645 -50.131 7.157 1.00 37.82 ? 106 GLY A C 1 ATOM 811 O O . GLY A 1 106 ? 36.726 -50.952 7.124 1.00 37.96 ? 106 GLY A O 1 ATOM 812 N N . GLY A 1 107 ? 37.859 -49.315 8.193 1.00 37.57 ? 107 GLY A N 1 ATOM 813 C CA . GLY A 1 107 ? 37.100 -49.393 9.437 1.00 38.82 ? 107 GLY A CA 1 ATOM 814 C C . GLY A 1 107 ? 37.752 -50.225 10.532 1.00 39.56 ? 107 GLY A C 1 ATOM 815 O O . GLY A 1 107 ? 38.873 -50.724 10.383 1.00 39.37 ? 107 GLY A O 1 ATOM 816 N N . ILE A 1 108 ? 37.012 -50.411 11.620 1.00 40.70 ? 108 ILE A N 1 ATOM 817 C CA . ILE A 1 108 ? 37.552 -50.987 12.845 1.00 42.10 ? 108 ILE A CA 1 ATOM 818 C C . ILE A 1 108 ? 36.673 -52.072 13.451 1.00 44.02 ? 108 ILE A C 1 ATOM 819 O O . ILE A 1 108 ? 35.446 -52.002 13.404 1.00 43.01 ? 108 ILE A O 1 ATOM 820 C CB . ILE A 1 108 ? 37.763 -49.902 13.924 1.00 42.31 ? 108 ILE A CB 1 ATOM 821 C CG1 . ILE A 1 108 ? 36.440 -49.178 14.223 1.00 42.43 ? 108 ILE A CG1 1 ATOM 822 C CG2 . ILE A 1 108 ? 38.835 -48.919 13.466 1.00 42.00 ? 108 ILE A CG2 1 ATOM 823 C CD1 . ILE A 1 108 ? 36.581 -47.904 15.020 1.00 43.47 ? 108 ILE A CD1 1 ATOM 824 N N . ASP A 1 109 ? 37.343 -53.056 14.041 1.00 46.45 ? 109 ASP A N 1 ATOM 825 C CA . ASP A 1 109 ? 36.728 -54.113 14.821 1.00 49.94 ? 109 ASP A CA 1 ATOM 826 C C . ASP A 1 109 ? 37.288 -53.962 16.238 1.00 50.99 ? 109 ASP A C 1 ATOM 827 O O . ASP A 1 109 ? 38.479 -53.677 16.407 1.00 52.10 ? 109 ASP A O 1 ATOM 828 C CB . ASP A 1 109 ? 37.090 -55.462 14.193 1.00 52.88 ? 109 ASP A CB 1 ATOM 829 C CG . ASP A 1 109 ? 36.926 -56.618 15.134 1.00 56.48 ? 109 ASP A CG 1 ATOM 830 O OD1 . ASP A 1 109 ? 35.894 -56.697 15.837 1.00 61.72 ? 109 ASP A OD1 1 ATOM 831 O OD2 . ASP A 1 109 ? 37.832 -57.472 15.153 1.00 59.26 ? 109 ASP A OD2 1 ATOM 832 N N . LYS A 1 110 ? 36.436 -54.141 17.244 1.00 50.23 ? 110 LYS A N 1 ATOM 833 C CA . LYS A 1 110 ? 36.810 -53.876 18.633 1.00 50.93 ? 110 LYS A CA 1 ATOM 834 C C . LYS A 1 110 ? 36.877 -55.167 19.438 1.00 52.68 ? 110 LYS A C 1 ATOM 835 O O . LYS A 1 110 ? 36.138 -56.110 19.170 1.00 53.16 ? 110 LYS A O 1 ATOM 836 C CB . LYS A 1 110 ? 35.805 -52.918 19.283 1.00 50.23 ? 110 LYS A CB 1 ATOM 837 C CG . LYS A 1 110 ? 35.879 -51.485 18.770 1.00 48.58 ? 110 LYS A CG 1 ATOM 838 C CD . LYS A 1 110 ? 36.781 -50.609 19.624 1.00 48.24 ? 110 LYS A CD 1 ATOM 839 C CE . LYS A 1 110 ? 36.930 -49.212 19.033 1.00 47.15 ? 110 LYS A CE 1 ATOM 840 N NZ . LYS A 1 110 ? 35.650 -48.463 18.994 1.00 46.70 ? 110 LYS A NZ 1 ATOM 841 N N . GLU A 1 111 ? 37.757 -55.195 20.433 1.00 54.10 ? 111 GLU A N 1 ATOM 842 C CA . GLU A 1 111 ? 37.897 -56.363 21.296 1.00 56.21 ? 111 GLU A CA 1 ATOM 843 C C . GLU A 1 111 ? 38.339 -55.965 22.697 1.00 56.54 ? 111 GLU A C 1 ATOM 844 O O . GLU A 1 111 ? 39.187 -55.095 22.854 1.00 56.32 ? 111 GLU A O 1 ATOM 845 C CB . GLU A 1 111 ? 38.905 -57.326 20.682 1.00 57.79 ? 111 GLU A CB 1 ATOM 846 C CG . GLU A 1 111 ? 38.909 -58.717 21.284 1.00 59.98 ? 111 GLU A CG 1 ATOM 847 C CD . GLU A 1 111 ? 39.880 -59.639 20.574 1.00 61.06 ? 111 GLU A CD 1 ATOM 848 O OE1 . GLU A 1 111 ? 39.936 -59.602 19.325 1.00 60.40 ? 111 GLU A OE1 1 ATOM 849 O OE2 . GLU A 1 111 ? 40.594 -60.393 21.266 1.00 62.96 ? 111 GLU A OE2 1 ATOM 850 N N . ALA A 1 112 ? 37.766 -56.618 23.704 1.00 58.32 ? 112 ALA A N 1 ATOM 851 C CA . ALA A 1 112 ? 38.080 -56.345 25.112 1.00 59.60 ? 112 ALA A CA 1 ATOM 852 C C . ALA A 1 112 ? 39.568 -56.519 25.415 1.00 60.80 ? 112 ALA A C 1 ATOM 853 O O . ALA A 1 112 ? 40.205 -57.448 24.916 1.00 60.17 ? 112 ALA A O 1 ATOM 854 C CB . ALA A 1 112 ? 37.257 -57.249 26.022 1.00 60.61 ? 112 ALA A CB 1 ATOM 855 N N . MET A 1 113 ? 40.106 -55.611 26.229 1.00 62.29 ? 113 MET A N 1 ATOM 856 C CA . MET A 1 113 ? 41.513 -55.650 26.633 1.00 63.87 ? 113 MET A CA 1 ATOM 857 C C . MET A 1 113 ? 41.694 -56.695 27.732 1.00 64.93 ? 113 MET A C 1 ATOM 858 O O . MET A 1 113 ? 42.720 -57.370 27.790 1.00 66.10 ? 113 MET A O 1 ATOM 859 C CB . MET A 1 113 ? 41.977 -54.287 27.165 1.00 65.28 ? 113 MET A CB 1 ATOM 860 C CG . MET A 1 113 ? 41.816 -53.098 26.218 1.00 64.04 ? 113 MET A CG 1 ATOM 861 S SD . MET A 1 113 ? 43.251 -52.675 25.207 1.00 65.44 ? 113 MET A SD 1 ATOM 862 C CE . MET A 1 113 ? 44.581 -52.683 26.405 1.00 66.89 ? 113 MET A CE 1 ATOM 863 N N . GLY A 1 114 ? 40.702 -56.804 28.612 1.00 64.06 ? 114 GLY A N 1 ATOM 864 C CA . GLY A 1 114 ? 40.722 -57.781 29.692 1.00 65.71 ? 114 GLY A CA 1 ATOM 865 C C . GLY A 1 114 ? 41.174 -57.258 31.047 1.00 67.05 ? 114 GLY A C 1 ATOM 866 O O . GLY A 1 114 ? 41.451 -58.053 31.951 1.00 68.92 ? 114 GLY A O 1 ATOM 867 N N . PHE A 1 115 ? 41.236 -55.936 31.210 1.00 71.24 ? 115 PHE A N 1 ATOM 868 C CA . PHE A 1 115 ? 41.640 -55.343 32.488 1.00 72.47 ? 115 PHE A CA 1 ATOM 869 C C . PHE A 1 115 ? 40.572 -55.512 33.568 1.00 74.13 ? 115 PHE A C 1 ATOM 870 O O . PHE A 1 115 ? 39.395 -55.235 33.338 1.00 73.22 ? 115 PHE A O 1 ATOM 871 C CB . PHE A 1 115 ? 41.954 -53.849 32.340 1.00 70.48 ? 115 PHE A CB 1 ATOM 872 C CG . PHE A 1 115 ? 43.167 -53.545 31.497 1.00 69.78 ? 115 PHE A CG 1 ATOM 873 C CD1 . PHE A 1 115 ? 44.157 -54.494 31.266 1.00 71.19 ? 115 PHE A CD1 1 ATOM 874 C CD2 . PHE A 1 115 ? 43.312 -52.290 30.932 1.00 67.91 ? 115 PHE A CD2 1 ATOM 875 C CE1 . PHE A 1 115 ? 45.258 -54.189 30.493 1.00 70.85 ? 115 PHE A CE1 1 ATOM 876 C CE2 . PHE A 1 115 ? 44.418 -51.978 30.161 1.00 67.66 ? 115 PHE A CE2 1 ATOM 877 C CZ . PHE A 1 115 ? 45.393 -52.930 29.941 1.00 69.32 ? 115 PHE A CZ 1 ATOM 878 N N . THR A 1 116 ? 41.006 -55.974 34.740 1.00 76.98 ? 116 THR A N 1 ATOM 879 C CA . THR A 1 116 ? 40.171 -56.046 35.935 1.00 78.95 ? 116 THR A CA 1 ATOM 880 C C . THR A 1 116 ? 40.859 -55.254 37.042 1.00 80.56 ? 116 THR A C 1 ATOM 881 O O . THR A 1 116 ? 42.088 -55.193 37.092 1.00 81.52 ? 116 THR A O 1 ATOM 882 C CB . THR A 1 116 ? 39.985 -57.495 36.394 1.00 81.84 ? 116 THR A CB 1 ATOM 883 O OG1 . THR A 1 116 ? 41.269 -58.112 36.535 1.00 83.59 ? 116 THR A OG1 1 ATOM 884 C CG2 . THR A 1 116 ? 39.163 -58.268 35.380 1.00 80.85 ? 116 THR A CG2 1 ATOM 885 N N . TYR A 1 117 ? 40.073 -54.658 37.933 1.00 81.02 ? 117 TYR A N 1 ATOM 886 C CA . TYR A 1 117 ? 40.613 -53.703 38.902 1.00 82.15 ? 117 TYR A CA 1 ATOM 887 C C . TYR A 1 117 ? 40.253 -54.043 40.347 1.00 85.75 ? 117 TYR A C 1 ATOM 888 O O . TYR A 1 117 ? 39.144 -54.505 40.625 1.00 85.99 ? 117 TYR A O 1 ATOM 889 C CB . TYR A 1 117 ? 40.125 -52.294 38.552 1.00 79.38 ? 117 TYR A CB 1 ATOM 890 C CG . TYR A 1 117 ? 40.571 -51.842 37.182 1.00 75.97 ? 117 TYR A CG 1 ATOM 891 C CD1 . TYR A 1 117 ? 41.882 -51.438 36.962 1.00 75.63 ? 117 TYR A CD1 1 ATOM 892 C CD2 . TYR A 1 117 ? 39.693 -51.845 36.101 1.00 73.50 ? 117 TYR A CD2 1 ATOM 893 C CE1 . TYR A 1 117 ? 42.306 -51.031 35.709 1.00 73.18 ? 117 TYR A CE1 1 ATOM 894 C CE2 . TYR A 1 117 ? 40.106 -51.434 34.843 1.00 70.43 ? 117 TYR A CE2 1 ATOM 895 C CZ . TYR A 1 117 ? 41.415 -51.032 34.654 1.00 70.57 ? 117 TYR A CZ 1 ATOM 896 O OH . TYR A 1 117 ? 41.848 -50.627 33.414 1.00 68.65 ? 117 TYR A OH 1 ATOM 897 N N . SER A 1 118 ? 41.201 -53.812 41.255 1.00 88.48 ? 118 SER A N 1 ATOM 898 C CA . SER A 1 118 ? 40.978 -54.010 42.687 1.00 93.12 ? 118 SER A CA 1 ATOM 899 C C . SER A 1 118 ? 41.603 -52.878 43.509 1.00 94.61 ? 118 SER A C 1 ATOM 900 O O . SER A 1 118 ? 42.759 -52.511 43.289 1.00 95.17 ? 118 SER A O 1 ATOM 901 C CB . SER A 1 118 ? 41.528 -55.367 43.143 1.00 96.09 ? 118 SER A CB 1 ATOM 902 O OG . SER A 1 118 ? 42.926 -55.453 42.939 1.00 96.48 ? 118 SER A OG 1 ATOM 903 N N . GLY A 1 119 ? 40.829 -52.327 44.444 1.00 95.94 ? 119 GLY A N 1 ATOM 904 C CA . GLY A 1 119 ? 41.295 -51.253 45.323 1.00 97.44 ? 119 GLY A CA 1 ATOM 905 C C . GLY A 1 119 ? 41.094 -49.844 44.783 1.00 94.98 ? 119 GLY A C 1 ATOM 906 O O . GLY A 1 119 ? 41.708 -48.896 45.283 1.00 95.69 ? 119 GLY A O 1 ATOM 907 N N . ILE A 1 120 ? 40.230 -49.703 43.775 1.00 92.16 ? 120 ILE A N 1 ATOM 908 C CA . ILE A 1 120 ? 39.951 -48.409 43.137 1.00 89.69 ? 120 ILE A CA 1 ATOM 909 C C . ILE A 1 120 ? 38.542 -48.369 42.532 1.00 87.89 ? 120 ILE A C 1 ATOM 910 O O . ILE A 1 120 ? 37.852 -49.382 42.476 1.00 87.23 ? 120 ILE A O 1 ATOM 911 C CB . ILE A 1 120 ? 40.970 -48.098 42.014 1.00 87.52 ? 120 ILE A CB 1 ATOM 912 C CG1 . ILE A 1 120 ? 41.158 -49.316 41.099 1.00 86.54 ? 120 ILE A CG1 1 ATOM 913 C CG2 . ILE A 1 120 ? 42.306 -47.652 42.595 1.00 89.07 ? 120 ILE A CG2 1 ATOM 914 C CD1 . ILE A 1 120 ? 41.822 -48.986 39.782 1.00 83.60 ? 120 ILE A CD1 1 ATOM 915 N N . ARG A 1 121 ? 38.134 -47.187 42.079 1.00 87.38 ? 121 ARG A N 1 ATOM 916 C CA . ARG A 1 121 ? 36.853 -46.996 41.395 1.00 86.99 ? 121 ARG A CA 1 ATOM 917 C C . ARG A 1 121 ? 37.086 -47.022 39.880 1.00 83.41 ? 121 ARG A C 1 ATOM 918 O O . ARG A 1 121 ? 38.198 -46.752 39.427 1.00 82.89 ? 121 ARG A O 1 ATOM 919 C CB . ARG A 1 121 ? 36.236 -45.662 41.830 1.00 88.91 ? 121 ARG A CB 1 ATOM 920 C CG . ARG A 1 121 ? 34.719 -45.670 41.954 1.00 90.80 ? 121 ARG A CG 1 ATOM 921 C CD . ARG A 1 121 ? 34.238 -45.165 43.312 1.00 95.04 ? 121 ARG A CD 1 ATOM 922 N NE . ARG A 1 121 ? 33.900 -43.737 43.335 1.00 96.00 ? 121 ARG A NE 1 ATOM 923 C CZ . ARG A 1 121 ? 34.675 -42.758 43.809 1.00 97.54 ? 121 ARG A CZ 1 ATOM 924 N NH1 . ARG A 1 121 ? 35.882 -43.008 44.302 1.00 98.62 ? 121 ARG A NH1 1 ATOM 925 N NH2 . ARG A 1 121 ? 34.238 -41.503 43.782 1.00 98.12 ? 121 ARG A NH2 1 ATOM 926 N N . THR A 1 122 ? 36.056 -47.364 39.101 1.00 81.53 ? 122 THR A N 1 ATOM 927 C CA . THR A 1 122 ? 36.197 -47.473 37.635 1.00 78.07 ? 122 THR A CA 1 ATOM 928 C C . THR A 1 122 ? 35.038 -46.869 36.829 1.00 77.05 ? 122 THR A C 1 ATOM 929 O O . THR A 1 122 ? 34.991 -47.028 35.609 1.00 74.43 ? 122 THR A O 1 ATOM 930 C CB . THR A 1 122 ? 36.342 -48.951 37.190 1.00 77.87 ? 122 THR A CB 1 ATOM 931 O OG1 . THR A 1 122 ? 35.128 -49.663 37.462 1.00 77.77 ? 122 THR A OG1 1 ATOM 932 C CG2 . THR A 1 122 ? 37.498 -49.639 37.904 1.00 79.67 ? 122 THR A CG2 1 ATOM 933 N N . ASN A 1 123 ? 34.130 -46.160 37.496 1.00 79.52 ? 123 ASN A N 1 ATOM 934 C CA . ASN A 1 123 ? 32.861 -45.739 36.895 1.00 79.70 ? 123 ASN A CA 1 ATOM 935 C C . ASN A 1 123 ? 32.686 -44.217 36.839 1.00 77.36 ? 123 ASN A C 1 ATOM 936 O O . ASN A 1 123 ? 31.563 -43.715 36.927 1.00 77.49 ? 123 ASN A O 1 ATOM 937 C CB . ASN A 1 123 ? 31.691 -46.375 37.668 1.00 86.37 ? 123 ASN A CB 1 ATOM 938 C CG . ASN A 1 123 ? 31.735 -46.076 39.163 1.00 94.00 ? 123 ASN A CG 1 ATOM 939 O OD1 . ASN A 1 123 ? 32.487 -45.213 39.611 1.00 93.16 ? 123 ASN A OD1 1 ATOM 940 N ND2 . ASN A 1 123 ? 30.922 -46.803 39.945 1.00 104.60 ? 123 ASN A ND2 1 ATOM 941 N N . GLY A 1 124 ? 33.788 -43.484 36.692 1.00 74.49 ? 124 GLY A N 1 ATOM 942 C CA . GLY A 1 124 ? 33.737 -42.018 36.661 1.00 73.21 ? 124 GLY A CA 1 ATOM 943 C C . GLY A 1 124 ? 33.004 -41.495 35.437 1.00 70.30 ? 124 GLY A C 1 ATOM 944 O O . GLY A 1 124 ? 33.212 -41.995 34.329 1.00 67.73 ? 124 GLY A O 1 ATOM 945 N N . THR A 1 125 ? 32.143 -40.496 35.638 1.00 70.06 ? 125 THR A N 1 ATOM 946 C CA . THR A 1 125 ? 31.333 -39.919 34.556 1.00 68.30 ? 125 THR A CA 1 ATOM 947 C C . THR A 1 125 ? 31.412 -38.388 34.550 1.00 68.47 ? 125 THR A C 1 ATOM 948 O O . THR A 1 125 ? 32.208 -37.810 35.282 1.00 69.39 ? 125 THR A O 1 ATOM 949 C CB . THR A 1 125 ? 29.857 -40.359 34.672 1.00 69.04 ? 125 THR A CB 1 ATOM 950 O OG1 . THR A 1 125 ? 29.278 -39.796 35.855 1.00 71.56 ? 125 THR A OG1 1 ATOM 951 C CG2 . THR A 1 125 ? 29.748 -41.882 34.709 1.00 68.24 ? 125 THR A CG2 1 ATOM 952 N N . THR A 1 126 ? 30.600 -37.746 33.708 1.00 67.71 ? 126 THR A N 1 ATOM 953 C CA . THR A 1 126 ? 30.546 -36.283 33.619 1.00 68.38 ? 126 THR A CA 1 ATOM 954 C C . THR A 1 126 ? 29.317 -35.811 32.839 1.00 68.56 ? 126 THR A C 1 ATOM 955 O O . THR A 1 126 ? 28.733 -36.571 32.072 1.00 67.67 ? 126 THR A O 1 ATOM 956 C CB . THR A 1 126 ? 31.816 -35.721 32.948 1.00 67.02 ? 126 THR A CB 1 ATOM 957 O OG1 . THR A 1 126 ? 31.588 -34.371 32.524 1.00 68.01 ? 126 THR A OG1 1 ATOM 958 C CG2 . THR A 1 126 ? 32.215 -36.565 31.742 1.00 64.28 ? 126 THR A CG2 1 ATOM 959 N N . SER A 1 127 ? 28.938 -34.551 33.031 1.00 70.88 ? 127 SER A N 1 ATOM 960 C CA . SER A 1 127 ? 27.779 -33.963 32.345 1.00 71.90 ? 127 SER A CA 1 ATOM 961 C C . SER A 1 127 ? 28.039 -33.667 30.864 1.00 70.04 ? 127 SER A C 1 ATOM 962 O O . SER A 1 127 ? 27.099 -33.569 30.076 1.00 70.79 ? 127 SER A O 1 ATOM 963 C CB . SER A 1 127 ? 27.323 -32.681 33.053 1.00 74.86 ? 127 SER A CB 1 ATOM 964 O OG . SER A 1 127 ? 28.375 -31.737 33.156 1.00 74.85 ? 127 SER A OG 1 ATOM 965 N N . ALA A 1 128 ? 29.304 -33.524 30.488 1.00 68.31 ? 128 ALA A N 1 ATOM 966 C CA . ALA A 1 128 ? 29.664 -33.268 29.094 1.00 66.59 ? 128 ALA A CA 1 ATOM 967 C C . ALA A 1 128 ? 29.428 -34.474 28.176 1.00 64.74 ? 128 ALA A C 1 ATOM 968 O O . ALA A 1 128 ? 29.266 -34.304 26.968 1.00 63.29 ? 128 ALA A O 1 ATOM 969 C CB . ALA A 1 128 ? 31.111 -32.807 28.998 1.00 65.65 ? 128 ALA A CB 1 ATOM 970 N N . CYS A 1 129 ? 29.423 -35.685 28.734 1.00 64.71 ? 129 CYS A N 1 ATOM 971 C CA . CYS A 1 129 ? 29.122 -36.891 27.951 1.00 63.53 ? 129 CYS A CA 1 ATOM 972 C C . CYS A 1 129 ? 27.736 -37.419 28.339 1.00 66.10 ? 129 CYS A C 1 ATOM 973 O O . CYS A 1 129 ? 27.587 -38.169 29.309 1.00 67.36 ? 129 CYS A O 1 ATOM 974 C CB . CYS A 1 129 ? 30.210 -37.962 28.132 1.00 61.28 ? 129 CYS A CB 1 ATOM 975 S SG . CYS A 1 129 ? 31.912 -37.347 28.008 0.80 60.40 ? 129 CYS A SG 1 ATOM 976 N N . ARG A 1 130 ? 26.729 -37.023 27.563 1.00 67.68 ? 130 ARG A N 1 ATOM 977 C CA . ARG A 1 130 ? 25.326 -37.253 27.906 1.00 70.96 ? 130 ARG A CA 1 ATOM 978 C C . ARG A 1 130 ? 24.705 -38.494 27.240 1.00 69.56 ? 130 ARG A C 1 ATOM 979 O O . ARG A 1 130 ? 24.522 -38.537 26.018 1.00 68.80 ? 130 ARG A O 1 ATOM 980 C CB . ARG A 1 130 ? 24.514 -35.998 27.557 1.00 74.74 ? 130 ARG A CB 1 ATOM 981 C CG . ARG A 1 130 ? 23.015 -36.118 27.788 1.00 79.35 ? 130 ARG A CG 1 ATOM 982 C CD . ARG A 1 130 ? 22.383 -34.778 28.148 1.00 83.75 ? 130 ARG A CD 1 ATOM 983 N NE . ARG A 1 130 ? 21.090 -34.571 27.494 1.00 87.16 ? 130 ARG A NE 1 ATOM 984 C CZ . ARG A 1 130 ? 19.968 -35.236 27.771 1.00 89.95 ? 130 ARG A CZ 1 ATOM 985 N NH1 . ARG A 1 130 ? 19.941 -36.192 28.699 1.00 90.65 ? 130 ARG A NH1 1 ATOM 986 N NH2 . ARG A 1 130 ? 18.855 -34.944 27.104 1.00 92.25 ? 130 ARG A NH2 1 ATOM 987 N N . ARG A 1 131 ? 24.397 -39.497 28.062 1.00 69.04 ? 131 ARG A N 1 ATOM 988 C CA . ARG A 1 131 ? 23.554 -40.628 27.668 1.00 68.82 ? 131 ARG A CA 1 ATOM 989 C C . ARG A 1 131 ? 22.451 -40.797 28.712 1.00 72.50 ? 131 ARG A C 1 ATOM 990 O O . ARG A 1 131 ? 22.586 -41.603 29.639 1.00 73.20 ? 131 ARG A O 1 ATOM 991 C CB . ARG A 1 131 ? 24.365 -41.924 27.584 1.00 66.13 ? 131 ARG A CB 1 ATOM 992 C CG . ARG A 1 131 ? 25.309 -42.031 26.402 1.00 62.69 ? 131 ARG A CG 1 ATOM 993 C CD . ARG A 1 131 ? 25.926 -43.420 26.353 1.00 60.85 ? 131 ARG A CD 1 ATOM 994 N NE . ARG A 1 131 ? 27.029 -43.501 25.400 1.00 57.96 ? 131 ARG A NE 1 ATOM 995 C CZ . ARG A 1 131 ? 28.281 -43.119 25.647 1.00 56.64 ? 131 ARG A CZ 1 ATOM 996 N NH1 . ARG A 1 131 ? 28.621 -42.621 26.829 1.00 57.48 ? 131 ARG A NH1 1 ATOM 997 N NH2 . ARG A 1 131 ? 29.204 -43.228 24.697 1.00 54.91 ? 131 ARG A NH2 1 ATOM 998 N N . SER A 1 132 ? 21.367 -40.037 28.563 1.00 74.76 ? 132 SER A N 1 ATOM 999 C CA . SER A 1 132 ? 20.276 -40.031 29.543 1.00 78.49 ? 132 SER A CA 1 ATOM 1000 C C . SER A 1 132 ? 20.845 -39.905 30.958 1.00 78.96 ? 132 SER A C 1 ATOM 1001 O O . SER A 1 132 ? 20.796 -40.848 31.751 1.00 79.52 ? 132 SER A O 1 ATOM 1002 C CB . SER A 1 132 ? 19.408 -41.289 29.409 1.00 79.57 ? 132 SER A CB 1 ATOM 1003 O OG . SER A 1 132 ? 20.103 -42.452 29.826 1.00 78.33 ? 132 SER A OG 1 ATOM 1004 N N . GLY A 1 133 ? 21.391 -38.729 31.251 1.00 78.75 ? 133 GLY A N 1 ATOM 1005 C CA . GLY A 1 133 ? 22.192 -38.513 32.452 1.00 78.29 ? 133 GLY A CA 1 ATOM 1006 C C . GLY A 1 133 ? 23.669 -38.572 32.103 1.00 74.50 ? 133 GLY A C 1 ATOM 1007 O O . GLY A 1 133 ? 24.034 -38.817 30.948 1.00 71.52 ? 133 GLY A O 1 ATOM 1008 N N . SER A 1 134 ? 24.515 -38.354 33.106 1.00 73.78 ? 134 SER A N 1 ATOM 1009 C CA . SER A 1 134 ? 25.963 -38.288 32.912 1.00 70.91 ? 134 SER A CA 1 ATOM 1010 C C . SER A 1 134 ? 26.548 -39.642 32.544 1.00 68.10 ? 134 SER A C 1 ATOM 1011 O O . SER A 1 134 ? 26.093 -40.670 33.036 1.00 68.86 ? 134 SER A O 1 ATOM 1012 C CB . SER A 1 134 ? 26.645 -37.768 34.178 1.00 72.59 ? 134 SER A CB 1 ATOM 1013 O OG . SER A 1 134 ? 26.277 -36.426 34.434 1.00 74.85 ? 134 SER A OG 1 ATOM 1014 N N . SER A 1 135 ? 27.563 -39.628 31.682 1.00 65.26 ? 135 SER A N 1 ATOM 1015 C CA . SER A 1 135 ? 28.230 -40.853 31.235 1.00 62.61 ? 135 SER A CA 1 ATOM 1016 C C . SER A 1 135 ? 29.710 -40.593 30.914 1.00 61.06 ? 135 SER A C 1 ATOM 1017 O O . SER A 1 135 ? 30.307 -39.655 31.446 1.00 61.43 ? 135 SER A O 1 ATOM 1018 C CB . SER A 1 135 ? 27.491 -41.434 30.029 1.00 61.11 ? 135 SER A CB 1 ATOM 1019 O OG . SER A 1 135 ? 28.006 -42.706 29.686 1.00 59.14 ? 135 SER A OG 1 ATOM 1020 N N . PHE A 1 136 ? 30.306 -41.436 30.072 1.00 59.64 ? 136 PHE A N 1 ATOM 1021 C CA . PHE A 1 136 ? 31.722 -41.310 29.721 1.00 58.41 ? 136 PHE A CA 1 ATOM 1022 C C . PHE A 1 136 ? 31.990 -41.920 28.342 1.00 57.12 ? 136 PHE A C 1 ATOM 1023 O O . PHE A 1 136 ? 31.067 -42.406 27.688 1.00 58.72 ? 136 PHE A O 1 ATOM 1024 C CB . PHE A 1 136 ? 32.591 -41.982 30.801 1.00 58.35 ? 136 PHE A CB 1 ATOM 1025 C CG . PHE A 1 136 ? 34.031 -41.538 30.788 1.00 57.75 ? 136 PHE A CG 1 ATOM 1026 C CD1 . PHE A 1 136 ? 34.359 -40.185 30.858 1.00 58.19 ? 136 PHE A CD1 1 ATOM 1027 C CD2 . PHE A 1 136 ? 35.059 -42.465 30.696 1.00 56.95 ? 136 PHE A CD2 1 ATOM 1028 C CE1 . PHE A 1 136 ? 35.681 -39.771 30.834 1.00 57.82 ? 136 PHE A CE1 1 ATOM 1029 C CE2 . PHE A 1 136 ? 36.385 -42.053 30.672 1.00 56.69 ? 136 PHE A CE2 1 ATOM 1030 C CZ . PHE A 1 136 ? 36.696 -40.706 30.741 1.00 56.83 ? 136 PHE A CZ 1 ATOM 1031 N N . TYR A 1 137 ? 33.244 -41.874 27.895 1.00 55.47 ? 137 TYR A N 1 ATOM 1032 C CA . TYR A 1 137 ? 33.653 -42.513 26.644 1.00 53.16 ? 137 TYR A CA 1 ATOM 1033 C C . TYR A 1 137 ? 33.396 -44.024 26.699 1.00 53.08 ? 137 TYR A C 1 ATOM 1034 O O . TYR A 1 137 ? 33.952 -44.721 27.548 1.00 53.65 ? 137 TYR A O 1 ATOM 1035 C CB . TYR A 1 137 ? 35.133 -42.237 26.362 1.00 51.94 ? 137 TYR A CB 1 ATOM 1036 C CG . TYR A 1 137 ? 35.435 -40.791 26.025 1.00 51.65 ? 137 TYR A CG 1 ATOM 1037 C CD1 . TYR A 1 137 ? 35.744 -39.874 27.021 1.00 53.13 ? 137 TYR A CD1 1 ATOM 1038 C CD2 . TYR A 1 137 ? 35.418 -40.344 24.709 1.00 50.29 ? 137 TYR A CD2 1 ATOM 1039 C CE1 . TYR A 1 137 ? 36.020 -38.547 26.718 1.00 53.35 ? 137 TYR A CE1 1 ATOM 1040 C CE2 . TYR A 1 137 ? 35.692 -39.023 24.394 1.00 50.48 ? 137 TYR A CE2 1 ATOM 1041 C CZ . TYR A 1 137 ? 35.997 -38.127 25.400 1.00 51.90 ? 137 TYR A CZ 1 ATOM 1042 O OH . TYR A 1 137 ? 36.267 -36.813 25.091 1.00 51.73 ? 137 TYR A OH 1 ATOM 1043 N N . ALA A 1 138 ? 32.565 -44.519 25.783 1.00 52.46 ? 138 ALA A N 1 ATOM 1044 C CA . ALA A 1 138 ? 32.108 -45.913 25.796 1.00 52.67 ? 138 ALA A CA 1 ATOM 1045 C C . ALA A 1 138 ? 33.236 -46.947 25.864 1.00 52.58 ? 138 ALA A C 1 ATOM 1046 O O . ALA A 1 138 ? 33.084 -47.972 26.527 1.00 53.15 ? 138 ALA A O 1 ATOM 1047 C CB . ALA A 1 138 ? 31.228 -46.182 24.587 1.00 52.43 ? 138 ALA A CB 1 ATOM 1048 N N . GLU A 1 139 ? 34.358 -46.671 25.194 1.00 51.61 ? 139 GLU A N 1 ATOM 1049 C CA . GLU A 1 139 ? 35.485 -47.615 25.119 1.00 51.37 ? 139 GLU A CA 1 ATOM 1050 C C . GLU A 1 139 ? 36.533 -47.421 26.206 1.00 53.27 ? 139 GLU A C 1 ATOM 1051 O O . GLU A 1 139 ? 37.528 -48.148 26.232 1.00 53.83 ? 139 GLU A O 1 ATOM 1052 C CB . GLU A 1 139 ? 36.198 -47.505 23.758 1.00 49.95 ? 139 GLU A CB 1 ATOM 1053 C CG . GLU A 1 139 ? 35.298 -47.531 22.532 1.00 48.84 ? 139 GLU A CG 1 ATOM 1054 C CD . GLU A 1 139 ? 34.557 -48.843 22.379 1.00 48.77 ? 139 GLU A CD 1 ATOM 1055 O OE1 . GLU A 1 139 ? 34.442 -49.569 23.379 1.00 49.79 ? 139 GLU A OE1 1 ATOM 1056 O OE2 . GLU A 1 139 ? 34.085 -49.146 21.262 1.00 47.35 ? 139 GLU A OE2 1 ATOM 1057 N N . MET A 1 140 ? 36.327 -46.444 27.088 1.00 54.97 ? 140 MET A N 1 ATOM 1058 C CA . MET A 1 140 ? 37.316 -46.090 28.101 1.00 57.00 ? 140 MET A CA 1 ATOM 1059 C C . MET A 1 140 ? 36.718 -46.236 29.497 1.00 58.79 ? 140 MET A C 1 ATOM 1060 O O . MET A 1 140 ? 35.506 -46.382 29.647 1.00 59.17 ? 140 MET A O 1 ATOM 1061 C CB . MET A 1 140 ? 37.781 -44.643 27.908 1.00 58.01 ? 140 MET A CB 1 ATOM 1062 C CG . MET A 1 140 ? 38.082 -44.251 26.470 1.00 57.77 ? 140 MET A CG 1 ATOM 1063 S SD . MET A 1 140 ? 39.482 -45.172 25.808 1.00 60.65 ? 140 MET A SD 1 ATOM 1064 C CE . MET A 1 140 ? 40.830 -44.243 26.537 1.00 60.24 ? 140 MET A CE 1 ATOM 1065 N N . LYS A 1 141 ? 37.577 -46.178 30.512 1.00 59.53 ? 141 LYS A N 1 ATOM 1066 C CA . LYS A 1 141 ? 37.134 -46.178 31.900 1.00 61.74 ? 141 LYS A CA 1 ATOM 1067 C C . LYS A 1 141 ? 37.933 -45.168 32.735 1.00 62.07 ? 141 LYS A C 1 ATOM 1068 O O . LYS A 1 141 ? 39.167 -45.199 32.771 1.00 61.43 ? 141 LYS A O 1 ATOM 1069 C CB . LYS A 1 141 ? 37.230 -47.592 32.490 1.00 63.99 ? 141 LYS A CB 1 ATOM 1070 C CG . LYS A 1 141 ? 35.978 -48.435 32.260 1.00 64.62 ? 141 LYS A CG 1 ATOM 1071 C CD . LYS A 1 141 ? 36.235 -49.919 32.466 1.00 66.69 ? 141 LYS A CD 1 ATOM 1072 C CE . LYS A 1 141 ? 34.957 -50.670 32.826 1.00 68.77 ? 141 LYS A CE 1 ATOM 1073 N NZ . LYS A 1 141 ? 33.865 -50.484 31.828 1.00 67.80 ? 141 LYS A NZ 1 ATOM 1074 N N . TRP A 1 142 ? 37.209 -44.264 33.389 1.00 62.48 ? 142 TRP A N 1 ATOM 1075 C CA . TRP A 1 142 ? 37.815 -43.247 34.235 1.00 63.64 ? 142 TRP A CA 1 ATOM 1076 C C . TRP A 1 142 ? 38.202 -43.860 35.583 1.00 66.09 ? 142 TRP A C 1 ATOM 1077 O O . TRP A 1 142 ? 37.344 -44.084 36.443 1.00 66.96 ? 142 TRP A O 1 ATOM 1078 C CB . TRP A 1 142 ? 36.839 -42.083 34.440 1.00 63.99 ? 142 TRP A CB 1 ATOM 1079 C CG . TRP A 1 142 ? 37.482 -40.805 34.891 1.00 64.45 ? 142 TRP A CG 1 ATOM 1080 C CD1 . TRP A 1 142 ? 38.696 -40.656 35.508 1.00 65.46 ? 142 TRP A CD1 1 ATOM 1081 C CD2 . TRP A 1 142 ? 36.926 -39.494 34.782 1.00 65.03 ? 142 TRP A CD2 1 ATOM 1082 N NE1 . TRP A 1 142 ? 38.931 -39.334 35.775 1.00 66.46 ? 142 TRP A NE1 1 ATOM 1083 C CE2 . TRP A 1 142 ? 37.861 -38.596 35.342 1.00 66.37 ? 142 TRP A CE2 1 ATOM 1084 C CE3 . TRP A 1 142 ? 35.728 -38.987 34.261 1.00 64.68 ? 142 TRP A CE3 1 ATOM 1085 C CZ2 . TRP A 1 142 ? 37.636 -37.217 35.393 1.00 67.31 ? 142 TRP A CZ2 1 ATOM 1086 C CZ3 . TRP A 1 142 ? 35.505 -37.618 34.315 1.00 65.71 ? 142 TRP A CZ3 1 ATOM 1087 C CH2 . TRP A 1 142 ? 36.454 -36.749 34.880 1.00 66.95 ? 142 TRP A CH2 1 ATOM 1088 N N . LEU A 1 143 ? 39.499 -44.123 35.757 1.00 66.94 ? 143 LEU A N 1 ATOM 1089 C CA . LEU A 1 143 ? 40.014 -44.757 36.975 1.00 69.24 ? 143 LEU A CA 1 ATOM 1090 C C . LEU A 1 143 ? 40.267 -43.736 38.084 1.00 71.26 ? 143 LEU A C 1 ATOM 1091 O O . LEU A 1 143 ? 40.998 -42.763 37.897 1.00 70.46 ? 143 LEU A O 1 ATOM 1092 C CB . LEU A 1 143 ? 41.300 -45.535 36.681 1.00 69.27 ? 143 LEU A CB 1 ATOM 1093 C CG . LEU A 1 143 ? 41.211 -46.687 35.674 1.00 67.84 ? 143 LEU A CG 1 ATOM 1094 C CD1 . LEU A 1 143 ? 42.449 -47.567 35.778 1.00 69.04 ? 143 LEU A CD1 1 ATOM 1095 C CD2 . LEU A 1 143 ? 39.954 -47.518 35.891 1.00 67.92 ? 143 LEU A CD2 1 ATOM 1096 N N . LEU A 1 144 ? 39.678 -44.003 39.246 1.00 73.76 ? 144 LEU A N 1 ATOM 1097 C CA . LEU A 1 144 ? 39.629 -43.064 40.356 1.00 76.50 ? 144 LEU A CA 1 ATOM 1098 C C . LEU A 1 144 ? 40.197 -43.712 41.624 1.00 78.97 ? 144 LEU A C 1 ATOM 1099 O O . LEU A 1 144 ? 40.565 -44.884 41.617 1.00 79.20 ? 144 LEU A O 1 ATOM 1100 C CB . LEU A 1 144 ? 38.166 -42.666 40.583 1.00 77.35 ? 144 LEU A CB 1 ATOM 1101 C CG . LEU A 1 144 ? 37.850 -41.193 40.830 1.00 78.60 ? 144 LEU A CG 1 ATOM 1102 C CD1 . LEU A 1 144 ? 38.408 -40.329 39.708 1.00 76.71 ? 144 LEU A CD1 1 ATOM 1103 C CD2 . LEU A 1 144 ? 36.346 -41.006 40.959 1.00 79.23 ? 144 LEU A CD2 1 ATOM 1104 N N . SER A 1 145 ? 40.278 -42.939 42.703 1.00 81.12 ? 145 SER A N 1 ATOM 1105 C CA . SER A 1 145 ? 40.596 -43.490 44.028 1.00 84.50 ? 145 SER A CA 1 ATOM 1106 C C . SER A 1 145 ? 39.292 -43.812 44.751 1.00 85.43 ? 145 SER A C 1 ATOM 1107 O O . SER A 1 145 ? 38.346 -43.026 44.695 1.00 84.92 ? 145 SER A O 1 ATOM 1108 C CB . SER A 1 145 ? 41.429 -42.508 44.862 1.00 87.01 ? 145 SER A CB 1 ATOM 1109 O OG . SER A 1 145 ? 42.806 -42.595 44.537 1.00 86.98 ? 145 SER A OG 1 ATOM 1110 N N . ASN A 1 146 ? 39.253 -44.956 45.436 1.00 87.18 ? 146 ASN A N 1 ATOM 1111 C CA . ASN A 1 146 ? 38.032 -45.443 46.102 1.00 88.94 ? 146 ASN A CA 1 ATOM 1112 C C . ASN A 1 146 ? 37.166 -44.342 46.716 1.00 90.58 ? 146 ASN A C 1 ATOM 1113 O O . ASN A 1 146 ? 35.942 -44.353 46.561 1.00 90.00 ? 146 ASN A O 1 ATOM 1114 C CB . ASN A 1 146 ? 38.381 -46.479 47.182 1.00 92.49 ? 146 ASN A CB 1 ATOM 1115 C CG . ASN A 1 146 ? 38.534 -47.889 46.629 1.00 91.61 ? 146 ASN A CG 1 ATOM 1116 O OD1 . ASN A 1 146 ? 37.943 -48.242 45.607 1.00 89.30 ? 146 ASN A OD1 1 ATOM 1117 N ND2 . ASN A 1 146 ? 39.318 -48.711 47.318 1.00 94.03 ? 146 ASN A ND2 1 ATOM 1118 N N . THR A 1 147 ? 37.805 -43.395 47.400 1.00 92.68 ? 147 THR A N 1 ATOM 1119 C CA . THR A 1 147 ? 37.103 -42.272 48.022 1.00 94.62 ? 147 THR A CA 1 ATOM 1120 C C . THR A 1 147 ? 37.929 -40.983 47.905 1.00 94.24 ? 147 THR A C 1 ATOM 1121 O O . THR A 1 147 ? 39.062 -41.006 47.415 1.00 93.18 ? 147 THR A O 1 ATOM 1122 C CB . THR A 1 147 ? 36.757 -42.587 49.494 1.00 99.06 ? 147 THR A CB 1 ATOM 1123 O OG1 . THR A 1 147 ? 36.026 -41.497 50.066 1.00 101.66 ? 147 THR A OG1 1 ATOM 1124 C CG2 . THR A 1 147 ? 38.014 -42.854 50.317 1.00 101.51 ? 147 THR A CG2 1 ATOM 1125 N N . ASP A 1 148 ? 37.357 -39.865 48.346 1.00 95.52 ? 148 ASP A N 1 ATOM 1126 C CA . ASP A 1 148 ? 38.003 -38.553 48.209 1.00 95.28 ? 148 ASP A CA 1 ATOM 1127 C C . ASP A 1 148 ? 39.316 -38.489 48.986 1.00 97.40 ? 148 ASP A C 1 ATOM 1128 O O . ASP A 1 148 ? 39.393 -38.953 50.123 1.00 100.24 ? 148 ASP A O 1 ATOM 1129 C CB . ASP A 1 148 ? 37.074 -37.431 48.677 1.00 97.23 ? 148 ASP A CB 1 ATOM 1130 C CG . ASP A 1 148 ? 35.774 -37.388 47.900 1.00 95.54 ? 148 ASP A CG 1 ATOM 1131 O OD1 . ASP A 1 148 ? 35.267 -38.466 47.522 1.00 94.54 ? 148 ASP A OD1 1 ATOM 1132 O OD2 . ASP A 1 148 ? 35.250 -36.281 47.673 1.00 95.73 ? 148 ASP A OD2 1 ATOM 1133 N N . ASN A 1 149 ? 40.345 -37.938 48.342 1.00 95.85 ? 149 ASN A N 1 ATOM 1134 C CA . ASN A 1 149 ? 41.698 -37.816 48.911 1.00 97.91 ? 149 ASN A CA 1 ATOM 1135 C C . ASN A 1 149 ? 42.426 -39.139 49.196 1.00 98.76 ? 149 ASN A C 1 ATOM 1136 O O . ASN A 1 149 ? 43.556 -39.125 49.688 1.00 100.95 ? 149 ASN A O 1 ATOM 1137 C CB . ASN A 1 149 ? 41.686 -36.940 50.177 1.00 101.68 ? 149 ASN A CB 1 ATOM 1138 C CG . ASN A 1 149 ? 41.347 -35.491 49.886 1.00 101.42 ? 149 ASN A CG 1 ATOM 1139 O OD1 . ASN A 1 149 ? 41.217 -35.087 48.728 1.00 97.17 ? 149 ASN A OD1 1 ATOM 1140 N ND2 . ASN A 1 149 ? 41.215 -34.695 50.942 1.00 104.79 ? 149 ASN A ND2 1 ATOM 1141 N N . ALA A 1 150 ? 41.805 -40.272 48.875 1.00 97.49 ? 150 ALA A N 1 ATOM 1142 C CA . ALA A 1 150 ? 42.409 -41.566 49.158 1.00 98.66 ? 150 ALA A CA 1 ATOM 1143 C C . ALA A 1 150 ? 43.530 -41.850 48.165 1.00 96.95 ? 150 ALA A C 1 ATOM 1144 O O . ALA A 1 150 ? 43.444 -41.476 46.991 1.00 93.26 ? 150 ALA A O 1 ATOM 1145 C CB . ALA A 1 150 ? 41.364 -42.666 49.114 1.00 98.21 ? 150 ALA A CB 1 ATOM 1146 N N . ALA A 1 151 ? 44.578 -42.514 48.647 1.00 99.71 ? 151 ALA A N 1 ATOM 1147 C CA . ALA A 1 151 ? 45.726 -42.871 47.813 1.00 98.72 ? 151 ALA A CA 1 ATOM 1148 C C . ALA A 1 151 ? 45.310 -43.715 46.608 1.00 95.69 ? 151 ALA A C 1 ATOM 1149 O O . ALA A 1 151 ? 44.288 -44.404 46.639 1.00 95.39 ? 151 ALA A O 1 ATOM 1150 C CB . ALA A 1 151 ? 46.769 -43.611 48.642 1.00 101.91 ? 151 ALA A CB 1 ATOM 1151 N N . PHE A 1 152 ? 46.098 -43.633 45.542 1.00 93.99 ? 152 PHE A N 1 ATOM 1152 C CA . PHE A 1 152 ? 45.898 -44.455 44.358 1.00 91.21 ? 152 PHE A CA 1 ATOM 1153 C C . PHE A 1 152 ? 47.098 -45.391 44.226 1.00 92.42 ? 152 PHE A C 1 ATOM 1154 O O . PHE A 1 152 ? 48.199 -44.932 43.929 1.00 92.50 ? 152 PHE A O 1 ATOM 1155 C CB . PHE A 1 152 ? 45.768 -43.572 43.117 1.00 88.30 ? 152 PHE A CB 1 ATOM 1156 C CG . PHE A 1 152 ? 45.359 -44.321 41.879 1.00 85.97 ? 152 PHE A CG 1 ATOM 1157 C CD1 . PHE A 1 152 ? 46.284 -45.078 41.170 1.00 85.58 ? 152 PHE A CD1 1 ATOM 1158 C CD2 . PHE A 1 152 ? 44.047 -44.276 41.424 1.00 84.53 ? 152 PHE A CD2 1 ATOM 1159 C CE1 . PHE A 1 152 ? 45.912 -45.768 40.032 1.00 83.52 ? 152 PHE A CE1 1 ATOM 1160 C CE2 . PHE A 1 152 ? 43.666 -44.964 40.281 1.00 82.20 ? 152 PHE A CE2 1 ATOM 1161 C CZ . PHE A 1 152 ? 44.600 -45.713 39.585 1.00 81.61 ? 152 PHE A CZ 1 ATOM 1162 N N . PRO A 1 153 ? 46.890 -46.710 44.431 1.00 93.54 ? 153 PRO A N 1 ATOM 1163 C CA . PRO A 1 153 ? 48.004 -47.664 44.486 1.00 95.80 ? 153 PRO A CA 1 ATOM 1164 C C . PRO A 1 153 ? 48.728 -47.838 43.150 1.00 94.78 ? 153 PRO A C 1 ATOM 1165 O O . PRO A 1 153 ? 48.077 -47.948 42.104 1.00 91.77 ? 153 PRO A O 1 ATOM 1166 C CB . PRO A 1 153 ? 47.318 -48.971 44.880 1.00 96.68 ? 153 PRO A CB 1 ATOM 1167 C CG . PRO A 1 153 ? 45.944 -48.843 44.328 1.00 93.57 ? 153 PRO A CG 1 ATOM 1168 C CD . PRO A 1 153 ? 45.584 -47.395 44.470 1.00 92.44 ? 153 PRO A CD 1 ATOM 1169 N N . GLN A 1 154 ? 50.061 -47.875 43.198 1.00 97.68 ? 154 GLN A N 1 ATOM 1170 C CA . GLN A 1 154 ? 50.881 -48.014 41.993 1.00 97.08 ? 154 GLN A CA 1 ATOM 1171 C C . GLN A 1 154 ? 50.547 -49.324 41.276 1.00 96.72 ? 154 GLN A C 1 ATOM 1172 O O . GLN A 1 154 ? 50.863 -50.415 41.762 1.00 99.60 ? 154 GLN A O 1 ATOM 1173 C CB . GLN A 1 154 ? 52.375 -47.955 42.336 1.00 100.49 ? 154 GLN A CB 1 ATOM 1174 C CG . GLN A 1 154 ? 53.291 -47.804 41.127 1.00 99.50 ? 154 GLN A CG 1 ATOM 1175 C CD . GLN A 1 154 ? 53.168 -46.442 40.457 1.00 97.21 ? 154 GLN A CD 1 ATOM 1176 O OE1 . GLN A 1 154 ? 53.211 -45.406 41.125 1.00 99.03 ? 154 GLN A OE1 1 ATOM 1177 N NE2 . GLN A 1 154 ? 53.024 -46.436 39.133 1.00 93.44 ? 154 GLN A NE2 1 ATOM 1178 N N . MET A 1 155 ? 49.907 -49.199 40.116 1.00 93.41 ? 155 MET A N 1 ATOM 1179 C CA . MET A 1 155 ? 49.350 -50.346 39.407 1.00 92.35 ? 155 MET A CA 1 ATOM 1180 C C . MET A 1 155 ? 50.125 -50.699 38.151 1.00 91.41 ? 155 MET A C 1 ATOM 1181 O O . MET A 1 155 ? 50.775 -49.848 37.540 1.00 89.90 ? 155 MET A O 1 ATOM 1182 C CB . MET A 1 155 ? 47.896 -50.076 39.032 1.00 89.34 ? 155 MET A CB 1 ATOM 1183 C CG . MET A 1 155 ? 46.907 -50.567 40.067 1.00 91.30 ? 155 MET A CG 1 ATOM 1184 S SD . MET A 1 155 ? 45.226 -50.180 39.564 1.00 88.72 ? 155 MET A SD 1 ATOM 1185 C CE . MET A 1 155 ? 44.302 -51.322 40.592 1.00 91.30 ? 155 MET A CE 1 ATOM 1186 N N . THR A 1 156 ? 50.024 -51.970 37.774 1.00 91.82 ? 156 THR A N 1 ATOM 1187 C CA . THR A 1 156 ? 50.664 -52.489 36.577 1.00 90.80 ? 156 THR A CA 1 ATOM 1188 C C . THR A 1 156 ? 49.697 -53.442 35.876 1.00 88.52 ? 156 THR A C 1 ATOM 1189 O O . THR A 1 156 ? 49.453 -54.548 36.358 1.00 90.10 ? 156 THR A O 1 ATOM 1190 C CB . THR A 1 156 ? 51.972 -53.233 36.927 1.00 94.82 ? 156 THR A CB 1 ATOM 1191 O OG1 . THR A 1 156 ? 52.776 -52.421 37.794 1.00 97.09 ? 156 THR A OG1 1 ATOM 1192 C CG2 . THR A 1 156 ? 52.764 -53.562 35.666 1.00 94.37 ? 156 THR A CG2 1 ATOM 1193 N N . LYS A 1 157 ? 49.133 -52.996 34.754 1.00 84.79 ? 157 LYS A N 1 ATOM 1194 C CA . LYS A 1 157 ? 48.266 -53.838 33.930 1.00 82.19 ? 157 LYS A CA 1 ATOM 1195 C C . LYS A 1 157 ? 48.883 -54.026 32.558 1.00 80.13 ? 157 LYS A C 1 ATOM 1196 O O . LYS A 1 157 ? 49.492 -53.106 32.010 1.00 79.08 ? 157 LYS A O 1 ATOM 1197 C CB . LYS A 1 157 ? 46.867 -53.232 33.810 1.00 79.94 ? 157 LYS A CB 1 ATOM 1198 C CG . LYS A 1 157 ? 46.171 -52.997 35.144 1.00 81.90 ? 157 LYS A CG 1 ATOM 1199 C CD . LYS A 1 157 ? 46.097 -54.260 35.994 1.00 85.35 ? 157 LYS A CD 1 ATOM 1200 C CE . LYS A 1 157 ? 45.615 -53.973 37.404 1.00 87.68 ? 157 LYS A CE 1 ATOM 1201 N NZ . LYS A 1 157 ? 44.132 -53.871 37.461 1.00 86.97 ? 157 LYS A NZ 1 ATOM 1202 N N . SER A 1 158 ? 48.721 -55.228 32.013 1.00 79.60 ? 158 SER A N 1 ATOM 1203 C CA . SER A 1 158 ? 49.352 -55.602 30.753 1.00 78.00 ? 158 SER A CA 1 ATOM 1204 C C . SER A 1 158 ? 48.351 -56.210 29.777 1.00 74.36 ? 158 SER A C 1 ATOM 1205 O O . SER A 1 158 ? 47.291 -56.682 30.178 1.00 73.56 ? 158 SER A O 1 ATOM 1206 C CB . SER A 1 158 ? 50.492 -56.588 31.023 1.00 81.50 ? 158 SER A CB 1 ATOM 1207 O OG . SER A 1 158 ? 51.148 -56.948 29.823 1.00 81.57 ? 158 SER A OG 1 ATOM 1208 N N . TYR A 1 159 ? 48.697 -56.182 28.494 1.00 72.07 ? 159 TYR A N 1 ATOM 1209 C CA . TYR A 1 159 ? 47.860 -56.756 27.441 1.00 69.88 ? 159 TYR A CA 1 ATOM 1210 C C . TYR A 1 159 ? 48.717 -57.204 26.263 1.00 70.27 ? 159 TYR A C 1 ATOM 1211 O O . TYR A 1 159 ? 49.426 -56.394 25.666 1.00 69.33 ? 159 TYR A O 1 ATOM 1212 C CB . TYR A 1 159 ? 46.821 -55.737 26.963 1.00 66.32 ? 159 TYR A CB 1 ATOM 1213 C CG . TYR A 1 159 ? 46.092 -56.140 25.691 1.00 64.09 ? 159 TYR A CG 1 ATOM 1214 C CD1 . TYR A 1 159 ? 45.031 -57.037 25.728 1.00 64.25 ? 159 TYR A CD1 1 ATOM 1215 C CD2 . TYR A 1 159 ? 46.467 -55.623 24.455 1.00 62.23 ? 159 TYR A CD2 1 ATOM 1216 C CE1 . TYR A 1 159 ? 44.362 -57.411 24.572 1.00 62.80 ? 159 TYR A CE1 1 ATOM 1217 C CE2 . TYR A 1 159 ? 45.808 -55.990 23.296 1.00 61.23 ? 159 TYR A CE2 1 ATOM 1218 C CZ . TYR A 1 159 ? 44.756 -56.884 23.358 1.00 61.28 ? 159 TYR A CZ 1 ATOM 1219 O OH . TYR A 1 159 ? 44.097 -57.243 22.205 1.00 60.61 ? 159 TYR A OH 1 ATOM 1220 N N . LYS A 1 160 ? 48.648 -58.492 25.935 1.00 71.80 ? 160 LYS A N 1 ATOM 1221 C CA . LYS A 1 160 ? 49.361 -59.037 24.781 1.00 72.23 ? 160 LYS A CA 1 ATOM 1222 C C . LYS A 1 160 ? 48.426 -59.094 23.578 1.00 69.83 ? 160 LYS A C 1 ATOM 1223 O O . LYS A 1 160 ? 47.266 -59.492 23.696 1.00 68.91 ? 160 LYS A O 1 ATOM 1224 C CB . LYS A 1 160 ? 49.906 -60.437 25.081 1.00 75.40 ? 160 LYS A CB 1 ATOM 1225 C CG . LYS A 1 160 ? 50.840 -60.982 24.006 1.00 76.75 ? 160 LYS A CG 1 ATOM 1226 C CD . LYS A 1 160 ? 51.215 -62.435 24.258 1.00 80.25 ? 160 LYS A CD 1 ATOM 1227 C CE . LYS A 1 160 ? 52.027 -63.003 23.105 1.00 81.59 ? 160 LYS A CE 1 ATOM 1228 N NZ . LYS A 1 160 ? 52.338 -64.449 23.279 1.00 85.41 ? 160 LYS A NZ 1 ATOM 1229 N N . ASN A 1 161 ? 48.944 -58.689 22.424 1.00 69.06 ? 161 ASN A N 1 ATOM 1230 C CA . ASN A 1 161 ? 48.211 -58.787 21.172 1.00 67.77 ? 161 ASN A CA 1 ATOM 1231 C C . ASN A 1 161 ? 48.383 -60.190 20.581 1.00 70.09 ? 161 ASN A C 1 ATOM 1232 O O . ASN A 1 161 ? 49.454 -60.531 20.075 1.00 71.57 ? 161 ASN A O 1 ATOM 1233 C CB . ASN A 1 161 ? 48.706 -57.720 20.197 1.00 66.25 ? 161 ASN A CB 1 ATOM 1234 C CG . ASN A 1 161 ? 47.967 -57.741 18.878 1.00 65.25 ? 161 ASN A CG 1 ATOM 1235 O OD1 . ASN A 1 161 ? 46.934 -58.399 18.733 1.00 65.24 ? 161 ASN A OD1 1 ATOM 1236 N ND2 . ASN A 1 161 ? 48.496 -57.014 17.899 1.00 64.86 ? 161 ASN A ND2 1 ATOM 1237 N N . THR A 1 162 ? 47.321 -60.993 20.648 1.00 70.32 ? 162 THR A N 1 ATOM 1238 C CA . THR A 1 162 ? 47.364 -62.381 20.186 1.00 73.11 ? 162 THR A CA 1 ATOM 1239 C C . THR A 1 162 ? 46.762 -62.567 18.791 1.00 72.20 ? 162 THR A C 1 ATOM 1240 O O . THR A 1 162 ? 46.431 -63.686 18.409 1.00 73.86 ? 162 THR A O 1 ATOM 1241 C CB . THR A 1 162 ? 46.626 -63.323 21.165 1.00 74.52 ? 162 THR A CB 1 ATOM 1242 O OG1 . THR A 1 162 ? 45.213 -63.231 20.960 1.00 72.19 ? 162 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 162 ? 46.953 -62.975 22.614 1.00 75.48 ? 162 THR A CG2 1 ATOM 1244 N N . ARG A 1 163 ? 46.630 -61.484 18.033 1.00 69.81 ? 163 ARG A N 1 ATOM 1245 C CA . ARG A 1 163 ? 46.066 -61.550 16.690 1.00 69.49 ? 163 ARG A CA 1 ATOM 1246 C C . ARG A 1 163 ? 47.138 -61.291 15.637 1.00 70.17 ? 163 ARG A C 1 ATOM 1247 O O . ARG A 1 163 ? 48.249 -60.895 15.970 1.00 71.43 ? 163 ARG A O 1 ATOM 1248 C CB . ARG A 1 163 ? 44.901 -60.567 16.572 1.00 67.45 ? 163 ARG A CB 1 ATOM 1249 C CG . ARG A 1 163 ? 43.649 -61.102 17.251 1.00 68.50 ? 163 ARG A CG 1 ATOM 1250 C CD . ARG A 1 163 ? 42.517 -60.092 17.363 1.00 66.48 ? 163 ARG A CD 1 ATOM 1251 N NE . ARG A 1 163 ? 41.983 -59.682 16.062 1.00 65.59 ? 163 ARG A NE 1 ATOM 1252 C CZ . ARG A 1 163 ? 40.787 -59.120 15.870 1.00 63.96 ? 163 ARG A CZ 1 ATOM 1253 N NH1 . ARG A 1 163 ? 39.952 -58.905 16.886 1.00 62.69 ? 163 ARG A NH1 1 ATOM 1254 N NH2 . ARG A 1 163 ? 40.417 -58.777 14.640 1.00 63.20 ? 163 ARG A NH2 1 ATOM 1255 N N . LYS A 1 164 ? 46.799 -61.524 14.373 1.00 70.65 ? 164 LYS A N 1 ATOM 1256 C CA . LYS A 1 164 ? 47.769 -61.449 13.270 1.00 72.31 ? 164 LYS A CA 1 ATOM 1257 C C . LYS A 1 164 ? 48.057 -60.036 12.766 1.00 69.89 ? 164 LYS A C 1 ATOM 1258 O O . LYS A 1 164 ? 49.027 -59.835 12.038 1.00 70.71 ? 164 LYS A O 1 ATOM 1259 C CB . LYS A 1 164 ? 47.305 -62.294 12.077 1.00 74.27 ? 164 LYS A CB 1 ATOM 1260 C CG . LYS A 1 164 ? 47.857 -63.706 12.022 1.00 78.27 ? 164 LYS A CG 1 ATOM 1261 C CD . LYS A 1 164 ? 47.723 -64.253 10.607 1.00 80.05 ? 164 LYS A CD 1 ATOM 1262 C CE . LYS A 1 164 ? 47.675 -65.771 10.573 1.00 83.43 ? 164 LYS A CE 1 ATOM 1263 N NZ . LYS A 1 164 ? 47.272 -66.252 9.222 1.00 84.60 ? 164 LYS A NZ 1 ATOM 1264 N N . SER A 1 165 ? 47.217 -59.068 13.122 1.00 67.32 ? 165 SER A N 1 ATOM 1265 C CA . SER A 1 165 ? 47.418 -57.682 12.689 1.00 65.19 ? 165 SER A CA 1 ATOM 1266 C C . SER A 1 165 ? 47.682 -56.784 13.893 1.00 63.56 ? 165 SER A C 1 ATOM 1267 O O . SER A 1 165 ? 47.297 -57.127 15.010 1.00 64.05 ? 165 SER A O 1 ATOM 1268 C CB . SER A 1 165 ? 46.209 -57.178 11.902 1.00 63.37 ? 165 SER A CB 1 ATOM 1269 O OG . SER A 1 165 ? 45.040 -57.180 12.700 1.00 62.73 ? 165 SER A OG 1 ATOM 1270 N N . PRO A 1 166 ? 48.348 -55.635 13.673 1.00 62.27 ? 166 PRO A N 1 ATOM 1271 C CA . PRO A 1 166 ? 48.668 -54.730 14.776 1.00 60.98 ? 166 PRO A CA 1 ATOM 1272 C C . PRO A 1 166 ? 47.441 -54.139 15.470 1.00 58.13 ? 166 PRO A C 1 ATOM 1273 O O . PRO A 1 166 ? 46.444 -53.832 14.817 1.00 56.43 ? 166 PRO A O 1 ATOM 1274 C CB . PRO A 1 166 ? 49.479 -53.619 14.100 1.00 61.45 ? 166 PRO A CB 1 ATOM 1275 C CG . PRO A 1 166 ? 50.009 -54.225 12.851 1.00 63.01 ? 166 PRO A CG 1 ATOM 1276 C CD . PRO A 1 166 ? 48.947 -55.179 12.405 1.00 62.95 ? 166 PRO A CD 1 ATOM 1277 N N . ALA A 1 167 ? 47.533 -53.973 16.785 1.00 57.27 ? 167 ALA A N 1 ATOM 1278 C CA . ALA A 1 167 ? 46.424 -53.466 17.582 1.00 55.11 ? 167 ALA A CA 1 ATOM 1279 C C . ALA A 1 167 ? 46.596 -51.975 17.872 1.00 53.92 ? 167 ALA A C 1 ATOM 1280 O O . ALA A 1 167 ? 47.663 -51.538 18.299 1.00 55.42 ? 167 ALA A O 1 ATOM 1281 C CB . ALA A 1 167 ? 46.322 -54.243 18.880 1.00 55.77 ? 167 ALA A CB 1 ATOM 1282 N N . LEU A 1 168 ? 45.545 -51.197 17.636 1.00 51.79 ? 168 LEU A N 1 ATOM 1283 C CA . LEU A 1 168 ? 45.545 -49.783 17.996 1.00 50.69 ? 168 LEU A CA 1 ATOM 1284 C C . LEU A 1 168 ? 45.105 -49.633 19.455 1.00 50.49 ? 168 LEU A C 1 ATOM 1285 O O . LEU A 1 168 ? 43.990 -50.005 19.821 1.00 49.93 ? 168 LEU A O 1 ATOM 1286 C CB . LEU A 1 168 ? 44.635 -48.989 17.059 1.00 48.90 ? 168 LEU A CB 1 ATOM 1287 C CG . LEU A 1 168 ? 44.310 -47.545 17.450 1.00 47.94 ? 168 LEU A CG 1 ATOM 1288 C CD1 . LEU A 1 168 ? 45.577 -46.740 17.676 1.00 48.68 ? 168 LEU A CD1 1 ATOM 1289 C CD2 . LEU A 1 168 ? 43.436 -46.912 16.379 1.00 46.68 ? 168 LEU A CD2 1 ATOM 1290 N N . ILE A 1 169 ? 45.994 -49.100 20.282 1.00 51.54 ? 169 ILE A N 1 ATOM 1291 C CA . ILE A 1 169 ? 45.725 -48.906 21.700 1.00 52.65 ? 169 ILE A CA 1 ATOM 1292 C C . ILE A 1 169 ? 45.665 -47.414 22.012 1.00 52.44 ? 169 ILE A C 1 ATOM 1293 O O . ILE A 1 169 ? 46.557 -46.663 21.614 1.00 53.12 ? 169 ILE A O 1 ATOM 1294 C CB . ILE A 1 169 ? 46.834 -49.534 22.572 1.00 54.98 ? 169 ILE A CB 1 ATOM 1295 C CG1 . ILE A 1 169 ? 47.118 -50.982 22.138 1.00 56.16 ? 169 ILE A CG1 1 ATOM 1296 C CG2 . ILE A 1 169 ? 46.447 -49.485 24.047 1.00 55.48 ? 169 ILE A CG2 1 ATOM 1297 C CD1 . ILE A 1 169 ? 45.976 -51.939 22.380 1.00 55.51 ? 169 ILE A CD1 1 ATOM 1298 N N . VAL A 1 170 ? 44.623 -46.996 22.727 1.00 51.81 ? 170 VAL A N 1 ATOM 1299 C CA . VAL A 1 170 ? 44.478 -45.602 23.147 1.00 52.05 ? 170 VAL A CA 1 ATOM 1300 C C . VAL A 1 170 ? 44.287 -45.531 24.653 1.00 52.46 ? 170 VAL A C 1 ATOM 1301 O O . VAL A 1 170 ? 43.543 -46.325 25.219 1.00 52.74 ? 170 VAL A O 1 ATOM 1302 C CB . VAL A 1 170 ? 43.263 -44.921 22.481 1.00 51.15 ? 170 VAL A CB 1 ATOM 1303 C CG1 . VAL A 1 170 ? 43.132 -43.480 22.949 1.00 51.89 ? 170 VAL A CG1 1 ATOM 1304 C CG2 . VAL A 1 170 ? 43.387 -44.970 20.971 1.00 51.04 ? 170 VAL A CG2 1 ATOM 1305 N N . TRP A 1 171 ? 44.960 -44.577 25.293 1.00 53.12 ? 171 TRP A N 1 ATOM 1306 C CA . TRP A 1 171 ? 44.714 -44.271 26.699 1.00 54.34 ? 171 TRP A CA 1 ATOM 1307 C C . TRP A 1 171 ? 44.667 -42.761 26.882 1.00 55.10 ? 171 TRP A C 1 ATOM 1308 O O . TRP A 1 171 ? 44.975 -42.005 25.952 1.00 55.00 ? 171 TRP A O 1 ATOM 1309 C CB . TRP A 1 171 ? 45.762 -44.921 27.611 1.00 55.85 ? 171 TRP A CB 1 ATOM 1310 C CG . TRP A 1 171 ? 47.135 -44.387 27.469 1.00 56.70 ? 171 TRP A CG 1 ATOM 1311 C CD1 . TRP A 1 171 ? 47.764 -43.514 28.306 1.00 58.25 ? 171 TRP A CD1 1 ATOM 1312 C CD2 . TRP A 1 171 ? 48.072 -44.699 26.437 1.00 56.66 ? 171 TRP A CD2 1 ATOM 1313 N NE1 . TRP A 1 171 ? 49.035 -43.258 27.854 1.00 59.11 ? 171 TRP A NE1 1 ATOM 1314 C CE2 . TRP A 1 171 ? 49.250 -43.972 26.706 1.00 58.29 ? 171 TRP A CE2 1 ATOM 1315 C CE3 . TRP A 1 171 ? 48.029 -45.519 25.309 1.00 55.83 ? 171 TRP A CE3 1 ATOM 1316 C CZ2 . TRP A 1 171 ? 50.374 -44.035 25.879 1.00 59.02 ? 171 TRP A CZ2 1 ATOM 1317 C CZ3 . TRP A 1 171 ? 49.136 -45.584 24.495 1.00 56.70 ? 171 TRP A CZ3 1 ATOM 1318 C CH2 . TRP A 1 171 ? 50.302 -44.847 24.783 1.00 58.18 ? 171 TRP A CH2 1 ATOM 1319 N N . GLY A 1 172 ? 44.249 -42.324 28.064 1.00 56.29 ? 172 GLY A N 1 ATOM 1320 C CA . GLY A 1 172 ? 44.079 -40.903 28.332 1.00 57.03 ? 172 GLY A CA 1 ATOM 1321 C C . GLY A 1 172 ? 44.715 -40.449 29.632 1.00 59.44 ? 172 GLY A C 1 ATOM 1322 O O . GLY A 1 172 ? 45.034 -41.263 30.492 1.00 60.45 ? 172 GLY A O 1 ATOM 1323 N N . ILE A 1 173 ? 44.907 -39.138 29.758 1.00 60.66 ? 173 ILE A N 1 ATOM 1324 C CA . ILE A 1 173 ? 45.465 -38.538 30.964 1.00 63.44 ? 173 ILE A CA 1 ATOM 1325 C C . ILE A 1 173 ? 44.599 -37.352 31.364 1.00 64.39 ? 173 ILE A C 1 ATOM 1326 O O . ILE A 1 173 ? 44.465 -36.391 30.605 1.00 64.64 ? 173 ILE A O 1 ATOM 1327 C CB . ILE A 1 173 ? 46.917 -38.064 30.755 1.00 64.66 ? 173 ILE A CB 1 ATOM 1328 C CG1 . ILE A 1 173 ? 47.816 -39.219 30.290 1.00 64.53 ? 173 ILE A CG1 1 ATOM 1329 C CG2 . ILE A 1 173 ? 47.469 -37.451 32.034 1.00 67.49 ? 173 ILE A CG2 1 ATOM 1330 C CD1 . ILE A 1 173 ? 48.037 -40.312 31.316 1.00 65.85 ? 173 ILE A CD1 1 ATOM 1331 N N . HIS A 1 174 ? 44.009 -37.429 32.551 1.00 65.48 ? 174 HIS A N 1 ATOM 1332 C CA . HIS A 1 174 ? 43.124 -36.381 33.024 1.00 67.17 ? 174 HIS A CA 1 ATOM 1333 C C . HIS A 1 174 ? 43.889 -35.310 33.784 1.00 69.86 ? 174 HIS A C 1 ATOM 1334 O O . HIS A 1 174 ? 44.500 -35.591 34.816 1.00 72.05 ? 174 HIS A O 1 ATOM 1335 C CB . HIS A 1 174 ? 42.036 -36.945 33.933 1.00 67.68 ? 174 HIS A CB 1 ATOM 1336 C CG . HIS A 1 174 ? 41.184 -35.887 34.554 1.00 69.75 ? 174 HIS A CG 1 ATOM 1337 N ND1 . HIS A 1 174 ? 41.253 -35.565 35.891 1.00 72.17 ? 174 HIS A ND1 1 ATOM 1338 C CD2 . HIS A 1 174 ? 40.279 -35.040 34.008 1.00 69.62 ? 174 HIS A CD2 1 ATOM 1339 C CE1 . HIS A 1 174 ? 40.406 -34.584 36.149 1.00 73.42 ? 174 HIS A CE1 1 ATOM 1340 N NE2 . HIS A 1 174 ? 39.802 -34.248 35.024 1.00 71.88 ? 174 HIS A NE2 1 ATOM 1341 N N . HIS A 1 175 ? 43.842 -34.085 33.272 1.00 70.42 ? 175 HIS A N 1 ATOM 1342 C CA . HIS A 1 175 ? 44.368 -32.930 33.989 1.00 72.96 ? 175 HIS A CA 1 ATOM 1343 C C . HIS A 1 175 ? 43.194 -32.204 34.628 1.00 74.90 ? 175 HIS A C 1 ATOM 1344 O O . HIS A 1 175 ? 42.359 -31.629 33.925 1.00 74.30 ? 175 HIS A O 1 ATOM 1345 C CB . HIS A 1 175 ? 45.110 -31.987 33.043 1.00 72.78 ? 175 HIS A CB 1 ATOM 1346 C CG . HIS A 1 175 ? 46.115 -32.667 32.169 1.00 71.86 ? 175 HIS A CG 1 ATOM 1347 N ND1 . HIS A 1 175 ? 47.208 -33.337 32.673 1.00 72.74 ? 175 HIS A ND1 1 ATOM 1348 C CD2 . HIS A 1 175 ? 46.197 -32.773 30.821 1.00 69.41 ? 175 HIS A CD2 1 ATOM 1349 C CE1 . HIS A 1 175 ? 47.918 -33.831 31.674 1.00 71.21 ? 175 HIS A CE1 1 ATOM 1350 N NE2 . HIS A 1 175 ? 47.326 -33.503 30.541 1.00 69.09 ? 175 HIS A NE2 1 ATOM 1351 N N . SER A 1 176 ? 43.125 -32.229 35.957 1.00 77.58 ? 176 SER A N 1 ATOM 1352 C CA . SER A 1 176 ? 42.026 -31.582 36.671 1.00 79.78 ? 176 SER A CA 1 ATOM 1353 C C . SER A 1 176 ? 42.174 -30.056 36.677 1.00 82.20 ? 176 SER A C 1 ATOM 1354 O O . SER A 1 176 ? 43.204 -29.514 36.271 1.00 82.46 ? 176 SER A O 1 ATOM 1355 C CB . SER A 1 176 ? 41.927 -32.113 38.102 1.00 82.41 ? 176 SER A CB 1 ATOM 1356 O OG . SER A 1 176 ? 40.671 -31.786 38.676 1.00 84.06 ? 176 SER A OG 1 ATOM 1357 N N . VAL A 1 177 ? 41.132 -29.378 37.150 1.00 83.83 ? 177 VAL A N 1 ATOM 1358 C CA . VAL A 1 177 ? 41.050 -27.917 37.103 1.00 86.31 ? 177 VAL A CA 1 ATOM 1359 C C . VAL A 1 177 ? 42.016 -27.253 38.091 1.00 89.14 ? 177 VAL A C 1 ATOM 1360 O O . VAL A 1 177 ? 42.412 -26.099 37.900 1.00 90.54 ? 177 VAL A O 1 ATOM 1361 C CB . VAL A 1 177 ? 39.597 -27.438 37.376 1.00 88.17 ? 177 VAL A CB 1 ATOM 1362 C CG1 . VAL A 1 177 ? 39.509 -25.919 37.463 1.00 91.24 ? 177 VAL A CG1 1 ATOM 1363 C CG2 . VAL A 1 177 ? 38.650 -27.947 36.295 1.00 85.81 ? 177 VAL A CG2 1 ATOM 1364 N N . SER A 1 178 ? 42.396 -27.975 39.142 1.00 89.69 ? 178 SER A N 1 ATOM 1365 C CA . SER A 1 178 ? 43.284 -27.422 40.165 1.00 92.47 ? 178 SER A CA 1 ATOM 1366 C C . SER A 1 178 ? 44.233 -28.468 40.750 1.00 92.05 ? 178 SER A C 1 ATOM 1367 O O . SER A 1 178 ? 44.141 -29.657 40.440 1.00 89.38 ? 178 SER A O 1 ATOM 1368 C CB . SER A 1 178 ? 42.455 -26.785 41.284 1.00 95.22 ? 178 SER A CB 1 ATOM 1369 O OG . SER A 1 178 ? 41.721 -27.765 41.989 1.00 94.81 ? 178 SER A OG 1 ATOM 1370 N N . THR A 1 179 ? 45.153 -28.001 41.590 1.00 94.71 ? 179 THR A N 1 ATOM 1371 C CA . THR A 1 179 ? 46.073 -28.876 42.309 1.00 95.17 ? 179 THR A CA 1 ATOM 1372 C C . THR A 1 179 ? 45.296 -29.672 43.351 1.00 95.59 ? 179 THR A C 1 ATOM 1373 O O . THR A 1 179 ? 45.603 -30.836 43.615 1.00 94.46 ? 179 THR A O 1 ATOM 1374 C CB . THR A 1 179 ? 47.189 -28.072 43.010 1.00 98.83 ? 179 THR A CB 1 ATOM 1375 O OG1 . THR A 1 179 ? 46.618 -27.185 43.984 1.00 102.19 ? 179 THR A OG1 1 ATOM 1376 C CG2 . THR A 1 179 ? 47.992 -27.259 41.996 1.00 98.37 ? 179 THR A CG2 1 ATOM 1377 N N . ALA A 1 180 ? 44.280 -29.027 43.923 1.00 97.07 ? 180 ALA A N 1 ATOM 1378 C CA . ALA A 1 180 ? 43.410 -29.642 44.922 1.00 98.29 ? 180 ALA A CA 1 ATOM 1379 C C . ALA A 1 180 ? 42.557 -30.756 44.327 1.00 95.08 ? 180 ALA A C 1 ATOM 1380 O O . ALA A 1 180 ? 42.508 -31.859 44.866 1.00 94.97 ? 180 ALA A O 1 ATOM 1381 C CB . ALA A 1 180 ? 42.514 -28.590 45.555 1.00 100.84 ? 180 ALA A CB 1 ATOM 1382 N N . GLU A 1 181 ? 41.893 -30.469 43.211 1.00 93.20 ? 181 GLU A N 1 ATOM 1383 C CA . GLU A 1 181 ? 40.968 -31.432 42.601 1.00 90.12 ? 181 GLU A CA 1 ATOM 1384 C C . GLU A 1 181 ? 41.654 -32.682 42.049 1.00 86.23 ? 181 GLU A C 1 ATOM 1385 O O . GLU A 1 181 ? 41.006 -33.712 41.890 1.00 84.50 ? 181 GLU A O 1 ATOM 1386 C CB . GLU A 1 181 ? 40.107 -30.760 41.522 1.00 89.18 ? 181 GLU A CB 1 ATOM 1387 C CG . GLU A 1 181 ? 39.173 -29.674 42.058 1.00 92.66 ? 181 GLU A CG 1 ATOM 1388 C CD . GLU A 1 181 ? 38.388 -30.103 43.290 1.00 95.34 ? 181 GLU A CD 1 ATOM 1389 O OE1 . GLU A 1 181 ? 37.794 -31.202 43.267 1.00 94.73 ? 181 GLU A OE1 1 ATOM 1390 O OE2 . GLU A 1 181 ? 38.359 -29.341 44.282 1.00 99.91 ? 181 GLU A OE2 1 ATOM 1391 N N . GLN A 1 182 ? 42.953 -32.596 41.770 1.00 84.99 ? 182 GLN A N 1 ATOM 1392 C CA . GLN A 1 182 ? 43.737 -33.783 41.424 1.00 82.57 ? 182 GLN A CA 1 ATOM 1393 C C . GLN A 1 182 ? 43.938 -34.673 42.647 1.00 84.21 ? 182 GLN A C 1 ATOM 1394 O O . GLN A 1 182 ? 43.806 -35.891 42.548 1.00 83.14 ? 182 GLN A O 1 ATOM 1395 C CB . GLN A 1 182 ? 45.093 -33.406 40.818 1.00 82.42 ? 182 GLN A CB 1 ATOM 1396 C CG . GLN A 1 182 ? 46.041 -34.584 40.637 1.00 81.55 ? 182 GLN A CG 1 ATOM 1397 C CD . GLN A 1 182 ? 47.097 -34.339 39.574 1.00 80.85 ? 182 GLN A CD 1 ATOM 1398 O OE1 . GLN A 1 182 ? 46.782 -34.207 38.387 1.00 79.02 ? 182 GLN A OE1 1 ATOM 1399 N NE2 . GLN A 1 182 ? 48.362 -34.302 39.990 1.00 82.77 ? 182 GLN A NE2 1 ATOM 1400 N N . THR A 1 183 ? 44.256 -34.076 43.795 1.00 86.94 ? 183 THR A N 1 ATOM 1401 C CA . THR A 1 183 ? 44.434 -34.857 45.022 1.00 89.04 ? 183 THR A CA 1 ATOM 1402 C C . THR A 1 183 ? 43.117 -35.501 45.464 1.00 88.35 ? 183 THR A C 1 ATOM 1403 O O . THR A 1 183 ? 43.111 -36.650 45.905 1.00 88.04 ? 183 THR A O 1 ATOM 1404 C CB . THR A 1 183 ? 45.029 -34.034 46.191 1.00 93.14 ? 183 THR A CB 1 ATOM 1405 O OG1 . THR A 1 183 ? 44.082 -33.057 46.642 1.00 94.82 ? 183 THR A OG1 1 ATOM 1406 C CG2 . THR A 1 183 ? 46.338 -33.356 45.779 1.00 93.54 ? 183 THR A CG2 1 ATOM 1407 N N . LYS A 1 184 ? 42.011 -34.769 45.331 1.00 82.56 ? 184 LYS A N 1 ATOM 1408 C CA . LYS A 1 184 ? 40.685 -35.319 45.625 1.00 83.11 ? 184 LYS A CA 1 ATOM 1409 C C . LYS A 1 184 ? 40.415 -36.602 44.841 1.00 84.39 ? 184 LYS A C 1 ATOM 1410 O O . LYS A 1 184 ? 40.006 -37.610 45.417 1.00 85.73 ? 184 LYS A O 1 ATOM 1411 C CB . LYS A 1 184 ? 39.584 -34.301 45.323 1.00 82.62 ? 184 LYS A CB 1 ATOM 1412 C CG . LYS A 1 184 ? 38.182 -34.876 45.459 1.00 83.67 ? 184 LYS A CG 1 ATOM 1413 C CD . LYS A 1 184 ? 37.103 -33.855 45.150 1.00 83.94 ? 184 LYS A CD 1 ATOM 1414 C CE . LYS A 1 184 ? 35.774 -34.542 44.869 1.00 85.47 ? 184 LYS A CE 1 ATOM 1415 N NZ . LYS A 1 184 ? 34.608 -33.660 45.147 1.00 86.28 ? 184 LYS A NZ 1 ATOM 1416 N N . LEU A 1 185 ? 40.644 -36.555 43.531 1.00 84.23 ? 185 LEU A N 1 ATOM 1417 C CA . LEU A 1 185 ? 40.335 -37.683 42.652 1.00 85.45 ? 185 LEU A CA 1 ATOM 1418 C C . LEU A 1 185 ? 41.322 -38.849 42.780 1.00 86.41 ? 185 LEU A C 1 ATOM 1419 O O . LEU A 1 185 ? 40.911 -40.004 42.709 1.00 88.23 ? 185 LEU A O 1 ATOM 1420 C CB . LEU A 1 185 ? 40.261 -37.225 41.187 1.00 85.07 ? 185 LEU A CB 1 ATOM 1421 C CG . LEU A 1 185 ? 39.174 -36.213 40.796 1.00 84.81 ? 185 LEU A CG 1 ATOM 1422 C CD1 . LEU A 1 185 ? 39.301 -35.868 39.319 1.00 84.77 ? 185 LEU A CD1 1 ATOM 1423 C CD2 . LEU A 1 185 ? 37.767 -36.703 41.099 1.00 86.22 ? 185 LEU A CD2 1 ATOM 1424 N N . TYR A 1 186 ? 42.611 -38.555 42.961 1.00 85.84 ? 186 TYR A N 1 ATOM 1425 C CA . TYR A 1 186 ? 43.656 -39.595 42.918 1.00 87.30 ? 186 TYR A CA 1 ATOM 1426 C C . TYR A 1 186 ? 44.674 -39.567 44.071 1.00 88.01 ? 186 TYR A C 1 ATOM 1427 O O . TYR A 1 186 ? 45.695 -40.255 44.005 1.00 88.97 ? 186 TYR A O 1 ATOM 1428 C CB . TYR A 1 186 ? 44.425 -39.509 41.591 1.00 87.03 ? 186 TYR A CB 1 ATOM 1429 C CG . TYR A 1 186 ? 43.586 -39.132 40.385 1.00 86.22 ? 186 TYR A CG 1 ATOM 1430 C CD1 . TYR A 1 186 ? 42.874 -40.098 39.666 1.00 87.52 ? 186 TYR A CD1 1 ATOM 1431 C CD2 . TYR A 1 186 ? 43.513 -37.810 39.954 1.00 84.54 ? 186 TYR A CD2 1 ATOM 1432 C CE1 . TYR A 1 186 ? 42.118 -39.748 38.554 1.00 86.98 ? 186 TYR A CE1 1 ATOM 1433 C CE2 . TYR A 1 186 ? 42.759 -37.454 38.848 1.00 84.28 ? 186 TYR A CE2 1 ATOM 1434 C CZ . TYR A 1 186 ? 42.060 -38.425 38.153 1.00 85.31 ? 186 TYR A CZ 1 ATOM 1435 O OH . TYR A 1 186 ? 41.312 -38.063 37.057 1.00 84.88 ? 186 TYR A OH 1 ATOM 1436 N N . GLY A 1 187 ? 44.405 -38.788 45.118 1.00 87.90 ? 187 GLY A N 1 ATOM 1437 C CA . GLY A 1 187 ? 45.348 -38.638 46.235 1.00 89.06 ? 187 GLY A CA 1 ATOM 1438 C C . GLY A 1 187 ? 46.512 -37.718 45.904 1.00 88.99 ? 187 GLY A C 1 ATOM 1439 O O . GLY A 1 187 ? 46.797 -37.460 44.731 1.00 88.01 ? 187 GLY A O 1 ATOM 1440 N N . SER A 1 188 ? 47.193 -37.223 46.936 1.00 89.96 ? 188 SER A N 1 ATOM 1441 C CA . SER A 1 188 ? 48.303 -36.283 46.739 1.00 90.59 ? 188 SER A CA 1 ATOM 1442 C C . SER A 1 188 ? 49.563 -36.991 46.228 1.00 92.62 ? 188 SER A C 1 ATOM 1443 O O . SER A 1 188 ? 49.596 -38.219 46.125 1.00 94.06 ? 188 SER A O 1 ATOM 1444 C CB . SER A 1 188 ? 48.605 -35.519 48.033 1.00 91.03 ? 188 SER A CB 1 ATOM 1445 O OG . SER A 1 188 ? 49.157 -36.372 49.018 1.00 93.13 ? 188 SER A OG 1 ATOM 1446 N N . GLY A 1 189 ? 50.588 -36.203 45.903 1.00 93.40 ? 189 GLY A N 1 ATOM 1447 C CA . GLY A 1 189 ? 51.869 -36.726 45.420 1.00 95.71 ? 189 GLY A CA 1 ATOM 1448 C C . GLY A 1 189 ? 52.033 -36.560 43.919 1.00 95.23 ? 189 GLY A C 1 ATOM 1449 O O . GLY A 1 189 ? 51.089 -36.179 43.222 1.00 93.33 ? 189 GLY A O 1 ATOM 1450 N N . ASN A 1 190 ? 53.237 -36.843 43.422 1.00 97.38 ? 190 ASN A N 1 ATOM 1451 C CA . ASN A 1 190 ? 53.542 -36.732 41.986 1.00 96.82 ? 190 ASN A CA 1 ATOM 1452 C C . ASN A 1 190 ? 53.127 -37.996 41.236 1.00 96.26 ? 190 ASN A C 1 ATOM 1453 O O . ASN A 1 190 ? 53.780 -39.038 41.353 1.00 98.48 ? 190 ASN A O 1 ATOM 1454 C CB . ASN A 1 190 ? 55.040 -36.484 41.762 1.00 99.35 ? 190 ASN A CB 1 ATOM 1455 C CG . ASN A 1 190 ? 55.537 -35.221 42.441 1.00 100.01 ? 190 ASN A CG 1 ATOM 1456 O OD1 . ASN A 1 190 ? 54.819 -34.226 42.539 1.00 98.83 ? 190 ASN A OD1 1 ATOM 1457 N ND2 . ASN A 1 190 ? 56.778 -35.255 42.908 1.00 102.83 ? 190 ASN A ND2 1 ATOM 1458 N N . LYS A 1 191 ? 52.045 -37.903 40.468 1.00 93.49 ? 191 LYS A N 1 ATOM 1459 C CA . LYS A 1 191 ? 51.518 -39.058 39.752 1.00 93.24 ? 191 LYS A CA 1 ATOM 1460 C C . LYS A 1 191 ? 52.341 -39.288 38.483 1.00 93.39 ? 191 LYS A C 1 ATOM 1461 O O . LYS A 1 191 ? 52.676 -38.336 37.781 1.00 92.45 ? 191 LYS A O 1 ATOM 1462 C CB . LYS A 1 191 ? 50.043 -38.853 39.389 1.00 91.32 ? 191 LYS A CB 1 ATOM 1463 C CG . LYS A 1 191 ? 49.119 -38.465 40.539 1.00 90.39 ? 191 LYS A CG 1 ATOM 1464 C CD . LYS A 1 191 ? 49.122 -39.475 41.677 1.00 92.30 ? 191 LYS A CD 1 ATOM 1465 C CE . LYS A 1 191 ? 49.926 -38.973 42.866 1.00 93.19 ? 191 LYS A CE 1 ATOM 1466 N NZ . LYS A 1 191 ? 49.958 -39.930 44.005 1.00 95.15 ? 191 LYS A NZ 1 ATOM 1467 N N . LEU A 1 192 ? 52.676 -40.547 38.203 1.00 94.48 ? 192 LEU A N 1 ATOM 1468 C CA . LEU A 1 192 ? 53.408 -40.909 36.985 1.00 94.54 ? 192 LEU A CA 1 ATOM 1469 C C . LEU A 1 192 ? 52.682 -42.033 36.239 1.00 94.46 ? 192 LEU A C 1 ATOM 1470 O O . LEU A 1 192 ? 52.046 -42.886 36.860 1.00 95.28 ? 192 LEU A O 1 ATOM 1471 C CB . LEU A 1 192 ? 54.843 -41.336 37.331 1.00 97.25 ? 192 LEU A CB 1 ATOM 1472 C CG . LEU A 1 192 ? 55.695 -41.986 36.225 1.00 99.12 ? 192 LEU A CG 1 ATOM 1473 C CD1 . LEU A 1 192 ? 56.029 -41.002 35.108 1.00 97.52 ? 192 LEU A CD1 1 ATOM 1474 C CD2 . LEU A 1 192 ? 56.967 -42.589 36.805 1.00 102.54 ? 192 LEU A CD2 1 ATOM 1475 N N . VAL A 1 193 ? 52.774 -42.012 34.909 1.00 93.23 ? 193 VAL A N 1 ATOM 1476 C CA . VAL A 1 193 ? 52.247 -43.084 34.065 1.00 93.59 ? 193 VAL A CA 1 ATOM 1477 C C . VAL A 1 193 ? 53.260 -43.401 32.956 1.00 94.21 ? 193 VAL A C 1 ATOM 1478 O O . VAL A 1 193 ? 53.723 -42.494 32.263 1.00 92.60 ? 193 VAL A O 1 ATOM 1479 C CB . VAL A 1 193 ? 50.882 -42.703 33.452 1.00 91.73 ? 193 VAL A CB 1 ATOM 1480 C CG1 . VAL A 1 193 ? 50.336 -43.842 32.599 1.00 93.39 ? 193 VAL A CG1 1 ATOM 1481 C CG2 . VAL A 1 193 ? 49.889 -42.332 34.546 1.00 90.68 ? 193 VAL A CG2 1 ATOM 1482 N N . THR A 1 194 ? 53.604 -44.683 32.802 1.00 96.27 ? 194 THR A N 1 ATOM 1483 C CA . THR A 1 194 ? 54.603 -45.118 31.812 1.00 97.33 ? 194 THR A CA 1 ATOM 1484 C C . THR A 1 194 ? 54.057 -46.177 30.844 1.00 98.16 ? 194 THR A C 1 ATOM 1485 O O . THR A 1 194 ? 53.115 -46.906 31.164 1.00 98.73 ? 194 THR A O 1 ATOM 1486 C CB . THR A 1 194 ? 55.883 -45.668 32.484 1.00 100.44 ? 194 THR A CB 1 ATOM 1487 O OG1 . THR A 1 194 ? 55.669 -47.012 32.931 1.00 103.49 ? 194 THR A OG1 1 ATOM 1488 C CG2 . THR A 1 194 ? 56.299 -44.797 33.659 1.00 99.78 ? 194 THR A CG2 1 ATOM 1489 N N . VAL A 1 195 ? 54.679 -46.254 29.667 1.00 98.02 ? 195 VAL A N 1 ATOM 1490 C CA . VAL A 1 195 ? 54.203 -47.079 28.560 1.00 98.79 ? 195 VAL A CA 1 ATOM 1491 C C . VAL A 1 195 ? 55.378 -47.648 27.755 1.00 100.86 ? 195 VAL A C 1 ATOM 1492 O O . VAL A 1 195 ? 56.203 -46.894 27.229 1.00 99.61 ? 195 VAL A O 1 ATOM 1493 C CB . VAL A 1 195 ? 53.305 -46.251 27.615 1.00 95.82 ? 195 VAL A CB 1 ATOM 1494 C CG1 . VAL A 1 195 ? 52.795 -47.111 26.461 1.00 97.35 ? 195 VAL A CG1 1 ATOM 1495 C CG2 . VAL A 1 195 ? 52.145 -45.636 28.387 1.00 93.67 ? 195 VAL A CG2 1 ATOM 1496 N N . GLY A 1 196 ? 55.430 -48.977 27.645 1.00 103.88 ? 196 GLY A N 1 ATOM 1497 C CA . GLY A 1 196 ? 56.557 -49.668 27.027 1.00 106.55 ? 196 GLY A CA 1 ATOM 1498 C C . GLY A 1 196 ? 56.152 -50.811 26.115 1.00 108.90 ? 196 GLY A C 1 ATOM 1499 O O . GLY A 1 196 ? 55.599 -51.815 26.564 1.00 111.47 ? 196 GLY A O 1 ATOM 1500 N N . SER A 1 197 ? 56.434 -50.642 24.827 1.00 108.00 ? 197 SER A N 1 ATOM 1501 C CA . SER A 1 197 ? 56.266 -51.688 23.824 1.00 110.61 ? 197 SER A CA 1 ATOM 1502 C C . SER A 1 197 ? 57.595 -51.892 23.098 1.00 112.40 ? 197 SER A C 1 ATOM 1503 O O . SER A 1 197 ? 58.490 -51.051 23.192 1.00 110.82 ? 197 SER A O 1 ATOM 1504 C CB . SER A 1 197 ? 55.160 -51.293 22.840 1.00 108.09 ? 197 SER A CB 1 ATOM 1505 O OG . SER A 1 197 ? 55.515 -51.585 21.501 1.00 109.04 ? 197 SER A OG 1 ATOM 1506 N N . SER A 1 198 ? 57.723 -53.005 22.378 1.00 115.83 ? 198 SER A N 1 ATOM 1507 C CA . SER A 1 198 ? 58.943 -53.302 21.612 1.00 118.01 ? 198 SER A CA 1 ATOM 1508 C C . SER A 1 198 ? 59.425 -52.100 20.806 1.00 114.14 ? 198 SER A C 1 ATOM 1509 O O . SER A 1 198 ? 60.618 -51.813 20.764 1.00 114.76 ? 198 SER A O 1 ATOM 1510 C CB . SER A 1 198 ? 58.714 -54.479 20.660 1.00 121.73 ? 198 SER A CB 1 ATOM 1511 O OG . SER A 1 198 ? 58.406 -55.663 21.373 1.00 126.12 ? 198 SER A OG 1 ATOM 1512 N N . ASN A 1 199 ? 58.485 -51.401 20.180 1.00 110.43 ? 199 ASN A N 1 ATOM 1513 C CA . ASN A 1 199 ? 58.790 -50.246 19.340 1.00 107.15 ? 199 ASN A CA 1 ATOM 1514 C C . ASN A 1 199 ? 58.806 -48.927 20.100 1.00 103.45 ? 199 ASN A C 1 ATOM 1515 O O . ASN A 1 199 ? 59.343 -47.936 19.609 1.00 101.51 ? 199 ASN A O 1 ATOM 1516 C CB . ASN A 1 199 ? 57.747 -50.123 18.225 1.00 105.57 ? 199 ASN A CB 1 ATOM 1517 C CG . ASN A 1 199 ? 57.620 -51.383 17.397 1.00 109.20 ? 199 ASN A CG 1 ATOM 1518 O OD1 . ASN A 1 199 ? 58.083 -52.455 17.790 1.00 113.15 ? 199 ASN A OD1 1 ATOM 1519 N ND2 . ASN A 1 199 ? 56.978 -51.262 16.244 1.00 108.34 ? 199 ASN A ND2 1 ATOM 1520 N N . TYR A 1 200 ? 58.222 -48.919 21.294 1.00 102.72 ? 200 TYR A N 1 ATOM 1521 C CA . TYR A 1 200 ? 57.754 -47.686 21.915 1.00 98.94 ? 200 TYR A CA 1 ATOM 1522 C C . TYR A 1 200 ? 58.196 -47.562 23.373 1.00 99.62 ? 200 TYR A C 1 ATOM 1523 O O . TYR A 1 200 ? 58.254 -48.550 24.103 1.00 102.31 ? 200 TYR A O 1 ATOM 1524 C CB . TYR A 1 200 ? 56.228 -47.651 21.804 1.00 96.94 ? 200 TYR A CB 1 ATOM 1525 C CG . TYR A 1 200 ? 55.564 -46.416 22.358 1.00 93.26 ? 200 TYR A CG 1 ATOM 1526 C CD1 . TYR A 1 200 ? 55.273 -46.311 23.718 1.00 92.61 ? 200 TYR A CD1 1 ATOM 1527 C CD2 . TYR A 1 200 ? 55.199 -45.363 21.521 1.00 90.46 ? 200 TYR A CD2 1 ATOM 1528 C CE1 . TYR A 1 200 ? 54.655 -45.190 24.229 1.00 89.60 ? 200 TYR A CE1 1 ATOM 1529 C CE2 . TYR A 1 200 ? 54.576 -44.236 22.026 1.00 87.72 ? 200 TYR A CE2 1 ATOM 1530 C CZ . TYR A 1 200 ? 54.308 -44.157 23.385 1.00 87.26 ? 200 TYR A CZ 1 ATOM 1531 O OH . TYR A 1 200 ? 53.693 -43.045 23.902 1.00 84.80 ? 200 TYR A OH 1 ATOM 1532 N N . GLN A 1 201 ? 58.478 -46.328 23.786 1.00 97.40 ? 201 GLN A N 1 ATOM 1533 C CA . GLN A 1 201 ? 59.081 -46.045 25.085 1.00 98.15 ? 201 GLN A CA 1 ATOM 1534 C C . GLN A 1 201 ? 58.772 -44.590 25.464 1.00 95.10 ? 201 GLN A C 1 ATOM 1535 O O . GLN A 1 201 ? 59.325 -43.669 24.864 1.00 94.00 ? 201 GLN A O 1 ATOM 1536 C CB . GLN A 1 201 ? 60.598 -46.265 24.984 1.00 101.00 ? 201 GLN A CB 1 ATOM 1537 C CG . GLN A 1 201 ? 61.314 -46.646 26.270 1.00 103.60 ? 201 GLN A CG 1 ATOM 1538 C CD . GLN A 1 201 ? 62.769 -47.010 26.011 1.00 107.12 ? 201 GLN A CD 1 ATOM 1539 O OE1 . GLN A 1 201 ? 63.070 -48.113 25.554 1.00 110.01 ? 201 GLN A OE1 1 ATOM 1540 N NE2 . GLN A 1 201 ? 63.677 -46.077 26.286 1.00 107.04 ? 201 GLN A NE2 1 ATOM 1541 N N . GLN A 1 202 ? 57.879 -44.390 26.437 1.00 94.17 ? 202 GLN A N 1 ATOM 1542 C CA . GLN A 1 202 ? 57.487 -43.037 26.871 1.00 91.71 ? 202 GLN A CA 1 ATOM 1543 C C . GLN A 1 202 ? 56.888 -42.991 28.280 1.00 91.52 ? 202 GLN A C 1 ATOM 1544 O O . GLN A 1 202 ? 56.566 -44.024 28.867 1.00 92.87 ? 202 GLN A O 1 ATOM 1545 C CB . GLN A 1 202 ? 56.486 -42.417 25.887 1.00 89.15 ? 202 GLN A CB 1 ATOM 1546 C CG . GLN A 1 202 ? 57.113 -41.706 24.695 1.00 88.77 ? 202 GLN A CG 1 ATOM 1547 C CD . GLN A 1 202 ? 56.241 -40.587 24.153 1.00 86.21 ? 202 GLN A CD 1 ATOM 1548 O OE1 . GLN A 1 202 ? 55.780 -39.727 24.908 1.00 84.87 ? 202 GLN A OE1 1 ATOM 1549 N NE2 . GLN A 1 202 ? 56.019 -40.586 22.840 1.00 85.70 ? 202 GLN A NE2 1 ATOM 1550 N N . SER A 1 203 ? 56.738 -41.772 28.799 1.00 89.99 ? 203 SER A N 1 ATOM 1551 C CA . SER A 1 203 ? 56.158 -41.546 30.124 1.00 89.82 ? 203 SER A CA 1 ATOM 1552 C C . SER A 1 203 ? 55.325 -40.271 30.172 1.00 87.43 ? 203 SER A C 1 ATOM 1553 O O . SER A 1 203 ? 55.469 -39.394 29.316 1.00 86.35 ? 203 SER A O 1 ATOM 1554 C CB . SER A 1 203 ? 57.255 -41.488 31.177 1.00 91.71 ? 203 SER A CB 1 ATOM 1555 O OG . SER A 1 203 ? 57.845 -42.764 31.331 1.00 94.83 ? 203 SER A OG 1 ATOM 1556 N N . PHE A 1 204 ? 54.456 -40.182 31.181 1.00 87.02 ? 204 PHE A N 1 ATOM 1557 C CA . PHE A 1 204 ? 53.462 -39.109 31.275 1.00 85.04 ? 204 PHE A CA 1 ATOM 1558 C C . PHE A 1 204 ? 53.154 -38.725 32.720 1.00 84.86 ? 204 PHE A C 1 ATOM 1559 O O . PHE A 1 204 ? 52.483 -39.465 33.440 1.00 85.11 ? 204 PHE A O 1 ATOM 1560 C CB . PHE A 1 204 ? 52.164 -39.519 30.565 1.00 84.24 ? 204 PHE A CB 1 ATOM 1561 C CG . PHE A 1 204 ? 52.345 -39.807 29.109 1.00 84.62 ? 204 PHE A CG 1 ATOM 1562 C CD1 . PHE A 1 204 ? 52.460 -38.770 28.196 1.00 83.70 ? 204 PHE A CD1 1 ATOM 1563 C CD2 . PHE A 1 204 ? 52.437 -41.114 28.651 1.00 86.45 ? 204 PHE A CD2 1 ATOM 1564 C CE1 . PHE A 1 204 ? 52.648 -39.027 26.850 1.00 84.10 ? 204 PHE A CE1 1 ATOM 1565 C CE2 . PHE A 1 204 ? 52.621 -41.379 27.306 1.00 86.93 ? 204 PHE A CE2 1 ATOM 1566 C CZ . PHE A 1 204 ? 52.725 -40.334 26.402 1.00 85.68 ? 204 PHE A CZ 1 ATOM 1567 N N . VAL A 1 205 ? 53.663 -37.563 33.126 1.00 84.93 ? 205 VAL A N 1 ATOM 1568 C CA . VAL A 1 205 ? 53.320 -36.931 34.399 1.00 84.31 ? 205 VAL A CA 1 ATOM 1569 C C . VAL A 1 205 ? 52.257 -35.875 34.076 1.00 82.37 ? 205 VAL A C 1 ATOM 1570 O O . VAL A 1 205 ? 52.372 -35.190 33.053 1.00 81.92 ? 205 VAL A O 1 ATOM 1571 C CB . VAL A 1 205 ? 54.558 -36.262 35.041 1.00 85.82 ? 205 VAL A CB 1 ATOM 1572 C CG1 . VAL A 1 205 ? 54.258 -35.771 36.457 1.00 85.72 ? 205 VAL A CG1 1 ATOM 1573 C CG2 . VAL A 1 205 ? 55.740 -37.225 35.052 1.00 88.22 ? 205 VAL A CG2 1 ATOM 1574 N N . PRO A 1 206 ? 51.209 -35.753 34.920 1.00 81.27 ? 206 PRO A N 1 ATOM 1575 C CA . PRO A 1 206 ? 50.142 -34.800 34.608 1.00 79.89 ? 206 PRO A CA 1 ATOM 1576 C C . PRO A 1 206 ? 50.499 -33.348 34.960 1.00 79.95 ? 206 PRO A C 1 ATOM 1577 O O . PRO A 1 206 ? 51.611 -33.063 35.423 1.00 80.93 ? 206 PRO A O 1 ATOM 1578 C CB . PRO A 1 206 ? 48.970 -35.300 35.461 1.00 79.28 ? 206 PRO A CB 1 ATOM 1579 C CG . PRO A 1 206 ? 49.613 -35.943 36.633 1.00 80.28 ? 206 PRO A CG 1 ATOM 1580 C CD . PRO A 1 206 ? 50.932 -36.494 36.165 1.00 81.64 ? 206 PRO A CD 1 ATOM 1581 N N . SER A 1 207 ? 49.539 -32.450 34.751 1.00 79.03 ? 207 SER A N 1 ATOM 1582 C CA . SER A 1 207 ? 49.730 -31.028 34.969 1.00 79.06 ? 207 SER A CA 1 ATOM 1583 C C . SER A 1 207 ? 48.384 -30.327 35.160 1.00 77.98 ? 207 SER A C 1 ATOM 1584 O O . SER A 1 207 ? 47.824 -29.785 34.209 1.00 77.65 ? 207 SER A O 1 ATOM 1585 C CB . SER A 1 207 ? 50.453 -30.429 33.773 1.00 79.95 ? 207 SER A CB 1 ATOM 1586 O OG . SER A 1 207 ? 49.741 -30.706 32.581 1.00 79.33 ? 207 SER A OG 1 ATOM 1587 N N . PRO A 1 208 ? 47.862 -30.329 36.392 1.00 77.38 ? 208 PRO A N 1 ATOM 1588 C CA . PRO A 1 208 ? 46.603 -29.645 36.671 1.00 77.01 ? 208 PRO A CA 1 ATOM 1589 C C . PRO A 1 208 ? 46.748 -28.117 36.691 1.00 77.89 ? 208 PRO A C 1 ATOM 1590 O O . PRO A 1 208 ? 47.858 -27.593 36.819 1.00 78.30 ? 208 PRO A O 1 ATOM 1591 C CB . PRO A 1 208 ? 46.229 -30.165 38.057 1.00 76.79 ? 208 PRO A CB 1 ATOM 1592 C CG . PRO A 1 208 ? 47.529 -30.478 38.704 1.00 77.27 ? 208 PRO A CG 1 ATOM 1593 C CD . PRO A 1 208 ? 48.473 -30.886 37.611 1.00 77.64 ? 208 PRO A CD 1 ATOM 1594 N N . GLY A 1 209 ? 45.617 -27.424 36.576 1.00 78.13 ? 209 GLY A N 1 ATOM 1595 C CA . GLY A 1 209 ? 45.591 -25.968 36.401 1.00 79.65 ? 209 GLY A CA 1 ATOM 1596 C C . GLY A 1 209 ? 44.392 -25.525 35.575 1.00 80.21 ? 209 GLY A C 1 ATOM 1597 O O . GLY A 1 209 ? 43.734 -26.341 34.926 1.00 79.36 ? 209 GLY A O 1 ATOM 1598 N N . ALA A 1 210 ? 44.115 -24.227 35.594 1.00 82.13 ? 210 ALA A N 1 ATOM 1599 C CA . ALA A 1 210 ? 42.897 -23.678 34.993 1.00 83.39 ? 210 ALA A CA 1 ATOM 1600 C C . ALA A 1 210 ? 42.994 -23.484 33.474 1.00 84.18 ? 210 ALA A C 1 ATOM 1601 O O . ALA A 1 210 ? 43.873 -22.766 33.000 1.00 85.22 ? 210 ALA A O 1 ATOM 1602 C CB . ALA A 1 210 ? 42.554 -22.356 35.663 1.00 85.42 ? 210 ALA A CB 1 ATOM 1603 N N . ARG A 1 211 ? 42.083 -24.123 32.730 1.00 83.94 ? 211 ARG A N 1 ATOM 1604 C CA . ARG A 1 211 ? 41.902 -23.887 31.288 1.00 85.19 ? 211 ARG A CA 1 ATOM 1605 C C . ARG A 1 211 ? 40.586 -23.151 31.047 1.00 87.39 ? 211 ARG A C 1 ATOM 1606 O O . ARG A 1 211 ? 39.736 -23.108 31.936 1.00 87.92 ? 211 ARG A O 1 ATOM 1607 C CB . ARG A 1 211 ? 41.860 -25.207 30.518 1.00 83.89 ? 211 ARG A CB 1 ATOM 1608 C CG . ARG A 1 211 ? 43.188 -25.922 30.404 1.00 82.59 ? 211 ARG A CG 1 ATOM 1609 C CD . ARG A 1 211 ? 43.416 -26.821 31.600 1.00 81.20 ? 211 ARG A CD 1 ATOM 1610 N NE . ARG A 1 211 ? 44.722 -27.458 31.539 1.00 80.70 ? 211 ARG A NE 1 ATOM 1611 C CZ . ARG A 1 211 ? 45.154 -28.371 32.402 1.00 79.87 ? 211 ARG A CZ 1 ATOM 1612 N NH1 . ARG A 1 211 ? 44.380 -28.768 33.407 1.00 79.48 ? 211 ARG A NH1 1 ATOM 1613 N NH2 . ARG A 1 211 ? 46.368 -28.889 32.252 1.00 79.74 ? 211 ARG A NH2 1 ATOM 1614 N N . PRO A 1 212 ? 40.403 -22.576 29.842 1.00 89.24 ? 212 PRO A N 1 ATOM 1615 C CA . PRO A 1 212 ? 39.122 -21.923 29.554 1.00 91.67 ? 212 PRO A CA 1 ATOM 1616 C C . PRO A 1 212 ? 37.973 -22.927 29.468 1.00 90.93 ? 212 PRO A C 1 ATOM 1617 O O . PRO A 1 212 ? 38.179 -24.066 29.050 1.00 89.02 ? 212 PRO A O 1 ATOM 1618 C CB . PRO A 1 212 ? 39.362 -21.248 28.194 1.00 93.77 ? 212 PRO A CB 1 ATOM 1619 C CG . PRO A 1 212 ? 40.478 -22.013 27.574 1.00 91.65 ? 212 PRO A CG 1 ATOM 1620 C CD . PRO A 1 212 ? 41.348 -22.451 28.713 1.00 89.47 ? 212 PRO A CD 1 ATOM 1621 N N . GLN A 1 213 ? 36.777 -22.497 29.859 1.00 92.83 ? 213 GLN A N 1 ATOM 1622 C CA . GLN A 1 213 ? 35.622 -23.387 29.916 1.00 92.93 ? 213 GLN A CA 1 ATOM 1623 C C . GLN A 1 213 ? 35.163 -23.816 28.530 1.00 94.29 ? 213 GLN A C 1 ATOM 1624 O O . GLN A 1 213 ? 34.691 -22.999 27.741 1.00 97.05 ? 213 GLN A O 1 ATOM 1625 C CB . GLN A 1 213 ? 34.459 -22.739 30.676 1.00 95.08 ? 213 GLN A CB 1 ATOM 1626 C CG . GLN A 1 213 ? 34.653 -22.733 32.186 1.00 93.53 ? 213 GLN A CG 1 ATOM 1627 C CD . GLN A 1 213 ? 33.423 -22.272 32.946 1.00 95.53 ? 213 GLN A CD 1 ATOM 1628 O OE1 . GLN A 1 213 ? 32.395 -21.944 32.353 1.00 98.39 ? 213 GLN A OE1 1 ATOM 1629 N NE2 . GLN A 1 213 ? 33.524 -22.250 34.270 1.00 94.20 ? 213 GLN A NE2 1 ATOM 1630 N N . VAL A 1 214 ? 35.326 -25.106 28.246 1.00 92.83 ? 214 VAL A N 1 ATOM 1631 C CA . VAL A 1 214 ? 34.808 -25.728 27.031 1.00 94.37 ? 214 VAL A CA 1 ATOM 1632 C C . VAL A 1 214 ? 33.742 -26.734 27.458 1.00 95.30 ? 214 VAL A C 1 ATOM 1633 O O . VAL A 1 214 ? 33.968 -27.524 28.379 1.00 93.56 ? 214 VAL A O 1 ATOM 1634 C CB . VAL A 1 214 ? 35.930 -26.431 26.244 1.00 92.29 ? 214 VAL A CB 1 ATOM 1635 C CG1 . VAL A 1 214 ? 35.361 -27.273 25.109 1.00 93.48 ? 214 VAL A CG1 1 ATOM 1636 C CG2 . VAL A 1 214 ? 36.917 -25.404 25.709 1.00 92.45 ? 214 VAL A CG2 1 ATOM 1637 N N . ASN A 1 215 ? 32.582 -26.686 26.802 1.00 98.79 ? 215 ASN A N 1 ATOM 1638 C CA . ASN A 1 215 ? 31.383 -27.425 27.233 1.00 100.49 ? 215 ASN A CA 1 ATOM 1639 C C . ASN A 1 215 ? 30.979 -27.110 28.681 1.00 100.33 ? 215 ASN A C 1 ATOM 1640 O O . ASN A 1 215 ? 30.311 -27.915 29.332 1.00 100.50 ? 215 ASN A O 1 ATOM 1641 C CB . ASN A 1 215 ? 31.571 -28.943 27.058 1.00 99.14 ? 215 ASN A CB 1 ATOM 1642 C CG . ASN A 1 215 ? 31.753 -29.353 25.610 1.00 99.94 ? 215 ASN A CG 1 ATOM 1643 O OD1 . ASN A 1 215 ? 31.142 -28.781 24.707 1.00 102.74 ? 215 ASN A OD1 1 ATOM 1644 N ND2 . ASN A 1 215 ? 32.583 -30.365 25.383 1.00 97.80 ? 215 ASN A ND2 1 ATOM 1645 N N . GLY A 1 216 ? 31.377 -25.934 29.169 1.00 100.30 ? 216 GLY A N 1 ATOM 1646 C CA . GLY A 1 216 ? 31.160 -25.545 30.561 1.00 99.87 ? 216 GLY A CA 1 ATOM 1647 C C . GLY A 1 216 ? 32.208 -26.057 31.539 1.00 96.35 ? 216 GLY A C 1 ATOM 1648 O O . GLY A 1 216 ? 32.122 -25.773 32.732 1.00 95.62 ? 216 GLY A O 1 ATOM 1649 N N . LEU A 1 217 ? 33.206 -26.787 31.040 1.00 94.41 ? 217 LEU A N 1 ATOM 1650 C CA . LEU A 1 217 ? 34.206 -27.441 31.890 1.00 91.59 ? 217 LEU A CA 1 ATOM 1651 C C . LEU A 1 217 ? 35.631 -26.979 31.572 1.00 90.33 ? 217 LEU A C 1 ATOM 1652 O O . LEU A 1 217 ? 35.981 -26.779 30.406 1.00 90.73 ? 217 LEU A O 1 ATOM 1653 C CB . LEU A 1 217 ? 34.105 -28.955 31.721 1.00 90.80 ? 217 LEU A CB 1 ATOM 1654 C CG . LEU A 1 217 ? 32.707 -29.533 31.960 1.00 92.82 ? 217 LEU A CG 1 ATOM 1655 C CD1 . LEU A 1 217 ? 32.634 -30.978 31.501 1.00 92.83 ? 217 LEU A CD1 1 ATOM 1656 C CD2 . LEU A 1 217 ? 32.320 -29.411 33.427 1.00 92.57 ? 217 LEU A CD2 1 ATOM 1657 N N . SER A 1 218 ? 36.445 -26.835 32.618 1.00 61.81 ? 218 SER A N 1 ATOM 1658 C CA . SER A 1 218 ? 37.814 -26.311 32.509 1.00 62.42 ? 218 SER A CA 1 ATOM 1659 C C . SER A 1 218 ? 38.889 -27.383 32.695 1.00 62.44 ? 218 SER A C 1 ATOM 1660 O O . SER A 1 218 ? 40.085 -27.075 32.696 1.00 62.09 ? 218 SER A O 1 ATOM 1661 C CB . SER A 1 218 ? 38.032 -25.189 33.530 1.00 64.99 ? 218 SER A CB 1 ATOM 1662 O OG . SER A 1 218 ? 37.446 -23.976 33.095 1.00 65.39 ? 218 SER A OG 1 ATOM 1663 N N . GLY A 1 219 ? 38.467 -28.633 32.873 1.00 62.61 ? 219 GLY A N 1 ATOM 1664 C CA . GLY A 1 219 ? 39.393 -29.763 32.892 1.00 62.86 ? 219 GLY A CA 1 ATOM 1665 C C . GLY A 1 219 ? 39.684 -30.222 31.475 1.00 60.99 ? 219 GLY A C 1 ATOM 1666 O O . GLY A 1 219 ? 38.965 -29.859 30.547 1.00 59.87 ? 219 GLY A O 1 ATOM 1667 N N . ARG A 1 220 ? 40.743 -31.014 31.307 1.00 61.14 ? 220 ARG A N 1 ATOM 1668 C CA . ARG A 1 220 ? 41.081 -31.596 30.009 1.00 59.66 ? 220 ARG A CA 1 ATOM 1669 C C . ARG A 1 220 ? 41.532 -33.051 30.153 1.00 60.53 ? 220 ARG A C 1 ATOM 1670 O O . ARG A 1 220 ? 42.064 -33.450 31.193 1.00 61.77 ? 220 ARG A O 1 ATOM 1671 C CB . ARG A 1 220 ? 42.193 -30.790 29.330 1.00 59.33 ? 220 ARG A CB 1 ATOM 1672 C CG . ARG A 1 220 ? 41.865 -29.328 29.044 1.00 58.45 ? 220 ARG A CG 1 ATOM 1673 C CD . ARG A 1 220 ? 40.848 -29.163 27.927 1.00 56.15 ? 220 ARG A CD 1 ATOM 1674 N NE . ARG A 1 220 ? 40.709 -27.760 27.554 1.00 55.75 ? 220 ARG A NE 1 ATOM 1675 C CZ . ARG A 1 220 ? 39.835 -26.897 28.072 1.00 57.26 ? 220 ARG A CZ 1 ATOM 1676 N NH1 . ARG A 1 220 ? 38.957 -27.263 29.006 1.00 58.43 ? 220 ARG A NH1 1 ATOM 1677 N NH2 . ARG A 1 220 ? 39.837 -25.638 27.644 1.00 57.61 ? 220 ARG A NH2 1 ATOM 1678 N N . ILE A 1 221 ? 41.323 -33.833 29.097 1.00 59.31 ? 221 ILE A N 1 ATOM 1679 C CA . ILE A 1 221 ? 41.858 -35.194 29.013 1.00 60.09 ? 221 ILE A CA 1 ATOM 1680 C C . ILE A 1 221 ? 42.748 -35.331 27.765 1.00 58.99 ? 221 ILE A C 1 ATOM 1681 O O . ILE A 1 221 ? 42.265 -35.194 26.644 1.00 57.37 ? 221 ILE A O 1 ATOM 1682 C CB . ILE A 1 221 ? 40.715 -36.243 28.996 1.00 59.61 ? 221 ILE A CB 1 ATOM 1683 C CG1 . ILE A 1 221 ? 40.014 -36.277 30.358 1.00 61.19 ? 221 ILE A CG1 1 ATOM 1684 C CG2 . ILE A 1 221 ? 41.241 -37.633 28.647 1.00 59.55 ? 221 ILE A CG2 1 ATOM 1685 C CD1 . ILE A 1 221 ? 38.777 -37.151 30.404 1.00 60.79 ? 221 ILE A CD1 1 ATOM 1686 N N . ASP A 1 222 ? 44.045 -35.573 27.964 1.00 60.56 ? 222 ASP A N 1 ATOM 1687 C CA . ASP A 1 222 ? 44.941 -35.957 26.858 1.00 60.14 ? 222 ASP A CA 1 ATOM 1688 C C . ASP A 1 222 ? 44.618 -37.391 26.429 1.00 59.22 ? 222 ASP A C 1 ATOM 1689 O O . ASP A 1 222 ? 44.399 -38.242 27.278 1.00 60.36 ? 222 ASP A O 1 ATOM 1690 C CB . ASP A 1 222 ? 46.416 -35.930 27.285 1.00 62.38 ? 222 ASP A CB 1 ATOM 1691 C CG . ASP A 1 222 ? 46.973 -34.524 27.440 1.00 63.67 ? 222 ASP A CG 1 ATOM 1692 O OD1 . ASP A 1 222 ? 46.284 -33.665 28.027 1.00 64.34 ? 222 ASP A OD1 1 ATOM 1693 O OD2 . ASP A 1 222 ? 48.118 -34.285 26.990 1.00 63.84 ? 222 ASP A OD2 1 ATOM 1694 N N . PHE A 1 223 ? 44.596 -37.649 25.126 1.00 57.70 ? 223 PHE A N 1 ATOM 1695 C CA . PHE A 1 223 ? 44.484 -39.006 24.595 1.00 57.55 ? 223 PHE A CA 1 ATOM 1696 C C . PHE A 1 223 ? 45.757 -39.356 23.831 1.00 58.05 ? 223 PHE A C 1 ATOM 1697 O O . PHE A 1 223 ? 46.179 -38.598 22.967 1.00 58.19 ? 223 PHE A O 1 ATOM 1698 C CB . PHE A 1 223 ? 43.273 -39.130 23.669 1.00 55.34 ? 223 PHE A CB 1 ATOM 1699 C CG . PHE A 1 223 ? 41.951 -39.139 24.388 1.00 54.78 ? 223 PHE A CG 1 ATOM 1700 C CD1 . PHE A 1 223 ? 41.538 -40.256 25.092 1.00 55.57 ? 223 PHE A CD1 1 ATOM 1701 C CD2 . PHE A 1 223 ? 41.113 -38.031 24.351 1.00 54.54 ? 223 PHE A CD2 1 ATOM 1702 C CE1 . PHE A 1 223 ? 40.317 -40.272 25.744 1.00 55.52 ? 223 PHE A CE1 1 ATOM 1703 C CE2 . PHE A 1 223 ? 39.893 -38.037 25.007 1.00 54.25 ? 223 PHE A CE2 1 ATOM 1704 C CZ . PHE A 1 223 ? 39.495 -39.159 25.701 1.00 54.89 ? 223 PHE A CZ 1 ATOM 1705 N N . HIS A 1 224 ? 46.359 -40.496 24.170 1.00 59.80 ? 224 HIS A N 1 ATOM 1706 C CA . HIS A 1 224 ? 47.596 -40.987 23.553 1.00 60.71 ? 224 HIS A CA 1 ATOM 1707 C C . HIS A 1 224 ? 47.373 -42.368 22.933 1.00 59.88 ? 224 HIS A C 1 ATOM 1708 O O . HIS A 1 224 ? 46.485 -43.103 23.368 1.00 58.52 ? 224 HIS A O 1 ATOM 1709 C CB . HIS A 1 224 ? 48.683 -41.133 24.609 1.00 64.15 ? 224 HIS A CB 1 ATOM 1710 C CG . HIS A 1 224 ? 48.985 -39.871 25.352 1.00 66.01 ? 224 HIS A CG 1 ATOM 1711 N ND1 . HIS A 1 224 ? 48.307 -39.497 26.493 1.00 66.58 ? 224 HIS A ND1 1 ATOM 1712 C CD2 . HIS A 1 224 ? 49.908 -38.908 25.129 1.00 66.85 ? 224 HIS A CD2 1 ATOM 1713 C CE1 . HIS A 1 224 ? 48.789 -38.351 26.933 1.00 67.40 ? 224 HIS A CE1 1 ATOM 1714 N NE2 . HIS A 1 224 ? 49.760 -37.971 26.122 1.00 68.09 ? 224 HIS A NE2 1 ATOM 1715 N N . TRP A 1 225 ? 48.210 -42.737 21.961 1.00 59.60 ? 225 TRP A N 1 ATOM 1716 C CA . TRP A 1 225 ? 48.036 -44.000 21.241 1.00 58.90 ? 225 TRP A CA 1 ATOM 1717 C C . TRP A 1 225 ? 49.318 -44.639 20.699 1.00 60.67 ? 225 TRP A C 1 ATOM 1718 O O . TRP A 1 225 ? 50.296 -43.951 20.417 1.00 60.77 ? 225 TRP A O 1 ATOM 1719 C CB . TRP A 1 225 ? 47.070 -43.780 20.079 1.00 56.25 ? 225 TRP A CB 1 ATOM 1720 C CG . TRP A 1 225 ? 47.605 -42.848 19.048 1.00 55.22 ? 225 TRP A CG 1 ATOM 1721 C CD1 . TRP A 1 225 ? 47.537 -41.491 19.061 1.00 54.28 ? 225 TRP A CD1 1 ATOM 1722 C CD2 . TRP A 1 225 ? 48.305 -43.206 17.852 1.00 55.12 ? 225 TRP A CD2 1 ATOM 1723 N NE1 . TRP A 1 225 ? 48.147 -40.976 17.944 1.00 53.94 ? 225 TRP A NE1 1 ATOM 1724 C CE2 . TRP A 1 225 ? 48.630 -42.009 17.186 1.00 54.15 ? 225 TRP A CE2 1 ATOM 1725 C CE3 . TRP A 1 225 ? 48.683 -44.426 17.275 1.00 55.59 ? 225 TRP A CE3 1 ATOM 1726 C CZ2 . TRP A 1 225 ? 49.313 -41.990 15.970 1.00 54.20 ? 225 TRP A CZ2 1 ATOM 1727 C CZ3 . TRP A 1 225 ? 49.365 -44.407 16.070 1.00 55.41 ? 225 TRP A CZ3 1 ATOM 1728 C CH2 . TRP A 1 225 ? 49.677 -43.195 15.432 1.00 55.10 ? 225 TRP A CH2 1 ATOM 1729 N N . LEU A 1 226 ? 49.288 -45.967 20.544 1.00 62.48 ? 226 LEU A N 1 ATOM 1730 C CA . LEU A 1 226 ? 50.341 -46.704 19.827 1.00 63.75 ? 226 LEU A CA 1 ATOM 1731 C C . LEU A 1 226 ? 49.798 -47.935 19.104 1.00 63.45 ? 226 LEU A C 1 ATOM 1732 O O . LEU A 1 226 ? 48.741 -48.457 19.464 1.00 62.31 ? 226 LEU A O 1 ATOM 1733 C CB . LEU A 1 226 ? 51.493 -47.106 20.761 1.00 66.76 ? 226 LEU A CB 1 ATOM 1734 C CG . LEU A 1 226 ? 51.446 -48.296 21.745 1.00 69.00 ? 226 LEU A CG 1 ATOM 1735 C CD1 . LEU A 1 226 ? 50.483 -48.050 22.890 1.00 68.76 ? 226 LEU A CD1 1 ATOM 1736 C CD2 . LEU A 1 226 ? 51.148 -49.643 21.097 1.00 68.92 ? 226 LEU A CD2 1 ATOM 1737 N N . MET A 1 227 ? 50.541 -48.391 18.091 1.00 64.20 ? 227 MET A N 1 ATOM 1738 C CA . MET A 1 227 ? 50.231 -49.625 17.366 1.00 64.01 ? 227 MET A CA 1 ATOM 1739 C C . MET A 1 227 ? 51.033 -50.780 17.957 1.00 66.49 ? 227 MET A C 1 ATOM 1740 O O . MET A 1 227 ? 52.267 -50.779 17.911 1.00 67.94 ? 227 MET A O 1 ATOM 1741 C CB . MET A 1 227 ? 50.556 -49.484 15.874 1.00 63.52 ? 227 MET A CB 1 ATOM 1742 C CG . MET A 1 227 ? 49.783 -48.384 15.158 1.00 61.54 ? 227 MET A CG 1 ATOM 1743 S SD . MET A 1 227 ? 48.007 -48.687 15.040 1.00 59.77 ? 227 MET A SD 1 ATOM 1744 C CE . MET A 1 227 ? 47.974 -50.005 13.832 1.00 60.43 ? 227 MET A CE 1 ATOM 1745 N N . LEU A 1 228 ? 50.327 -51.754 18.527 1.00 66.82 ? 228 LEU A N 1 ATOM 1746 C CA . LEU A 1 228 ? 50.954 -52.910 19.152 1.00 69.60 ? 228 LEU A CA 1 ATOM 1747 C C . LEU A 1 228 ? 51.001 -54.080 18.175 1.00 70.10 ? 228 LEU A C 1 ATOM 1748 O O . LEU A 1 228 ? 49.960 -54.581 17.741 1.00 69.05 ? 228 LEU A O 1 ATOM 1749 C CB . LEU A 1 228 ? 50.193 -53.313 20.419 1.00 70.00 ? 228 LEU A CB 1 ATOM 1750 C CG . LEU A 1 228 ? 50.842 -54.400 21.281 1.00 73.18 ? 228 LEU A CG 1 ATOM 1751 C CD1 . LEU A 1 228 ? 52.230 -53.973 21.744 1.00 75.41 ? 228 LEU A CD1 1 ATOM 1752 C CD2 . LEU A 1 228 ? 49.955 -54.730 22.472 1.00 73.64 ? 228 LEU A CD2 1 ATOM 1753 N N . ASN A 1 229 ? 52.213 -54.513 17.842 1.00 72.41 ? 229 ASN A N 1 ATOM 1754 C CA . ASN A 1 229 ? 52.426 -55.597 16.889 1.00 73.58 ? 229 ASN A CA 1 ATOM 1755 C C . ASN A 1 229 ? 51.944 -56.961 17.404 1.00 75.28 ? 229 ASN A C 1 ATOM 1756 O O . ASN A 1 229 ? 51.792 -57.150 18.614 1.00 75.56 ? 229 ASN A O 1 ATOM 1757 C CB . ASN A 1 229 ? 53.917 -55.692 16.530 1.00 75.98 ? 229 ASN A CB 1 ATOM 1758 C CG . ASN A 1 229 ? 54.378 -54.563 15.629 1.00 74.62 ? 229 ASN A CG 1 ATOM 1759 O OD1 . ASN A 1 229 ? 53.638 -54.105 14.757 1.00 72.16 ? 229 ASN A OD1 1 ATOM 1760 N ND2 . ASN A 1 229 ? 55.615 -54.118 15.821 1.00 76.69 ? 229 ASN A ND2 1 ATOM 1761 N N . PRO A 1 230 ? 51.701 -57.914 16.480 1.00 76.32 ? 230 PRO A N 1 ATOM 1762 C CA . PRO A 1 230 ? 51.346 -59.292 16.838 1.00 78.99 ? 230 PRO A CA 1 ATOM 1763 C C . PRO A 1 230 ? 52.347 -59.945 17.795 1.00 83.79 ? 230 PRO A C 1 ATOM 1764 O O . PRO A 1 230 ? 53.551 -59.881 17.562 1.00 84.85 ? 230 PRO A O 1 ATOM 1765 C CB . PRO A 1 230 ? 51.356 -60.011 15.485 1.00 78.40 ? 230 PRO A CB 1 ATOM 1766 C CG . PRO A 1 230 ? 50.976 -58.954 14.510 1.00 75.23 ? 230 PRO A CG 1 ATOM 1767 C CD . PRO A 1 230 ? 51.634 -57.701 15.021 1.00 75.13 ? 230 PRO A CD 1 ATOM 1768 N N . ASN A 1 231 ? 51.831 -60.555 18.861 1.00 87.51 ? 231 ASN A N 1 ATOM 1769 C CA . ASN A 1 231 ? 52.636 -61.194 19.916 1.00 94.00 ? 231 ASN A CA 1 ATOM 1770 C C . ASN A 1 231 ? 53.445 -60.238 20.803 1.00 93.00 ? 231 ASN A C 1 ATOM 1771 O O . ASN A 1 231 ? 54.173 -60.686 21.690 1.00 96.10 ? 231 ASN A O 1 ATOM 1772 C CB . ASN A 1 231 ? 53.552 -62.301 19.347 1.00 101.07 ? 231 ASN A CB 1 ATOM 1773 C CG . ASN A 1 231 ? 52.801 -63.584 19.026 1.00 107.70 ? 231 ASN A CG 1 ATOM 1774 O OD1 . ASN A 1 231 ? 51.679 -63.796 19.488 1.00 105.89 ? 231 ASN A OD1 1 ATOM 1775 N ND2 . ASN A 1 231 ? 53.429 -64.452 18.228 1.00 118.50 ? 231 ASN A ND2 1 ATOM 1776 N N . ASP A 1 232 ? 53.306 -58.932 20.585 1.00 88.41 ? 232 ASP A N 1 ATOM 1777 C CA . ASP A 1 232 ? 53.971 -57.941 21.427 1.00 88.37 ? 232 ASP A CA 1 ATOM 1778 C C . ASP A 1 232 ? 53.091 -57.647 22.638 1.00 86.86 ? 232 ASP A C 1 ATOM 1779 O O . ASP A 1 232 ? 51.868 -57.760 22.567 1.00 84.87 ? 232 ASP A O 1 ATOM 1780 C CB . ASP A 1 232 ? 54.250 -56.660 20.632 1.00 85.82 ? 232 ASP A CB 1 ATOM 1781 C CG . ASP A 1 232 ? 55.207 -55.706 21.348 1.00 87.28 ? 232 ASP A CG 1 ATOM 1782 O OD1 . ASP A 1 232 ? 55.728 -56.042 22.435 1.00 89.74 ? 232 ASP A OD1 1 ATOM 1783 O OD2 . ASP A 1 232 ? 55.442 -54.605 20.808 1.00 85.94 ? 232 ASP A OD2 1 ATOM 1784 N N . THR A 1 233 ? 53.726 -57.278 23.747 1.00 88.08 ? 233 THR A N 1 ATOM 1785 C CA . THR A 1 233 ? 53.026 -56.977 24.989 1.00 87.56 ? 233 THR A CA 1 ATOM 1786 C C . THR A 1 233 ? 53.234 -55.505 25.359 1.00 86.76 ? 233 THR A C 1 ATOM 1787 O O . THR A 1 233 ? 54.322 -54.956 25.156 1.00 87.82 ? 233 THR A O 1 ATOM 1788 C CB . THR A 1 233 ? 53.530 -57.875 26.141 1.00 91.10 ? 233 THR A CB 1 ATOM 1789 O OG1 . THR A 1 233 ? 53.467 -59.255 25.749 1.00 92.09 ? 233 THR A OG1 1 ATOM 1790 C CG2 . THR A 1 233 ? 52.693 -57.674 27.392 1.00 90.99 ? 233 THR A CG2 1 ATOM 1791 N N . VAL A 1 234 ? 52.184 -54.881 25.897 1.00 84.63 ? 234 VAL A N 1 ATOM 1792 C CA . VAL A 1 234 ? 52.232 -53.491 26.368 1.00 83.10 ? 234 VAL A CA 1 ATOM 1793 C C . VAL A 1 234 ? 51.849 -53.425 27.845 1.00 84.01 ? 234 VAL A C 1 ATOM 1794 O O . VAL A 1 234 ? 50.925 -54.111 28.278 1.00 82.64 ? 234 VAL A O 1 ATOM 1795 C CB . VAL A 1 234 ? 51.310 -52.556 25.542 1.00 79.54 ? 234 VAL A CB 1 ATOM 1796 C CG1 . VAL A 1 234 ? 49.859 -53.024 25.558 1.00 77.89 ? 234 VAL A CG1 1 ATOM 1797 C CG2 . VAL A 1 234 ? 51.407 -51.120 26.046 1.00 79.11 ? 234 VAL A CG2 1 ATOM 1798 N N . THR A 1 235 ? 52.558 -52.591 28.607 1.00 85.54 ? 235 THR A N 1 ATOM 1799 C CA . THR A 1 235 ? 52.324 -52.476 30.046 1.00 87.56 ? 235 THR A CA 1 ATOM 1800 C C . THR A 1 235 ? 52.088 -51.026 30.475 1.00 86.74 ? 235 THR A C 1 ATOM 1801 O O . THR A 1 235 ? 52.735 -50.098 29.973 1.00 85.50 ? 235 THR A O 1 ATOM 1802 C CB . THR A 1 235 ? 53.496 -53.070 30.852 1.00 91.74 ? 235 THR A CB 1 ATOM 1803 O OG1 . THR A 1 235 ? 53.843 -54.354 30.319 1.00 93.06 ? 235 THR A OG1 1 ATOM 1804 C CG2 . THR A 1 235 ? 53.124 -53.223 32.324 1.00 93.97 ? 235 THR A CG2 1 ATOM 1805 N N . PHE A 1 236 ? 51.154 -50.855 31.411 1.00 87.09 ? 236 PHE A N 1 ATOM 1806 C CA . PHE A 1 236 ? 50.785 -49.549 31.941 1.00 86.51 ? 236 PHE A CA 1 ATOM 1807 C C . PHE A 1 236 ? 51.085 -49.481 33.436 1.00 90.26 ? 236 PHE A C 1 ATOM 1808 O O . PHE A 1 236 ? 50.384 -50.105 34.237 1.00 91.88 ? 236 PHE A O 1 ATOM 1809 C CB . PHE A 1 236 ? 49.288 -49.294 31.729 1.00 83.86 ? 236 PHE A CB 1 ATOM 1810 C CG . PHE A 1 236 ? 48.883 -49.161 30.287 1.00 80.42 ? 236 PHE A CG 1 ATOM 1811 C CD1 . PHE A 1 236 ? 49.098 -47.975 29.598 1.00 78.68 ? 236 PHE A CD1 1 ATOM 1812 C CD2 . PHE A 1 236 ? 48.268 -50.216 29.622 1.00 79.38 ? 236 PHE A CD2 1 ATOM 1813 C CE1 . PHE A 1 236 ? 48.719 -47.845 28.271 1.00 75.50 ? 236 PHE A CE1 1 ATOM 1814 C CE2 . PHE A 1 236 ? 47.887 -50.093 28.295 1.00 76.77 ? 236 PHE A CE2 1 ATOM 1815 C CZ . PHE A 1 236 ? 48.112 -48.905 27.619 1.00 74.93 ? 236 PHE A CZ 1 ATOM 1816 N N . SER A 1 237 ? 52.118 -48.725 33.808 1.00 91.88 ? 237 SER A N 1 ATOM 1817 C CA . SER A 1 237 ? 52.385 -48.416 35.214 1.00 95.10 ? 237 SER A CA 1 ATOM 1818 C C . SER A 1 237 ? 51.847 -47.016 35.500 1.00 93.46 ? 237 SER A C 1 ATOM 1819 O O . SER A 1 237 ? 52.260 -46.054 34.852 1.00 90.99 ? 237 SER A O 1 ATOM 1820 C CB . SER A 1 237 ? 53.884 -48.485 35.531 1.00 98.35 ? 237 SER A CB 1 ATOM 1821 O OG . SER A 1 237 ? 54.513 -47.222 35.373 1.00 97.74 ? 237 SER A OG 1 ATOM 1822 N N . PHE A 1 238 ? 50.927 -46.909 36.458 1.00 94.03 ? 238 PHE A N 1 ATOM 1823 C CA . PHE A 1 238 ? 50.257 -45.638 36.736 1.00 92.45 ? 238 PHE A CA 1 ATOM 1824 C C . PHE A 1 238 ? 49.967 -45.414 38.222 1.00 94.87 ? 238 PHE A C 1 ATOM 1825 O O . PHE A 1 238 ? 49.571 -46.333 38.941 1.00 96.31 ? 238 PHE A O 1 ATOM 1826 C CB . PHE A 1 238 ? 48.970 -45.505 35.909 1.00 89.42 ? 238 PHE A CB 1 ATOM 1827 C CG . PHE A 1 238 ? 48.064 -46.705 35.975 1.00 89.97 ? 238 PHE A CG 1 ATOM 1828 C CD1 . PHE A 1 238 ? 48.328 -47.835 35.206 1.00 90.03 ? 238 PHE A CD1 1 ATOM 1829 C CD2 . PHE A 1 238 ? 46.936 -46.699 36.785 1.00 90.06 ? 238 PHE A CD2 1 ATOM 1830 C CE1 . PHE A 1 238 ? 47.495 -48.941 35.257 1.00 90.03 ? 238 PHE A CE1 1 ATOM 1831 C CE2 . PHE A 1 238 ? 46.096 -47.801 36.836 1.00 90.35 ? 238 PHE A CE2 1 ATOM 1832 C CZ . PHE A 1 238 ? 46.376 -48.923 36.072 1.00 90.16 ? 238 PHE A CZ 1 ATOM 1833 N N . ASN A 1 239 ? 50.182 -44.174 38.659 1.00 94.86 ? 239 ASN A N 1 ATOM 1834 C CA . ASN A 1 239 ? 49.947 -43.751 40.036 1.00 97.41 ? 239 ASN A CA 1 ATOM 1835 C C . ASN A 1 239 ? 48.611 -43.012 40.161 1.00 94.79 ? 239 ASN A C 1 ATOM 1836 O O . ASN A 1 239 ? 48.217 -42.610 41.255 1.00 96.33 ? 239 ASN A O 1 ATOM 1837 C CB . ASN A 1 239 ? 51.094 -42.837 40.492 1.00 99.64 ? 239 ASN A CB 1 ATOM 1838 C CG . ASN A 1 239 ? 51.269 -42.806 42.004 1.00 104.01 ? 239 ASN A CG 1 ATOM 1839 O OD1 . ASN A 1 239 ? 50.382 -43.209 42.756 1.00 105.67 ? 239 ASN A OD1 1 ATOM 1840 N ND2 . ASN A 1 239 ? 52.420 -42.316 42.457 1.00 106.41 ? 239 ASN A ND2 1 ATOM 1841 N N . GLY A 1 240 ? 47.920 -42.842 39.037 1.00 90.88 ? 240 GLY A N 1 ATOM 1842 C CA . GLY A 1 240 ? 46.642 -42.134 39.000 1.00 88.45 ? 240 GLY A CA 1 ATOM 1843 C C . GLY A 1 240 ? 46.540 -41.242 37.781 1.00 84.51 ? 240 GLY A C 1 ATOM 1844 O O . GLY A 1 240 ? 47.435 -41.236 36.932 1.00 84.07 ? 240 GLY A O 1 ATOM 1845 N N . ALA A 1 241 ? 45.440 -40.495 37.700 1.00 82.23 ? 241 ALA A N 1 ATOM 1846 C CA . ALA A 1 241 ? 45.191 -39.538 36.614 1.00 79.01 ? 241 ALA A CA 1 ATOM 1847 C C . ALA A 1 241 ? 45.217 -40.214 35.246 1.00 76.31 ? 241 ALA A C 1 ATOM 1848 O O . ALA A 1 241 ? 45.715 -39.652 34.269 1.00 75.28 ? 241 ALA A O 1 ATOM 1849 C CB . ALA A 1 241 ? 46.199 -38.397 36.668 1.00 79.62 ? 241 ALA A CB 1 ATOM 1850 N N . PHE A 1 242 ? 44.648 -41.412 35.186 1.00 75.74 ? 242 PHE A N 1 ATOM 1851 C CA . PHE A 1 242 ? 44.785 -42.289 34.030 1.00 73.87 ? 242 PHE A CA 1 ATOM 1852 C C . PHE A 1 242 ? 43.403 -42.757 33.561 1.00 71.49 ? 242 PHE A C 1 ATOM 1853 O O . PHE A 1 242 ? 42.615 -43.264 34.363 1.00 71.78 ? 242 PHE A O 1 ATOM 1854 C CB . PHE A 1 242 ? 45.675 -43.477 34.430 1.00 76.21 ? 242 PHE A CB 1 ATOM 1855 C CG . PHE A 1 242 ? 45.768 -44.562 33.396 1.00 74.74 ? 242 PHE A CG 1 ATOM 1856 C CD1 . PHE A 1 242 ? 46.559 -44.402 32.271 1.00 73.46 ? 242 PHE A CD1 1 ATOM 1857 C CD2 . PHE A 1 242 ? 45.087 -45.760 33.566 1.00 75.35 ? 242 PHE A CD2 1 ATOM 1858 C CE1 . PHE A 1 242 ? 46.654 -45.406 31.320 1.00 72.75 ? 242 PHE A CE1 1 ATOM 1859 C CE2 . PHE A 1 242 ? 45.175 -46.768 32.620 1.00 74.44 ? 242 PHE A CE2 1 ATOM 1860 C CZ . PHE A 1 242 ? 45.961 -46.592 31.495 1.00 73.00 ? 242 PHE A CZ 1 ATOM 1861 N N . ILE A 1 243 ? 43.116 -42.547 32.273 1.00 68.09 ? 243 ILE A N 1 ATOM 1862 C CA . ILE A 1 243 ? 41.878 -43.000 31.643 1.00 66.00 ? 243 ILE A CA 1 ATOM 1863 C C . ILE A 1 243 ? 42.166 -44.294 30.885 1.00 65.51 ? 243 ILE A C 1 ATOM 1864 O O . ILE A 1 243 ? 42.785 -44.267 29.823 1.00 64.82 ? 243 ILE A O 1 ATOM 1865 C CB . ILE A 1 243 ? 41.329 -41.946 30.660 1.00 63.70 ? 243 ILE A CB 1 ATOM 1866 C CG1 . ILE A 1 243 ? 41.095 -40.605 31.369 1.00 64.71 ? 243 ILE A CG1 1 ATOM 1867 C CG2 . ILE A 1 243 ? 40.048 -42.435 29.992 1.00 61.95 ? 243 ILE A CG2 1 ATOM 1868 C CD1 . ILE A 1 243 ? 40.084 -40.656 32.496 1.00 65.82 ? 243 ILE A CD1 1 ATOM 1869 N N . ALA A 1 244 ? 41.707 -45.419 31.428 1.00 66.18 ? 244 ALA A N 1 ATOM 1870 C CA . ALA A 1 244 ? 42.123 -46.745 30.956 1.00 66.15 ? 244 ALA A CA 1 ATOM 1871 C C . ALA A 1 244 ? 41.309 -47.257 29.768 1.00 63.14 ? 244 ALA A C 1 ATOM 1872 O O . ALA A 1 244 ? 40.085 -47.120 29.751 1.00 62.32 ? 244 ALA A O 1 ATOM 1873 C CB . ALA A 1 244 ? 42.032 -47.746 32.096 1.00 68.81 ? 244 ALA A CB 1 ATOM 1874 N N . PRO A 1 245 ? 41.980 -47.887 28.789 1.00 61.90 ? 245 PRO A N 1 ATOM 1875 C CA . PRO A 1 245 ? 41.236 -48.496 27.687 1.00 59.86 ? 245 PRO A CA 1 ATOM 1876 C C . PRO A 1 245 ? 40.490 -49.746 28.128 1.00 60.64 ? 245 PRO A C 1 ATOM 1877 O O . PRO A 1 245 ? 41.040 -50.559 28.869 1.00 62.66 ? 245 PRO A O 1 ATOM 1878 C CB . PRO A 1 245 ? 42.328 -48.879 26.689 1.00 59.51 ? 245 PRO A CB 1 ATOM 1879 C CG . PRO A 1 245 ? 43.546 -49.089 27.522 1.00 62.25 ? 245 PRO A CG 1 ATOM 1880 C CD . PRO A 1 245 ? 43.428 -48.151 28.694 1.00 63.24 ? 245 PRO A CD 1 ATOM 1881 N N . ASP A 1 246 ? 39.249 -49.883 27.672 1.00 59.19 ? 246 ASP A N 1 ATOM 1882 C CA . ASP A 1 246 ? 38.479 -51.102 27.866 1.00 59.62 ? 246 ASP A CA 1 ATOM 1883 C C . ASP A 1 246 ? 38.620 -52.044 26.666 1.00 58.84 ? 246 ASP A C 1 ATOM 1884 O O . ASP A 1 246 ? 38.697 -53.262 26.834 1.00 60.19 ? 246 ASP A O 1 ATOM 1885 C CB . ASP A 1 246 ? 37.004 -50.775 28.087 1.00 58.65 ? 246 ASP A CB 1 ATOM 1886 C CG . ASP A 1 246 ? 36.189 -51.998 28.434 1.00 59.71 ? 246 ASP A CG 1 ATOM 1887 O OD1 . ASP A 1 246 ? 36.585 -52.721 29.367 1.00 62.42 ? 246 ASP A OD1 1 ATOM 1888 O OD2 . ASP A 1 246 ? 35.165 -52.252 27.767 1.00 58.49 ? 246 ASP A OD2 1 ATOM 1889 N N . ARG A 1 247 ? 38.634 -51.483 25.460 1.00 56.68 ? 247 ARG A N 1 ATOM 1890 C CA . ARG A 1 247 ? 38.764 -52.277 24.240 1.00 55.88 ? 247 ARG A CA 1 ATOM 1891 C C . ARG A 1 247 ? 39.902 -51.781 23.356 1.00 54.52 ? 247 ARG A C 1 ATOM 1892 O O . ARG A 1 247 ? 40.300 -50.621 23.423 1.00 53.45 ? 247 ARG A O 1 ATOM 1893 C CB . ARG A 1 247 ? 37.475 -52.232 23.430 1.00 54.77 ? 247 ARG A CB 1 ATOM 1894 C CG . ARG A 1 247 ? 36.265 -52.864 24.096 1.00 56.19 ? 247 ARG A CG 1 ATOM 1895 C CD . ARG A 1 247 ? 34.992 -52.388 23.417 1.00 54.89 ? 247 ARG A CD 1 ATOM 1896 N NE . ARG A 1 247 ? 34.311 -53.412 22.643 1.00 55.02 ? 247 ARG A NE 1 ATOM 1897 C CZ . ARG A 1 247 ? 33.349 -53.174 21.752 1.00 53.71 ? 247 ARG A CZ 1 ATOM 1898 N NH1 . ARG A 1 247 ? 32.953 -51.932 21.478 1.00 52.09 ? 247 ARG A NH1 1 ATOM 1899 N NH2 . ARG A 1 247 ? 32.785 -54.194 21.117 1.00 53.50 ? 247 ARG A NH2 1 ATOM 1900 N N . ALA A 1 248 ? 40.405 -52.686 22.522 1.00 54.05 ? 248 ALA A N 1 ATOM 1901 C CA . ALA A 1 248 ? 41.427 -52.381 21.537 1.00 53.23 ? 248 ALA A CA 1 ATOM 1902 C C . ALA A 1 248 ? 40.788 -52.439 20.163 1.00 50.86 ? 248 ALA A C 1 ATOM 1903 O O . ALA A 1 248 ? 39.828 -53.177 19.948 1.00 50.19 ? 248 ALA A O 1 ATOM 1904 C CB . ALA A 1 248 ? 42.562 -53.392 21.622 1.00 55.50 ? 248 ALA A CB 1 ATOM 1905 N N . SER A 1 249 ? 41.336 -51.668 19.230 1.00 49.72 ? 249 SER A N 1 ATOM 1906 C CA . SER A 1 249 ? 40.814 -51.627 17.872 1.00 47.82 ? 249 SER A CA 1 ATOM 1907 C C . SER A 1 249 ? 41.741 -52.339 16.909 1.00 47.72 ? 249 SER A C 1 ATOM 1908 O O . SER A 1 249 ? 42.959 -52.265 17.049 1.00 49.12 ? 249 SER A O 1 ATOM 1909 C CB . SER A 1 249 ? 40.635 -50.180 17.436 1.00 46.24 ? 249 SER A CB 1 ATOM 1910 O OG . SER A 1 249 ? 39.799 -49.512 18.350 1.00 46.17 ? 249 SER A OG 1 ATOM 1911 N N . PHE A 1 250 ? 41.154 -53.031 15.938 1.00 46.60 ? 250 PHE A N 1 ATOM 1912 C CA . PHE A 1 250 ? 41.913 -53.666 14.864 1.00 46.98 ? 250 PHE A CA 1 ATOM 1913 C C . PHE A 1 250 ? 41.390 -53.177 13.527 1.00 45.73 ? 250 PHE A C 1 ATOM 1914 O O . PHE A 1 250 ? 40.191 -52.932 13.376 1.00 44.73 ? 250 PHE A O 1 ATOM 1915 C CB . PHE A 1 250 ? 41.803 -55.180 14.954 1.00 47.89 ? 250 PHE A CB 1 ATOM 1916 C CG . PHE A 1 250 ? 42.539 -55.761 16.120 1.00 49.88 ? 250 PHE A CG 1 ATOM 1917 C CD1 . PHE A 1 250 ? 41.972 -55.749 17.386 1.00 50.21 ? 250 PHE A CD1 1 ATOM 1918 C CD2 . PHE A 1 250 ? 43.808 -56.303 15.957 1.00 51.51 ? 250 PHE A CD2 1 ATOM 1919 C CE1 . PHE A 1 250 ? 42.657 -56.267 18.471 1.00 52.58 ? 250 PHE A CE1 1 ATOM 1920 C CE2 . PHE A 1 250 ? 44.496 -56.824 17.039 1.00 53.79 ? 250 PHE A CE2 1 ATOM 1921 C CZ . PHE A 1 250 ? 43.920 -56.805 18.298 1.00 54.20 ? 250 PHE A CZ 1 ATOM 1922 N N . LEU A 1 251 ? 42.293 -53.020 12.565 1.00 46.20 ? 251 LEU A N 1 ATOM 1923 C CA . LEU A 1 251 ? 41.935 -52.467 11.263 1.00 45.26 ? 251 LEU A CA 1 ATOM 1924 C C . LEU A 1 251 ? 41.430 -53.570 10.339 1.00 45.65 ? 251 LEU A C 1 ATOM 1925 O O . LEU A 1 251 ? 42.055 -54.628 10.224 1.00 47.30 ? 251 LEU A O 1 ATOM 1926 C CB . LEU A 1 251 ? 43.130 -51.752 10.631 1.00 45.56 ? 251 LEU A CB 1 ATOM 1927 C CG . LEU A 1 251 ? 43.891 -50.754 11.515 1.00 46.16 ? 251 LEU A CG 1 ATOM 1928 C CD1 . LEU A 1 251 ? 44.856 -49.930 10.671 1.00 46.20 ? 251 LEU A CD1 1 ATOM 1929 C CD2 . LEU A 1 251 ? 42.941 -49.849 12.283 1.00 45.07 ? 251 LEU A CD2 1 ATOM 1930 N N . ARG A 1 252 ? 40.311 -53.300 9.671 1.00 44.46 ? 252 ARG A N 1 ATOM 1931 C CA . ARG A 1 252 ? 39.602 -54.300 8.878 1.00 44.50 ? 252 ARG A CA 1 ATOM 1932 C C . ARG A 1 252 ? 40.235 -54.597 7.534 1.00 45.43 ? 252 ARG A C 1 ATOM 1933 O O . ARG A 1 252 ? 40.173 -55.736 7.067 1.00 46.13 ? 252 ARG A O 1 ATOM 1934 C CB . ARG A 1 252 ? 38.156 -53.854 8.637 1.00 43.35 ? 252 ARG A CB 1 ATOM 1935 C CG . ARG A 1 252 ? 37.280 -53.927 9.869 1.00 43.43 ? 252 ARG A CG 1 ATOM 1936 C CD . ARG A 1 252 ? 35.866 -53.467 9.569 1.00 42.92 ? 252 ARG A CD 1 ATOM 1937 N NE . ARG A 1 252 ? 35.043 -53.461 10.778 1.00 42.99 ? 252 ARG A NE 1 ATOM 1938 C CZ . ARG A 1 252 ? 34.469 -54.539 11.309 1.00 43.80 ? 252 ARG A CZ 1 ATOM 1939 N NH1 . ARG A 1 252 ? 34.610 -55.740 10.743 1.00 44.38 ? 252 ARG A NH1 1 ATOM 1940 N NH2 . ARG A 1 252 ? 33.750 -54.417 12.416 1.00 44.05 ? 252 ARG A NH2 1 ATOM 1941 N N . GLY A 1 253 ? 40.813 -53.583 6.892 1.00 45.51 ? 253 GLY A N 1 ATOM 1942 C CA . GLY A 1 253 ? 41.311 -53.745 5.525 1.00 46.40 ? 253 GLY A CA 1 ATOM 1943 C C . GLY A 1 253 ? 41.761 -52.458 4.851 1.00 46.74 ? 253 GLY A C 1 ATOM 1944 O O . GLY A 1 253 ? 42.751 -51.855 5.263 1.00 47.46 ? 253 GLY A O 1 ATOM 1945 N N . LYS A 1 254 ? 41.041 -52.049 3.808 1.00 46.42 ? 254 LYS A N 1 ATOM 1946 C CA . LYS A 1 254 ? 41.391 -50.856 3.034 1.00 47.13 ? 254 LYS A CA 1 ATOM 1947 C C . LYS A 1 254 ? 40.192 -49.924 2.844 1.00 43.74 ? 254 LYS A C 1 ATOM 1948 O O . LYS A 1 254 ? 39.072 -50.384 2.667 1.00 41.74 ? 254 LYS A O 1 ATOM 1949 C CB . LYS A 1 254 ? 41.929 -51.258 1.661 1.00 50.43 ? 254 LYS A CB 1 ATOM 1950 C CG . LYS A 1 254 ? 43.317 -51.884 1.683 1.00 55.03 ? 254 LYS A CG 1 ATOM 1951 C CD . LYS A 1 254 ? 43.643 -52.542 0.342 1.00 57.94 ? 254 LYS A CD 1 ATOM 1952 C CE . LYS A 1 254 ? 45.021 -53.188 0.335 1.00 61.78 ? 254 LYS A CE 1 ATOM 1953 N NZ . LYS A 1 254 ? 46.125 -52.183 0.325 1.00 64.19 ? 254 LYS A NZ 1 ATOM 1954 N N . SER A 1 255 ? 40.453 -48.619 2.886 1.00 41.61 ? 255 SER A N 1 ATOM 1955 C CA . SER A 1 255 ? 39.473 -47.599 2.533 1.00 40.38 ? 255 SER A CA 1 ATOM 1956 C C . SER A 1 255 ? 40.177 -46.332 2.055 1.00 41.53 ? 255 SER A C 1 ATOM 1957 O O . SER A 1 255 ? 41.399 -46.290 1.974 1.00 41.78 ? 255 SER A O 1 ATOM 1958 C CB . SER A 1 255 ? 38.578 -47.264 3.726 1.00 38.97 ? 255 SER A CB 1 ATOM 1959 O OG . SER A 1 255 ? 39.330 -46.930 4.879 1.00 38.67 ? 255 SER A OG 1 ATOM 1960 N N . MET A 1 256 ? 39.393 -45.316 1.713 1.00 42.35 ? 256 MET A N 1 ATOM 1961 C CA . MET A 1 256 ? 39.906 -43.974 1.529 1.00 44.87 ? 256 MET A CA 1 ATOM 1962 C C . MET A 1 256 ? 39.041 -43.030 2.331 1.00 42.89 ? 256 MET A C 1 ATOM 1963 O O . MET A 1 256 ? 37.835 -43.252 2.459 1.00 41.65 ? 256 MET A O 1 ATOM 1964 C CB . MET A 1 256 ? 39.850 -43.555 0.069 1.00 49.33 ? 256 MET A CB 1 ATOM 1965 C CG . MET A 1 256 ? 41.108 -42.812 -0.376 1.00 54.35 ? 256 MET A CG 1 ATOM 1966 S SD . MET A 1 256 ? 40.887 -41.568 -1.666 1.00 60.65 ? 256 MET A SD 1 ATOM 1967 C CE . MET A 1 256 ? 39.323 -42.042 -2.414 1.00 56.99 ? 256 MET A CE 1 ATOM 1968 N N . GLY A 1 257 ? 39.652 -41.976 2.856 1.00 41.79 ? 257 GLY A N 1 ATOM 1969 C CA . GLY A 1 257 ? 38.926 -40.977 3.631 1.00 40.67 ? 257 GLY A CA 1 ATOM 1970 C C . GLY A 1 257 ? 38.946 -39.612 2.972 1.00 40.27 ? 257 GLY A C 1 ATOM 1971 O O . GLY A 1 257 ? 39.973 -39.198 2.432 1.00 41.04 ? 257 GLY A O 1 ATOM 1972 N N . ILE A 1 258 ? 37.810 -38.917 3.018 1.00 38.77 ? 258 ILE A N 1 ATOM 1973 C CA . ILE A 1 258 ? 37.712 -37.548 2.519 1.00 38.94 ? 258 ILE A CA 1 ATOM 1974 C C . ILE A 1 258 ? 37.063 -36.600 3.529 1.00 38.80 ? 258 ILE A C 1 ATOM 1975 O O . ILE A 1 258 ? 36.402 -37.032 4.475 1.00 38.30 ? 258 ILE A O 1 ATOM 1976 C CB . ILE A 1 258 ? 36.909 -37.483 1.209 1.00 39.36 ? 258 ILE A CB 1 ATOM 1977 C CG1 . ILE A 1 258 ? 35.460 -37.933 1.426 1.00 38.29 ? 258 ILE A CG1 1 ATOM 1978 C CG2 . ILE A 1 258 ? 37.578 -38.342 0.142 1.00 40.00 ? 258 ILE A CG2 1 ATOM 1979 C CD1 . ILE A 1 258 ? 34.544 -37.542 0.291 1.00 38.93 ? 258 ILE A CD1 1 ATOM 1980 N N . GLN A 1 259 ? 37.271 -35.305 3.309 1.00 39.35 ? 259 GLN A N 1 ATOM 1981 C CA . GLN A 1 259 ? 36.583 -34.249 4.039 1.00 39.34 ? 259 GLN A CA 1 ATOM 1982 C C . GLN A 1 259 ? 35.661 -33.536 3.056 1.00 40.35 ? 259 GLN A C 1 ATOM 1983 O O . GLN A 1 259 ? 36.062 -33.242 1.931 1.00 41.97 ? 259 GLN A O 1 ATOM 1984 C CB . GLN A 1 259 ? 37.606 -33.271 4.627 1.00 39.57 ? 259 GLN A CB 1 ATOM 1985 C CG . GLN A 1 259 ? 38.629 -33.950 5.532 1.00 38.82 ? 259 GLN A CG 1 ATOM 1986 C CD . GLN A 1 259 ? 39.569 -32.977 6.208 1.00 39.18 ? 259 GLN A CD 1 ATOM 1987 O OE1 . GLN A 1 259 ? 40.323 -32.262 5.548 1.00 39.56 ? 259 GLN A OE1 1 ATOM 1988 N NE2 . GLN A 1 259 ? 39.542 -32.957 7.534 1.00 38.82 ? 259 GLN A NE2 1 ATOM 1989 N N . SER A 1 260 ? 34.429 -33.258 3.465 1.00 40.59 ? 260 SER A N 1 ATOM 1990 C CA . SER A 1 260 ? 33.441 -32.700 2.540 1.00 41.99 ? 260 SER A CA 1 ATOM 1991 C C . SER A 1 260 ? 32.271 -32.031 3.231 1.00 41.98 ? 260 SER A C 1 ATOM 1992 O O . SER A 1 260 ? 31.879 -32.424 4.333 1.00 41.27 ? 260 SER A O 1 ATOM 1993 C CB . SER A 1 260 ? 32.886 -33.803 1.637 1.00 42.17 ? 260 SER A CB 1 ATOM 1994 O OG . SER A 1 260 ? 31.984 -33.274 0.679 1.00 43.39 ? 260 SER A OG 1 ATOM 1995 N N . GLY A 1 261 ? 31.701 -31.039 2.552 1.00 43.27 ? 261 GLY A N 1 ATOM 1996 C CA . GLY A 1 261 ? 30.479 -30.381 3.012 1.00 44.22 ? 261 GLY A CA 1 ATOM 1997 C C . GLY A 1 261 ? 29.283 -30.565 2.088 1.00 44.82 ? 261 GLY A C 1 ATOM 1998 O O . GLY A 1 261 ? 28.322 -29.802 2.180 1.00 46.58 ? 261 GLY A O 1 ATOM 1999 N N . VAL A 1 262 ? 29.326 -31.570 1.210 1.00 44.12 ? 262 VAL A N 1 ATOM 2000 C CA . VAL A 1 262 ? 28.226 -31.825 0.273 1.00 44.71 ? 262 VAL A CA 1 ATOM 2001 C C . VAL A 1 262 ? 27.621 -33.218 0.458 1.00 43.99 ? 262 VAL A C 1 ATOM 2002 O O . VAL A 1 262 ? 28.225 -34.107 1.069 1.00 41.87 ? 262 VAL A O 1 ATOM 2003 C CB . VAL A 1 262 ? 28.636 -31.591 -1.202 1.00 45.65 ? 262 VAL A CB 1 ATOM 2004 C CG1 . VAL A 1 262 ? 29.031 -30.135 -1.406 1.00 47.11 ? 262 VAL A CG1 1 ATOM 2005 C CG2 . VAL A 1 262 ? 29.771 -32.511 -1.633 1.00 44.78 ? 262 VAL A CG2 1 ATOM 2006 N N . GLN A 1 263 ? 26.420 -33.387 -0.080 1.00 45.17 ? 263 GLN A N 1 ATOM 2007 C CA . GLN A 1 263 ? 25.625 -34.579 0.164 1.00 45.45 ? 263 GLN A CA 1 ATOM 2008 C C . GLN A 1 263 ? 26.176 -35.785 -0.570 1.00 44.02 ? 263 GLN A C 1 ATOM 2009 O O . GLN A 1 263 ? 26.831 -35.663 -1.603 1.00 44.41 ? 263 GLN A O 1 ATOM 2010 C CB . GLN A 1 263 ? 24.172 -34.369 -0.273 1.00 47.77 ? 263 GLN A CB 1 ATOM 2011 C CG . GLN A 1 263 ? 23.465 -33.225 0.437 1.00 51.27 ? 263 GLN A CG 1 ATOM 2012 C CD . GLN A 1 263 ? 22.563 -32.430 -0.498 1.00 55.42 ? 263 GLN A CD 1 ATOM 2013 O OE1 . GLN A 1 263 ? 21.788 -33.003 -1.272 1.00 57.49 ? 263 GLN A OE1 1 ATOM 2014 N NE2 . GLN A 1 263 ? 22.664 -31.105 -0.436 1.00 57.39 ? 263 GLN A NE2 1 ATOM 2015 N N . VAL A 1 264 ? 25.869 -36.948 -0.020 1.00 42.78 ? 264 VAL A N 1 ATOM 2016 C CA . VAL A 1 264 ? 26.171 -38.232 -0.629 1.00 42.54 ? 264 VAL A CA 1 ATOM 2017 C C . VAL A 1 264 ? 25.155 -38.508 -1.731 1.00 42.85 ? 264 VAL A C 1 ATOM 2018 O O . VAL A 1 264 ? 24.004 -38.081 -1.645 1.00 43.97 ? 264 VAL A O 1 ATOM 2019 C CB . VAL A 1 264 ? 26.136 -39.343 0.444 1.00 41.71 ? 264 VAL A CB 1 ATOM 2020 C CG1 . VAL A 1 264 ? 26.212 -40.735 -0.170 1.00 42.08 ? 264 VAL A CG1 1 ATOM 2021 C CG2 . VAL A 1 264 ? 27.282 -39.133 1.426 1.00 41.10 ? 264 VAL A CG2 1 ATOM 2022 N N . ASP A 1 265 ? 25.596 -39.208 -2.772 1.00 42.17 ? 265 ASP A N 1 ATOM 2023 C CA . ASP A 1 265 ? 24.734 -39.564 -3.898 1.00 41.86 ? 265 ASP A CA 1 ATOM 2024 C C . ASP A 1 265 ? 25.127 -40.943 -4.423 1.00 39.95 ? 265 ASP A C 1 ATOM 2025 O O . ASP A 1 265 ? 26.255 -41.135 -4.862 1.00 39.66 ? 265 ASP A O 1 ATOM 2026 C CB . ASP A 1 265 ? 24.867 -38.504 -4.997 1.00 43.41 ? 265 ASP A CB 1 ATOM 2027 C CG . ASP A 1 265 ? 23.869 -38.699 -6.135 1.00 45.06 ? 265 ASP A CG 1 ATOM 2028 O OD1 . ASP A 1 265 ? 23.199 -39.748 -6.164 1.00 44.48 ? 265 ASP A OD1 1 ATOM 2029 O OD2 . ASP A 1 265 ? 23.756 -37.800 -7.005 1.00 46.18 ? 265 ASP A OD2 1 ATOM 2030 N N . ALA A 1 266 ? 24.193 -41.897 -4.365 1.00 38.60 ? 266 ALA A N 1 ATOM 2031 C CA . ALA A 1 266 ? 24.451 -43.274 -4.791 1.00 37.64 ? 266 ALA A CA 1 ATOM 2032 C C . ALA A 1 266 ? 24.005 -43.520 -6.230 1.00 38.61 ? 266 ALA A C 1 ATOM 2033 O O . ALA A 1 266 ? 23.982 -44.661 -6.688 1.00 37.95 ? 266 ALA A O 1 ATOM 2034 C CB . ALA A 1 266 ? 23.768 -44.261 -3.850 1.00 36.66 ? 266 ALA A CB 1 ATOM 2035 N N . ASN A 1 267 ? 23.648 -42.446 -6.931 1.00 40.05 ? 267 ASN A N 1 ATOM 2036 C CA . ASN A 1 267 ? 23.239 -42.498 -8.334 1.00 41.10 ? 267 ASN A CA 1 ATOM 2037 C C . ASN A 1 267 ? 24.390 -42.194 -9.294 1.00 42.65 ? 267 ASN A C 1 ATOM 2038 O O . ASN A 1 267 ? 24.309 -42.518 -10.477 1.00 43.30 ? 267 ASN A O 1 ATOM 2039 C CB . ASN A 1 267 ? 22.069 -41.522 -8.567 1.00 42.01 ? 267 ASN A CB 1 ATOM 2040 C CG . ASN A 1 267 ? 21.688 -41.394 -10.027 1.00 43.14 ? 267 ASN A CG 1 ATOM 2041 O OD1 . ASN A 1 267 ? 22.055 -40.425 -10.677 1.00 44.15 ? 267 ASN A OD1 1 ATOM 2042 N ND2 . ASN A 1 267 ? 20.976 -42.378 -10.550 1.00 42.93 ? 267 ASN A ND2 1 ATOM 2043 N N . CYS A 1 268 ? 25.455 -41.569 -8.795 1.00 43.87 ? 268 CYS A N 1 ATOM 2044 C CA . CYS A 1 268 ? 26.631 -41.299 -9.614 1.00 45.85 ? 268 CYS A CA 1 ATOM 2045 C C . CYS A 1 268 ? 27.856 -42.009 -9.051 1.00 45.04 ? 268 CYS A C 1 ATOM 2046 O O . CYS A 1 268 ? 27.956 -42.246 -7.846 1.00 43.59 ? 268 CYS A O 1 ATOM 2047 C CB . CYS A 1 268 ? 26.888 -39.789 -9.764 1.00 48.16 ? 268 CYS A CB 1 ATOM 2048 S SG . CYS A 1 268 ? 27.094 -38.842 -8.238 0.80 48.39 ? 268 CYS A SG 1 ATOM 2049 N N . GLU A 1 269 ? 28.777 -42.362 -9.939 1.00 55.47 ? 269 GLU A N 1 ATOM 2050 C CA . GLU A 1 269 ? 30.009 -43.026 -9.549 1.00 55.05 ? 269 GLU A CA 1 ATOM 2051 C C . GLU A 1 269 ? 31.197 -42.120 -9.820 1.00 51.13 ? 269 GLU A C 1 ATOM 2052 O O . GLU A 1 269 ? 31.254 -41.444 -10.845 1.00 50.83 ? 269 GLU A O 1 ATOM 2053 C CB . GLU A 1 269 ? 30.178 -44.323 -10.325 1.00 59.52 ? 269 GLU A CB 1 ATOM 2054 C CG . GLU A 1 269 ? 31.211 -45.256 -9.715 1.00 61.23 ? 269 GLU A CG 1 ATOM 2055 C CD . GLU A 1 269 ? 31.346 -46.562 -10.471 1.00 66.26 ? 269 GLU A CD 1 ATOM 2056 O OE1 . GLU A 1 269 ? 30.439 -46.893 -11.272 1.00 70.76 ? 269 GLU A OE1 1 ATOM 2057 O OE2 . GLU A 1 269 ? 32.364 -47.261 -10.257 1.00 68.29 ? 269 GLU A OE2 1 ATOM 2058 N N . GLY A 1 270 ? 32.142 -42.093 -8.894 1.00 48.45 ? 270 GLY A N 1 ATOM 2059 C CA . GLY A 1 270 ? 33.380 -41.349 -9.105 1.00 46.36 ? 270 GLY A CA 1 ATOM 2060 C C . GLY A 1 270 ? 34.474 -41.882 -8.215 1.00 44.48 ? 270 GLY A C 1 ATOM 2061 O O . GLY A 1 270 ? 34.192 -42.551 -7.230 1.00 44.82 ? 270 GLY A O 1 ATOM 2062 N N . ASP A 1 271 ? 35.718 -41.592 -8.581 1.00 42.96 ? 271 ASP A N 1 ATOM 2063 C CA . ASP A 1 271 ? 36.886 -41.988 -7.797 1.00 41.90 ? 271 ASP A CA 1 ATOM 2064 C C . ASP A 1 271 ? 37.783 -40.811 -7.428 1.00 38.82 ? 271 ASP A C 1 ATOM 2065 O O . ASP A 1 271 ? 38.799 -41.008 -6.775 1.00 37.72 ? 271 ASP A O 1 ATOM 2066 C CB . ASP A 1 271 ? 37.718 -43.016 -8.563 1.00 43.35 ? 271 ASP A CB 1 ATOM 2067 C CG . ASP A 1 271 ? 37.049 -44.357 -8.660 1.00 46.43 ? 271 ASP A CG 1 ATOM 2068 O OD1 . ASP A 1 271 ? 36.362 -44.778 -7.701 1.00 48.52 ? 271 ASP A OD1 1 ATOM 2069 O OD2 . ASP A 1 271 ? 37.229 -45.013 -9.703 1.00 49.39 ? 271 ASP A OD2 1 ATOM 2070 N N . CYS A 1 272 ? 37.398 -39.601 -7.819 1.00 37.73 ? 272 CYS A N 1 ATOM 2071 C CA . CYS A 1 272 ? 38.169 -38.406 -7.520 1.00 36.64 ? 272 CYS A CA 1 ATOM 2072 C C . CYS A 1 272 ? 37.285 -37.436 -6.754 1.00 36.27 ? 272 CYS A C 1 ATOM 2073 O O . CYS A 1 272 ? 36.260 -36.986 -7.275 1.00 37.26 ? 272 CYS A O 1 ATOM 2074 C CB . CYS A 1 272 ? 38.679 -37.744 -8.803 1.00 36.29 ? 272 CYS A CB 1 ATOM 2075 S SG . CYS A 1 272 ? 39.704 -36.293 -8.492 1.00 35.84 ? 272 CYS A SG 1 ATOM 2076 N N . TYR A 1 273 ? 37.698 -37.114 -5.530 1.00 35.10 ? 273 TYR A N 1 ATOM 2077 C CA . TYR A 1 273 ? 36.865 -36.392 -4.585 1.00 35.27 ? 273 TYR A CA 1 ATOM 2078 C C . TYR A 1 273 ? 37.609 -35.170 -4.045 1.00 34.85 ? 273 TYR A C 1 ATOM 2079 O O . TYR A 1 273 ? 38.830 -35.188 -3.923 1.00 34.39 ? 273 TYR A O 1 ATOM 2080 C CB . TYR A 1 273 ? 36.510 -37.293 -3.407 1.00 35.68 ? 273 TYR A CB 1 ATOM 2081 C CG . TYR A 1 273 ? 35.720 -38.549 -3.720 1.00 36.24 ? 273 TYR A CG 1 ATOM 2082 C CD1 . TYR A 1 273 ? 34.413 -38.474 -4.182 1.00 37.31 ? 273 TYR A CD1 1 ATOM 2083 C CD2 . TYR A 1 273 ? 36.265 -39.807 -3.509 1.00 36.34 ? 273 TYR A CD2 1 ATOM 2084 C CE1 . TYR A 1 273 ? 33.678 -39.622 -4.439 1.00 38.81 ? 273 TYR A CE1 1 ATOM 2085 C CE2 . TYR A 1 273 ? 35.536 -40.965 -3.757 1.00 37.91 ? 273 TYR A CE2 1 ATOM 2086 C CZ . TYR A 1 273 ? 34.239 -40.864 -4.224 1.00 38.83 ? 273 TYR A CZ 1 ATOM 2087 O OH . TYR A 1 273 ? 33.504 -41.993 -4.487 1.00 40.12 ? 273 TYR A OH 1 ATOM 2088 N N . HIS A 1 274 ? 36.863 -34.110 -3.742 1.00 35.63 ? 274 HIS A N 1 ATOM 2089 C CA . HIS A 1 274 ? 37.385 -32.949 -3.008 1.00 35.82 ? 274 HIS A CA 1 ATOM 2090 C C . HIS A 1 274 ? 36.257 -32.450 -2.084 1.00 37.04 ? 274 HIS A C 1 ATOM 2091 O O . HIS A 1 274 ? 35.171 -33.042 -2.078 1.00 38.32 ? 274 HIS A O 1 ATOM 2092 C CB . HIS A 1 274 ? 37.873 -31.863 -3.972 1.00 35.36 ? 274 HIS A CB 1 ATOM 2093 C CG . HIS A 1 274 ? 36.792 -31.273 -4.820 1.00 36.78 ? 274 HIS A CG 1 ATOM 2094 N ND1 . HIS A 1 274 ? 36.425 -29.948 -4.743 1.00 38.34 ? 274 HIS A ND1 1 ATOM 2095 C CD2 . HIS A 1 274 ? 35.985 -31.830 -5.753 1.00 38.55 ? 274 HIS A CD2 1 ATOM 2096 C CE1 . HIS A 1 274 ? 35.440 -29.712 -5.591 1.00 38.82 ? 274 HIS A CE1 1 ATOM 2097 N NE2 . HIS A 1 274 ? 35.155 -30.839 -6.217 1.00 39.40 ? 274 HIS A NE2 1 ATOM 2098 N N . SER A 1 275 ? 36.481 -31.388 -1.312 1.00 37.00 ? 275 SER A N 1 ATOM 2099 C CA . SER A 1 275 ? 35.447 -30.963 -0.346 1.00 39.15 ? 275 SER A CA 1 ATOM 2100 C C . SER A 1 275 ? 34.181 -30.460 -1.036 1.00 39.64 ? 275 SER A C 1 ATOM 2101 O O . SER A 1 275 ? 33.094 -30.615 -0.511 1.00 42.25 ? 275 SER A O 1 ATOM 2102 C CB . SER A 1 275 ? 35.972 -29.938 0.670 1.00 39.15 ? 275 SER A CB 1 ATOM 2103 O OG . SER A 1 275 ? 36.475 -28.778 0.052 1.00 39.53 ? 275 SER A OG 1 ATOM 2104 N N . GLY A 1 276 ? 34.330 -29.901 -2.230 1.00 39.46 ? 276 GLY A N 1 ATOM 2105 C CA . GLY A 1 276 ? 33.197 -29.429 -3.019 1.00 40.17 ? 276 GLY A CA 1 ATOM 2106 C C . GLY A 1 276 ? 32.456 -30.486 -3.827 1.00 40.67 ? 276 GLY A C 1 ATOM 2107 O O . GLY A 1 276 ? 31.424 -30.182 -4.425 1.00 42.16 ? 276 GLY A O 1 ATOM 2108 N N . GLY A 1 277 ? 32.965 -31.718 -3.865 1.00 39.22 ? 277 GLY A N 1 ATOM 2109 C CA . GLY A 1 277 ? 32.278 -32.793 -4.587 1.00 40.15 ? 277 GLY A CA 1 ATOM 2110 C C . GLY A 1 277 ? 33.156 -33.820 -5.287 1.00 38.97 ? 277 GLY A C 1 ATOM 2111 O O . GLY A 1 277 ? 34.181 -34.255 -4.755 1.00 37.86 ? 277 GLY A O 1 ATOM 2112 N N . THR A 1 278 ? 32.740 -34.205 -6.491 1.00 39.43 ? 278 THR A N 1 ATOM 2113 C CA . THR A 1 278 ? 33.370 -35.288 -7.241 1.00 38.97 ? 278 THR A CA 1 ATOM 2114 C C . THR A 1 278 ? 33.761 -34.823 -8.640 1.00 38.75 ? 278 THR A C 1 ATOM 2115 O O . THR A 1 278 ? 32.976 -34.182 -9.327 1.00 39.20 ? 278 THR A O 1 ATOM 2116 C CB . THR A 1 278 ? 32.402 -36.484 -7.401 1.00 40.58 ? 278 THR A CB 1 ATOM 2117 O OG1 . THR A 1 278 ? 31.824 -36.809 -6.133 1.00 40.95 ? 278 THR A OG1 1 ATOM 2118 C CG2 . THR A 1 278 ? 33.134 -37.708 -7.955 1.00 40.46 ? 278 THR A CG2 1 ATOM 2119 N N . ILE A 1 279 ? 34.969 -35.176 -9.064 1.00 38.34 ? 279 ILE A N 1 ATOM 2120 C CA . ILE A 1 279 ? 35.429 -34.874 -10.415 1.00 38.34 ? 279 ILE A CA 1 ATOM 2121 C C . ILE A 1 279 ? 35.247 -36.130 -11.255 1.00 40.23 ? 279 ILE A C 1 ATOM 2122 O O . ILE A 1 279 ? 35.989 -37.079 -11.093 1.00 40.06 ? 279 ILE A O 1 ATOM 2123 C CB . ILE A 1 279 ? 36.905 -34.445 -10.410 1.00 36.41 ? 279 ILE A CB 1 ATOM 2124 C CG1 . ILE A 1 279 ? 37.082 -33.222 -9.504 1.00 35.53 ? 279 ILE A CG1 1 ATOM 2125 C CG2 . ILE A 1 279 ? 37.385 -34.152 -11.827 1.00 36.45 ? 279 ILE A CG2 1 ATOM 2126 C CD1 . ILE A 1 279 ? 38.515 -32.798 -9.294 1.00 34.30 ? 279 ILE A CD1 1 ATOM 2127 N N . ILE A 1 280 ? 34.231 -36.149 -12.114 1.00 42.94 ? 280 ILE A N 1 ATOM 2128 C CA . ILE A 1 280 ? 34.023 -37.260 -13.044 1.00 45.54 ? 280 ILE A CA 1 ATOM 2129 C C . ILE A 1 280 ? 34.523 -36.819 -14.400 1.00 46.29 ? 280 ILE A C 1 ATOM 2130 O O . ILE A 1 280 ? 33.988 -35.878 -14.977 1.00 47.67 ? 280 ILE A O 1 ATOM 2131 C CB . ILE A 1 280 ? 32.538 -37.647 -13.181 1.00 48.17 ? 280 ILE A CB 1 ATOM 2132 C CG1 . ILE A 1 280 ? 31.992 -38.130 -11.840 1.00 48.36 ? 280 ILE A CG1 1 ATOM 2133 C CG2 . ILE A 1 280 ? 32.364 -38.728 -14.246 1.00 50.18 ? 280 ILE A CG2 1 ATOM 2134 C CD1 . ILE A 1 280 ? 30.537 -38.534 -11.892 1.00 51.44 ? 280 ILE A CD1 1 ATOM 2135 N N . SER A 1 281 ? 35.534 -37.510 -14.913 1.00 46.72 ? 281 SER A N 1 ATOM 2136 C CA . SER A 1 281 ? 36.224 -37.074 -16.119 1.00 46.79 ? 281 SER A CA 1 ATOM 2137 C C . SER A 1 281 ? 37.217 -38.138 -16.570 1.00 47.03 ? 281 SER A C 1 ATOM 2138 O O . SER A 1 281 ? 37.737 -38.893 -15.751 1.00 45.37 ? 281 SER A O 1 ATOM 2139 C CB . SER A 1 281 ? 36.978 -35.766 -15.823 1.00 45.07 ? 281 SER A CB 1 ATOM 2140 O OG . SER A 1 281 ? 37.556 -35.204 -16.985 1.00 44.53 ? 281 SER A OG 1 ATOM 2141 N N . ASN A 1 282 ? 37.475 -38.187 -17.874 1.00 49.30 ? 282 ASN A N 1 ATOM 2142 C CA . ASN A 1 282 ? 38.583 -38.966 -18.417 1.00 50.48 ? 282 ASN A CA 1 ATOM 2143 C C . ASN A 1 282 ? 39.695 -38.073 -18.969 1.00 48.02 ? 282 ASN A C 1 ATOM 2144 O O . ASN A 1 282 ? 40.648 -38.564 -19.571 1.00 46.92 ? 282 ASN A O 1 ATOM 2145 C CB . ASN A 1 282 ? 38.081 -39.897 -19.511 1.00 55.07 ? 282 ASN A CB 1 ATOM 2146 C CG . ASN A 1 282 ? 37.046 -40.877 -19.001 1.00 59.51 ? 282 ASN A CG 1 ATOM 2147 O OD1 . ASN A 1 282 ? 37.280 -41.576 -18.008 1.00 60.93 ? 282 ASN A OD1 1 ATOM 2148 N ND2 . ASN A 1 282 ? 35.891 -40.931 -19.667 1.00 62.44 ? 282 ASN A ND2 1 ATOM 2149 N N . LEU A 1 283 ? 39.586 -36.763 -18.759 1.00 46.07 ? 283 LEU A N 1 ATOM 2150 C CA . LEU A 1 283 ? 40.618 -35.851 -19.242 1.00 44.08 ? 283 LEU A CA 1 ATOM 2151 C C . LEU A 1 283 ? 41.871 -36.011 -18.381 1.00 42.17 ? 283 LEU A C 1 ATOM 2152 O O . LEU A 1 283 ? 41.776 -36.331 -17.201 1.00 42.28 ? 283 LEU A O 1 ATOM 2153 C CB . LEU A 1 283 ? 40.128 -34.409 -19.225 1.00 43.53 ? 283 LEU A CB 1 ATOM 2154 C CG . LEU A 1 283 ? 38.804 -34.115 -19.941 1.00 46.77 ? 283 LEU A CG 1 ATOM 2155 C CD1 . LEU A 1 283 ? 38.616 -32.608 -20.071 1.00 46.67 ? 283 LEU A CD1 1 ATOM 2156 C CD2 . LEU A 1 283 ? 38.731 -34.774 -21.312 1.00 48.38 ? 283 LEU A CD2 1 ATOM 2157 N N . PRO A 1 284 ? 43.058 -35.805 -18.972 1.00 40.88 ? 284 PRO A N 1 ATOM 2158 C CA . PRO A 1 284 ? 44.279 -36.031 -18.205 1.00 39.47 ? 284 PRO A CA 1 ATOM 2159 C C . PRO A 1 284 ? 44.540 -34.976 -17.120 1.00 37.42 ? 284 PRO A C 1 ATOM 2160 O O . PRO A 1 284 ? 45.309 -35.233 -16.196 1.00 36.95 ? 284 PRO A O 1 ATOM 2161 C CB . PRO A 1 284 ? 45.369 -35.985 -19.274 1.00 39.63 ? 284 PRO A CB 1 ATOM 2162 C CG . PRO A 1 284 ? 44.808 -35.101 -20.332 1.00 40.13 ? 284 PRO A CG 1 ATOM 2163 C CD . PRO A 1 284 ? 43.339 -35.383 -20.354 1.00 40.66 ? 284 PRO A CD 1 ATOM 2164 N N . PHE A 1 285 ? 43.905 -33.809 -17.224 1.00 35.89 ? 285 PHE A N 1 ATOM 2165 C CA . PHE A 1 285 ? 44.173 -32.705 -16.297 1.00 34.64 ? 285 PHE A CA 1 ATOM 2166 C C . PHE A 1 285 ? 42.896 -32.121 -15.697 1.00 34.79 ? 285 PHE A C 1 ATOM 2167 O O . PHE A 1 285 ? 41.806 -32.279 -16.260 1.00 35.80 ? 285 PHE A O 1 ATOM 2168 C CB . PHE A 1 285 ? 44.960 -31.588 -17.001 1.00 33.72 ? 285 PHE A CB 1 ATOM 2169 C CG . PHE A 1 285 ? 46.133 -32.080 -17.813 1.00 33.53 ? 285 PHE A CG 1 ATOM 2170 C CD1 . PHE A 1 285 ? 47.176 -32.767 -17.210 1.00 33.06 ? 285 PHE A CD1 1 ATOM 2171 C CD2 . PHE A 1 285 ? 46.186 -31.859 -19.188 1.00 34.07 ? 285 PHE A CD2 1 ATOM 2172 C CE1 . PHE A 1 285 ? 48.254 -33.223 -17.955 1.00 33.18 ? 285 PHE A CE1 1 ATOM 2173 C CE2 . PHE A 1 285 ? 47.260 -32.308 -19.939 1.00 33.96 ? 285 PHE A CE2 1 ATOM 2174 C CZ . PHE A 1 285 ? 48.293 -33.000 -19.322 1.00 33.92 ? 285 PHE A CZ 1 ATOM 2175 N N . GLN A 1 286 ? 43.042 -31.425 -14.567 1.00 34.05 ? 286 GLN A N 1 ATOM 2176 C CA . GLN A 1 286 ? 41.921 -30.704 -13.939 1.00 34.48 ? 286 GLN A CA 1 ATOM 2177 C C . GLN A 1 286 ? 42.357 -29.396 -13.275 1.00 34.07 ? 286 GLN A C 1 ATOM 2178 O O . GLN A 1 286 ? 43.473 -29.295 -12.753 1.00 34.63 ? 286 GLN A O 1 ATOM 2179 C CB . GLN A 1 286 ? 41.215 -31.603 -12.925 1.00 34.89 ? 286 GLN A CB 1 ATOM 2180 C CG . GLN A 1 286 ? 42.089 -32.076 -11.769 1.00 34.74 ? 286 GLN A CG 1 ATOM 2181 C CD . GLN A 1 286 ? 41.904 -31.292 -10.478 1.00 34.69 ? 286 GLN A CD 1 ATOM 2182 O OE1 . GLN A 1 286 ? 41.188 -30.292 -10.430 1.00 35.33 ? 286 GLN A OE1 1 ATOM 2183 N NE2 . GLN A 1 286 ? 42.569 -31.747 -9.418 1.00 34.62 ? 286 GLN A NE2 1 ATOM 2184 N N . ASN A 1 287 ? 41.478 -28.395 -13.310 1.00 34.51 ? 287 ASN A N 1 ATOM 2185 C CA . ASN A 1 287 ? 41.737 -27.092 -12.696 1.00 35.55 ? 287 ASN A CA 1 ATOM 2186 C C . ASN A 1 287 ? 40.695 -26.781 -11.606 1.00 37.14 ? 287 ASN A C 1 ATOM 2187 O O . ASN A 1 287 ? 40.377 -25.618 -11.347 1.00 38.01 ? 287 ASN A O 1 ATOM 2188 C CB . ASN A 1 287 ? 41.738 -26.010 -13.787 1.00 36.31 ? 287 ASN A CB 1 ATOM 2189 C CG . ASN A 1 287 ? 42.028 -24.612 -13.252 1.00 37.48 ? 287 ASN A CG 1 ATOM 2190 O OD1 . ASN A 1 287 ? 41.243 -23.690 -13.460 1.00 39.24 ? 287 ASN A OD1 1 ATOM 2191 N ND2 . ASN A 1 287 ? 43.160 -24.445 -12.573 1.00 37.36 ? 287 ASN A ND2 1 ATOM 2192 N N . ILE A 1 288 ? 40.179 -27.823 -10.955 1.00 37.42 ? 288 ILE A N 1 ATOM 2193 C CA . ILE A 1 288 ? 39.142 -27.654 -9.932 1.00 38.33 ? 288 ILE A CA 1 ATOM 2194 C C . ILE A 1 288 ? 39.720 -27.522 -8.516 1.00 37.61 ? 288 ILE A C 1 ATOM 2195 O O . ILE A 1 288 ? 39.333 -26.635 -7.777 1.00 38.33 ? 288 ILE A O 1 ATOM 2196 C CB . ILE A 1 288 ? 38.102 -28.795 -9.994 1.00 38.76 ? 288 ILE A CB 1 ATOM 2197 C CG1 . ILE A 1 288 ? 37.320 -28.714 -11.313 1.00 40.10 ? 288 ILE A CG1 1 ATOM 2198 C CG2 . ILE A 1 288 ? 37.113 -28.687 -8.843 1.00 39.73 ? 288 ILE A CG2 1 ATOM 2199 C CD1 . ILE A 1 288 ? 36.620 -29.997 -11.703 1.00 40.75 ? 288 ILE A CD1 1 ATOM 2200 N N . ASP A 1 289 ? 40.639 -28.402 -8.135 1.00 37.56 ? 289 ASP A N 1 ATOM 2201 C CA . ASP A 1 289 ? 41.140 -28.432 -6.754 1.00 36.67 ? 289 ASP A CA 1 ATOM 2202 C C . ASP A 1 289 ? 42.439 -29.207 -6.675 1.00 34.87 ? 289 ASP A C 1 ATOM 2203 O O . ASP A 1 289 ? 42.469 -30.419 -6.913 1.00 34.80 ? 289 ASP A O 1 ATOM 2204 C CB . ASP A 1 289 ? 40.096 -29.092 -5.836 1.00 37.59 ? 289 ASP A CB 1 ATOM 2205 C CG . ASP A 1 289 ? 40.369 -28.862 -4.341 1.00 38.06 ? 289 ASP A CG 1 ATOM 2206 O OD1 . ASP A 1 289 ? 41.516 -28.592 -3.933 1.00 36.02 ? 289 ASP A OD1 1 ATOM 2207 O OD2 . ASP A 1 289 ? 39.394 -28.959 -3.567 1.00 40.84 ? 289 ASP A OD2 1 ATOM 2208 N N . SER A 1 290 ? 43.501 -28.513 -6.299 1.00 34.41 ? 290 SER A N 1 ATOM 2209 C CA . SER A 1 290 ? 44.825 -29.116 -6.194 1.00 34.16 ? 290 SER A CA 1 ATOM 2210 C C . SER A 1 290 ? 44.954 -30.145 -5.063 1.00 33.66 ? 290 SER A C 1 ATOM 2211 O O . SER A 1 290 ? 45.931 -30.867 -5.026 1.00 33.99 ? 290 SER A O 1 ATOM 2212 C CB . SER A 1 290 ? 45.872 -28.029 -5.991 1.00 34.86 ? 290 SER A CB 1 ATOM 2213 O OG . SER A 1 290 ? 45.736 -27.446 -4.705 1.00 36.09 ? 290 SER A OG 1 ATOM 2214 N N . ARG A 1 291 ? 43.994 -30.193 -4.143 1.00 33.50 ? 291 ARG A N 1 ATOM 2215 C CA . ARG A 1 291 ? 44.032 -31.134 -3.018 1.00 33.75 ? 291 ARG A CA 1 ATOM 2216 C C . ARG A 1 291 ? 43.030 -32.287 -3.196 1.00 33.90 ? 291 ARG A C 1 ATOM 2217 O O . ARG A 1 291 ? 42.778 -33.051 -2.260 1.00 35.31 ? 291 ARG A O 1 ATOM 2218 C CB . ARG A 1 291 ? 43.771 -30.398 -1.692 1.00 33.82 ? 291 ARG A CB 1 ATOM 2219 C CG . ARG A 1 291 ? 44.875 -29.414 -1.299 1.00 34.31 ? 291 ARG A CG 1 ATOM 2220 C CD . ARG A 1 291 ? 44.626 -28.705 0.034 1.00 35.02 ? 291 ARG A CD 1 ATOM 2221 N NE . ARG A 1 291 ? 44.428 -29.628 1.154 1.00 35.06 ? 291 ARG A NE 1 ATOM 2222 C CZ . ARG A 1 291 ? 43.242 -30.020 1.621 1.00 35.06 ? 291 ARG A CZ 1 ATOM 2223 N NH1 . ARG A 1 291 ? 42.111 -29.581 1.080 1.00 35.00 ? 291 ARG A NH1 1 ATOM 2224 N NH2 . ARG A 1 291 ? 43.183 -30.861 2.638 1.00 35.37 ? 291 ARG A NH2 1 ATOM 2225 N N . ALA A 1 292 ? 42.467 -32.418 -4.393 1.00 33.34 ? 292 ALA A N 1 ATOM 2226 C CA . ALA A 1 292 ? 41.591 -33.547 -4.718 1.00 33.58 ? 292 ALA A CA 1 ATOM 2227 C C . ALA A 1 292 ? 42.305 -34.860 -4.465 1.00 33.39 ? 292 ALA A C 1 ATOM 2228 O O . ALA A 1 292 ? 43.500 -34.963 -4.700 1.00 32.81 ? 292 ALA A O 1 ATOM 2229 C CB . ALA A 1 292 ? 41.159 -33.475 -6.174 1.00 34.28 ? 292 ALA A CB 1 ATOM 2230 N N . VAL A 1 293 ? 41.566 -35.864 -4.004 1.00 33.33 ? 293 VAL A N 1 ATOM 2231 C CA . VAL A 1 293 ? 42.147 -37.158 -3.711 1.00 33.76 ? 293 VAL A CA 1 ATOM 2232 C C . VAL A 1 293 ? 41.381 -38.285 -4.368 1.00 34.22 ? 293 VAL A C 1 ATOM 2233 O O . VAL A 1 293 ? 40.278 -38.085 -4.872 1.00 34.04 ? 293 VAL A O 1 ATOM 2234 C CB . VAL A 1 293 ? 42.246 -37.404 -2.186 1.00 34.83 ? 293 VAL A CB 1 ATOM 2235 C CG1 . VAL A 1 293 ? 43.340 -36.521 -1.595 1.00 34.83 ? 293 VAL A CG1 1 ATOM 2236 C CG2 . VAL A 1 293 ? 40.912 -37.152 -1.506 1.00 35.14 ? 293 VAL A CG2 1 ATOM 2237 N N . GLY A 1 294 ? 41.989 -39.468 -4.340 1.00 35.11 ? 294 GLY A N 1 ATOM 2238 C CA . GLY A 1 294 ? 41.480 -40.654 -5.015 1.00 36.94 ? 294 GLY A CA 1 ATOM 2239 C C . GLY A 1 294 ? 42.282 -40.856 -6.287 1.00 37.25 ? 294 GLY A C 1 ATOM 2240 O O . GLY A 1 294 ? 43.491 -40.610 -6.301 1.00 36.78 ? 294 GLY A O 1 ATOM 2241 N N . LYS A 1 295 ? 41.614 -41.281 -7.354 1.00 38.03 ? 295 LYS A N 1 ATOM 2242 C CA . LYS A 1 295 ? 42.250 -41.441 -8.663 1.00 38.77 ? 295 LYS A CA 1 ATOM 2243 C C . LYS A 1 295 ? 41.788 -40.310 -9.550 1.00 38.01 ? 295 LYS A C 1 ATOM 2244 O O . LYS A 1 295 ? 40.650 -40.296 -10.010 1.00 40.48 ? 295 LYS A O 1 ATOM 2245 C CB . LYS A 1 295 ? 41.880 -42.794 -9.263 1.00 41.37 ? 295 LYS A CB 1 ATOM 2246 C CG . LYS A 1 295 ? 42.385 -43.952 -8.423 1.00 42.41 ? 295 LYS A CG 1 ATOM 2247 C CD . LYS A 1 295 ? 41.811 -45.284 -8.863 1.00 45.70 ? 295 LYS A CD 1 ATOM 2248 C CE . LYS A 1 295 ? 42.239 -46.370 -7.901 1.00 47.32 ? 295 LYS A CE 1 ATOM 2249 N NZ . LYS A 1 295 ? 41.808 -47.704 -8.369 1.00 52.23 ? 295 LYS A NZ 1 ATOM 2250 N N . CYS A 1 296 ? 42.675 -39.350 -9.774 1.00 36.79 ? 296 CYS A N 1 ATOM 2251 C CA . CYS A 1 296 ? 42.311 -38.060 -10.321 1.00 35.93 ? 296 CYS A CA 1 ATOM 2252 C C . CYS A 1 296 ? 43.158 -37.683 -11.535 1.00 35.60 ? 296 CYS A C 1 ATOM 2253 O O . CYS A 1 296 ? 44.290 -38.118 -11.653 1.00 33.57 ? 296 CYS A O 1 ATOM 2254 C CB . CYS A 1 296 ? 42.543 -36.986 -9.246 1.00 35.30 ? 296 CYS A CB 1 ATOM 2255 S SG . CYS A 1 296 ? 41.471 -37.114 -7.803 0.80 35.61 ? 296 CYS A SG 1 ATOM 2256 N N . PRO A 1 297 ? 42.606 -36.833 -12.423 1.00 35.85 ? 297 PRO A N 1 ATOM 2257 C CA . PRO A 1 297 ? 43.446 -36.112 -13.364 1.00 35.59 ? 297 PRO A CA 1 ATOM 2258 C C . PRO A 1 297 ? 44.463 -35.252 -12.603 1.00 35.40 ? 297 PRO A C 1 ATOM 2259 O O . PRO A 1 297 ? 44.222 -34.894 -11.449 1.00 36.25 ? 297 PRO A O 1 ATOM 2260 C CB . PRO A 1 297 ? 42.460 -35.212 -14.117 1.00 35.76 ? 297 PRO A CB 1 ATOM 2261 C CG . PRO A 1 297 ? 41.101 -35.769 -13.856 1.00 36.70 ? 297 PRO A CG 1 ATOM 2262 C CD . PRO A 1 297 ? 41.185 -36.452 -12.525 1.00 36.49 ? 297 PRO A CD 1 ATOM 2263 N N . ARG A 1 298 ? 45.585 -34.935 -13.236 1.00 34.81 ? 298 ARG A N 1 ATOM 2264 C CA . ARG A 1 298 ? 46.609 -34.106 -12.604 1.00 35.11 ? 298 ARG A CA 1 ATOM 2265 C C . ARG A 1 298 ? 46.119 -32.670 -12.548 1.00 33.14 ? 298 ARG A C 1 ATOM 2266 O O . ARG A 1 298 ? 45.581 -32.162 -13.531 1.00 31.71 ? 298 ARG A O 1 ATOM 2267 C CB . ARG A 1 298 ? 47.928 -34.143 -13.391 1.00 37.04 ? 298 ARG A CB 1 ATOM 2268 C CG . ARG A 1 298 ? 48.859 -35.306 -13.083 1.00 40.21 ? 298 ARG A CG 1 ATOM 2269 C CD . ARG A 1 298 ? 48.275 -36.659 -13.395 1.00 43.38 ? 298 ARG A CD 1 ATOM 2270 N NE . ARG A 1 298 ? 47.788 -36.779 -14.773 1.00 46.09 ? 298 ARG A NE 1 ATOM 2271 C CZ . ARG A 1 298 ? 46.863 -37.659 -15.169 1.00 47.42 ? 298 ARG A CZ 1 ATOM 2272 N NH1 . ARG A 1 298 ? 46.300 -38.505 -14.301 1.00 47.55 ? 298 ARG A NH1 1 ATOM 2273 N NH2 . ARG A 1 298 ? 46.488 -37.687 -16.442 1.00 48.15 ? 298 ARG A NH2 1 ATOM 2274 N N . TYR A 1 299 ? 46.330 -32.019 -11.408 1.00 32.02 ? 299 TYR A N 1 ATOM 2275 C CA . TYR A 1 299 ? 46.006 -30.613 -11.264 1.00 31.41 ? 299 TYR A CA 1 ATOM 2276 C C . TYR A 1 299 ? 46.994 -29.753 -12.034 1.00 31.81 ? 299 TYR A C 1 ATOM 2277 O O . TYR A 1 299 ? 48.207 -29.957 -11.948 1.00 32.78 ? 299 TYR A O 1 ATOM 2278 C CB . TYR A 1 299 ? 46.016 -30.164 -9.794 1.00 31.31 ? 299 TYR A CB 1 ATOM 2279 C CG . TYR A 1 299 ? 45.661 -28.697 -9.652 1.00 30.66 ? 299 TYR A CG 1 ATOM 2280 C CD1 . TYR A 1 299 ? 44.341 -28.285 -9.693 1.00 30.91 ? 299 TYR A CD1 1 ATOM 2281 C CD2 . TYR A 1 299 ? 46.637 -27.738 -9.519 1.00 31.29 ? 299 TYR A CD2 1 ATOM 2282 C CE1 . TYR A 1 299 ? 43.998 -26.955 -9.590 1.00 31.78 ? 299 TYR A CE1 1 ATOM 2283 C CE2 . TYR A 1 299 ? 46.313 -26.393 -9.411 1.00 32.58 ? 299 TYR A CE2 1 ATOM 2284 C CZ . TYR A 1 299 ? 44.987 -26.009 -9.446 1.00 32.49 ? 299 TYR A CZ 1 ATOM 2285 O OH . TYR A 1 299 ? 44.649 -24.681 -9.346 1.00 33.19 ? 299 TYR A OH 1 ATOM 2286 N N . VAL A 1 300 ? 46.456 -28.776 -12.756 1.00 32.21 ? 300 VAL A N 1 ATOM 2287 C CA . VAL A 1 300 ? 47.237 -27.765 -13.458 1.00 32.10 ? 300 VAL A CA 1 ATOM 2288 C C . VAL A 1 300 ? 46.634 -26.385 -13.205 1.00 33.50 ? 300 VAL A C 1 ATOM 2289 O O . VAL A 1 300 ? 45.450 -26.280 -12.883 1.00 33.92 ? 300 VAL A O 1 ATOM 2290 C CB . VAL A 1 300 ? 47.267 -28.031 -14.975 1.00 31.91 ? 300 VAL A CB 1 ATOM 2291 C CG1 . VAL A 1 300 ? 47.871 -29.393 -15.260 1.00 31.92 ? 300 VAL A CG1 1 ATOM 2292 C CG2 . VAL A 1 300 ? 45.876 -27.929 -15.594 1.00 32.38 ? 300 VAL A CG2 1 ATOM 2293 N N . LYS A 1 301 ? 47.445 -25.338 -13.362 1.00 35.03 ? 301 LYS A N 1 ATOM 2294 C CA . LYS A 1 301 ? 47.012 -23.962 -13.103 1.00 36.93 ? 301 LYS A CA 1 ATOM 2295 C C . LYS A 1 301 ? 46.156 -23.367 -14.224 1.00 37.13 ? 301 LYS A C 1 ATOM 2296 O O . LYS A 1 301 ? 45.432 -22.397 -13.996 1.00 38.39 ? 301 LYS A O 1 ATOM 2297 C CB . LYS A 1 301 ? 48.225 -23.045 -12.929 1.00 39.61 ? 301 LYS A CB 1 ATOM 2298 C CG . LYS A 1 301 ? 49.076 -23.291 -11.693 1.00 42.02 ? 301 LYS A CG 1 ATOM 2299 C CD . LYS A 1 301 ? 50.267 -22.336 -11.628 1.00 45.28 ? 301 LYS A CD 1 ATOM 2300 C CE . LYS A 1 301 ? 51.068 -22.311 -12.928 1.00 46.98 ? 301 LYS A CE 1 ATOM 2301 N NZ . LYS A 1 301 ? 52.385 -21.604 -12.835 1.00 49.50 ? 301 LYS A NZ 1 ATOM 2302 N N . GLN A 1 302 ? 46.278 -23.899 -15.439 1.00 36.03 ? 302 GLN A N 1 ATOM 2303 C CA . GLN A 1 302 ? 45.561 -23.350 -16.581 1.00 36.67 ? 302 GLN A CA 1 ATOM 2304 C C . GLN A 1 302 ? 44.111 -23.782 -16.508 1.00 37.86 ? 302 GLN A C 1 ATOM 2305 O O . GLN A 1 302 ? 43.823 -24.921 -16.125 1.00 37.71 ? 302 GLN A O 1 ATOM 2306 C CB . GLN A 1 302 ? 46.163 -23.819 -17.909 1.00 36.19 ? 302 GLN A CB 1 ATOM 2307 C CG . GLN A 1 302 ? 47.628 -23.451 -18.120 1.00 35.80 ? 302 GLN A CG 1 ATOM 2308 C CD . GLN A 1 302 ? 48.589 -24.558 -17.687 1.00 35.24 ? 302 GLN A CD 1 ATOM 2309 O OE1 . GLN A 1 302 ? 48.352 -25.263 -16.698 1.00 34.22 ? 302 GLN A OE1 1 ATOM 2310 N NE2 . GLN A 1 302 ? 49.685 -24.702 -18.416 1.00 34.82 ? 302 GLN A NE2 1 ATOM 2311 N N . ARG A 1 303 ? 43.200 -22.886 -16.873 1.00 40.17 ? 303 ARG A N 1 ATOM 2312 C CA . ARG A 1 303 ? 41.785 -23.222 -16.894 1.00 42.84 ? 303 ARG A CA 1 ATOM 2313 C C . ARG A 1 303 ? 41.464 -24.064 -18.121 1.00 42.27 ? 303 ARG A C 1 ATOM 2314 O O . ARG A 1 303 ? 40.539 -24.870 -18.091 1.00 42.96 ? 303 ARG A O 1 ATOM 2315 C CB . ARG A 1 303 ? 40.902 -21.967 -16.845 1.00 47.14 ? 303 ARG A CB 1 ATOM 2316 C CG . ARG A 1 303 ? 40.829 -21.182 -18.143 1.00 51.95 ? 303 ARG A CG 1 ATOM 2317 C CD . ARG A 1 303 ? 39.748 -20.102 -18.119 1.00 57.56 ? 303 ARG A CD 1 ATOM 2318 N NE . ARG A 1 303 ? 38.480 -20.538 -18.716 1.00 60.35 ? 303 ARG A NE 1 ATOM 2319 C CZ . ARG A 1 303 ? 37.400 -20.949 -18.046 1.00 63.39 ? 303 ARG A CZ 1 ATOM 2320 N NH1 . ARG A 1 303 ? 37.379 -21.008 -16.713 1.00 63.66 ? 303 ARG A NH1 1 ATOM 2321 N NH2 . ARG A 1 303 ? 36.319 -21.314 -18.726 1.00 65.92 ? 303 ARG A NH2 1 ATOM 2322 N N . SER A 1 304 ? 42.245 -23.889 -19.185 1.00 41.17 ? 304 SER A N 1 ATOM 2323 C CA . SER A 1 304 ? 41.936 -24.489 -20.478 1.00 41.35 ? 304 SER A CA 1 ATOM 2324 C C . SER A 1 304 ? 43.182 -24.702 -21.337 1.00 40.20 ? 304 SER A C 1 ATOM 2325 O O . SER A 1 304 ? 44.058 -23.831 -21.425 1.00 40.28 ? 304 SER A O 1 ATOM 2326 C CB . SER A 1 304 ? 40.940 -23.593 -21.227 1.00 43.34 ? 304 SER A CB 1 ATOM 2327 O OG . SER A 1 304 ? 40.531 -24.180 -22.448 1.00 44.41 ? 304 SER A OG 1 ATOM 2328 N N . LEU A 1 305 ? 43.248 -25.872 -21.964 1.00 39.56 ? 305 LEU A N 1 ATOM 2329 C CA . LEU A 1 305 ? 44.311 -26.216 -22.903 1.00 39.17 ? 305 LEU A CA 1 ATOM 2330 C C . LEU A 1 305 ? 43.700 -27.077 -24.007 1.00 40.48 ? 305 LEU A C 1 ATOM 2331 O O . LEU A 1 305 ? 43.489 -28.281 -23.821 1.00 40.26 ? 305 LEU A O 1 ATOM 2332 C CB . LEU A 1 305 ? 45.431 -26.988 -22.202 1.00 37.57 ? 305 LEU A CB 1 ATOM 2333 C CG . LEU A 1 305 ? 46.262 -26.239 -21.154 1.00 36.76 ? 305 LEU A CG 1 ATOM 2334 C CD1 . LEU A 1 305 ? 47.121 -27.215 -20.360 1.00 35.49 ? 305 LEU A CD1 1 ATOM 2335 C CD2 . LEU A 1 305 ? 47.120 -25.146 -21.779 1.00 36.32 ? 305 LEU A CD2 1 ATOM 2336 N N . LEU A 1 306 ? 43.409 -26.453 -25.147 1.00 41.64 ? 306 LEU A N 1 ATOM 2337 C CA . LEU A 1 306 ? 42.679 -27.113 -26.229 1.00 42.80 ? 306 LEU A CA 1 ATOM 2338 C C . LEU A 1 306 ? 43.618 -27.885 -27.151 1.00 42.54 ? 306 LEU A C 1 ATOM 2339 O O . LEU A 1 306 ? 44.661 -27.367 -27.568 1.00 41.71 ? 306 LEU A O 1 ATOM 2340 C CB . LEU A 1 306 ? 41.892 -26.086 -27.040 1.00 44.49 ? 306 LEU A CB 1 ATOM 2341 C CG . LEU A 1 306 ? 40.916 -25.219 -26.238 1.00 45.29 ? 306 LEU A CG 1 ATOM 2342 C CD1 . LEU A 1 306 ? 40.268 -24.179 -27.145 1.00 47.05 ? 306 LEU A CD1 1 ATOM 2343 C CD2 . LEU A 1 306 ? 39.858 -26.072 -25.551 1.00 45.92 ? 306 LEU A CD2 1 ATOM 2344 N N . LEU A 1 307 ? 43.234 -29.126 -27.455 1.00 42.12 ? 307 LEU A N 1 ATOM 2345 C CA . LEU A 1 307 ? 44.003 -30.012 -28.319 1.00 41.52 ? 307 LEU A CA 1 ATOM 2346 C C . LEU A 1 307 ? 43.357 -30.044 -29.698 1.00 43.66 ? 307 LEU A C 1 ATOM 2347 O O . LEU A 1 307 ? 42.168 -30.354 -29.827 1.00 45.54 ? 307 LEU A O 1 ATOM 2348 C CB . LEU A 1 307 ? 44.006 -31.413 -27.730 1.00 41.35 ? 307 LEU A CB 1 ATOM 2349 C CG . LEU A 1 307 ? 44.855 -32.466 -28.436 1.00 41.81 ? 307 LEU A CG 1 ATOM 2350 C CD1 . LEU A 1 307 ? 46.306 -32.392 -27.986 1.00 40.48 ? 307 LEU A CD1 1 ATOM 2351 C CD2 . LEU A 1 307 ? 44.287 -33.840 -28.157 1.00 42.87 ? 307 LEU A CD2 1 ATOM 2352 N N . ALA A 1 308 ? 44.132 -29.720 -30.729 1.00 43.33 ? 308 ALA A N 1 ATOM 2353 C CA . ALA A 1 308 ? 43.623 -29.756 -32.097 1.00 44.87 ? 308 ALA A CA 1 ATOM 2354 C C . ALA A 1 308 ? 43.242 -31.175 -32.481 1.00 45.85 ? 308 ALA A C 1 ATOM 2355 O O . ALA A 1 308 ? 43.996 -32.120 -32.223 1.00 44.21 ? 308 ALA A O 1 ATOM 2356 C CB . ALA A 1 308 ? 44.655 -29.214 -33.070 1.00 44.91 ? 308 ALA A CB 1 ATOM 2357 N N . THR A 1 309 ? 42.055 -31.316 -33.069 1.00 47.65 ? 309 THR A N 1 ATOM 2358 C CA . THR A 1 309 ? 41.607 -32.588 -33.634 1.00 49.78 ? 309 THR A CA 1 ATOM 2359 C C . THR A 1 309 ? 41.256 -32.427 -35.119 1.00 52.12 ? 309 THR A C 1 ATOM 2360 O O . THR A 1 309 ? 40.603 -33.286 -35.714 1.00 54.41 ? 309 THR A O 1 ATOM 2361 C CB . THR A 1 309 ? 40.396 -33.142 -32.863 1.00 50.58 ? 309 THR A CB 1 ATOM 2362 O OG1 . THR A 1 309 ? 39.338 -32.180 -32.870 1.00 51.92 ? 309 THR A OG1 1 ATOM 2363 C CG2 . THR A 1 309 ? 40.781 -33.444 -31.433 1.00 48.21 ? 309 THR A CG2 1 ATOM 2364 N N . GLY A 1 310 ? 41.711 -31.328 -35.713 1.00 51.58 ? 310 GLY A N 1 ATOM 2365 C CA . GLY A 1 310 ? 41.466 -31.052 -37.121 1.00 53.87 ? 310 GLY A CA 1 ATOM 2366 C C . GLY A 1 310 ? 42.614 -30.270 -37.711 1.00 52.85 ? 310 GLY A C 1 ATOM 2367 O O . GLY A 1 310 ? 43.500 -29.814 -36.986 1.00 51.07 ? 310 GLY A O 1 ATOM 2368 N N . MET A 1 311 ? 42.597 -30.118 -39.031 1.00 55.01 ? 311 MET A N 1 ATOM 2369 C CA . MET A 1 311 ? 43.632 -29.374 -39.742 1.00 54.14 ? 311 MET A CA 1 ATOM 2370 C C . MET A 1 311 ? 43.499 -27.883 -39.476 1.00 53.60 ? 311 MET A C 1 ATOM 2371 O O . MET A 1 311 ? 42.509 -27.437 -38.908 1.00 54.17 ? 311 MET A O 1 ATOM 2372 C CB . MET A 1 311 ? 43.524 -29.631 -41.245 1.00 56.81 ? 311 MET A CB 1 ATOM 2373 C CG . MET A 1 311 ? 42.289 -29.025 -41.898 1.00 59.43 ? 311 MET A CG 1 ATOM 2374 S SD . MET A 1 311 ? 42.235 -29.336 -43.664 1.00 62.73 ? 311 MET A SD 1 ATOM 2375 C CE . MET A 1 311 ? 41.906 -31.097 -43.682 1.00 64.10 ? 311 MET A CE 1 ATOM 2376 N N . LYS A 1 312 ? 44.497 -27.117 -39.903 1.00 53.35 ? 312 LYS A N 1 ATOM 2377 C CA . LYS A 1 312 ? 44.439 -25.658 -39.830 1.00 54.07 ? 312 LYS A CA 1 ATOM 2378 C C . LYS A 1 312 ? 43.278 -25.138 -40.679 1.00 57.46 ? 312 LYS A C 1 ATOM 2379 O O . LYS A 1 312 ? 43.076 -25.585 -41.809 1.00 59.79 ? 312 LYS A O 1 ATOM 2380 C CB . LYS A 1 312 ? 45.757 -25.046 -40.323 1.00 53.79 ? 312 LYS A CB 1 ATOM 2381 C CG . LYS A 1 312 ? 45.774 -23.524 -40.402 1.00 54.77 ? 312 LYS A CG 1 ATOM 2382 C CD . LYS A 1 312 ? 47.018 -23.033 -41.123 1.00 55.16 ? 312 LYS A CD 1 ATOM 2383 C CE . LYS A 1 312 ? 46.946 -21.544 -41.424 1.00 56.86 ? 312 LYS A CE 1 ATOM 2384 N NZ . LYS A 1 312 ? 46.935 -20.730 -40.179 1.00 55.98 ? 312 LYS A NZ 1 ATOM 2385 N N . ASN A 1 313 ? 42.526 -24.188 -40.135 1.00 57.95 ? 313 ASN A N 1 ATOM 2386 C CA . ASN A 1 313 ? 41.395 -23.621 -40.846 1.00 60.78 ? 313 ASN A CA 1 ATOM 2387 C C . ASN A 1 313 ? 41.854 -22.477 -41.742 1.00 62.11 ? 313 ASN A C 1 ATOM 2388 O O . ASN A 1 313 ? 42.405 -21.488 -41.255 1.00 60.31 ? 313 ASN A O 1 ATOM 2389 C CB . ASN A 1 313 ? 40.331 -23.126 -39.868 1.00 61.09 ? 313 ASN A CB 1 ATOM 2390 C CG . ASN A 1 313 ? 38.990 -22.904 -40.540 1.00 64.61 ? 313 ASN A CG 1 ATOM 2391 O OD1 . ASN A 1 313 ? 38.487 -23.785 -41.234 1.00 66.47 ? 313 ASN A OD1 1 ATOM 2392 N ND2 . ASN A 1 313 ? 38.401 -21.727 -40.335 1.00 65.60 ? 313 ASN A ND2 1 ATOM 2393 N N . VAL A 1 314 ? 41.625 -22.628 -43.048 1.00 64.87 ? 314 VAL A N 1 ATOM 2394 C CA . VAL A 1 314 ? 41.997 -21.624 -44.037 1.00 66.65 ? 314 VAL A CA 1 ATOM 2395 C C . VAL A 1 314 ? 40.744 -21.259 -44.838 1.00 71.24 ? 314 VAL A C 1 ATOM 2396 O O . VAL A 1 314 ? 40.461 -21.867 -45.872 1.00 73.27 ? 314 VAL A O 1 ATOM 2397 C CB . VAL A 1 314 ? 43.105 -22.138 -44.985 1.00 66.29 ? 314 VAL A CB 1 ATOM 2398 C CG1 . VAL A 1 314 ? 43.736 -20.981 -45.746 1.00 67.05 ? 314 VAL A CG1 1 ATOM 2399 C CG2 . VAL A 1 314 ? 44.171 -22.894 -44.207 1.00 63.27 ? 314 VAL A CG2 1 ATOM 2400 N N . PRO A 1 315 ? 39.984 -20.263 -44.356 1.00 72.97 ? 315 PRO A N 1 ATOM 2401 C CA . PRO A 1 315 ? 38.717 -19.902 -44.982 1.00 77.75 ? 315 PRO A CA 1 ATOM 2402 C C . PRO A 1 315 ? 38.882 -19.112 -46.287 1.00 81.26 ? 315 PRO A C 1 ATOM 2403 O O . PRO A 1 315 ? 39.956 -18.576 -46.556 1.00 79.92 ? 315 PRO A O 1 ATOM 2404 C CB . PRO A 1 315 ? 38.032 -19.049 -43.912 1.00 77.49 ? 315 PRO A CB 1 ATOM 2405 C CG . PRO A 1 315 ? 39.138 -18.470 -43.101 1.00 73.79 ? 315 PRO A CG 1 ATOM 2406 C CD . PRO A 1 315 ? 40.328 -19.369 -43.235 1.00 70.96 ? 315 PRO A CD 1 ATOM 2407 N N . GLU A 1 316 ? 37.814 -19.058 -47.081 1.00 86.51 ? 316 GLU A N 1 ATOM 2408 C CA . GLU A 1 316 ? 37.796 -18.298 -48.338 1.00 90.91 ? 316 GLU A CA 1 ATOM 2409 C C . GLU A 1 316 ? 38.201 -16.833 -48.154 1.00 90.67 ? 316 GLU A C 1 ATOM 2410 O O . GLU A 1 316 ? 37.739 -16.147 -47.242 1.00 90.27 ? 316 GLU A O 1 ATOM 2411 C CB . GLU A 1 316 ? 36.404 -18.361 -48.990 1.00 96.52 ? 316 GLU A CB 1 ATOM 2412 C CG . GLU A 1 316 ? 36.332 -19.192 -50.265 1.00 99.77 ? 316 GLU A CG 1 ATOM 2413 C CD . GLU A 1 316 ? 36.877 -18.454 -51.476 1.00 101.98 ? 316 GLU A CD 1 ATOM 2414 O OE1 . GLU A 1 316 ? 37.986 -17.885 -51.380 1.00 100.56 ? 316 GLU A OE1 1 ATOM 2415 O OE2 . GLU A 1 316 ? 36.198 -18.435 -52.524 1.00 105.82 ? 316 GLU A OE2 1 ATOM 2416 N N . ILE A 1 317 ? 38.997 -16.298 -48.926 1.00 91.07 ? 317 ILE A N 1 ATOM 2417 N N . GLY B 2 1 ? 52.143 -25.183 -42.494 1.00 66.36 ? 1 GLY B N 1 ATOM 2418 C CA . GLY B 2 1 ? 52.718 -26.502 -42.098 1.00 65.61 ? 1 GLY B CA 1 ATOM 2419 C C . GLY B 2 1 ? 54.031 -26.803 -42.795 1.00 66.78 ? 1 GLY B C 1 ATOM 2420 O O . GLY B 2 1 ? 54.444 -26.076 -43.692 1.00 68.05 ? 1 GLY B O 1 ATOM 2421 N N . LEU B 2 2 ? 54.675 -27.894 -42.389 1.00 66.33 ? 2 LEU B N 1 ATOM 2422 C CA . LEU B 2 2 ? 55.982 -28.257 -42.930 1.00 68.05 ? 2 LEU B CA 1 ATOM 2423 C C . LEU B 2 2 ? 55.945 -28.708 -44.387 1.00 69.20 ? 2 LEU B C 1 ATOM 2424 O O . LEU B 2 2 ? 56.961 -28.624 -45.081 1.00 71.05 ? 2 LEU B O 1 ATOM 2425 C CB . LEU B 2 2 ? 56.621 -29.361 -42.091 1.00 67.56 ? 2 LEU B CB 1 ATOM 2426 C CG . LEU B 2 2 ? 56.990 -29.028 -40.651 1.00 66.98 ? 2 LEU B CG 1 ATOM 2427 C CD1 . LEU B 2 2 ? 57.598 -30.258 -40.007 1.00 66.88 ? 2 LEU B CD1 1 ATOM 2428 C CD2 . LEU B 2 2 ? 57.951 -27.853 -40.574 1.00 69.04 ? 2 LEU B CD2 1 ATOM 2429 N N . PHE B 2 3 ? 54.789 -29.180 -44.847 1.00 68.12 ? 3 PHE B N 1 ATOM 2430 C CA . PHE B 2 3 ? 54.672 -29.749 -46.192 1.00 69.36 ? 3 PHE B CA 1 ATOM 2431 C C . PHE B 2 3 ? 54.111 -28.777 -47.233 1.00 70.33 ? 3 PHE B C 1 ATOM 2432 O O . PHE B 2 3 ? 54.004 -29.122 -48.405 1.00 72.30 ? 3 PHE B O 1 ATOM 2433 C CB . PHE B 2 3 ? 53.885 -31.060 -46.123 1.00 68.09 ? 3 PHE B CB 1 ATOM 2434 C CG . PHE B 2 3 ? 54.583 -32.114 -45.308 1.00 67.82 ? 3 PHE B CG 1 ATOM 2435 C CD1 . PHE B 2 3 ? 54.420 -32.169 -43.931 1.00 66.36 ? 3 PHE B CD1 1 ATOM 2436 C CD2 . PHE B 2 3 ? 55.452 -33.011 -45.912 1.00 69.45 ? 3 PHE B CD2 1 ATOM 2437 C CE1 . PHE B 2 3 ? 55.087 -33.121 -43.177 1.00 66.56 ? 3 PHE B CE1 1 ATOM 2438 C CE2 . PHE B 2 3 ? 56.121 -33.966 -45.167 1.00 69.62 ? 3 PHE B CE2 1 ATOM 2439 C CZ . PHE B 2 3 ? 55.941 -34.019 -43.796 1.00 68.29 ? 3 PHE B CZ 1 ATOM 2440 N N . GLY B 2 4 ? 53.779 -27.560 -46.807 1.00 70.30 ? 4 GLY B N 1 ATOM 2441 C CA . GLY B 2 4 ? 53.533 -26.446 -47.730 1.00 71.36 ? 4 GLY B CA 1 ATOM 2442 C C . GLY B 2 4 ? 52.332 -26.543 -48.658 1.00 70.96 ? 4 GLY B C 1 ATOM 2443 O O . GLY B 2 4 ? 52.304 -25.881 -49.691 1.00 72.87 ? 4 GLY B O 1 ATOM 2444 N N . ALA B 2 5 ? 51.341 -27.351 -48.293 1.00 69.35 ? 5 ALA B N 1 ATOM 2445 C CA . ALA B 2 5 ? 50.116 -27.487 -49.079 1.00 69.02 ? 5 ALA B CA 1 ATOM 2446 C C . ALA B 2 5 ? 48.980 -26.697 -48.436 1.00 68.36 ? 5 ALA B C 1 ATOM 2447 O O . ALA B 2 5 ? 48.489 -25.735 -49.020 1.00 68.89 ? 5 ALA B O 1 ATOM 2448 C CB . ALA B 2 5 ? 49.737 -28.954 -49.221 1.00 68.38 ? 5 ALA B CB 1 ATOM 2449 N N . ILE B 2 6 ? 48.577 -27.098 -47.229 1.00 67.67 ? 6 ILE B N 1 ATOM 2450 C CA . ILE B 2 6 ? 47.525 -26.393 -46.491 1.00 67.25 ? 6 ILE B CA 1 ATOM 2451 C C . ILE B 2 6 ? 48.066 -25.051 -46.008 1.00 68.27 ? 6 ILE B C 1 ATOM 2452 O O . ILE B 2 6 ? 49.049 -25.006 -45.261 1.00 68.08 ? 6 ILE B O 1 ATOM 2453 C CB . ILE B 2 6 ? 47.014 -27.198 -45.282 1.00 66.19 ? 6 ILE B CB 1 ATOM 2454 C CG1 . ILE B 2 6 ? 46.421 -28.536 -45.738 1.00 66.25 ? 6 ILE B CG1 1 ATOM 2455 C CG2 . ILE B 2 6 ? 45.963 -26.402 -44.517 1.00 65.97 ? 6 ILE B CG2 1 ATOM 2456 C CD1 . ILE B 2 6 ? 46.104 -29.483 -44.602 1.00 65.43 ? 6 ILE B CD1 1 ATOM 2457 N N . ALA B 2 7 ? 47.413 -23.970 -46.437 1.00 69.26 ? 7 ALA B N 1 ATOM 2458 C CA . ALA B 2 7 ? 47.899 -22.609 -46.221 1.00 70.95 ? 7 ALA B CA 1 ATOM 2459 C C . ALA B 2 7 ? 49.266 -22.434 -46.878 1.00 73.04 ? 7 ALA B C 1 ATOM 2460 O O . ALA B 2 7 ? 50.120 -21.699 -46.382 1.00 74.04 ? 7 ALA B O 1 ATOM 2461 C CB . ALA B 2 7 ? 47.957 -22.277 -44.733 1.00 70.60 ? 7 ALA B CB 1 ATOM 2462 N N . GLY B 2 8 ? 49.452 -23.121 -48.002 1.00 74.39 ? 8 GLY B N 1 ATOM 2463 C CA . GLY B 2 8 ? 50.684 -23.057 -48.779 1.00 76.69 ? 8 GLY B CA 1 ATOM 2464 C C . GLY B 2 8 ? 50.351 -22.810 -50.236 1.00 78.43 ? 8 GLY B C 1 ATOM 2465 O O . GLY B 2 8 ? 49.782 -21.771 -50.569 1.00 80.00 ? 8 GLY B O 1 ATOM 2466 N N . PHE B 2 9 ? 50.687 -23.758 -51.110 1.00 79.11 ? 9 PHE B N 1 ATOM 2467 C CA . PHE B 2 9 ? 50.428 -23.576 -52.543 1.00 80.87 ? 9 PHE B CA 1 ATOM 2468 C C . PHE B 2 9 ? 48.963 -23.838 -52.903 1.00 79.78 ? 9 PHE B C 1 ATOM 2469 O O . PHE B 2 9 ? 48.553 -23.580 -54.027 1.00 80.30 ? 9 PHE B O 1 ATOM 2470 C CB . PHE B 2 9 ? 51.396 -24.399 -53.410 1.00 82.63 ? 9 PHE B CB 1 ATOM 2471 C CG . PHE B 2 9 ? 51.020 -25.845 -53.563 1.00 81.98 ? 9 PHE B CG 1 ATOM 2472 C CD1 . PHE B 2 9 ? 51.354 -26.771 -52.590 1.00 80.87 ? 9 PHE B CD1 1 ATOM 2473 C CD2 . PHE B 2 9 ? 50.355 -26.285 -54.695 1.00 83.16 ? 9 PHE B CD2 1 ATOM 2474 C CE1 . PHE B 2 9 ? 51.019 -28.105 -52.731 1.00 80.54 ? 9 PHE B CE1 1 ATOM 2475 C CE2 . PHE B 2 9 ? 50.016 -27.620 -54.844 1.00 82.70 ? 9 PHE B CE2 1 ATOM 2476 C CZ . PHE B 2 9 ? 50.348 -28.531 -53.862 1.00 81.25 ? 9 PHE B CZ 1 ATOM 2477 N N . ILE B 2 10 ? 48.185 -24.362 -51.955 1.00 78.39 ? 10 ILE B N 1 ATOM 2478 C CA . ILE B 2 10 ? 46.730 -24.320 -52.060 1.00 77.88 ? 10 ILE B CA 1 ATOM 2479 C C . ILE B 2 10 ? 46.281 -23.060 -51.330 1.00 77.80 ? 10 ILE B C 1 ATOM 2480 O O . ILE B 2 10 ? 46.623 -22.853 -50.164 1.00 77.26 ? 10 ILE B O 1 ATOM 2481 C CB . ILE B 2 10 ? 46.033 -25.552 -51.453 1.00 76.81 ? 10 ILE B CB 1 ATOM 2482 C CG1 . ILE B 2 10 ? 46.360 -26.812 -52.257 1.00 77.78 ? 10 ILE B CG1 1 ATOM 2483 C CG2 . ILE B 2 10 ? 44.523 -25.357 -51.448 1.00 76.61 ? 10 ILE B CG2 1 ATOM 2484 C CD1 . ILE B 2 10 ? 47.783 -27.297 -52.104 1.00 78.49 ? 10 ILE B CD1 1 ATOM 2485 N N . GLU B 2 11 ? 45.523 -22.226 -52.033 1.00 79.08 ? 11 GLU B N 1 ATOM 2486 C CA . GLU B 2 11 ? 45.113 -20.912 -51.544 1.00 79.65 ? 11 GLU B CA 1 ATOM 2487 C C . GLU B 2 11 ? 44.289 -21.009 -50.269 1.00 77.36 ? 11 GLU B C 1 ATOM 2488 O O . GLU B 2 11 ? 44.560 -20.312 -49.292 1.00 77.69 ? 11 GLU B O 1 ATOM 2489 C CB . GLU B 2 11 ? 44.293 -20.197 -52.623 1.00 81.87 ? 11 GLU B CB 1 ATOM 2490 C CG . GLU B 2 11 ? 43.912 -18.756 -52.303 1.00 83.81 ? 11 GLU B CG 1 ATOM 2491 C CD . GLU B 2 11 ? 45.047 -17.779 -52.544 1.00 85.79 ? 11 GLU B CD 1 ATOM 2492 O OE1 . GLU B 2 11 ? 46.127 -17.956 -51.936 1.00 86.14 ? 11 GLU B OE1 1 ATOM 2493 O OE2 . GLU B 2 11 ? 44.849 -16.832 -53.335 1.00 87.30 ? 11 GLU B OE2 1 ATOM 2494 N N . ASN B 2 12 ? 43.279 -21.871 -50.295 1.00 75.62 ? 12 ASN B N 1 ATOM 2495 C CA . ASN B 2 12 ? 42.369 -22.023 -49.170 1.00 74.33 ? 12 ASN B CA 1 ATOM 2496 C C . ASN B 2 12 ? 41.575 -23.315 -49.252 1.00 73.09 ? 12 ASN B C 1 ATOM 2497 O O . ASN B 2 12 ? 41.651 -24.048 -50.238 1.00 73.08 ? 12 ASN B O 1 ATOM 2498 C CB . ASN B 2 12 ? 41.423 -20.816 -49.085 1.00 75.67 ? 12 ASN B CB 1 ATOM 2499 C CG . ASN B 2 12 ? 40.725 -20.520 -50.399 1.00 76.69 ? 12 ASN B CG 1 ATOM 2500 O OD1 . ASN B 2 12 ? 40.962 -19.486 -51.016 1.00 78.11 ? 12 ASN B OD1 1 ATOM 2501 N ND2 . ASN B 2 12 ? 39.859 -21.429 -50.831 1.00 76.45 ? 12 ASN B ND2 1 ATOM 2502 N N . GLY B 2 13 ? 40.817 -23.590 -48.199 1.00 72.44 ? 13 GLY B N 1 ATOM 2503 C CA . GLY B 2 13 ? 39.948 -24.751 -48.164 1.00 72.35 ? 13 GLY B CA 1 ATOM 2504 C C . GLY B 2 13 ? 38.598 -24.451 -48.771 1.00 73.82 ? 13 GLY B C 1 ATOM 2505 O O . GLY B 2 13 ? 38.283 -23.301 -49.080 1.00 74.36 ? 13 GLY B O 1 ATOM 2506 N N . TRP B 2 14 ? 37.804 -25.503 -48.931 1.00 74.56 ? 14 TRP B N 1 ATOM 2507 C CA . TRP B 2 14 ? 36.464 -25.397 -49.473 1.00 76.50 ? 14 TRP B CA 1 ATOM 2508 C C . TRP B 2 14 ? 35.437 -25.586 -48.368 1.00 77.27 ? 14 TRP B C 1 ATOM 2509 O O . TRP B 2 14 ? 35.405 -26.626 -47.719 1.00 77.54 ? 14 TRP B O 1 ATOM 2510 C CB . TRP B 2 14 ? 36.257 -26.456 -50.551 1.00 77.49 ? 14 TRP B CB 1 ATOM 2511 C CG . TRP B 2 14 ? 37.200 -26.330 -51.709 1.00 77.49 ? 14 TRP B CG 1 ATOM 2512 C CD1 . TRP B 2 14 ? 37.689 -25.175 -52.251 1.00 77.68 ? 14 TRP B CD1 1 ATOM 2513 C CD2 . TRP B 2 14 ? 37.746 -27.399 -52.486 1.00 77.64 ? 14 TRP B CD2 1 ATOM 2514 N NE1 . TRP B 2 14 ? 38.518 -25.460 -53.307 1.00 77.72 ? 14 TRP B NE1 1 ATOM 2515 C CE2 . TRP B 2 14 ? 38.568 -26.819 -53.475 1.00 77.95 ? 14 TRP B CE2 1 ATOM 2516 C CE3 . TRP B 2 14 ? 37.624 -28.792 -52.439 1.00 78.02 ? 14 TRP B CE3 1 ATOM 2517 C CZ2 . TRP B 2 14 ? 39.264 -27.586 -54.413 1.00 78.59 ? 14 TRP B CZ2 1 ATOM 2518 C CZ3 . TRP B 2 14 ? 38.317 -29.554 -53.371 1.00 78.56 ? 14 TRP B CZ3 1 ATOM 2519 C CH2 . TRP B 2 14 ? 39.124 -28.949 -54.346 1.00 78.89 ? 14 TRP B CH2 1 ATOM 2520 N N . GLU B 2 15 ? 34.598 -24.578 -48.158 1.00 78.47 ? 15 GLU B N 1 ATOM 2521 C CA . GLU B 2 15 ? 33.524 -24.661 -47.172 1.00 80.04 ? 15 GLU B CA 1 ATOM 2522 C C . GLU B 2 15 ? 32.376 -25.537 -47.678 1.00 82.38 ? 15 GLU B C 1 ATOM 2523 O O . GLU B 2 15 ? 31.553 -26.005 -46.892 1.00 83.90 ? 15 GLU B O 1 ATOM 2524 C CB . GLU B 2 15 ? 33.031 -23.257 -46.804 1.00 81.16 ? 15 GLU B CB 1 ATOM 2525 C CG . GLU B 2 15 ? 34.106 -22.398 -46.144 1.00 79.99 ? 15 GLU B CG 1 ATOM 2526 C CD . GLU B 2 15 ? 33.715 -20.937 -45.992 1.00 81.60 ? 15 GLU B CD 1 ATOM 2527 O OE1 . GLU B 2 15 ? 32.513 -20.647 -45.821 1.00 83.77 ? 15 GLU B OE1 1 ATOM 2528 O OE2 . GLU B 2 15 ? 34.623 -20.077 -46.028 1.00 81.01 ? 15 GLU B OE2 1 ATOM 2529 N N . GLY B 2 16 ? 32.330 -25.761 -48.990 1.00 83.22 ? 16 GLY B N 1 ATOM 2530 C CA . GLY B 2 16 ? 31.352 -26.659 -49.597 1.00 85.37 ? 16 GLY B CA 1 ATOM 2531 C C . GLY B 2 16 ? 31.666 -28.130 -49.381 1.00 85.20 ? 16 GLY B C 1 ATOM 2532 O O . GLY B 2 16 ? 30.776 -28.978 -49.483 1.00 87.34 ? 16 GLY B O 1 ATOM 2533 N N . LEU B 2 17 ? 32.929 -28.439 -49.086 1.00 82.79 ? 17 LEU B N 1 ATOM 2534 C CA . LEU B 2 17 ? 33.351 -29.823 -48.889 1.00 82.22 ? 17 LEU B CA 1 ATOM 2535 C C . LEU B 2 17 ? 32.944 -30.322 -47.504 1.00 82.58 ? 17 LEU B C 1 ATOM 2536 O O . LEU B 2 17 ? 33.738 -30.303 -46.565 1.00 80.97 ? 17 LEU B O 1 ATOM 2537 C CB . LEU B 2 17 ? 34.865 -29.965 -49.093 1.00 79.65 ? 17 LEU B CB 1 ATOM 2538 C CG . LEU B 2 17 ? 35.408 -31.400 -49.073 1.00 79.44 ? 17 LEU B CG 1 ATOM 2539 C CD1 . LEU B 2 17 ? 34.874 -32.193 -50.259 1.00 81.36 ? 17 LEU B CD1 1 ATOM 2540 C CD2 . LEU B 2 17 ? 36.930 -31.407 -49.059 1.00 77.04 ? 17 LEU B CD2 1 ATOM 2541 N N . ILE B 2 18 ? 31.698 -30.771 -47.394 1.00 85.39 ? 18 ILE B N 1 ATOM 2542 C CA . ILE B 2 18 ? 31.182 -31.355 -46.150 1.00 86.68 ? 18 ILE B CA 1 ATOM 2543 C C . ILE B 2 18 ? 31.278 -32.887 -46.160 1.00 87.49 ? 18 ILE B C 1 ATOM 2544 O O . ILE B 2 18 ? 30.990 -33.538 -45.156 1.00 88.31 ? 18 ILE B O 1 ATOM 2545 C CB . ILE B 2 18 ? 29.731 -30.890 -45.833 1.00 89.99 ? 18 ILE B CB 1 ATOM 2546 C CG1 . ILE B 2 18 ? 28.809 -30.915 -47.061 1.00 92.55 ? 18 ILE B CG1 1 ATOM 2547 C CG2 . ILE B 2 18 ? 29.740 -29.471 -45.285 1.00 89.21 ? 18 ILE B CG2 1 ATOM 2548 C CD1 . ILE B 2 18 ? 28.678 -32.259 -47.741 1.00 94.31 ? 18 ILE B CD1 1 ATOM 2549 N N . ASP B 2 19 ? 31.694 -33.449 -47.294 1.00 87.53 ? 19 ASP B N 1 ATOM 2550 C CA . ASP B 2 19 ? 31.796 -34.901 -47.476 1.00 88.79 ? 19 ASP B CA 1 ATOM 2551 C C . ASP B 2 19 ? 32.949 -35.507 -46.684 1.00 85.40 ? 19 ASP B C 1 ATOM 2552 O O . ASP B 2 19 ? 32.819 -36.592 -46.122 1.00 86.45 ? 19 ASP B O 1 ATOM 2553 C CB . ASP B 2 19 ? 31.998 -35.242 -48.958 1.00 89.94 ? 19 ASP B CB 1 ATOM 2554 C CG . ASP B 2 19 ? 30.759 -35.031 -49.783 1.00 93.58 ? 19 ASP B CG 1 ATOM 2555 O OD1 . ASP B 2 19 ? 29.754 -35.719 -49.514 1.00 97.70 ? 19 ASP B OD1 1 ATOM 2556 O OD2 . ASP B 2 19 ? 30.795 -34.198 -50.717 1.00 93.61 ? 19 ASP B OD2 1 ATOM 2557 N N . GLY B 2 20 ? 34.083 -34.812 -46.674 1.00 81.67 ? 20 GLY B N 1 ATOM 2558 C CA . GLY B 2 20 ? 35.286 -35.287 -45.993 1.00 78.85 ? 20 GLY B CA 1 ATOM 2559 C C . GLY B 2 20 ? 36.293 -34.172 -45.785 1.00 75.52 ? 20 GLY B C 1 ATOM 2560 O O . GLY B 2 20 ? 35.981 -32.997 -45.982 1.00 75.11 ? 20 GLY B O 1 ATOM 2561 N N . TRP B 2 21 ? 37.504 -34.543 -45.384 1.00 73.19 ? 21 TRP B N 1 ATOM 2562 C CA . TRP B 2 21 ? 38.562 -33.569 -45.128 1.00 70.38 ? 21 TRP B CA 1 ATOM 2563 C C . TRP B 2 21 ? 39.188 -33.108 -46.434 1.00 69.65 ? 21 TRP B C 1 ATOM 2564 O O . TRP B 2 21 ? 39.442 -31.922 -46.610 1.00 68.90 ? 21 TRP B O 1 ATOM 2565 C CB . TRP B 2 21 ? 39.647 -34.159 -44.220 1.00 68.80 ? 21 TRP B CB 1 ATOM 2566 C CG . TRP B 2 21 ? 39.226 -34.347 -42.786 1.00 68.66 ? 21 TRP B CG 1 ATOM 2567 C CD1 . TRP B 2 21 ? 37.975 -34.639 -42.328 1.00 70.42 ? 21 TRP B CD1 1 ATOM 2568 C CD2 . TRP B 2 21 ? 40.069 -34.285 -41.631 1.00 66.87 ? 21 TRP B CD2 1 ATOM 2569 N NE1 . TRP B 2 21 ? 37.983 -34.748 -40.963 1.00 70.12 ? 21 TRP B NE1 1 ATOM 2570 C CE2 . TRP B 2 21 ? 39.256 -34.540 -40.508 1.00 67.99 ? 21 TRP B CE2 1 ATOM 2571 C CE3 . TRP B 2 21 ? 41.432 -34.036 -41.437 1.00 65.11 ? 21 TRP B CE3 1 ATOM 2572 C CZ2 . TRP B 2 21 ? 39.758 -34.554 -39.204 1.00 67.05 ? 21 TRP B CZ2 1 ATOM 2573 C CZ3 . TRP B 2 21 ? 41.934 -34.050 -40.138 1.00 64.49 ? 21 TRP B CZ3 1 ATOM 2574 C CH2 . TRP B 2 21 ? 41.097 -34.310 -39.040 1.00 65.26 ? 21 TRP B CH2 1 ATOM 2575 N N . TYR B 2 22 ? 39.437 -34.054 -47.336 1.00 70.48 ? 22 TYR B N 1 ATOM 2576 C CA . TYR B 2 22 ? 40.091 -33.779 -48.619 1.00 70.45 ? 22 TYR B CA 1 ATOM 2577 C C . TYR B 2 22 ? 39.206 -34.227 -49.782 1.00 73.06 ? 22 TYR B C 1 ATOM 2578 O O . TYR B 2 22 ? 38.361 -35.112 -49.627 1.00 74.59 ? 22 TYR B O 1 ATOM 2579 C CB . TYR B 2 22 ? 41.439 -34.502 -48.691 1.00 69.49 ? 22 TYR B CB 1 ATOM 2580 C CG . TYR B 2 22 ? 42.252 -34.403 -47.421 1.00 67.61 ? 22 TYR B CG 1 ATOM 2581 C CD1 . TYR B 2 22 ? 43.109 -33.332 -47.203 1.00 65.97 ? 22 TYR B CD1 1 ATOM 2582 C CD2 . TYR B 2 22 ? 42.158 -35.380 -46.436 1.00 67.49 ? 22 TYR B CD2 1 ATOM 2583 C CE1 . TYR B 2 22 ? 43.851 -33.238 -46.041 1.00 64.74 ? 22 TYR B CE1 1 ATOM 2584 C CE2 . TYR B 2 22 ? 42.897 -35.293 -45.268 1.00 66.05 ? 22 TYR B CE2 1 ATOM 2585 C CZ . TYR B 2 22 ? 43.741 -34.220 -45.075 1.00 64.53 ? 22 TYR B CZ 1 ATOM 2586 O OH . TYR B 2 22 ? 44.479 -34.131 -43.921 1.00 62.96 ? 22 TYR B OH 1 ATOM 2587 N N . GLY B 2 23 ? 39.405 -33.617 -50.947 1.00 73.71 ? 23 GLY B N 1 ATOM 2588 C CA . GLY B 2 23 ? 38.576 -33.922 -52.105 1.00 76.64 ? 23 GLY B CA 1 ATOM 2589 C C . GLY B 2 23 ? 39.077 -33.381 -53.431 1.00 77.44 ? 23 GLY B C 1 ATOM 2590 O O . GLY B 2 23 ? 40.122 -32.731 -53.502 1.00 76.07 ? 23 GLY B O 1 ATOM 2591 N N . PHE B 2 24 ? 38.308 -33.671 -54.478 1.00 80.53 ? 24 PHE B N 1 ATOM 2592 C CA . PHE B 2 24 ? 38.586 -33.220 -55.842 1.00 82.10 ? 24 PHE B CA 1 ATOM 2593 C C . PHE B 2 24 ? 37.449 -32.321 -56.311 1.00 83.28 ? 24 PHE B C 1 ATOM 2594 O O . PHE B 2 24 ? 36.283 -32.589 -56.014 1.00 83.73 ? 24 PHE B O 1 ATOM 2595 C CB . PHE B 2 24 ? 38.688 -34.410 -56.808 1.00 84.50 ? 24 PHE B CB 1 ATOM 2596 C CG . PHE B 2 24 ? 39.408 -35.610 -56.246 1.00 84.69 ? 24 PHE B CG 1 ATOM 2597 C CD1 . PHE B 2 24 ? 38.739 -36.519 -55.434 1.00 85.38 ? 24 PHE B CD1 1 ATOM 2598 C CD2 . PHE B 2 24 ? 40.744 -35.847 -56.552 1.00 84.36 ? 24 PHE B CD2 1 ATOM 2599 C CE1 . PHE B 2 24 ? 39.389 -37.628 -54.924 1.00 85.70 ? 24 PHE B CE1 1 ATOM 2600 C CE2 . PHE B 2 24 ? 41.401 -36.956 -56.043 1.00 84.83 ? 24 PHE B CE2 1 ATOM 2601 C CZ . PHE B 2 24 ? 40.723 -37.846 -55.226 1.00 85.38 ? 24 PHE B CZ 1 ATOM 2602 N N . ARG B 2 25 ? 37.799 -31.259 -57.036 1.00 84.18 ? 25 ARG B N 1 ATOM 2603 C CA . ARG B 2 25 ? 36.826 -30.393 -57.713 1.00 86.35 ? 25 ARG B CA 1 ATOM 2604 C C . ARG B 2 25 ? 37.259 -30.203 -59.164 1.00 87.95 ? 25 ARG B C 1 ATOM 2605 O O . ARG B 2 25 ? 38.290 -29.580 -59.424 1.00 87.60 ? 25 ARG B O 1 ATOM 2606 C CB . ARG B 2 25 ? 36.735 -29.035 -57.010 1.00 85.26 ? 25 ARG B CB 1 ATOM 2607 C CG . ARG B 2 25 ? 35.803 -28.026 -57.669 1.00 86.68 ? 25 ARG B CG 1 ATOM 2608 C CD . ARG B 2 25 ? 35.633 -26.783 -56.806 1.00 86.00 ? 25 ARG B CD 1 ATOM 2609 N NE . ARG B 2 25 ? 34.828 -27.031 -55.606 1.00 86.19 ? 25 ARG B NE 1 ATOM 2610 C CZ . ARG B 2 25 ? 34.670 -26.163 -54.605 1.00 85.63 ? 25 ARG B CZ 1 ATOM 2611 N NH1 . ARG B 2 25 ? 35.279 -24.977 -54.622 1.00 84.96 ? 25 ARG B NH1 1 ATOM 2612 N NH2 . ARG B 2 25 ? 33.910 -26.490 -53.565 1.00 85.89 ? 25 ARG B NH2 1 ATOM 2613 N N . HIS B 2 26 ? 36.474 -30.729 -60.101 1.00 90.73 ? 26 HIS B N 1 ATOM 2614 C CA . HIS B 2 26 ? 36.864 -30.749 -61.518 1.00 92.51 ? 26 HIS B CA 1 ATOM 2615 C C . HIS B 2 26 ? 36.090 -29.761 -62.389 1.00 94.47 ? 26 HIS B C 1 ATOM 2616 O O . HIS B 2 26 ? 35.088 -29.187 -61.969 1.00 94.42 ? 26 HIS B O 1 ATOM 2617 C CB . HIS B 2 26 ? 36.718 -32.162 -62.097 1.00 94.56 ? 26 HIS B CB 1 ATOM 2618 C CG . HIS B 2 26 ? 35.328 -32.711 -62.019 1.00 96.29 ? 26 HIS B CG 1 ATOM 2619 N ND1 . HIS B 2 26 ? 34.322 -32.326 -62.880 1.00 98.57 ? 26 HIS B ND1 1 ATOM 2620 C CD2 . HIS B 2 26 ? 34.778 -33.622 -61.183 1.00 96.54 ? 26 HIS B CD2 1 ATOM 2621 C CE1 . HIS B 2 26 ? 33.212 -32.973 -62.573 1.00 100.13 ? 26 HIS B CE1 1 ATOM 2622 N NE2 . HIS B 2 26 ? 33.462 -33.765 -61.547 1.00 99.10 ? 26 HIS B NE2 1 ATOM 2623 N N . GLN B 2 27 ? 36.588 -29.578 -63.610 1.00 96.43 ? 27 GLN B N 1 ATOM 2624 C CA . GLN B 2 27 ? 35.941 -28.763 -64.630 1.00 98.80 ? 27 GLN B CA 1 ATOM 2625 C C . GLN B 2 27 ? 36.131 -29.466 -65.974 1.00 101.44 ? 27 GLN B C 1 ATOM 2626 O O . GLN B 2 27 ? 37.242 -29.895 -66.298 1.00 101.36 ? 27 GLN B O 1 ATOM 2627 C CB . GLN B 2 27 ? 36.557 -27.358 -64.664 1.00 98.15 ? 27 GLN B CB 1 ATOM 2628 C CG . GLN B 2 27 ? 35.931 -26.400 -65.679 1.00 100.28 ? 27 GLN B CG 1 ATOM 2629 C CD . GLN B 2 27 ? 34.616 -25.798 -65.210 1.00 100.68 ? 27 GLN B CD 1 ATOM 2630 O OE1 . GLN B 2 27 ? 33.569 -26.004 -65.827 1.00 102.96 ? 27 GLN B OE1 1 ATOM 2631 N NE2 . GLN B 2 27 ? 34.666 -25.043 -64.116 1.00 99.01 ? 27 GLN B NE2 1 ATOM 2632 N N . ASN B 2 28 ? 35.047 -29.595 -66.741 1.00 103.73 ? 28 ASN B N 1 ATOM 2633 C CA . ASN B 2 28 ? 35.085 -30.281 -68.037 1.00 106.76 ? 28 ASN B CA 1 ATOM 2634 C C . ASN B 2 28 ? 33.907 -29.877 -68.932 1.00 109.35 ? 28 ASN B C 1 ATOM 2635 O O . ASN B 2 28 ? 33.235 -28.881 -68.656 1.00 108.65 ? 28 ASN B O 1 ATOM 2636 C CB . ASN B 2 28 ? 35.130 -31.805 -67.824 1.00 107.93 ? 28 ASN B CB 1 ATOM 2637 C CG . ASN B 2 28 ? 33.883 -32.350 -67.144 1.00 108.53 ? 28 ASN B CG 1 ATOM 2638 O OD1 . ASN B 2 28 ? 32.998 -31.601 -66.734 1.00 107.97 ? 28 ASN B OD1 1 ATOM 2639 N ND2 . ASN B 2 28 ? 33.816 -33.669 -67.017 1.00 110.02 ? 28 ASN B ND2 1 ATOM 2640 N N . ALA B 2 29 ? 33.667 -30.637 -70.002 1.00 112.42 ? 29 ALA B N 1 ATOM 2641 C CA . ALA B 2 29 ? 32.545 -30.379 -70.905 1.00 115.40 ? 29 ALA B CA 1 ATOM 2642 C C . ALA B 2 29 ? 31.200 -30.372 -70.176 1.00 115.46 ? 29 ALA B C 1 ATOM 2643 O O . ALA B 2 29 ? 30.369 -29.496 -70.419 1.00 116.00 ? 29 ALA B O 1 ATOM 2644 C CB . ALA B 2 29 ? 32.527 -31.400 -72.035 1.00 119.12 ? 29 ALA B CB 1 ATOM 2645 N N . GLN B 2 30 ? 30.994 -31.338 -69.281 1.00 114.99 ? 30 GLN B N 1 ATOM 2646 C CA . GLN B 2 30 ? 29.741 -31.428 -68.521 1.00 115.48 ? 30 GLN B CA 1 ATOM 2647 C C . GLN B 2 30 ? 29.605 -30.366 -67.424 1.00 112.16 ? 30 GLN B C 1 ATOM 2648 O O . GLN B 2 30 ? 28.507 -30.151 -66.914 1.00 112.95 ? 30 GLN B O 1 ATOM 2649 C CB . GLN B 2 30 ? 29.560 -32.822 -67.906 1.00 116.55 ? 30 GLN B CB 1 ATOM 2650 C CG . GLN B 2 30 ? 29.252 -33.925 -68.912 1.00 120.56 ? 30 GLN B CG 1 ATOM 2651 C CD . GLN B 2 30 ? 30.442 -34.820 -69.214 1.00 120.67 ? 30 GLN B CD 1 ATOM 2652 O OE1 . GLN B 2 30 ? 31.594 -34.383 -69.193 1.00 118.18 ? 30 GLN B OE1 1 ATOM 2653 N NE2 . GLN B 2 30 ? 30.163 -36.086 -69.503 1.00 123.94 ? 30 GLN B NE2 1 ATOM 2654 N N . GLY B 2 31 ? 30.707 -29.714 -67.059 1.00 108.92 ? 31 GLY B N 1 ATOM 2655 C CA . GLY B 2 31 ? 30.677 -28.633 -66.070 1.00 106.54 ? 31 GLY B CA 1 ATOM 2656 C C . GLY B 2 31 ? 31.549 -28.925 -64.863 1.00 103.63 ? 31 GLY B C 1 ATOM 2657 O O . GLY B 2 31 ? 32.546 -29.640 -64.970 1.00 102.87 ? 31 GLY B O 1 ATOM 2658 N N . GLU B 2 32 ? 31.171 -28.369 -63.712 1.00 103.83 ? 32 GLU B N 1 ATOM 2659 C CA . GLU B 2 32 ? 31.938 -28.533 -62.474 1.00 100.02 ? 32 GLU B CA 1 ATOM 2660 C C . GLU B 2 32 ? 31.283 -29.541 -61.521 1.00 98.63 ? 32 GLU B C 1 ATOM 2661 O O . GLU B 2 32 ? 30.056 -29.650 -61.459 1.00 101.40 ? 32 GLU B O 1 ATOM 2662 C CB . GLU B 2 32 ? 32.129 -27.175 -61.780 1.00 101.36 ? 32 GLU B CB 1 ATOM 2663 C CG . GLU B 2 32 ? 32.777 -27.254 -60.400 1.00 98.36 ? 32 GLU B CG 1 ATOM 2664 C CD . GLU B 2 32 ? 33.469 -25.968 -59.980 1.00 99.94 ? 32 GLU B CD 1 ATOM 2665 O OE1 . GLU B 2 32 ? 34.324 -25.473 -60.745 1.00 101.22 ? 32 GLU B OE1 1 ATOM 2666 O OE2 . GLU B 2 32 ? 33.171 -25.463 -58.875 1.00 100.67 ? 32 GLU B OE2 1 ATOM 2667 N N . GLY B 2 33 ? 32.122 -30.277 -60.793 1.00 94.97 ? 33 GLY B N 1 ATOM 2668 C CA . GLY B 2 33 ? 31.674 -31.214 -59.757 1.00 93.92 ? 33 GLY B CA 1 ATOM 2669 C C . GLY B 2 33 ? 32.717 -31.372 -58.661 1.00 89.73 ? 33 GLY B C 1 ATOM 2670 O O . GLY B 2 33 ? 33.911 -31.192 -58.909 1.00 87.46 ? 33 GLY B O 1 ATOM 2671 N N . THR B 2 34 ? 32.265 -31.712 -57.453 1.00 89.22 ? 34 THR B N 1 ATOM 2672 C CA . THR B 2 34 ? 33.147 -31.826 -56.282 1.00 85.81 ? 34 THR B CA 1 ATOM 2673 C C . THR B 2 34 ? 32.852 -33.110 -55.489 1.00 84.56 ? 34 THR B C 1 ATOM 2674 O O . THR B 2 34 ? 31.688 -33.443 -55.264 1.00 87.23 ? 34 THR B O 1 ATOM 2675 C CB . THR B 2 34 ? 32.999 -30.610 -55.332 1.00 86.99 ? 34 THR B CB 1 ATOM 2676 O OG1 . THR B 2 34 ? 32.037 -30.900 -54.311 1.00 89.53 ? 34 THR B OG1 1 ATOM 2677 C CG2 . THR B 2 34 ? 32.560 -29.357 -56.084 1.00 90.80 ? 34 THR B CG2 1 ATOM 2678 N N . ALA B 2 35 ? 33.898 -33.816 -55.061 1.00 81.00 ? 35 ALA B N 1 ATOM 2679 C CA . ALA B 2 35 ? 33.730 -35.053 -54.282 1.00 80.67 ? 35 ALA B CA 1 ATOM 2680 C C . ALA B 2 35 ? 34.890 -35.276 -53.318 1.00 77.01 ? 35 ALA B C 1 ATOM 2681 O O . ALA B 2 35 ? 35.990 -34.781 -53.544 1.00 75.30 ? 35 ALA B O 1 ATOM 2682 C CB . ALA B 2 35 ? 33.587 -36.248 -55.209 1.00 82.77 ? 35 ALA B CB 1 ATOM 2683 N N . ALA B 2 36 ? 34.639 -36.039 -52.256 1.00 76.84 ? 36 ALA B N 1 ATOM 2684 C CA . ALA B 2 36 ? 35.640 -36.280 -51.212 1.00 73.69 ? 36 ALA B CA 1 ATOM 2685 C C . ALA B 2 36 ? 36.436 -37.562 -51.444 1.00 74.05 ? 36 ALA B C 1 ATOM 2686 O O . ALA B 2 36 ? 35.910 -38.542 -51.979 1.00 76.59 ? 36 ALA B O 1 ATOM 2687 C CB . ALA B 2 36 ? 34.978 -36.329 -49.846 1.00 73.70 ? 36 ALA B CB 1 ATOM 2688 N N . ASP B 2 37 ? 37.702 -37.541 -51.021 1.00 71.90 ? 37 ASP B N 1 ATOM 2689 C CA . ASP B 2 37 ? 38.565 -38.720 -51.048 1.00 72.69 ? 37 ASP B CA 1 ATOM 2690 C C . ASP B 2 37 ? 38.526 -39.419 -49.689 1.00 72.69 ? 37 ASP B C 1 ATOM 2691 O O . ASP B 2 37 ? 38.982 -38.866 -48.680 1.00 70.33 ? 37 ASP B O 1 ATOM 2692 C CB . ASP B 2 37 ? 40.007 -38.332 -51.390 1.00 71.60 ? 37 ASP B CB 1 ATOM 2693 C CG . ASP B 2 37 ? 40.918 -39.540 -51.520 1.00 73.50 ? 37 ASP B CG 1 ATOM 2694 O OD1 . ASP B 2 37 ? 40.624 -40.425 -52.349 1.00 76.65 ? 37 ASP B OD1 1 ATOM 2695 O OD2 . ASP B 2 37 ? 41.930 -39.611 -50.791 1.00 72.56 ? 37 ASP B OD2 1 ATOM 2696 N N . TYR B 2 38 ? 37.988 -40.637 -49.675 1.00 75.97 ? 38 TYR B N 1 ATOM 2697 C CA . TYR B 2 38 ? 37.820 -41.412 -48.448 1.00 76.67 ? 38 TYR B CA 1 ATOM 2698 C C . TYR B 2 38 ? 39.158 -41.775 -47.794 1.00 73.94 ? 38 TYR B C 1 ATOM 2699 O O . TYR B 2 38 ? 39.351 -41.537 -46.606 1.00 71.47 ? 38 TYR B O 1 ATOM 2700 C CB . TYR B 2 38 ? 37.019 -42.686 -48.748 1.00 82.72 ? 38 TYR B CB 1 ATOM 2701 C CG . TYR B 2 38 ? 36.684 -43.529 -47.534 1.00 85.60 ? 38 TYR B CG 1 ATOM 2702 C CD1 . TYR B 2 38 ? 35.611 -43.199 -46.708 1.00 86.82 ? 38 TYR B CD1 1 ATOM 2703 C CD2 . TYR B 2 38 ? 37.428 -44.664 -47.221 1.00 88.22 ? 38 TYR B CD2 1 ATOM 2704 C CE1 . TYR B 2 38 ? 35.296 -43.970 -45.600 1.00 89.61 ? 38 TYR B CE1 1 ATOM 2705 C CE2 . TYR B 2 38 ? 37.122 -45.440 -46.113 1.00 90.82 ? 38 TYR B CE2 1 ATOM 2706 C CZ . TYR B 2 38 ? 36.056 -45.089 -45.306 1.00 91.34 ? 38 TYR B CZ 1 ATOM 2707 O OH . TYR B 2 38 ? 35.744 -45.854 -44.204 1.00 94.33 ? 38 TYR B OH 1 ATOM 2708 N N . LYS B 2 39 ? 40.074 -42.336 -48.581 1.00 75.18 ? 39 LYS B N 1 ATOM 2709 C CA . LYS B 2 39 ? 41.330 -42.898 -48.062 1.00 74.72 ? 39 LYS B CA 1 ATOM 2710 C C . LYS B 2 39 ? 42.151 -41.865 -47.275 1.00 70.17 ? 39 LYS B C 1 ATOM 2711 O O . LYS B 2 39 ? 42.612 -42.142 -46.165 1.00 68.61 ? 39 LYS B O 1 ATOM 2712 C CB . LYS B 2 39 ? 42.182 -43.472 -49.206 1.00 78.79 ? 39 LYS B CB 1 ATOM 2713 C CG . LYS B 2 39 ? 42.581 -44.931 -49.027 1.00 84.00 ? 39 LYS B CG 1 ATOM 2714 C CD . LYS B 2 39 ? 41.401 -45.863 -49.289 1.00 88.21 ? 39 LYS B CD 1 ATOM 2715 C CE . LYS B 2 39 ? 41.822 -47.321 -49.373 1.00 94.87 ? 39 LYS B CE 1 ATOM 2716 N NZ . LYS B 2 39 ? 42.507 -47.645 -50.653 1.00 99.67 ? 39 LYS B NZ 1 ATOM 2717 N N . SER B 2 40 ? 42.329 -40.682 -47.859 1.00 67.63 ? 40 SER B N 1 ATOM 2718 C CA . SER B 2 40 ? 43.094 -39.605 -47.228 1.00 64.02 ? 40 SER B CA 1 ATOM 2719 C C . SER B 2 40 ? 42.383 -39.075 -45.989 1.00 61.27 ? 40 SER B C 1 ATOM 2720 O O . SER B 2 40 ? 43.002 -38.906 -44.930 1.00 59.26 ? 40 SER B O 1 ATOM 2721 C CB . SER B 2 40 ? 43.308 -38.456 -48.213 1.00 63.91 ? 40 SER B CB 1 ATOM 2722 O OG . SER B 2 40 ? 42.064 -37.965 -48.680 1.00 63.07 ? 40 SER B OG 1 ATOM 2723 N N . THR B 2 41 ? 41.087 -38.802 -46.134 1.00 60.83 ? 41 THR B N 1 ATOM 2724 C CA . THR B 2 41 ? 40.266 -38.349 -45.014 1.00 59.82 ? 41 THR B CA 1 ATOM 2725 C C . THR B 2 41 ? 40.385 -39.328 -43.849 1.00 60.05 ? 41 THR B C 1 ATOM 2726 O O . THR B 2 41 ? 40.606 -38.920 -42.714 1.00 59.03 ? 41 THR B O 1 ATOM 2727 C CB . THR B 2 41 ? 38.786 -38.179 -45.430 1.00 61.62 ? 41 THR B CB 1 ATOM 2728 O OG1 . THR B 2 41 ? 38.653 -37.026 -46.272 1.00 61.23 ? 41 THR B OG1 1 ATOM 2729 C CG2 . THR B 2 41 ? 37.879 -38.006 -44.218 1.00 62.06 ? 41 THR B CG2 1 ATOM 2730 N N . GLN B 2 42 ? 40.277 -40.619 -44.147 1.00 62.57 ? 42 GLN B N 1 ATOM 2731 C CA . GLN B 2 42 ? 40.253 -41.652 -43.113 1.00 63.89 ? 42 GLN B CA 1 ATOM 2732 C C . GLN B 2 42 ? 41.608 -41.834 -42.421 1.00 62.57 ? 42 GLN B C 1 ATOM 2733 O O . GLN B 2 42 ? 41.668 -42.049 -41.208 1.00 61.61 ? 42 GLN B O 1 ATOM 2734 C CB . GLN B 2 42 ? 39.777 -42.979 -43.711 1.00 68.17 ? 42 GLN B CB 1 ATOM 2735 C CG . GLN B 2 42 ? 39.294 -43.990 -42.685 1.00 71.10 ? 42 GLN B CG 1 ATOM 2736 C CD . GLN B 2 42 ? 38.108 -43.494 -41.876 1.00 71.64 ? 42 GLN B CD 1 ATOM 2737 O OE1 . GLN B 2 42 ? 37.349 -42.627 -42.320 1.00 71.51 ? 42 GLN B OE1 1 ATOM 2738 N NE2 . GLN B 2 42 ? 37.943 -44.044 -40.679 1.00 73.00 ? 42 GLN B NE2 1 ATOM 2739 N N . SER B 2 43 ? 42.686 -41.740 -43.193 1.00 62.89 ? 43 SER B N 1 ATOM 2740 C CA . SER B 2 43 ? 44.040 -41.851 -42.657 1.00 62.40 ? 43 SER B CA 1 ATOM 2741 C C . SER B 2 43 ? 44.357 -40.730 -41.659 1.00 59.56 ? 43 SER B C 1 ATOM 2742 O O . SER B 2 43 ? 44.997 -40.970 -40.633 1.00 58.60 ? 43 SER B O 1 ATOM 2743 C CB . SER B 2 43 ? 45.058 -41.835 -43.793 1.00 64.94 ? 43 SER B CB 1 ATOM 2744 O OG . SER B 2 43 ? 46.324 -42.266 -43.334 1.00 67.49 ? 43 SER B OG 1 ATOM 2745 N N . ALA B 2 44 ? 43.907 -39.512 -41.959 1.00 57.49 ? 44 ALA B N 1 ATOM 2746 C CA . ALA B 2 44 ? 44.096 -38.380 -41.049 1.00 55.43 ? 44 ALA B CA 1 ATOM 2747 C C . ALA B 2 44 ? 43.230 -38.529 -39.797 1.00 54.46 ? 44 ALA B C 1 ATOM 2748 O O . ALA B 2 44 ? 43.703 -38.330 -38.681 1.00 54.09 ? 44 ALA B O 1 ATOM 2749 C CB . ALA B 2 44 ? 43.777 -37.072 -41.754 1.00 55.61 ? 44 ALA B CB 1 ATOM 2750 N N . ILE B 2 45 ? 41.962 -38.877 -40.000 1.00 54.84 ? 45 ILE B N 1 ATOM 2751 C CA . ILE B 2 45 ? 41.021 -39.097 -38.908 1.00 55.13 ? 45 ILE B CA 1 ATOM 2752 C C . ILE B 2 45 ? 41.513 -40.181 -37.942 1.00 55.44 ? 45 ILE B C 1 ATOM 2753 O O . ILE B 2 45 ? 41.468 -40.001 -36.726 1.00 54.59 ? 45 ILE B O 1 ATOM 2754 C CB . ILE B 2 45 ? 39.617 -39.457 -39.454 1.00 57.21 ? 45 ILE B CB 1 ATOM 2755 C CG1 . ILE B 2 45 ? 38.961 -38.205 -40.048 1.00 57.76 ? 45 ILE B CG1 1 ATOM 2756 C CG2 . ILE B 2 45 ? 38.729 -40.048 -38.363 1.00 59.35 ? 45 ILE B CG2 1 ATOM 2757 C CD1 . ILE B 2 45 ? 37.615 -38.444 -40.702 1.00 60.58 ? 45 ILE B CD1 1 ATOM 2758 N N . ASP B 2 46 ? 41.975 -41.301 -38.490 1.00 56.94 ? 46 ASP B N 1 ATOM 2759 C CA . ASP B 2 46 ? 42.449 -42.417 -37.673 1.00 58.49 ? 46 ASP B CA 1 ATOM 2760 C C . ASP B 2 46 ? 43.662 -42.033 -36.839 1.00 56.77 ? 46 ASP B C 1 ATOM 2761 O O . ASP B 2 46 ? 43.758 -42.409 -35.672 1.00 57.29 ? 46 ASP B O 1 ATOM 2762 C CB . ASP B 2 46 ? 42.790 -43.630 -38.545 1.00 61.23 ? 46 ASP B CB 1 ATOM 2763 C CG . ASP B 2 46 ? 41.560 -44.299 -39.126 1.00 64.33 ? 46 ASP B CG 1 ATOM 2764 O OD1 . ASP B 2 46 ? 40.430 -43.980 -38.696 1.00 64.31 ? 46 ASP B OD1 1 ATOM 2765 O OD2 . ASP B 2 46 ? 41.728 -45.152 -40.021 1.00 67.69 ? 46 ASP B OD2 1 ATOM 2766 N N . GLN B 2 47 ? 44.580 -41.287 -37.444 1.00 55.94 ? 47 GLN B N 1 ATOM 2767 C CA . GLN B 2 47 ? 45.785 -40.845 -36.753 1.00 55.58 ? 47 GLN B CA 1 ATOM 2768 C C . GLN B 2 47 ? 45.469 -39.869 -35.608 1.00 53.84 ? 47 GLN B C 1 ATOM 2769 O O . GLN B 2 47 ? 46.054 -39.970 -34.527 1.00 52.97 ? 47 GLN B O 1 ATOM 2770 C CB . GLN B 2 47 ? 46.775 -40.213 -37.739 1.00 56.18 ? 47 GLN B CB 1 ATOM 2771 C CG . GLN B 2 47 ? 47.425 -41.199 -38.701 1.00 59.39 ? 47 GLN B CG 1 ATOM 2772 C CD . GLN B 2 47 ? 48.340 -40.512 -39.700 1.00 61.03 ? 47 GLN B CD 1 ATOM 2773 O OE1 . GLN B 2 47 ? 49.481 -40.182 -39.386 1.00 63.00 ? 47 GLN B OE1 1 ATOM 2774 N NE2 . GLN B 2 47 ? 47.843 -40.291 -40.907 1.00 61.72 ? 47 GLN B NE2 1 ATOM 2775 N N . ILE B 2 48 ? 44.549 -38.937 -35.851 1.00 53.59 ? 48 ILE B N 1 ATOM 2776 C CA . ILE B 2 48 ? 44.153 -37.953 -34.836 1.00 53.74 ? 48 ILE B CA 1 ATOM 2777 C C . ILE B 2 48 ? 43.406 -38.630 -33.694 1.00 54.37 ? 48 ILE B C 1 ATOM 2778 O O . ILE B 2 48 ? 43.691 -38.374 -32.526 1.00 55.30 ? 48 ILE B O 1 ATOM 2779 C CB . ILE B 2 48 ? 43.294 -36.801 -35.431 1.00 54.81 ? 48 ILE B CB 1 ATOM 2780 C CG1 . ILE B 2 48 ? 44.173 -35.609 -35.817 1.00 55.06 ? 48 ILE B CG1 1 ATOM 2781 C CG2 . ILE B 2 48 ? 42.256 -36.295 -34.434 1.00 56.65 ? 48 ILE B CG2 1 ATOM 2782 C CD1 . ILE B 2 48 ? 45.040 -35.845 -37.025 1.00 55.03 ? 48 ILE B CD1 1 ATOM 2783 N N . THR B 2 49 ? 42.455 -39.490 -34.027 1.00 55.11 ? 49 THR B N 1 ATOM 2784 C CA . THR B 2 49 ? 41.678 -40.186 -33.006 1.00 57.08 ? 49 THR B CA 1 ATOM 2785 C C . THR B 2 49 ? 42.568 -41.087 -32.144 1.00 56.31 ? 49 THR B C 1 ATOM 2786 O O . THR B 2 49 ? 42.299 -41.285 -30.958 1.00 57.35 ? 49 THR B O 1 ATOM 2787 C CB . THR B 2 49 ? 40.560 -41.030 -33.638 1.00 60.10 ? 49 THR B CB 1 ATOM 2788 O OG1 . THR B 2 49 ? 41.112 -41.823 -34.695 1.00 61.11 ? 49 THR B OG1 1 ATOM 2789 C CG2 . THR B 2 49 ? 39.467 -40.132 -34.199 1.00 61.21 ? 49 THR B CG2 1 ATOM 2790 N N . GLY B 2 50 ? 43.623 -41.630 -32.745 1.00 54.52 ? 50 GLY B N 1 ATOM 2791 C CA . GLY B 2 50 ? 44.609 -42.418 -32.012 1.00 54.53 ? 50 GLY B CA 1 ATOM 2792 C C . GLY B 2 50 ? 45.420 -41.603 -31.010 1.00 52.91 ? 50 GLY B C 1 ATOM 2793 O O . GLY B 2 50 ? 45.862 -42.133 -29.995 1.00 53.13 ? 50 GLY B O 1 ATOM 2794 N N . LYS B 2 51 ? 45.634 -40.319 -31.301 1.00 51.08 ? 51 LYS B N 1 ATOM 2795 C CA . LYS B 2 51 ? 46.247 -39.407 -30.334 1.00 50.49 ? 51 LYS B CA 1 ATOM 2796 C C . LYS B 2 51 ? 45.346 -39.234 -29.134 1.00 51.24 ? 51 LYS B C 1 ATOM 2797 O O . LYS B 2 51 ? 45.806 -39.265 -27.989 1.00 51.48 ? 51 LYS B O 1 ATOM 2798 C CB . LYS B 2 51 ? 46.466 -38.019 -30.922 1.00 50.11 ? 51 LYS B CB 1 ATOM 2799 C CG . LYS B 2 51 ? 47.668 -37.869 -31.815 1.00 50.61 ? 51 LYS B CG 1 ATOM 2800 C CD . LYS B 2 51 ? 47.875 -36.392 -32.088 1.00 51.76 ? 51 LYS B CD 1 ATOM 2801 C CE . LYS B 2 51 ? 49.117 -36.131 -32.905 1.00 53.06 ? 51 LYS B CE 1 ATOM 2802 N NZ . LYS B 2 51 ? 49.478 -34.692 -32.866 1.00 55.61 ? 51 LYS B NZ 1 ATOM 2803 N N . LEU B 2 52 ? 44.064 -39.011 -29.425 1.00 52.46 ? 52 LEU B N 1 ATOM 2804 C CA . LEU B 2 52 ? 43.044 -38.783 -28.410 1.00 54.70 ? 52 LEU B CA 1 ATOM 2805 C C . LEU B 2 52 ? 42.941 -39.933 -27.432 1.00 55.81 ? 52 LEU B C 1 ATOM 2806 O O . LEU B 2 52 ? 43.010 -39.722 -26.224 1.00 57.07 ? 52 LEU B O 1 ATOM 2807 C CB . LEU B 2 52 ? 41.678 -38.553 -29.059 1.00 56.75 ? 52 LEU B CB 1 ATOM 2808 C CG . LEU B 2 52 ? 41.397 -37.110 -29.462 1.00 57.93 ? 52 LEU B CG 1 ATOM 2809 C CD1 . LEU B 2 52 ? 40.281 -37.054 -30.495 1.00 59.76 ? 52 LEU B CD1 1 ATOM 2810 C CD2 . LEU B 2 52 ? 41.043 -36.275 -28.243 1.00 61.03 ? 52 LEU B CD2 1 ATOM 2811 N N . ASN B 2 53 ? 42.782 -41.146 -27.958 1.00 56.52 ? 53 ASN B N 1 ATOM 2812 C CA . ASN B 2 53 ? 42.594 -42.331 -27.118 1.00 59.28 ? 53 ASN B CA 1 ATOM 2813 C C . ASN B 2 53 ? 43.784 -42.528 -26.197 1.00 58.24 ? 53 ASN B C 1 ATOM 2814 O O . ASN B 2 53 ? 43.642 -43.016 -25.084 1.00 59.29 ? 53 ASN B O 1 ATOM 2815 C CB . ASN B 2 53 ? 42.386 -43.589 -27.968 1.00 61.20 ? 53 ASN B CB 1 ATOM 2816 C CG . ASN B 2 53 ? 41.180 -43.487 -28.888 1.00 63.63 ? 53 ASN B CG 1 ATOM 2817 O OD1 . ASN B 2 53 ? 40.235 -42.742 -28.621 1.00 65.28 ? 53 ASN B OD1 1 ATOM 2818 N ND2 . ASN B 2 53 ? 41.214 -44.233 -29.986 1.00 64.74 ? 53 ASN B ND2 1 ATOM 2819 N N . ARG B 2 54 ? 44.954 -42.124 -26.675 1.00 56.67 ? 54 ARG B N 1 ATOM 2820 C CA . ARG B 2 54 ? 46.179 -42.209 -25.901 1.00 57.84 ? 54 ARG B CA 1 ATOM 2821 C C . ARG B 2 54 ? 46.232 -41.172 -24.767 1.00 57.42 ? 54 ARG B C 1 ATOM 2822 O O . ARG B 2 54 ? 46.737 -41.462 -23.691 1.00 56.96 ? 54 ARG B O 1 ATOM 2823 C CB . ARG B 2 54 ? 47.382 -42.016 -26.824 1.00 58.26 ? 54 ARG B CB 1 ATOM 2824 C CG . ARG B 2 54 ? 48.650 -42.738 -26.379 1.00 61.56 ? 54 ARG B CG 1 ATOM 2825 C CD . ARG B 2 54 ? 49.828 -41.782 -26.283 1.00 63.14 ? 54 ARG B CD 1 ATOM 2826 N NE . ARG B 2 54 ? 49.733 -40.734 -27.293 1.00 63.86 ? 54 ARG B NE 1 ATOM 2827 C CZ . ARG B 2 54 ? 50.378 -39.572 -27.250 1.00 64.90 ? 54 ARG B CZ 1 ATOM 2828 N NH1 . ARG B 2 54 ? 51.221 -39.288 -26.253 1.00 66.25 ? 54 ARG B NH1 1 ATOM 2829 N NH2 . ARG B 2 54 ? 50.179 -38.695 -28.231 1.00 64.02 ? 54 ARG B NH2 1 ATOM 2830 N N . LEU B 2 55 ? 45.724 -39.967 -25.015 1.00 57.54 ? 55 LEU B N 1 ATOM 2831 C CA . LEU B 2 55 ? 45.786 -38.888 -24.022 1.00 59.64 ? 55 LEU B CA 1 ATOM 2832 C C . LEU B 2 55 ? 44.587 -38.868 -23.090 1.00 63.05 ? 55 LEU B C 1 ATOM 2833 O O . LEU B 2 55 ? 44.726 -38.549 -21.915 1.00 63.40 ? 55 LEU B O 1 ATOM 2834 C CB . LEU B 2 55 ? 45.882 -37.528 -24.707 1.00 59.75 ? 55 LEU B CB 1 ATOM 2835 C CG . LEU B 2 55 ? 47.127 -37.312 -25.546 1.00 58.46 ? 55 LEU B CG 1 ATOM 2836 C CD1 . LEU B 2 55 ? 47.045 -35.963 -26.235 1.00 59.90 ? 55 LEU B CD1 1 ATOM 2837 C CD2 . LEU B 2 55 ? 48.374 -37.422 -24.687 1.00 59.43 ? 55 LEU B CD2 1 ATOM 2838 N N . ILE B 2 56 ? 43.408 -39.174 -23.623 1.00 66.39 ? 56 ILE B N 1 ATOM 2839 C CA . ILE B 2 56 ? 42.186 -39.188 -22.818 1.00 72.48 ? 56 ILE B CA 1 ATOM 2840 C C . ILE B 2 56 ? 42.151 -40.517 -22.081 1.00 76.22 ? 56 ILE B C 1 ATOM 2841 O O . ILE B 2 56 ? 41.480 -41.468 -22.475 1.00 78.41 ? 56 ILE B O 1 ATOM 2842 C CB . ILE B 2 56 ? 40.907 -38.916 -23.654 1.00 74.37 ? 56 ILE B CB 1 ATOM 2843 C CG1 . ILE B 2 56 ? 40.787 -37.421 -23.966 1.00 75.44 ? 56 ILE B CG1 1 ATOM 2844 C CG2 . ILE B 2 56 ? 39.638 -39.328 -22.909 1.00 79.69 ? 56 ILE B CG2 1 ATOM 2845 C CD1 . ILE B 2 56 ? 41.960 -36.822 -24.713 1.00 71.83 ? 56 ILE B CD1 1 ATOM 2846 N N . GLU B 2 57 ? 42.945 -40.567 -21.021 1.00 79.54 ? 57 GLU B N 1 ATOM 2847 C CA . GLU B 2 57 ? 42.923 -41.659 -20.077 1.00 83.65 ? 57 GLU B CA 1 ATOM 2848 C C . GLU B 2 57 ? 43.405 -41.086 -18.746 1.00 85.62 ? 57 GLU B C 1 ATOM 2849 O O . GLU B 2 57 ? 44.201 -40.139 -18.713 1.00 83.64 ? 57 GLU B O 1 ATOM 2850 C CB . GLU B 2 57 ? 43.787 -42.834 -20.568 1.00 82.97 ? 57 GLU B CB 1 ATOM 2851 C CG . GLU B 2 57 ? 45.297 -42.671 -20.395 1.00 81.23 ? 57 GLU B CG 1 ATOM 2852 C CD . GLU B 2 57 ? 45.812 -43.182 -19.057 1.00 83.27 ? 57 GLU B CD 1 ATOM 2853 O OE1 . GLU B 2 57 ? 45.140 -44.037 -18.442 1.00 87.90 ? 57 GLU B OE1 1 ATOM 2854 O OE2 . GLU B 2 57 ? 46.891 -42.731 -18.615 1.00 82.08 ? 57 GLU B OE2 1 ATOM 2855 N N . LYS B 2 58 ? 42.886 -41.643 -17.659 1.00 89.85 ? 58 LYS B N 1 ATOM 2856 C CA . LYS B 2 58 ? 43.277 -41.247 -16.316 1.00 91.88 ? 58 LYS B CA 1 ATOM 2857 C C . LYS B 2 58 ? 44.015 -42.421 -15.679 1.00 91.72 ? 58 LYS B C 1 ATOM 2858 O O . LYS B 2 58 ? 43.704 -43.583 -15.959 1.00 92.24 ? 58 LYS B O 1 ATOM 2859 C CB . LYS B 2 58 ? 42.035 -40.896 -15.503 1.00 97.49 ? 58 LYS B CB 1 ATOM 2860 C CG . LYS B 2 58 ? 42.311 -40.108 -14.237 1.00 99.38 ? 58 LYS B CG 1 ATOM 2861 C CD . LYS B 2 58 ? 41.294 -40.430 -13.153 1.00 105.48 ? 58 LYS B CD 1 ATOM 2862 C CE . LYS B 2 58 ? 39.861 -40.147 -13.584 1.00 109.86 ? 58 LYS B CE 1 ATOM 2863 N NZ . LYS B 2 58 ? 38.887 -40.539 -12.530 1.00 116.45 ? 58 LYS B NZ 1 ATOM 2864 N N . THR B 2 59 ? 44.987 -42.115 -14.824 1.00 91.52 ? 59 THR B N 1 ATOM 2865 C CA . THR B 2 59 ? 45.824 -43.147 -14.214 1.00 91.19 ? 59 THR B CA 1 ATOM 2866 C C . THR B 2 59 ? 45.112 -43.809 -13.047 1.00 95.09 ? 59 THR B C 1 ATOM 2867 O O . THR B 2 59 ? 44.298 -43.186 -12.370 1.00 98.02 ? 59 THR B O 1 ATOM 2868 C CB . THR B 2 59 ? 47.173 -42.579 -13.721 1.00 90.22 ? 59 THR B CB 1 ATOM 2869 O OG1 . THR B 2 59 ? 46.960 -41.691 -12.615 1.00 92.29 ? 59 THR B OG1 1 ATOM 2870 C CG2 . THR B 2 59 ? 47.894 -41.841 -14.857 1.00 86.79 ? 59 THR B CG2 1 ATOM 2871 N N . ASN B 2 60 ? 45.447 -45.074 -12.811 1.00 63.71 ? 60 ASN B N 1 ATOM 2872 C CA . ASN B 2 60 ? 44.885 -45.847 -11.699 1.00 64.88 ? 60 ASN B CA 1 ATOM 2873 C C . ASN B 2 60 ? 45.634 -45.577 -10.383 1.00 60.69 ? 60 ASN B C 1 ATOM 2874 O O . ASN B 2 60 ? 45.506 -46.344 -9.419 1.00 62.19 ? 60 ASN B O 1 ATOM 2875 C CB . ASN B 2 60 ? 44.925 -47.351 -12.033 1.00 69.13 ? 60 ASN B CB 1 ATOM 2876 C CG . ASN B 2 60 ? 43.880 -48.159 -11.272 1.00 73.32 ? 60 ASN B CG 1 ATOM 2877 O OD1 . ASN B 2 60 ? 42.733 -48.285 -11.706 1.00 74.95 ? 60 ASN B OD1 1 ATOM 2878 N ND2 . ASN B 2 60 ? 44.283 -48.728 -10.141 1.00 75.06 ? 60 ASN B ND2 1 ATOM 2879 N N . GLN B 2 61 ? 46.412 -44.497 -10.341 1.00 54.29 ? 61 GLN B N 1 ATOM 2880 C CA . GLN B 2 61 ? 47.251 -44.205 -9.183 1.00 51.24 ? 61 GLN B CA 1 ATOM 2881 C C . GLN B 2 61 ? 46.458 -43.432 -8.137 1.00 46.70 ? 61 GLN B C 1 ATOM 2882 O O . GLN B 2 61 ? 45.980 -42.332 -8.391 1.00 43.17 ? 61 GLN B O 1 ATOM 2883 C CB . GLN B 2 61 ? 48.486 -43.414 -9.606 1.00 51.21 ? 61 GLN B CB 1 ATOM 2884 C CG . GLN B 2 61 ? 49.332 -42.896 -8.453 1.00 52.40 ? 61 GLN B CG 1 ATOM 2885 C CD . GLN B 2 61 ? 50.405 -43.866 -8.007 1.00 56.40 ? 61 GLN B CD 1 ATOM 2886 O OE1 . GLN B 2 61 ? 50.114 -44.993 -7.565 1.00 58.83 ? 61 GLN B OE1 1 ATOM 2887 N NE2 . GLN B 2 61 ? 51.673 -43.432 -8.120 1.00 56.44 ? 61 GLN B NE2 1 ATOM 2888 N N . GLN B 2 62 ? 46.329 -44.014 -6.954 1.00 45.73 ? 62 GLN B N 1 ATOM 2889 C CA . GLN B 2 62 ? 45.579 -43.382 -5.890 1.00 45.65 ? 62 GLN B CA 1 ATOM 2890 C C . GLN B 2 62 ? 46.476 -42.517 -5.020 1.00 42.21 ? 62 GLN B C 1 ATOM 2891 O O . GLN B 2 62 ? 47.586 -42.907 -4.688 1.00 41.30 ? 62 GLN B O 1 ATOM 2892 C CB . GLN B 2 62 ? 44.880 -44.428 -5.031 1.00 48.61 ? 62 GLN B CB 1 ATOM 2893 C CG . GLN B 2 62 ? 44.041 -43.808 -3.933 1.00 50.23 ? 62 GLN B CG 1 ATOM 2894 C CD . GLN B 2 62 ? 42.911 -44.694 -3.500 1.00 54.81 ? 62 GLN B CD 1 ATOM 2895 O OE1 . GLN B 2 62 ? 42.924 -45.240 -2.395 1.00 58.76 ? 62 GLN B OE1 1 ATOM 2896 N NE2 . GLN B 2 62 ? 41.922 -44.857 -4.375 1.00 57.21 ? 62 GLN B NE2 1 ATOM 2897 N N . PHE B 2 63 ? 45.978 -41.341 -4.661 1.00 40.56 ? 63 PHE B N 1 ATOM 2898 C CA . PHE B 2 63 ? 46.623 -40.482 -3.666 1.00 38.88 ? 63 PHE B CA 1 ATOM 2899 C C . PHE B 2 63 ? 45.650 -40.203 -2.517 1.00 39.58 ? 63 PHE B C 1 ATOM 2900 O O . PHE B 2 63 ? 44.438 -40.091 -2.736 1.00 39.82 ? 63 PHE B O 1 ATOM 2901 C CB . PHE B 2 63 ? 47.079 -39.172 -4.304 1.00 36.63 ? 63 PHE B CB 1 ATOM 2902 C CG . PHE B 2 63 ? 48.274 -39.319 -5.196 1.00 36.35 ? 63 PHE B CG 1 ATOM 2903 C CD1 . PHE B 2 63 ? 48.120 -39.624 -6.541 1.00 37.68 ? 63 PHE B CD1 1 ATOM 2904 C CD2 . PHE B 2 63 ? 49.559 -39.158 -4.695 1.00 36.17 ? 63 PHE B CD2 1 ATOM 2905 C CE1 . PHE B 2 63 ? 49.219 -39.775 -7.368 1.00 36.32 ? 63 PHE B CE1 1 ATOM 2906 C CE2 . PHE B 2 63 ? 50.665 -39.291 -5.516 1.00 35.88 ? 63 PHE B CE2 1 ATOM 2907 C CZ . PHE B 2 63 ? 50.494 -39.611 -6.856 1.00 36.07 ? 63 PHE B CZ 1 ATOM 2908 N N . GLU B 2 64 ? 46.191 -40.087 -1.305 1.00 39.73 ? 64 GLU B N 1 ATOM 2909 C CA . GLU B 2 64 ? 45.403 -39.786 -0.107 1.00 41.67 ? 64 GLU B CA 1 ATOM 2910 C C . GLU B 2 64 ? 45.702 -38.380 0.393 1.00 39.69 ? 64 GLU B C 1 ATOM 2911 O O . GLU B 2 64 ? 46.712 -37.772 0.028 1.00 36.20 ? 64 GLU B O 1 ATOM 2912 C CB . GLU B 2 64 ? 45.723 -40.736 1.052 1.00 44.76 ? 64 GLU B CB 1 ATOM 2913 C CG . GLU B 2 64 ? 46.288 -42.096 0.693 1.00 47.75 ? 64 GLU B CG 1 ATOM 2914 C CD . GLU B 2 64 ? 45.309 -42.943 -0.057 1.00 52.15 ? 64 GLU B CD 1 ATOM 2915 O OE1 . GLU B 2 64 ? 44.115 -42.913 0.306 1.00 58.14 ? 64 GLU B OE1 1 ATOM 2916 O OE2 . GLU B 2 64 ? 45.742 -43.646 -0.997 1.00 55.58 ? 64 GLU B OE2 1 ATOM 2917 N N . LEU B 2 65 ? 44.822 -37.895 1.263 1.00 40.07 ? 65 LEU B N 1 ATOM 2918 C CA . LEU B 2 65 ? 45.082 -36.702 2.080 1.00 39.81 ? 65 LEU B CA 1 ATOM 2919 C C . LEU B 2 65 ? 46.400 -36.816 2.859 1.00 38.55 ? 65 LEU B C 1 ATOM 2920 O O . LEU B 2 65 ? 46.643 -37.835 3.491 1.00 37.61 ? 65 LEU B O 1 ATOM 2921 C CB . LEU B 2 65 ? 43.922 -36.513 3.084 1.00 41.90 ? 65 LEU B CB 1 ATOM 2922 C CG . LEU B 2 65 ? 42.835 -35.456 2.846 1.00 43.08 ? 65 LEU B CG 1 ATOM 2923 C CD1 . LEU B 2 65 ? 42.676 -35.057 1.393 1.00 42.81 ? 65 LEU B CD1 1 ATOM 2924 C CD2 . LEU B 2 65 ? 41.500 -35.923 3.403 1.00 46.15 ? 65 LEU B CD2 1 ATOM 2925 N N . ILE B 2 66 ? 47.253 -35.787 2.785 1.00 38.80 ? 66 ILE B N 1 ATOM 2926 C CA . ILE B 2 66 ? 48.359 -35.617 3.761 1.00 39.32 ? 66 ILE B CA 1 ATOM 2927 C C . ILE B 2 66 ? 48.243 -34.340 4.616 1.00 37.92 ? 66 ILE B C 1 ATOM 2928 O O . ILE B 2 66 ? 49.089 -34.101 5.469 1.00 36.71 ? 66 ILE B O 1 ATOM 2929 C CB . ILE B 2 66 ? 49.795 -35.727 3.160 1.00 39.85 ? 66 ILE B CB 1 ATOM 2930 C CG1 . ILE B 2 66 ? 49.870 -35.195 1.738 1.00 40.61 ? 66 ILE B CG1 1 ATOM 2931 C CG2 . ILE B 2 66 ? 50.281 -37.170 3.196 1.00 40.77 ? 66 ILE B CG2 1 ATOM 2932 C CD1 . ILE B 2 66 ? 49.572 -33.722 1.629 1.00 42.09 ? 66 ILE B CD1 1 ATOM 2933 N N . ASP B 2 67 ? 47.201 -33.537 4.399 1.00 37.99 ? 67 ASP B N 1 ATOM 2934 C CA . ASP B 2 67 ? 46.884 -32.432 5.302 1.00 38.17 ? 67 ASP B CA 1 ATOM 2935 C C . ASP B 2 67 ? 45.388 -32.356 5.560 1.00 40.80 ? 67 ASP B C 1 ATOM 2936 O O . ASP B 2 67 ? 44.644 -33.274 5.204 1.00 42.84 ? 67 ASP B O 1 ATOM 2937 C CB . ASP B 2 67 ? 47.485 -31.089 4.823 1.00 37.66 ? 67 ASP B CB 1 ATOM 2938 C CG . ASP B 2 67 ? 47.085 -30.707 3.400 1.00 36.79 ? 67 ASP B CG 1 ATOM 2939 O OD1 . ASP B 2 67 ? 46.111 -31.251 2.837 1.00 37.57 ? 67 ASP B OD1 1 ATOM 2940 O OD2 . ASP B 2 67 ? 47.762 -29.822 2.843 1.00 35.05 ? 67 ASP B OD2 1 ATOM 2941 N N . ASN B 2 68 ? 44.952 -31.282 6.206 1.00 42.38 ? 68 ASN B N 1 ATOM 2942 C CA . ASN B 2 68 ? 43.634 -31.234 6.806 1.00 44.57 ? 68 ASN B CA 1 ATOM 2943 C C . ASN B 2 68 ? 43.029 -29.846 6.662 1.00 46.89 ? 68 ASN B C 1 ATOM 2944 O O . ASN B 2 68 ? 43.668 -28.832 6.946 1.00 47.23 ? 68 ASN B O 1 ATOM 2945 C CB . ASN B 2 68 ? 43.745 -31.632 8.276 1.00 45.04 ? 68 ASN B CB 1 ATOM 2946 C CG . ASN B 2 68 ? 42.398 -31.851 8.933 1.00 47.53 ? 68 ASN B CG 1 ATOM 2947 O OD1 . ASN B 2 68 ? 41.390 -31.307 8.500 1.00 50.23 ? 68 ASN B OD1 1 ATOM 2948 N ND2 . ASN B 2 68 ? 42.379 -32.642 9.998 1.00 48.18 ? 68 ASN B ND2 1 ATOM 2949 N N . GLU B 2 69 ? 41.779 -29.830 6.232 1.00 49.07 ? 69 GLU B N 1 ATOM 2950 C CA . GLU B 2 69 ? 41.077 -28.627 5.830 1.00 51.89 ? 69 GLU B CA 1 ATOM 2951 C C . GLU B 2 69 ? 40.181 -28.113 6.949 1.00 54.94 ? 69 GLU B C 1 ATOM 2952 O O . GLU B 2 69 ? 39.681 -26.998 6.876 1.00 57.23 ? 69 GLU B O 1 ATOM 2953 C CB . GLU B 2 69 ? 40.241 -28.980 4.603 1.00 53.24 ? 69 GLU B CB 1 ATOM 2954 C CG . GLU B 2 69 ? 39.546 -27.842 3.890 1.00 55.91 ? 69 GLU B CG 1 ATOM 2955 C CD . GLU B 2 69 ? 38.946 -28.299 2.568 1.00 56.53 ? 69 GLU B CD 1 ATOM 2956 O OE1 . GLU B 2 69 ? 39.632 -29.031 1.816 1.00 53.95 ? 69 GLU B OE1 1 ATOM 2957 O OE2 . GLU B 2 69 ? 37.788 -27.942 2.285 1.00 58.20 ? 69 GLU B OE2 1 ATOM 2958 N N . PHE B 2 70 ? 39.955 -28.943 7.966 1.00 55.64 ? 70 PHE B N 1 ATOM 2959 C CA . PHE B 2 70 ? 39.126 -28.575 9.113 1.00 58.39 ? 70 PHE B CA 1 ATOM 2960 C C . PHE B 2 70 ? 39.963 -28.368 10.369 1.00 58.61 ? 70 PHE B C 1 ATOM 2961 O O . PHE B 2 70 ? 39.511 -27.733 11.314 1.00 61.27 ? 70 PHE B O 1 ATOM 2962 C CB . PHE B 2 70 ? 38.084 -29.663 9.411 1.00 59.42 ? 70 PHE B CB 1 ATOM 2963 C CG . PHE B 2 70 ? 37.115 -29.948 8.285 1.00 59.75 ? 70 PHE B CG 1 ATOM 2964 C CD1 . PHE B 2 70 ? 36.953 -29.083 7.207 1.00 59.49 ? 70 PHE B CD1 1 ATOM 2965 C CD2 . PHE B 2 70 ? 36.347 -31.106 8.320 1.00 61.02 ? 70 PHE B CD2 1 ATOM 2966 C CE1 . PHE B 2 70 ? 36.051 -29.370 6.196 1.00 60.30 ? 70 PHE B CE1 1 ATOM 2967 C CE2 . PHE B 2 70 ? 35.439 -31.394 7.312 1.00 62.23 ? 70 PHE B CE2 1 ATOM 2968 C CZ . PHE B 2 70 ? 35.289 -30.524 6.251 1.00 61.94 ? 70 PHE B CZ 1 ATOM 2969 N N . ASN B 2 71 ? 41.169 -28.921 10.385 1.00 57.01 ? 71 ASN B N 1 ATOM 2970 C CA . ASN B 2 71 ? 42.012 -28.913 11.570 1.00 58.15 ? 71 ASN B CA 1 ATOM 2971 C C . ASN B 2 71 ? 43.460 -28.850 11.122 1.00 54.44 ? 71 ASN B C 1 ATOM 2972 O O . ASN B 2 71 ? 44.110 -29.878 10.939 1.00 52.16 ? 71 ASN B O 1 ATOM 2973 C CB . ASN B 2 71 ? 41.740 -30.170 12.405 1.00 60.84 ? 71 ASN B CB 1 ATOM 2974 C CG . ASN B 2 71 ? 41.825 -29.915 13.897 1.00 64.49 ? 71 ASN B CG 1 ATOM 2975 O OD1 . ASN B 2 71 ? 42.805 -29.347 14.395 1.00 65.11 ? 71 ASN B OD1 1 ATOM 2976 N ND2 . ASN B 2 71 ? 40.790 -30.344 14.626 1.00 67.65 ? 71 ASN B ND2 1 ATOM 2977 N N . GLU B 2 72 ? 43.953 -27.629 10.937 1.00 53.97 ? 72 GLU B N 1 ATOM 2978 C CA . GLU B 2 72 ? 45.245 -27.400 10.304 1.00 51.51 ? 72 GLU B CA 1 ATOM 2979 C C . GLU B 2 72 ? 46.355 -28.225 10.934 1.00 48.13 ? 72 GLU B C 1 ATOM 2980 O O . GLU B 2 72 ? 46.467 -28.299 12.150 1.00 47.71 ? 72 GLU B O 1 ATOM 2981 C CB . GLU B 2 72 ? 45.625 -25.920 10.342 1.00 54.58 ? 72 GLU B CB 1 ATOM 2982 C CG . GLU B 2 72 ? 46.643 -25.554 9.269 1.00 54.65 ? 72 GLU B CG 1 ATOM 2983 C CD . GLU B 2 72 ? 47.241 -24.167 9.436 1.00 57.89 ? 72 GLU B CD 1 ATOM 2984 O OE1 . GLU B 2 72 ? 47.029 -23.526 10.492 1.00 60.93 ? 72 GLU B OE1 1 ATOM 2985 O OE2 . GLU B 2 72 ? 47.932 -23.714 8.499 1.00 58.74 ? 72 GLU B OE2 1 ATOM 2986 N N . VAL B 2 73 ? 47.171 -28.853 10.095 1.00 45.64 ? 73 VAL B N 1 ATOM 2987 C CA . VAL B 2 73 ? 48.344 -29.573 10.586 1.00 44.45 ? 73 VAL B CA 1 ATOM 2988 C C . VAL B 2 73 ? 49.383 -28.574 11.084 1.00 44.46 ? 73 VAL B C 1 ATOM 2989 O O . VAL B 2 73 ? 49.302 -27.384 10.782 1.00 43.22 ? 73 VAL B O 1 ATOM 2990 C CB . VAL B 2 73 ? 48.985 -30.478 9.514 1.00 42.52 ? 73 VAL B CB 1 ATOM 2991 C CG1 . VAL B 2 73 ? 47.966 -31.475 8.980 1.00 42.63 ? 73 VAL B CG1 1 ATOM 2992 C CG2 . VAL B 2 73 ? 49.599 -29.649 8.386 1.00 41.64 ? 73 VAL B CG2 1 ATOM 2993 N N . GLU B 2 74 ? 50.341 -29.077 11.859 1.00 45.67 ? 74 GLU B N 1 ATOM 2994 C CA . GLU B 2 74 ? 51.462 -28.281 12.367 1.00 47.48 ? 74 GLU B CA 1 ATOM 2995 C C . GLU B 2 74 ? 52.109 -27.479 11.231 1.00 46.32 ? 74 GLU B C 1 ATOM 2996 O O . GLU B 2 74 ? 52.230 -27.961 10.113 1.00 44.39 ? 74 GLU B O 1 ATOM 2997 C CB . GLU B 2 74 ? 52.488 -29.198 13.047 1.00 48.17 ? 74 GLU B CB 1 ATOM 2998 C CG . GLU B 2 74 ? 53.631 -28.477 13.750 1.00 50.72 ? 74 GLU B CG 1 ATOM 2999 C CD . GLU B 2 74 ? 54.823 -28.180 12.849 1.00 50.89 ? 74 GLU B CD 1 ATOM 3000 O OE1 . GLU B 2 74 ? 55.132 -29.002 11.943 1.00 49.59 ? 74 GLU B OE1 1 ATOM 3001 O OE2 . GLU B 2 74 ? 55.460 -27.118 13.063 1.00 51.87 ? 74 GLU B OE2 1 ATOM 3002 N N . LYS B 2 75 ? 52.535 -26.260 11.535 1.00 48.37 ? 75 LYS B N 1 ATOM 3003 C CA . LYS B 2 75 ? 52.932 -25.300 10.509 1.00 48.84 ? 75 LYS B CA 1 ATOM 3004 C C . LYS B 2 75 ? 54.144 -25.744 9.680 1.00 45.28 ? 75 LYS B C 1 ATOM 3005 O O . LYS B 2 75 ? 54.117 -25.683 8.453 1.00 43.89 ? 75 LYS B O 1 ATOM 3006 C CB . LYS B 2 75 ? 53.195 -23.935 11.145 1.00 53.73 ? 75 LYS B CB 1 ATOM 3007 C CG . LYS B 2 75 ? 52.923 -22.764 10.216 1.00 57.80 ? 75 LYS B CG 1 ATOM 3008 C CD . LYS B 2 75 ? 51.434 -22.461 10.122 1.00 60.87 ? 75 LYS B CD 1 ATOM 3009 C CE . LYS B 2 75 ? 51.156 -21.352 9.115 1.00 64.35 ? 75 LYS B CE 1 ATOM 3010 N NZ . LYS B 2 75 ? 49.718 -20.952 9.087 1.00 67.90 ? 75 LYS B NZ 1 ATOM 3011 N N . GLN B 2 76 ? 55.204 -26.189 10.340 1.00 44.36 ? 76 GLN B N 1 ATOM 3012 C CA . GLN B 2 76 ? 56.409 -26.619 9.622 1.00 42.58 ? 76 GLN B CA 1 ATOM 3013 C C . GLN B 2 76 ? 56.103 -27.732 8.620 1.00 39.68 ? 76 GLN B C 1 ATOM 3014 O O . GLN B 2 76 ? 56.453 -27.622 7.451 1.00 37.18 ? 76 GLN B O 1 ATOM 3015 C CB . GLN B 2 76 ? 57.515 -27.063 10.586 1.00 43.53 ? 76 GLN B CB 1 ATOM 3016 C CG . GLN B 2 76 ? 58.821 -27.394 9.876 1.00 44.07 ? 76 GLN B CG 1 ATOM 3017 C CD . GLN B 2 76 ? 60.009 -27.511 10.814 1.00 45.69 ? 76 GLN B CD 1 ATOM 3018 O OE1 . GLN B 2 76 ? 59.949 -28.201 11.831 1.00 46.66 ? 76 GLN B OE1 1 ATOM 3019 N NE2 . GLN B 2 76 ? 61.102 -26.846 10.468 1.00 46.77 ? 76 GLN B NE2 1 ATOM 3020 N N . ILE B 2 77 ? 55.442 -28.797 9.068 1.00 39.47 ? 77 ILE B N 1 ATOM 3021 C CA . ILE B 2 77 ? 55.118 -29.896 8.159 1.00 38.35 ? 77 ILE B CA 1 ATOM 3022 C C . ILE B 2 77 ? 54.144 -29.407 7.073 1.00 36.45 ? 77 ILE B C 1 ATOM 3023 O O . ILE B 2 77 ? 54.269 -29.781 5.910 1.00 34.56 ? 77 ILE B O 1 ATOM 3024 C CB . ILE B 2 77 ? 54.602 -31.153 8.908 1.00 39.73 ? 77 ILE B CB 1 ATOM 3025 C CG1 . ILE B 2 77 ? 54.588 -32.376 7.986 1.00 39.77 ? 77 ILE B CG1 1 ATOM 3026 C CG2 . ILE B 2 77 ? 53.216 -30.934 9.497 1.00 40.47 ? 77 ILE B CG2 1 ATOM 3027 C CD1 . ILE B 2 77 ? 55.968 -32.854 7.585 1.00 40.85 ? 77 ILE B CD1 1 ATOM 3028 N N . GLY B 2 78 ? 53.207 -28.544 7.451 1.00 36.95 ? 78 GLY B N 1 ATOM 3029 C CA . GLY B 2 78 ? 52.273 -27.944 6.504 1.00 35.95 ? 78 GLY B CA 1 ATOM 3030 C C . GLY B 2 78 ? 52.938 -27.151 5.391 1.00 35.08 ? 78 GLY B C 1 ATOM 3031 O O . GLY B 2 78 ? 52.555 -27.277 4.217 1.00 34.17 ? 78 GLY B O 1 ATOM 3032 N N . ASN B 2 79 ? 53.933 -26.340 5.749 1.00 34.80 ? 79 ASN B N 1 ATOM 3033 C CA . ASN B 2 79 ? 54.727 -25.607 4.751 1.00 34.52 ? 79 ASN B CA 1 ATOM 3034 C C . ASN B 2 79 ? 55.569 -26.509 3.817 1.00 32.91 ? 79 ASN B C 1 ATOM 3035 O O . ASN B 2 79 ? 55.691 -26.236 2.619 1.00 31.89 ? 79 ASN B O 1 ATOM 3036 C CB . ASN B 2 79 ? 55.606 -24.549 5.431 1.00 35.75 ? 79 ASN B CB 1 ATOM 3037 C CG . ASN B 2 79 ? 54.820 -23.311 5.849 1.00 37.64 ? 79 ASN B CG 1 ATOM 3038 O OD1 . ASN B 2 79 ? 53.724 -23.061 5.356 1.00 38.26 ? 79 ASN B OD1 1 ATOM 3039 N ND2 . ASN B 2 79 ? 55.382 -22.529 6.759 1.00 39.60 ? 79 ASN B ND2 1 ATOM 3040 N N . VAL B 2 80 ? 56.129 -27.587 4.343 1.00 32.52 ? 80 VAL B N 1 ATOM 3041 C CA . VAL B 2 80 ? 56.813 -28.558 3.482 1.00 32.14 ? 80 VAL B CA 1 ATOM 3042 C C . VAL B 2 80 ? 55.825 -29.183 2.484 1.00 31.41 ? 80 VAL B C 1 ATOM 3043 O O . VAL B 2 80 ? 56.111 -29.288 1.299 1.00 31.51 ? 80 VAL B O 1 ATOM 3044 C CB . VAL B 2 80 ? 57.507 -29.661 4.298 1.00 32.46 ? 80 VAL B CB 1 ATOM 3045 C CG1 . VAL B 2 80 ? 58.038 -30.759 3.382 1.00 32.20 ? 80 VAL B CG1 1 ATOM 3046 C CG2 . VAL B 2 80 ? 58.637 -29.072 5.124 1.00 33.80 ? 80 VAL B CG2 1 ATOM 3047 N N . ILE B 2 81 ? 54.656 -29.583 2.967 1.00 31.86 ? 81 ILE B N 1 ATOM 3048 C CA . ILE B 2 81 ? 53.619 -30.188 2.117 1.00 30.66 ? 81 ILE B CA 1 ATOM 3049 C C . ILE B 2 81 ? 53.167 -29.253 0.980 1.00 32.04 ? 81 ILE B C 1 ATOM 3050 O O . ILE B 2 81 ? 53.056 -29.666 -0.181 1.00 31.02 ? 81 ILE B O 1 ATOM 3051 C CB . ILE B 2 81 ? 52.401 -30.573 2.979 1.00 31.10 ? 81 ILE B CB 1 ATOM 3052 C CG1 . ILE B 2 81 ? 52.730 -31.806 3.839 1.00 30.84 ? 81 ILE B CG1 1 ATOM 3053 C CG2 . ILE B 2 81 ? 51.162 -30.809 2.117 1.00 31.26 ? 81 ILE B CG2 1 ATOM 3054 C CD1 . ILE B 2 81 ? 51.757 -32.048 4.972 1.00 31.69 ? 81 ILE B CD1 1 ATOM 3055 N N . ASN B 2 82 ? 52.889 -28.001 1.332 1.00 33.67 ? 82 ASN B N 1 ATOM 3056 C CA . ASN B 2 82 ? 52.458 -26.997 0.371 1.00 35.58 ? 82 ASN B CA 1 ATOM 3057 C C . ASN B 2 82 ? 53.527 -26.682 -0.686 1.00 33.91 ? 82 ASN B C 1 ATOM 3058 O O . ASN B 2 82 ? 53.230 -26.508 -1.856 1.00 32.77 ? 82 ASN B O 1 ATOM 3059 C CB . ASN B 2 82 ? 52.065 -25.708 1.113 1.00 39.61 ? 82 ASN B CB 1 ATOM 3060 C CG . ASN B 2 82 ? 50.676 -25.783 1.736 1.00 45.26 ? 82 ASN B CG 1 ATOM 3061 O OD1 . ASN B 2 82 ? 50.061 -26.855 1.834 1.00 42.52 ? 82 ASN B OD1 1 ATOM 3062 N ND2 . ASN B 2 82 ? 50.171 -24.619 2.163 1.00 53.84 ? 82 ASN B ND2 1 ATOM 3063 N N . TRP B 2 83 ? 54.765 -26.581 -0.239 1.00 34.68 ? 83 TRP B N 1 ATOM 3064 C CA . TRP B 2 83 ? 55.910 -26.333 -1.105 1.00 34.77 ? 83 TRP B CA 1 ATOM 3065 C C . TRP B 2 83 ? 56.048 -27.469 -2.100 1.00 32.38 ? 83 TRP B C 1 ATOM 3066 O O . TRP B 2 83 ? 56.191 -27.232 -3.291 1.00 31.48 ? 83 TRP B O 1 ATOM 3067 C CB . TRP B 2 83 ? 57.149 -26.195 -0.225 1.00 36.34 ? 83 TRP B CB 1 ATOM 3068 C CG . TRP B 2 83 ? 58.488 -26.139 -0.886 1.00 37.41 ? 83 TRP B CG 1 ATOM 3069 C CD1 . TRP B 2 83 ? 59.078 -25.059 -1.465 1.00 38.83 ? 83 TRP B CD1 1 ATOM 3070 C CD2 . TRP B 2 83 ? 59.445 -27.199 -0.935 1.00 37.97 ? 83 TRP B CD2 1 ATOM 3071 N NE1 . TRP B 2 83 ? 60.340 -25.387 -1.902 1.00 40.09 ? 83 TRP B NE1 1 ATOM 3072 C CE2 . TRP B 2 83 ? 60.590 -26.697 -1.585 1.00 39.64 ? 83 TRP B CE2 1 ATOM 3073 C CE3 . TRP B 2 83 ? 59.439 -28.531 -0.500 1.00 38.30 ? 83 TRP B CE3 1 ATOM 3074 C CZ2 . TRP B 2 83 ? 61.724 -27.484 -1.825 1.00 40.90 ? 83 TRP B CZ2 1 ATOM 3075 C CZ3 . TRP B 2 83 ? 60.569 -29.318 -0.730 1.00 40.05 ? 83 TRP B CZ3 1 ATOM 3076 C CH2 . TRP B 2 83 ? 61.700 -28.786 -1.383 1.00 41.22 ? 83 TRP B CH2 1 ATOM 3077 N N . THR B 2 84 ? 55.946 -28.699 -1.607 1.00 32.03 ? 84 THR B N 1 ATOM 3078 C CA . THR B 2 84 ? 56.000 -29.887 -2.461 1.00 31.47 ? 84 THR B CA 1 ATOM 3079 C C . THR B 2 84 ? 54.822 -29.936 -3.447 1.00 31.95 ? 84 THR B C 1 ATOM 3080 O O . THR B 2 84 ? 55.023 -30.143 -4.640 1.00 31.48 ? 84 THR B O 1 ATOM 3081 C CB . THR B 2 84 ? 56.018 -31.185 -1.629 1.00 31.07 ? 84 THR B CB 1 ATOM 3082 O OG1 . THR B 2 84 ? 57.107 -31.152 -0.698 1.00 30.05 ? 84 THR B OG1 1 ATOM 3083 C CG2 . THR B 2 84 ? 56.162 -32.417 -2.536 1.00 30.85 ? 84 THR B CG2 1 ATOM 3084 N N . ARG B 2 85 ? 53.601 -29.736 -2.960 1.00 32.70 ? 85 ARG B N 1 ATOM 3085 C CA . ARG B 2 85 ? 52.436 -29.718 -3.853 1.00 32.58 ? 85 ARG B CA 1 ATOM 3086 C C . ARG B 2 85 ? 52.572 -28.641 -4.945 1.00 31.70 ? 85 ARG B C 1 ATOM 3087 O O . ARG B 2 85 ? 52.426 -28.925 -6.128 1.00 29.65 ? 85 ARG B O 1 ATOM 3088 C CB . ARG B 2 85 ? 51.152 -29.505 -3.066 1.00 35.01 ? 85 ARG B CB 1 ATOM 3089 C CG . ARG B 2 85 ? 49.888 -29.577 -3.912 1.00 36.77 ? 85 ARG B CG 1 ATOM 3090 C CD . ARG B 2 85 ? 48.666 -29.165 -3.109 1.00 39.03 ? 85 ARG B CD 1 ATOM 3091 N NE . ARG B 2 85 ? 48.424 -30.096 -2.008 1.00 41.09 ? 85 ARG B NE 1 ATOM 3092 C CZ . ARG B 2 85 ? 48.410 -29.790 -0.707 1.00 41.67 ? 85 ARG B CZ 1 ATOM 3093 N NH1 . ARG B 2 85 ? 48.601 -28.543 -0.281 1.00 42.74 ? 85 ARG B NH1 1 ATOM 3094 N NH2 . ARG B 2 85 ? 48.179 -30.750 0.177 1.00 40.82 ? 85 ARG B NH2 1 ATOM 3095 N N . ASP B 2 86 ? 52.863 -27.410 -4.545 1.00 31.59 ? 86 ASP B N 1 ATOM 3096 C CA . ASP B 2 86 ? 53.094 -26.334 -5.506 1.00 31.59 ? 86 ASP B CA 1 ATOM 3097 C C . ASP B 2 86 ? 54.212 -26.675 -6.516 1.00 30.44 ? 86 ASP B C 1 ATOM 3098 O O . ASP B 2 86 ? 54.085 -26.373 -7.694 1.00 29.51 ? 86 ASP B O 1 ATOM 3099 C CB . ASP B 2 86 ? 53.421 -25.034 -4.773 1.00 33.39 ? 86 ASP B CB 1 ATOM 3100 C CG . ASP B 2 86 ? 52.233 -24.463 -4.026 1.00 34.73 ? 86 ASP B CG 1 ATOM 3101 O OD1 . ASP B 2 86 ? 51.098 -24.957 -4.204 1.00 35.63 ? 86 ASP B OD1 1 ATOM 3102 O OD2 . ASP B 2 86 ? 52.434 -23.502 -3.258 1.00 36.11 ? 86 ASP B OD2 1 ATOM 3103 N N . SER B 2 87 ? 55.280 -27.331 -6.061 1.00 29.87 ? 87 SER B N 1 ATOM 3104 C CA . SER B 2 87 ? 56.363 -27.749 -6.961 1.00 29.94 ? 87 SER B CA 1 ATOM 3105 C C . SER B 2 87 ? 55.865 -28.749 -8.011 1.00 30.22 ? 87 SER B C 1 ATOM 3106 O O . SER B 2 87 ? 56.187 -28.632 -9.199 1.00 29.68 ? 87 SER B O 1 ATOM 3107 C CB . SER B 2 87 ? 57.522 -28.375 -6.179 1.00 29.70 ? 87 SER B CB 1 ATOM 3108 O OG . SER B 2 87 ? 58.069 -27.471 -5.238 1.00 29.74 ? 87 SER B OG 1 ATOM 3109 N N . ILE B 2 88 ? 55.076 -29.720 -7.559 1.00 29.90 ? 88 ILE B N 1 ATOM 3110 C CA . ILE B 2 88 ? 54.409 -30.678 -8.447 1.00 29.86 ? 88 ILE B CA 1 ATOM 3111 C C . ILE B 2 88 ? 53.425 -29.986 -9.412 1.00 29.60 ? 88 ILE B C 1 ATOM 3112 O O . ILE B 2 88 ? 53.441 -30.258 -10.610 1.00 29.72 ? 88 ILE B O 1 ATOM 3113 C CB . ILE B 2 88 ? 53.683 -31.780 -7.629 1.00 30.18 ? 88 ILE B CB 1 ATOM 3114 C CG1 . ILE B 2 88 ? 54.696 -32.621 -6.842 1.00 30.64 ? 88 ILE B CG1 1 ATOM 3115 C CG2 . ILE B 2 88 ? 52.847 -32.702 -8.517 1.00 30.39 ? 88 ILE B CG2 1 ATOM 3116 C CD1 . ILE B 2 88 ? 55.747 -33.321 -7.685 1.00 30.60 ? 88 ILE B CD1 1 ATOM 3117 N N . THR B 2 89 ? 52.579 -29.092 -8.906 1.00 29.80 ? 89 THR B N 1 ATOM 3118 C CA . THR B 2 89 ? 51.670 -28.327 -9.769 1.00 30.28 ? 89 THR B CA 1 ATOM 3119 C C . THR B 2 89 ? 52.426 -27.634 -10.917 1.00 31.26 ? 89 THR B C 1 ATOM 3120 O O . THR B 2 89 ? 51.982 -27.637 -12.072 1.00 31.26 ? 89 THR B O 1 ATOM 3121 C CB . THR B 2 89 ? 50.891 -27.288 -8.960 1.00 31.38 ? 89 THR B CB 1 ATOM 3122 O OG1 . THR B 2 89 ? 49.942 -27.957 -8.127 1.00 32.96 ? 89 THR B OG1 1 ATOM 3123 C CG2 . THR B 2 89 ? 50.139 -26.305 -9.869 1.00 32.54 ? 89 THR B CG2 1 ATOM 3124 N N . GLU B 2 90 ? 53.578 -27.064 -10.590 1.00 31.05 ? 90 GLU B N 1 ATOM 3125 C CA . GLU B 2 90 ? 54.389 -26.359 -11.568 1.00 32.84 ? 90 GLU B CA 1 ATOM 3126 C C . GLU B 2 90 ? 54.908 -27.331 -12.652 1.00 31.65 ? 90 GLU B C 1 ATOM 3127 O O . GLU B 2 90 ? 54.896 -27.016 -13.848 1.00 31.16 ? 90 GLU B O 1 ATOM 3128 C CB . GLU B 2 90 ? 55.529 -25.651 -10.842 1.00 35.16 ? 90 GLU B CB 1 ATOM 3129 C CG . GLU B 2 90 ? 55.944 -24.322 -11.418 1.00 39.72 ? 90 GLU B CG 1 ATOM 3130 C CD . GLU B 2 90 ? 54.842 -23.267 -11.469 1.00 42.81 ? 90 GLU B CD 1 ATOM 3131 O OE1 . GLU B 2 90 ? 53.811 -23.372 -10.769 1.00 44.83 ? 90 GLU B OE1 1 ATOM 3132 O OE2 . GLU B 2 90 ? 55.017 -22.307 -12.247 1.00 49.44 ? 90 GLU B OE2 1 ATOM 3133 N N . VAL B 2 91 ? 55.325 -28.524 -12.241 1.00 30.16 ? 91 VAL B N 1 ATOM 3134 C CA . VAL B 2 91 ? 55.733 -29.555 -13.195 1.00 30.13 ? 91 VAL B CA 1 ATOM 3135 C C . VAL B 2 91 ? 54.591 -29.983 -14.145 1.00 31.13 ? 91 VAL B C 1 ATOM 3136 O O . VAL B 2 91 ? 54.765 -29.997 -15.374 1.00 31.60 ? 91 VAL B O 1 ATOM 3137 C CB . VAL B 2 91 ? 56.318 -30.785 -12.472 1.00 29.71 ? 91 VAL B CB 1 ATOM 3138 C CG1 . VAL B 2 91 ? 56.514 -31.955 -13.431 1.00 30.15 ? 91 VAL B CG1 1 ATOM 3139 C CG2 . VAL B 2 91 ? 57.641 -30.421 -11.823 1.00 29.88 ? 91 VAL B CG2 1 ATOM 3140 N N . TRP B 2 92 ? 53.428 -30.320 -13.594 1.00 30.54 ? 92 TRP B N 1 ATOM 3141 C CA . TRP B 2 92 ? 52.293 -30.725 -14.430 1.00 30.63 ? 92 TRP B CA 1 ATOM 3142 C C . TRP B 2 92 ? 51.762 -29.612 -15.317 1.00 31.00 ? 92 TRP B C 1 ATOM 3143 O O . TRP B 2 92 ? 51.333 -29.874 -16.445 1.00 30.56 ? 92 TRP B O 1 ATOM 3144 C CB . TRP B 2 92 ? 51.162 -31.308 -13.587 1.00 30.98 ? 92 TRP B CB 1 ATOM 3145 C CG . TRP B 2 92 ? 51.512 -32.663 -13.095 1.00 31.39 ? 92 TRP B CG 1 ATOM 3146 C CD1 . TRP B 2 92 ? 51.733 -33.037 -11.805 1.00 30.51 ? 92 TRP B CD1 1 ATOM 3147 C CD2 . TRP B 2 92 ? 51.736 -33.821 -13.897 1.00 31.97 ? 92 TRP B CD2 1 ATOM 3148 N NE1 . TRP B 2 92 ? 52.048 -34.366 -11.751 1.00 31.65 ? 92 TRP B NE1 1 ATOM 3149 C CE2 . TRP B 2 92 ? 52.072 -34.872 -13.023 1.00 32.30 ? 92 TRP B CE2 1 ATOM 3150 C CE3 . TRP B 2 92 ? 51.673 -34.078 -15.269 1.00 32.41 ? 92 TRP B CE3 1 ATOM 3151 C CZ2 . TRP B 2 92 ? 52.350 -36.160 -13.475 1.00 32.73 ? 92 TRP B CZ2 1 ATOM 3152 C CZ3 . TRP B 2 92 ? 51.953 -35.361 -15.717 1.00 32.95 ? 92 TRP B CZ3 1 ATOM 3153 C CH2 . TRP B 2 92 ? 52.282 -36.384 -14.821 1.00 33.16 ? 92 TRP B CH2 1 ATOM 3154 N N . SER B 2 93 ? 51.788 -28.383 -14.815 1.00 31.37 ? 93 SER B N 1 ATOM 3155 C CA . SER B 2 93 ? 51.311 -27.237 -15.594 1.00 32.44 ? 93 SER B CA 1 ATOM 3156 C C . SER B 2 93 ? 52.203 -27.037 -16.821 1.00 33.02 ? 93 SER B C 1 ATOM 3157 O O . SER B 2 93 ? 51.717 -26.712 -17.905 1.00 33.99 ? 93 SER B O 1 ATOM 3158 C CB . SER B 2 93 ? 51.278 -25.978 -14.729 1.00 33.28 ? 93 SER B CB 1 ATOM 3159 O OG . SER B 2 93 ? 50.335 -26.104 -13.657 1.00 34.14 ? 93 SER B OG 1 ATOM 3160 N N . TYR B 2 94 ? 53.505 -27.249 -16.638 1.00 32.23 ? 94 TYR B N 1 ATOM 3161 C CA . TYR B 2 94 ? 54.471 -27.239 -17.725 1.00 33.15 ? 94 TYR B CA 1 ATOM 3162 C C . TYR B 2 94 ? 54.241 -28.417 -18.678 1.00 32.83 ? 94 TYR B C 1 ATOM 3163 O O . TYR B 2 94 ? 54.163 -28.231 -19.888 1.00 33.06 ? 94 TYR B O 1 ATOM 3164 C CB . TYR B 2 94 ? 55.896 -27.292 -17.158 1.00 34.07 ? 94 TYR B CB 1 ATOM 3165 C CG . TYR B 2 94 ? 56.975 -27.558 -18.182 1.00 36.13 ? 94 TYR B CG 1 ATOM 3166 C CD1 . TYR B 2 94 ? 57.555 -26.515 -18.894 1.00 39.08 ? 94 TYR B CD1 1 ATOM 3167 C CD2 . TYR B 2 94 ? 57.425 -28.845 -18.428 1.00 37.64 ? 94 TYR B CD2 1 ATOM 3168 C CE1 . TYR B 2 94 ? 58.546 -26.750 -19.832 1.00 40.64 ? 94 TYR B CE1 1 ATOM 3169 C CE2 . TYR B 2 94 ? 58.416 -29.096 -19.370 1.00 39.39 ? 94 TYR B CE2 1 ATOM 3170 C CZ . TYR B 2 94 ? 58.976 -28.044 -20.068 1.00 41.41 ? 94 TYR B CZ 1 ATOM 3171 O OH . TYR B 2 94 ? 59.968 -28.278 -21.006 1.00 44.78 ? 94 TYR B OH 1 ATOM 3172 N N . ASN B 2 95 ? 54.146 -29.626 -18.131 1.00 31.97 ? 95 ASN B N 1 ATOM 3173 C CA . ASN B 2 95 ? 53.926 -30.816 -18.949 1.00 32.49 ? 95 ASN B CA 1 ATOM 3174 C C . ASN B 2 95 ? 52.695 -30.685 -19.837 1.00 32.71 ? 95 ASN B C 1 ATOM 3175 O O . ASN B 2 95 ? 52.759 -30.996 -21.022 1.00 32.63 ? 95 ASN B O 1 ATOM 3176 C CB . ASN B 2 95 ? 53.793 -32.067 -18.084 1.00 32.59 ? 95 ASN B CB 1 ATOM 3177 C CG . ASN B 2 95 ? 55.109 -32.493 -17.468 1.00 34.04 ? 95 ASN B CG 1 ATOM 3178 O OD1 . ASN B 2 95 ? 56.175 -31.962 -17.801 1.00 33.73 ? 95 ASN B OD1 1 ATOM 3179 N ND2 . ASN B 2 95 ? 55.041 -33.456 -16.551 1.00 34.31 ? 95 ASN B ND2 1 ATOM 3180 N N . ALA B 2 96 ? 51.591 -30.215 -19.264 1.00 33.12 ? 96 ALA B N 1 ATOM 3181 C CA . ALA B 2 96 ? 50.324 -30.071 -20.009 1.00 34.88 ? 96 ALA B CA 1 ATOM 3182 C C . ALA B 2 96 ? 50.437 -29.072 -21.157 1.00 36.01 ? 96 ALA B C 1 ATOM 3183 O O . ALA B 2 96 ? 49.970 -29.338 -22.266 1.00 36.76 ? 96 ALA B O 1 ATOM 3184 C CB . ALA B 2 96 ? 49.199 -29.656 -19.077 1.00 34.85 ? 96 ALA B CB 1 ATOM 3185 N N . GLU B 2 97 ? 51.055 -27.928 -20.874 1.00 36.58 ? 97 GLU B N 1 ATOM 3186 C CA . GLU B 2 97 ? 51.252 -26.863 -21.857 1.00 37.79 ? 97 GLU B CA 1 ATOM 3187 C C . GLU B 2 97 ? 52.137 -27.342 -23.012 1.00 37.22 ? 97 GLU B C 1 ATOM 3188 O O . GLU B 2 97 ? 51.852 -27.066 -24.184 1.00 37.89 ? 97 GLU B O 1 ATOM 3189 C CB . GLU B 2 97 ? 51.906 -25.651 -21.181 1.00 38.88 ? 97 GLU B CB 1 ATOM 3190 C CG . GLU B 2 97 ? 52.025 -24.402 -22.050 1.00 41.11 ? 97 GLU B CG 1 ATOM 3191 C CD . GLU B 2 97 ? 50.846 -23.457 -21.902 1.00 43.80 ? 97 GLU B CD 1 ATOM 3192 O OE1 . GLU B 2 97 ? 50.461 -23.134 -20.755 1.00 44.26 ? 97 GLU B OE1 1 ATOM 3193 O OE2 . GLU B 2 97 ? 50.311 -23.013 -22.937 1.00 47.03 ? 97 GLU B OE2 1 ATOM 3194 N N . LEU B 2 98 ? 53.203 -28.065 -22.675 1.00 34.78 ? 98 LEU B N 1 ATOM 3195 C CA . LEU B 2 98 ? 54.151 -28.543 -23.674 1.00 35.12 ? 98 LEU B CA 1 ATOM 3196 C C . LEU B 2 98 ? 53.555 -29.664 -24.506 1.00 34.71 ? 98 LEU B C 1 ATOM 3197 O O . LEU B 2 98 ? 53.766 -29.721 -25.716 1.00 35.02 ? 98 LEU B O 1 ATOM 3198 C CB . LEU B 2 98 ? 55.441 -29.022 -23.010 1.00 35.82 ? 98 LEU B CB 1 ATOM 3199 C CG . LEU B 2 98 ? 56.514 -29.605 -23.935 1.00 38.50 ? 98 LEU B CG 1 ATOM 3200 C CD1 . LEU B 2 98 ? 56.953 -28.571 -24.970 1.00 39.91 ? 98 LEU B CD1 1 ATOM 3201 C CD2 . LEU B 2 98 ? 57.710 -30.107 -23.138 1.00 39.09 ? 98 LEU B CD2 1 ATOM 3202 N N . LEU B 2 99 ? 52.816 -30.559 -23.858 1.00 34.00 ? 99 LEU B N 1 ATOM 3203 C CA . LEU B 2 99 ? 52.206 -31.694 -24.551 1.00 34.82 ? 99 LEU B CA 1 ATOM 3204 C C . LEU B 2 99 ? 51.251 -31.210 -25.634 1.00 35.67 ? 99 LEU B C 1 ATOM 3205 O O . LEU B 2 99 ? 51.352 -31.606 -26.781 1.00 35.85 ? 99 LEU B O 1 ATOM 3206 C CB . LEU B 2 99 ? 51.452 -32.576 -23.566 1.00 35.04 ? 99 LEU B CB 1 ATOM 3207 C CG . LEU B 2 99 ? 50.632 -33.741 -24.134 1.00 36.38 ? 99 LEU B CG 1 ATOM 3208 C CD1 . LEU B 2 99 ? 51.528 -34.856 -24.644 1.00 36.44 ? 99 LEU B CD1 1 ATOM 3209 C CD2 . LEU B 2 99 ? 49.688 -34.261 -23.062 1.00 36.69 ? 99 LEU B CD2 1 ATOM 3210 N N . VAL B 2 100 ? 50.332 -30.339 -25.256 1.00 35.86 ? 100 VAL B N 1 ATOM 3211 C CA . VAL B 2 100 ? 49.308 -29.863 -26.171 1.00 38.09 ? 100 VAL B CA 1 ATOM 3212 C C . VAL B 2 100 ? 49.910 -29.045 -27.319 1.00 39.23 ? 100 VAL B C 1 ATOM 3213 O O . VAL B 2 100 ? 49.462 -29.151 -28.450 1.00 40.87 ? 100 VAL B O 1 ATOM 3214 C CB . VAL B 2 100 ? 48.237 -29.053 -25.421 1.00 38.75 ? 100 VAL B CB 1 ATOM 3215 C CG1 . VAL B 2 100 ? 47.212 -28.481 -26.380 1.00 41.37 ? 100 VAL B CG1 1 ATOM 3216 C CG2 . VAL B 2 100 ? 47.540 -29.946 -24.408 1.00 38.78 ? 100 VAL B CG2 1 ATOM 3217 N N . ALA B 2 101 ? 50.937 -28.258 -27.029 1.00 39.02 ? 101 ALA B N 1 ATOM 3218 C CA . ALA B 2 101 ? 51.582 -27.443 -28.049 1.00 40.82 ? 101 ALA B CA 1 ATOM 3219 C C . ALA B 2 101 ? 52.297 -28.302 -29.089 1.00 41.85 ? 101 ALA B C 1 ATOM 3220 O O . ALA B 2 101 ? 52.141 -28.090 -30.295 1.00 43.22 ? 101 ALA B O 1 ATOM 3221 C CB . ALA B 2 101 ? 52.559 -26.477 -27.409 1.00 40.35 ? 101 ALA B CB 1 ATOM 3222 N N . MET B 2 102 ? 53.077 -29.269 -28.622 1.00 41.73 ? 102 MET B N 1 ATOM 3223 C CA . MET B 2 102 ? 53.793 -30.146 -29.531 1.00 43.92 ? 102 MET B CA 1 ATOM 3224 C C . MET B 2 102 ? 52.829 -31.073 -30.290 1.00 43.49 ? 102 MET B C 1 ATOM 3225 O O . MET B 2 102 ? 53.006 -31.283 -31.493 1.00 44.31 ? 102 MET B O 1 ATOM 3226 C CB . MET B 2 102 ? 54.941 -30.884 -28.816 1.00 45.74 ? 102 MET B CB 1 ATOM 3227 C CG . MET B 2 102 ? 54.607 -32.194 -28.141 1.00 49.03 ? 102 MET B CG 1 ATOM 3228 S SD . MET B 2 102 ? 54.887 -33.614 -29.219 1.00 57.54 ? 102 MET B SD 1 ATOM 3229 C CE . MET B 2 102 ? 54.374 -34.934 -28.120 1.00 54.41 ? 102 MET B CE 1 ATOM 3230 N N . GLU B 2 103 ? 51.794 -31.589 -29.624 1.00 41.31 ? 103 GLU B N 1 ATOM 3231 C CA . GLU B 2 103 ? 50.765 -32.374 -30.327 1.00 42.75 ? 103 GLU B CA 1 ATOM 3232 C C . GLU B 2 103 ? 50.078 -31.544 -31.417 1.00 43.38 ? 103 GLU B C 1 ATOM 3233 O O . GLU B 2 103 ? 49.850 -32.032 -32.533 1.00 44.10 ? 103 GLU B O 1 ATOM 3234 C CB . GLU B 2 103 ? 49.695 -32.891 -29.372 1.00 42.98 ? 103 GLU B CB 1 ATOM 3235 C CG . GLU B 2 103 ? 50.204 -33.852 -28.317 1.00 42.82 ? 103 GLU B CG 1 ATOM 3236 C CD . GLU B 2 103 ? 50.214 -35.294 -28.757 1.00 44.49 ? 103 GLU B CD 1 ATOM 3237 O OE1 . GLU B 2 103 ? 50.240 -35.576 -29.972 1.00 46.08 ? 103 GLU B OE1 1 ATOM 3238 O OE2 . GLU B 2 103 ? 50.215 -36.154 -27.856 1.00 45.82 ? 103 GLU B OE2 1 ATOM 3239 N N . ASN B 2 104 ? 49.749 -30.297 -31.085 1.00 41.99 ? 104 ASN B N 1 ATOM 3240 C CA . ASN B 2 104 ? 49.079 -29.407 -32.025 1.00 43.83 ? 104 ASN B CA 1 ATOM 3241 C C . ASN B 2 104 ? 49.948 -29.088 -33.234 1.00 44.72 ? 104 ASN B C 1 ATOM 3242 O O . ASN B 2 104 ? 49.447 -29.021 -34.351 1.00 46.76 ? 104 ASN B O 1 ATOM 3243 C CB . ASN B 2 104 ? 48.631 -28.116 -31.334 1.00 43.66 ? 104 ASN B CB 1 ATOM 3244 C CG . ASN B 2 104 ? 47.452 -28.331 -30.403 1.00 44.07 ? 104 ASN B CG 1 ATOM 3245 O OD1 . ASN B 2 104 ? 46.905 -29.432 -30.303 1.00 44.60 ? 104 ASN B OD1 1 ATOM 3246 N ND2 . ASN B 2 104 ? 47.053 -27.276 -29.715 1.00 44.73 ? 104 ASN B ND2 1 ATOM 3247 N N . GLN B 2 105 ? 51.246 -28.895 -33.010 1.00 44.82 ? 105 GLN B N 1 ATOM 3248 C CA . GLN B 2 105 ? 52.191 -28.679 -34.107 1.00 45.71 ? 105 GLN B CA 1 ATOM 3249 C C . GLN B 2 105 ? 52.185 -29.895 -35.028 1.00 46.42 ? 105 GLN B C 1 ATOM 3250 O O . GLN B 2 105 ? 52.092 -29.759 -36.251 1.00 47.36 ? 105 GLN B O 1 ATOM 3251 C CB . GLN B 2 105 ? 53.605 -28.438 -33.564 1.00 45.97 ? 105 GLN B CB 1 ATOM 3252 C CG . GLN B 2 105 ? 54.588 -27.836 -34.563 1.00 47.26 ? 105 GLN B CG 1 ATOM 3253 C CD . GLN B 2 105 ? 54.467 -26.323 -34.708 1.00 48.08 ? 105 GLN B CD 1 ATOM 3254 O OE1 . GLN B 2 105 ? 54.211 -25.603 -33.739 1.00 48.02 ? 105 GLN B OE1 1 ATOM 3255 N NE2 . GLN B 2 105 ? 54.684 -25.833 -35.920 1.00 49.32 ? 105 GLN B NE2 1 ATOM 3256 N N . HIS B 2 106 ? 52.268 -31.082 -34.431 1.00 46.11 ? 106 HIS B N 1 ATOM 3257 C CA . HIS B 2 106 ? 52.308 -32.334 -35.189 1.00 46.63 ? 106 HIS B CA 1 ATOM 3258 C C . HIS B 2 106 ? 51.000 -32.618 -35.932 1.00 46.55 ? 106 HIS B C 1 ATOM 3259 O O . HIS B 2 106 ? 51.023 -33.129 -37.047 1.00 47.44 ? 106 HIS B O 1 ATOM 3260 C CB . HIS B 2 106 ? 52.654 -33.501 -34.262 1.00 46.26 ? 106 HIS B CB 1 ATOM 3261 C CG . HIS B 2 106 ? 52.800 -34.809 -34.969 1.00 47.25 ? 106 HIS B CG 1 ATOM 3262 N ND1 . HIS B 2 106 ? 51.823 -35.781 -34.949 1.00 47.45 ? 106 HIS B ND1 1 ATOM 3263 C CD2 . HIS B 2 106 ? 53.807 -35.305 -35.724 1.00 48.55 ? 106 HIS B CD2 1 ATOM 3264 C CE1 . HIS B 2 106 ? 52.220 -36.819 -35.662 1.00 48.46 ? 106 HIS B CE1 1 ATOM 3265 N NE2 . HIS B 2 106 ? 53.420 -36.554 -36.146 1.00 49.51 ? 106 HIS B NE2 1 ATOM 3266 N N . THR B 2 107 ? 49.869 -32.285 -35.310 1.00 45.90 ? 107 THR B N 1 ATOM 3267 C CA . THR B 2 107 ? 48.542 -32.509 -35.904 1.00 45.48 ? 107 THR B CA 1 ATOM 3268 C C . THR B 2 107 ? 48.339 -31.670 -37.166 1.00 46.87 ? 107 THR B C 1 ATOM 3269 O O . THR B 2 107 ? 47.757 -32.137 -38.150 1.00 47.52 ? 107 THR B O 1 ATOM 3270 C CB . THR B 2 107 ? 47.423 -32.211 -34.880 1.00 44.47 ? 107 THR B CB 1 ATOM 3271 O OG1 . THR B 2 107 ? 47.426 -33.225 -33.868 1.00 44.21 ? 107 THR B OG1 1 ATOM 3272 C CG2 . THR B 2 107 ? 46.039 -32.169 -35.526 1.00 45.04 ? 107 THR B CG2 1 ATOM 3273 N N . ILE B 2 108 ? 48.818 -30.432 -37.134 1.00 47.36 ? 108 ILE B N 1 ATOM 3274 C CA . ILE B 2 108 ? 48.689 -29.528 -38.275 1.00 48.71 ? 108 ILE B CA 1 ATOM 3275 C C . ILE B 2 108 ? 49.613 -29.967 -39.414 1.00 49.62 ? 108 ILE B C 1 ATOM 3276 O O . ILE B 2 108 ? 49.210 -29.980 -40.584 1.00 49.43 ? 108 ILE B O 1 ATOM 3277 C CB . ILE B 2 108 ? 48.958 -28.068 -37.835 1.00 49.08 ? 108 ILE B CB 1 ATOM 3278 C CG1 . ILE B 2 108 ? 47.764 -27.571 -37.008 1.00 48.98 ? 108 ILE B CG1 1 ATOM 3279 C CG2 . ILE B 2 108 ? 49.212 -27.153 -39.030 1.00 49.92 ? 108 ILE B CG2 1 ATOM 3280 C CD1 . ILE B 2 108 ? 48.061 -26.385 -36.117 1.00 49.11 ? 108 ILE B CD1 1 ATOM 3281 N N . ASP B 2 109 ? 50.846 -30.330 -39.064 1.00 49.64 ? 109 ASP B N 1 ATOM 3282 C CA . ASP B 2 109 ? 51.808 -30.860 -40.035 1.00 51.07 ? 109 ASP B CA 1 ATOM 3283 C C . ASP B 2 109 ? 51.326 -32.189 -40.622 1.00 51.93 ? 109 ASP B C 1 ATOM 3284 O O . ASP B 2 109 ? 51.508 -32.462 -41.810 1.00 53.62 ? 109 ASP B O 1 ATOM 3285 C CB . ASP B 2 109 ? 53.185 -31.043 -39.385 1.00 50.89 ? 109 ASP B CB 1 ATOM 3286 C CG . ASP B 2 109 ? 53.863 -29.725 -39.067 1.00 51.14 ? 109 ASP B CG 1 ATOM 3287 O OD1 . ASP B 2 109 ? 53.485 -28.699 -39.666 1.00 52.20 ? 109 ASP B OD1 1 ATOM 3288 O OD2 . ASP B 2 109 ? 54.789 -29.709 -38.226 1.00 51.35 ? 109 ASP B OD2 1 ATOM 3289 N N . LEU B 2 110 ? 50.703 -33.006 -39.783 1.00 51.44 ? 110 LEU B N 1 ATOM 3290 C CA . LEU B 2 110 ? 50.161 -34.292 -40.211 1.00 52.46 ? 110 LEU B CA 1 ATOM 3291 C C . LEU B 2 110 ? 49.053 -34.131 -41.249 1.00 52.81 ? 110 LEU B C 1 ATOM 3292 O O . LEU B 2 110 ? 48.990 -34.891 -42.218 1.00 53.96 ? 110 LEU B O 1 ATOM 3293 C CB . LEU B 2 110 ? 49.646 -35.049 -38.989 1.00 52.23 ? 110 LEU B CB 1 ATOM 3294 C CG . LEU B 2 110 ? 49.066 -36.450 -39.149 1.00 52.89 ? 110 LEU B CG 1 ATOM 3295 C CD1 . LEU B 2 110 ? 49.420 -37.258 -37.910 1.00 52.77 ? 110 LEU B CD1 1 ATOM 3296 C CD2 . LEU B 2 110 ? 47.559 -36.414 -39.365 1.00 52.89 ? 110 LEU B CD2 1 ATOM 3297 N N . ALA B 2 111 ? 48.185 -33.144 -41.052 1.00 51.96 ? 111 ALA B N 1 ATOM 3298 C CA . ALA B 2 111 ? 47.109 -32.863 -42.010 1.00 52.55 ? 111 ALA B CA 1 ATOM 3299 C C . ALA B 2 111 ? 47.648 -32.288 -43.317 1.00 54.26 ? 111 ALA B C 1 ATOM 3300 O O . ALA B 2 111 ? 47.132 -32.582 -44.398 1.00 55.42 ? 111 ALA B O 1 ATOM 3301 C CB . ALA B 2 111 ? 46.106 -31.903 -41.401 1.00 52.11 ? 111 ALA B CB 1 ATOM 3302 N N . ASP B 2 112 ? 48.673 -31.448 -43.197 1.00 54.57 ? 112 ASP B N 1 ATOM 3303 C CA . ASP B 2 112 ? 49.355 -30.859 -44.341 1.00 56.23 ? 112 ASP B CA 1 ATOM 3304 C C . ASP B 2 112 ? 49.959 -31.987 -45.170 1.00 57.32 ? 112 ASP B C 1 ATOM 3305 O O . ASP B 2 112 ? 49.782 -32.041 -46.383 1.00 57.71 ? 112 ASP B O 1 ATOM 3306 C CB . ASP B 2 112 ? 50.447 -29.897 -43.844 1.00 56.45 ? 112 ASP B CB 1 ATOM 3307 C CG . ASP B 2 112 ? 51.020 -29.004 -44.941 1.00 58.52 ? 112 ASP B CG 1 ATOM 3308 O OD1 . ASP B 2 112 ? 50.383 -28.813 -45.999 1.00 59.40 ? 112 ASP B OD1 1 ATOM 3309 O OD2 . ASP B 2 112 ? 52.129 -28.473 -44.723 1.00 58.70 ? 112 ASP B OD2 1 ATOM 3310 N N . SER B 2 113 ? 50.657 -32.893 -44.490 1.00 56.74 ? 113 SER B N 1 ATOM 3311 C CA . SER B 2 113 ? 51.259 -34.063 -45.125 1.00 57.71 ? 113 SER B CA 1 ATOM 3312 C C . SER B 2 113 ? 50.260 -34.882 -45.946 1.00 58.52 ? 113 SER B C 1 ATOM 3313 O O . SER B 2 113 ? 50.535 -35.216 -47.099 1.00 59.78 ? 113 SER B O 1 ATOM 3314 C CB . SER B 2 113 ? 51.903 -34.964 -44.071 1.00 56.52 ? 113 SER B CB 1 ATOM 3315 O OG . SER B 2 113 ? 52.185 -36.241 -44.608 1.00 57.84 ? 113 SER B OG 1 ATOM 3316 N N . GLU B 2 114 ? 49.114 -35.206 -45.351 1.00 57.56 ? 114 GLU B N 1 ATOM 3317 C CA . GLU B 2 114 ? 48.120 -36.061 -46.009 1.00 58.12 ? 114 GLU B CA 1 ATOM 3318 C C . GLU B 2 114 ? 47.579 -35.434 -47.280 1.00 59.83 ? 114 GLU B C 1 ATOM 3319 O O . GLU B 2 114 ? 47.315 -36.142 -48.262 1.00 61.94 ? 114 GLU B O 1 ATOM 3320 C CB . GLU B 2 114 ? 46.964 -36.394 -45.067 1.00 57.13 ? 114 GLU B CB 1 ATOM 3321 C CG . GLU B 2 114 ? 47.341 -37.352 -43.947 1.00 56.78 ? 114 GLU B CG 1 ATOM 3322 C CD . GLU B 2 114 ? 47.660 -38.755 -44.432 1.00 57.66 ? 114 GLU B CD 1 ATOM 3323 O OE1 . GLU B 2 114 ? 46.993 -39.237 -45.361 1.00 59.71 ? 114 GLU B OE1 1 ATOM 3324 O OE2 . GLU B 2 114 ? 48.569 -39.391 -43.867 1.00 57.88 ? 114 GLU B OE2 1 ATOM 3325 N N . MET B 2 115 ? 47.406 -34.115 -47.259 1.00 59.25 ? 115 MET B N 1 ATOM 3326 C CA . MET B 2 115 ? 47.019 -33.374 -48.457 1.00 60.60 ? 115 MET B CA 1 ATOM 3327 C C . MET B 2 115 ? 48.076 -33.550 -49.540 1.00 62.11 ? 115 MET B C 1 ATOM 3328 O O . MET B 2 115 ? 47.740 -33.796 -50.703 1.00 64.06 ? 115 MET B O 1 ATOM 3329 C CB . MET B 2 115 ? 46.838 -31.884 -48.134 1.00 60.31 ? 115 MET B CB 1 ATOM 3330 C CG . MET B 2 115 ? 46.524 -30.970 -49.319 1.00 61.86 ? 115 MET B CG 1 ATOM 3331 S SD . MET B 2 115 ? 44.768 -30.815 -49.705 1.00 62.33 ? 115 MET B SD 1 ATOM 3332 C CE . MET B 2 115 ? 44.535 -32.156 -50.868 1.00 63.62 ? 115 MET B CE 1 ATOM 3333 N N . ASP B 2 116 ? 49.347 -33.428 -49.156 1.00 61.37 ? 116 ASP B N 1 ATOM 3334 C CA . ASP B 2 116 ? 50.455 -33.530 -50.111 1.00 63.35 ? 116 ASP B CA 1 ATOM 3335 C C . ASP B 2 116 ? 50.513 -34.926 -50.727 1.00 63.78 ? 116 ASP B C 1 ATOM 3336 O O . ASP B 2 116 ? 50.652 -35.073 -51.946 1.00 65.51 ? 116 ASP B O 1 ATOM 3337 C CB . ASP B 2 116 ? 51.791 -33.191 -49.437 1.00 63.08 ? 116 ASP B CB 1 ATOM 3338 C CG . ASP B 2 116 ? 52.930 -33.038 -50.436 1.00 65.55 ? 116 ASP B CG 1 ATOM 3339 O OD1 . ASP B 2 116 ? 52.826 -32.176 -51.331 1.00 66.66 ? 116 ASP B OD1 1 ATOM 3340 O OD2 . ASP B 2 116 ? 53.934 -33.773 -50.317 1.00 66.30 ? 116 ASP B OD2 1 ATOM 3341 N N . LYS B 2 117 ? 50.388 -35.943 -49.875 1.00 61.73 ? 117 LYS B N 1 ATOM 3342 C CA . LYS B 2 117 ? 50.364 -37.338 -50.316 1.00 62.09 ? 117 LYS B CA 1 ATOM 3343 C C . LYS B 2 117 ? 49.275 -37.597 -51.364 1.00 63.23 ? 117 LYS B C 1 ATOM 3344 O O . LYS B 2 117 ? 49.510 -38.306 -52.345 1.00 64.57 ? 117 LYS B O 1 ATOM 3345 C CB . LYS B 2 117 ? 50.195 -38.269 -49.113 1.00 60.28 ? 117 LYS B CB 1 ATOM 3346 C CG . LYS B 2 117 ? 51.472 -38.415 -48.300 1.00 59.70 ? 117 LYS B CG 1 ATOM 3347 C CD . LYS B 2 117 ? 51.229 -38.540 -46.804 1.00 58.00 ? 117 LYS B CD 1 ATOM 3348 C CE . LYS B 2 117 ? 50.728 -39.915 -46.396 1.00 57.60 ? 117 LYS B CE 1 ATOM 3349 N NZ . LYS B 2 117 ? 51.137 -40.219 -44.992 1.00 55.60 ? 117 LYS B NZ 1 ATOM 3350 N N . LEU B 2 118 ? 48.100 -37.008 -51.157 1.00 62.36 ? 118 LEU B N 1 ATOM 3351 C CA . LEU B 2 118 ? 47.003 -37.117 -52.114 1.00 63.49 ? 118 LEU B CA 1 ATOM 3352 C C . LEU B 2 118 ? 47.329 -36.393 -53.419 1.00 65.76 ? 118 LEU B C 1 ATOM 3353 O O . LEU B 2 118 ? 47.096 -36.925 -54.505 1.00 67.35 ? 118 LEU B O 1 ATOM 3354 C CB . LEU B 2 118 ? 45.709 -36.556 -51.522 1.00 62.26 ? 118 LEU B CB 1 ATOM 3355 C CG . LEU B 2 118 ? 44.495 -36.545 -52.461 1.00 63.52 ? 118 LEU B CG 1 ATOM 3356 C CD1 . LEU B 2 118 ? 44.158 -37.958 -52.908 1.00 64.29 ? 118 LEU B CD1 1 ATOM 3357 C CD2 . LEU B 2 118 ? 43.289 -35.894 -51.799 1.00 62.66 ? 118 LEU B CD2 1 ATOM 3358 N N . TYR B 2 119 ? 47.858 -35.178 -53.307 1.00 66.02 ? 119 TYR B N 1 ATOM 3359 C CA . TYR B 2 119 ? 48.250 -34.396 -54.480 1.00 68.32 ? 119 TYR B CA 1 ATOM 3360 C C . TYR B 2 119 ? 49.275 -35.148 -55.327 1.00 69.97 ? 119 TYR B C 1 ATOM 3361 O O . TYR B 2 119 ? 49.137 -35.227 -56.546 1.00 72.29 ? 119 TYR B O 1 ATOM 3362 C CB . TYR B 2 119 ? 48.810 -33.030 -54.060 1.00 68.15 ? 119 TYR B CB 1 ATOM 3363 C CG . TYR B 2 119 ? 49.221 -32.148 -55.220 1.00 70.95 ? 119 TYR B CG 1 ATOM 3364 C CD1 . TYR B 2 119 ? 48.265 -31.533 -56.024 1.00 72.68 ? 119 TYR B CD1 1 ATOM 3365 C CD2 . TYR B 2 119 ? 50.563 -31.930 -55.517 1.00 72.30 ? 119 TYR B CD2 1 ATOM 3366 C CE1 . TYR B 2 119 ? 48.632 -30.727 -57.092 1.00 75.35 ? 119 TYR B CE1 1 ATOM 3367 C CE2 . TYR B 2 119 ? 50.942 -31.123 -56.581 1.00 74.95 ? 119 TYR B CE2 1 ATOM 3368 C CZ . TYR B 2 119 ? 49.973 -30.521 -57.370 1.00 76.60 ? 119 TYR B CZ 1 ATOM 3369 O OH . TYR B 2 119 ? 50.328 -29.716 -58.438 1.00 79.67 ? 119 TYR B OH 1 ATOM 3370 N N . GLU B 2 120 ? 50.291 -35.705 -54.673 1.00 69.30 ? 120 GLU B N 1 ATOM 3371 C CA . GLU B 2 120 ? 51.365 -36.415 -55.364 1.00 71.22 ? 120 GLU B CA 1 ATOM 3372 C C . GLU B 2 120 ? 50.880 -37.707 -56.014 1.00 71.92 ? 120 GLU B C 1 ATOM 3373 O O . GLU B 2 120 ? 51.309 -38.038 -57.117 1.00 74.00 ? 120 GLU B O 1 ATOM 3374 C CB . GLU B 2 120 ? 52.522 -36.719 -54.407 1.00 70.58 ? 120 GLU B CB 1 ATOM 3375 C CG . GLU B 2 120 ? 53.257 -35.486 -53.896 1.00 70.76 ? 120 GLU B CG 1 ATOM 3376 C CD . GLU B 2 120 ? 54.014 -34.756 -54.990 1.00 73.65 ? 120 GLU B CD 1 ATOM 3377 O OE1 . GLU B 2 120 ? 54.866 -35.390 -55.646 1.00 75.84 ? 120 GLU B OE1 1 ATOM 3378 O OE2 . GLU B 2 120 ? 53.748 -33.553 -55.199 1.00 74.23 ? 120 GLU B OE2 1 ATOM 3379 N N . ARG B 2 121 ? 49.992 -38.429 -55.334 1.00 70.04 ? 121 ARG B N 1 ATOM 3380 C CA . ARG B 2 121 ? 49.385 -39.640 -55.890 1.00 70.95 ? 121 ARG B CA 1 ATOM 3381 C C . ARG B 2 121 ? 48.781 -39.363 -57.261 1.00 73.54 ? 121 ARG B C 1 ATOM 3382 O O . ARG B 2 121 ? 49.017 -40.104 -58.213 1.00 75.22 ? 121 ARG B O 1 ATOM 3383 C CB . ARG B 2 121 ? 48.282 -40.163 -54.967 1.00 68.97 ? 121 ARG B CB 1 ATOM 3384 C CG . ARG B 2 121 ? 47.568 -41.412 -55.473 1.00 69.82 ? 121 ARG B CG 1 ATOM 3385 C CD . ARG B 2 121 ? 46.066 -41.350 -55.239 1.00 69.28 ? 121 ARG B CD 1 ATOM 3386 N NE . ARG B 2 121 ? 45.733 -41.437 -53.819 1.00 67.42 ? 121 ARG B NE 1 ATOM 3387 C CZ . ARG B 2 121 ? 44.498 -41.397 -53.319 1.00 66.82 ? 121 ARG B CZ 1 ATOM 3388 N NH1 . ARG B 2 121 ? 43.441 -41.270 -54.120 1.00 67.62 ? 121 ARG B NH1 1 ATOM 3389 N NH2 . ARG B 2 121 ? 44.318 -41.482 -52.000 1.00 64.99 ? 121 ARG B NH2 1 ATOM 3390 N N . VAL B 2 122 ? 47.996 -38.294 -57.343 1.00 73.92 ? 122 VAL B N 1 ATOM 3391 C CA . VAL B 2 122 ? 47.301 -37.941 -58.573 1.00 76.48 ? 122 VAL B CA 1 ATOM 3392 C C . VAL B 2 122 ? 48.301 -37.596 -59.669 1.00 79.18 ? 122 VAL B C 1 ATOM 3393 O O . VAL B 2 122 ? 48.175 -38.085 -60.784 1.00 81.08 ? 122 VAL B O 1 ATOM 3394 C CB . VAL B 2 122 ? 46.308 -36.780 -58.357 1.00 76.14 ? 122 VAL B CB 1 ATOM 3395 C CG1 . VAL B 2 122 ? 45.718 -36.316 -59.682 1.00 78.71 ? 122 VAL B CG1 1 ATOM 3396 C CG2 . VAL B 2 122 ? 45.199 -37.204 -57.402 1.00 74.32 ? 122 VAL B CG2 1 ATOM 3397 N N . LYS B 2 123 ? 49.298 -36.773 -59.351 1.00 79.59 ? 123 LYS B N 1 ATOM 3398 C CA . LYS B 2 123 ? 50.344 -36.449 -60.323 1.00 82.74 ? 123 LYS B CA 1 ATOM 3399 C C . LYS B 2 123 ? 50.953 -37.722 -60.897 1.00 84.26 ? 123 LYS B C 1 ATOM 3400 O O . LYS B 2 123 ? 51.124 -37.848 -62.114 1.00 86.71 ? 123 LYS B O 1 ATOM 3401 C CB . LYS B 2 123 ? 51.459 -35.616 -59.691 1.00 82.66 ? 123 LYS B CB 1 ATOM 3402 C CG . LYS B 2 123 ? 52.479 -35.108 -60.705 1.00 86.04 ? 123 LYS B CG 1 ATOM 3403 C CD . LYS B 2 123 ? 53.910 -35.300 -60.227 1.00 86.48 ? 123 LYS B CD 1 ATOM 3404 C CE . LYS B 2 123 ? 54.307 -34.266 -59.187 1.00 85.38 ? 123 LYS B CE 1 ATOM 3405 N NZ . LYS B 2 123 ? 54.432 -32.911 -59.790 1.00 87.65 ? 123 LYS B NZ 1 ATOM 3406 N N . ARG B 2 124 ? 51.274 -38.664 -60.016 1.00 82.64 ? 124 ARG B N 1 ATOM 3407 C CA . ARG B 2 124 ? 51.908 -39.912 -60.429 1.00 84.33 ? 124 ARG B CA 1 ATOM 3408 C C . ARG B 2 124 ? 51.015 -40.760 -61.334 1.00 85.76 ? 124 ARG B C 1 ATOM 3409 O O . ARG B 2 124 ? 51.526 -41.495 -62.180 1.00 88.27 ? 124 ARG B O 1 ATOM 3410 C CB . ARG B 2 124 ? 52.356 -40.721 -59.212 1.00 82.61 ? 124 ARG B CB 1 ATOM 3411 C CG . ARG B 2 124 ? 53.410 -40.011 -58.377 1.00 81.89 ? 124 ARG B CG 1 ATOM 3412 C CD . ARG B 2 124 ? 54.248 -40.976 -57.562 1.00 81.42 ? 124 ARG B CD 1 ATOM 3413 N NE . ARG B 2 124 ? 55.403 -40.303 -56.970 1.00 81.27 ? 124 ARG B NE 1 ATOM 3414 C CZ . ARG B 2 124 ? 55.404 -39.657 -55.807 1.00 78.72 ? 124 ARG B CZ 1 ATOM 3415 N NH1 . ARG B 2 124 ? 54.306 -39.582 -55.057 1.00 76.52 ? 124 ARG B NH1 1 ATOM 3416 N NH2 . ARG B 2 124 ? 56.522 -39.083 -55.387 1.00 78.98 ? 124 ARG B NH2 1 ATOM 3417 N N . GLN B 2 125 ? 49.696 -40.655 -61.164 1.00 84.40 ? 125 GLN B N 1 ATOM 3418 C CA . GLN B 2 125 ? 48.743 -41.344 -62.045 1.00 85.73 ? 125 GLN B CA 1 ATOM 3419 C C . GLN B 2 125 ? 48.748 -40.787 -63.473 1.00 88.60 ? 125 GLN B C 1 ATOM 3420 O O . GLN B 2 125 ? 48.730 -41.549 -64.441 1.00 91.36 ? 125 GLN B O 1 ATOM 3421 C CB . GLN B 2 125 ? 47.317 -41.249 -61.489 1.00 84.07 ? 125 GLN B CB 1 ATOM 3422 C CG . GLN B 2 125 ? 47.084 -41.990 -60.185 1.00 81.51 ? 125 GLN B CG 1 ATOM 3423 C CD . GLN B 2 125 ? 45.720 -41.698 -59.580 1.00 80.09 ? 125 GLN B CD 1 ATOM 3424 O OE1 . GLN B 2 125 ? 45.610 -40.981 -58.585 1.00 78.27 ? 125 GLN B OE1 1 ATOM 3425 N NE2 . GLN B 2 125 ? 44.672 -42.251 -60.181 1.00 81.22 ? 125 GLN B NE2 1 ATOM 3426 N N . LEU B 2 126 ? 48.774 -39.462 -63.598 1.00 88.66 ? 126 LEU B N 1 ATOM 3427 C CA . LEU B 2 126 ? 48.556 -38.803 -64.890 1.00 91.49 ? 126 LEU B CA 1 ATOM 3428 C C . LEU B 2 126 ? 49.709 -38.962 -65.883 1.00 93.79 ? 126 LEU B C 1 ATOM 3429 O O . LEU B 2 126 ? 49.471 -38.997 -67.084 1.00 97.13 ? 126 LEU B O 1 ATOM 3430 C CB . LEU B 2 126 ? 48.214 -37.322 -64.689 1.00 91.41 ? 126 LEU B CB 1 ATOM 3431 C CG . LEU B 2 126 ? 47.015 -37.059 -63.765 1.00 89.26 ? 126 LEU B CG 1 ATOM 3432 C CD1 . LEU B 2 126 ? 46.628 -35.586 -63.769 1.00 89.73 ? 126 LEU B CD1 1 ATOM 3433 C CD2 . LEU B 2 126 ? 45.818 -37.925 -64.134 1.00 89.72 ? 126 LEU B CD2 1 ATOM 3434 N N . ARG B 2 127 ? 50.942 -39.038 -65.393 1.00 92.83 ? 127 ARG B N 1 ATOM 3435 C CA . ARG B 2 127 ? 52.088 -39.431 -66.217 1.00 95.56 ? 127 ARG B CA 1 ATOM 3436 C C . ARG B 2 127 ? 52.174 -38.736 -67.584 1.00 99.34 ? 127 ARG B C 1 ATOM 3437 O O . ARG B 2 127 ? 51.971 -39.367 -68.631 1.00 101.94 ? 127 ARG B O 1 ATOM 3438 C CB . ARG B 2 127 ? 52.058 -40.945 -66.441 1.00 96.05 ? 127 ARG B CB 1 ATOM 3439 C CG . ARG B 2 127 ? 52.407 -41.775 -65.221 1.00 93.52 ? 127 ARG B CG 1 ATOM 3440 C CD . ARG B 2 127 ? 52.943 -43.143 -65.612 1.00 94.95 ? 127 ARG B CD 1 ATOM 3441 N NE . ARG B 2 127 ? 54.047 -43.048 -66.565 1.00 97.98 ? 127 ARG B NE 1 ATOM 3442 C CZ . ARG B 2 127 ? 54.746 -44.087 -67.010 1.00 99.87 ? 127 ARG B CZ 1 ATOM 3443 N NH1 . ARG B 2 127 ? 54.490 -45.314 -66.569 1.00 98.71 ? 127 ARG B NH1 1 ATOM 3444 N NH2 . ARG B 2 127 ? 55.723 -43.890 -67.890 1.00 102.94 ? 127 ARG B NH2 1 ATOM 3445 N N . GLU B 2 128 ? 52.466 -37.440 -67.577 1.00 99.64 ? 128 GLU B N 1 ATOM 3446 C CA . GLU B 2 128 ? 52.682 -36.683 -68.822 1.00 102.95 ? 128 GLU B CA 1 ATOM 3447 C C . GLU B 2 128 ? 51.407 -36.430 -69.653 1.00 104.19 ? 128 GLU B C 1 ATOM 3448 O O . GLU B 2 128 ? 51.478 -35.837 -70.733 1.00 107.88 ? 128 GLU B O 1 ATOM 3449 C CB . GLU B 2 128 ? 53.758 -37.366 -69.683 1.00 105.89 ? 128 GLU B CB 1 ATOM 3450 C CG . GLU B 2 128 ? 54.616 -36.405 -70.494 1.00 109.47 ? 128 GLU B CG 1 ATOM 3451 C CD . GLU B 2 128 ? 55.439 -35.469 -69.627 1.00 108.26 ? 128 GLU B CD 1 ATOM 3452 O OE1 . GLU B 2 128 ? 55.807 -35.861 -68.499 1.00 105.12 ? 128 GLU B OE1 1 ATOM 3453 O OE2 . GLU B 2 128 ? 55.712 -34.337 -70.078 1.00 110.42 ? 128 GLU B OE2 1 ATOM 3454 N N . ASN B 2 129 ? 50.251 -36.875 -69.156 1.00 101.85 ? 129 ASN B N 1 ATOM 3455 C CA . ASN B 2 129 ? 48.957 -36.506 -69.736 1.00 102.74 ? 129 ASN B CA 1 ATOM 3456 C C . ASN B 2 129 ? 48.424 -35.206 -69.125 1.00 101.70 ? 129 ASN B C 1 ATOM 3457 O O . ASN B 2 129 ? 47.380 -34.709 -69.543 1.00 102.80 ? 129 ASN B O 1 ATOM 3458 C CB . ASN B 2 129 ? 47.920 -37.618 -69.532 1.00 101.11 ? 129 ASN B CB 1 ATOM 3459 C CG . ASN B 2 129 ? 48.369 -38.959 -70.084 1.00 102.17 ? 129 ASN B CG 1 ATOM 3460 O OD1 . ASN B 2 129 ? 49.548 -39.171 -70.368 1.00 103.28 ? 129 ASN B OD1 1 ATOM 3461 N ND2 . ASN B 2 129 ? 47.423 -39.879 -70.227 1.00 101.89 ? 129 ASN B ND2 1 ATOM 3462 N N . ALA B 2 130 ? 49.131 -34.672 -68.127 1.00 99.99 ? 130 ALA B N 1 ATOM 3463 C CA . ALA B 2 130 ? 48.759 -33.411 -67.481 1.00 98.72 ? 130 ALA B CA 1 ATOM 3464 C C . ALA B 2 130 ? 49.989 -32.642 -66.994 1.00 98.54 ? 130 ALA B C 1 ATOM 3465 O O . ALA B 2 130 ? 51.090 -33.190 -66.919 1.00 98.21 ? 130 ALA B O 1 ATOM 3466 C CB . ALA B 2 130 ? 47.818 -33.681 -66.318 1.00 95.21 ? 130 ALA B CB 1 ATOM 3467 N N . GLU B 2 131 ? 49.787 -31.366 -66.672 1.00 98.84 ? 131 GLU B N 1 ATOM 3468 C CA . GLU B 2 131 ? 50.836 -30.524 -66.096 1.00 98.94 ? 131 GLU B CA 1 ATOM 3469 C C . GLU B 2 131 ? 50.334 -29.824 -64.834 1.00 96.54 ? 131 GLU B C 1 ATOM 3470 O O . GLU B 2 131 ? 49.126 -29.709 -64.615 1.00 95.26 ? 131 GLU B O 1 ATOM 3471 C CB . GLU B 2 131 ? 51.318 -29.491 -67.116 1.00 102.78 ? 131 GLU B CB 1 ATOM 3472 C CG . GLU B 2 131 ? 52.045 -30.097 -68.311 1.00 106.09 ? 131 GLU B CG 1 ATOM 3473 C CD . GLU B 2 131 ? 52.798 -29.073 -69.146 1.00 109.83 ? 131 GLU B CD 1 ATOM 3474 O OE1 . GLU B 2 131 ? 52.612 -27.857 -68.923 1.00 110.25 ? 131 GLU B OE1 1 ATOM 3475 O OE2 . GLU B 2 131 ? 53.579 -29.486 -70.032 1.00 112.21 ? 131 GLU B OE2 1 ATOM 3476 N N . GLU B 2 132 ? 51.273 -29.365 -64.009 1.00 96.11 ? 132 GLU B N 1 ATOM 3477 C CA . GLU B 2 132 ? 50.942 -28.692 -62.754 1.00 93.82 ? 132 GLU B CA 1 ATOM 3478 C C . GLU B 2 132 ? 50.564 -27.238 -62.976 1.00 95.49 ? 132 GLU B C 1 ATOM 3479 O O . GLU B 2 132 ? 51.332 -26.469 -63.549 1.00 97.95 ? 132 GLU B O 1 ATOM 3480 C CB . GLU B 2 132 ? 52.112 -28.748 -61.771 1.00 92.40 ? 132 GLU B CB 1 ATOM 3481 C CG . GLU B 2 132 ? 52.270 -30.082 -61.067 1.00 90.18 ? 132 GLU B CG 1 ATOM 3482 C CD . GLU B 2 132 ? 53.225 -30.009 -59.891 1.00 88.58 ? 132 GLU B CD 1 ATOM 3483 O OE1 . GLU B 2 132 ? 54.223 -29.261 -59.961 1.00 90.52 ? 132 GLU B OE1 1 ATOM 3484 O OE2 . GLU B 2 132 ? 52.985 -30.718 -58.896 1.00 85.92 ? 132 GLU B OE2 1 ATOM 3485 N N . ASP B 2 133 ? 49.379 -26.873 -62.502 1.00 94.57 ? 133 ASP B N 1 ATOM 3486 C CA . ASP B 2 133 ? 48.932 -25.487 -62.489 1.00 96.00 ? 133 ASP B CA 1 ATOM 3487 C C . ASP B 2 133 ? 49.774 -24.672 -61.505 1.00 94.43 ? 133 ASP B C 1 ATOM 3488 O O . ASP B 2 133 ? 50.287 -23.609 -61.850 1.00 96.63 ? 133 ASP B O 1 ATOM 3489 C CB . ASP B 2 133 ? 47.453 -25.431 -62.093 1.00 95.03 ? 133 ASP B CB 1 ATOM 3490 C CG . ASP B 2 133 ? 46.937 -24.021 -61.948 1.00 96.26 ? 133 ASP B CG 1 ATOM 3491 O OD1 . ASP B 2 133 ? 47.200 -23.191 -62.840 1.00 98.93 ? 133 ASP B OD1 1 ATOM 3492 O OD2 . ASP B 2 133 ? 46.261 -23.750 -60.934 1.00 94.54 ? 133 ASP B OD2 1 ATOM 3493 N N . GLY B 2 134 ? 49.912 -25.184 -60.285 1.00 90.88 ? 134 GLY B N 1 ATOM 3494 C CA . GLY B 2 134 ? 50.681 -24.511 -59.238 1.00 89.11 ? 134 GLY B CA 1 ATOM 3495 C C . GLY B 2 134 ? 49.826 -23.939 -58.121 1.00 86.49 ? 134 GLY B C 1 ATOM 3496 O O . GLY B 2 134 ? 50.356 -23.381 -57.160 1.00 85.15 ? 134 GLY B O 1 ATOM 3497 N N . THR B 2 135 ? 48.507 -24.072 -58.248 1.00 86.03 ? 135 THR B N 1 ATOM 3498 C CA . THR B 2 135 ? 47.565 -23.638 -57.215 1.00 83.79 ? 135 THR B CA 1 ATOM 3499 C C . THR B 2 135 ? 46.896 -24.849 -56.559 1.00 81.43 ? 135 THR B C 1 ATOM 3500 O O . THR B 2 135 ? 45.900 -24.708 -55.842 1.00 80.06 ? 135 THR B O 1 ATOM 3501 C CB . THR B 2 135 ? 46.468 -22.729 -57.805 1.00 85.75 ? 135 THR B CB 1 ATOM 3502 O OG1 . THR B 2 135 ? 45.620 -23.495 -58.671 1.00 86.23 ? 135 THR B OG1 1 ATOM 3503 C CG2 . THR B 2 135 ? 47.083 -21.565 -58.580 1.00 88.70 ? 135 THR B CG2 1 ATOM 3504 N N . GLY B 2 136 ? 47.458 -26.033 -56.795 1.00 81.21 ? 136 GLY B N 1 ATOM 3505 C CA . GLY B 2 136 ? 46.855 -27.281 -56.346 1.00 79.20 ? 136 GLY B CA 1 ATOM 3506 C C . GLY B 2 136 ? 45.832 -27.743 -57.357 1.00 80.85 ? 136 GLY B C 1 ATOM 3507 O O . GLY B 2 136 ? 44.686 -28.021 -57.005 1.00 80.15 ? 136 GLY B O 1 ATOM 3508 N N . CYS B 2 137 ? 46.253 -27.819 -58.618 1.00 100.86 ? 137 CYS B N 1 ATOM 3509 C CA . CYS B 2 137 ? 45.355 -28.185 -59.706 1.00 100.43 ? 137 CYS B CA 1 ATOM 3510 C C . CYS B 2 137 ? 46.125 -28.743 -60.914 1.00 98.15 ? 137 CYS B C 1 ATOM 3511 O O . CYS B 2 137 ? 47.288 -28.401 -61.129 1.00 97.42 ? 137 CYS B O 1 ATOM 3512 C CB . CYS B 2 137 ? 44.499 -26.975 -60.103 1.00 102.62 ? 137 CYS B CB 1 ATOM 3513 S SG . CYS B 2 137 ? 42.913 -27.422 -60.845 1.00 104.14 ? 137 CYS B SG 1 ATOM 3514 N N . PHE B 2 138 ? 45.470 -29.615 -61.680 1.00 97.04 ? 138 PHE B N 1 ATOM 3515 C CA . PHE B 2 138 ? 46.091 -30.282 -62.828 1.00 95.99 ? 138 PHE B CA 1 ATOM 3516 C C . PHE B 2 138 ? 45.359 -29.976 -64.136 1.00 96.74 ? 138 PHE B C 1 ATOM 3517 O O . PHE B 2 138 ? 44.216 -30.396 -64.324 1.00 97.02 ? 138 PHE B O 1 ATOM 3518 C CB . PHE B 2 138 ? 46.102 -31.798 -62.615 1.00 95.10 ? 138 PHE B CB 1 ATOM 3519 C CG . PHE B 2 138 ? 47.034 -32.256 -61.533 1.00 94.60 ? 138 PHE B CG 1 ATOM 3520 C CD1 . PHE B 2 138 ? 48.396 -32.361 -61.773 1.00 94.21 ? 138 PHE B CD1 1 ATOM 3521 C CD2 . PHE B 2 138 ? 46.551 -32.588 -60.276 1.00 94.73 ? 138 PHE B CD2 1 ATOM 3522 C CE1 . PHE B 2 138 ? 49.259 -32.787 -60.779 1.00 94.06 ? 138 PHE B CE1 1 ATOM 3523 C CE2 . PHE B 2 138 ? 47.409 -33.014 -59.279 1.00 94.63 ? 138 PHE B CE2 1 ATOM 3524 C CZ . PHE B 2 138 ? 48.764 -33.113 -59.530 1.00 94.45 ? 138 PHE B CZ 1 ATOM 3525 N N . GLU B 2 139 ? 46.023 -29.257 -65.039 1.00 97.00 ? 139 GLU B N 1 ATOM 3526 C CA . GLU B 2 139 ? 45.468 -28.990 -66.371 1.00 98.31 ? 139 GLU B CA 1 ATOM 3527 C C . GLU B 2 139 ? 45.642 -30.210 -67.273 1.00 98.21 ? 139 GLU B C 1 ATOM 3528 O O . GLU B 2 139 ? 46.762 -30.656 -67.516 1.00 97.35 ? 139 GLU B O 1 ATOM 3529 C CB . GLU B 2 139 ? 46.112 -27.753 -67.004 1.00 98.82 ? 139 GLU B CB 1 ATOM 3530 C CG . GLU B 2 139 ? 45.524 -26.445 -66.494 1.00 100.13 ? 139 GLU B CG 1 ATOM 3531 C CD . GLU B 2 139 ? 46.262 -25.215 -66.995 1.00 100.73 ? 139 GLU B CD 1 ATOM 3532 O OE1 . GLU B 2 139 ? 47.054 -25.332 -67.954 1.00 100.02 ? 139 GLU B OE1 1 ATOM 3533 O OE2 . GLU B 2 139 ? 46.048 -24.125 -66.421 1.00 101.72 ? 139 GLU B OE2 1 ATOM 3534 N N . ILE B 2 140 ? 44.521 -30.735 -67.761 1.00 99.62 ? 140 ILE B N 1 ATOM 3535 C CA . ILE B 2 140 ? 44.489 -31.962 -68.552 1.00 100.59 ? 140 ILE B CA 1 ATOM 3536 C C . ILE B 2 140 ? 44.353 -31.606 -70.033 1.00 103.15 ? 140 ILE B C 1 ATOM 3537 O O . ILE B 2 140 ? 43.405 -30.922 -70.424 1.00 104.63 ? 140 ILE B O 1 ATOM 3538 C CB . ILE B 2 140 ? 43.306 -32.864 -68.126 1.00 100.90 ? 140 ILE B CB 1 ATOM 3539 C CG1 . ILE B 2 140 ? 43.282 -33.031 -66.598 1.00 99.35 ? 140 ILE B CG1 1 ATOM 3540 C CG2 . ILE B 2 140 ? 43.390 -34.224 -68.810 1.00 101.38 ? 140 ILE B CG2 1 ATOM 3541 C CD1 . ILE B 2 140 ? 42.073 -33.772 -66.068 1.00 99.79 ? 140 ILE B CD1 1 ATOM 3542 N N . PHE B 2 141 ? 45.296 -32.077 -70.849 1.00 104.26 ? 141 PHE B N 1 ATOM 3543 C CA . PHE B 2 141 ? 45.308 -31.761 -72.280 1.00 107.34 ? 141 PHE B CA 1 ATOM 3544 C C . PHE B 2 141 ? 44.215 -32.490 -73.051 1.00 109.89 ? 141 PHE B C 1 ATOM 3545 O O . PHE B 2 141 ? 43.550 -31.890 -73.901 1.00 112.78 ? 141 PHE B O 1 ATOM 3546 C CB . PHE B 2 141 ? 46.669 -32.082 -72.903 1.00 107.82 ? 141 PHE B CB 1 ATOM 3547 C CG . PHE B 2 141 ? 47.796 -31.273 -72.338 1.00 106.65 ? 141 PHE B CG 1 ATOM 3548 C CD1 . PHE B 2 141 ? 47.773 -29.885 -72.406 1.00 107.33 ? 141 PHE B CD1 1 ATOM 3549 C CD2 . PHE B 2 141 ? 48.875 -31.895 -71.726 1.00 105.61 ? 141 PHE B CD2 1 ATOM 3550 C CE1 . PHE B 2 141 ? 48.807 -29.133 -71.873 1.00 106.55 ? 141 PHE B CE1 1 ATOM 3551 C CE2 . PHE B 2 141 ? 49.914 -31.150 -71.196 1.00 104.73 ? 141 PHE B CE2 1 ATOM 3552 C CZ . PHE B 2 141 ? 49.879 -29.767 -71.266 1.00 105.06 ? 141 PHE B CZ 1 ATOM 3553 N N . HIS B 2 142 ? 44.037 -33.779 -72.769 1.00 109.65 ? 142 HIS B N 1 ATOM 3554 C CA . HIS B 2 142 ? 42.991 -34.559 -73.430 1.00 112.25 ? 142 HIS B CA 1 ATOM 3555 C C . HIS B 2 142 ? 41.633 -34.299 -72.785 1.00 112.50 ? 142 HIS B C 1 ATOM 3556 O O . HIS B 2 142 ? 41.547 -33.713 -71.704 1.00 109.96 ? 142 HIS B O 1 ATOM 3557 C CB . HIS B 2 142 ? 43.319 -36.057 -73.418 1.00 112.54 ? 142 HIS B CB 1 ATOM 3558 C CG . HIS B 2 142 ? 43.104 -36.721 -72.093 1.00 110.62 ? 142 HIS B CG 1 ATOM 3559 N ND1 . HIS B 2 142 ? 41.878 -37.209 -71.695 1.00 111.47 ? 142 HIS B ND1 1 ATOM 3560 C CD2 . HIS B 2 142 ? 43.964 -37.000 -71.085 1.00 107.93 ? 142 HIS B CD2 1 ATOM 3561 C CE1 . HIS B 2 142 ? 41.988 -37.747 -70.493 1.00 109.34 ? 142 HIS B CE1 1 ATOM 3562 N NE2 . HIS B 2 142 ? 43.245 -37.636 -70.102 1.00 107.27 ? 142 HIS B NE2 1 ATOM 3563 N N . LYS B 2 143 ? 40.577 -34.749 -73.457 1.00 115.51 ? 143 LYS B N 1 ATOM 3564 C CA . LYS B 2 143 ? 39.211 -34.522 -72.995 1.00 116.68 ? 143 LYS B CA 1 ATOM 3565 C C . LYS B 2 143 ? 38.872 -35.559 -71.928 1.00 114.80 ? 143 LYS B C 1 ATOM 3566 O O . LYS B 2 143 ? 38.954 -36.760 -72.180 1.00 115.50 ? 143 LYS B O 1 ATOM 3567 C CB . LYS B 2 143 ? 38.215 -34.615 -74.161 1.00 121.14 ? 143 LYS B CB 1 ATOM 3568 C CG . LYS B 2 143 ? 38.573 -33.798 -75.403 1.00 123.78 ? 143 LYS B CG 1 ATOM 3569 C CD . LYS B 2 143 ? 38.064 -32.362 -75.357 1.00 124.82 ? 143 LYS B CD 1 ATOM 3570 C CE . LYS B 2 143 ? 38.797 -31.515 -74.327 1.00 121.37 ? 143 LYS B CE 1 ATOM 3571 N NZ . LYS B 2 143 ? 38.593 -30.061 -74.569 1.00 122.85 ? 143 LYS B NZ 1 ATOM 3572 N N . CYS B 2 144 ? 38.510 -35.092 -70.736 1.00 112.62 ? 144 CYS B N 1 ATOM 3573 C CA . CYS B 2 144 ? 38.211 -35.982 -69.613 1.00 111.05 ? 144 CYS B CA 1 ATOM 3574 C C . CYS B 2 144 ? 36.784 -35.738 -69.125 1.00 112.10 ? 144 CYS B C 1 ATOM 3575 O O . CYS B 2 144 ? 36.522 -34.786 -68.387 1.00 111.32 ? 144 CYS B O 1 ATOM 3576 C CB . CYS B 2 144 ? 39.230 -35.768 -68.486 1.00 107.87 ? 144 CYS B CB 1 ATOM 3577 S SG . CYS B 2 144 ? 39.154 -36.940 -67.102 1.00 106.42 ? 144 CYS B SG 1 ATOM 3578 N N . ASP B 2 145 ? 35.864 -36.598 -69.561 1.00 113.97 ? 145 ASP B N 1 ATOM 3579 C CA . ASP B 2 145 ? 34.453 -36.501 -69.174 1.00 115.48 ? 145 ASP B CA 1 ATOM 3580 C C . ASP B 2 145 ? 34.241 -36.965 -67.730 1.00 113.04 ? 145 ASP B C 1 ATOM 3581 O O . ASP B 2 145 ? 35.176 -37.419 -67.074 1.00 110.50 ? 145 ASP B O 1 ATOM 3582 C CB . ASP B 2 145 ? 33.563 -37.301 -70.145 1.00 118.97 ? 145 ASP B CB 1 ATOM 3583 C CG . ASP B 2 145 ? 33.707 -38.813 -69.987 1.00 118.65 ? 145 ASP B CG 1 ATOM 3584 O OD1 . ASP B 2 145 ? 34.784 -39.285 -69.564 1.00 116.26 ? 145 ASP B OD1 1 ATOM 3585 O OD2 . ASP B 2 145 ? 32.736 -39.534 -70.298 1.00 121.00 ? 145 ASP B OD2 1 ATOM 3586 N N . ASP B 2 146 ? 33.008 -36.847 -67.244 1.00 114.11 ? 146 ASP B N 1 ATOM 3587 C CA . ASP B 2 146 ? 32.673 -37.241 -65.873 1.00 112.38 ? 146 ASP B CA 1 ATOM 3588 C C . ASP B 2 146 ? 33.058 -38.691 -65.573 1.00 111.05 ? 146 ASP B C 1 ATOM 3589 O O . ASP B 2 146 ? 33.517 -38.998 -64.473 1.00 108.72 ? 146 ASP B O 1 ATOM 3590 C CB . ASP B 2 146 ? 31.180 -37.023 -65.595 1.00 114.80 ? 146 ASP B CB 1 ATOM 3591 C CG . ASP B 2 146 ? 30.804 -35.549 -65.501 1.00 115.97 ? 146 ASP B CG 1 ATOM 3592 O OD1 . ASP B 2 146 ? 31.707 -34.690 -65.396 1.00 114.15 ? 146 ASP B OD1 1 ATOM 3593 O OD2 . ASP B 2 146 ? 29.593 -35.250 -65.528 1.00 118.89 ? 146 ASP B OD2 1 ATOM 3594 N N . ASP B 2 147 ? 32.878 -39.574 -66.552 1.00 112.70 ? 147 ASP B N 1 ATOM 3595 C CA . ASP B 2 147 ? 33.313 -40.968 -66.432 1.00 111.97 ? 147 ASP B CA 1 ATOM 3596 C C . ASP B 2 147 ? 34.828 -41.032 -66.211 1.00 109.09 ? 147 ASP B C 1 ATOM 3597 O O . ASP B 2 147 ? 35.311 -41.789 -65.369 1.00 107.24 ? 147 ASP B O 1 ATOM 3598 C CB . ASP B 2 147 ? 32.925 -41.753 -67.693 1.00 115.10 ? 147 ASP B CB 1 ATOM 3599 C CG . ASP B 2 147 ? 32.936 -43.260 -67.483 1.00 115.42 ? 147 ASP B CG 1 ATOM 3600 O OD1 . ASP B 2 147 ? 33.869 -43.782 -66.841 1.00 113.03 ? 147 ASP B OD1 1 ATOM 3601 O OD2 . ASP B 2 147 ? 32.001 -43.928 -67.970 1.00 118.49 ? 147 ASP B OD2 1 ATOM 3602 N N . CYS B 2 148 ? 35.559 -40.224 -66.974 1.00 109.03 ? 148 CYS B N 1 ATOM 3603 C CA . CYS B 2 148 ? 37.017 -40.145 -66.887 1.00 106.93 ? 148 CYS B CA 1 ATOM 3604 C C . CYS B 2 148 ? 37.482 -39.562 -65.544 1.00 103.94 ? 148 CYS B C 1 ATOM 3605 O O . CYS B 2 148 ? 38.419 -40.080 -64.928 1.00 102.01 ? 148 CYS B O 1 ATOM 3606 C CB . CYS B 2 148 ? 37.557 -39.321 -68.067 1.00 108.41 ? 148 CYS B CB 1 ATOM 3607 S SG . CYS B 2 148 ? 39.278 -38.787 -67.959 1.00 106.85 ? 148 CYS B SG 1 ATOM 3608 N N . MET B 2 149 ? 36.822 -38.499 -65.088 1.00 103.40 ? 149 MET B N 1 ATOM 3609 C CA . MET B 2 149 ? 37.167 -37.866 -63.808 1.00 101.03 ? 149 MET B CA 1 ATOM 3610 C C . MET B 2 149 ? 37.009 -38.844 -62.640 1.00 99.74 ? 149 MET B C 1 ATOM 3611 O O . MET B 2 149 ? 37.862 -38.902 -61.754 1.00 98.12 ? 149 MET B O 1 ATOM 3612 C CB . MET B 2 149 ? 36.302 -36.623 -63.565 1.00 102.15 ? 149 MET B CB 1 ATOM 3613 C CG . MET B 2 149 ? 36.531 -35.477 -64.544 1.00 103.02 ? 149 MET B CG 1 ATOM 3614 S SD . MET B 2 149 ? 38.147 -34.691 -64.381 1.00 100.83 ? 149 MET B SD 1 ATOM 3615 C CE . MET B 2 149 ? 37.972 -33.311 -65.505 1.00 102.53 ? 149 MET B CE 1 ATOM 3616 N N . ALA B 2 150 ? 35.921 -39.610 -62.649 1.00 100.66 ? 150 ALA B N 1 ATOM 3617 C CA . ALA B 2 150 ? 35.663 -40.618 -61.618 1.00 99.82 ? 150 ALA B CA 1 ATOM 3618 C C . ALA B 2 150 ? 36.753 -41.695 -61.574 1.00 98.46 ? 150 ALA B C 1 ATOM 3619 O O . ALA B 2 150 ? 37.093 -42.197 -60.497 1.00 97.39 ? 150 ALA B O 1 ATOM 3620 C CB . ALA B 2 150 ? 34.298 -41.258 -61.835 1.00 101.80 ? 150 ALA B CB 1 ATOM 3621 N N . SER B 2 151 ? 37.295 -42.042 -62.742 1.00 98.54 ? 151 SER B N 1 ATOM 3622 C CA . SER B 2 151 ? 38.366 -43.039 -62.835 1.00 97.55 ? 151 SER B CA 1 ATOM 3623 C C . SER B 2 151 ? 39.636 -42.566 -62.133 1.00 95.13 ? 151 SER B C 1 ATOM 3624 O O . SER B 2 151 ? 40.362 -43.370 -61.547 1.00 94.66 ? 151 SER B O 1 ATOM 3625 C CB . SER B 2 151 ? 38.684 -43.361 -64.296 1.00 98.99 ? 151 SER B CB 1 ATOM 3626 O OG . SER B 2 151 ? 39.454 -42.328 -64.884 1.00 98.34 ? 151 SER B OG 1 ATOM 3627 N N . ILE B 2 152 ? 39.907 -41.265 -62.209 1.00 93.94 ? 152 ILE B N 1 ATOM 3628 C CA . ILE B 2 152 ? 41.046 -40.679 -61.510 1.00 92.32 ? 152 ILE B CA 1 ATOM 3629 C C . ILE B 2 152 ? 40.833 -40.800 -60.001 1.00 91.53 ? 152 ILE B C 1 ATOM 3630 O O . ILE B 2 152 ? 41.707 -41.285 -59.290 1.00 90.39 ? 152 ILE B O 1 ATOM 3631 C CB . ILE B 2 152 ? 41.264 -39.199 -61.899 1.00 91.98 ? 152 ILE B CB 1 ATOM 3632 C CG1 . ILE B 2 152 ? 41.721 -39.099 -63.358 1.00 92.60 ? 152 ILE B CG1 1 ATOM 3633 C CG2 . ILE B 2 152 ? 42.291 -38.544 -60.978 1.00 90.82 ? 152 ILE B CG2 1 ATOM 3634 C CD1 . ILE B 2 152 ? 41.750 -37.688 -63.906 1.00 92.66 ? 152 ILE B CD1 1 ATOM 3635 N N . ARG B 2 153 ? 39.658 -40.374 -59.541 1.00 92.19 ? 153 ARG B N 1 ATOM 3636 C CA . ARG B 2 153 ? 39.287 -40.418 -58.125 1.00 92.38 ? 153 ARG B CA 1 ATOM 3637 C C . ARG B 2 153 ? 39.330 -41.824 -57.525 1.00 92.59 ? 153 ARG B C 1 ATOM 3638 O O . ARG B 2 153 ? 39.679 -41.987 -56.359 1.00 92.47 ? 153 ARG B O 1 ATOM 3639 C CB . ARG B 2 153 ? 37.884 -39.834 -57.925 1.00 93.47 ? 153 ARG B CB 1 ATOM 3640 C CG . ARG B 2 153 ? 37.768 -38.350 -58.236 1.00 93.85 ? 153 ARG B CG 1 ATOM 3641 C CD . ARG B 2 153 ? 36.511 -37.757 -57.619 1.00 95.33 ? 153 ARG B CD 1 ATOM 3642 N NE . ARG B 2 153 ? 35.296 -38.338 -58.191 1.00 96.74 ? 153 ARG B NE 1 ATOM 3643 C CZ . ARG B 2 153 ? 34.574 -37.805 -59.180 1.00 98.20 ? 153 ARG B CZ 1 ATOM 3644 N NH1 . ARG B 2 153 ? 34.914 -36.647 -59.742 1.00 98.47 ? 153 ARG B NH1 1 ATOM 3645 N NH2 . ARG B 2 153 ? 33.488 -38.440 -59.610 1.00 99.63 ? 153 ARG B NH2 1 ATOM 3646 N N . ASN B 2 154 ? 38.974 -42.827 -58.326 1.00 93.71 ? 154 ASN B N 1 ATOM 3647 C CA . ASN B 2 154 ? 38.910 -44.218 -57.869 1.00 94.36 ? 154 ASN B CA 1 ATOM 3648 C C . ASN B 2 154 ? 40.171 -45.026 -58.186 1.00 94.13 ? 154 ASN B C 1 ATOM 3649 O O . ASN B 2 154 ? 40.193 -46.240 -57.985 1.00 94.76 ? 154 ASN B O 1 ATOM 3650 C CB . ASN B 2 154 ? 37.682 -44.911 -58.479 1.00 96.09 ? 154 ASN B CB 1 ATOM 3651 C CG . ASN B 2 154 ? 36.371 -44.265 -58.056 1.00 96.92 ? 154 ASN B CG 1 ATOM 3652 O OD1 . ASN B 2 154 ? 36.314 -43.524 -57.071 1.00 96.63 ? 154 ASN B OD1 1 ATOM 3653 N ND2 . ASN B 2 154 ? 35.306 -44.550 -58.800 1.00 98.55 ? 154 ASN B ND2 1 ATOM 3654 N N . ASN B 2 155 ? 41.209 -44.351 -58.681 1.00 93.52 ? 155 ASN B N 1 ATOM 3655 C CA . ASN B 2 155 ? 42.516 -44.966 -58.938 1.00 93.67 ? 155 ASN B CA 1 ATOM 3656 C C . ASN B 2 155 ? 42.520 -45.969 -60.104 1.00 95.31 ? 155 ASN B C 1 ATOM 3657 O O . ASN B 2 155 ? 43.398 -46.831 -60.182 1.00 96.01 ? 155 ASN B O 1 ATOM 3658 C CB . ASN B 2 155 ? 43.042 -45.637 -57.658 1.00 93.63 ? 155 ASN B CB 1 ATOM 3659 C CG . ASN B 2 155 ? 44.552 -45.550 -57.519 1.00 93.50 ? 155 ASN B CG 1 ATOM 3660 O OD1 . ASN B 2 155 ? 45.073 -45.525 -56.406 1.00 93.57 ? 155 ASN B OD1 1 ATOM 3661 N ND2 . ASN B 2 155 ? 45.260 -45.501 -58.641 1.00 93.65 ? 155 ASN B ND2 1 ATOM 3662 N N . THR B 2 156 ? 41.554 -45.841 -61.014 1.00 96.38 ? 156 THR B N 1 ATOM 3663 C CA . THR B 2 156 ? 41.414 -46.758 -62.152 1.00 98.36 ? 156 THR B CA 1 ATOM 3664 C C . THR B 2 156 ? 41.754 -46.089 -63.495 1.00 98.91 ? 156 THR B C 1 ATOM 3665 O O . THR B 2 156 ? 41.482 -46.650 -64.557 1.00 100.96 ? 156 THR B O 1 ATOM 3666 C CB . THR B 2 156 ? 39.979 -47.330 -62.223 1.00 99.75 ? 156 THR B CB 1 ATOM 3667 O OG1 . THR B 2 156 ? 39.051 -46.280 -62.524 1.00 99.74 ? 156 THR B OG1 1 ATOM 3668 C CG2 . THR B 2 156 ? 39.584 -47.981 -60.900 1.00 99.30 ? 156 THR B CG2 1 ATOM 3669 N N . TYR B 2 157 ? 42.357 -44.902 -63.443 1.00 97.44 ? 157 TYR B N 1 ATOM 3670 C CA . TYR B 2 157 ? 42.663 -44.121 -64.646 1.00 97.62 ? 157 TYR B CA 1 ATOM 3671 C C . TYR B 2 157 ? 43.889 -44.681 -65.361 1.00 98.70 ? 157 TYR B C 1 ATOM 3672 O O . TYR B 2 157 ? 44.976 -44.734 -64.790 1.00 97.59 ? 157 TYR B O 1 ATOM 3673 C CB . TYR B 2 157 ? 42.894 -42.649 -64.272 1.00 95.73 ? 157 TYR B CB 1 ATOM 3674 C CG . TYR B 2 157 ? 43.442 -41.776 -65.382 1.00 95.66 ? 157 TYR B CG 1 ATOM 3675 C CD1 . TYR B 2 157 ? 42.590 -41.114 -66.261 1.00 96.75 ? 157 TYR B CD1 1 ATOM 3676 C CD2 . TYR B 2 157 ? 44.812 -41.596 -65.540 1.00 94.95 ? 157 TYR B CD2 1 ATOM 3677 C CE1 . TYR B 2 157 ? 43.089 -40.309 -67.276 1.00 97.00 ? 157 TYR B CE1 1 ATOM 3678 C CE2 . TYR B 2 157 ? 45.321 -40.795 -66.549 1.00 95.25 ? 157 TYR B CE2 1 ATOM 3679 C CZ . TYR B 2 157 ? 44.457 -40.153 -67.416 1.00 96.11 ? 157 TYR B CZ 1 ATOM 3680 O OH . TYR B 2 157 ? 44.962 -39.353 -68.415 1.00 96.15 ? 157 TYR B OH 1 ATOM 3681 N N . ASP B 2 158 ? 43.704 -45.093 -66.612 1.00 101.22 ? 158 ASP B N 1 ATOM 3682 C CA . ASP B 2 158 ? 44.788 -45.642 -67.418 1.00 103.03 ? 158 ASP B CA 1 ATOM 3683 C C . ASP B 2 158 ? 45.381 -44.540 -68.298 1.00 103.14 ? 158 ASP B C 1 ATOM 3684 O O . ASP B 2 158 ? 44.753 -44.098 -69.266 1.00 104.13 ? 158 ASP B O 1 ATOM 3685 C CB . ASP B 2 158 ? 44.268 -46.801 -68.275 1.00 106.32 ? 158 ASP B CB 1 ATOM 3686 C CG . ASP B 2 158 ? 45.379 -47.558 -68.989 1.00 108.47 ? 158 ASP B CG 1 ATOM 3687 O OD1 . ASP B 2 158 ? 46.567 -47.206 -68.822 1.00 107.50 ? 158 ASP B OD1 1 ATOM 3688 O OD2 . ASP B 2 158 ? 45.058 -48.516 -69.723 1.00 111.56 ? 158 ASP B OD2 1 ATOM 3689 N N . HIS B 2 159 ? 46.595 -44.110 -67.957 1.00 102.05 ? 159 HIS B N 1 ATOM 3690 C CA . HIS B 2 159 ? 47.262 -43.014 -68.662 1.00 102.03 ? 159 HIS B CA 1 ATOM 3691 C C . HIS B 2 159 ? 47.600 -43.356 -70.116 1.00 105.04 ? 159 HIS B C 1 ATOM 3692 O O . HIS B 2 159 ? 47.617 -42.471 -70.969 1.00 105.24 ? 159 HIS B O 1 ATOM 3693 C CB . HIS B 2 159 ? 48.543 -42.597 -67.928 1.00 100.44 ? 159 HIS B CB 1 ATOM 3694 C CG . HIS B 2 159 ? 49.741 -43.425 -68.278 1.00 102.09 ? 159 HIS B CG 1 ATOM 3695 N ND1 . HIS B 2 159 ? 49.863 -44.749 -67.917 1.00 103.53 ? 159 HIS B ND1 1 ATOM 3696 C CD2 . HIS B 2 159 ? 50.870 -43.115 -68.959 1.00 102.88 ? 159 HIS B CD2 1 ATOM 3697 C CE1 . HIS B 2 159 ? 51.015 -45.220 -68.360 1.00 105.18 ? 159 HIS B CE1 1 ATOM 3698 N NE2 . HIS B 2 159 ? 51.646 -44.248 -68.994 1.00 104.79 ? 159 HIS B NE2 1 ATOM 3699 N N . SER B 2 160 ? 47.869 -44.634 -70.388 1.00 107.70 ? 160 SER B N 1 ATOM 3700 C CA . SER B 2 160 ? 48.298 -45.076 -71.718 1.00 111.28 ? 160 SER B CA 1 ATOM 3701 C C . SER B 2 160 ? 47.214 -44.924 -72.789 1.00 114.16 ? 160 SER B C 1 ATOM 3702 O O . SER B 2 160 ? 47.528 -44.794 -73.973 1.00 116.53 ? 160 SER B O 1 ATOM 3703 C CB . SER B 2 160 ? 48.782 -46.530 -71.672 1.00 113.36 ? 160 SER B CB 1 ATOM 3704 O OG . SER B 2 160 ? 47.746 -47.402 -71.258 1.00 113.85 ? 160 SER B OG 1 ATOM 3705 N N . LYS B 2 161 ? 45.948 -44.945 -72.374 1.00 114.52 ? 161 LYS B N 1 ATOM 3706 C CA . LYS B 2 161 ? 44.826 -44.818 -73.307 1.00 117.76 ? 161 LYS B CA 1 ATOM 3707 C C . LYS B 2 161 ? 44.741 -43.418 -73.899 1.00 117.14 ? 161 LYS B C 1 ATOM 3708 O O . LYS B 2 161 ? 44.517 -43.258 -75.100 1.00 120.05 ? 161 LYS B O 1 ATOM 3709 C CB . LYS B 2 161 ? 43.503 -45.155 -72.616 1.00 118.10 ? 161 LYS B CB 1 ATOM 3710 C CG . LYS B 2 161 ? 43.429 -46.580 -72.095 1.00 119.83 ? 161 LYS B CG 1 ATOM 3711 C CD . LYS B 2 161 ? 41.997 -47.004 -71.806 1.00 121.40 ? 161 LYS B CD 1 ATOM 3712 C CE . LYS B 2 161 ? 41.950 -48.240 -70.919 1.00 121.71 ? 161 LYS B CE 1 ATOM 3713 N NZ . LYS B 2 161 ? 40.612 -48.895 -70.938 1.00 123.98 ? 161 LYS B NZ 1 ATOM 3714 N N . TYR B 2 162 ? 44.926 -42.412 -73.050 1.00 113.60 ? 162 TYR B N 1 ATOM 3715 C CA . TYR B 2 162 ? 44.810 -41.018 -73.460 1.00 113.05 ? 162 TYR B CA 1 ATOM 3716 C C . TYR B 2 162 ? 46.165 -40.370 -73.754 1.00 111.64 ? 162 TYR B C 1 ATOM 3717 O O . TYR B 2 162 ? 46.227 -39.165 -73.997 1.00 110.66 ? 162 TYR B O 1 ATOM 3718 C CB . TYR B 2 162 ? 44.113 -40.213 -72.361 1.00 111.08 ? 162 TYR B CB 1 ATOM 3719 C CG . TYR B 2 162 ? 42.762 -40.745 -71.934 1.00 112.38 ? 162 TYR B CG 1 ATOM 3720 C CD1 . TYR B 2 162 ? 42.651 -41.690 -70.915 1.00 111.71 ? 162 TYR B CD1 1 ATOM 3721 C CD2 . TYR B 2 162 ? 41.591 -40.286 -72.532 1.00 114.46 ? 162 TYR B CD2 1 ATOM 3722 C CE1 . TYR B 2 162 ? 41.414 -42.172 -70.514 1.00 112.60 ? 162 TYR B CE1 1 ATOM 3723 C CE2 . TYR B 2 162 ? 40.351 -40.759 -72.136 1.00 115.59 ? 162 TYR B CE2 1 ATOM 3724 C CZ . TYR B 2 162 ? 40.268 -41.703 -71.129 1.00 114.60 ? 162 TYR B CZ 1 ATOM 3725 O OH . TYR B 2 162 ? 39.040 -42.177 -70.733 1.00 115.96 ? 162 TYR B OH 1 ATOM 3726 N N . ARG B 2 163 ? 47.243 -41.153 -73.742 1.00 111.73 ? 163 ARG B N 1 ATOM 3727 C CA . ARG B 2 163 ? 48.594 -40.584 -73.794 1.00 110.74 ? 163 ARG B CA 1 ATOM 3728 C C . ARG B 2 163 ? 48.866 -39.815 -75.082 1.00 112.50 ? 163 ARG B C 1 ATOM 3729 O O . ARG B 2 163 ? 49.214 -38.635 -75.043 1.00 111.03 ? 163 ARG B O 1 ATOM 3730 C CB . ARG B 2 163 ? 49.669 -41.665 -73.610 1.00 111.50 ? 163 ARG B CB 1 ATOM 3731 C CG . ARG B 2 163 ? 51.078 -41.089 -73.542 1.00 110.43 ? 163 ARG B CG 1 ATOM 3732 C CD . ARG B 2 163 ? 52.134 -42.109 -73.145 1.00 111.13 ? 163 ARG B CD 1 ATOM 3733 N NE . ARG B 2 163 ? 53.334 -41.450 -72.624 1.00 109.63 ? 163 ARG B NE 1 ATOM 3734 C CZ . ARG B 2 163 ? 54.488 -42.060 -72.355 1.00 110.51 ? 163 ARG B CZ 1 ATOM 3735 N NH1 . ARG B 2 163 ? 54.633 -43.367 -72.553 1.00 113.09 ? 163 ARG B NH1 1 ATOM 3736 N NH2 . ARG B 2 163 ? 55.509 -41.355 -71.882 1.00 109.09 ? 163 ARG B NH2 1 ATOM 3737 N N . GLU B 2 164 ? 48.704 -40.487 -76.215 1.00 116.18 ? 164 GLU B N 1 ATOM 3738 C CA . GLU B 2 164 ? 49.055 -39.905 -77.511 1.00 118.58 ? 164 GLU B CA 1 ATOM 3739 C C . GLU B 2 164 ? 48.358 -38.565 -77.753 1.00 117.65 ? 164 GLU B C 1 ATOM 3740 O O . GLU B 2 164 ? 49.011 -37.580 -78.096 1.00 116.85 ? 164 GLU B O 1 ATOM 3741 C CB . GLU B 2 164 ? 48.733 -40.884 -78.647 1.00 123.44 ? 164 GLU B CB 1 ATOM 3742 C CG . GLU B 2 164 ? 49.523 -42.190 -78.619 1.00 125.24 ? 164 GLU B CG 1 ATOM 3743 C CD . GLU B 2 164 ? 51.012 -41.996 -78.850 1.00 125.25 ? 164 GLU B CD 1 ATOM 3744 O OE1 . GLU B 2 164 ? 51.700 -41.490 -77.936 1.00 121.89 ? 164 GLU B OE1 1 ATOM 3745 O OE2 . GLU B 2 164 ? 51.497 -42.365 -79.942 1.00 128.96 ? 164 GLU B OE2 1 ATOM 3746 N N . GLU B 2 165 ? 47.043 -38.531 -77.554 1.00 117.72 ? 165 GLU B N 1 ATOM 3747 C CA . GLU B 2 165 ? 46.260 -37.302 -77.757 1.00 117.59 ? 165 GLU B CA 1 ATOM 3748 C C . GLU B 2 165 ? 46.657 -36.164 -76.805 1.00 114.11 ? 165 GLU B C 1 ATOM 3749 O O . GLU B 2 165 ? 46.693 -35.003 -77.214 1.00 114.18 ? 165 GLU B O 1 ATOM 3750 C CB . GLU B 2 165 ? 44.742 -37.567 -77.686 1.00 119.09 ? 165 GLU B CB 1 ATOM 3751 C CG . GLU B 2 165 ? 44.290 -38.597 -76.656 1.00 117.91 ? 165 GLU B CG 1 ATOM 3752 C CD . GLU B 2 165 ? 42.781 -38.655 -76.492 1.00 119.19 ? 165 GLU B CD 1 ATOM 3753 O OE1 . GLU B 2 165 ? 42.134 -37.586 -76.451 1.00 118.83 ? 165 GLU B OE1 1 ATOM 3754 O OE2 . GLU B 2 165 ? 42.243 -39.779 -76.392 1.00 120.64 ? 165 GLU B OE2 1 ATOM 3755 N N . ALA B 2 166 ? 46.957 -36.497 -75.549 1.00 111.28 ? 166 ALA B N 1 ATOM 3756 C CA . ALA B 2 166 ? 47.400 -35.503 -74.566 1.00 108.24 ? 166 ALA B CA 1 ATOM 3757 C C . ALA B 2 166 ? 48.820 -35.025 -74.865 1.00 107.77 ? 166 ALA B C 1 ATOM 3758 O O . ALA B 2 166 ? 49.102 -33.826 -74.818 1.00 106.69 ? 166 ALA B O 1 ATOM 3759 C CB . ALA B 2 166 ? 47.327 -36.079 -73.162 1.00 106.02 ? 166 ALA B CB 1 ATOM 3760 N N . MET B 2 167 ? 49.706 -35.978 -75.151 1.00 108.79 ? 167 MET B N 1 ATOM 3761 C CA . MET B 2 167 ? 51.080 -35.690 -75.574 1.00 109.12 ? 167 MET B CA 1 ATOM 3762 C C . MET B 2 167 ? 51.121 -34.698 -76.734 1.00 110.97 ? 167 MET B C 1 ATOM 3763 O O . MET B 2 167 ? 51.832 -33.695 -76.675 1.00 109.56 ? 167 MET B O 1 ATOM 3764 C CB . MET B 2 167 ? 51.783 -36.980 -76.012 1.00 111.09 ? 167 MET B CB 1 ATOM 3765 C CG . MET B 2 167 ? 52.374 -37.799 -74.881 1.00 109.62 ? 167 MET B CG 1 ATOM 3766 S SD . MET B 2 167 ? 53.981 -37.160 -74.377 1.00 108.01 ? 167 MET B SD 1 ATOM 3767 C CE . MET B 2 167 ? 54.674 -38.569 -73.519 1.00 108.20 ? 167 MET B CE 1 ATOM 3768 N N . GLN B 2 168 ? 50.359 -34.996 -77.785 1.00 114.09 ? 168 GLN B N 1 ATOM 3769 C CA . GLN B 2 168 ? 50.309 -34.153 -78.980 1.00 116.61 ? 168 GLN B CA 1 ATOM 3770 C C . GLN B 2 168 ? 49.815 -32.744 -78.646 1.00 114.97 ? 168 GLN B C 1 ATOM 3771 O O . GLN B 2 168 ? 50.349 -31.755 -79.153 1.00 115.42 ? 168 GLN B O 1 ATOM 3772 C CB . GLN B 2 168 ? 49.399 -34.779 -80.044 1.00 120.89 ? 168 GLN B CB 1 ATOM 3773 C CG . GLN B 2 168 ? 49.875 -36.125 -80.584 1.00 123.69 ? 168 GLN B CG 1 ATOM 3774 C CD . GLN B 2 168 ? 50.707 -36.016 -81.849 1.00 127.16 ? 168 GLN B CD 1 ATOM 3775 O OE1 . GLN B 2 168 ? 51.837 -36.500 -81.898 1.00 128.14 ? 168 GLN B OE1 1 ATOM 3776 N NE2 . GLN B 2 168 ? 50.150 -35.391 -82.881 1.00 129.75 ? 168 GLN B NE2 1 ATOM 3777 N N . ASN B 2 169 ? 48.809 -32.662 -77.777 1.00 113.33 ? 169 ASN B N 1 ATOM 3778 C CA . ASN B 2 169 ? 48.210 -31.381 -77.393 1.00 112.29 ? 169 ASN B CA 1 ATOM 3779 C C . ASN B 2 169 ? 49.085 -30.513 -76.474 1.00 109.52 ? 169 ASN B C 1 ATOM 3780 O O . ASN B 2 169 ? 48.670 -29.417 -76.094 1.00 108.92 ? 169 ASN B O 1 ATOM 3781 C CB . ASN B 2 169 ? 46.837 -31.612 -76.742 1.00 112.17 ? 169 ASN B CB 1 ATOM 3782 C CG . ASN B 2 169 ? 45.791 -32.113 -77.730 1.00 115.67 ? 169 ASN B CG 1 ATOM 3783 O OD1 . ASN B 2 169 ? 45.954 -32.000 -78.949 1.00 118.22 ? 169 ASN B OD1 1 ATOM 3784 N ND2 . ASN B 2 169 ? 44.703 -32.667 -77.203 1.00 115.80 ? 169 ASN B ND2 1 ATOM 3785 N N . ARG B 2 170 ? 50.276 -31.003 -76.114 1.00 108.16 ? 170 ARG B N 1 ATOM 3786 C CA . ARG B 2 170 ? 51.274 -30.215 -75.371 1.00 105.86 ? 170 ARG B CA 1 ATOM 3787 C C . ARG B 2 170 ? 51.320 -28.757 -75.830 1.00 106.56 ? 170 ARG B C 1 ATOM 3788 O O . ARG B 2 170 ? 52.134 -27.966 -75.349 1.00 105.52 ? 170 ARG B O 1 ATOM 3789 C CB . ARG B 2 170 ? 52.672 -30.845 -75.507 1.00 105.34 ? 170 ARG B CB 1 ATOM 3790 C CG . ARG B 2 170 ? 53.172 -31.007 -76.941 1.00 107.43 ? 170 ARG B CG 1 ATOM 3791 C CD . ARG B 2 170 ? 54.084 -29.877 -77.408 1.00 107.30 ? 170 ARG B CD 1 ATOM 3792 N NE . ARG B 2 170 ? 54.027 -29.698 -78.865 1.00 109.60 ? 170 ARG B NE 1 ATOM 3793 C CZ . ARG B 2 170 ? 53.433 -28.688 -79.506 1.00 110.61 ? 170 ARG B CZ 1 ATOM 3794 N NH1 . ARG B 2 170 ? 52.825 -27.706 -78.847 1.00 109.28 ? 170 ARG B NH1 1 ATOM 3795 N NH2 . ARG B 2 170 ? 53.453 -28.651 -80.833 1.00 113.32 ? 170 ARG B NH2 1 HETATM 3796 C C1 . NAG C 3 . ? 34.735 -32.113 -32.888 1.00 73.38 ? 1317 NAG A C1 1 HETATM 3797 C C2 . NAG C 3 . ? 33.764 -33.238 -33.270 1.00 80.44 ? 1317 NAG A C2 1 HETATM 3798 C C3 . NAG C 3 . ? 32.871 -33.661 -32.096 1.00 83.87 ? 1317 NAG A C3 1 HETATM 3799 C C4 . NAG C 3 . ? 33.650 -33.804 -30.792 1.00 84.77 ? 1317 NAG A C4 1 HETATM 3800 C C5 . NAG C 3 . ? 34.540 -32.584 -30.567 1.00 84.19 ? 1317 NAG A C5 1 HETATM 3801 C C6 . NAG C 3 . ? 35.371 -32.711 -29.289 1.00 84.00 ? 1317 NAG A C6 1 HETATM 3802 C C7 . NAG C 3 . ? 33.281 -32.993 -35.667 1.00 81.13 ? 1317 NAG A C7 1 HETATM 3803 C C8 . NAG C 3 . ? 32.318 -32.493 -36.707 1.00 80.54 ? 1317 NAG A C8 1 HETATM 3804 N N2 . NAG C 3 . ? 32.936 -32.813 -34.388 1.00 80.15 ? 1317 NAG A N2 1 HETATM 3805 O O3 . NAG C 3 . ? 32.240 -34.891 -32.382 1.00 85.45 ? 1317 NAG A O3 1 HETATM 3806 O O4 . NAG C 3 . ? 32.750 -33.987 -29.717 1.00 84.87 ? 1317 NAG A O4 1 HETATM 3807 O O5 . NAG C 3 . ? 35.405 -32.454 -31.680 1.00 79.69 ? 1317 NAG A O5 1 HETATM 3808 O O6 . NAG C 3 . ? 34.944 -31.796 -28.298 1.00 81.68 ? 1317 NAG A O6 1 HETATM 3809 O O7 . NAG C 3 . ? 34.327 -33.535 -36.023 1.00 81.49 ? 1317 NAG A O7 1 HETATM 3810 C C1 . NAG D 3 . ? 52.868 -65.723 17.822 1.00 75.71 ? 1318 NAG A C1 1 HETATM 3811 C C2 . NAG D 3 . ? 53.222 -66.291 16.451 1.00 86.34 ? 1318 NAG A C2 1 HETATM 3812 C C3 . NAG D 3 . ? 52.310 -67.484 16.172 1.00 87.88 ? 1318 NAG A C3 1 HETATM 3813 C C4 . NAG D 3 . ? 52.435 -68.525 17.283 1.00 88.84 ? 1318 NAG A C4 1 HETATM 3814 C C5 . NAG D 3 . ? 52.390 -67.908 18.685 1.00 88.16 ? 1318 NAG A C5 1 HETATM 3815 C C6 . NAG D 3 . ? 52.894 -68.910 19.728 1.00 88.47 ? 1318 NAG A C6 1 HETATM 3816 C C7 . NAG D 3 . ? 54.095 -64.412 15.127 1.00 94.88 ? 1318 NAG A C7 1 HETATM 3817 C C8 . NAG D 3 . ? 53.857 -63.439 14.006 1.00 94.65 ? 1318 NAG A C8 1 HETATM 3818 N N2 . NAG D 3 . ? 53.120 -65.291 15.394 1.00 91.45 ? 1318 NAG A N2 1 HETATM 3819 O O3 . NAG D 3 . ? 52.644 -68.083 14.939 1.00 87.91 ? 1318 NAG A O3 1 HETATM 3820 O O4 . NAG D 3 . ? 51.398 -69.474 17.150 1.00 90.83 ? 1318 NAG A O4 1 HETATM 3821 O O5 . NAG D 3 . ? 53.179 -66.730 18.766 1.00 82.81 ? 1318 NAG A O5 1 HETATM 3822 O O6 . NAG D 3 . ? 52.060 -68.916 20.867 1.00 87.20 ? 1318 NAG A O6 1 HETATM 3823 O O7 . NAG D 3 . ? 55.156 -64.362 15.753 1.00 99.09 ? 1318 NAG A O7 1 HETATM 3824 C C1 . NAG E 3 . ? 32.284 -17.664 -35.450 1.00 79.80 ? 1319 NAG A C1 1 HETATM 3825 C C2 . NAG E 3 . ? 32.265 -18.734 -34.335 1.00 86.48 ? 1319 NAG A C2 1 HETATM 3826 C C3 . NAG E 3 . ? 30.924 -18.872 -33.611 1.00 89.07 ? 1319 NAG A C3 1 HETATM 3827 C C4 . NAG E 3 . ? 30.275 -17.533 -33.290 1.00 92.46 ? 1319 NAG A C4 1 HETATM 3828 C C5 . NAG E 3 . ? 30.228 -16.683 -34.555 1.00 93.31 ? 1319 NAG A C5 1 HETATM 3829 C C6 . NAG E 3 . ? 29.637 -15.293 -34.301 1.00 95.26 ? 1319 NAG A C6 1 HETATM 3830 C C7 . NAG E 3 . ? 33.317 -20.959 -34.174 1.00 88.04 ? 1319 NAG A C7 1 HETATM 3831 C C8 . NAG E 3 . ? 33.521 -22.299 -34.821 1.00 88.47 ? 1319 NAG A C8 1 HETATM 3832 N N2 . NAG E 3 . ? 32.563 -20.071 -34.835 1.00 88.07 ? 1319 NAG A N2 1 HETATM 3833 O O3 . NAG E 3 . ? 31.107 -19.601 -32.417 1.00 88.68 ? 1319 NAG A O3 1 HETATM 3834 O O4 . NAG E 3 . ? 28.974 -17.759 -32.788 1.00 92.05 ? 1319 NAG A O4 1 HETATM 3835 O O5 . NAG E 3 . ? 31.545 -16.515 -35.049 1.00 86.76 ? 1319 NAG A O5 1 HETATM 3836 O O6 . NAG E 3 . ? 28.522 -15.336 -33.431 1.00 97.75 ? 1319 NAG A O6 1 HETATM 3837 O O7 . NAG E 3 . ? 33.846 -20.728 -33.088 1.00 89.87 ? 1319 NAG A O7 1 HETATM 3838 C C1 . NAG F 3 . ? 30.876 -46.616 41.391 1.00 68.30 ? 1320 NAG A C1 1 HETATM 3839 C C2 . NAG F 3 . ? 29.460 -46.296 41.881 1.00 76.67 ? 1320 NAG A C2 1 HETATM 3840 C C3 . NAG F 3 . ? 29.376 -46.233 43.405 1.00 80.02 ? 1320 NAG A C3 1 HETATM 3841 C C4 . NAG F 3 . ? 29.953 -47.513 44.001 1.00 80.40 ? 1320 NAG A C4 1 HETATM 3842 C C5 . NAG F 3 . ? 31.391 -47.677 43.517 1.00 78.79 ? 1320 NAG A C5 1 HETATM 3843 C C6 . NAG F 3 . ? 32.000 -48.951 44.105 1.00 80.26 ? 1320 NAG A C6 1 HETATM 3844 C C7 . NAG F 3 . ? 27.744 -44.865 40.871 1.00 78.42 ? 1320 NAG A C7 1 HETATM 3845 C C8 . NAG F 3 . ? 27.394 -43.512 40.318 1.00 77.54 ? 1320 NAG A C8 1 HETATM 3846 N N2 . NAG F 3 . ? 28.994 -45.040 41.314 1.00 76.70 ? 1320 NAG A N2 1 HETATM 3847 O O3 . NAG F 3 . ? 28.035 -46.051 43.823 1.00 79.55 ? 1320 NAG A O3 1 HETATM 3848 O O4 . NAG F 3 . ? 29.910 -47.468 45.415 1.00 81.68 ? 1320 NAG A O4 1 HETATM 3849 O O5 . NAG F 3 . ? 31.442 -47.713 42.095 1.00 75.32 ? 1320 NAG A O5 1 HETATM 3850 O O6 . NAG F 3 . ? 33.064 -49.440 43.317 1.00 79.44 ? 1320 NAG A O6 1 HETATM 3851 O O7 . NAG F 3 . ? 26.883 -45.745 40.895 1.00 81.49 ? 1320 NAG A O7 1 HETATM 3852 C C1 . SIA G 4 . ? 31.182 -33.238 35.656 1.00 67.92 ? 1321 SIA A C1 1 HETATM 3853 C C2 . SIA G 4 . ? 31.368 -33.180 37.163 1.00 66.71 ? 1321 SIA A C2 1 HETATM 3854 C C3 . SIA G 4 . ? 30.637 -34.333 37.867 1.00 64.20 ? 1321 SIA A C3 1 HETATM 3855 C C4 . SIA G 4 . ? 31.387 -35.652 37.740 1.00 63.09 ? 1321 SIA A C4 1 HETATM 3856 C C5 . SIA G 4 . ? 32.834 -35.502 38.188 1.00 62.43 ? 1321 SIA A C5 1 HETATM 3857 C C6 . SIA G 4 . ? 33.467 -34.408 37.331 1.00 61.89 ? 1321 SIA A C6 1 HETATM 3858 C C7 . SIA G 4 . ? 34.967 -34.214 37.561 1.00 60.91 ? 1321 SIA A C7 1 HETATM 3859 C C8 . SIA G 4 . ? 35.499 -32.967 36.857 1.00 60.47 ? 1321 SIA A C8 1 HETATM 3860 C C9 . SIA G 4 . ? 37.022 -32.966 36.817 1.00 58.87 ? 1321 SIA A C9 1 HETATM 3861 C C10 . SIA G 4 . ? 34.502 -37.293 38.487 1.00 61.62 ? 1321 SIA A C10 1 HETATM 3862 C C11 . SIA G 4 . ? 34.997 -38.607 37.967 1.00 62.51 ? 1321 SIA A C11 1 HETATM 3863 N N5 . SIA G 4 . ? 33.464 -36.771 37.847 1.00 60.44 ? 1321 SIA A N5 1 HETATM 3864 O O1A . SIA G 4 . ? 30.014 -33.280 35.199 1.00 66.35 ? 1321 SIA A O1A 1 HETATM 3865 O O1B . SIA G 4 . ? 32.189 -33.193 34.911 1.00 67.72 ? 1321 SIA A O1B 1 HETATM 3866 O O4 . SIA G 4 . ? 30.738 -36.682 38.490 1.00 65.57 ? 1321 SIA A O4 1 HETATM 3867 O O6 . SIA G 4 . ? 32.759 -33.180 37.548 1.00 63.36 ? 1321 SIA A O6 1 HETATM 3868 O O7 . SIA G 4 . ? 35.251 -34.120 38.954 1.00 61.90 ? 1321 SIA A O7 1 HETATM 3869 O O8 . SIA G 4 . ? 34.990 -32.905 35.520 1.00 59.31 ? 1321 SIA A O8 1 HETATM 3870 O O9 . SIA G 4 . ? 37.473 -31.811 36.104 1.00 60.23 ? 1321 SIA A O9 1 HETATM 3871 O O10 . SIA G 4 . ? 35.032 -36.749 39.435 1.00 65.72 ? 1321 SIA A O10 1 HETATM 3872 C C1 . GAL H 5 . ? 29.369 -28.425 39.184 1.00 96.06 ? 1322 GAL A C1 1 HETATM 3873 C C2 . GAL H 5 . ? 29.657 -27.087 38.504 1.00 92.96 ? 1322 GAL A C2 1 HETATM 3874 C C3 . GAL H 5 . ? 29.680 -27.279 36.988 1.00 90.93 ? 1322 GAL A C3 1 HETATM 3875 C C4 . GAL H 5 . ? 30.662 -28.381 36.607 1.00 87.64 ? 1322 GAL A C4 1 HETATM 3876 C C5 . GAL H 5 . ? 30.300 -29.653 37.356 1.00 84.50 ? 1322 GAL A C5 1 HETATM 3877 C C6 . GAL H 5 . ? 31.282 -30.768 37.051 1.00 78.52 ? 1322 GAL A C6 1 HETATM 3878 O O2 . GAL H 5 . ? 28.649 -26.131 38.853 1.00 91.35 ? 1322 GAL A O2 1 HETATM 3879 O O3 . GAL H 5 . ? 30.035 -26.059 36.333 1.00 95.52 ? 1322 GAL A O3 1 HETATM 3880 O O4 . GAL H 5 . ? 32.004 -28.002 36.942 1.00 82.69 ? 1322 GAL A O4 1 HETATM 3881 O O5 . GAL H 5 . ? 30.322 -29.404 38.762 1.00 92.70 ? 1322 GAL A O5 1 HETATM 3882 O O6 . GAL H 5 . ? 30.745 -31.972 37.597 1.00 72.52 ? 1322 GAL A O6 1 HETATM 3883 C C1 . NAG I 3 . ? 27.615 -30.252 43.840 1.00 107.55 ? 1323 NAG A C1 1 HETATM 3884 C C2 . NAG I 3 . ? 28.519 -31.113 42.958 1.00 108.04 ? 1323 NAG A C2 1 HETATM 3885 C C3 . NAG I 3 . ? 29.415 -30.259 42.062 1.00 106.37 ? 1323 NAG A C3 1 HETATM 3886 C C4 . NAG I 3 . ? 28.581 -29.221 41.312 1.00 104.67 ? 1323 NAG A C4 1 HETATM 3887 C C5 . NAG I 3 . ? 27.676 -28.452 42.278 1.00 105.37 ? 1323 NAG A C5 1 HETATM 3888 C C6 . NAG I 3 . ? 26.777 -27.451 41.556 1.00 104.15 ? 1323 NAG A C6 1 HETATM 3889 C C7 . NAG I 3 . ? 29.309 -33.152 44.154 1.00 108.08 ? 1323 NAG A C7 1 HETATM 3890 C C8 . NAG I 3 . ? 28.206 -33.968 43.539 1.00 106.21 ? 1323 NAG A C8 1 HETATM 3891 N N2 . NAG I 3 . ? 29.408 -31.850 43.855 1.00 108.42 ? 1323 NAG A N2 1 HETATM 3892 O O1 . NAG I 3 . ? 26.727 -31.075 44.598 1.00 106.50 ? 1323 NAG A O1 1 HETATM 3893 O O3 . NAG I 3 . ? 30.099 -31.105 41.130 1.00 103.52 ? 1323 NAG A O3 1 HETATM 3894 O O4 . NAG I 3 . ? 29.433 -28.304 40.611 1.00 101.39 ? 1323 NAG A O4 1 HETATM 3895 O O5 . NAG I 3 . ? 26.857 -29.370 43.010 1.00 107.33 ? 1323 NAG A O5 1 HETATM 3896 O O6 . NAG I 3 . ? 25.922 -28.126 40.625 1.00 103.12 ? 1323 NAG A O6 1 HETATM 3897 O O7 . NAG I 3 . ? 30.104 -33.671 44.917 1.00 109.31 ? 1323 NAG A O7 1 HETATM 3898 S S . SO4 J 6 . ? 37.770 -53.633 44.705 1.00 121.71 ? 1324 SO4 A S 1 HETATM 3899 O O1 . SO4 J 6 . ? 38.047 -52.197 44.948 1.00 119.29 ? 1324 SO4 A O1 1 HETATM 3900 O O2 . SO4 J 6 . ? 38.929 -54.438 45.152 1.00 121.22 ? 1324 SO4 A O2 1 HETATM 3901 O O3 . SO4 J 6 . ? 37.538 -53.856 43.261 1.00 119.96 ? 1324 SO4 A O3 1 HETATM 3902 O O4 . SO4 J 6 . ? 36.563 -54.047 45.457 1.00 120.41 ? 1324 SO4 A O4 1 HETATM 3903 S S . SO4 K 6 . ? 29.759 -26.481 -8.484 1.00 111.75 ? 1325 SO4 A S 1 HETATM 3904 O O1 . SO4 K 6 . ? 30.556 -25.248 -8.686 1.00 112.21 ? 1325 SO4 A O1 1 HETATM 3905 O O2 . SO4 K 6 . ? 29.762 -27.285 -9.727 1.00 110.76 ? 1325 SO4 A O2 1 HETATM 3906 O O3 . SO4 K 6 . ? 28.359 -26.123 -8.151 1.00 114.48 ? 1325 SO4 A O3 1 HETATM 3907 O O4 . SO4 K 6 . ? 30.344 -27.262 -7.372 1.00 108.69 ? 1325 SO4 A O4 1 HETATM 3908 S S . SO4 L 6 . ? 33.529 -23.117 -16.823 1.00 122.77 ? 1326 SO4 A S 1 HETATM 3909 O O1 . SO4 L 6 . ? 34.523 -22.904 -15.745 1.00 117.12 ? 1326 SO4 A O1 1 HETATM 3910 O O2 . SO4 L 6 . ? 33.581 -24.527 -17.274 1.00 120.48 ? 1326 SO4 A O2 1 HETATM 3911 O O3 . SO4 L 6 . ? 33.820 -22.223 -17.967 1.00 119.14 ? 1326 SO4 A O3 1 HETATM 3912 O O4 . SO4 L 6 . ? 32.177 -22.815 -16.303 1.00 124.80 ? 1326 SO4 A O4 1 HETATM 3913 S S . SO4 M 6 . ? 24.387 -32.269 -11.758 1.00 110.27 ? 1327 SO4 A S 1 HETATM 3914 O O1 . SO4 M 6 . ? 25.519 -31.431 -11.301 1.00 108.43 ? 1327 SO4 A O1 1 HETATM 3915 O O2 . SO4 M 6 . ? 24.881 -33.611 -12.146 1.00 106.80 ? 1327 SO4 A O2 1 HETATM 3916 O O3 . SO4 M 6 . ? 23.740 -31.630 -12.925 1.00 111.04 ? 1327 SO4 A O3 1 HETATM 3917 O O4 . SO4 M 6 . ? 23.395 -32.390 -10.665 1.00 109.35 ? 1327 SO4 A O4 1 HETATM 3918 S S . SO4 N 6 . ? 37.090 -31.737 18.430 1.00 92.22 ? 1328 SO4 A S 1 HETATM 3919 O O1 . SO4 N 6 . ? 37.921 -31.834 19.652 1.00 91.77 ? 1328 SO4 A O1 1 HETATM 3920 O O2 . SO4 N 6 . ? 37.131 -33.027 17.701 1.00 83.84 ? 1328 SO4 A O2 1 HETATM 3921 O O3 . SO4 N 6 . ? 37.639 -30.676 17.558 1.00 97.19 ? 1328 SO4 A O3 1 HETATM 3922 O O4 . SO4 N 6 . ? 35.700 -31.373 18.801 1.00 86.57 ? 1328 SO4 A O4 1 HETATM 3923 S S . SO4 O 6 . ? 43.525 -60.500 12.560 1.00 91.74 ? 1329 SO4 A S 1 HETATM 3924 O O1 . SO4 O 6 . ? 43.285 -61.631 13.492 1.00 88.76 ? 1329 SO4 A O1 1 HETATM 3925 O O2 . SO4 O 6 . ? 42.999 -60.835 11.219 1.00 91.86 ? 1329 SO4 A O2 1 HETATM 3926 O O3 . SO4 O 6 . ? 44.975 -60.264 12.433 1.00 85.73 ? 1329 SO4 A O3 1 HETATM 3927 O O4 . SO4 O 6 . ? 42.863 -59.274 13.070 1.00 86.42 ? 1329 SO4 A O4 1 HETATM 3928 S S . SO4 P 6 . ? 34.191 -57.693 22.640 1.00 112.09 ? 1330 SO4 A S 1 HETATM 3929 O O1 . SO4 P 6 . ? 35.567 -58.133 22.969 1.00 107.27 ? 1330 SO4 A O1 1 HETATM 3930 O O2 . SO4 P 6 . ? 34.136 -57.227 21.235 1.00 113.69 ? 1330 SO4 A O2 1 HETATM 3931 O O3 . SO4 P 6 . ? 33.770 -56.594 23.541 1.00 108.06 ? 1330 SO4 A O3 1 HETATM 3932 O O4 . SO4 P 6 . ? 33.278 -58.844 22.814 1.00 114.97 ? 1330 SO4 A O4 1 HETATM 3933 S S . SO4 Q 6 . ? 50.025 -33.007 18.002 1.00 85.05 ? 1331 SO4 A S 1 HETATM 3934 O O1 . SO4 Q 6 . ? 50.862 -33.823 18.916 1.00 86.57 ? 1331 SO4 A O1 1 HETATM 3935 O O2 . SO4 Q 6 . ? 50.723 -32.837 16.707 1.00 82.83 ? 1331 SO4 A O2 1 HETATM 3936 O O3 . SO4 Q 6 . ? 49.802 -31.680 18.620 1.00 83.92 ? 1331 SO4 A O3 1 HETATM 3937 O O4 . SO4 Q 6 . ? 48.724 -33.678 17.770 1.00 80.19 ? 1331 SO4 A O4 1 HETATM 3938 S S . SO4 R 6 . ? 52.860 -16.160 -31.879 1.00 115.60 ? 1332 SO4 A S 1 HETATM 3939 O O1 . SO4 R 6 . ? 53.113 -17.072 -30.740 1.00 116.21 ? 1332 SO4 A O1 1 HETATM 3940 O O2 . SO4 R 6 . ? 53.647 -16.596 -33.055 1.00 115.20 ? 1332 SO4 A O2 1 HETATM 3941 O O3 . SO4 R 6 . ? 53.264 -14.787 -31.501 1.00 119.19 ? 1332 SO4 A O3 1 HETATM 3942 O O4 . SO4 R 6 . ? 51.419 -16.180 -32.220 1.00 115.24 ? 1332 SO4 A O4 1 HETATM 3943 S S . SO4 S 6 . ? 44.516 -19.948 -18.470 1.00 86.00 ? 1333 SO4 A S 1 HETATM 3944 O O1 . SO4 S 6 . ? 45.968 -19.764 -18.713 1.00 80.95 ? 1333 SO4 A O1 1 HETATM 3945 O O2 . SO4 S 6 . ? 43.999 -21.019 -19.366 1.00 77.75 ? 1333 SO4 A O2 1 HETATM 3946 O O3 . SO4 S 6 . ? 43.800 -18.679 -18.754 1.00 81.86 ? 1333 SO4 A O3 1 HETATM 3947 O O4 . SO4 S 6 . ? 44.307 -20.314 -17.045 1.00 75.32 ? 1333 SO4 A O4 1 HETATM 3948 C C1 . NAG T 3 . ? 48.851 -24.473 2.751 1.00 54.41 ? 1171 NAG B C1 1 HETATM 3949 C C2 . NAG T 3 . ? 48.709 -23.471 3.899 1.00 60.02 ? 1171 NAG B C2 1 HETATM 3950 C C3 . NAG T 3 . ? 47.265 -23.251 4.324 1.00 64.19 ? 1171 NAG B C3 1 HETATM 3951 C C4 . NAG T 3 . ? 46.349 -23.040 3.124 1.00 67.33 ? 1171 NAG B C4 1 HETATM 3952 C C5 . NAG T 3 . ? 46.580 -24.131 2.079 1.00 66.62 ? 1171 NAG B C5 1 HETATM 3953 C C6 . NAG T 3 . ? 45.753 -23.887 0.820 1.00 67.81 ? 1171 NAG B C6 1 HETATM 3954 C C7 . NAG T 3 . ? 50.283 -23.196 5.756 1.00 59.26 ? 1171 NAG B C7 1 HETATM 3955 C C8 . NAG T 3 . ? 50.995 -23.891 6.871 1.00 58.71 ? 1171 NAG B C8 1 HETATM 3956 N N2 . NAG T 3 . ? 49.471 -23.960 5.029 1.00 60.19 ? 1171 NAG B N2 1 HETATM 3957 O O3 . NAG T 3 . ? 47.216 -22.118 5.161 1.00 66.79 ? 1171 NAG B O3 1 HETATM 3958 O O4 . NAG T 3 . ? 45.009 -23.081 3.574 1.00 72.97 ? 1171 NAG B O4 1 HETATM 3959 O O5 . NAG T 3 . ? 47.944 -24.160 1.709 1.00 58.39 ? 1171 NAG B O5 1 HETATM 3960 O O6 . NAG T 3 . ? 46.031 -24.886 -0.140 1.00 70.26 ? 1171 NAG B O6 1 HETATM 3961 O O7 . NAG T 3 . ? 50.474 -21.995 5.557 1.00 60.67 ? 1171 NAG B O7 1 HETATM 3962 C C1 . NAG U 3 . ? 44.235 -21.945 3.130 1.00 75.42 ? 1172 NAG B C1 1 HETATM 3963 C C2 . NAG U 3 . ? 42.748 -22.293 3.244 1.00 73.16 ? 1172 NAG B C2 1 HETATM 3964 C C3 . NAG U 3 . ? 41.833 -21.093 2.973 1.00 77.51 ? 1172 NAG B C3 1 HETATM 3965 C C4 . NAG U 3 . ? 42.346 -19.788 3.582 1.00 80.03 ? 1172 NAG B C4 1 HETATM 3966 C C5 . NAG U 3 . ? 43.860 -19.630 3.404 1.00 80.00 ? 1172 NAG B C5 1 HETATM 3967 C C6 . NAG U 3 . ? 44.393 -18.412 4.150 1.00 80.99 ? 1172 NAG B C6 1 HETATM 3968 C C7 . NAG U 3 . ? 42.433 -24.672 2.696 1.00 67.61 ? 1172 NAG B C7 1 HETATM 3969 C C8 . NAG U 3 . ? 42.076 -25.690 1.650 1.00 66.27 ? 1172 NAG B C8 1 HETATM 3970 N N2 . NAG U 3 . ? 42.419 -23.382 2.332 1.00 68.64 ? 1172 NAG B N2 1 HETATM 3971 O O3 . NAG U 3 . ? 40.542 -21.355 3.482 1.00 76.70 ? 1172 NAG B O3 1 HETATM 3972 O O4 . NAG U 3 . ? 41.661 -18.708 2.975 1.00 80.10 ? 1172 NAG B O4 1 HETATM 3973 O O5 . NAG U 3 . ? 44.535 -20.782 3.877 1.00 78.09 ? 1172 NAG B O5 1 HETATM 3974 O O6 . NAG U 3 . ? 44.270 -18.617 5.540 1.00 83.28 ? 1172 NAG B O6 1 HETATM 3975 O O7 . NAG U 3 . ? 42.722 -25.054 3.829 1.00 65.00 ? 1172 NAG B O7 1 HETATM 3976 S S . SO4 V 6 . ? 33.769 -23.005 -51.232 1.00 108.58 ? 1173 SO4 B S 1 HETATM 3977 O O1 . SO4 V 6 . ? 34.648 -22.814 -52.407 1.00 108.26 ? 1173 SO4 B O1 1 HETATM 3978 O O2 . SO4 V 6 . ? 33.455 -24.449 -51.117 1.00 103.40 ? 1173 SO4 B O2 1 HETATM 3979 O O3 . SO4 V 6 . ? 32.510 -22.247 -51.410 1.00 109.01 ? 1173 SO4 B O3 1 HETATM 3980 O O4 . SO4 V 6 . ? 34.456 -22.506 -50.015 1.00 105.67 ? 1173 SO4 B O4 1 HETATM 3981 S S . SO4 W 6 . ? 42.508 -25.115 13.649 1.00 97.44 ? 1174 SO4 B S 1 HETATM 3982 O O1 . SO4 W 6 . ? 42.345 -26.418 14.336 1.00 97.70 ? 1174 SO4 B O1 1 HETATM 3983 O O2 . SO4 W 6 . ? 42.244 -25.267 12.197 1.00 94.94 ? 1174 SO4 B O2 1 HETATM 3984 O O3 . SO4 W 6 . ? 43.892 -24.621 13.841 1.00 97.39 ? 1174 SO4 B O3 1 HETATM 3985 O O4 . SO4 W 6 . ? 41.552 -24.146 14.232 1.00 99.46 ? 1174 SO4 B O4 1 HETATM 3986 S S . SO4 X 6 . ? 53.977 -23.248 -17.306 1.00 128.62 ? 1175 SO4 B S 1 HETATM 3987 O O1 . SO4 X 6 . ? 53.323 -24.146 -16.330 1.00 124.71 ? 1175 SO4 B O1 1 HETATM 3988 O O2 . SO4 X 6 . ? 53.449 -23.511 -18.665 1.00 126.37 ? 1175 SO4 B O2 1 HETATM 3989 O O3 . SO4 X 6 . ? 55.437 -23.493 -17.287 1.00 130.21 ? 1175 SO4 B O3 1 HETATM 3990 O O4 . SO4 X 6 . ? 53.710 -21.841 -16.926 1.00 130.13 ? 1175 SO4 B O4 1 HETATM 3991 S S . SO4 Y 6 . ? 59.600 -32.930 -62.452 0.33 101.26 ? 1176 SO4 B S 1 HETATM 3992 O O1 . SO4 Y 6 . ? 60.886 -33.649 -62.303 1.00 122.17 ? 1176 SO4 B O1 1 HETATM 3993 O O2 . SO4 Y 6 . ? 58.984 -33.276 -63.752 0.33 106.00 ? 1176 SO4 B O2 1 HETATM 3994 O O3 . SO4 Y 6 . ? 59.851 -31.472 -62.397 1.00 109.29 ? 1176 SO4 B O3 1 HETATM 3995 O O4 . SO4 Y 6 . ? 58.683 -33.322 -61.358 0.33 98.50 ? 1176 SO4 B O4 1 HETATM 3996 O O . HOH Z 7 . ? 41.113 -25.370 -43.729 1.00 44.77 ? 2001 HOH A O 1 HETATM 3997 O O . HOH Z 7 . ? 45.036 -23.683 -47.833 1.00 56.97 ? 2002 HOH A O 1 HETATM 3998 O O . HOH Z 7 . ? 35.347 -30.188 -21.045 1.00 53.02 ? 2003 HOH A O 1 HETATM 3999 O O . HOH Z 7 . ? 45.891 -25.040 -27.259 1.00 38.21 ? 2004 HOH A O 1 HETATM 4000 O O . HOH Z 7 . ? 52.097 -22.813 -26.583 1.00 52.65 ? 2005 HOH A O 1 HETATM 4001 O O . HOH Z 7 . ? 35.671 -29.864 -25.708 1.00 50.58 ? 2006 HOH A O 1 HETATM 4002 O O . HOH Z 7 . ? 36.295 -28.859 -18.993 1.00 49.04 ? 2007 HOH A O 1 HETATM 4003 O O . HOH Z 7 . ? 47.667 -32.043 13.562 1.00 48.71 ? 2008 HOH A O 1 HETATM 4004 O O . HOH Z 7 . ? 33.776 -31.092 -19.066 1.00 49.08 ? 2009 HOH A O 1 HETATM 4005 O O . HOH Z 7 . ? 32.800 -33.870 -12.624 1.00 42.93 ? 2010 HOH A O 1 HETATM 4006 O O . HOH Z 7 . ? 31.074 -27.211 -12.348 1.00 49.29 ? 2011 HOH A O 1 HETATM 4007 O O . HOH Z 7 . ? 22.961 -30.690 -6.421 1.00 65.92 ? 2012 HOH A O 1 HETATM 4008 O O . HOH Z 7 . ? 36.506 -53.001 5.524 1.00 48.19 ? 2013 HOH A O 1 HETATM 4009 O O . HOH Z 7 . ? 24.916 -39.136 4.277 0.50 15.37 ? 2014 HOH A O 1 HETATM 4010 O O . HOH Z 7 . ? 25.751 -35.327 6.403 1.00 48.00 ? 2015 HOH A O 1 HETATM 4011 O O . HOH Z 7 . ? 26.138 -37.736 13.160 1.00 43.61 ? 2016 HOH A O 1 HETATM 4012 O O . HOH Z 7 . ? 32.687 -36.086 11.060 1.00 37.67 ? 2017 HOH A O 1 HETATM 4013 O O . HOH Z 7 . ? 36.721 -36.290 11.932 1.00 44.36 ? 2018 HOH A O 1 HETATM 4014 O O . HOH Z 7 . ? 38.652 -36.272 13.799 1.00 40.72 ? 2019 HOH A O 1 HETATM 4015 O O . HOH Z 7 . ? 28.382 -48.919 16.645 1.00 55.91 ? 2020 HOH A O 1 HETATM 4016 O O . HOH Z 7 . ? 24.395 -48.002 20.269 1.00 61.89 ? 2021 HOH A O 1 HETATM 4017 O O . HOH Z 7 . ? 29.819 -49.526 13.750 1.00 74.67 ? 2022 HOH A O 1 HETATM 4018 O O . HOH Z 7 . ? 35.393 -55.895 6.574 1.00 47.92 ? 2023 HOH A O 1 HETATM 4019 O O . HOH Z 7 . ? 35.336 -34.016 11.244 1.00 38.38 ? 2024 HOH A O 1 HETATM 4020 O O . HOH Z 7 . ? 31.457 -30.577 6.289 1.00 28.83 ? 2025 HOH A O 1 HETATM 4021 O O . HOH Z 7 . ? 35.931 -29.236 12.493 1.00 52.25 ? 2026 HOH A O 1 HETATM 4022 O O . HOH Z 7 . ? 38.803 -30.058 23.730 1.00 57.66 ? 2027 HOH A O 1 HETATM 4023 O O . HOH Z 7 . ? 43.257 -34.284 18.968 1.00 48.83 ? 2028 HOH A O 1 HETATM 4024 O O . HOH Z 7 . ? 52.514 -34.839 16.649 1.00 60.56 ? 2029 HOH A O 1 HETATM 4025 O O . HOH Z 7 . ? 48.934 -34.048 14.681 1.00 47.57 ? 2030 HOH A O 1 HETATM 4026 O O . HOH Z 7 . ? 50.371 -36.336 13.736 1.00 52.17 ? 2031 HOH A O 1 HETATM 4027 O O . HOH Z 7 . ? 45.561 -31.846 11.976 1.00 46.58 ? 2032 HOH A O 1 HETATM 4028 O O . HOH Z 7 . ? 46.003 -35.705 6.605 1.00 38.80 ? 2033 HOH A O 1 HETATM 4029 O O . HOH Z 7 . ? 39.998 -32.669 11.720 1.00 58.31 ? 2034 HOH A O 1 HETATM 4030 O O . HOH Z 7 . ? 48.448 -43.933 6.744 1.00 53.33 ? 2035 HOH A O 1 HETATM 4031 O O . HOH Z 7 . ? 44.808 -42.076 4.894 1.00 37.42 ? 2036 HOH A O 1 HETATM 4032 O O . HOH Z 7 . ? 44.628 -39.372 4.894 1.00 42.02 ? 2037 HOH A O 1 HETATM 4033 O O . HOH Z 7 . ? 47.352 -42.815 4.041 1.00 50.49 ? 2038 HOH A O 1 HETATM 4034 O O . HOH Z 7 . ? 26.571 -39.003 -13.034 1.00 62.64 ? 2039 HOH A O 1 HETATM 4035 O O . HOH Z 7 . ? 28.461 -28.463 34.281 1.00 75.44 ? 2040 HOH A O 1 HETATM 4036 O O . HOH Z 7 . ? 24.106 -43.096 31.360 1.00 66.15 ? 2041 HOH A O 1 HETATM 4037 O O . HOH Z 7 . ? 31.959 -53.263 34.378 1.00 56.94 ? 2042 HOH A O 1 HETATM 4038 O O . HOH Z 7 . ? 38.596 -39.772 44.222 1.00 55.52 ? 2043 HOH A O 1 HETATM 4039 O O . HOH Z 7 . ? 38.374 -30.425 38.154 1.00 49.15 ? 2044 HOH A O 1 HETATM 4040 O O . HOH Z 7 . ? 42.811 -25.617 45.026 1.00 67.48 ? 2045 HOH A O 1 HETATM 4041 O O . HOH Z 7 . ? 59.647 -53.039 24.837 1.00 45.10 ? 2046 HOH A O 1 HETATM 4042 O O . HOH Z 7 . ? 62.297 -50.940 24.313 1.00 62.67 ? 2047 HOH A O 1 HETATM 4043 O O . HOH Z 7 . ? 52.904 -44.163 18.713 1.00 55.27 ? 2048 HOH A O 1 HETATM 4044 O O . HOH Z 7 . ? 52.880 -46.671 17.040 1.00 50.35 ? 2049 HOH A O 1 HETATM 4045 O O . HOH Z 7 . ? 32.821 -58.250 12.690 1.00 63.18 ? 2050 HOH A O 1 HETATM 4046 O O . HOH Z 7 . ? 41.371 -56.257 2.552 1.00 56.89 ? 2051 HOH A O 1 HETATM 4047 O O . HOH Z 7 . ? 42.732 -42.160 3.020 1.00 35.57 ? 2052 HOH A O 1 HETATM 4048 O O . HOH Z 7 . ? 42.483 -39.789 1.879 1.00 39.68 ? 2053 HOH A O 1 HETATM 4049 O O . HOH Z 7 . ? 38.880 -33.830 1.489 1.00 41.56 ? 2054 HOH A O 1 HETATM 4050 O O . HOH Z 7 . ? 40.517 -31.935 2.975 1.00 38.55 ? 2055 HOH A O 1 HETATM 4051 O O . HOH Z 7 . ? 30.429 -27.611 -4.003 1.00 45.53 ? 2056 HOH A O 1 HETATM 4052 O O . HOH Z 7 . ? 35.908 -40.459 -13.421 1.00 55.30 ? 2057 HOH A O 1 HETATM 4053 O O . HOH Z 7 . ? 35.747 -37.219 -19.925 1.00 57.07 ? 2058 HOH A O 1 HETATM 4054 O O . HOH Z 7 . ? 42.186 -24.077 -9.665 1.00 41.54 ? 2059 HOH A O 1 HETATM 4055 O O . HOH Z 7 . ? 38.311 -23.439 -13.477 1.00 50.06 ? 2060 HOH A O 1 HETATM 4056 O O . HOH Z 7 . ? 41.565 -27.737 -1.022 1.00 41.08 ? 2061 HOH A O 1 HETATM 4057 O O . HOH Z 7 . ? 47.847 -31.946 -6.677 1.00 33.72 ? 2062 HOH A O 1 HETATM 4058 O O . HOH Z 7 . ? 45.679 -23.763 -5.848 1.00 51.34 ? 2063 HOH A O 1 HETATM 4059 O O . HOH Z 7 . ? 40.217 -32.935 -1.035 1.00 36.58 ? 2064 HOH A O 1 HETATM 4060 O O . HOH Z 7 . ? 45.200 -33.691 -1.054 1.00 40.87 ? 2065 HOH A O 1 HETATM 4061 O O . HOH Z 7 . ? 43.944 -27.436 3.846 1.00 51.49 ? 2066 HOH A O 1 HETATM 4062 O O . HOH Z 7 . ? 45.007 -37.014 -6.853 1.00 57.16 ? 2067 HOH A O 1 HETATM 4063 O O . HOH Z 7 . ? 45.264 -39.557 -8.534 1.00 38.05 ? 2068 HOH A O 1 HETATM 4064 O O . HOH Z 7 . ? 41.618 -49.199 -5.287 1.00 65.92 ? 2069 HOH A O 1 HETATM 4065 O O . HOH Z 7 . ? 43.851 -50.011 -7.393 1.00 74.78 ? 2070 HOH A O 1 HETATM 4066 O O . HOH Z 7 . ? 46.932 -37.758 -10.206 1.00 42.95 ? 2071 HOH A O 1 HETATM 4067 O O . HOH Z 7 . ? 48.236 -38.446 -19.659 1.00 56.63 ? 2072 HOH A O 1 HETATM 4068 O O . HOH Z 7 . ? 47.962 -33.236 -9.172 1.00 37.95 ? 2073 HOH A O 1 HETATM 4069 O O . HOH Z 7 . ? 49.578 -31.219 -10.017 1.00 31.55 ? 2074 HOH A O 1 HETATM 4070 O O . HOH Z 7 . ? 44.220 -23.777 -25.425 1.00 45.53 ? 2075 HOH A O 1 HETATM 4071 O O . HOH Z 7 . ? 46.692 -32.058 -31.684 1.00 41.75 ? 2076 HOH A O 1 HETATM 4072 O O . HOH Z 7 . ? 46.977 -28.066 -41.461 1.00 46.57 ? 2077 HOH A O 1 HETATM 4073 O O . HOH Z 7 . ? 33.109 -36.826 -30.082 1.00 73.31 ? 2078 HOH A O 1 HETATM 4074 O O . HOH Z 7 . ? 26.387 -14.272 -31.290 1.00 75.49 ? 2079 HOH A O 1 HETATM 4075 O O . HOH Z 7 . ? 25.337 -36.525 -12.786 1.00 70.35 ? 2080 HOH A O 1 HETATM 4076 O O . HOH Z 7 . ? 41.350 -17.634 -17.376 1.00 64.93 ? 2081 HOH A O 1 HETATM 4077 O O . HOH AA 7 . ? 51.591 -25.783 -45.019 1.00 53.29 ? 2001 HOH B O 1 HETATM 4078 O O . HOH AA 7 . ? 53.872 -22.830 -42.529 1.00 54.97 ? 2002 HOH B O 1 HETATM 4079 O O . HOH AA 7 . ? 33.865 -34.245 -43.276 1.00 64.77 ? 2003 HOH B O 1 HETATM 4080 O O . HOH AA 7 . ? 51.376 -39.922 -23.467 1.00 57.97 ? 2004 HOH B O 1 HETATM 4081 O O . HOH AA 7 . ? 43.984 -46.126 -14.941 1.00 71.59 ? 2005 HOH B O 1 HETATM 4082 O O . HOH AA 7 . ? 48.890 -38.974 -11.728 1.00 52.41 ? 2006 HOH B O 1 HETATM 4083 O O . HOH AA 7 . ? 46.960 -46.863 -6.737 1.00 42.23 ? 2007 HOH B O 1 HETATM 4084 O O . HOH AA 7 . ? 49.095 -40.286 -0.742 1.00 41.33 ? 2008 HOH B O 1 HETATM 4085 O O . HOH AA 7 . ? 46.987 -35.708 -1.954 1.00 46.73 ? 2009 HOH B O 1 HETATM 4086 O O . HOH AA 7 . ? 46.382 -33.302 1.192 1.00 30.87 ? 2010 HOH B O 1 HETATM 4087 O O . HOH AA 7 . ? 49.695 -28.496 4.303 1.00 31.67 ? 2011 HOH B O 1 HETATM 4088 O O . HOH AA 7 . ? 46.175 -28.831 7.411 1.00 34.35 ? 2012 HOH B O 1 HETATM 4089 O O . HOH AA 7 . ? 49.686 -26.082 8.400 1.00 49.81 ? 2013 HOH B O 1 HETATM 4090 O O . HOH AA 7 . ? 51.785 -25.319 14.173 1.00 48.59 ? 2014 HOH B O 1 HETATM 4091 O O . HOH AA 7 . ? 55.873 -23.348 1.846 1.00 41.21 ? 2015 HOH B O 1 HETATM 4092 O O . HOH AA 7 . ? 58.171 -33.585 0.064 0.33 30.81 ? 2016 HOH B O 1 HETATM 4093 O O . HOH AA 7 . ? 47.735 -32.800 -2.354 1.00 50.23 ? 2017 HOH B O 1 HETATM 4094 O O . HOH AA 7 . ? 49.410 -25.906 -1.851 1.00 57.21 ? 2018 HOH B O 1 HETATM 4095 O O . HOH AA 7 . ? 49.463 -26.317 -6.099 1.00 38.40 ? 2019 HOH B O 1 HETATM 4096 O O . HOH AA 7 . ? 51.404 -22.818 -0.847 1.00 54.21 ? 2020 HOH B O 1 HETATM 4097 O O . HOH AA 7 . ? 52.534 -36.311 -9.648 1.00 30.29 ? 2021 HOH B O 1 HETATM 4098 O O . HOH AA 7 . ? 54.646 -33.106 -21.672 1.00 34.85 ? 2022 HOH B O 1 HETATM 4099 O O . HOH AA 7 . ? 55.807 -31.474 -33.143 1.00 53.33 ? 2023 HOH B O 1 HETATM 4100 O O . HOH AA 7 . ? 55.771 -31.611 -36.173 1.00 58.96 ? 2024 HOH B O 1 HETATM 4101 O O . HOH AA 7 . ? 54.204 -35.784 -48.184 1.00 59.00 ? 2025 HOH B O 1 HETATM 4102 O O . HOH AA 7 . ? 45.708 -53.345 -71.182 1.00 69.20 ? 2026 HOH B O 1 HETATM 4103 O O . HOH AA 7 . ? 43.197 -22.620 -0.766 1.00 55.03 ? 2027 HOH B O 1 HETATM 4104 O O . HOH AA 7 . ? 36.756 -21.260 1.784 1.00 60.46 ? 2028 HOH B O 1 HETATM 4105 O O . HOH AA 7 . ? 20.805 -48.006 28.986 1.00 65.76 ? 2029 HOH B O 1 HETATM 4106 O O . HOH AA 7 . ? 29.514 -50.725 -65.389 1.00 66.14 ? 2030 HOH B O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . ASP A 1 ? 1.6651 1.7341 0.5948 0.0051 -0.2349 0.2193 1 ASP A N 2 C CA . ASP A 1 ? 1.6680 1.6958 0.5824 0.0119 -0.2024 0.2154 1 ASP A CA 3 C C . ASP A 1 ? 1.6240 1.6349 0.5832 0.0127 -0.1804 0.1985 1 ASP A C 4 O O . ASP A 1 ? 1.6327 1.6130 0.5770 0.0118 -0.1556 0.1867 1 ASP A O 5 C CB . ASP A 1 ? 1.6772 1.7011 0.5860 0.0313 -0.1938 0.2451 1 ASP A CB 6 C CG . ASP A 1 ? 1.7128 1.7005 0.5738 0.0322 -0.1704 0.2446 1 ASP A CG 7 O OD1 . ASP A 1 ? 1.6986 1.6605 0.5560 0.0251 -0.1491 0.2237 1 ASP A OD1 8 O OD2 . ASP A 1 ? 1.7523 1.7387 0.5790 0.0405 -0.1732 0.2661 1 ASP A OD2 9 N N . LYS A 2 ? 1.5800 1.6121 0.5930 0.0145 -0.1889 0.1975 2 LYS A N 10 C CA . LYS A 2 ? 1.5356 1.5534 0.5920 0.0166 -0.1684 0.1840 2 LYS A CA 11 C C . LYS A 2 ? 1.4863 1.5247 0.5890 0.0104 -0.1811 0.1722 2 LYS A C 12 O O . LYS A 2 ? 1.4843 1.5535 0.5954 0.0061 -0.2065 0.1779 2 LYS A O 13 C CB . LYS A 2 ? 1.5250 1.5336 0.6072 0.0341 -0.1495 0.2033 2 LYS A CB 14 C CG . LYS A 2 ? 1.5089 1.5440 0.6305 0.0468 -0.1631 0.2248 2 LYS A CG 15 C CD . LYS A 2 ? 1.5118 1.5302 0.6456 0.0636 -0.1434 0.2453 2 LYS A CD 16 C CE . LYS A 2 ? 1.4903 1.5310 0.6670 0.0777 -0.1534 0.2641 2 LYS A CE 17 N NZ . LYS A 2 ? 1.5055 1.5270 0.6822 0.0950 -0.1368 0.2878 2 LYS A NZ 18 N N . ILE A 3 ? 1.4480 1.4706 0.5807 0.0098 -0.1626 0.1565 3 ILE A N 19 C CA . ILE A 3 ? 1.3983 1.4357 0.5788 0.0058 -0.1695 0.1458 3 ILE A CA 20 C C . ILE A 3 ? 1.3565 1.3820 0.5798 0.0156 -0.1465 0.1450 3 ILE A C 21 O O . ILE A 3 ? 1.3524 1.3532 0.5664 0.0154 -0.1241 0.1343 3 ILE A O 22 C CB . ILE A 3 ? 1.4011 1.4308 0.5648 -0.0119 -0.1755 0.1189 3 ILE A CB 23 C CG1 . ILE A 3 ? 1.3534 1.4010 0.5644 -0.0168 -0.1856 0.1106 3 ILE A CG1 24 C CG2 . ILE A 3 ? 1.4070 1.4019 0.5494 -0.0136 -0.1500 0.1007 3 ILE A CG2 25 C CD1 . ILE A 3 ? 1.3637 1.4027 0.5567 -0.0351 -0.1934 0.0859 3 ILE A CD1 26 N N . CYS A 4 ? 1.3267 1.3709 0.5960 0.0238 -0.1520 0.1567 4 CYS A N 27 C CA . CYS A 4 ? 1.2912 1.3251 0.6000 0.0326 -0.1318 0.1585 4 CYS A CA 28 C C . CYS A 4 ? 1.2431 1.2844 0.5929 0.0268 -0.1333 0.1419 4 CYS A C 29 O O . CYS A 4 ? 1.2375 1.3001 0.5995 0.0205 -0.1534 0.1381 4 CYS A O 30 C CB . CYS A 4 ? 1.2920 1.3350 0.6209 0.0481 -0.1326 0.1845 4 CYS A CB 31 S SG . CYS A 4 ? 1.3558 1.3816 0.6434 0.0592 -0.1227 0.2079 4 CYS A SG 32 N N . LEU A 5 ? 1.2100 1.2348 0.5806 0.0285 -0.1118 0.1328 5 LEU A N 33 C CA . LEU A 5 ? 1.1623 1.1919 0.5737 0.0251 -0.1100 0.1190 5 LEU A CA 34 C C . LEU A 5 ? 1.1239 1.1595 0.5779 0.0354 -0.1037 0.1324 5 LEU A C 35 O O . LEU A 5 ? 1.1324 1.1553 0.5840 0.0432 -0.0886 0.1449 5 LEU A O 36 C CB . LEU A 5 ? 1.1519 1.1617 0.5584 0.0205 -0.0904 0.0995 5 LEU A CB 37 C CG . LEU A 5 ? 1.1743 1.1748 0.5488 0.0101 -0.0944 0.0798 5 LEU A CG 38 C CD1 . LEU A 5 ? 1.1565 1.1693 0.5486 0.0017 -0.1122 0.0688 5 LEU A CD1 39 C CD2 . LEU A 5 ? 1.2228 1.2177 0.5460 0.0071 -0.1014 0.0847 5 LEU A CD2 40 N N . GLY A 6 ? 1.0854 1.1378 0.5760 0.0345 -0.1142 0.1293 6 GLY A N 41 C CA . GLY A 6 ? 1.0487 1.1052 0.5794 0.0438 -0.1078 0.1400 6 GLY A CA 42 C C . GLY A 6 ? 1.0031 1.0697 0.5719 0.0390 -0.1115 0.1270 6 GLY A C 43 O O . GLY A 6 ? 0.9981 1.0665 0.5622 0.0286 -0.1178 0.1096 6 GLY A O 44 N N . HIS A 7 ? 0.9725 1.0429 0.5766 0.0470 -0.1065 0.1359 7 HIS A N 45 C CA . HIS A 7 ? 0.9273 1.0067 0.5696 0.0439 -0.1083 0.1260 7 HIS A CA 46 C C . HIS A 7 ? 0.9141 1.0107 0.5849 0.0543 -0.1161 0.1430 7 HIS A C 47 O O . HIS A 7 ? 0.9360 1.0318 0.5980 0.0654 -0.1152 0.1621 7 HIS A O 48 C CB . HIS A 7 ? 0.9022 0.9630 0.5595 0.0427 -0.0869 0.1160 7 HIS A CB 49 C CG . HIS A 7 ? 0.9052 0.9506 0.5635 0.0509 -0.0702 0.1299 7 HIS A CG 50 N ND1 . HIS A 7 ? 0.8886 0.9342 0.5746 0.0588 -0.0663 0.1410 7 HIS A ND1 51 C CD2 . HIS A 7 ? 0.9283 0.9554 0.5609 0.0516 -0.0555 0.1347 7 HIS A CD2 52 C CE1 . HIS A 7 ? 0.9040 0.9293 0.5797 0.0634 -0.0498 0.1513 7 HIS A CE1 53 N NE2 . HIS A 7 ? 0.9290 0.9440 0.5732 0.0587 -0.0432 0.1480 7 HIS A NE2 54 N N . HIS A 8 ? 0.8819 0.9932 0.5859 0.0516 -0.1228 0.1366 8 HIS A N 55 C CA . HIS A 8 ? 0.8753 1.0063 0.6083 0.0620 -0.1302 0.1522 8 HIS A CA 56 C C . HIS A 8 ? 0.8722 0.9849 0.6238 0.0731 -0.1111 0.1611 8 HIS A C 57 O O . HIS A 8 ? 0.8625 0.9511 0.6106 0.0694 -0.0934 0.1523 8 HIS A O 58 C CB . HIS A 8 ? 0.8470 1.0022 0.6072 0.0540 -0.1447 0.1427 8 HIS A CB 59 C CG . HIS A 8 ? 0.8079 0.9514 0.5927 0.0485 -0.1334 0.1270 8 HIS A CG 60 N ND1 . HIS A 8 ? 0.7803 0.9414 0.5953 0.0442 -0.1416 0.1215 8 HIS A ND1 61 C CD2 . HIS A 8 ? 0.7986 0.9170 0.5823 0.0463 -0.1150 0.1163 8 HIS A CD2 62 C CE1 . HIS A 8 ? 0.7547 0.9000 0.5847 0.0405 -0.1288 0.1082 8 HIS A CE1 63 N NE2 . HIS A 8 ? 0.7635 0.8844 0.5757 0.0417 -0.1130 0.1050 8 HIS A NE2 64 N N . ALA A 9 ? 0.8816 1.0064 0.6516 0.0867 -0.1144 0.1790 9 ALA A N 65 C CA . ALA A 9 ? 0.8879 0.9918 0.6713 0.0982 -0.0961 0.1891 9 ALA A CA 66 C C . ALA A 9 ? 0.8981 1.0217 0.7086 0.1129 -0.1025 0.2054 9 ALA A C 67 O O . ALA A 9 ? 0.9051 1.0618 0.7211 0.1157 -0.1216 0.2129 9 ALA A O 68 C CB . ALA A 9 ? 0.9205 0.9977 0.6722 0.1046 -0.0829 0.2009 9 ALA A CB 69 N N . LEU A 10 ? 0.9059 1.0098 0.7326 0.1216 -0.0858 0.2106 10 LEU A N 70 C CA . LEU A 10 ? 0.9152 1.0323 0.7665 0.1385 -0.0871 0.2271 10 LEU A CA 71 C C . LEU A 10 ? 0.9569 1.0407 0.7942 0.1543 -0.0681 0.2442 10 LEU A C 72 O O . LEU A 10 ? 0.9631 1.0126 0.7782 0.1481 -0.0523 0.2394 10 LEU A O 73 C CB . LEU A 10 ? 0.8799 1.0019 0.7660 0.1335 -0.0836 0.2149 10 LEU A CB 74 C CG . LEU A 10 ? 0.8513 0.9969 0.7507 0.1159 -0.0979 0.1951 10 LEU A CG 75 C CD1 . LEU A 10 ? 0.8184 0.9583 0.7467 0.1108 -0.0892 0.1827 10 LEU A CD1 76 C CD2 . LEU A 10 ? 0.8538 1.0424 0.7619 0.1174 -0.1212 0.2028 10 LEU A CD2 77 N N . SER A 11 ? 1.0048 1.0986 0.8540 0.1748 -0.0691 0.2647 11 SER A N 78 C CA . SER A 11 ? 1.0642 1.1217 0.9016 0.1920 -0.0489 0.2815 11 SER A CA 79 C C . SER A 11 ? 1.0865 1.1082 0.9324 0.1838 -0.0276 0.2681 11 SER A C 80 O O . SER A 11 ? 1.1203 1.1001 0.9431 0.1820 -0.0084 0.2692 11 SER A O 81 C CB . SER A 11 ? 1.0741 1.1530 0.9290 0.2173 -0.0537 0.3048 11 SER A CB 82 O OG . SER A 11 ? 1.1073 1.1455 0.9540 0.2343 -0.0311 0.3185 11 SER A OG 83 N N . ASN A 12 ? 1.0818 1.1212 0.9599 0.1774 -0.0316 0.2554 12 ASN A N 84 C CA . ASN A 12 ? 1.0976 1.1097 0.9872 0.1691 -0.0142 0.2421 12 ASN A CA 85 C C . ASN A 12 ? 1.0179 1.0462 0.9228 0.1474 -0.0221 0.2176 12 ASN A C 86 O O . ASN A 12 ? 0.9876 1.0527 0.9119 0.1444 -0.0401 0.2128 12 ASN A O 87 C CB . ASN A 12 ? 1.1675 1.1818 1.0822 0.1859 -0.0083 0.2524 12 ASN A CB 88 C CG . ASN A 12 ? 1.2818 1.2494 1.1793 0.1997 0.0154 0.2655 12 ASN A CG 89 O OD1 . ASN A 12 ? 1.3077 1.2393 1.1752 0.1936 0.0284 0.2653 12 ASN A OD1 90 N ND2 . ASN A 12 ? 1.3951 1.3607 1.3100 0.2179 0.0227 0.2769 12 ASN A ND2 91 N N . GLY A 13 ? 0.9679 0.9690 0.8638 0.1324 -0.0081 0.2028 13 GLY A N 92 C CA . GLY A 13 ? 0.9111 0.9240 0.8206 0.1138 -0.0126 0.1804 13 GLY A CA 93 C C . GLY A 13 ? 0.8656 0.8685 0.7976 0.1104 -0.0021 0.1718 13 GLY A C 94 O O . GLY A 13 ? 0.8674 0.8581 0.8076 0.1230 0.0068 0.1826 13 GLY A O 95 N N . THR A 14 ? 0.8103 0.8177 0.7510 0.0941 -0.0026 0.1525 14 THR A N 96 C CA . THR A 14 ? 0.7636 0.7608 0.7224 0.0883 0.0075 0.1428 14 THR A CA 97 C C . THR A 14 ? 0.7463 0.7196 0.6902 0.0735 0.0224 0.1319 14 THR A C 98 O O . THR A 14 ? 0.7273 0.7094 0.6631 0.0625 0.0184 0.1214 14 THR A O 99 C CB . THR A 14 ? 0.7327 0.7585 0.7170 0.0821 -0.0060 0.1302 14 THR A CB 100 O OG1 . THR A 14 ? 0.7424 0.7962 0.7381 0.0922 -0.0221 0.1398 14 THR A OG1 101 C CG2 . THR A 14 ? 0.7173 0.7340 0.7212 0.0797 0.0038 0.1238 14 THR A CG2 102 N N . LYS A 15 ? 0.7383 0.6818 0.6776 0.0731 0.0401 0.1347 15 LYS A N 103 C CA . LYS A 15 ? 0.7399 0.6621 0.6655 0.0569 0.0548 0.1251 15 LYS A CA 104 C C . LYS A 15 ? 0.6887 0.6280 0.6321 0.0425 0.0516 0.1066 15 LYS A C 105 O O . LYS A 15 ? 0.6576 0.6073 0.6229 0.0445 0.0470 0.1019 15 LYS A O 106 C CB . LYS A 15 ? 0.7802 0.6635 0.6942 0.0580 0.0746 0.1319 15 LYS A CB 107 C CG . LYS A 15 ? 0.8389 0.6960 0.7261 0.0685 0.0831 0.1492 15 LYS A CG 108 C CD . LYS A 15 ? 0.8867 0.6996 0.7597 0.0705 0.1041 0.1559 15 LYS A CD 109 C CE . LYS A 15 ? 0.8976 0.7095 0.7892 0.0870 0.1040 0.1624 15 LYS A CE 110 N NZ . LYS A 15 ? 0.9526 0.7216 0.8234 0.1014 0.1217 0.1785 15 LYS A NZ 111 N N . VAL A 16 ? 0.6646 0.6080 0.5981 0.0291 0.0543 0.0971 16 VAL A N 112 C CA . VAL A 16 ? 0.6220 0.5808 0.5693 0.0160 0.0535 0.0809 16 VAL A CA 113 C C . VAL A 16 ? 0.6331 0.5819 0.5652 0.0007 0.0672 0.0760 16 VAL A C 114 O O . VAL A 16 ? 0.6491 0.5817 0.5592 -0.0001 0.0751 0.0841 16 VAL A O 115 C CB . VAL A 16 ? 0.5947 0.5832 0.5506 0.0173 0.0373 0.0729 16 VAL A CB 116 C CG1 . VAL A 16 ? 0.5822 0.5840 0.5547 0.0283 0.0234 0.0762 16 VAL A CG1 117 C CG2 . VAL A 16 ? 0.6136 0.6058 0.5484 0.0182 0.0345 0.0762 16 VAL A CG2 118 N N . ASN A 17 ? 0.6088 0.5695 0.5529 -0.0115 0.0697 0.0633 17 ASN A N 119 C CA . ASN A 17 ? 0.6143 0.5739 0.5486 -0.0279 0.0815 0.0577 17 ASN A CA 120 C C . ASN A 17 ? 0.5829 0.5722 0.5205 -0.0309 0.0752 0.0494 17 ASN A C 121 O O . ASN A 17 ? 0.5678 0.5764 0.5188 -0.0236 0.0628 0.0439 17 ASN A O 122 C CB . ASN A 17 ? 0.6182 0.5717 0.5621 -0.0405 0.0900 0.0504 17 ASN A CB 123 C CG . ASN A 17 ? 0.6515 0.5707 0.5884 -0.0374 0.0990 0.0580 17 ASN A CG 124 O OD1 . ASN A 17 ? 0.6933 0.5868 0.6110 -0.0322 0.1063 0.0693 17 ASN A OD1 125 N ND2 . ASN A 17 ? 0.6410 0.5581 0.5920 -0.0397 0.0995 0.0524 17 ASN A ND2 126 N N . THR A 18 ? 0.5836 0.5752 0.5078 -0.0416 0.0849 0.0487 18 THR A N 127 C CA . THR A 18 ? 0.5660 0.5856 0.4922 -0.0438 0.0822 0.0414 18 THR A CA 128 C C . THR A 18 ? 0.5693 0.5998 0.4977 -0.0615 0.0944 0.0359 18 THR A C 129 O O . THR A 18 ? 0.5790 0.5949 0.5079 -0.0728 0.1027 0.0360 18 THR A O 130 C CB . THR A 18 ? 0.5832 0.6004 0.4884 -0.0373 0.0813 0.0479 18 THR A CB 131 O OG1 . THR A 18 ? 0.6022 0.6022 0.4880 -0.0473 0.0957 0.0548 18 THR A OG1 132 C CG2 . THR A 18 ? 0.5913 0.5972 0.4918 -0.0220 0.0695 0.0555 18 THR A CG2 133 N N . LEU A 19 ? 0.5752 0.6320 0.5044 -0.0643 0.0958 0.0310 19 LEU A N 134 C CA . LEU A 19 ? 0.5858 0.6604 0.5184 -0.0817 0.1072 0.0269 19 LEU A CA 135 C C . LEU A 19 ? 0.6363 0.6891 0.5475 -0.0949 0.1212 0.0343 19 LEU A C 136 O O . LEU A 19 ? 0.6499 0.7024 0.5608 -0.1137 0.1317 0.0325 19 LEU A O 137 C CB . LEU A 19 ? 0.5749 0.6847 0.5131 -0.0784 0.1064 0.0218 19 LEU A CB 138 C CG . LEU A 19 ? 0.5482 0.6801 0.5049 -0.0660 0.0951 0.0140 19 LEU A CG 139 C CD1 . LEU A 19 ? 0.5466 0.7076 0.5029 -0.0609 0.0979 0.0109 19 LEU A CD1 140 C CD2 . LEU A 19 ? 0.5259 0.6692 0.5030 -0.0737 0.0937 0.0083 19 LEU A CD2 141 N N . THR A 20 ? 0.6766 0.7108 0.5682 -0.0855 0.1210 0.0427 20 THR A N 142 C CA . THR A 20 ? 0.7329 0.7444 0.6001 -0.0953 0.1344 0.0511 20 THR A CA 143 C C . THR A 20 ? 0.7779 0.7469 0.6322 -0.0956 0.1391 0.0592 20 THR A C 144 O O . THR A 20 ? 0.8036 0.7499 0.6410 -0.1106 0.1536 0.0634 20 THR A O 145 C CB . THR A 20 ? 0.7505 0.7624 0.6000 -0.0836 0.1320 0.0572 20 THR A CB 146 O OG1 . THR A 20 ? 0.7464 0.7921 0.6004 -0.0879 0.1352 0.0511 20 THR A OG1 147 C CG2 . THR A 20 ? 0.8042 0.7827 0.6251 -0.0881 0.1432 0.0690 20 THR A CG2 148 N N . GLU A 21 ? 0.7807 0.7387 0.6424 -0.0791 0.1280 0.0617 21 GLU A N 149 C CA . GLU A 21 ? 0.8261 0.7448 0.6721 -0.0715 0.1316 0.0731 21 GLU A CA 150 C C . GLU A 21 ? 0.8111 0.7198 0.6729 -0.0636 0.1258 0.0720 21 GLU A C 151 O O . GLU A 21 ? 0.7734 0.7057 0.6570 -0.0554 0.1126 0.0654 21 GLU A O 152 C CB . GLU A 21 ? 0.8577 0.7724 0.6892 -0.0543 0.1241 0.0833 21 GLU A CB 153 C CG . GLU A 21 ? 0.9168 0.7918 0.7247 -0.0471 0.1316 0.0984 21 GLU A CG 154 C CD . GLU A 21 ? 0.9527 0.8267 0.7413 -0.0343 0.1261 0.1090 21 GLU A CD 155 O OE1 . GLU A 21 ? 0.9532 0.8513 0.7395 -0.0367 0.1222 0.1040 21 GLU A OE1 156 O OE2 . GLU A 21 ? 0.9949 0.8440 0.7694 -0.0211 0.1262 0.1227 21 GLU A OE2 157 N N . ARG A 22 ? 0.8402 0.7115 0.6888 -0.0660 0.1371 0.0787 22 ARG A N 158 C CA . ARG A 22 ? 0.8507 0.7067 0.7097 -0.0548 0.1338 0.0808 22 ARG A CA 159 C C . ARG A 22 ? 0.8504 0.6918 0.7009 -0.0325 0.1283 0.0954 22 ARG A C 160 O O . ARG A 22 ? 0.8717 0.6883 0.6974 -0.0299 0.1369 0.1067 22 ARG A O 161 C CB . ARG A 22 ? 0.9069 0.7269 0.7538 -0.0684 0.1507 0.0802 22 ARG A CB 162 C CG . ARG A 22 ? 0.9140 0.7503 0.7768 -0.0865 0.1520 0.0656 22 ARG A CG 163 C CD . ARG A 22 ? 0.9676 0.7719 0.8279 -0.0882 0.1604 0.0648 22 ARG A CD 164 N NE . ARG A 22 ? 0.9730 0.8036 0.8593 -0.0902 0.1511 0.0534 22 ARG A NE 165 C CZ . ARG A 22 ? 1.0063 0.8222 0.9001 -0.0835 0.1516 0.0524 22 ARG A CZ 166 N NH1 . ARG A 22 ? 1.0499 0.8246 0.9282 -0.0729 0.1616 0.0621 22 ARG A NH1 167 N NH2 . ARG A 22 ? 0.9885 0.8309 0.9050 -0.0864 0.1427 0.0420 22 ARG A NH2 168 N N . GLY A 23 ? 0.8123 0.6705 0.6830 -0.0168 0.1139 0.0958 23 GLY A N 169 C CA . GLY A 23 ? 0.8146 0.6628 0.6816 0.0046 0.1083 0.1104 23 GLY A CA 170 C C . GLY A 23 ? 0.8136 0.6725 0.6676 0.0145 0.0995 0.1193 23 GLY A C 171 O O . GLY A 23 ? 0.8453 0.6850 0.6836 0.0279 0.1018 0.1346 23 GLY A O 172 N N . VAL A 24 ? 0.7838 0.6720 0.6423 0.0087 0.0898 0.1104 24 VAL A N 173 C CA . VAL A 24 ? 0.7871 0.6879 0.6337 0.0184 0.0791 0.1173 24 VAL A CA 174 C C . VAL A 24 ? 0.7665 0.6861 0.6299 0.0343 0.0613 0.1212 24 VAL A C 175 O O . VAL A 24 ? 0.7257 0.6625 0.6133 0.0334 0.0537 0.1119 24 VAL A O 176 C CB . VAL A 24 ? 0.7750 0.6984 0.6176 0.0082 0.0760 0.1064 24 VAL A CB 177 C CG1 . VAL A 24 ? 0.7362 0.6873 0.6040 0.0033 0.0671 0.0909 24 VAL A CG1 178 C CG2 . VAL A 24 ? 0.7909 0.7227 0.6166 0.0180 0.0656 0.1137 24 VAL A CG2 179 N N . GLU A 25 ? 0.7823 0.6997 0.6325 0.0482 0.0549 0.1357 25 GLU A N 180 C CA . GLU A 25 ? 0.7721 0.7112 0.6379 0.0622 0.0376 0.1412 25 GLU A CA 181 C C . GLU A 25 ? 0.7496 0.7182 0.6158 0.0594 0.0207 0.1331 25 GLU A C 182 O O . GLU A 25 ? 0.7702 0.7382 0.6144 0.0556 0.0209 0.1329 25 GLU A O 183 C CB . GLU A 25 ? 0.8106 0.7371 0.6638 0.0799 0.0379 0.1622 25 GLU A CB 184 C CG . GLU A 25 ? 0.8325 0.7314 0.6901 0.0875 0.0524 0.1706 25 GLU A CG 185 C CD . GLU A 25 ? 0.8714 0.7626 0.7210 0.1095 0.0514 0.1926 25 GLU A CD 186 O OE1 . GLU A 25 ? 0.8730 0.7933 0.7271 0.1198 0.0338 0.2001 25 GLU A OE1 187 O OE2 . GLU A 25 ? 0.8965 0.7523 0.7342 0.1166 0.0684 0.2028 25 GLU A OE2 188 N N . VAL A 26 ? 0.7195 0.7115 0.6089 0.0607 0.0071 0.1262 26 VAL A N 189 C CA . VAL A 26 ? 0.7115 0.7281 0.6007 0.0571 -0.0091 0.1173 26 VAL A CA 190 C C . VAL A 26 ? 0.7172 0.7551 0.6185 0.0667 -0.0264 0.1251 26 VAL A C 191 O O . VAL A 26 ? 0.7147 0.7522 0.6307 0.0766 -0.0253 0.1356 26 VAL A O 192 C CB . VAL A 26 ? 0.6786 0.7041 0.5828 0.0455 -0.0089 0.0984 26 VAL A CB 193 C CG1 . VAL A 26 ? 0.6791 0.6931 0.5699 0.0355 0.0054 0.0908 26 VAL A CG1 194 C CG2 . VAL A 26 ? 0.6544 0.6808 0.5862 0.0459 -0.0066 0.0954 26 VAL A CG2 195 N N . VAL A 27 ? 0.7279 0.7851 0.6224 0.0632 -0.0417 0.1198 27 VAL A N 196 C CA . VAL A 27 ? 0.7425 0.8239 0.6448 0.0695 -0.0598 0.1277 27 VAL A CA 197 C C . VAL A 27 ? 0.7233 0.8199 0.6580 0.0690 -0.0651 0.1230 27 VAL A C 198 O O . VAL A 27 ? 0.7147 0.8259 0.6649 0.0789 -0.0713 0.1353 27 VAL A O 199 C CB . VAL A 27 ? 0.7549 0.8501 0.6371 0.0625 -0.0745 0.1214 27 VAL A CB 200 C CG1 . VAL A 27 ? 0.7553 0.8798 0.6475 0.0651 -0.0946 0.1279 27 VAL A CG1 201 C CG2 . VAL A 27 ? 0.7876 0.8693 0.6367 0.0649 -0.0697 0.1289 27 VAL A CG2 202 N N . ASN A 28 ? 0.7277 0.8219 0.6725 0.0584 -0.0621 0.1060 28 ASN A N 203 C CA . ASN A 28 ? 0.7258 0.8307 0.6998 0.0568 -0.0649 0.1007 28 ASN A CA 204 C C . ASN A 28 ? 0.6766 0.7665 0.6587 0.0492 -0.0519 0.0869 28 ASN A C 205 O O . ASN A 28 ? 0.6655 0.7453 0.6324 0.0423 -0.0459 0.0776 28 ASN A O 206 C CB . ASN A 28 ? 0.7728 0.9017 0.7517 0.0502 -0.0835 0.0942 28 ASN A CB 207 C CG . ASN A 28 ? 0.8365 0.9815 0.8460 0.0504 -0.0883 0.0938 28 ASN A CG 208 O OD1 . ASN A 28 ? 0.7969 0.9368 0.8241 0.0581 -0.0785 0.1004 28 ASN A OD1 209 N ND2 . ASN A 28 ? 0.9497 1.1126 0.9639 0.0412 -0.1026 0.0859 28 ASN A ND2 210 N N . ALA A 29 ? 0.6368 0.7270 0.6427 0.0509 -0.0475 0.0865 29 ALA A N 211 C CA . ALA A 29 ? 0.6090 0.6884 0.6242 0.0434 -0.0369 0.0741 29 ALA A CA 212 C C . ALA A 29 ? 0.5792 0.6687 0.6208 0.0431 -0.0402 0.0706 29 ALA A C 213 O O . ALA A 29 ? 0.5833 0.6871 0.6382 0.0497 -0.0479 0.0795 29 ALA A O 214 C CB . ALA A 29 ? 0.6164 0.6726 0.6244 0.0443 -0.0192 0.0782 29 ALA A CB 215 N N . THR A 30 ? 0.5477 0.6317 0.5969 0.0355 -0.0342 0.0583 30 THR A N 216 C CA . THR A 30 ? 0.5253 0.6171 0.5973 0.0340 -0.0364 0.0538 30 THR A CA 217 C C . THR A 30 ? 0.4985 0.5764 0.5774 0.0297 -0.0230 0.0470 30 THR A C 218 O O . THR A 30 ? 0.4968 0.5648 0.5640 0.0241 -0.0150 0.0411 30 THR A O 219 C CB . THR A 30 ? 0.5191 0.6247 0.5930 0.0271 -0.0495 0.0435 30 THR A CB 220 O OG1 . THR A 30 ? 0.5219 0.6395 0.6177 0.0271 -0.0547 0.0442 30 THR A OG1 221 C CG2 . THR A 30 ? 0.5152 0.6126 0.5817 0.0196 -0.0446 0.0296 30 THR A CG2 222 N N . GLU A 31 ? 0.4767 0.5562 0.5745 0.0316 -0.0208 0.0480 31 GLU A N 223 C CA . GLU A 31 ? 0.4623 0.5282 0.5658 0.0275 -0.0083 0.0428 31 GLU A CA 224 C C . GLU A 31 ? 0.4368 0.5076 0.5434 0.0183 -0.0102 0.0288 31 GLU A C 225 O O . GLU A 31 ? 0.4193 0.5027 0.5326 0.0169 -0.0207 0.0240 31 GLU A O 226 C CB . GLU A 31 ? 0.4588 0.5245 0.5799 0.0342 -0.0048 0.0494 31 GLU A CB 227 C CG . GLU A 31 ? 0.4600 0.5088 0.5844 0.0301 0.0088 0.0447 31 GLU A CG 228 C CD . GLU A 31 ? 0.4757 0.5020 0.5815 0.0262 0.0221 0.0452 31 GLU A CD 229 O OE1 . GLU A 31 ? 0.4973 0.5073 0.5957 0.0337 0.0306 0.0557 31 GLU A OE1 230 O OE2 . GLU A 31 ? 0.4654 0.4904 0.5636 0.0155 0.0245 0.0356 31 GLU A OE2 231 N N . THR A 32 ? 0.4346 0.4957 0.5355 0.0117 0.0000 0.0227 32 THR A N 232 C CA . THR A 32 ? 0.4096 0.4769 0.5144 0.0049 -0.0008 0.0111 32 THR A CA 233 C C . THR A 32 ? 0.3966 0.4584 0.5128 0.0012 0.0064 0.0079 32 THR A C 234 O O . THR A 32 ? 0.3877 0.4557 0.5087 -0.0031 0.0050 -0.0003 32 THR A O 235 C CB . THR A 32 ? 0.4226 0.4906 0.5137 -0.0007 0.0042 0.0060 32 THR A CB 236 O OG1 . THR A 32 ? 0.4287 0.4848 0.5144 -0.0060 0.0167 0.0083 32 THR A OG1 237 C CG2 . THR A 32 ? 0.4405 0.5121 0.5173 0.0027 -0.0014 0.0085 32 THR A CG2 238 N N . VAL A 33 ? 0.4033 0.4520 0.5218 0.0036 0.0147 0.0146 33 VAL A N 239 C CA . VAL A 33 ? 0.4020 0.4417 0.5276 -0.0003 0.0232 0.0116 33 VAL A CA 240 C C . VAL A 33 ? 0.4097 0.4499 0.5502 0.0078 0.0217 0.0173 33 VAL A C 241 O O . VAL A 33 ? 0.4095 0.4443 0.5504 0.0166 0.0241 0.0275 33 VAL A O 242 C CB . VAL A 33 ? 0.4222 0.4409 0.5345 -0.0054 0.0375 0.0135 33 VAL A CB 243 C CG1 . VAL A 33 ? 0.4236 0.4306 0.5397 -0.0106 0.0466 0.0095 33 VAL A CG1 244 C CG2 . VAL A 33 ? 0.4317 0.4539 0.5309 -0.0148 0.0396 0.0085 33 VAL A CG2 245 N N . GLU A 34 ? 0.4067 0.4545 0.5594 0.0053 0.0186 0.0116 34 GLU A N 246 C CA . GLU A 34 ? 0.4113 0.4635 0.5801 0.0118 0.0173 0.0165 34 GLU A CA 247 C C . GLU A 34 ? 0.4310 0.4647 0.5999 0.0144 0.0316 0.0203 34 GLU A C 248 O O . GLU A 34 ? 0.4331 0.4539 0.5948 0.0064 0.0402 0.0135 34 GLU A O 249 C CB . GLU A 34 ? 0.3966 0.4605 0.5760 0.0072 0.0103 0.0089 34 GLU A CB 250 C CG . GLU A 34 ? 0.3930 0.4656 0.5904 0.0121 0.0083 0.0139 34 GLU A CG 251 C CD . GLU A 34 ? 0.3936 0.4819 0.5981 0.0191 -0.0009 0.0229 34 GLU A CD 252 O OE1 . GLU A 34 ? 0.3902 0.4897 0.5915 0.0156 -0.0127 0.0199 34 GLU A OE1 253 O OE2 . GLU A 34 ? 0.4164 0.5054 0.6282 0.0283 0.0039 0.0333 34 GLU A OE2 254 N N . ARG A 35 ? 0.4542 0.4870 0.6301 0.0259 0.0344 0.0314 35 ARG A N 255 C CA . ARG A 35 ? 0.4807 0.4945 0.6570 0.0317 0.0492 0.0361 35 ARG A CA 256 C C . ARG A 35 ? 0.4709 0.4986 0.6685 0.0399 0.0482 0.0411 35 ARG A C 257 O O . ARG A 35 ? 0.4931 0.5058 0.6919 0.0447 0.0613 0.0435 35 ARG A O 258 C CB . ARG A 35 ? 0.5206 0.5161 0.6842 0.0411 0.0583 0.0468 35 ARG A CB 259 C CG . ARG A 35 ? 0.5457 0.5220 0.6861 0.0315 0.0638 0.0424 35 ARG A CG 260 C CD . ARG A 35 ? 0.5905 0.5427 0.7157 0.0409 0.0752 0.0537 35 ARG A CD 261 N NE . ARG A 35 ? 0.6028 0.5722 0.7350 0.0548 0.0658 0.0661 35 ARG A NE 262 C CZ . ARG A 35 ? 0.6110 0.5947 0.7382 0.0526 0.0544 0.0667 35 ARG A CZ 263 N NH1 . ARG A 35 ? 0.6096 0.5934 0.7260 0.0384 0.0515 0.0561 35 ARG A NH1 264 N NH2 . ARG A 35 ? 0.6113 0.6110 0.7440 0.0651 0.0458 0.0786 35 ARG A NH2 265 N N . THR A 36 ? 0.4507 0.5065 0.6640 0.0407 0.0336 0.0424 36 THR A N 266 C CA . THR A 36 ? 0.4481 0.5221 0.6835 0.0475 0.0321 0.0484 36 THR A CA 267 C C . THR A 36 ? 0.4292 0.5027 0.6710 0.0385 0.0339 0.0387 36 THR A C 268 O O . THR A 36 ? 0.4182 0.4982 0.6578 0.0279 0.0247 0.0295 36 THR A O 269 C CB . THR A 36 ? 0.4406 0.5464 0.6894 0.0493 0.0153 0.0540 36 THR A CB 270 O OG1 . THR A 36 ? 0.4534 0.5601 0.6939 0.0573 0.0126 0.0631 36 THR A OG1 271 C CG2 . THR A 36 ? 0.4410 0.5702 0.7148 0.0560 0.0145 0.0622 36 THR A CG2 272 N N . ASN A 37 ? 0.4366 0.5006 0.6842 0.0438 0.0469 0.0415 37 ASN A N 273 C CA . ASN A 37 ? 0.4309 0.4951 0.6853 0.0370 0.0498 0.0343 37 ASN A CA 274 C C . ASN A 37 ? 0.4245 0.5158 0.7038 0.0421 0.0452 0.0412 37 ASN A C 275 O O . ASN A 37 ? 0.4308 0.5364 0.7225 0.0542 0.0457 0.0533 37 ASN A O 276 C CB . ASN A 37 ? 0.4482 0.4839 0.6912 0.0383 0.0682 0.0321 37 ASN A CB 277 C CG . ASN A 37 ? 0.4494 0.4835 0.6958 0.0304 0.0715 0.0242 37 ASN A CG 278 O OD1 . ASN A 37 ? 0.4487 0.4884 0.6922 0.0192 0.0625 0.0153 37 ASN A OD1 279 N ND2 . ASN A 37 ? 0.4611 0.4867 0.7125 0.0373 0.0851 0.0280 37 ASN A ND2 280 N N . ILE A 38 ? 0.4163 0.5161 0.7028 0.0327 0.0407 0.0343 38 ILE A N 281 C CA . ILE A 38 ? 0.4124 0.5351 0.7219 0.0351 0.0400 0.0400 38 ILE A CA 282 C C . ILE A 38 ? 0.4039 0.5103 0.7122 0.0348 0.0548 0.0365 38 ILE A C 283 O O . ILE A 38 ? 0.3931 0.4849 0.6889 0.0243 0.0553 0.0259 38 ILE A O 284 C CB . ILE A 38 ? 0.4157 0.5592 0.7326 0.0233 0.0239 0.0354 38 ILE A CB 285 C CG1 . ILE A 38 ? 0.4367 0.5969 0.7539 0.0245 0.0101 0.0400 38 ILE A CG1 286 C CG2 . ILE A 38 ? 0.4095 0.5746 0.7488 0.0220 0.0249 0.0397 38 ILE A CG2 287 C CD1 . ILE A 38 ? 0.4484 0.6255 0.7684 0.0120 -0.0056 0.0352 38 ILE A CD1 288 N N . PRO A 39 ? 0.4104 0.5191 0.7303 0.0473 0.0676 0.0458 39 PRO A N 289 C CA . PRO A 39 ? 0.4300 0.5170 0.7435 0.0482 0.0846 0.0423 39 PRO A CA 290 C C . PRO A 39 ? 0.4269 0.5279 0.7540 0.0410 0.0841 0.0393 39 PRO A C 291 O O . PRO A 39 ? 0.4343 0.5341 0.7694 0.0478 0.0978 0.0434 39 PRO A O 292 C CB . PRO A 39 ? 0.4442 0.5272 0.7636 0.0670 0.0994 0.0547 39 PRO A CB 293 C CG . PRO A 39 ? 0.4356 0.5562 0.7787 0.0752 0.0877 0.0668 39 PRO A CG 294 C CD . PRO A 39 ? 0.4168 0.5472 0.7543 0.0627 0.0681 0.0606 39 PRO A CD 295 N N . ARG A 40 ? 0.4290 0.5404 0.7564 0.0275 0.0698 0.0323 40 ARG A N 296 C CA . ARG A 40 ? 0.4278 0.5472 0.7630 0.0183 0.0690 0.0284 40 ARG A CA 297 C C . ARG A 40 ? 0.4094 0.5151 0.7263 0.0048 0.0598 0.0165 40 ARG A C 298 O O . ARG A 40 ? 0.3986 0.4975 0.7026 0.0029 0.0519 0.0127 40 ARG A O 299 C CB . ARG A 40 ? 0.4353 0.5910 0.7967 0.0174 0.0599 0.0363 40 ARG A CB 300 C CG . ARG A 40 ? 0.4680 0.6434 0.8511 0.0324 0.0697 0.0496 40 ARG A CG 301 C CD . ARG A 40 ? 0.4977 0.7161 0.9081 0.0306 0.0587 0.0585 40 ARG A CD 302 N NE . ARG A 40 ? 0.5249 0.7566 0.9337 0.0273 0.0414 0.0596 40 ARG A NE 303 C CZ . ARG A 40 ? 0.5462 0.7871 0.9581 0.0400 0.0392 0.0687 40 ARG A CZ 304 N NH1 . ARG A 40 ? 0.5627 0.7986 0.9789 0.0584 0.0540 0.0782 40 ARG A NH1 305 N NH2 . ARG A 40 ? 0.5451 0.7975 0.9530 0.0346 0.0228 0.0684 40 ARG A NH2 306 N N . ILE A 41 ? 0.4022 0.5035 0.7170 -0.0034 0.0620 0.0114 41 ILE A N 307 C CA . ILE A 41 ? 0.4013 0.4927 0.7006 -0.0142 0.0530 0.0021 41 ILE A CA 308 C C . ILE A 41 ? 0.3884 0.4986 0.6986 -0.0212 0.0400 0.0033 41 ILE A C 309 O O . ILE A 41 ? 0.3797 0.5012 0.7026 -0.0259 0.0415 0.0058 41 ILE A O 310 C CB . ILE A 41 ? 0.4224 0.4973 0.7105 -0.0194 0.0617 -0.0034 41 ILE A CB 311 C CG1 . ILE A 41 ? 0.4467 0.5015 0.7211 -0.0149 0.0750 -0.0053 41 ILE A CG1 312 C CG2 . ILE A 41 ? 0.4218 0.4879 0.6939 -0.0279 0.0523 -0.0111 41 ILE A CG2 313 C CD1 . ILE A 41 ? 0.4580 0.5021 0.7166 -0.0145 0.0714 -0.0092 41 ILE A CD1 314 N N . CYS A 42 ? 0.3769 0.4901 0.6809 -0.0228 0.0279 0.0013 42 CYS A N 315 C CA . CYS A 42 ? 0.3746 0.5024 0.6843 -0.0308 0.0150 0.0014 42 CYS A CA 316 C C . CYS A 42 ? 0.3770 0.4894 0.6722 -0.0407 0.0118 -0.0065 42 CYS A C 317 O O . CYS A 42 ? 0.3677 0.4635 0.6437 -0.0408 0.0087 -0.0129 42 CYS A O 318 C CB . CYS A 42 ? 0.3647 0.4968 0.6683 -0.0286 0.0044 0.0015 42 CYS A CB 319 S SG . CYS A 42 ? 0.3671 0.5198 0.6876 -0.0167 0.0057 0.0130 42 CYS A SG 320 N N . SER A 43 ? 0.3814 0.5000 0.6857 -0.0485 0.0134 -0.0051 43 SER A N 321 C CA . SER A 43 ? 0.3908 0.4909 0.6802 -0.0566 0.0139 -0.0112 43 SER A CA 322 C C . SER A 43 ? 0.3816 0.4858 0.6711 -0.0695 0.0052 -0.0124 43 SER A C 323 O O . SER A 43 ? 0.3834 0.4721 0.6622 -0.0770 0.0072 -0.0157 43 SER A O 324 C CB . SER A 43 ? 0.3939 0.4893 0.6876 -0.0558 0.0269 -0.0095 43 SER A CB 325 O OG . SER A 43 ? 0.4165 0.5344 0.7336 -0.0585 0.0305 -0.0025 43 SER A OG 326 N N . LYS A 44 ? 0.3748 0.4982 0.6741 -0.0729 -0.0043 -0.0096 44 LYS A N 327 C CA . LYS A 44 ? 0.3876 0.5142 0.6840 -0.0879 -0.0135 -0.0117 44 LYS A CA 328 C C . LYS A 44 ? 0.3910 0.4845 0.6582 -0.0930 -0.0160 -0.0205 44 LYS A C 329 O O . LYS A 44 ? 0.3732 0.4523 0.6237 -0.0857 -0.0190 -0.0248 44 LYS A O 330 C CB . LYS A 44 ? 0.3996 0.5474 0.7028 -0.0901 -0.0253 -0.0091 44 LYS A CB 331 C CG . LYS A 44 ? 0.4282 0.5756 0.7231 -0.1085 -0.0353 -0.0130 44 LYS A CG 332 C CD . LYS A 44 ? 0.4454 0.6224 0.7517 -0.1134 -0.0472 -0.0087 44 LYS A CD 333 C CE . LYS A 44 ? 0.4551 0.6199 0.7422 -0.1066 -0.0545 -0.0129 44 LYS A CE 334 N NZ . LYS A 44 ? 0.4633 0.6612 0.7663 -0.1036 -0.0631 -0.0053 44 LYS A NZ 335 N N . GLY A 45 ? 0.4022 0.4841 0.6629 -0.1054 -0.0141 -0.0226 45 GLY A N 336 C CA . GLY A 45 ? 0.4199 0.4677 0.6510 -0.1101 -0.0157 -0.0299 45 GLY A CA 337 C C . GLY A 45 ? 0.4214 0.4452 0.6374 -0.1001 -0.0069 -0.0318 45 GLY A C 338 O O . GLY A 45 ? 0.4408 0.4357 0.6317 -0.1004 -0.0068 -0.0365 45 GLY A O 339 N N . LYS A 46 ? 0.3972 0.4321 0.6269 -0.0912 0.0009 -0.0279 46 LYS A N 340 C CA . LYS A 46 ? 0.4060 0.4225 0.6215 -0.0822 0.0082 -0.0294 46 LYS A CA 341 C C . LYS A 46 ? 0.4016 0.4162 0.6225 -0.0856 0.0184 -0.0264 46 LYS A C 342 O O . LYS A 46 ? 0.3901 0.4248 0.6325 -0.0865 0.0236 -0.0218 46 LYS A O 343 C CB . LYS A 46 ? 0.3969 0.4225 0.6164 -0.0694 0.0093 -0.0291 46 LYS A CB 344 C CG . LYS A 46 ? 0.3972 0.4198 0.6056 -0.0642 0.0010 -0.0325 46 LYS A CG 345 C CD . LYS A 46 ? 0.3816 0.4128 0.5933 -0.0539 0.0029 -0.0320 46 LYS A CD 346 C CE . LYS A 46 ? 0.3786 0.4101 0.5816 -0.0497 -0.0050 -0.0347 46 LYS A CE 347 N NZ . LYS A 46 ? 0.3638 0.4062 0.5729 -0.0424 -0.0029 -0.0332 46 LYS A NZ 348 N N . ARG A 47 ? 0.4228 0.4129 0.6230 -0.0858 0.0221 -0.0283 47 ARG A N 349 C CA . ARG A 47 ? 0.4341 0.4196 0.6349 -0.0872 0.0325 -0.0256 47 ARG A CA 350 C C . ARG A 47 ? 0.3943 0.3901 0.6019 -0.0770 0.0382 -0.0245 47 ARG A C 351 O O . ARG A 47 ? 0.3706 0.3588 0.5645 -0.0683 0.0367 -0.0270 47 ARG A O 352 C CB . ARG A 47 ? 0.4854 0.4408 0.6592 -0.0876 0.0348 -0.0270 47 ARG A CB 353 C CG . ARG A 47 ? 0.5443 0.4838 0.7089 -0.1006 0.0326 -0.0280 47 ARG A CG 354 C CD . ARG A 47 ? 0.6089 0.5146 0.7448 -0.0999 0.0371 -0.0281 47 ARG A CD 355 N NE . ARG A 47 ? 0.6711 0.5577 0.7844 -0.0896 0.0316 -0.0313 47 ARG A NE 356 C CZ . ARG A 47 ? 0.7240 0.6023 0.8224 -0.0748 0.0326 -0.0305 47 ARG A CZ 357 N NH1 . ARG A 47 ? 0.7379 0.6227 0.8383 -0.0697 0.0384 -0.0274 47 ARG A NH1 358 N NH2 . ARG A 47 ? 0.7659 0.6301 0.8461 -0.0650 0.0280 -0.0328 47 ARG A NH2 359 N N . THR A 48 ? 0.3747 0.3881 0.6030 -0.0784 0.0451 -0.0206 48 THR A N 360 C CA . THR A 48 ? 0.3686 0.3899 0.6033 -0.0697 0.0517 -0.0197 48 THR A CA 361 C C . THR A 48 ? 0.3800 0.3972 0.6149 -0.0709 0.0647 -0.0176 48 THR A C 362 O O . THR A 48 ? 0.3946 0.4185 0.6413 -0.0776 0.0701 -0.0139 48 THR A O 363 C CB . THR A 48 ? 0.3581 0.4027 0.6161 -0.0667 0.0503 -0.0163 48 THR A CB 364 O OG1 . THR A 48 ? 0.3626 0.4115 0.6198 -0.0677 0.0379 -0.0179 48 THR A OG1 365 C CG2 . THR A 48 ? 0.3509 0.3963 0.6094 -0.0570 0.0571 -0.0162 48 THR A CG2 366 N N . VAL A 49 ? 0.3847 0.3918 0.6058 -0.0652 0.0698 -0.0200 49 VAL A N 367 C CA . VAL A 49 ? 0.3907 0.3911 0.6071 -0.0658 0.0826 -0.0190 49 VAL A CA 368 C C . VAL A 49 ? 0.3896 0.3938 0.6097 -0.0592 0.0898 -0.0197 49 VAL A C 369 O O . VAL A 49 ? 0.3773 0.3752 0.5837 -0.0560 0.0867 -0.0237 49 VAL A O 370 C CB . VAL A 49 ? 0.4093 0.3904 0.5991 -0.0666 0.0822 -0.0217 49 VAL A CB 371 C CG1 . VAL A 49 ? 0.4262 0.3996 0.6068 -0.0670 0.0949 -0.0217 49 VAL A CG1 372 C CG2 . VAL A 49 ? 0.4177 0.3892 0.6010 -0.0725 0.0781 -0.0201 49 VAL A CG2 373 N N . ASP A 50 ? 0.3915 0.4060 0.6295 -0.0573 0.0999 -0.0155 50 ASP A N 374 C CA . ASP A 50 ? 0.3872 0.3997 0.6260 -0.0503 0.1099 -0.0156 50 ASP A CA 375 C C . ASP A 50 ? 0.4044 0.4009 0.6276 -0.0520 0.1238 -0.0173 50 ASP A C 376 O O . ASP A 50 ? 0.4047 0.4047 0.6364 -0.0536 0.1332 -0.0135 50 ASP A O 377 C CB . ASP A 50 ? 0.3824 0.4150 0.6485 -0.0442 0.1141 -0.0088 50 ASP A CB 378 C CG . ASP A 50 ? 0.3940 0.4197 0.6590 -0.0350 0.1273 -0.0078 50 ASP A CG 379 O OD1 . ASP A 50 ? 0.4094 0.4138 0.6512 -0.0359 0.1327 -0.0136 50 ASP A OD1 380 O OD2 . ASP A 50 ? 0.3945 0.4360 0.6807 -0.0270 0.1327 -0.0009 50 ASP A OD2 381 N N . LEU A 51 ? 0.4174 0.3976 0.6171 -0.0526 0.1250 -0.0231 51 LEU A N 382 C CA . LEU A 51 ? 0.4447 0.4080 0.6231 -0.0564 0.1356 -0.0260 51 LEU A CA 383 C C . LEU A 51 ? 0.4688 0.4252 0.6497 -0.0524 0.1543 -0.0245 51 LEU A C 384 O O . LEU A 51 ? 0.4973 0.4434 0.6671 -0.0553 0.1652 -0.0248 51 LEU A O 385 C CB . LEU A 51 ? 0.4471 0.3989 0.5995 -0.0599 0.1300 -0.0326 51 LEU A CB 386 C CG . LEU A 51 ? 0.4359 0.3927 0.5811 -0.0621 0.1141 -0.0335 51 LEU A CG 387 C CD1 . LEU A 51 ? 0.4376 0.3909 0.5620 -0.0648 0.1086 -0.0389 51 LEU A CD1 388 C CD2 . LEU A 51 ? 0.4465 0.3980 0.5841 -0.0654 0.1145 -0.0310 51 LEU A CD2 389 N N . GLY A 52 ? 0.4747 0.4355 0.6686 -0.0447 0.1591 -0.0224 52 GLY A N 390 C CA . GLY A 52 ? 0.4989 0.4526 0.6962 -0.0377 0.1783 -0.0197 52 GLY A CA 391 C C . GLY A 52 ? 0.5354 0.4610 0.7006 -0.0420 0.1903 -0.0268 52 GLY A C 392 O O . GLY A 52 ? 0.5437 0.4552 0.6882 -0.0461 0.1866 -0.0332 52 GLY A O 393 N N . GLN A 53 ? 0.5490 0.4672 0.7090 -0.0424 0.2047 -0.0256 53 GLN A N 394 C CA . GLN A 53 ? 0.5840 0.4739 0.7110 -0.0472 0.2176 -0.0325 53 GLN A CA 395 C C . GLN A 53 ? 0.5691 0.4519 0.6703 -0.0596 0.2070 -0.0384 53 GLN A C 396 O O . GLN A 53 ? 0.5712 0.4326 0.6418 -0.0663 0.2138 -0.0451 53 GLN A O 397 C CB . GLN A 53 ? 0.6241 0.5081 0.7536 -0.0419 0.2386 -0.0288 53 GLN A CB 398 C CG . GLN A 53 ? 0.6611 0.5430 0.8045 -0.0278 0.2545 -0.0242 53 GLN A CG 399 C CD . GLN A 53 ? 0.7119 0.5899 0.8583 -0.0212 0.2764 -0.0200 53 GLN A CD 400 O OE1 . GLN A 53 ? 0.7313 0.6362 0.9085 -0.0154 0.2785 -0.0110 53 GLN A OE1 401 N NE2 . GLN A 53 ? 0.7570 0.6023 0.8705 -0.0231 0.2932 -0.0266 53 GLN A NE2 402 N N . CYS A 54 ? 0.5396 0.4397 0.6518 -0.0625 0.1909 -0.0356 54 CYS A N 403 C CA . CYS A 54 ? 0.5438 0.4403 0.6338 -0.0711 0.1793 -0.0393 54 CYS A CA 404 C C . CYS A 54 ? 0.5380 0.4355 0.6172 -0.0741 0.1668 -0.0445 54 CYS A C 405 O O . CYS A 54 ? 0.5224 0.4330 0.6196 -0.0699 0.1570 -0.0429 54 CYS A O 406 C CB . CYS A 54 ? 0.5279 0.4389 0.6320 -0.0714 0.1679 -0.0338 54 CYS A CB 407 S SG . CYS A 54 ? 0.5323 0.4397 0.6105 -0.0776 0.1539 -0.0357 54 CYS A SG 408 N N . GLY A 55 ? 0.5499 0.4354 0.5994 -0.0823 0.1668 -0.0507 55 GLY A N 409 C CA . GLY A 55 ? 0.5388 0.4307 0.5777 -0.0874 0.1534 -0.0550 55 GLY A CA 410 C C . GLY A 55 ? 0.5243 0.4334 0.5672 -0.0863 0.1365 -0.0514 55 GLY A C 411 O O . GLY A 55 ? 0.5313 0.4390 0.5694 -0.0861 0.1366 -0.0479 55 GLY A O 412 N N . LEU A 56 ? 0.4961 0.4194 0.5461 -0.0849 0.1232 -0.0519 56 LEU A N 413 C CA . LEU A 56 ? 0.4878 0.4257 0.5417 -0.0812 0.1083 -0.0480 56 LEU A CA 414 C C . LEU A 56 ? 0.4966 0.4344 0.5266 -0.0851 0.1044 -0.0476 56 LEU A C 415 O O . LEU A 56 ? 0.4902 0.4295 0.5202 -0.0804 0.0994 -0.0424 56 LEU A O 416 C CB . LEU A 56 ? 0.4755 0.4286 0.5376 -0.0792 0.0965 -0.0493 56 LEU A CB 417 C CG . LEU A 56 ? 0.4625 0.4299 0.5265 -0.0736 0.0821 -0.0457 56 LEU A CG 418 C CD1 . LEU A 56 ? 0.4587 0.4221 0.5360 -0.0670 0.0812 -0.0403 56 LEU A CD1 419 C CD2 . LEU A 56 ? 0.4534 0.4354 0.5261 -0.0716 0.0731 -0.0473 56 LEU A CD2 420 N N . LEU A 57 ? 0.5122 0.4472 0.5200 -0.0941 0.1067 -0.0528 57 LEU A N 421 C CA . LEU A 57 ? 0.5284 0.4664 0.5119 -0.0984 0.1022 -0.0519 57 LEU A CA 422 C C . LEU A 57 ? 0.5431 0.4640 0.5163 -0.0987 0.1130 -0.0493 57 LEU A C 423 O O . LEU A 57 ? 0.5522 0.4747 0.5101 -0.0979 0.1085 -0.0452 57 LEU A O 424 C CB . LEU A 57 ? 0.5461 0.4877 0.5075 -0.1108 0.1012 -0.0587 57 LEU A CB 425 C CG . LEU A 57 ? 0.5404 0.4998 0.5101 -0.1132 0.0918 -0.0615 57 LEU A CG 426 C CD1 . LEU A 57 ? 0.5605 0.5249 0.5050 -0.1288 0.0905 -0.0681 57 LEU A CD1 427 C CD2 . LEU A 57 ? 0.5263 0.5089 0.5099 -0.1024 0.0769 -0.0551 57 LEU A CD2 428 N N . GLY A 58 ? 0.5412 0.4464 0.5228 -0.0988 0.1277 -0.0508 58 GLY A N 429 C CA . GLY A 58 ? 0.5546 0.4450 0.5305 -0.0986 0.1398 -0.0479 58 GLY A CA 430 C C . GLY A 58 ? 0.5415 0.4355 0.5314 -0.0915 0.1356 -0.0399 58 GLY A C 431 O O . GLY A 58 ? 0.5513 0.4347 0.5316 -0.0925 0.1431 -0.0365 58 GLY A O 432 N N . THR A 59 ? 0.5171 0.4237 0.5269 -0.0853 0.1242 -0.0371 59 THR A N 433 C CA . THR A 59 ? 0.5094 0.4153 0.5278 -0.0803 0.1199 -0.0304 59 THR A CA 434 C C . THR A 59 ? 0.5372 0.4395 0.5311 -0.0791 0.1137 -0.0264 59 THR A C 435 O O . THR A 59 ? 0.5441 0.4364 0.5348 -0.0772 0.1156 -0.0207 59 THR A O 436 C CB . THR A 59 ? 0.4858 0.4032 0.5266 -0.0744 0.1091 -0.0291 59 THR A CB 437 O OG1 . THR A 59 ? 0.4702 0.3989 0.5032 -0.0711 0.0962 -0.0303 59 THR A OG1 438 C CG2 . THR A 59 ? 0.4702 0.3932 0.5352 -0.0744 0.1143 -0.0317 59 THR A CG2 439 N N . ILE A 60 ? 0.5515 0.4621 0.5271 -0.0807 0.1068 -0.0288 60 ILE A N 440 C CA . ILE A 60 ? 0.5767 0.4889 0.5287 -0.0780 0.0997 -0.0238 60 ILE A CA 441 C C . ILE A 60 ? 0.6070 0.5059 0.5339 -0.0846 0.1094 -0.0234 60 ILE A C 442 O O . ILE A 60 ? 0.6350 0.5278 0.5447 -0.0810 0.1075 -0.0166 60 ILE A O 443 C CB . ILE A 60 ? 0.5804 0.5144 0.5252 -0.0772 0.0867 -0.0255 60 ILE A CB 444 C CG1 . ILE A 60 ? 0.5598 0.5069 0.5279 -0.0706 0.0780 -0.0261 60 ILE A CG1 445 C CG2 . ILE A 60 ? 0.6047 0.5452 0.5272 -0.0716 0.0783 -0.0183 60 ILE A CG2 446 C CD1 . ILE A 60 ? 0.5581 0.4985 0.5355 -0.0599 0.0742 -0.0196 60 ILE A CD1 447 N N . THR A 61 ? 0.6086 0.5007 0.5308 -0.0937 0.1204 -0.0303 61 THR A N 448 C CA . THR A 61 ? 0.6334 0.5118 0.5279 -0.1011 0.1304 -0.0314 61 THR A CA 449 C C . THR A 61 ? 0.6416 0.5010 0.5422 -0.1020 0.1476 -0.0301 61 THR A C 450 O O . THR A 61 ? 0.6612 0.5081 0.5422 -0.1040 0.1544 -0.0264 61 THR A O 451 C CB . THR A 61 ? 0.6474 0.5268 0.5247 -0.1121 0.1330 -0.0406 61 THR A CB 452 O OG1 . THR A 61 ? 0.6380 0.5120 0.5339 -0.1137 0.1418 -0.0469 61 THR A OG1 453 C CG2 . THR A 61 ? 0.6429 0.5455 0.5118 -0.1137 0.1159 -0.0411 61 THR A CG2 454 N N . GLY A 62 ? 0.6209 0.4803 0.5487 -0.1004 0.1547 -0.0325 62 GLY A N 455 C CA . GLY A 62 ? 0.6255 0.4750 0.5675 -0.0996 0.1695 -0.0296 62 GLY A CA 456 C C . GLY A 62 ? 0.6443 0.4802 0.5780 -0.1042 0.1887 -0.0341 62 GLY A C 457 O O . GLY A 62 ? 0.6751 0.4990 0.5974 -0.1064 0.2007 -0.0312 62 GLY A O 458 N N . PRO A 63 ? 0.6399 0.4755 0.5783 -0.1050 0.1931 -0.0409 63 PRO A N 459 C CA . PRO A 63 ? 0.6573 0.4775 0.5915 -0.1061 0.2139 -0.0444 63 PRO A CA 460 C C . PRO A 63 ? 0.6439 0.4714 0.6123 -0.0989 0.2234 -0.0383 63 PRO A C 461 O O . PRO A 63 ? 0.6200 0.4641 0.6150 -0.0947 0.2123 -0.0339 63 PRO A O 462 C CB . PRO A 63 ? 0.6540 0.4710 0.5845 -0.1079 0.2138 -0.0524 63 PRO A CB 463 C CG . PRO A 63 ? 0.6188 0.4562 0.5719 -0.1039 0.1956 -0.0505 63 PRO A CG 464 C CD . PRO A 63 ? 0.6168 0.4644 0.5654 -0.1038 0.1810 -0.0449 63 PRO A CD 465 N N . PRO A 64 ? 0.6721 0.4889 0.6397 -0.0976 0.2441 -0.0380 64 PRO A N 466 C CA . PRO A 64 ? 0.6625 0.4918 0.6626 -0.0920 0.2532 -0.0304 64 PRO A CA 467 C C . PRO A 64 ? 0.6281 0.4785 0.6658 -0.0850 0.2455 -0.0277 64 PRO A C 468 O O . PRO A 64 ? 0.6013 0.4690 0.6654 -0.0841 0.2410 -0.0211 64 PRO A O 469 C CB . PRO A 64 ? 0.6920 0.5070 0.6839 -0.0896 0.2780 -0.0318 64 PRO A CB 470 C CG . PRO A 64 ? 0.7265 0.5166 0.6744 -0.0968 0.2815 -0.0400 64 PRO A CG 471 C CD . PRO A 64 ? 0.7104 0.5044 0.6489 -0.1009 0.2607 -0.0448 64 PRO A CD 472 N N . GLN A 65 ? 0.6232 0.4713 0.6611 -0.0815 0.2438 -0.0328 65 GLN A N 473 C CA . GLN A 65 ? 0.5959 0.4628 0.6659 -0.0744 0.2361 -0.0302 65 GLN A CA 474 C C . GLN A 65 ? 0.5692 0.4517 0.6505 -0.0767 0.2136 -0.0283 65 GLN A C 475 O O . GLN A 65 ? 0.5428 0.4427 0.6514 -0.0720 0.2062 -0.0252 65 GLN A O 476 C CB . GLN A 65 ? 0.6016 0.4573 0.6635 -0.0707 0.2402 -0.0362 65 GLN A CB 477 C CG . GLN A 65 ? 0.6044 0.4506 0.6396 -0.0786 0.2270 -0.0439 65 GLN A CG 478 C CD . GLN A 65 ? 0.6437 0.4649 0.6390 -0.0869 0.2366 -0.0511 65 GLN A CD 479 O OE1 . GLN A 65 ? 0.6681 0.4777 0.6519 -0.0878 0.2511 -0.0503 65 GLN A OE1 480 N NE2 . GLN A 65 ? 0.6592 0.4728 0.6324 -0.0944 0.2286 -0.0585 65 GLN A NE2 481 N N . CYS A 66 ? 0.5782 0.4542 0.6371 -0.0830 0.2033 -0.0297 66 CYS A N 482 C CA . CYS A 66 ? 0.5656 0.4525 0.6311 -0.0836 0.1842 -0.0274 66 CYS A CA 483 C C . CYS A 66 ? 0.5664 0.4529 0.6332 -0.0868 0.1829 -0.0212 66 CYS A C 484 O O . CYS A 66 ? 0.5524 0.4409 0.6168 -0.0872 0.1691 -0.0194 66 CYS A O 485 C CB . CYS A 66 ? 0.5688 0.4510 0.6090 -0.0861 0.1718 -0.0324 66 CYS A CB 486 S SG . CYS A 66 ? 0.5669 0.4514 0.6070 -0.0851 0.1689 -0.0395 66 CYS A SG 487 N N . ASP A 67 ? 0.5886 0.4714 0.6585 -0.0889 0.1984 -0.0179 67 ASP A N 488 C CA . ASP A 67 ? 0.6047 0.4836 0.6719 -0.0941 0.1996 -0.0120 67 ASP A CA 489 C C . ASP A 67 ? 0.5828 0.4744 0.6735 -0.0954 0.1884 -0.0080 67 ASP A C 490 O O . ASP A 67 ? 0.5965 0.4791 0.6765 -0.0995 0.1826 -0.0048 67 ASP A O 491 C CB . ASP A 67 ? 0.6223 0.4983 0.6923 -0.0966 0.2200 -0.0089 67 ASP A CB 492 C CG . ASP A 67 ? 0.6570 0.5122 0.6920 -0.0986 0.2302 -0.0119 67 ASP A CG 493 O OD1 . ASP A 67 ? 0.6663 0.5106 0.6740 -0.1001 0.2197 -0.0144 67 ASP A OD1 494 O OD2 . ASP A 67 ? 0.6644 0.5153 0.6984 -0.0986 0.2490 -0.0114 67 ASP A OD2 495 N N . GLN A 68 ? 0.5653 0.4756 0.6848 -0.0921 0.1856 -0.0081 68 GLN A N 496 C CA . GLN A 68 ? 0.5577 0.4814 0.6988 -0.0948 0.1746 -0.0051 68 GLN A CA 497 C C . GLN A 68 ? 0.5399 0.4625 0.6754 -0.0912 0.1566 -0.0086 68 GLN A C 498 O O . GLN A 68 ? 0.5189 0.4506 0.6695 -0.0931 0.1469 -0.0073 68 GLN A O 499 C CB . GLN A 68 ? 0.5537 0.5024 0.7302 -0.0932 0.1805 -0.0021 68 GLN A CB 500 C CG . GLN A 68 ? 0.5707 0.5259 0.7576 -0.0954 0.1993 0.0026 68 GLN A CG 501 C CD . GLN A 68 ? 0.6065 0.5557 0.7880 -0.1068 0.2023 0.0068 68 GLN A CD 502 O OE1 . GLN A 68 ? 0.6385 0.5719 0.8004 -0.1094 0.2138 0.0077 68 GLN A OE1 503 N NE2 . GLN A 68 ? 0.6085 0.5682 0.8050 -0.1146 0.1923 0.0094 68 GLN A NE2 504 N N . PHE A 69 ? 0.5457 0.4581 0.6585 -0.0870 0.1522 -0.0128 69 PHE A N 505 C CA . PHE A 69 ? 0.5306 0.4445 0.6376 -0.0828 0.1363 -0.0157 69 PHE A CA 506 C C . PHE A 69 ? 0.5461 0.4457 0.6233 -0.0816 0.1297 -0.0154 69 PHE A C 507 O O . PHE A 69 ? 0.5546 0.4574 0.6238 -0.0768 0.1186 -0.0177 69 PHE A O 508 C CB . PHE A 69 ? 0.5127 0.4350 0.6245 -0.0782 0.1355 -0.0205 69 PHE A CB 509 C CG . PHE A 69 ? 0.5010 0.4378 0.6412 -0.0761 0.1412 -0.0194 69 PHE A CG 510 C CD1 . PHE A 69 ? 0.5083 0.4450 0.6548 -0.0756 0.1575 -0.0182 69 PHE A CD1 511 C CD2 . PHE A 69 ? 0.4814 0.4323 0.6413 -0.0735 0.1308 -0.0189 69 PHE A CD2 512 C CE1 . PHE A 69 ? 0.5004 0.4527 0.6738 -0.0712 0.1632 -0.0155 69 PHE A CE1 513 C CE2 . PHE A 69 ? 0.4741 0.4408 0.6600 -0.0705 0.1353 -0.0165 69 PHE A CE2 514 C CZ . PHE A 69 ? 0.4799 0.4483 0.6734 -0.0686 0.1515 -0.0142 69 PHE A CZ 515 N N . LEU A 70 ? 0.5649 0.4503 0.6258 -0.0852 0.1367 -0.0118 70 LEU A N 516 C CA . LEU A 70 ? 0.5854 0.4582 0.6162 -0.0825 0.1316 -0.0101 70 LEU A CA 517 C C . LEU A 70 ? 0.5900 0.4579 0.6157 -0.0774 0.1189 -0.0073 70 LEU A C 518 O O . LEU A 70 ? 0.5946 0.4596 0.6000 -0.0711 0.1113 -0.0059 70 LEU A O 519 C CB . LEU A 70 ? 0.6025 0.4593 0.6152 -0.0873 0.1434 -0.0060 70 LEU A CB 520 C CG . LEU A 70 ? 0.6118 0.4691 0.6233 -0.0915 0.1581 -0.0087 70 LEU A CG 521 C CD1 . LEU A 70 ? 0.6393 0.4801 0.6318 -0.0963 0.1698 -0.0041 70 LEU A CD1 522 C CD2 . LEU A 70 ? 0.6092 0.4703 0.6063 -0.0897 0.1556 -0.0146 70 LEU A CD2 523 N N . GLU A 71 ? 0.5913 0.4589 0.6342 -0.0800 0.1168 -0.0062 71 GLU A N 524 C CA . GLU A 71 ? 0.6117 0.4694 0.6472 -0.0756 0.1068 -0.0042 71 GLU A CA 525 C C . GLU A 71 ? 0.6044 0.4736 0.6635 -0.0767 0.0998 -0.0074 71 GLU A C 526 O O . GLU A 71 ? 0.6255 0.4834 0.6835 -0.0789 0.0962 -0.0061 71 GLU A O 527 C CB . GLU A 71 ? 0.6339 0.4671 0.6531 -0.0801 0.1124 0.0014 71 GLU A CB 528 C CG . GLU A 71 ? 0.6648 0.4833 0.6541 -0.0757 0.1160 0.0060 71 GLU A CG 529 C CD . GLU A 71 ? 0.7030 0.4924 0.6714 -0.0772 0.1196 0.0125 71 GLU A CD 530 O OE1 . GLU A 71 ? 0.7181 0.4988 0.6930 -0.0889 0.1290 0.0139 71 GLU A OE1 531 O OE2 . GLU A 71 ? 0.7155 0.4908 0.6610 -0.0665 0.1136 0.0166 71 GLU A OE2 532 N N . PHE A 72 ? 0.5979 0.4876 0.6755 -0.0752 0.0981 -0.0115 72 PHE A N 533 C CA . PHE A 72 ? 0.5803 0.4832 0.6810 -0.0765 0.0922 -0.0138 72 PHE A CA 534 C C . PHE A 72 ? 0.5864 0.4837 0.6791 -0.0706 0.0802 -0.0148 72 PHE A C 535 O O . PHE A 72 ? 0.6085 0.4967 0.6805 -0.0626 0.0759 -0.0138 72 PHE A O 536 C CB . PHE A 72 ? 0.5452 0.4681 0.6638 -0.0745 0.0938 -0.0172 72 PHE A CB 537 C CG . PHE A 72 ? 0.5389 0.4670 0.6479 -0.0672 0.0869 -0.0206 72 PHE A CG 538 C CD1 . PHE A 72 ? 0.5463 0.4711 0.6373 -0.0659 0.0905 -0.0215 72 PHE A CD1 539 C CD2 . PHE A 72 ? 0.5154 0.4532 0.6330 -0.0629 0.0770 -0.0228 72 PHE A CD2 540 C CE1 . PHE A 72 ? 0.5396 0.4728 0.6225 -0.0617 0.0838 -0.0246 72 PHE A CE1 541 C CE2 . PHE A 72 ? 0.5106 0.4558 0.6206 -0.0575 0.0713 -0.0257 72 PHE A CE2 542 C CZ . PHE A 72 ? 0.5294 0.4734 0.6227 -0.0574 0.0744 -0.0265 72 PHE A CZ 543 N N . SER A 73 ? 0.5644 0.4684 0.6737 -0.0743 0.0753 -0.0164 73 SER A N 544 C CA . SER A 73 ? 0.5592 0.4567 0.6617 -0.0697 0.0653 -0.0181 73 SER A CA 545 C C . SER A 73 ? 0.5178 0.4364 0.6431 -0.0703 0.0595 -0.0213 73 SER A C 546 O O . SER A 73 ? 0.5084 0.4405 0.6546 -0.0777 0.0629 -0.0206 73 SER A O 547 C CB . SER A 73 ? 0.5921 0.4669 0.6836 -0.0771 0.0661 -0.0164 73 SER A CB 548 O OG . SER A 73 ? 0.6216 0.4823 0.6981 -0.0706 0.0585 -0.0179 73 SER A OG 549 N N . ALA A 74 ? 0.4935 0.4168 0.6151 -0.0618 0.0513 -0.0238 74 ALA A N 550 C CA . ALA A 74 ? 0.4704 0.4140 0.6113 -0.0609 0.0466 -0.0263 74 ALA A CA 551 C C . ALA A 74 ? 0.4636 0.4086 0.5983 -0.0532 0.0372 -0.0290 74 ALA A C 552 O O . ALA A 74 ? 0.4792 0.4160 0.5960 -0.0449 0.0349 -0.0290 74 ALA A O 553 C CB . ALA A 74 ? 0.4572 0.4152 0.6072 -0.0588 0.0521 -0.0266 74 ALA A CB 554 N N . ASP A 75 ? 0.4339 0.3912 0.5838 -0.0555 0.0323 -0.0306 75 ASP A N 555 C CA . ASP A 75 ? 0.4262 0.3904 0.5745 -0.0484 0.0248 -0.0332 75 ASP A CA 556 C C . ASP A 75 ? 0.4012 0.3842 0.5618 -0.0453 0.0264 -0.0336 75 ASP A C 557 O O . ASP A 75 ? 0.3961 0.3847 0.5508 -0.0388 0.0231 -0.0352 75 ASP A O 558 C CB . ASP A 75 ? 0.4261 0.3919 0.5813 -0.0535 0.0183 -0.0347 75 ASP A CB 559 C CG . ASP A 75 ? 0.4621 0.4055 0.6025 -0.0595 0.0173 -0.0354 75 ASP A CG 560 O OD1 . ASP A 75 ? 0.4889 0.4121 0.6076 -0.0535 0.0186 -0.0355 75 ASP A OD1 561 O OD2 . ASP A 75 ? 0.4818 0.4278 0.6314 -0.0706 0.0154 -0.0355 75 ASP A OD2 562 N N . LEU A 76 ? 0.3886 0.3807 0.5656 -0.0501 0.0322 -0.0317 76 LEU A N 563 C CA . LEU A 76 ? 0.3820 0.3863 0.5686 -0.0476 0.0358 -0.0318 76 LEU A CA 564 C C . LEU A 76 ? 0.3902 0.3917 0.5777 -0.0500 0.0468 -0.0305 76 LEU A C 565 O O . LEU A 76 ? 0.4071 0.4071 0.6020 -0.0545 0.0520 -0.0279 76 LEU A O 566 C CB . LEU A 76 ? 0.3693 0.3872 0.5749 -0.0482 0.0331 -0.0300 76 LEU A CB 567 C CG . LEU A 76 ? 0.3650 0.3923 0.5804 -0.0445 0.0379 -0.0288 76 LEU A CG 568 C CD1 . LEU A 76 ? 0.3677 0.3944 0.5715 -0.0405 0.0345 -0.0322 76 LEU A CD1 569 C CD2 . LEU A 76 ? 0.3566 0.3984 0.5915 -0.0442 0.0353 -0.0247 76 LEU A CD2 570 N N . ILE A 77 ? 0.3829 0.3835 0.5612 -0.0480 0.0506 -0.0327 77 ILE A N 571 C CA . ILE A 77 ? 0.3901 0.3850 0.5642 -0.0507 0.0616 -0.0326 77 ILE A CA 572 C C . ILE A 77 ? 0.3888 0.3871 0.5688 -0.0495 0.0679 -0.0336 77 ILE A C 573 O O . ILE A 77 ? 0.3971 0.3985 0.5715 -0.0483 0.0639 -0.0362 77 ILE A O 574 C CB . ILE A 77 ? 0.4026 0.3903 0.5546 -0.0514 0.0612 -0.0348 77 ILE A CB 575 C CG1 . ILE A 77 ? 0.4110 0.3910 0.5540 -0.0505 0.0566 -0.0326 77 ILE A CG1 576 C CG2 . ILE A 77 ? 0.4180 0.3984 0.5621 -0.0554 0.0727 -0.0358 77 ILE A CG2 577 C CD1 . ILE A 77 ? 0.4208 0.3982 0.5428 -0.0477 0.0531 -0.0330 77 ILE A CD1 578 N N . ILE A 78 ? 0.3850 0.3818 0.5750 -0.0496 0.0789 -0.0311 78 ILE A N 579 C CA . ILE A 78 ? 0.3885 0.3837 0.5825 -0.0467 0.0874 -0.0310 78 ILE A CA 580 C C . ILE A 78 ? 0.4087 0.3889 0.5880 -0.0495 0.1009 -0.0335 78 ILE A C 581 O O . ILE A 78 ? 0.4087 0.3852 0.5904 -0.0502 0.1094 -0.0314 78 ILE A O 582 C CB . ILE A 78 ? 0.3894 0.3960 0.6076 -0.0414 0.0907 -0.0248 78 ILE A CB 583 C CG1 . ILE A 78 ? 0.3793 0.4009 0.6106 -0.0408 0.0771 -0.0225 78 ILE A CG1 584 C CG2 . ILE A 78 ? 0.3931 0.3951 0.6127 -0.0357 0.0994 -0.0237 78 ILE A CG2 585 C CD1 . ILE A 78 ? 0.3787 0.4170 0.6347 -0.0375 0.0786 -0.0156 78 ILE A CD1 586 N N . GLU A 79 ? 0.4221 0.3931 0.5846 -0.0523 0.1033 -0.0383 79 GLU A N 587 C CA . GLU A 79 ? 0.4435 0.3969 0.5877 -0.0566 0.1166 -0.0420 79 GLU A CA 588 C C . GLU A 79 ? 0.4522 0.3958 0.6025 -0.0509 0.1300 -0.0401 79 GLU A C 589 O O . GLU A 79 ? 0.4367 0.3849 0.5962 -0.0463 0.1268 -0.0381 79 GLU A O 590 C CB . GLU A 79 ? 0.4565 0.4052 0.5774 -0.0650 0.1124 -0.0486 79 GLU A CB 591 C CG . GLU A 79 ? 0.4542 0.4130 0.5661 -0.0687 0.1006 -0.0496 79 GLU A CG 592 C CD . GLU A 79 ? 0.4631 0.4227 0.5534 -0.0777 0.0970 -0.0553 79 GLU A CD 593 O OE1 . GLU A 79 ? 0.4408 0.4112 0.5335 -0.0783 0.0891 -0.0564 79 GLU A OE1 594 O OE2 . GLU A 79 ? 0.4998 0.4507 0.5704 -0.0850 0.1023 -0.0585 79 GLU A OE2 595 N N . ARG A 80 ? 0.4684 0.3972 0.6119 -0.0502 0.1456 -0.0401 80 ARG A N 596 C CA . ARG A 80 ? 0.4939 0.4098 0.6405 -0.0423 0.1614 -0.0375 80 ARG A CA 597 C C . ARG A 80 ? 0.5351 0.4213 0.6507 -0.0489 0.1752 -0.0447 80 ARG A C 598 O O . ARG A 80 ? 0.5440 0.4223 0.6391 -0.0589 0.1754 -0.0504 80 ARG A O 599 C CB . ARG A 80 ? 0.4873 0.4112 0.6541 -0.0336 0.1712 -0.0302 80 ARG A CB 600 C CG . ARG A 80 ? 0.4595 0.4126 0.6556 -0.0302 0.1585 -0.0234 80 ARG A CG 601 C CD . ARG A 80 ? 0.4456 0.4113 0.6575 -0.0233 0.1505 -0.0193 80 ARG A CD 602 N NE . ARG A 80 ? 0.4265 0.4198 0.6670 -0.0194 0.1418 -0.0118 80 ARG A NE 603 C CZ . ARG A 80 ? 0.4235 0.4326 0.6804 -0.0135 0.1336 -0.0069 80 ARG A CZ 604 N NH1 . ARG A 80 ? 0.4395 0.4381 0.6871 -0.0095 0.1338 -0.0080 80 ARG A NH1 605 N NH2 . ARG A 80 ? 0.4149 0.4500 0.6958 -0.0126 0.1252 -0.0008 80 ARG A NH2 606 N N . ARG A 81 ? 0.5654 0.4337 0.6757 -0.0434 0.1872 -0.0441 81 ARG A N 607 C CA . ARG A 81 ? 0.6246 0.4590 0.7018 -0.0507 0.2022 -0.0516 81 ARG A CA 608 C C . ARG A 81 ? 0.6456 0.4648 0.7090 -0.0523 0.2166 -0.0539 81 ARG A C 609 O O . ARG A 81 ? 0.6584 0.4567 0.6903 -0.0652 0.2217 -0.0625 81 ARG A O 610 C CB . ARG A 81 ? 0.6774 0.4907 0.7515 -0.0413 0.2158 -0.0488 81 ARG A CB 611 C CG . ARG A 81 ? 0.7433 0.5227 0.7805 -0.0541 0.2241 -0.0582 81 ARG A CG 612 C CD . ARG A 81 ? 0.7944 0.5494 0.8263 -0.0444 0.2374 -0.0548 81 ARG A CD 613 N NE . ARG A 81 ? 0.8490 0.5936 0.8621 -0.0578 0.2311 -0.0608 81 ARG A NE 614 C CZ . ARG A 81 ? 0.8461 0.6129 0.8760 -0.0566 0.2158 -0.0572 81 ARG A CZ 615 N NH1 . ARG A 81 ? 0.8427 0.6420 0.9073 -0.0430 0.2045 -0.0479 81 ARG A NH1 616 N NH2 . ARG A 81 ? 0.8721 0.6286 0.8829 -0.0702 0.2122 -0.0630 81 ARG A NH2 617 N N . GLU A 82 ? 0.6299 0.4614 0.7164 -0.0404 0.2229 -0.0461 82 GLU A N 618 C CA . GLU A 82 ? 0.6528 0.4717 0.7286 -0.0404 0.2382 -0.0471 82 GLU A CA 619 C C . GLU A 82 ? 0.6436 0.4720 0.7104 -0.0526 0.2277 -0.0509 82 GLU A C 620 O O . GLU A 82 ? 0.6600 0.4775 0.7145 -0.0546 0.2392 -0.0522 82 GLU A O 621 C CB . GLU A 82 ? 0.6557 0.4880 0.7610 -0.0235 0.2498 -0.0364 82 GLU A CB 622 C CG . GLU A 82 ? 0.6260 0.4975 0.7675 -0.0202 0.2350 -0.0283 82 GLU A CG 623 C CD . GLU A 82 ? 0.6146 0.5087 0.7826 -0.0123 0.2226 -0.0218 82 GLU A CD 624 O OE1 . GLU A 82 ? 0.6284 0.5089 0.7855 -0.0113 0.2215 -0.0243 82 GLU A OE1 625 O OE2 . GLU A 82 ? 0.5888 0.5137 0.7870 -0.0084 0.2138 -0.0143 82 GLU A OE2 626 N N . GLY A 83 ? 0.6169 0.4647 0.6887 -0.0596 0.2069 -0.0520 83 GLY A N 627 C CA . GLY A 83 ? 0.6120 0.4688 0.6750 -0.0686 0.1966 -0.0540 83 GLY A CA 628 C C . GLY A 83 ? 0.6440 0.4788 0.6692 -0.0813 0.2027 -0.0625 83 GLY A C 629 O O . GLY A 83 ? 0.6799 0.4980 0.6839 -0.0884 0.2059 -0.0692 83 GLY A O 630 N N . SER A 84 ? 0.6398 0.4740 0.6549 -0.0852 0.2044 -0.0624 84 SER A N 631 C CA . SER A 84 ? 0.6565 0.4743 0.6347 -0.0984 0.2070 -0.0699 84 SER A CA 632 C C . SER A 84 ? 0.6378 0.4725 0.6123 -0.1030 0.1925 -0.0677 84 SER A C 633 O O . SER A 84 ? 0.6323 0.4766 0.6233 -0.0966 0.1918 -0.0610 84 SER A O 634 C CB . SER A 84 ? 0.6992 0.4896 0.6588 -0.0980 0.2298 -0.0724 84 SER A CB 635 O OG . SER A 84 ? 0.7276 0.5019 0.6487 -0.1123 0.2317 -0.0802 84 SER A OG 636 N N . ASP A 85 ? 0.6327 0.4712 0.5849 -0.1141 0.1812 -0.0727 85 ASP A N 637 C CA . ASP A 85 ? 0.6209 0.4754 0.5652 -0.1174 0.1670 -0.0700 85 ASP A CA 638 C C . ASP A 85 ? 0.6495 0.4893 0.5669 -0.1233 0.1762 -0.0712 85 ASP A C 639 O O . ASP A 85 ? 0.6524 0.5024 0.5633 -0.1234 0.1672 -0.0669 85 ASP A O 640 C CB . ASP A 85 ? 0.6120 0.4812 0.5429 -0.1268 0.1517 -0.0741 85 ASP A CB 641 C CG . ASP A 85 ? 0.5841 0.4723 0.5405 -0.1207 0.1397 -0.0718 85 ASP A CG 642 O OD1 . ASP A 85 ? 0.5637 0.4624 0.5459 -0.1092 0.1349 -0.0651 85 ASP A OD1 643 O OD2 . ASP A 85 ? 0.5915 0.4845 0.5405 -0.1286 0.1348 -0.0768 85 ASP A OD2 644 N N . VAL A 86 ? 0.6726 0.4866 0.5718 -0.1276 0.1946 -0.0767 86 VAL A N 645 C CA . VAL A 86 ? 0.7085 0.5056 0.5755 -0.1356 0.2041 -0.0796 86 VAL A CA 646 C C . VAL A 86 ? 0.7312 0.5063 0.5993 -0.1292 0.2269 -0.0787 86 VAL A C 647 O O . VAL A 86 ? 0.7238 0.4931 0.6124 -0.1201 0.2377 -0.0775 86 VAL A O 648 C CB . VAL A 86 ? 0.7386 0.5221 0.5671 -0.1525 0.2048 -0.0901 86 VAL A CB 649 C CG1 . VAL A 86 ? 0.7240 0.5346 0.5473 -0.1604 0.1822 -0.0899 86 VAL A CG1 650 C CG2 . VAL A 86 ? 0.7523 0.5147 0.5778 -0.1548 0.2170 -0.0971 86 VAL A CG2 651 N N . CYS A 87 ? 0.7698 0.5343 0.6157 -0.1332 0.2344 -0.0784 87 CYS A N 652 C CA . CYS A 87 ? 0.8059 0.5461 0.6426 -0.1301 0.2584 -0.0795 87 CYS A CA 653 C C . CYS A 87 ? 0.8568 0.5708 0.6455 -0.1447 0.2665 -0.0897 87 CYS A C 654 O O . CYS A 87 ? 0.8884 0.5763 0.6612 -0.1471 0.2823 -0.0971 87 CYS A O 655 C CB . CYS A 87 ? 0.8088 0.5567 0.6590 -0.1232 0.2628 -0.0705 87 CYS A CB 656 S SG . CYS A 87 ? 0.8159 0.5746 0.6461 -0.1303 0.2469 -0.0662 87 CYS A SG 657 N N . TYR A 88 ? 0.8656 0.5855 0.6293 -0.1548 0.2557 -0.0900 88 TYR A N 658 C CA . TYR A 88 ? 0.9051 0.6056 0.6215 -0.1720 0.2586 -0.1002 88 TYR A CA 659 C C . TYR A 88 ? 0.9061 0.6145 0.6173 -0.1826 0.2451 -0.1070 88 TYR A C 660 O O . TYR A 88 ? 0.8804 0.6198 0.6134 -0.1803 0.2245 -0.1021 88 TYR A O 661 C CB . TYR A 88 ? 0.9145 0.6240 0.6065 -0.1792 0.2489 -0.0971 88 TYR A CB 662 C CG . TYR A 88 ? 0.9580 0.6450 0.5980 -0.1975 0.2554 -0.1074 88 TYR A CG 663 C CD1 . TYR A 88 ? 1.0016 0.6570 0.6149 -0.1990 0.2778 -0.1109 88 TYR A CD1 664 C CD2 . TYR A 88 ? 0.9649 0.6631 0.5817 -0.2141 0.2393 -0.1137 88 TYR A CD2 665 C CE1 . TYR A 88 ? 1.0493 0.6814 0.6113 -0.2170 0.2841 -0.1211 88 TYR A CE1 666 C CE2 . TYR A 88 ? 1.0093 0.6878 0.5767 -0.2334 0.2444 -0.1237 88 TYR A CE2 667 C CZ . TYR A 88 ? 1.0538 0.6975 0.5925 -0.2350 0.2668 -0.1278 88 TYR A CZ 668 O OH . TYR A 88 ? 1.0905 0.7122 0.5768 -0.2554 0.2720 -0.1384 88 TYR A OH 669 N N . PRO A 89 ? 0.9487 0.6279 0.6295 -0.1948 0.2575 -0.1184 89 PRO A N 670 C CA . PRO A 89 ? 0.9535 0.6380 0.6290 -0.2068 0.2468 -0.1252 89 PRO A CA 671 C C . PRO A 89 ? 0.9444 0.6651 0.6160 -0.2176 0.2207 -0.1235 89 PRO A C 672 O O . PRO A 89 ? 0.9605 0.6883 0.6087 -0.2251 0.2147 -0.1226 89 PRO A O 673 C CB . PRO A 89 ? 1.0049 0.6471 0.6339 -0.2231 0.2651 -0.1385 89 PRO A CB 674 C CG . PRO A 89 ? 1.0287 0.6408 0.6541 -0.2106 0.2903 -0.1371 89 PRO A CG 675 C CD . PRO A 89 ? 0.9991 0.6368 0.6464 -0.1988 0.2831 -0.1258 89 PRO A CD 676 N N . GLY A 90 ? 0.9246 0.6690 0.6191 -0.2173 0.2060 -0.1222 90 GLY A N 677 C CA . GLY A 90 ? 0.9130 0.6973 0.6110 -0.2237 0.1813 -0.1187 90 GLY A CA 678 C C . GLY A 90 ? 0.8812 0.6901 0.6156 -0.2155 0.1690 -0.1147 90 GLY A C 679 O O . GLY A 90 ? 0.8728 0.6685 0.6300 -0.2046 0.1786 -0.1139 90 GLY A O 680 N N . LYS A 91 ? 0.8739 0.7200 0.6133 -0.2201 0.1481 -0.1115 91 LYS A N 681 C CA . LYS A 91 ? 0.8610 0.7333 0.6341 -0.2116 0.1357 -0.1070 91 LYS A CA 682 C C . LYS A 91 ? 0.8354 0.7498 0.6205 -0.2052 0.1145 -0.0977 91 LYS A C 683 O O . LYS A 91 ? 0.8568 0.7804 0.6222 -0.2087 0.1091 -0.0950 91 LYS A O 684 C CB . LYS A 91 ? 0.8952 0.7645 0.6580 -0.2286 0.1358 -0.1161 91 LYS A CB 685 C CG . LYS A 91 ? 0.9382 0.8231 0.6684 -0.2525 0.1263 -0.1224 91 LYS A CG 686 C CD . LYS A 91 ? 0.9582 0.8661 0.6942 -0.2651 0.1158 -0.1258 91 LYS A CD 687 C CE . LYS A 91 ? 0.9848 0.8556 0.7118 -0.2745 0.1318 -0.1353 91 LYS A CE 688 N NZ . LYS A 91 ? 0.9612 0.8259 0.7243 -0.2538 0.1364 -0.1298 91 LYS A NZ 689 N N . PHE A 92 ? 0.7970 0.7354 0.6127 -0.1949 0.1036 -0.0926 92 PHE A N 690 C CA . PHE A 92 ? 0.7731 0.7516 0.6014 -0.1867 0.0844 -0.0836 92 PHE A CA 691 C C . PHE A 92 ? 0.7656 0.7755 0.5887 -0.2009 0.0717 -0.0868 92 PHE A C 692 O O . PHE A 92 ? 0.7718 0.7762 0.5990 -0.2099 0.0754 -0.0934 92 PHE A O 693 C CB . PHE A 92 ? 0.7354 0.7213 0.6001 -0.1656 0.0805 -0.0757 92 PHE A CB 694 C CG . PHE A 92 ? 0.7249 0.6969 0.5974 -0.1503 0.0854 -0.0684 92 PHE A CG 695 C CD1 . PHE A 92 ? 0.7361 0.6766 0.6123 -0.1476 0.1018 -0.0707 92 PHE A CD1 696 C CD2 . PHE A 92 ? 0.7127 0.7036 0.5894 -0.1381 0.0741 -0.0585 92 PHE A CD2 697 C CE1 . PHE A 92 ? 0.7266 0.6568 0.6111 -0.1355 0.1064 -0.0638 92 PHE A CE1 698 C CE2 . PHE A 92 ? 0.7167 0.6920 0.5985 -0.1260 0.0793 -0.0520 92 PHE A CE2 699 C CZ . PHE A 92 ? 0.7158 0.6619 0.6022 -0.1259 0.0952 -0.0549 92 PHE A CZ 700 N N . VAL A 93 ? 0.7725 0.8167 0.5871 -0.2022 0.0570 -0.0811 93 VAL A N 701 C CA . VAL A 93 ? 0.7600 0.8461 0.5775 -0.2115 0.0422 -0.0806 93 VAL A CA 702 C C . VAL A 93 ? 0.7295 0.8387 0.5824 -0.1910 0.0336 -0.0720 93 VAL A C 703 O O . VAL A 93 ? 0.7158 0.8229 0.5823 -0.1700 0.0320 -0.0630 93 VAL A O 704 C CB . VAL A 93 ? 0.7925 0.9113 0.5891 -0.2179 0.0293 -0.0757 93 VAL A CB 705 C CG1 . VAL A 93 ? 0.7774 0.9477 0.5817 -0.2256 0.0132 -0.0732 93 VAL A CG1 706 C CG2 . VAL A 93 ? 0.8293 0.9238 0.5870 -0.2396 0.0378 -0.0848 93 VAL A CG2 707 N N . ASN A 94 ? 0.7188 0.8478 0.5843 -0.1979 0.0289 -0.0750 94 ASN A N 708 C CA . ASN A 94 ? 0.6848 0.8320 0.5819 -0.1798 0.0226 -0.0684 94 ASN A CA 709 C C . ASN A 94 ? 0.6505 0.7617 0.5651 -0.1639 0.0334 -0.0678 94 ASN A C 710 O O . ASN A 94 ? 0.6202 0.7353 0.5524 -0.1434 0.0295 -0.0595 94 ASN A O 711 C CB . ASN A 94 ? 0.6896 0.8758 0.5949 -0.1631 0.0082 -0.0561 94 ASN A CB 712 C CG . ASN A 94 ? 0.7048 0.9407 0.6163 -0.1698 -0.0046 -0.0539 94 ASN A CG 713 O OD1 . ASN A 94 ? 0.7189 0.9754 0.6124 -0.1911 -0.0090 -0.0581 94 ASN A OD1 714 N ND2 . ASN A 94 ? 0.6929 0.9497 0.6296 -0.1523 -0.0103 -0.0471 94 ASN A ND2 715 N N . GLU A 95 ? 0.6433 0.7196 0.5518 -0.1735 0.0472 -0.0763 95 GLU A N 716 C CA . GLU A 95 ? 0.6292 0.6731 0.5519 -0.1601 0.0583 -0.0753 95 GLU A CA 717 C C . GLU A 95 ? 0.5873 0.6374 0.5395 -0.1463 0.0552 -0.0718 95 GLU A C 718 O O . GLU A 95 ? 0.5703 0.6113 0.5387 -0.1302 0.0565 -0.0664 95 GLU A O 719 C CB . GLU A 95 ? 0.6623 0.6676 0.5691 -0.1717 0.0753 -0.0841 95 GLU A CB 720 C CG . GLU A 95 ? 0.6826 0.6783 0.5853 -0.1854 0.0810 -0.0921 95 GLU A CG 721 C CD . GLU A 95 ? 0.7283 0.6804 0.6139 -0.1924 0.1002 -0.0994 95 GLU A CD 722 O OE1 . GLU A 95 ? 0.7666 0.7044 0.6214 -0.2081 0.1062 -0.1059 95 GLU A OE1 723 O OE2 . GLU A 95 ? 0.7396 0.6715 0.6417 -0.1813 0.1097 -0.0982 95 GLU A OE2 724 N N . GLU A 96 ? 0.5593 0.6242 0.5170 -0.1538 0.0515 -0.0749 96 GLU A N 725 C CA . GLU A 96 ? 0.5345 0.6020 0.5173 -0.1422 0.0500 -0.0724 96 GLU A CA 726 C C . GLU A 96 ? 0.5019 0.5967 0.5014 -0.1250 0.0376 -0.0637 96 GLU A C 727 O O . GLU A 96 ? 0.4675 0.5551 0.4854 -0.1108 0.0377 -0.0602 96 GLU A O 728 C CB . GLU A 96 ? 0.5306 0.6031 0.5125 -0.1555 0.0512 -0.0781 96 GLU A CB 729 C CG . GLU A 96 ? 0.5144 0.5781 0.5180 -0.1449 0.0539 -0.0765 96 GLU A CG 730 C CD . GLU A 96 ? 0.5145 0.5429 0.5233 -0.1370 0.0661 -0.0767 96 GLU A CD 731 O OE1 . GLU A 96 ? 0.5317 0.5364 0.5239 -0.1442 0.0765 -0.0807 96 GLU A OE1 732 O OE2 . GLU A 96 ? 0.5041 0.5300 0.5334 -0.1236 0.0655 -0.0728 96 GLU A OE2 733 N N . ALA A 97 ? 0.5025 0.6282 0.4944 -0.1264 0.0273 -0.0601 97 ALA A N 734 C CA . ALA A 97 ? 0.4927 0.6410 0.4960 -0.1077 0.0172 -0.0508 97 ALA A CA 735 C C . ALA A 97 ? 0.4924 0.6155 0.4983 -0.0926 0.0210 -0.0461 97 ALA A C 736 O O . ALA A 97 ? 0.4753 0.5953 0.4962 -0.0773 0.0190 -0.0416 97 ALA A O 737 C CB . ALA A 97 ? 0.5099 0.6942 0.5014 -0.1109 0.0071 -0.0465 97 ALA A CB 738 N N . LEU A 98 ? 0.5055 0.6093 0.4955 -0.0985 0.0273 -0.0474 98 LEU A N 739 C CA . LEU A 98 ? 0.5057 0.5855 0.4964 -0.0872 0.0321 -0.0430 98 LEU A CA 740 C C . LEU A 98 ? 0.4947 0.5514 0.5039 -0.0824 0.0395 -0.0451 98 LEU A C 741 O O . LEU A 98 ? 0.4846 0.5322 0.5034 -0.0698 0.0389 -0.0401 98 LEU A O 742 C CB . LEU A 98 ? 0.5291 0.5924 0.4983 -0.0964 0.0392 -0.0448 98 LEU A CB 743 C CG . LEU A 98 ? 0.5310 0.5704 0.4983 -0.0870 0.0452 -0.0398 98 LEU A CG 744 C CD1 . LEU A 98 ? 0.5278 0.5774 0.4979 -0.0702 0.0364 -0.0301 98 LEU A CD1 745 C CD2 . LEU A 98 ? 0.5556 0.5822 0.4984 -0.0971 0.0519 -0.0417 98 LEU A CD2 746 N N . ARG A 99 ? 0.4859 0.5330 0.4988 -0.0925 0.0466 -0.0519 99 ARG A N 747 C CA . ARG A 99 ? 0.4762 0.5066 0.5077 -0.0873 0.0526 -0.0528 99 ARG A CA 748 C C . ARG A 99 ? 0.4639 0.5083 0.5126 -0.0758 0.0437 -0.0490 99 ARG A C 749 O O . ARG A 99 ? 0.4744 0.5083 0.5360 -0.0667 0.0445 -0.0461 99 ARG A O 750 C CB . ARG A 99 ? 0.4778 0.4964 0.5083 -0.0982 0.0616 -0.0596 99 ARG A CB 751 C CG . ARG A 99 ? 0.4964 0.4917 0.5106 -0.1073 0.0744 -0.0637 99 ARG A CG 752 C CD . ARG A 99 ? 0.5001 0.4747 0.5183 -0.1108 0.0866 -0.0680 99 ARG A CD 753 N NE . ARG A 99 ? 0.5210 0.4717 0.5199 -0.1189 0.1004 -0.0723 99 ARG A NE 754 C CZ . ARG A 99 ? 0.5475 0.4910 0.5206 -0.1342 0.1044 -0.0791 99 ARG A CZ 755 N NH1 . ARG A 99 ? 0.5483 0.5101 0.5133 -0.1446 0.0952 -0.0822 99 ARG A NH1 756 N NH2 . ARG A 99 ? 0.5740 0.4921 0.5283 -0.1400 0.1182 -0.0830 99 ARG A NH2 757 N N . GLN A 100 ? 0.4542 0.5232 0.5021 -0.0768 0.0355 -0.0490 100 GLN A N 758 C CA . GLN A 100 ? 0.4359 0.5183 0.4981 -0.0657 0.0281 -0.0459 100 GLN A CA 759 C C . GLN A 100 ? 0.4348 0.5152 0.4972 -0.0507 0.0235 -0.0391 100 GLN A C 760 O O . GLN A 100 ? 0.4190 0.4923 0.4922 -0.0413 0.0221 -0.0374 100 GLN A O 761 C CB . GLN A 100 ? 0.4286 0.5406 0.4899 -0.0704 0.0215 -0.0469 100 GLN A CB 762 C CG . GLN A 100 ? 0.4272 0.5346 0.4897 -0.0843 0.0270 -0.0535 100 GLN A CG 763 C CD . GLN A 100 ? 0.4196 0.5553 0.4769 -0.0953 0.0222 -0.0556 100 GLN A CD 764 O OE1 . GLN A 100 ? 0.4151 0.5797 0.4697 -0.0922 0.0139 -0.0516 100 GLN A OE1 765 N NE2 . GLN A 100 ? 0.4243 0.5524 0.4800 -0.1083 0.0279 -0.0614 100 GLN A NE2 766 N N . ILE A 101 ? 0.4492 0.5333 0.4970 -0.0491 0.0218 -0.0354 101 ILE A N 767 C CA . ILE A 101 ? 0.4633 0.5395 0.5065 -0.0351 0.0194 -0.0284 101 ILE A CA 768 C C . ILE A 101 ? 0.4716 0.5172 0.5201 -0.0340 0.0264 -0.0287 101 ILE A C 769 O O . ILE A 101 ? 0.4881 0.5234 0.5412 -0.0241 0.0248 -0.0258 101 ILE A O 770 C CB . ILE A 101 ? 0.4837 0.5680 0.5078 -0.0345 0.0172 -0.0236 101 ILE A CB 771 C CG1 . ILE A 101 ? 0.4840 0.6053 0.5053 -0.0318 0.0080 -0.0205 101 ILE A CG1 772 C CG2 . ILE A 101 ? 0.4986 0.5642 0.5144 -0.0214 0.0180 -0.0163 101 ILE A CG2 773 C CD1 . ILE A 101 ? 0.5024 0.6387 0.5052 -0.0352 0.0047 -0.0165 101 ILE A CD1 774 N N . LEU A 102 ? 0.4754 0.5070 0.5227 -0.0448 0.0347 -0.0325 102 LEU A N 775 C CA . LEU A 102 ? 0.4688 0.4766 0.5224 -0.0450 0.0420 -0.0320 102 LEU A CA 776 C C . LEU A 102 ? 0.4519 0.4562 0.5257 -0.0442 0.0426 -0.0344 102 LEU A C 777 O O . LEU A 102 ? 0.4434 0.4347 0.5245 -0.0414 0.0443 -0.0324 102 LEU A O 778 C CB . LEU A 102 ? 0.4783 0.4742 0.5241 -0.0551 0.0521 -0.0345 102 LEU A CB 779 C CG . LEU A 102 ? 0.4986 0.4947 0.5221 -0.0563 0.0519 -0.0316 102 LEU A CG 780 C CD1 . LEU A 102 ? 0.5075 0.4909 0.5210 -0.0674 0.0628 -0.0354 102 LEU A CD1 781 C CD2 . LEU A 102 ? 0.5150 0.4998 0.5320 -0.0464 0.0502 -0.0243 102 LEU A CD2 782 N N . ARG A 103 ? 0.4442 0.4607 0.5259 -0.0474 0.0410 -0.0382 103 ARG A N 783 C CA . ARG A 103 ? 0.4350 0.4499 0.5344 -0.0458 0.0407 -0.0395 103 ARG A CA 784 C C . ARG A 103 ? 0.4362 0.4512 0.5398 -0.0362 0.0333 -0.0367 103 ARG A C 785 O O . ARG A 103 ? 0.4374 0.4442 0.5523 -0.0355 0.0337 -0.0364 103 ARG A O 786 C CB . ARG A 103 ? 0.4261 0.4522 0.5300 -0.0506 0.0406 -0.0435 103 ARG A CB 787 C CG . ARG A 103 ? 0.4377 0.4543 0.5391 -0.0601 0.0508 -0.0470 103 ARG A CG 788 C CD . ARG A 103 ? 0.4287 0.4492 0.5352 -0.0641 0.0524 -0.0503 103 ARG A CD 789 N NE . ARG A 103 ? 0.4376 0.4470 0.5330 -0.0741 0.0624 -0.0545 103 ARG A NE 790 C CZ . ARG A 103 ? 0.4549 0.4699 0.5351 -0.0841 0.0624 -0.0587 103 ARG A CZ 791 N NH1 . ARG A 103 ? 0.4480 0.4850 0.5251 -0.0850 0.0523 -0.0585 103 ARG A NH1 792 N NH2 . ARG A 103 ? 0.4817 0.4801 0.5488 -0.0939 0.0732 -0.0631 103 ARG A NH2 793 N N . GLU A 104 ? 0.4499 0.4741 0.5433 -0.0288 0.0270 -0.0343 104 GLU A N 794 C CA . GLU A 104 ? 0.4676 0.4879 0.5607 -0.0183 0.0216 -0.0319 104 GLU A CA 795 C C . GLU A 104 ? 0.4567 0.4603 0.5360 -0.0117 0.0222 -0.0273 104 GLU A C 796 O O . GLU A 104 ? 0.4587 0.4549 0.5320 -0.0020 0.0190 -0.0250 104 GLU A O 797 C CB . GLU A 104 ? 0.4940 0.5356 0.5861 -0.0114 0.0153 -0.0317 104 GLU A CB 798 C CG . GLU A 104 ? 0.5406 0.6000 0.6210 -0.0084 0.0128 -0.0285 104 GLU A CG 799 C CD . GLU A 104 ? 0.5868 0.6699 0.6677 0.0011 0.0068 -0.0265 104 GLU A CD 800 O OE1 . GLU A 104 ? 0.5965 0.6834 0.6869 0.0022 0.0054 -0.0291 104 GLU A OE1 801 O OE2 . GLU A 104 ? 0.5962 0.6956 0.6677 0.0079 0.0037 -0.0216 104 GLU A OE2 802 N N . SER A 105 ? 0.4512 0.4457 0.5234 -0.0170 0.0275 -0.0258 105 SER A N 803 C CA . SER A 105 ? 0.4637 0.4404 0.5201 -0.0116 0.0293 -0.0206 105 SER A CA 804 C C . SER A 105 ? 0.4703 0.4225 0.5276 -0.0117 0.0314 -0.0201 105 SER A C 805 O O . SER A 105 ? 0.4989 0.4328 0.5402 -0.0050 0.0322 -0.0157 105 SER A O 806 C CB . SER A 105 ? 0.4677 0.4398 0.5166 -0.0194 0.0356 -0.0197 105 SER A CB 807 O OG . SER A 105 ? 0.4386 0.4022 0.5003 -0.0300 0.0426 -0.0231 105 SER A OG 808 N N . GLY A 106 ? 0.4529 0.4044 0.5272 -0.0199 0.0327 -0.0241 106 GLY A N 809 C CA . GLY A 106 ? 0.4704 0.4020 0.5468 -0.0252 0.0353 -0.0238 106 GLY A CA 810 C C . GLY A 106 ? 0.4808 0.4012 0.5548 -0.0334 0.0435 -0.0216 106 GLY A C 811 O O . GLY A 106 ? 0.4889 0.3921 0.5614 -0.0391 0.0466 -0.0204 106 GLY A O 812 N N . GLY A 107 ? 0.4750 0.4050 0.5475 -0.0352 0.0474 -0.0213 107 GLY A N 813 C CA . GLY A 107 ? 0.4962 0.4160 0.5631 -0.0417 0.0562 -0.0191 107 GLY A CA 814 C C . GLY A 107 ? 0.5177 0.4254 0.5598 -0.0359 0.0571 -0.0141 107 GLY A C 815 O O . GLY A 107 ? 0.5190 0.4285 0.5484 -0.0252 0.0507 -0.0116 107 GLY A O 816 N N . ILE A 108 ? 0.5385 0.4342 0.5735 -0.0422 0.0655 -0.0116 108 ILE A N 817 C CA . ILE A 108 ? 0.5679 0.4535 0.5783 -0.0377 0.0675 -0.0064 108 ILE A CA 818 C C . ILE A 108 ? 0.6049 0.4641 0.6036 -0.0417 0.0751 -0.0017 108 ILE A C 819 O O . ILE A 108 ? 0.5895 0.4435 0.6010 -0.0523 0.0821 -0.0031 108 ILE A O 820 C CB . ILE A 108 ? 0.5678 0.4660 0.5739 -0.0424 0.0713 -0.0081 108 ILE A CB 821 C CG1 . ILE A 108 ? 0.5654 0.4611 0.5855 -0.0539 0.0821 -0.0113 108 ILE A CG1 822 C CG2 . ILE A 108 ? 0.5539 0.4764 0.5655 -0.0396 0.0636 -0.0121 108 ILE A CG2 823 C CD1 . ILE A 108 ? 0.5764 0.4818 0.5935 -0.0591 0.0872 -0.0152 108 ILE A CD1 824 N N . ASP A 109 ? 0.6491 0.4931 0.6229 -0.0327 0.0740 0.0047 109 ASP A N 825 C CA . ASP A 109 ? 0.7088 0.5245 0.6642 -0.0354 0.0818 0.0105 109 ASP A CA 826 C C . ASP A 109 ? 0.7283 0.5461 0.6630 -0.0316 0.0840 0.0154 109 ASP A C 827 O O . ASP A 109 ? 0.7393 0.5741 0.6662 -0.0217 0.0764 0.0171 109 ASP A O 828 C CB . ASP A 109 ? 0.7593 0.5506 0.6991 -0.0261 0.0789 0.0146 109 ASP A CB 829 C CG . ASP A 109 ? 0.8249 0.5845 0.7365 -0.0238 0.0860 0.0227 109 ASP A CG 830 O OD1 . ASP A 109 ? 0.8954 0.6434 0.8060 -0.0364 0.0953 0.0235 109 ASP A OD1 831 O OD2 . ASP A 109 ? 0.8722 0.6177 0.7617 -0.0086 0.0830 0.0290 109 ASP A OD2 832 N N . LYS A 110 ? 0.7265 0.5295 0.6524 -0.0402 0.0943 0.0180 110 LYS A N 833 C CA . LYS A 110 ? 0.7414 0.5465 0.6472 -0.0393 0.0974 0.0217 110 LYS A CA 834 C C . LYS A 110 ? 0.7830 0.5596 0.6590 -0.0334 0.1015 0.0316 110 LYS A C 835 O O . LYS A 110 ? 0.7988 0.5493 0.6716 -0.0369 0.1073 0.0340 110 LYS A O 836 C CB . LYS A 110 ? 0.7274 0.5377 0.6434 -0.0532 0.1078 0.0170 110 LYS A CB 837 C CG . LYS A 110 ? 0.6904 0.5266 0.6289 -0.0574 0.1053 0.0083 110 LYS A CG 838 C CD . LYS A 110 ? 0.6860 0.5371 0.6099 -0.0568 0.1026 0.0065 110 LYS A CD 839 C CE . LYS A 110 ? 0.6589 0.5308 0.6018 -0.0614 0.1006 -0.0022 110 LYS A CE 840 N NZ . LYS A 110 ? 0.6485 0.5169 0.6090 -0.0706 0.1127 -0.0069 110 LYS A NZ 841 N N . GLU A 111 ? 0.8070 0.5886 0.6600 -0.0253 0.0986 0.0375 111 GLU A N 842 C CA . GLU A 111 ? 0.8531 0.6080 0.6747 -0.0177 0.1026 0.0484 111 GLU A CA 843 C C . GLU A 111 ? 0.8612 0.6254 0.6614 -0.0174 0.1032 0.0526 111 GLU A C 844 O O . GLU A 111 ? 0.8477 0.6418 0.6506 -0.0154 0.0949 0.0498 111 GLU A O 845 C CB . GLU A 111 ? 0.8794 0.6271 0.6892 0.0011 0.0945 0.0553 111 GLU A CB 846 C CG . GLU A 111 ? 0.9302 0.6410 0.7077 0.0106 0.1004 0.0671 111 GLU A CG 847 C CD . GLU A 111 ? 0.9509 0.6523 0.7170 0.0314 0.0941 0.0738 111 GLU A CD 848 O OE1 . GLU A 111 ? 0.9352 0.6403 0.7196 0.0325 0.0902 0.0675 111 GLU A OE1 849 O OE2 . GLU A 111 ? 0.9880 0.6784 0.7259 0.0476 0.0937 0.0858 111 GLU A OE2 850 N N . ALA A 112 ? 0.9001 0.6382 0.6775 -0.0206 0.1132 0.0593 112 ALA A N 851 C CA . ALA A 112 ? 0.9231 0.6658 0.6756 -0.0212 0.1150 0.0640 112 ALA A CA 852 C C . ALA A 112 ? 0.9379 0.6998 0.6723 -0.0045 0.1019 0.0719 112 ALA A C 853 O O . ALA A 112 ? 0.9349 0.6892 0.6623 0.0119 0.0964 0.0797 112 ALA A O 854 C CB . ALA A 112 ? 0.9557 0.6629 0.6843 -0.0252 0.1280 0.0718 112 ALA A CB 855 N N . MET A 113 ? 0.9510 0.7385 0.6774 -0.0090 0.0974 0.0698 113 MET A N 856 C CA . MET A 113 ? 0.9675 0.7815 0.6776 0.0042 0.0842 0.0774 113 MET A CA 857 C C . MET A 113 ? 0.9998 0.7935 0.6737 0.0148 0.0869 0.0922 113 MET A C 858 O O . MET A 113 ? 1.0162 0.8192 0.6759 0.0337 0.0779 0.1038 113 MET A O 859 C CB . MET A 113 ? 0.9739 0.8214 0.6851 -0.0083 0.0786 0.0692 113 MET A CB 860 C CG . MET A 113 ? 0.9414 0.8075 0.6843 -0.0200 0.0771 0.0547 113 MET A CG 861 S SD . MET A 113 ? 0.9388 0.8475 0.7000 -0.0109 0.0597 0.0533 113 MET A SD 862 C CE . MET A 113 ? 0.9568 0.8963 0.6884 -0.0055 0.0478 0.0629 113 MET A CE 863 N N . GLY A 114 ? 1.0029 0.7698 0.6613 0.0034 0.0999 0.0924 114 GLY A N 864 C CA . GLY A 114 ? 1.0440 0.7866 0.6660 0.0116 0.1047 0.1064 114 GLY A CA 865 C C . GLY A 114 ? 1.0641 0.8238 0.6596 0.0073 0.1017 0.1095 114 GLY A C 866 O O . GLY A 114 ? 1.1032 0.8493 0.6661 0.0173 0.1024 0.1231 114 GLY A O 867 N N . PHE A 115 ? 1.1677 0.7229 0.8164 -0.1474 -0.1930 0.0841 115 PHE A N 868 C CA . PHE A 115 ? 1.1974 0.7502 0.8059 -0.1544 -0.1996 0.0892 115 PHE A CA 869 C C . PHE A 115 ? 1.2475 0.7698 0.7994 -0.1775 -0.1874 0.1105 115 PHE A C 870 O O . PHE A 115 ? 1.2341 0.7627 0.7851 -0.1920 -0.1582 0.1126 115 PHE A O 871 C CB . PHE A 115 ? 1.1527 0.7480 0.7772 -0.1559 -0.1817 0.0692 115 PHE A CB 872 C CG . PHE A 115 ? 1.1162 0.7454 0.7898 -0.1373 -0.1939 0.0486 115 PHE A CG 873 C CD1 . PHE A 115 ? 1.1286 0.7528 0.8235 -0.1177 -0.2248 0.0475 115 PHE A CD1 874 C CD2 . PHE A 115 ? 1.0718 0.7380 0.7706 -0.1395 -0.1734 0.0300 115 PHE A CD2 875 C CE1 . PHE A 115 ? 1.0957 0.7579 0.8384 -0.1016 -0.2330 0.0270 115 PHE A CE1 876 C CE2 . PHE A 115 ? 1.0427 0.7426 0.7854 -0.1262 -0.1819 0.0114 115 PHE A CE2 877 C CZ . PHE A 115 ? 1.0555 0.7570 0.8216 -0.1076 -0.2109 0.0092 115 PHE A CZ 878 N N . THR A 116 ? 1.3092 0.8013 0.8144 -0.1804 -0.2105 0.1263 116 THR A N 879 C CA . THR A 116 ? 1.3640 0.8289 0.8068 -0.2038 -0.2001 0.1462 116 THR A CA 880 C C . THR A 116 ? 1.3943 0.8668 0.7996 -0.2070 -0.2091 0.1426 116 THR A C 881 O O . THR A 116 ? 1.3988 0.8812 0.8174 -0.1906 -0.2370 0.1345 116 THR A O 882 C CB . THR A 116 ? 1.4299 0.8408 0.8388 -0.2082 -0.2218 0.1732 116 THR A CB 883 O OG1 . THR A 116 ? 1.4561 0.8508 0.8691 -0.1862 -0.2626 0.1757 116 THR A OG1 884 C CG2 . THR A 116 ? 1.4107 0.8107 0.8506 -0.2108 -0.2105 0.1762 116 THR A CG2 885 N N . TYR A 117 ? 1.4165 0.8865 0.7753 -0.2284 -0.1857 0.1475 117 TYR A N 886 C CA . TYR A 117 ? 1.4389 0.9200 0.7622 -0.2340 -0.1880 0.1385 117 TYR A CA 887 C C . TYR A 117 ? 1.5221 0.9692 0.7666 -0.2539 -0.1919 0.1599 117 TYR A C 888 O O . TYR A 117 ? 1.5411 0.9683 0.7577 -0.2712 -0.1721 0.1765 117 TYR A O 889 C CB . TYR A 117 ? 1.3853 0.9022 0.7288 -0.2391 -0.1515 0.1153 117 TYR A CB 890 C CG . TYR A 117 ? 1.3075 0.8575 0.7216 -0.2214 -0.1484 0.0949 117 TYR A CG 891 C CD1 . TYR A 117 ? 1.2879 0.8582 0.7275 -0.2080 -0.1706 0.0793 117 TYR A CD1 892 C CD2 . TYR A 117 ? 1.2582 0.8215 0.7130 -0.2194 -0.1240 0.0917 117 TYR A CD2 893 C CE1 . TYR A 117 ? 1.2260 0.8273 0.7272 -0.1942 -0.1661 0.0613 117 TYR A CE1 894 C CE2 . TYR A 117 ? 1.1900 0.7822 0.7036 -0.2045 -0.1213 0.0743 117 TYR A CE2 895 C CZ . TYR A 117 ? 1.1786 0.7888 0.7139 -0.1925 -0.1413 0.0595 117 TYR A CZ 896 O OH . TYR A 117 ? 1.1259 0.7657 0.7166 -0.1801 -0.1370 0.0428 117 TYR A OH 897 N N . SER A 118 ? 1.5701 1.0131 0.7787 -0.2527 -0.2178 0.1594 118 SER A N 898 C CA . SER A 118 ? 1.6661 1.0791 0.7929 -0.2722 -0.2232 0.1781 118 SER A CA 899 C C . SER A 118 ? 1.6890 1.1211 0.7845 -0.2780 -0.2258 0.1601 118 SER A C 900 O O . SER A 118 ? 1.6791 1.1330 0.8038 -0.2631 -0.2507 0.1449 118 SER A O 901 C CB . SER A 118 ? 1.7278 1.0980 0.8250 -0.2659 -0.2651 0.2069 118 SER A CB 902 O OG . SER A 118 ? 1.7185 1.1014 0.8459 -0.2420 -0.3048 0.1988 118 SER A OG 903 N N . GLY A 119 ? 1.7277 1.1531 0.7646 -0.3006 -0.1991 0.1603 119 GLY A N 904 C CA . GLY A 119 ? 1.7559 1.1936 0.7529 -0.3099 -0.1986 0.1421 119 GLY A CA 905 C C . GLY A 119 ? 1.7009 1.1727 0.7353 -0.3088 -0.1655 0.1089 119 GLY A C 906 O O . GLY A 119 ? 1.7122 1.1957 0.7279 -0.3132 -0.1696 0.0888 119 GLY A O 907 N N . ILE A 120 ? 1.6438 1.1293 0.7286 -0.3036 -0.1340 0.1036 120 ILE A N 908 C CA . ILE A 120 ? 1.5902 1.1038 0.7140 -0.2999 -0.1022 0.0752 120 ILE A CA 909 C C . ILE A 120 ? 1.5566 1.0776 0.7051 -0.3019 -0.0616 0.0774 120 ILE A C 910 O O . ILE A 120 ? 1.5541 1.0623 0.6978 -0.3067 -0.0593 0.0996 120 ILE A O 911 C CB . ILE A 120 ? 1.5311 1.0696 0.7245 -0.2806 -0.1201 0.0592 120 ILE A CB 912 C CG1 . ILE A 120 ? 1.5042 1.0408 0.7431 -0.2653 -0.1407 0.0762 120 ILE A CG1 913 C CG2 . ILE A 120 ? 1.5542 1.0990 0.7309 -0.2811 -0.1511 0.0469 120 ILE A CG2 914 C CD1 . ILE A 120 ? 1.4325 0.9985 0.7455 -0.2472 -0.1455 0.0594 120 ILE A CD1 915 N N . ARG A 121 ? 1.5343 1.0759 0.7098 -0.2983 -0.0309 0.0542 121 ARG A N 916 C CA . ARG A 121 ? 1.5133 1.0698 0.7219 -0.2962 0.0063 0.0532 121 ARG A CA 917 C C . ARG A 121 ? 1.4360 1.0124 0.7208 -0.2775 0.0012 0.0483 121 ARG A C 918 O O . ARG A 121 ? 1.4188 1.0016 0.7292 -0.2674 -0.0210 0.0377 121 ARG A O 919 C CB . ARG A 121 ? 1.5412 1.1054 0.7316 -0.3006 0.0426 0.0310 121 ARG A CB 920 C CG . ARG A 121 ? 1.5633 1.1372 0.7495 -0.3070 0.0819 0.0358 121 ARG A CG 921 C CD . ARG A 121 ? 1.6431 1.2071 0.7609 -0.3232 0.1046 0.0284 121 ARG A CD 922 N NE . ARG A 121 ? 1.6504 1.2236 0.7737 -0.3163 0.1354 -0.0002 121 ARG A NE 923 C CZ . ARG A 121 ? 1.6830 1.2433 0.7799 -0.3168 0.1303 -0.0226 121 ARG A CZ 924 N NH1 . ARG A 121 ? 1.7125 1.2565 0.7782 -0.3240 0.0943 -0.0205 121 ARG A NH1 925 N NH2 . ARG A 121 ? 1.6873 1.2507 0.7903 -0.3097 0.1609 -0.0479 121 ARG A NH2 926 N N . THR A 122 ? 1.3962 0.9850 0.7165 -0.2744 0.0212 0.0558 122 THR A N 927 C CA . THR A 122 ? 1.3237 0.9310 0.7116 -0.2581 0.0165 0.0525 122 THR A CA 928 C C . THR A 122 ? 1.2900 0.9213 0.7164 -0.2527 0.0507 0.0456 122 THR A C 929 O O . THR A 122 ? 1.2343 0.8813 0.7123 -0.2412 0.0484 0.0451 122 THR A O 930 C CB . THR A 122 ? 1.3198 0.9161 0.7226 -0.2564 -0.0084 0.0729 122 THR A CB 931 O OG1 . THR A 122 ? 1.3260 0.9162 0.7128 -0.2699 0.0085 0.0903 122 THR A OG1 932 C CG2 . THR A 122 ? 1.3615 0.9338 0.7317 -0.2571 -0.0459 0.0819 122 THR A CG2 933 N N . ASN A 123 ? 1.3280 0.9636 0.7296 -0.2598 0.0818 0.0395 123 ASN A N 934 C CA . ASN A 123 ? 1.3107 0.9714 0.7461 -0.2546 0.1141 0.0365 123 ASN A CA 935 C C . ASN A 123 ? 1.2759 0.9446 0.7187 -0.2441 0.1386 0.0139 123 ASN A C 936 O O . ASN A 123 ? 1.2702 0.9550 0.7192 -0.2418 0.1698 0.0094 123 ASN A O 937 C CB . ASN A 123 ? 1.4037 1.0674 0.8105 -0.2711 0.1338 0.0508 123 ASN A CB 938 C CG . ASN A 123 ? 1.5290 1.1747 0.8678 -0.2857 0.1427 0.0475 123 ASN A CG 939 O OD1 . ASN A 123 ? 1.5302 1.1636 0.8458 -0.2823 0.1387 0.0310 123 ASN A OD1 940 N ND2 . ASN A 123 ? 1.6753 1.3193 0.9797 -0.3044 0.1551 0.0631 123 ASN A ND2 941 N N . GLY A 124 ? 1.2431 0.9007 0.6866 -0.2378 0.1246 -0.0007 124 GLY A N 942 C CA . GLY A 124 ? 1.2267 0.8822 0.6726 -0.2294 0.1455 -0.0224 124 GLY A CA 943 C C . GLY A 124 ? 1.1647 0.8410 0.6655 -0.2124 0.1632 -0.0248 124 GLY A C 944 O O . GLY A 124 ? 1.1139 0.8032 0.6564 -0.2055 0.1488 -0.0162 124 GLY A O 945 N N . THR A 125 ? 1.1612 0.8403 0.6606 -0.2048 0.1941 -0.0368 125 THR A N 946 C CA . THR A 125 ? 1.1158 0.8146 0.6648 -0.1863 0.2115 -0.0383 125 THR A CA 947 C C . THR A 125 ? 1.1251 0.8054 0.6710 -0.1742 0.2288 -0.0589 125 THR A C 948 O O . THR A 125 ? 1.1586 0.8111 0.6668 -0.1821 0.2248 -0.0731 125 THR A O 949 C CB . THR A 125 ? 1.1107 0.8391 0.6733 -0.1849 0.2348 -0.0290 125 THR A CB 950 O OG1 . THR A 125 ? 1.1573 0.8799 0.6818 -0.1884 0.2611 -0.0409 125 THR A OG1 951 C CG2 . THR A 125 ? 1.0970 0.8371 0.6589 -0.2002 0.2183 -0.0082 125 THR A CG2 952 N N . THR A 126 ? 1.0978 0.7919 0.6828 -0.1551 0.2462 -0.0601 126 THR A N 953 C CA . THR A 126 ? 1.1140 0.7856 0.6984 -0.1406 0.2637 -0.0778 126 THR A CA 954 C C . THR A 126 ? 1.0943 0.7887 0.7220 -0.1173 0.2843 -0.0746 126 THR A C 955 O O . THR A 126 ? 1.0591 0.7879 0.7242 -0.1132 0.2793 -0.0583 126 THR A O 956 C CB . THR A 126 ? 1.1037 0.7500 0.6927 -0.1422 0.2441 -0.0832 126 THR A CB 957 O OG1 . THR A 126 ? 1.1201 0.7448 0.7190 -0.1258 0.2607 -0.0949 126 THR A OG1 958 C CG2 . THR A 126 ? 1.0486 0.7173 0.6766 -0.1421 0.2210 -0.0661 126 THR A CG2 959 N N . SER A 127 ? 1.1322 0.8062 0.7548 -0.1014 0.3063 -0.0906 127 SER A N 960 C CA . SER A 127 ? 1.1250 0.8183 0.7887 -0.0748 0.3254 -0.0888 127 SER A CA 961 C C . SER A 127 ? 1.0886 0.7812 0.7916 -0.0619 0.3103 -0.0777 127 SER A C 962 O O . SER A 127 ? 1.0752 0.7955 0.8191 -0.0423 0.3171 -0.0686 127 SER A O 963 C CB . SER A 127 ? 1.1783 0.8440 0.8221 -0.0591 0.3535 -0.1109 127 SER A CB 964 O OG . SER A 127 ? 1.2057 0.8181 0.8200 -0.0633 0.3471 -0.1254 127 SER A OG 965 N N . ALA A 128 ? 1.0804 0.7444 0.7709 -0.0736 0.2899 -0.0784 128 ALA A N 966 C CA . ALA A 128 ? 1.0488 0.7111 0.7703 -0.0654 0.2759 -0.0678 128 ALA A CA 967 C C . ALA A 128 ? 0.9989 0.7051 0.7556 -0.0680 0.2593 -0.0480 128 ALA A C 968 O O . ALA A 128 ? 0.9669 0.6832 0.7545 -0.0562 0.2530 -0.0375 128 ALA A O 969 C CB . ALA A 128 ? 1.0572 0.6816 0.7558 -0.0805 0.2609 -0.0755 128 ALA A CB 970 N N . CYS A 129 ? 0.9937 0.7224 0.7426 -0.0841 0.2514 -0.0428 129 CYS A N 971 C CA . CYS A 129 ? 0.9559 0.7225 0.7356 -0.0879 0.2367 -0.0259 129 CYS A CA 972 C C . CYS A 129 ? 0.9710 0.7745 0.7659 -0.0842 0.2526 -0.0201 129 CYS A C 973 O O . CYS A 129 ? 0.9922 0.8019 0.7654 -0.0996 0.2556 -0.0197 129 CYS A O 974 C CB . CYS A 129 ? 0.9343 0.6963 0.6976 -0.1091 0.2127 -0.0224 129 CYS A CB 975 S SG . CYS A 129 ? 0.9423 0.6676 0.6852 -0.1176 0.1964 -0.0332 129 CYS A SG 976 N N . ARG A 130 ? 0.9697 0.7993 0.8024 -0.0646 0.2622 -0.0148 130 ARG A N 977 C CA . ARG A 130 ? 0.9906 0.8607 0.8447 -0.0576 0.2813 -0.0122 130 ARG A CA 978 C C . ARG A 130 ? 0.9466 0.8624 0.8339 -0.0665 0.2696 0.0038 130 ARG A C 979 O O . ARG A 130 ? 0.9197 0.8539 0.8404 -0.0570 0.2574 0.0127 130 ARG A O 980 C CB . ARG A 130 ? 1.0291 0.9032 0.9073 -0.0278 0.2995 -0.0176 130 ARG A CB 981 C CG . ARG A 130 ? 1.0598 0.9847 0.9704 -0.0160 0.3200 -0.0161 130 ARG A CG 982 C CD . ARG A 130 ? 1.1172 1.0323 1.0325 0.0124 0.3452 -0.0299 130 ARG A CD 983 N NE . ARG A 130 ? 1.1259 1.0912 1.0946 0.0371 0.3534 -0.0234 130 ARG A NE 984 C CZ . ARG A 130 ? 1.1313 1.1565 1.1298 0.0343 0.3657 -0.0202 130 ARG A CZ 985 N NH1 . ARG A 130 ? 1.1429 1.1819 1.1195 0.0063 0.3724 -0.0212 130 ARG A NH1 986 N NH2 . ARG A 130 ? 1.1271 1.1999 1.1780 0.0590 0.3706 -0.0149 130 ARG A NH2 987 N N . ARG A 131 ? 0.9393 0.8706 0.8135 -0.0867 0.2730 0.0071 131 ARG A N 988 C CA . ARG A 131 ? 0.9116 0.8874 0.8158 -0.0976 0.2683 0.0202 131 ARG A CA 989 C C . ARG A 131 ? 0.9486 0.9546 0.8515 -0.1040 0.2945 0.0181 131 ARG A C 990 O O . ARG A 131 ? 0.9707 0.9686 0.8418 -0.1275 0.2961 0.0209 131 ARG A O 991 C CB . ARG A 131 ? 0.8884 0.8489 0.7753 -0.1218 0.2437 0.0292 131 ARG A CB 992 C CG . ARG A 131 ? 0.8468 0.7915 0.7438 -0.1177 0.2181 0.0320 131 ARG A CG 993 C CD . ARG A 131 ? 0.8307 0.7653 0.7159 -0.1391 0.1958 0.0398 131 ARG A CD 994 N NE . ARG A 131 ? 0.7991 0.7153 0.6877 -0.1356 0.1733 0.0386 131 ARG A NE 995 C CZ . ARG A 131 ? 0.8024 0.6840 0.6656 -0.1351 0.1645 0.0311 131 ARG A CZ 996 N NH1 . ARG A 131 ? 0.8323 0.6902 0.6614 -0.1384 0.1743 0.0239 131 ARG A NH1 997 N NH2 . ARG A 131 ? 0.7803 0.6537 0.6523 -0.1324 0.1462 0.0297 131 ARG A NH2 998 N N . SER A 132 ? 0.9541 0.9953 0.8911 -0.0828 0.3151 0.0135 132 SER A N 999 C CA . SER A 132 ? 0.9886 1.0648 0.9289 -0.0855 0.3447 0.0082 132 SER A CA 1000 C C . SER A 132 ? 1.0272 1.0647 0.9082 -0.0992 0.3578 -0.0023 132 SER A C 1001 O O . SER A 132 ? 1.0422 1.0827 0.8964 -0.1261 0.3603 0.0036 132 SER A O 1002 C CB . SER A 132 ? 0.9766 1.1031 0.9436 -0.1074 0.3432 0.0217 132 SER A CB 1003 O OG . SER A 132 ? 0.9823 1.0817 0.9121 -0.1388 0.3274 0.0309 132 SER A OG 1004 N N . GLY A 133 ? 1.0452 1.0438 0.9033 -0.0815 0.3652 -0.0176 133 GLY A N 1005 C CA . GLY A 133 ? 1.0748 1.0281 0.8718 -0.0944 0.3708 -0.0291 133 GLY A CA 1006 C C . GLY A 133 ? 1.0520 0.9559 0.8227 -0.1019 0.3411 -0.0270 133 GLY A C 1007 O O . GLY A 133 ? 1.0042 0.9102 0.8032 -0.0977 0.3187 -0.0169 133 GLY A O 1008 N N . SER A 134 ? 1.0746 0.9375 0.7912 -0.1138 0.3409 -0.0374 134 SER A N 1009 C CA . SER A 134 ? 1.0612 0.8804 0.7528 -0.1208 0.3145 -0.0387 134 SER A CA 1010 C C . SER A 134 ? 1.0238 0.8468 0.7167 -0.1401 0.2857 -0.0210 134 SER A C 1011 O O . SER A 134 ? 1.0306 0.8710 0.7146 -0.1572 0.2868 -0.0102 134 SER A O 1012 C CB . SER A 134 ? 1.1151 0.8952 0.7478 -0.1306 0.3210 -0.0549 134 SER A CB 1013 O OG . SER A 134 ? 1.1495 0.9157 0.7789 -0.1114 0.3453 -0.0744 134 SER A OG 1014 N N . SER A 135 ? 0.9904 0.7955 0.6937 -0.1375 0.2610 -0.0187 135 SER A N 1015 C CA . SER A 135 ? 0.9554 0.7608 0.6626 -0.1516 0.2327 -0.0048 135 SER A CA 1016 C C . SER A 135 ? 0.9498 0.7245 0.6456 -0.1524 0.2096 -0.0106 135 SER A C 1017 O O . SER A 135 ? 0.9720 0.7201 0.6417 -0.1508 0.2143 -0.0246 135 SER A O 1018 C CB . SER A 135 ? 0.9079 0.7490 0.6650 -0.1455 0.2280 0.0077 135 SER A CB 1019 O OG . SER A 135 ? 0.8829 0.7225 0.6415 -0.1597 0.2032 0.0195 135 SER A OG 1020 N N . PHE A 136 ? 0.9238 0.7033 0.6391 -0.1560 0.1853 -0.0012 136 PHE A N 1021 C CA . PHE A 136 ? 0.9166 0.6757 0.6270 -0.1574 0.1634 -0.0067 136 PHE A CA 1022 C C . PHE A 136 ? 0.8820 0.6575 0.6308 -0.1527 0.1461 0.0011 136 PHE A C 1023 O O . PHE A 136 ? 0.8849 0.6850 0.6612 -0.1490 0.1500 0.0104 136 PHE A O 1024 C CB . PHE A 136 ? 0.9360 0.6748 0.6063 -0.1734 0.1467 -0.0065 136 PHE A CB 1025 C CG . PHE A 136 ? 0.9381 0.6581 0.5982 -0.1752 0.1291 -0.0171 136 PHE A CG 1026 C CD1 . PHE A 136 ? 0.9511 0.6561 0.6036 -0.1709 0.1406 -0.0323 136 PHE A CD1 1027 C CD2 . PHE A 136 ? 0.9285 0.6463 0.5888 -0.1813 0.1011 -0.0126 136 PHE A CD2 1028 C CE1 . PHE A 136 ? 0.9533 0.6447 0.5989 -0.1762 0.1248 -0.0426 136 PHE A CE1 1029 C CE2 . PHE A 136 ? 0.9295 0.6382 0.5862 -0.1833 0.0851 -0.0234 136 PHE A CE2 1030 C CZ . PHE A 136 ? 0.9374 0.6347 0.5871 -0.1825 0.0972 -0.0383 136 PHE A CZ 1031 N N . TYR A 137 ? 0.8640 0.6287 0.6150 -0.1535 0.1277 -0.0041 137 TYR A N 1032 C CA . TYR A 137 ? 0.8192 0.5986 0.6018 -0.1501 0.1110 0.0007 137 TYR A CA 1033 C C . TYR A 137 ? 0.8148 0.6019 0.6004 -0.1577 0.0970 0.0118 137 TYR A C 1034 O O . TYR A 137 ? 0.8352 0.6068 0.5963 -0.1669 0.0836 0.0137 137 TYR A O 1035 C CB . TYR A 137 ? 0.8076 0.5767 0.5893 -0.1517 0.0951 -0.0089 137 TYR A CB 1036 C CG . TYR A 137 ? 0.8067 0.5663 0.5896 -0.1468 0.1075 -0.0186 137 TYR A CG 1037 C CD1 . TYR A 137 ? 0.8430 0.5795 0.5962 -0.1517 0.1160 -0.0291 137 TYR A CD1 1038 C CD2 . TYR A 137 ? 0.7767 0.5472 0.5868 -0.1386 0.1103 -0.0172 137 TYR A CD2 1039 C CE1 . TYR A 137 ? 0.8514 0.5722 0.6035 -0.1487 0.1272 -0.0382 137 TYR A CE1 1040 C CE2 . TYR A 137 ? 0.7850 0.5405 0.5927 -0.1355 0.1213 -0.0238 137 TYR A CE2 1041 C CZ . TYR A 137 ? 0.8211 0.5501 0.6006 -0.1407 0.1298 -0.0345 137 TYR A CZ 1042 O OH . TYR A 137 ? 0.8275 0.5351 0.6028 -0.1392 0.1406 -0.0412 137 TYR A OH 1043 N N . ALA A 138 ? 0.7900 0.5989 0.6043 -0.1542 0.0987 0.0195 138 ALA A N 1044 C CA . ALA A 138 ? 0.7899 0.6037 0.6076 -0.1634 0.0884 0.0300 138 ALA A CA 1045 C C . ALA A 138 ? 0.7977 0.5933 0.6067 -0.1682 0.0626 0.0301 138 ALA A C 1046 O O . ALA A 138 ? 0.8152 0.5973 0.6068 -0.1785 0.0539 0.0389 138 ALA A O 1047 C CB . ALA A 138 ? 0.7658 0.6073 0.6190 -0.1591 0.0911 0.0348 138 ALA A CB 1048 N N . GLU A 139 ? 0.7816 0.5769 0.6026 -0.1605 0.0508 0.0205 139 GLU A N 1049 C CA . GLU A 139 ? 0.7823 0.5663 0.6032 -0.1604 0.0259 0.0181 139 GLU A CA 1050 C C . GLU A 139 ? 0.8215 0.5872 0.6154 -0.1630 0.0152 0.0136 139 GLU A C 1051 O O . GLU A 139 ? 0.8304 0.5890 0.6258 -0.1604 -0.0069 0.0113 139 GLU A O 1052 C CB . GLU A 139 ? 0.7485 0.5490 0.6004 -0.1509 0.0190 0.0085 139 GLU A CB 1053 C CG . GLU A 139 ? 0.7190 0.5403 0.5965 -0.1476 0.0278 0.0110 139 GLU A CG 1054 C CD . GLU A 139 ? 0.7171 0.5365 0.5992 -0.1535 0.0198 0.0193 139 GLU A CD 1055 O OE1 . GLU A 139 ? 0.7438 0.5431 0.6049 -0.1616 0.0134 0.0268 139 GLU A OE1 1056 O OE2 . GLU A 139 ? 0.6862 0.5225 0.5903 -0.1516 0.0196 0.0187 139 GLU A OE2 1057 N N . MET A 140 ? 0.8533 0.6123 0.6231 -0.1672 0.0298 0.0112 140 MET A N 1058 C CA . MET A 140 ? 0.8931 0.6372 0.6354 -0.1714 0.0200 0.0048 140 MET A CA 1059 C C . MET A 140 ? 0.9360 0.6618 0.6361 -0.1821 0.0262 0.0128 140 MET A C 1060 O O . MET A 140 ? 0.9413 0.6698 0.6369 -0.1861 0.0432 0.0213 140 MET A O 1061 C CB . MET A 140 ? 0.9032 0.6518 0.6493 -0.1692 0.0320 -0.0092 140 MET A CB 1062 C CG . MET A 140 ? 0.8812 0.6487 0.6651 -0.1610 0.0344 -0.0152 140 MET A CG 1063 S SD . MET A 140 ? 0.9053 0.6855 0.7138 -0.1567 0.0067 -0.0207 140 MET A SD 1064 C CE . MET A 140 ? 0.9055 0.6829 0.7003 -0.1635 -0.0005 -0.0349 140 MET A CE 1065 N N . LYS A 141 ? 0.9608 0.6712 0.6297 -0.1876 0.0125 0.0095 141 LYS A N 1066 C CA . LYS A 141 ? 1.0109 0.7030 0.6320 -0.1992 0.0187 0.0153 141 LYS A CA 1067 C C . LYS A 141 ? 1.0275 0.7109 0.6201 -0.2038 0.0174 0.0013 141 LYS A C 1068 O O . LYS A 141 ? 1.0181 0.7022 0.6137 -0.2025 -0.0055 -0.0053 141 LYS A O 1069 C CB . LYS A 141 ? 1.0526 0.7271 0.6517 -0.2053 -0.0029 0.0319 141 LYS A CB 1070 C CG . LYS A 141 ? 1.0588 0.7334 0.6631 -0.2106 0.0085 0.0472 141 LYS A CG 1071 C CD . LYS A 141 ? 1.0962 0.7488 0.6891 -0.2144 -0.0169 0.0633 141 LYS A CD 1072 C CE . LYS A 141 ? 1.1311 0.7750 0.7068 -0.2292 -0.0035 0.0805 141 LYS A CE 1073 N NZ . LYS A 141 ? 1.0966 0.7676 0.7117 -0.2280 0.0187 0.0783 141 LYS A NZ 1074 N N . TRP A 142 ? 1.0433 0.7204 0.6102 -0.2092 0.0424 -0.0046 142 TRP A N 1075 C CA . TRP A 142 ? 1.0730 0.7376 0.6076 -0.2158 0.0444 -0.0200 142 TRP A CA 1076 C C . TRP A 142 ? 1.1269 0.7742 0.6099 -0.2281 0.0270 -0.0135 142 TRP A C 1077 O O . TRP A 142 ? 1.1536 0.7906 0.5997 -0.2366 0.0409 -0.0058 142 TRP A O 1078 C CB . TRP A 142 ? 1.0821 0.7427 0.6066 -0.2149 0.0788 -0.0302 142 TRP A CB 1079 C CG . TRP A 142 ? 1.0995 0.7456 0.6036 -0.2191 0.0838 -0.0507 142 TRP A CG 1080 C CD1 . TRP A 142 ? 1.1232 0.7602 0.6037 -0.2289 0.0619 -0.0598 142 TRP A CD1 1081 C CD2 . TRP A 142 ? 1.1097 0.7469 0.6142 -0.2140 0.1119 -0.0651 142 TRP A CD2 1082 N NE1 . TRP A 142 ? 1.1458 0.7681 0.6113 -0.2332 0.0751 -0.0798 142 TRP A NE1 1083 C CE2 . TRP A 142 ? 1.1415 0.7601 0.6201 -0.2233 0.1062 -0.0834 142 TRP A CE2 1084 C CE3 . TRP A 142 ? 1.0963 0.7393 0.6218 -0.2017 0.1402 -0.0646 142 TRP A CE3 1085 C CZ2 . TRP A 142 ? 1.1627 0.7618 0.6329 -0.2213 0.1288 -0.1014 142 TRP A CZ2 1086 C CZ3 . TRP A 142 ? 1.1173 0.7429 0.6364 -0.1964 0.1619 -0.0815 142 TRP A CZ3 1087 C CH2 . TRP A 142 ? 1.1511 0.7515 0.6411 -0.2066 0.1566 -0.0998 142 TRP A CH2 1088 N N . LEU A 143 ? 1.1387 0.7853 0.6194 -0.2291 -0.0035 -0.0164 143 LEU A N 1089 C CA . LEU A 143 ? 1.1892 0.8199 0.6217 -0.2388 -0.0267 -0.0084 143 LEU A CA 1090 C C . LEU A 143 ? 1.2348 0.8534 0.6192 -0.2515 -0.0203 -0.0240 143 LEU A C 1091 O O . LEU A 143 ? 1.2190 0.8435 0.6148 -0.2524 -0.0215 -0.0430 143 LEU A O 1092 C CB . LEU A 143 ? 1.1794 0.8184 0.6340 -0.2316 -0.0650 -0.0047 143 LEU A CB 1093 C CG . LEU A 143 ? 1.1449 0.7908 0.6417 -0.2186 -0.0762 0.0089 143 LEU A CG 1094 C CD1 . LEU A 143 ? 1.1570 0.8047 0.6616 -0.2108 -0.1159 0.0136 143 LEU A CD1 1095 C CD2 . LEU A 143 ? 1.1579 0.7871 0.6355 -0.2234 -0.0631 0.0285 143 LEU A CD2 1096 N N . LEU A 144 ? 1.2912 0.8918 0.6194 -0.2632 -0.0140 -0.0157 144 LEU A N 1097 C CA . LEU A 144 ? 1.3484 0.9350 0.6232 -0.2763 -0.0011 -0.0311 144 LEU A CA 1098 C C . LEU A 144 ? 1.4049 0.9761 0.6197 -0.2891 -0.0284 -0.0211 144 LEU A C 1099 O O . LEU A 144 ? 1.4077 0.9768 0.6246 -0.2860 -0.0562 -0.0008 144 LEU A O 1100 C CB . LEU A 144 ? 1.3659 0.9481 0.6250 -0.2785 0.0400 -0.0322 144 LEU A CB 1101 C CG . LEU A 144 ? 1.3884 0.9638 0.6343 -0.2799 0.0695 -0.0580 144 LEU A CG 1102 C CD1 . LEU A 144 ? 1.3442 0.9278 0.6428 -0.2688 0.0694 -0.0730 144 LEU A CD1 1103 C CD2 . LEU A 144 ? 1.3972 0.9755 0.6377 -0.2774 0.1090 -0.0566 144 LEU A CD2 1104 N N . SER A 145 ? 1.4549 1.0128 0.6144 -0.3030 -0.0214 -0.0358 145 SER A N 1105 C CA . SER A 145 ? 1.5263 1.0675 0.6166 -0.3175 -0.0426 -0.0253 145 SER A CA 1106 C C . SER A 145 ? 1.5586 1.0857 0.6017 -0.3277 -0.0135 -0.0132 145 SER A C 1107 O O . SER A 145 ? 1.5510 1.0803 0.5953 -0.3279 0.0257 -0.0270 145 SER A O 1108 C CB . SER A 145 ? 1.5735 1.1090 0.6234 -0.3301 -0.0525 -0.0490 145 SER A CB 1109 O OG . SER A 145 ? 1.5581 1.1089 0.6377 -0.3258 -0.0909 -0.0530 145 SER A OG 1110 N N . ASN A 146 ? 1.5993 1.1122 0.6010 -0.3360 -0.0325 0.0126 146 ASN A N 1111 C CA . ASN A 146 ? 1.6403 1.1416 0.5974 -0.3489 -0.0061 0.0284 146 ASN A CA 1112 C C . ASN A 146 ? 1.6722 1.1744 0.5951 -0.3583 0.0370 0.0062 146 ASN A C 1113 O O . ASN A 146 ? 1.6587 1.1698 0.5911 -0.3590 0.0732 0.0091 146 ASN A O 1114 C CB . ASN A 146 ? 1.7160 1.1930 0.6053 -0.3632 -0.0356 0.0538 146 ASN A CB 1115 C CG . ASN A 146 ? 1.6987 1.1669 0.6154 -0.3553 -0.0629 0.0844 146 ASN A CG 1116 O OD1 . ASN A 146 ? 1.6468 1.1259 0.6203 -0.3455 -0.0491 0.0900 146 ASN A OD1 1117 N ND2 . ASN A 146 ? 1.7507 1.1972 0.6250 -0.3593 -0.1028 0.1042 146 ASN A ND2 1118 N N . THR A 147 ? 1.7137 1.2085 0.5991 -0.3650 0.0329 -0.0173 147 THR A N 1119 C CA . THR A 147 ? 1.7515 1.2424 0.6013 -0.3723 0.0724 -0.0431 147 THR A CA 1120 C C . THR A 147 ? 1.7446 1.2324 0.6038 -0.3690 0.0682 -0.0760 147 THR A C 1121 O O . THR A 147 ? 1.7191 1.2118 0.6097 -0.3639 0.0341 -0.0772 147 THR A O 1122 C CB . THR A 147 ? 1.8442 1.3182 0.6013 -0.3948 0.0783 -0.0360 147 THR A CB 1123 O OG1 . THR A 147 ? 1.8886 1.3604 0.6134 -0.4000 0.1202 -0.0640 147 THR A OG1 1124 C CG2 . THR A 147 ? 1.8983 1.3563 0.6021 -0.4065 0.0331 -0.0318 147 THR A CG2 1125 N N . ASP A 148 ? 1.7721 1.2518 0.6055 -0.3723 0.1036 -0.1032 148 ASP A N 1126 C CA . ASP A 148 ? 1.7696 1.2397 0.6110 -0.3706 0.1050 -0.1361 148 ASP A CA 1127 C C . ASP A 148 ? 1.8154 1.2749 0.6106 -0.3871 0.0656 -0.1435 148 ASP A C 1128 O O . ASP A 148 ? 1.8782 1.3280 0.6025 -0.4036 0.0543 -0.1359 148 ASP A O 1129 C CB . ASP A 148 ? 1.8081 1.2649 0.6213 -0.3707 0.1513 -0.1643 148 ASP A CB 1130 C CG . ASP A 148 ? 1.7643 1.2371 0.6286 -0.3522 0.1898 -0.1594 148 ASP A CG 1131 O OD1 . ASP A 148 ? 1.7369 1.2291 0.6262 -0.3486 0.1873 -0.1308 148 ASP A OD1 1132 O OD2 . ASP A 148 ? 1.7642 1.2295 0.6436 -0.3411 0.2216 -0.1843 148 ASP A OD2 1133 N N . ASN A 149 ? 1.7805 1.2444 0.6170 -0.3835 0.0441 -0.1570 149 ASN A N 1134 C CA . ASN A 149 ? 1.8165 1.2791 0.6244 -0.3984 0.0036 -0.1660 149 ASN A CA 1135 C C . ASN A 149 ? 1.8262 1.3020 0.6241 -0.4006 -0.0420 -0.1362 149 ASN A C 1136 O O . ASN A 149 ? 1.8595 1.3398 0.6362 -0.4113 -0.0793 -0.1415 149 ASN A O 1137 C CB . ASN A 149 ? 1.8994 1.3376 0.6262 -0.4187 0.0150 -0.1936 149 ASN A CB 1138 C CG . ASN A 149 ? 1.8983 1.3179 0.6372 -0.4166 0.0503 -0.2285 149 ASN A CG 1139 O OD1 . ASN A 149 ? 1.8198 1.2449 0.6275 -0.4007 0.0632 -0.2313 149 ASN A OD1 1140 N ND2 . ASN A 149 ? 1.9727 1.3673 0.6416 -0.4325 0.0655 -0.2556 149 ASN A ND2 1141 N N . ALA A 150 ? 1.8027 1.2842 0.6174 -0.3903 -0.0407 -0.1054 150 ALA A N 1142 C CA . ALA A 150 ? 1.8201 1.3060 0.6224 -0.3902 -0.0827 -0.0755 150 ALA A CA 1143 C C . ALA A 150 ? 1.7664 1.2762 0.6411 -0.3759 -0.1177 -0.0722 150 ALA A C 1144 O O . ALA A 150 ? 1.6918 1.2155 0.6360 -0.3624 -0.1026 -0.0804 150 ALA A O 1145 C CB . ALA A 150 ? 1.8187 1.2978 0.6149 -0.3859 -0.0686 -0.0447 150 ALA A CB 1146 N N . ALA A 151 ? 1.8050 1.3210 0.6624 -0.3783 -0.1644 -0.0601 151 ALA A N 1147 C CA . ALA A 151 ? 1.7608 1.3046 0.6854 -0.3639 -0.2004 -0.0574 151 ALA A CA 1148 C C . ALA A 151 ? 1.6974 1.2494 0.6891 -0.3423 -0.1940 -0.0378 151 ALA A C 1149 O O . ALA A 151 ? 1.7047 1.2391 0.6806 -0.3399 -0.1758 -0.0173 151 ALA A O 1150 C CB . ALA A 151 ? 1.8111 1.3596 0.7014 -0.3669 -0.2524 -0.0433 151 ALA A CB 1151 N N . PHE A 152 ? 1.6419 1.2219 0.7074 -0.3287 -0.2076 -0.0456 152 PHE A N 1152 C CA . PHE A 152 ? 1.5816 1.1722 0.7118 -0.3080 -0.2068 -0.0298 152 PHE A CA 1153 C C . PHE A 152 ? 1.5811 1.1907 0.7395 -0.2946 -0.2553 -0.0178 152 PHE A C 1154 O O . PHE A 152 ? 1.5598 1.1999 0.7549 -0.2928 -0.2750 -0.0349 152 PHE A O 1155 C CB . PHE A 152 ? 1.5173 1.1259 0.7118 -0.3016 -0.1788 -0.0496 152 PHE A CB 1156 C CG . PHE A 152 ? 1.4649 1.0823 0.7194 -0.2825 -0.1714 -0.0355 152 PHE A CG 1157 C CD1 . PHE A 152 ? 1.4350 1.0755 0.7412 -0.2666 -0.2020 -0.0293 152 PHE A CD1 1158 C CD2 . PHE A 152 ? 1.4490 1.0539 0.7090 -0.2800 -0.1341 -0.0299 152 PHE A CD2 1159 C CE1 . PHE A 152 ? 1.3898 1.0363 0.7473 -0.2499 -0.1949 -0.0188 152 PHE A CE1 1160 C CE2 . PHE A 152 ? 1.3990 1.0126 0.7118 -0.2643 -0.1288 -0.0181 152 PHE A CE2 1161 C CZ . PHE A 152 ? 1.3697 1.0020 0.7290 -0.2499 -0.1589 -0.0130 152 PHE A CZ 1162 N N . PRO A 153 ? 1.6064 1.1981 0.7498 -0.2848 -0.2744 0.0114 153 PRO A N 1163 C CA . PRO A 153 ? 1.6249 1.2285 0.7864 -0.2695 -0.3234 0.0246 153 PRO A CA 1164 C C . PRO A 153 ? 1.5703 1.2093 0.8214 -0.2481 -0.3325 0.0155 153 PRO A C 1165 O O . PRO A 153 ? 1.5182 1.1571 0.8117 -0.2395 -0.3059 0.0157 153 PRO A O 1166 C CB . PRO A 153 ? 1.6617 1.2267 0.7851 -0.2650 -0.3311 0.0586 153 PRO A CB 1167 C CG . PRO A 153 ? 1.6252 1.1750 0.7549 -0.2699 -0.2843 0.0605 153 PRO A CG 1168 C CD . PRO A 153 ? 1.6111 1.1717 0.7293 -0.2861 -0.2498 0.0333 153 PRO A CD 1169 N N . GLN A 154 ? 1.5868 1.2586 0.8658 -0.2401 -0.3702 0.0072 154 GLN A N 1170 C CA . GLN A 154 ? 1.5373 1.2498 0.9015 -0.2206 -0.3798 -0.0041 154 GLN A CA 1171 C C . GLN A 154 ? 1.5281 1.2247 0.9222 -0.1967 -0.3853 0.0170 154 GLN A C 1172 O O . GLN A 154 ? 1.5759 1.2557 0.9526 -0.1833 -0.4195 0.0381 154 GLN A O 1173 C CB . GLN A 154 ? 1.5595 1.3134 0.9453 -0.2160 -0.4229 -0.0147 154 GLN A CB 1174 C CG . GLN A 154 ? 1.4998 1.3062 0.9747 -0.2014 -0.4267 -0.0334 154 GLN A CG 1175 C CD . GLN A 154 ? 1.4556 1.2815 0.9565 -0.2196 -0.3895 -0.0600 154 GLN A CD 1176 O OE1 . GLN A 154 ? 1.4914 1.3153 0.9561 -0.2437 -0.3818 -0.0746 154 GLN A OE1 1177 N NE2 . GLN A 154 ? 1.3824 1.2243 0.9435 -0.2086 -0.3670 -0.0664 154 GLN A NE2 1178 N N . MET A 155 ? 1.4708 1.1703 0.9079 -0.1918 -0.3524 0.0111 155 MET A N 1179 C CA . MET A 155 ? 1.4572 1.1356 0.9161 -0.1742 -0.3501 0.0289 155 MET A CA 1180 C C . MET A 155 ? 1.4070 1.1211 0.9452 -0.1512 -0.3594 0.0175 155 MET A C 1181 O O . MET A 155 ? 1.3588 1.1155 0.9414 -0.1529 -0.3519 -0.0059 155 MET A O 1182 C CB . MET A 155 ? 1.4321 1.0859 0.8766 -0.1859 -0.3058 0.0328 155 MET A CB 1183 C CG . MET A 155 ? 1.4962 1.1039 0.8688 -0.1992 -0.3005 0.0563 155 MET A CG 1184 S SD . MET A 155 ? 1.4704 1.0624 0.8380 -0.2119 -0.2475 0.0575 155 MET A SD 1185 C CE . MET A 155 ? 1.5434 1.0845 0.8412 -0.2226 -0.2519 0.0909 155 MET A CE 1186 N N . THR A 156 ? 1.4140 1.1077 0.9669 -0.1312 -0.3743 0.0339 156 THR A N 1187 C CA . THR A 156 ? 1.3681 1.0898 0.9923 -0.1069 -0.3822 0.0236 156 THR A CA 1188 C C . THR A 156 ? 1.3496 1.0350 0.9787 -0.0983 -0.3679 0.0377 156 THR A C 1189 O O . THR A 156 ? 1.3936 1.0367 0.9930 -0.0905 -0.3878 0.0603 156 THR A O 1190 C CB . THR A 156 ? 1.4061 1.1458 1.0509 -0.0838 -0.4298 0.0257 156 THR A CB 1191 O OG1 . THR A 156 ? 1.4302 1.1995 1.0592 -0.0957 -0.4470 0.0160 156 THR A OG1 1192 C CG2 . THR A 156 ? 1.3599 1.1409 1.0849 -0.0590 -0.4342 0.0080 156 THR A CG2 1193 N N . LYS A 157 ? 1.2860 0.9860 0.9496 -0.1017 -0.3342 0.0250 157 LYS A N 1194 C CA . LYS A 157 ? 1.2579 0.9313 0.9338 -0.0946 -0.3204 0.0341 157 LYS A CA 1195 C C . LYS A 157 ? 1.1971 0.9054 0.9420 -0.0749 -0.3193 0.0152 157 LYS A C 1196 O O . LYS A 157 ? 1.1563 0.9109 0.9376 -0.0765 -0.3090 -0.0060 157 LYS A O 1197 C CB . LYS A 157 ? 1.2428 0.9008 0.8937 -0.1165 -0.2807 0.0379 157 LYS A CB 1198 C CG . LYS A 157 ? 1.3010 0.9278 0.8829 -0.1372 -0.2759 0.0542 157 LYS A CG 1199 C CD . LYS A 157 ? 1.3740 0.9551 0.9139 -0.1336 -0.3036 0.0803 157 LYS A CD 1200 C CE . LYS A 157 ? 1.4362 0.9917 0.9035 -0.1551 -0.3015 0.0951 157 LYS A CE 1201 N NZ . LYS A 157 ? 1.4438 0.9779 0.8826 -0.1749 -0.2656 0.1049 157 LYS A NZ 1202 N N . SER A 158 ? 1.1935 0.8773 0.9536 -0.0578 -0.3292 0.0227 158 SER A N 1203 C CA . SER A 158 ? 1.1428 0.8558 0.9648 -0.0362 -0.3311 0.0043 158 SER A CA 1204 C C . SER A 158 ? 1.1025 0.7905 0.9326 -0.0360 -0.3110 0.0069 158 SER A C 1205 O O . SER A 158 ? 1.1210 0.7633 0.9108 -0.0482 -0.3048 0.0265 158 SER A O 1206 C CB . SER A 158 ? 1.1808 0.8935 1.0224 -0.0079 -0.3717 0.0051 158 SER A CB 1207 O OG . SER A 158 ? 1.1506 0.8951 1.0535 0.0145 -0.3721 -0.0155 158 SER A OG 1208 N N . TYR A 159 ? 1.0453 0.7661 0.9269 -0.0241 -0.3004 -0.0136 159 TYR A N 1209 C CA . TYR A 159 ? 1.0196 0.7227 0.9130 -0.0230 -0.2833 -0.0150 159 TYR A CA 1210 C C . TYR A 159 ? 0.9960 0.7291 0.9449 0.0008 -0.2885 -0.0377 159 TYR A C 1211 O O . TYR A 159 ? 0.9543 0.7405 0.9392 0.0026 -0.2782 -0.0576 159 TYR A O 1212 C CB . TYR A 159 ? 0.9728 0.6887 0.8585 -0.0463 -0.2465 -0.0168 159 TYR A CB 1213 C CG . TYR A 159 ? 0.9388 0.6517 0.8448 -0.0454 -0.2287 -0.0231 159 TYR A CG 1214 C CD1 . TYR A 159 ? 0.9639 0.6315 0.8458 -0.0519 -0.2277 -0.0076 159 TYR A CD1 1215 C CD2 . TYR A 159 ? 0.8872 0.6430 0.8343 -0.0403 -0.2131 -0.0444 159 TYR A CD2 1216 C CE1 . TYR A 159 ? 0.9401 0.6064 0.8396 -0.0530 -0.2133 -0.0145 159 TYR A CE1 1217 C CE2 . TYR A 159 ? 0.8704 0.6241 0.8318 -0.0403 -0.1984 -0.0505 159 TYR A CE2 1218 C CZ . TYR A 159 ? 0.8935 0.6031 0.8318 -0.0464 -0.1994 -0.0362 159 TYR A CZ 1219 O OH . TYR A 159 ? 0.8806 0.5899 0.8325 -0.0482 -0.1864 -0.0435 159 TYR A OH 1220 N N . LYS A 160 ? 1.0254 0.7231 0.9795 0.0181 -0.3033 -0.0352 160 LYS A N 1221 C CA . LYS A 160 ? 1.0065 0.7275 1.0106 0.0422 -0.3063 -0.0584 160 LYS A CA 1222 C C . LYS A 160 ? 0.9754 0.6923 0.9856 0.0322 -0.2791 -0.0663 160 LYS A C 1223 O O . LYS A 160 ? 0.9893 0.6623 0.9666 0.0171 -0.2721 -0.0502 160 LYS A O 1224 C CB . LYS A 160 ? 1.0585 0.7402 1.0663 0.0704 -0.3400 -0.0543 160 LYS A CB 1225 C CG . LYS A 160 ? 1.0474 0.7583 1.1105 0.1003 -0.3453 -0.0820 160 LYS A CG 1226 C CD . LYS A 160 ? 1.1082 0.7687 1.1720 0.1299 -0.3775 -0.0773 160 LYS A CD 1227 C CE . LYS A 160 ? 1.0980 0.7855 1.2166 0.1604 -0.3784 -0.1080 160 LYS A CE 1228 N NZ . LYS A 160 ? 1.1650 0.7960 1.2844 0.1918 -0.4089 -0.1051 160 LYS A NZ 1229 N N . ASN A 161 ? 0.9355 0.7011 0.9874 0.0392 -0.2641 -0.0910 161 ASN A N 1230 C CA . ASN A 161 ? 0.9160 0.6828 0.9760 0.0326 -0.2413 -0.1013 161 ASN A CA 1231 C C . ASN A 161 ? 0.9510 0.6870 1.0253 0.0552 -0.2561 -0.1117 161 ASN A C 1232 O O . ASN A 161 ? 0.9478 0.7110 1.0605 0.0799 -0.2648 -0.1333 161 ASN A O 1233 C CB . ASN A 161 ? 0.8648 0.6951 0.9573 0.0286 -0.2183 -0.1221 161 ASN A CB 1234 C CG . ASN A 161 ? 0.8490 0.6839 0.9462 0.0210 -0.1955 -0.1321 161 ASN A CG 1235 O OD1 . ASN A 161 ? 0.8701 0.6637 0.9450 0.0141 -0.1945 -0.1224 161 ASN A OD1 1236 N ND2 . ASN A 161 ? 0.8175 0.7042 0.9426 0.0203 -0.1774 -0.1512 161 ASN A ND2 1237 N N . THR A 162 ? 0.9827 0.6624 1.0266 0.0460 -0.2579 -0.0976 162 THR A N 1238 C CA . THR A 162 ? 1.0305 0.6671 1.0802 0.0645 -0.2730 -0.1057 162 THR A CA 1239 C C . THR A 162 ? 1.0133 0.6563 1.0737 0.0581 -0.2527 -0.1237 162 THR A C 1240 O O . THR A 162 ? 1.0515 0.6487 1.1060 0.0645 -0.2612 -0.1281 162 THR A O 1241 C CB . THR A 162 ? 1.0877 0.6493 1.0943 0.0570 -0.2914 -0.0784 162 THR A CB 1242 O OG1 . THR A 162 ? 1.0743 0.6155 1.0529 0.0269 -0.2723 -0.0661 162 THR A OG1 1243 C CG2 . THR A 162 ? 1.1102 0.6648 1.0930 0.0549 -0.3079 -0.0558 162 THR A CG2 1244 N N . ARG A 163 ? 0.9607 0.6574 1.0344 0.0451 -0.2270 -0.1340 163 ARG A N 1245 C CA . ARG A 163 ? 0.9505 0.6586 1.0311 0.0377 -0.2080 -0.1503 163 ARG A CA 1246 C C . ARG A 163 ? 0.9279 0.6899 1.0482 0.0555 -0.1990 -0.1809 163 ARG A C 1247 O O . ARG A 163 ? 0.9239 0.7213 1.0688 0.0700 -0.2046 -0.1881 163 ARG A O 1248 C CB . ARG A 163 ? 0.9269 0.6495 0.9864 0.0074 -0.1854 -0.1354 163 ARG A CB 1249 C CG . ARG A 163 ? 0.9696 0.6395 0.9936 -0.0113 -0.1904 -0.1112 163 ARG A CG 1250 C CD . ARG A 163 ? 0.9442 0.6315 0.9503 -0.0382 -0.1696 -0.0947 163 ARG A CD 1251 N NE . ARG A 163 ? 0.9190 0.6374 0.9355 -0.0469 -0.1505 -0.1072 163 ARG A NE 1252 C CZ . ARG A 163 ? 0.8997 0.6273 0.9033 -0.0682 -0.1348 -0.0953 163 ARG A CZ 1253 N NH1 . ARG A 163 ? 0.8969 0.6068 0.8782 -0.0839 -0.1330 -0.0719 163 ARG A NH1 1254 N NH2 . ARG A 163 ? 0.8770 0.6341 0.8901 -0.0733 -0.1209 -0.1070 163 ARG A NH2 1255 N N . LYS A 164 ? 0.9295 0.6999 1.0551 0.0530 -0.1849 -0.1992 164 LYS A N 1256 C CA . LYS A 164 ? 0.9232 0.7414 1.0830 0.0696 -0.1746 -0.2307 164 LYS A CA 1257 C C . LYS A 164 ? 0.8669 0.7501 1.0383 0.0560 -0.1506 -0.2346 164 LYS A C 1258 O O . LYS A 164 ? 0.8517 0.7820 1.0530 0.0681 -0.1414 -0.2585 164 LYS A O 1259 C CB . LYS A 164 ? 0.9557 0.7550 1.1114 0.0713 -0.1689 -0.2507 164 LYS A CB 1260 C CG . LYS A 164 ? 1.0155 0.7749 1.1836 0.0998 -0.1887 -0.2689 164 LYS A CG 1261 C CD . LYS A 164 ? 1.0360 0.7983 1.2073 0.1030 -0.1766 -0.2986 164 LYS A CD 1262 C CE . LYS A 164 ? 1.1025 0.7986 1.2688 0.1215 -0.1961 -0.3108 164 LYS A CE 1263 N NZ . LYS A 164 ? 1.1211 0.8134 1.2800 0.1167 -0.1834 -0.3377 164 LYS A NZ 1264 N N . SER A 165 ? 0.8417 0.7269 0.9894 0.0309 -0.1395 -0.2119 165 SER A N 1265 C CA . SER A 165 ? 0.7953 0.7325 0.9489 0.0165 -0.1173 -0.2126 165 SER A CA 1266 C C . SER A 165 ? 0.7735 0.7181 0.9233 0.0092 -0.1210 -0.1944 165 SER A C 1267 O O . SER A 165 ? 0.7986 0.7048 0.9303 0.0085 -0.1368 -0.1760 165 SER A O 1268 C CB . SER A 165 ? 0.7806 0.7169 0.9104 -0.0054 -0.0990 -0.2043 165 SER A CB 1269 O OG . SER A 165 ? 0.7946 0.6924 0.8965 -0.0197 -0.1041 -0.1788 165 SER A OG 1270 N N . PRO A 166 ? 0.7363 0.7290 0.9006 0.0019 -0.1062 -0.1999 166 PRO A N 1271 C CA . PRO A 166 ? 0.7187 0.7193 0.8789 -0.0068 -0.1093 -0.1861 166 PRO A CA 1272 C C . PRO A 166 ? 0.7059 0.6739 0.8291 -0.0264 -0.1042 -0.1600 166 PRO A C 1273 O O . PRO A 166 ? 0.6918 0.6535 0.7987 -0.0389 -0.0889 -0.1535 166 PRO A O 1274 C CB . PRO A 166 ? 0.6992 0.7554 0.8801 -0.0153 -0.0899 -0.1991 166 PRO A CB 1275 C CG . PRO A 166 ? 0.7016 0.7852 0.9072 -0.0025 -0.0830 -0.2240 166 PRO A CG 1276 C CD . PRO A 166 ? 0.7218 0.7634 0.9067 0.0009 -0.0865 -0.2209 166 PRO A CD 1277 N N . ALA A 167 ? 0.7050 0.6556 0.8155 -0.0283 -0.1171 -0.1461 167 ALA A N 1278 C CA . ALA A 167 ? 0.6993 0.6198 0.7749 -0.0451 -0.1121 -0.1231 167 ALA A CA 1279 C C . ALA A 167 ? 0.6783 0.6217 0.7486 -0.0605 -0.0969 -0.1195 167 ALA A C 1280 O O . ALA A 167 ? 0.6845 0.6518 0.7693 -0.0587 -0.1028 -0.1274 167 ALA A O 1281 C CB . ALA A 167 ? 0.7269 0.6082 0.7838 -0.0397 -0.1347 -0.1093 167 ALA A CB 1282 N N . LEU A 168 ? 0.6606 0.5963 0.7111 -0.0753 -0.0781 -0.1081 168 LEU A N 1283 C CA . LEU A 168 ? 0.6471 0.5922 0.6867 -0.0897 -0.0636 -0.1029 168 LEU A CA 1284 C C . LEU A 168 ? 0.6640 0.5792 0.6754 -0.0955 -0.0709 -0.0879 168 LEU A C 1285 O O . LEU A 168 ? 0.6735 0.5603 0.6635 -0.0986 -0.0698 -0.0737 168 LEU A O 1286 C CB . LEU A 168 ? 0.6256 0.5750 0.6574 -0.0996 -0.0410 -0.0975 168 LEU A CB 1287 C CG . LEU A 168 ? 0.6206 0.5661 0.6350 -0.1133 -0.0249 -0.0887 168 LEU A CG 1288 C CD1 . LEU A 168 ? 0.6189 0.5863 0.6446 -0.1191 -0.0240 -0.0998 168 LEU A CD1 1289 C CD2 . LEU A 168 ? 0.6050 0.5543 0.6145 -0.1184 -0.0060 -0.0827 168 LEU A CD2 1290 N N . ILE A 169 ? 0.6743 0.5984 0.6854 -0.0985 -0.0781 -0.0918 169 ILE A N 1291 C CA . ILE A 169 ? 0.7073 0.6053 0.6880 -0.1050 -0.0856 -0.0801 169 ILE A CA 1292 C C . ILE A 169 ? 0.7081 0.6098 0.6746 -0.1206 -0.0682 -0.0801 169 ILE A C 1293 O O . ILE A 169 ? 0.7016 0.6304 0.6862 -0.1256 -0.0633 -0.0925 169 ILE A O 1294 C CB . ILE A 169 ? 0.7336 0.6354 0.7202 -0.0960 -0.1126 -0.0846 169 ILE A CB 1295 C CG1 . ILE A 169 ? 0.7429 0.6413 0.7495 -0.0768 -0.1309 -0.0881 169 ILE A CG1 1296 C CG2 . ILE A 169 ? 0.7633 0.6338 0.7107 -0.1033 -0.1217 -0.0704 169 ILE A CG2 1297 C CD1 . ILE A 169 ? 0.7569 0.6130 0.7390 -0.0755 -0.1347 -0.0720 169 ILE A CD1 1298 N N . VAL A 170 ? 0.7200 0.5940 0.6545 -0.1288 -0.0583 -0.0673 170 VAL A N 1299 C CA . VAL A 170 ? 0.7309 0.5995 0.6473 -0.1419 -0.0419 -0.0679 170 VAL A CA 1300 C C . VAL A 170 ? 0.7560 0.5999 0.6373 -0.1480 -0.0491 -0.0616 170 VAL A C 1301 O O . VAL A 170 ? 0.7728 0.5958 0.6353 -0.1452 -0.0545 -0.0495 170 VAL A O 1302 C CB . VAL A 170 ? 0.7245 0.5843 0.6347 -0.1447 -0.0174 -0.0603 170 VAL A CB 1303 C CG1 . VAL A 170 ? 0.7445 0.5920 0.6351 -0.1557 -0.0010 -0.0619 170 VAL A CG1 1304 C CG2 . VAL A 170 ? 0.7060 0.5888 0.6443 -0.1401 -0.0104 -0.0651 170 VAL A CG2 1305 N N . TRP A 171 ? 0.7674 0.6132 0.6377 -0.1584 -0.0488 -0.0700 171 TRP A N 1306 C CA . TRP A 171 ? 0.8042 0.6256 0.6348 -0.1669 -0.0514 -0.0661 171 TRP A CA 1307 C C . TRP A 171 ? 0.8215 0.6348 0.6373 -0.1801 -0.0320 -0.0743 171 TRP A C 1308 O O . TRP A 171 ? 0.8087 0.6352 0.6459 -0.1833 -0.0199 -0.0818 171 TRP A O 1309 C CB . TRP A 171 ? 0.8232 0.6504 0.6484 -0.1658 -0.0808 -0.0690 171 TRP A CB 1310 C CG . TRP A 171 ? 0.8161 0.6735 0.6649 -0.1707 -0.0909 -0.0853 171 TRP A CG 1311 C CD1 . TRP A 171 ? 0.8414 0.6995 0.6724 -0.1852 -0.0949 -0.0949 171 TRP A CD1 1312 C CD2 . TRP A 171 ? 0.7877 0.6822 0.6830 -0.1630 -0.0979 -0.0956 171 TRP A CD2 1313 N NE1 . TRP A 171 ? 0.8279 0.7237 0.6942 -0.1883 -0.1046 -0.1097 171 TRP A NE1 1314 C CE2 . TRP A 171 ? 0.7959 0.7161 0.7027 -0.1742 -0.1056 -0.1104 171 TRP A CE2 1315 C CE3 . TRP A 171 ? 0.7613 0.6711 0.6890 -0.1486 -0.0977 -0.0951 171 TRP A CE3 1316 C CZ2 . TRP A 171 ? 0.7750 0.7397 0.7277 -0.1715 -0.1114 -0.1242 171 TRP A CZ2 1317 C CZ3 . TRP A 171 ? 0.7447 0.6953 0.7143 -0.1443 -0.1030 -0.1096 171 TRP A CZ3 1318 C CH2 . TRP A 171 ? 0.7491 0.7290 0.7326 -0.1557 -0.1092 -0.1237 171 TRP A CH2 1319 N N . GLY A 172 ? 0.8580 0.6463 0.6343 -0.1882 -0.0280 -0.0729 172 GLY A N 1320 C CA . GLY A 172 ? 0.8792 0.6511 0.6364 -0.1996 -0.0084 -0.0816 172 GLY A CA 1321 C C . GLY A 172 ? 0.9246 0.6852 0.6486 -0.2130 -0.0189 -0.0914 172 GLY A C 1322 O O . GLY A 172 ? 0.9425 0.7041 0.6502 -0.2127 -0.0401 -0.0874 172 GLY A O 1323 N N . ILE A 173 ? 0.9484 0.6959 0.6604 -0.2255 -0.0049 -0.1040 173 ILE A N 1324 C CA . ILE A 173 ? 0.9998 0.7339 0.6769 -0.2412 -0.0126 -0.1165 173 ILE A CA 1325 C C . ILE A 173 ? 1.0353 0.7320 0.6792 -0.2470 0.0147 -0.1226 173 ILE A C 1326 O O . ILE A 173 ? 1.0376 0.7241 0.6942 -0.2487 0.0333 -0.1276 173 ILE A O 1327 C CB . ILE A 173 ? 1.0000 0.7580 0.6988 -0.2551 -0.0272 -0.1318 173 ILE A CB 1328 C CG1 . ILE A 173 ? 0.9712 0.7711 0.7095 -0.2459 -0.0532 -0.1282 173 ILE A CG1 1329 C CG2 . ILE A 173 ? 1.0531 0.7978 0.7136 -0.2734 -0.0371 -0.1458 173 ILE A CG2 1330 C CD1 . ILE A 173 ? 0.9929 0.7965 0.7127 -0.2398 -0.0808 -0.1211 173 ILE A CD1 1331 N N . HIS A 174 ? 1.0709 0.7459 0.6709 -0.2492 0.0173 -0.1220 174 HIS A N 1332 C CA . HIS A 174 ? 1.1149 0.7549 0.6823 -0.2516 0.0443 -0.1297 174 HIS A CA 1333 C C . HIS A 174 ? 1.1656 0.7858 0.7031 -0.2712 0.0425 -0.1509 174 HIS A C 1334 O O . HIS A 174 ? 1.2021 0.8249 0.7107 -0.2828 0.0230 -0.1570 174 HIS A O 1335 C CB . HIS A 174 ? 1.1369 0.7648 0.6697 -0.2456 0.0527 -0.1206 174 HIS A CB 1336 C CG . HIS A 174 ? 1.1857 0.7808 0.6836 -0.2470 0.0806 -0.1319 174 HIS A CG 1337 N ND1 . HIS A 174 ? 1.2408 0.8153 0.6862 -0.2596 0.0809 -0.1443 174 HIS A ND1 1338 C CD2 . HIS A 174 ? 1.1864 0.7649 0.6941 -0.2362 0.1089 -0.1343 174 HIS A CD2 1339 C CE1 . HIS A 174 ? 1.2727 0.8192 0.6978 -0.2560 0.1101 -0.1553 174 HIS A CE1 1340 N NE2 . HIS A 174 ? 1.2397 0.7879 0.7035 -0.2407 0.1269 -0.1489 174 HIS A NE2 1341 N N . HIS A 175 ? 1.1784 0.7764 0.7207 -0.2754 0.0617 -0.1618 175 HIS A N 1342 C CA . HIS A 175 ? 1.2313 0.8001 0.7407 -0.2951 0.0652 -0.1838 175 HIS A CA 1343 C C . HIS A 175 ? 1.2829 0.8097 0.7533 -0.2886 0.0931 -0.1905 175 HIS A C 1344 O O . HIS A 175 ? 1.2769 0.7853 0.7609 -0.2747 0.1169 -0.1867 175 HIS A O 1345 C CB . HIS A 175 ? 1.2215 0.7859 0.7580 -0.3064 0.0692 -0.1922 175 HIS A CB 1346 C CG . HIS A 175 ? 1.1787 0.7895 0.7622 -0.3092 0.0486 -0.1852 175 HIS A CG 1347 N ND1 . HIS A 175 ? 1.1764 0.8218 0.7656 -0.3198 0.0191 -0.1897 175 HIS A ND1 1348 C CD2 . HIS A 175 ? 1.1269 0.7567 0.7536 -0.3017 0.0536 -0.1749 175 HIS A CD2 1349 C CE1 . HIS A 175 ? 1.1277 0.8129 0.7650 -0.3175 0.0082 -0.1839 175 HIS A CE1 1350 N NE2 . HIS A 175 ? 1.0969 0.7730 0.7554 -0.3078 0.0294 -0.1752 175 HIS A NE2 1351 N N . SER A 176 ? 1.3377 0.8508 0.7593 -0.2975 0.0900 -0.2009 176 SER A N 1352 C CA . SER A 176 ? 1.3909 0.8675 0.7729 -0.2911 0.1179 -0.2103 176 SER A CA 1353 C C . SER A 176 ? 1.4422 0.8734 0.8075 -0.3003 0.1353 -0.2331 176 SER A C 1354 O O . SER A 176 ? 1.4423 0.8702 0.8208 -0.3169 0.1237 -0.2419 176 SER A O 1355 C CB . SER A 176 ? 1.4418 0.9181 0.7714 -0.2997 0.1100 -0.2145 176 SER A CB 1356 O OG . SER A 176 ? 1.4806 0.9336 0.7797 -0.2889 0.1399 -0.2192 176 SER A OG 1357 N N . VAL A 177 ? 1.4841 0.8804 0.8208 -0.2896 0.1637 -0.2432 177 VAL A N 1358 C CA . VAL A 177 ? 1.5381 0.8822 0.8588 -0.2925 0.1842 -0.2640 177 VAL A CA 1359 C C . VAL A 177 ? 1.5982 0.9158 0.8730 -0.3217 0.1732 -0.2908 177 VAL A C 1360 O O . VAL A 177 ? 1.6320 0.9086 0.8995 -0.3332 0.1805 -0.3080 177 VAL A O 1361 C CB . VAL A 177 ? 1.5760 0.8929 0.8812 -0.2684 0.2183 -0.2685 177 VAL A CB 1362 C CG1 . VAL A 177 ? 1.6430 0.8979 0.9257 -0.2695 0.2391 -0.2925 177 VAL A CG1 1363 C CG2 . VAL A 177 ? 1.5207 0.8642 0.8755 -0.2408 0.2285 -0.2433 177 VAL A CG2 1364 N N . SER A 178 ? 1.6090 0.9479 0.8510 -0.3348 0.1545 -0.2940 178 SER A N 1365 C CA . SER A 178 ? 1.6668 0.9853 0.8614 -0.3634 0.1412 -0.3197 178 SER A CA 1366 C C . SER A 178 ? 1.6492 1.0122 0.8363 -0.3796 0.1042 -0.3127 178 SER A C 1367 O O . SER A 178 ? 1.5923 0.9969 0.8069 -0.3671 0.0905 -0.2880 178 SER A O 1368 C CB . SER A 178 ? 1.7360 1.0120 0.8701 -0.3615 0.1664 -0.3418 178 SER A CB 1369 O OG . SER A 178 ? 1.7300 1.0305 0.8419 -0.3507 0.1689 -0.3297 178 SER A OG 1370 N N . THR A 179 ? 1.6990 1.0511 0.8485 -0.4072 0.0870 -0.3350 179 THR A N 1371 C CA . THR A 179 ? 1.6968 1.0877 0.8316 -0.4228 0.0497 -0.3311 179 THR A CA 1372 C C . THR A 179 ? 1.7173 1.1108 0.8038 -0.4140 0.0520 -0.3227 179 THR A C 1373 O O . THR A 179 ? 1.6899 1.1205 0.7787 -0.4120 0.0257 -0.3034 179 THR A O 1374 C CB . THR A 179 ? 1.7583 1.1361 0.8607 -0.4564 0.0312 -0.3597 179 THR A CB 1375 O OG1 . THR A 179 ? 1.8401 1.1656 0.8769 -0.4646 0.0534 -0.3857 179 THR A OG1 1376 C CG2 . THR A 179 ? 1.7380 1.1130 0.8867 -0.4700 0.0301 -0.3680 179 THR A CG2 1377 N N . ALA A 180 ? 1.7641 1.1169 0.8073 -0.4085 0.0848 -0.3372 180 ALA A N 1378 C CA . ALA A 180 ? 1.7964 1.1487 0.7896 -0.4019 0.0949 -0.3316 180 ALA A CA 1379 C C . ALA A 180 ? 1.7332 1.1156 0.7637 -0.3770 0.1019 -0.2990 180 ALA A C 1380 O O . ALA A 180 ? 1.7301 1.1365 0.7418 -0.3775 0.0854 -0.2805 180 ALA A O 1381 C CB . ALA A 180 ? 1.8607 1.1645 0.8061 -0.4000 0.1327 -0.3582 180 ALA A CB 1382 N N . GLU A 181 ? 1.6934 1.0727 0.7751 -0.3562 0.1250 -0.2914 181 GLU A N 1383 C CA . GLU A 181 ? 1.6333 1.0398 0.7512 -0.3334 0.1346 -0.2632 181 GLU A CA 1384 C C . GLU A 181 ? 1.5570 1.0057 0.7138 -0.3324 0.1007 -0.2368 181 GLU A C 1385 O O . GLU A 181 ? 1.5234 0.9936 0.6936 -0.3198 0.1017 -0.2135 181 GLU A O 1386 C CB . GLU A 181 ? 1.6106 1.0046 0.7733 -0.3112 0.1652 -0.2624 181 GLU A CB 1387 C CG . GLU A 181 ? 1.6795 1.0332 0.8079 -0.3040 0.2024 -0.2857 181 GLU A CG 1388 C CD . GLU A 181 ? 1.7309 1.0865 0.8051 -0.3055 0.2170 -0.2888 181 GLU A CD 1389 O OE1 . GLU A 181 ? 1.7083 1.0969 0.7940 -0.2974 0.2163 -0.2648 181 GLU A OE1 1390 O OE2 . GLU A 181 ? 1.8182 1.1414 0.8364 -0.3162 0.2299 -0.3158 181 GLU A OE2 1391 N N . GLN A 182 ? 1.5309 0.9917 0.7065 -0.3458 0.0715 -0.2416 182 GLN A N 1392 C CA . GLN A 182 ? 1.4762 0.9774 0.6837 -0.3448 0.0365 -0.2206 182 GLN A CA 1393 C C . GLN A 182 ? 1.5114 1.0202 0.6680 -0.3540 0.0133 -0.2127 182 GLN A C 1394 O O . GLN A 182 ? 1.4866 1.0169 0.6554 -0.3442 -0.0016 -0.1880 182 GLN A O 1395 C CB . GLN A 182 ? 1.4563 0.9744 0.7007 -0.3568 0.0129 -0.2300 182 GLN A CB 1396 C CG . GLN A 182 ? 1.4211 0.9826 0.6948 -0.3555 -0.0258 -0.2133 182 GLN A CG 1397 C CD . GLN A 182 ? 1.3833 0.9721 0.7164 -0.3591 -0.0393 -0.2176 182 GLN A CD 1398 O OE1 . GLN A 182 ? 1.3434 0.9365 0.7226 -0.3468 -0.0227 -0.2109 182 GLN A OE1 1399 N NE2 . GLN A 182 ? 1.4005 1.0116 0.7330 -0.3766 -0.0702 -0.2286 182 GLN A NE2 1400 N N . THR A 183 ? 1.5729 1.0611 0.6694 -0.3734 0.0096 -0.2332 183 THR A N 1401 C CA . THR A 183 ? 1.6173 1.1095 0.6563 -0.3837 -0.0128 -0.2253 183 THR A CA 1402 C C . THR A 183 ? 1.6219 1.1048 0.6300 -0.3735 0.0110 -0.2085 183 THR A C 1403 O O . THR A 183 ? 1.6200 1.1154 0.6096 -0.3729 -0.0087 -0.1855 183 THR A O 1404 C CB . THR A 183 ? 1.6973 1.1691 0.6723 -0.4089 -0.0216 -0.2529 183 THR A CB 1405 O OG1 . THR A 183 ? 1.7451 1.1785 0.6793 -0.4109 0.0185 -0.2742 183 THR A OG1 1406 C CG2 . THR A 183 ? 1.6880 1.1715 0.6947 -0.4233 -0.0446 -0.2710 183 THR A CG2 1407 N N . LYS A 184 ? 1.4189 0.9533 0.7648 -0.4071 -0.0100 -0.1705 184 LYS A N 1408 C CA . LYS A 184 ? 1.4322 0.9562 0.7692 -0.4165 0.0008 -0.1721 184 LYS A CA 1409 C C . LYS A 184 ? 1.4600 0.9635 0.7828 -0.4309 0.0180 -0.1764 184 LYS A C 1410 O O . LYS A 184 ? 1.4958 0.9676 0.7938 -0.4346 0.0347 -0.1767 184 LYS A O 1411 C CB . LYS A 184 ? 1.4122 0.9640 0.7630 -0.4244 -0.0065 -0.1745 184 LYS A CB 1412 C CG . LYS A 184 ? 1.4243 0.9860 0.7686 -0.4382 0.0046 -0.1790 184 LYS A CG 1413 C CD . LYS A 184 ? 1.4102 1.0133 0.7658 -0.4373 -0.0029 -0.1801 184 LYS A CD 1414 C CE . LYS A 184 ? 1.4197 1.0556 0.7723 -0.4577 0.0089 -0.1886 184 LYS A CE 1415 N NZ . LYS A 184 ? 1.4126 1.0955 0.7699 -0.4477 0.0032 -0.1880 184 LYS A NZ 1416 N N . LEU A 185 ? 1.4499 0.9667 0.7835 -0.4408 0.0161 -0.1805 185 LEU A N 1417 C CA . LEU A 185 ? 1.4762 0.9755 0.7952 -0.4594 0.0333 -0.1881 185 LEU A CA 1418 C C . LEU A 185 ? 1.5146 0.9646 0.8038 -0.4463 0.0480 -0.1849 185 LEU A C 1419 O O . LEU A 185 ? 1.5625 0.9700 0.8199 -0.4593 0.0707 -0.1900 185 LEU A O 1420 C CB . LEU A 185 ? 1.4526 0.9872 0.7925 -0.4724 0.0262 -0.1935 185 LEU A CB 1421 C CG . LEU A 185 ? 1.4257 1.0104 0.7861 -0.4805 0.0164 -0.1957 185 LEU A CG 1422 C CD1 . LEU A 185 ? 1.4100 1.0255 0.7854 -0.4876 0.0112 -0.1986 185 LEU A CD1 1423 C CD2 . LEU A 185 ? 1.4409 1.0425 0.7925 -0.5001 0.0283 -0.2042 185 LEU A CD2 1424 N N . TYR A 186 ? 1.5039 0.9599 0.7979 -0.4205 0.0376 -0.1774 186 TYR A N 1425 C CA . TYR A 186 ? 1.5438 0.9649 0.8083 -0.3988 0.0506 -0.1729 186 TYR A CA 1426 C C . TYR A 186 ? 1.5550 0.9802 0.8087 -0.3628 0.0460 -0.1621 186 TYR A C 1427 O O . TYR A 186 ? 1.5786 0.9919 0.8098 -0.3357 0.0535 -0.1567 186 TYR A O 1428 C CB . TYR A 186 ? 1.5286 0.9711 0.8069 -0.4007 0.0449 -0.1766 186 TYR A CB 1429 C CG . TYR A 186 ? 1.5036 0.9683 0.8040 -0.4328 0.0417 -0.1866 186 TYR A CG 1430 C CD1 . TYR A 186 ? 1.5364 0.9722 0.8165 -0.4556 0.0614 -0.1965 186 TYR A CD1 1431 C CD2 . TYR A 186 ? 1.4541 0.9682 0.7899 -0.4402 0.0213 -0.1867 186 TYR A CD2 1432 C CE1 . TYR A 186 ? 1.5107 0.9824 0.8119 -0.4834 0.0578 -0.2066 186 TYR A CE1 1433 C CE2 . TYR A 186 ? 1.4366 0.9766 0.7889 -0.4621 0.0189 -0.1934 186 TYR A CE2 1434 C CZ . TYR A 186 ? 1.4589 0.9856 0.7970 -0.4829 0.0357 -0.2035 186 TYR A CZ 1435 O OH . TYR A 186 ? 1.4342 1.0013 0.7895 -0.5033 0.0327 -0.2110 186 TYR A OH 1436 N N . GLY A 187 ? 1.5418 0.9890 0.8090 -0.3600 0.0344 -0.1595 187 GLY A N 1437 C CA . GLY A 187 ? 1.5520 1.0193 0.8127 -0.3288 0.0282 -0.1517 187 GLY A CA 1438 C C . GLY A 187 ? 1.5220 1.0501 0.8093 -0.3241 0.0091 -0.1548 187 GLY A C 1439 O O . GLY A 187 ? 1.4992 1.0424 0.8023 -0.3380 0.0041 -0.1600 187 GLY A O 1440 N N . SER A 188 ? 1.5203 1.0869 0.8107 -0.3076 -0.0005 -0.1530 188 SER A N 1441 C CA . SER A 188 ? 1.4995 1.1308 0.8117 -0.3115 -0.0166 -0.1598 188 SER A CA 1442 C C . SER A 188 ? 1.5189 1.1800 0.8203 -0.2864 -0.0132 -0.1572 188 SER A C 1443 O O . SER A 188 ? 1.5600 1.1826 0.8313 -0.2600 0.0030 -0.1483 188 SER A O 1444 C CB . SER A 188 ? 1.4906 1.1611 0.8072 -0.3076 -0.0263 -0.1628 188 SER A CB 1445 O OG . SER A 188 ? 1.5208 1.2045 0.8132 -0.2695 -0.0191 -0.1541 188 SER A OG 1446 N N . GLY A 189 ? 1.5002 1.2276 0.8210 -0.2954 -0.0263 -0.1656 189 GLY A N 1447 C CA . GLY A 189 ? 1.5152 1.2919 0.8293 -0.2716 -0.0255 -0.1648 189 GLY A CA 1448 C C . GLY A 189 ? 1.5042 1.2806 0.8336 -0.2935 -0.0277 -0.1702 189 GLY A C 1449 O O . GLY A 189 ? 1.4905 1.2233 0.8323 -0.3231 -0.0280 -0.1727 189 GLY A O 1450 N N . ASN A 190 ? 1.5131 1.3460 0.8409 -0.2764 -0.0293 -0.1717 190 ASN A N 1451 C CA . ASN A 190 ? 1.4988 1.3399 0.8401 -0.2944 -0.0313 -0.1767 190 ASN A CA 1452 C C . ASN A 190 ? 1.5209 1.2974 0.8393 -0.2742 -0.0152 -0.1687 190 ASN A C 1453 O O . ASN A 190 ? 1.5581 1.3367 0.8471 -0.2316 -0.0041 -0.1612 190 ASN A O 1454 C CB . ASN A 190 ? 1.4958 1.4346 0.8446 -0.2867 -0.0394 -0.1837 190 ASN A CB 1455 C CG . ASN A 190 ? 1.4757 1.4822 0.8422 -0.3162 -0.0522 -0.1966 190 ASN A CG 1456 O OD1 . ASN A 190 ? 1.4679 1.4411 0.8461 -0.3543 -0.0565 -0.2024 190 ASN A OD1 1457 N ND2 . ASN A 190 ? 1.4797 1.5838 0.8436 -0.2984 -0.0565 -0.2021 190 ASN A ND2 1458 N N . LYS A 191 ? 1.5017 1.2218 0.8286 -0.3036 -0.0119 -0.1709 191 LYS A N 1459 C CA . LYS A 191 ? 1.5281 1.1838 0.8309 -0.2954 0.0058 -0.1678 191 LYS A CA 1460 C C . LYS A 191 ? 1.5191 1.2031 0.8261 -0.2924 0.0054 -0.1715 191 LYS A C 1461 O O . LYS A 191 ? 1.4807 1.2130 0.8189 -0.3182 -0.0090 -0.1782 191 LYS A O 1462 C CB . LYS A 191 ? 1.5176 1.1223 0.8297 -0.3308 0.0091 -0.1717 191 LYS A CB 1463 C CG . LYS A 191 ? 1.5124 1.0966 0.8253 -0.3385 0.0077 -0.1695 191 LYS A CG 1464 C CD . LYS A 191 ? 1.5623 1.1076 0.8370 -0.3064 0.0232 -0.1608 191 LYS A CD 1465 C CE . LYS A 191 ? 1.5556 1.1512 0.8342 -0.2837 0.0121 -0.1565 191 LYS A CE 1466 N NZ . LYS A 191 ? 1.6053 1.1664 0.8436 -0.2465 0.0276 -0.1455 191 LYS A NZ 1467 N N . LEU A 192 ? 1.5569 1.2057 0.8271 -0.2600 0.0233 -0.1668 192 LEU A N 1468 C CA . LEU A 192 ? 1.5514 1.2205 0.8201 -0.2531 0.0255 -0.1703 192 LEU A CA 1469 C C . LEU A 192 ? 1.5903 1.1731 0.8258 -0.2554 0.0486 -0.1721 192 LEU A C 1470 O O . LEU A 192 ? 1.6391 1.1464 0.8346 -0.2440 0.0687 -0.1678 192 LEU A O 1471 C CB . LEU A 192 ? 1.5730 1.2997 0.8223 -0.2030 0.0260 -0.1641 192 LEU A CB 1472 C CG . LEU A 192 ? 1.5959 1.3395 0.8307 -0.1806 0.0328 -0.1653 192 LEU A CG 1473 C CD1 . LEU A 192 ? 1.5382 1.3475 0.8197 -0.2201 0.0143 -0.1762 192 LEU A CD1 1474 C CD2 . LEU A 192 ? 1.6322 1.4279 0.8358 -0.1182 0.0377 -0.1562 192 LEU A CD2 1475 N N . VAL A 193 ? 1.5665 1.1602 0.8157 -0.2740 0.0471 -0.1800 193 VAL A N 1476 C CA . VAL A 193 ? 1.6064 1.1277 0.8221 -0.2792 0.0700 -0.1857 193 VAL A CA 1477 C C . VAL A 193 ? 1.6048 1.1577 0.8173 -0.2621 0.0705 -0.1885 193 VAL A C 1478 O O . VAL A 193 ? 1.5453 1.1721 0.8010 -0.2798 0.0501 -0.1924 193 VAL A O 1479 C CB . VAL A 193 ? 1.5818 1.0825 0.8209 -0.3321 0.0688 -0.1965 193 VAL A CB 1480 C CG1 . VAL A 193 ? 1.6383 1.0703 0.8399 -0.3444 0.0947 -0.2067 193 VAL A CG1 1481 C CG2 . VAL A 193 ? 1.5738 1.0540 0.8177 -0.3471 0.0671 -0.1939 193 VAL A CG2 1482 N N . THR A 194 ? 1.6699 1.1621 0.8258 -0.2268 0.0960 -0.1862 194 THR A N 1483 C CA . THR A 194 ? 1.6787 1.1963 0.8230 -0.2019 0.0996 -0.1881 194 THR A CA 1484 C C . THR A 194 ? 1.7324 1.1625 0.8347 -0.2137 0.1268 -0.1984 194 THR A C 1485 O O . THR A 194 ? 1.7849 1.1203 0.8460 -0.2271 0.1511 -0.2020 194 THR A O 1486 C CB . THR A 194 ? 1.7223 1.2647 0.8292 -0.1330 0.1056 -0.1747 194 THR A CB 1487 O OG1 . THR A 194 ? 1.8241 1.2553 0.8527 -0.0951 0.1404 -0.1677 194 THR A OG1 1488 C CG2 . THR A 194 ? 1.6781 1.2978 0.8151 -0.1228 0.0844 -0.1668 194 THR A CG2 1489 N N . VAL A 195 ? 1.7164 1.1810 0.8271 -0.2113 0.1240 -0.2048 195 VAL A N 1490 C CA . VAL A 195 ? 1.7582 1.1571 0.8383 -0.2311 0.1463 -0.2186 195 VAL A CA 1491 C C . VAL A 195 ? 1.7868 1.2034 0.8420 -0.1896 0.1533 -0.2179 195 VAL A C 1492 O O . VAL A 195 ? 1.7216 1.2395 0.8233 -0.1861 0.1286 -0.2167 195 VAL A O 1493 C CB . VAL A 195 ? 1.6882 1.1275 0.8250 -0.2950 0.1298 -0.2326 195 VAL A CB 1494 C CG1 . VAL A 195 ? 1.7367 1.1192 0.8428 -0.3196 0.1531 -0.2501 195 VAL A CG1 1495 C CG2 . VAL A 195 ? 1.6552 1.0875 0.8164 -0.3309 0.1222 -0.2327 195 VAL A CG2 1496 N N . GLY A 196 ? 1.8854 1.1992 0.8623 -0.1598 0.1892 -0.2194 196 GLY A N 1497 C CA . GLY A 196 ? 1.9314 1.2479 0.8692 -0.1077 0.2011 -0.2166 196 GLY A CA 1498 C C . GLY A 196 ? 2.0187 1.2260 0.8929 -0.1174 0.2371 -0.2315 196 GLY A C 1499 O O . GLY A 196 ? 2.1194 1.1984 0.9176 -0.1115 0.2738 -0.2330 196 GLY A O 1500 N N . SER A 197 ? 1.9816 1.2383 0.8838 -0.1354 0.2281 -0.2436 197 SER A N 1501 C CA . SER A 197 ? 2.0635 1.2324 0.9067 -0.1412 0.2606 -0.2598 197 SER A CA 1502 C C . SER A 197 ? 2.0708 1.2946 0.9053 -0.0878 0.2569 -0.2550 197 SER A C 1503 O O . SER A 197 ? 1.9908 1.3390 0.8809 -0.0649 0.2246 -0.2436 197 SER A O 1504 C CB . SER A 197 ? 2.0120 1.1952 0.8999 -0.2221 0.2540 -0.2829 197 SER A CB 1505 O OG . SER A 197 ? 2.0201 1.2185 0.9046 -0.2277 0.2588 -0.2968 197 SER A OG 1506 N N . SER A 198 ? 2.1692 1.3012 0.9306 -0.0701 0.2917 -0.2653 198 SER A N 1507 C CA . SER A 198 ? 2.1868 1.3648 0.9322 -0.0168 0.2918 -0.2622 198 SER A CA 1508 C C . SER A 198 ? 2.0507 1.3903 0.8960 -0.0432 0.2475 -0.2650 198 SER A C 1509 O O . SER A 198 ? 2.0199 1.4573 0.8830 0.0051 0.2303 -0.2535 198 SER A O 1510 C CB . SER A 198 ? 2.3000 1.3585 0.9665 -0.0202 0.3329 -0.2807 198 SER A CB 1511 O OG . SER A 198 ? 2.4468 1.3410 1.0040 0.0095 0.3804 -0.2775 198 SER A OG 1512 N N . ASN A 199 ? 1.9736 1.3427 0.8796 -0.1193 0.2311 -0.2801 199 ASN A N 1513 C CA . ASN A 199 ? 1.8578 1.3623 0.8510 -0.1510 0.1936 -0.2829 199 ASN A CA 1514 C C . ASN A 199 ? 1.7550 1.3553 0.8202 -0.1686 0.1580 -0.2702 199 ASN A C 1515 O O . ASN A 199 ? 1.6724 1.3855 0.7991 -0.1825 0.1289 -0.2681 199 ASN A O 1516 C CB . ASN A 199 ? 1.8340 1.3257 0.8517 -0.2201 0.1952 -0.3045 199 ASN A CB 1517 C CG . ASN A 199 ? 1.9358 1.3308 0.8824 -0.2161 0.2322 -0.3225 199 ASN A CG 1518 O OD1 . ASN A 199 ? 2.0437 1.3468 0.9088 -0.1641 0.2635 -0.3186 199 ASN A OD1 1519 N ND2 . ASN A 199 ? 1.9107 1.3233 0.8822 -0.2701 0.2310 -0.3427 199 ASN A ND2 1520 N N . TYR A 200 ? 1.7666 1.3170 0.8192 -0.1697 0.1626 -0.2626 200 TYR A N 1521 C CA . TYR A 200 ? 1.6767 1.2887 0.7937 -0.2063 0.1341 -0.2566 200 TYR A CA 1522 C C . TYR A 200 ? 1.6861 1.3067 0.7921 -0.1666 0.1299 -0.2397 200 TYR A C 1523 O O . TYR A 200 ? 1.7698 1.3073 0.8101 -0.1243 0.1557 -0.2333 200 TYR A O 1524 C CB . TYR A 200 ? 1.6701 1.2200 0.7934 -0.2654 0.1419 -0.2690 200 TYR A CB 1525 C CG . TYR A 200 ? 1.5866 1.1875 0.7694 -0.3030 0.1161 -0.2637 200 TYR A CG 1526 C CD1 . TYR A 200 ? 1.5912 1.1629 0.7648 -0.2923 0.1165 -0.2534 200 TYR A CD1 1527 C CD2 . TYR A 200 ? 1.5074 1.1799 0.7496 -0.3465 0.0935 -0.2684 200 TYR A CD2 1528 C CE1 . TYR A 200 ? 1.5232 1.1356 0.7458 -0.3244 0.0948 -0.2491 200 TYR A CE1 1529 C CE2 . TYR A 200 ? 1.4463 1.1542 0.7326 -0.3754 0.0735 -0.2625 200 TYR A CE2 1530 C CZ . TYR A 200 ? 1.4540 1.1311 0.7304 -0.3646 0.0742 -0.2535 200 TYR A CZ 1531 O OH . TYR A 200 ? 1.3998 1.1071 0.7151 -0.3906 0.0559 -0.2480 200 TYR A OH 1532 N N . GLN A 201 ? 1.6055 1.3232 0.7719 -0.1825 0.0992 -0.2330 201 GLN A N 1533 C CA . GLN A 201 ? 1.6022 1.3591 0.7677 -0.1476 0.0905 -0.2192 201 GLN A CA 1534 C C . GLN A 201 ? 1.5186 1.3451 0.7498 -0.1943 0.0616 -0.2185 201 GLN A C 1535 O O . GLN A 201 ? 1.4594 1.3765 0.7355 -0.2161 0.0408 -0.2215 201 GLN A O 1536 C CB . GLN A 201 ? 1.6147 1.4552 0.7678 -0.0912 0.0870 -0.2131 201 GLN A CB 1537 C CG . GLN A 201 ? 1.6539 1.5112 0.7713 -0.0289 0.0925 -0.1988 201 GLN A CG 1538 C CD . GLN A 201 ? 1.6753 1.6210 0.7736 0.0323 0.0924 -0.1941 201 GLN A CD 1539 O OE1 . GLN A 201 ? 1.7505 1.6394 0.7900 0.0797 0.1167 -0.1922 201 GLN A OE1 1540 N NE2 . GLN A 201 ? 1.6119 1.6990 0.7563 0.0300 0.0666 -0.1938 201 GLN A NE2 1541 N N . GLN A 202 ? 1.5231 1.3009 0.7542 -0.2104 0.0627 -0.2150 202 GLN A N 1542 C CA . GLN A 202 ? 1.4582 1.2849 0.7417 -0.2518 0.0392 -0.2141 202 GLN A CA 1543 C C . GLN A 202 ? 1.4734 1.2585 0.7455 -0.2470 0.0419 -0.2070 202 GLN A C 1544 O O . GLN A 202 ? 1.5328 1.2395 0.7565 -0.2189 0.0636 -0.2030 202 GLN A O 1545 C CB . GLN A 202 ? 1.4182 1.2340 0.7350 -0.3070 0.0327 -0.2227 202 GLN A CB 1546 C CG . GLN A 202 ? 1.3765 1.2685 0.7279 -0.3264 0.0178 -0.2271 202 GLN A CG 1547 C CD . GLN A 202 ? 1.3275 1.2306 0.7176 -0.3768 0.0050 -0.2294 202 GLN A CD 1548 O OE1 . GLN A 202 ? 1.3048 1.2085 0.7113 -0.3943 -0.0045 -0.2247 202 GLN A OE1 1549 N NE2 . GLN A 202 ? 1.3144 1.2266 0.7153 -0.3966 0.0056 -0.2359 202 GLN A NE2 1550 N N . SER A 203 ? 1.4246 1.2575 0.7372 -0.2757 0.0218 -0.2057 203 SER A N 1551 C CA . SER A 203 ? 1.4334 1.2373 0.7420 -0.2757 0.0211 -0.1999 203 SER A CA 1552 C C . SER A 203 ? 1.3861 1.2006 0.7351 -0.3248 0.0054 -0.2027 203 SER A C 1553 O O . SER A 203 ? 1.3475 1.2059 0.7274 -0.3543 -0.0072 -0.2069 203 SER A O 1554 C CB . SER A 203 ? 1.4399 1.3045 0.7403 -0.2371 0.0155 -0.1930 203 SER A CB 1555 O OG . SER A 203 ? 1.5046 1.3435 0.7551 -0.1805 0.0344 -0.1866 203 SER A OG 1556 N N . PHE A 204 ? 1.3975 1.1680 0.7408 -0.3302 0.0080 -0.1992 204 PHE A N 1557 C CA . PHE A 204 ? 1.3648 1.1299 0.7365 -0.3697 -0.0027 -0.2006 204 PHE A CA 1558 C C . PHE A 204 ? 1.3665 1.1217 0.7360 -0.3651 -0.0062 -0.1955 204 PHE A C 1559 O O . PHE A 204 ? 1.3965 1.0958 0.7415 -0.3526 0.0065 -0.1925 204 PHE A O 1560 C CB . PHE A 204 ? 1.3742 1.0849 0.7417 -0.3925 0.0080 -0.2057 204 PHE A CB 1561 C CG . PHE A 204 ? 1.3733 1.0966 0.7452 -0.4021 0.0110 -0.2124 204 PHE A CG 1562 C CD1 . PHE A 204 ? 1.3348 1.1067 0.7385 -0.4263 -0.0033 -0.2135 204 PHE A CD1 1563 C CD2 . PHE A 204 ? 1.4216 1.1032 0.7601 -0.3859 0.0303 -0.2175 204 PHE A CD2 1564 C CE1 . PHE A 204 ? 1.3329 1.1213 0.7413 -0.4341 -0.0010 -0.2193 204 PHE A CE1 1565 C CE2 . PHE A 204 ? 1.4219 1.1172 0.7639 -0.3952 0.0333 -0.2251 204 PHE A CE2 1566 C CZ . PHE A 204 ? 1.3738 1.1276 0.7539 -0.4192 0.0163 -0.2259 204 PHE A CZ 1567 N N . VAL A 205 ? 1.3425 1.1504 0.7340 -0.3781 -0.0217 -0.1959 205 VAL A N 1568 C CA . VAL A 205 ? 1.3354 1.1389 0.7291 -0.3821 -0.0270 -0.1934 205 VAL A CA 1569 C C . VAL A 205 ? 1.3124 1.0933 0.7239 -0.4179 -0.0328 -0.1946 205 VAL A C 1570 O O . VAL A 205 ? 1.2957 1.0954 0.7215 -0.4396 -0.0381 -0.1971 205 VAL A O 1571 C CB . VAL A 205 ? 1.3276 1.2048 0.7285 -0.3785 -0.0376 -0.1964 205 VAL A CB 1572 C CG1 . VAL A 205 ? 1.3287 1.2013 0.7270 -0.3789 -0.0411 -0.1953 205 VAL A CG1 1573 C CG2 . VAL A 205 ? 1.3484 1.2706 0.7329 -0.3387 -0.0331 -0.1950 205 VAL A CG2 1574 N N . PRO A 206 ? 1.3133 1.0542 0.7203 -0.4205 -0.0306 -0.1917 206 PRO A N 1575 C CA . PRO A 206 ? 1.2983 1.0206 0.7166 -0.4456 -0.0345 -0.1912 206 PRO A CA 1576 C C . PRO A 206 ? 1.2905 1.0320 0.7152 -0.4628 -0.0441 -0.1919 206 PRO A C 1577 O O . PRO A 206 ? 1.2908 1.0693 0.7149 -0.4626 -0.0486 -0.1958 206 PRO A O 1578 C CB . PRO A 206 ? 1.3082 0.9882 0.7158 -0.4392 -0.0272 -0.1889 206 PRO A CB 1579 C CG . PRO A 206 ? 1.3264 1.0053 0.7187 -0.4147 -0.0239 -0.1867 206 PRO A CG 1580 C CD . PRO A 206 ? 1.3341 1.0462 0.7218 -0.3978 -0.0231 -0.1878 206 PRO A CD 1581 N N . SER A 207 ? 1.2869 1.0036 0.7123 -0.4772 -0.0451 -0.1890 207 SER A N 1582 C CA . SER A 207 ? 1.2906 1.0035 0.7098 -0.4948 -0.0487 -0.1893 207 SER A CA 1583 C C . SER A 207 ? 1.2930 0.9663 0.7036 -0.4946 -0.0464 -0.1832 207 SER A C 1584 O O . SER A 207 ? 1.2934 0.9562 0.7007 -0.4991 -0.0444 -0.1782 207 SER A O 1585 C CB . SER A 207 ? 1.2950 1.0270 0.7156 -0.5130 -0.0493 -0.1908 207 SER A CB 1586 O OG . SER A 207 ? 1.2877 1.0124 0.7142 -0.5105 -0.0469 -0.1859 207 SER A OG 1587 N N . PRO A 208 ? 1.2931 0.9490 0.6980 -0.4858 -0.0464 -0.1828 208 PRO A N 1588 C CA . PRO A 208 ? 1.3022 0.9272 0.6968 -0.4813 -0.0442 -0.1772 208 PRO A CA 1589 C C . PRO A 208 ? 1.3303 0.9270 0.7022 -0.4925 -0.0419 -0.1755 208 PRO A C 1590 O O . PRO A 208 ? 1.3367 0.9377 0.7007 -0.5105 -0.0418 -0.1821 208 PRO A O 1591 C CB . PRO A 208 ? 1.3017 0.9201 0.6958 -0.4696 -0.0445 -0.1786 208 PRO A CB 1592 C CG . PRO A 208 ? 1.2996 0.9405 0.6957 -0.4710 -0.0474 -0.1847 208 PRO A CG 1593 C CD . PRO A 208 ? 1.2918 0.9613 0.6968 -0.4767 -0.0481 -0.1871 208 PRO A CD 1594 N N . GLY A 209 ? 1.3481 0.9161 0.7043 -0.4818 -0.0379 -0.1675 209 GLY A N 1595 C CA . GLY A 209 ? 1.3939 0.9171 0.7154 -0.4866 -0.0303 -0.1629 209 GLY A CA 1596 C C . GLY A 209 ? 1.4098 0.9206 0.7172 -0.4650 -0.0253 -0.1500 209 GLY A C 1597 O O . GLY A 209 ? 1.3785 0.9284 0.7083 -0.4544 -0.0289 -0.1474 209 GLY A O 1598 N N . ALA A 210 ? 1.4662 0.9231 0.7312 -0.4580 -0.0149 -0.1425 210 ALA A N 1599 C CA . ALA A 210 ? 1.4935 0.9391 0.7357 -0.4265 -0.0085 -0.1276 210 ALA A CA 1600 C C . ALA A 210 ? 1.5025 0.9576 0.7382 -0.4236 -0.0044 -0.1186 210 ALA A C 1601 O O . ALA A 210 ? 1.5379 0.9528 0.7473 -0.4414 0.0040 -0.1177 210 ALA A O 1602 C CB . ALA A 210 ? 1.5616 0.9342 0.7496 -0.4126 0.0045 -0.1214 210 ALA A CB 1603 N N . ARG A 211 ? 1.4733 0.9850 0.7311 -0.4041 -0.0093 -0.1134 211 ARG A N 1604 C CA . ARG A 211 ? 1.4859 1.0158 0.7350 -0.3927 -0.0051 -0.1028 211 ARG A CA 1605 C C . ARG A 211 ? 1.5248 1.0552 0.7405 -0.3487 0.0027 -0.0864 211 ARG A C 1606 O O . ARG A 211 ? 1.5313 1.0666 0.7428 -0.3294 0.0019 -0.0860 211 ARG A O 1607 C CB . ARG A 211 ? 1.4277 1.0345 0.7252 -0.4042 -0.0152 -0.1116 211 ARG A CB 1608 C CG . ARG A 211 ? 1.4007 1.0126 0.7246 -0.4380 -0.0208 -0.1242 211 ARG A CG 1609 C CD . ARG A 211 ? 1.3727 0.9916 0.7209 -0.4501 -0.0274 -0.1371 211 ARG A CD 1610 N NE . ARG A 211 ? 1.3572 0.9848 0.7243 -0.4738 -0.0316 -0.1473 211 ARG A NE 1611 C CZ . ARG A 211 ? 1.3371 0.9748 0.7227 -0.4809 -0.0361 -0.1573 211 ARG A CZ 1612 N NH1 . ARG A 211 ? 1.3320 0.9671 0.7208 -0.4711 -0.0368 -0.1591 211 ARG A NH1 1613 N NH2 . ARG A 211 ? 1.3264 0.9791 0.7243 -0.4951 -0.0390 -0.1647 211 ARG A NH2 1614 N N . PRO A 212 ? 1.5567 1.0876 0.7466 -0.3289 0.0107 -0.0719 212 PRO A N 1615 C CA . PRO A 212 ? 1.5941 1.1394 0.7496 -0.2778 0.0185 -0.0544 212 PRO A CA 1616 C C . PRO A 212 ? 1.5338 1.1886 0.7324 -0.2654 0.0071 -0.0613 212 PRO A C 1617 O O . PRO A 212 ? 1.4727 1.1894 0.7201 -0.2946 -0.0031 -0.0759 212 PRO A O 1618 C CB . PRO A 212 ? 1.6378 1.1658 0.7592 -0.2627 0.0295 -0.0381 212 PRO A CB 1619 C CG . PRO A 212 ? 1.5900 1.1398 0.7525 -0.3083 0.0210 -0.0514 212 PRO A CG 1620 C CD . PRO A 212 ? 1.5641 1.0846 0.7507 -0.3481 0.0141 -0.0696 212 PRO A CD 1621 N N . GLN A 213 ? 1.5578 1.2356 0.7338 -0.2236 0.0109 -0.0520 213 GLN A N 1622 C CA . GLN A 213 ? 1.5099 1.2982 0.7228 -0.2165 0.0020 -0.0614 213 GLN A CA 1623 C C . GLN A 213 ? 1.4897 1.3728 0.7199 -0.2093 -0.0001 -0.0607 213 GLN A C 1624 O O . GLN A 213 ? 1.5324 1.4296 0.7255 -0.1653 0.0081 -0.0416 213 GLN A O 1625 C CB . GLN A 213 ? 1.5440 1.3433 0.7254 -0.1701 0.0070 -0.0514 213 GLN A CB 1626 C CG . GLN A 213 ? 1.5435 1.2846 0.7254 -0.1848 0.0052 -0.0596 213 GLN A CG 1627 C CD . GLN A 213 ? 1.5677 1.3364 0.7257 -0.1409 0.0086 -0.0526 213 GLN A CD 1628 O OE1 . GLN A 213 ? 1.5870 1.4249 0.7266 -0.0958 0.0124 -0.0410 213 GLN A OE1 1629 N NE2 . GLN A 213 ? 1.5664 1.2888 0.7239 -0.1515 0.0072 -0.0597 213 GLN A NE2 1630 N N . VAL A 214 ? 1.4338 1.3778 0.7155 -0.2518 -0.0091 -0.0816 214 VAL A N 1631 C CA . VAL A 214 ? 1.4111 1.4590 0.7155 -0.2549 -0.0113 -0.0881 214 VAL A CA 1632 C C . VAL A 214 ? 1.3802 1.5247 0.7160 -0.2711 -0.0152 -0.1082 214 VAL A C 1633 O O . VAL A 214 ? 1.3592 1.4787 0.7170 -0.3062 -0.0179 -0.1243 214 VAL A O 1634 C CB . VAL A 214 ? 1.3810 1.4137 0.7121 -0.2964 -0.0146 -0.0988 214 VAL A CB 1635 C CG1 . VAL A 214 ? 1.3501 1.4935 0.7084 -0.3088 -0.0164 -0.1119 214 VAL A CG1 1636 C CG2 . VAL A 214 ? 1.4214 1.3722 0.7192 -0.2834 -0.0091 -0.0799 214 VAL A CG2 1637 N N . ASN A 215 ? 1.3877 1.6447 0.7213 -0.2455 -0.0137 -0.1074 215 ASN A N 1638 C CA . ASN A 215 ? 1.3672 1.7296 0.7215 -0.2571 -0.0146 -0.1259 215 ASN A CA 1639 C C . ASN A 215 ? 1.3821 1.7062 0.7239 -0.2432 -0.0145 -0.1227 215 ASN A C 1640 O O . ASN A 215 ? 1.3590 1.7377 0.7217 -0.2701 -0.0149 -0.1419 215 ASN A O 1641 C CB . ASN A 215 ? 1.3250 1.7220 0.7199 -0.3234 -0.0151 -0.1569 215 ASN A CB 1642 C CG . ASN A 215 ? 1.3108 1.7675 0.7190 -0.3387 -0.0144 -0.1645 215 ASN A CG 1643 O OD1 . ASN A 215 ? 1.3226 1.8618 0.7191 -0.3030 -0.0139 -0.1541 215 ASN A OD1 1644 N ND2 . ASN A 215 ? 1.2893 1.7074 0.7193 -0.3888 -0.0133 -0.1824 215 ASN A ND2 1645 N N . GLY A 216 ? 1.4263 1.6545 0.7301 -0.2037 -0.0120 -0.0996 216 GLY A N 1646 C CA . GLY A 216 ? 1.4437 1.6189 0.7320 -0.1905 -0.0113 -0.0960 216 GLY A CA 1647 C C . GLY A 216 ? 1.4257 1.5036 0.7315 -0.2352 -0.0147 -0.1069 216 GLY A C 1648 O O . GLY A 216 ? 1.4357 1.4671 0.7303 -0.2280 -0.0145 -0.1053 216 GLY A O 1649 N N . LEU A 217 ? 1.4019 1.4526 0.7325 -0.2770 -0.0173 -0.1174 217 LEU A N 1650 C CA . LEU A 217 ? 1.3848 1.3619 0.7333 -0.3168 -0.0202 -0.1287 217 LEU A CA 1651 C C . LEU A 217 ? 1.4013 1.2908 0.7399 -0.3247 -0.0205 -0.1209 217 LEU A C 1652 O O . LEU A 217 ? 1.4040 1.3038 0.7396 -0.3220 -0.0193 -0.1153 217 LEU A O 1653 C CB . LEU A 217 ? 1.3459 1.3741 0.7301 -0.3624 -0.0204 -0.1520 217 LEU A CB 1654 C CG . LEU A 217 ? 1.3363 1.4606 0.7298 -0.3678 -0.0174 -0.1651 217 LEU A CG 1655 C CD1 . LEU A 217 ? 1.3139 1.4817 0.7315 -0.4181 -0.0121 -0.1897 217 LEU A CD1 1656 C CD2 . LEU A 217 ? 1.3448 1.4416 0.7310 -0.3612 -0.0175 -0.1646 217 LEU A CD2 1657 N N . SER A 218 ? 1.1063 0.6050 0.6371 -0.4308 0.2608 -0.1767 218 SER A N 1658 C CA . SER A 218 ? 1.1076 0.6257 0.6383 -0.4347 0.2425 -0.1772 218 SER A CA 1659 C C . SER A 218 ? 1.1111 0.6448 0.6165 -0.4312 0.2071 -0.1665 218 SER A C 1660 O O . SER A 218 ? 1.1010 0.6532 0.6051 -0.4351 0.1892 -0.1681 218 SER A O 1661 C CB . SER A 218 ? 1.1553 0.6540 0.6599 -0.4607 0.2587 -0.1954 218 SER A CB 1662 O OG . SER A 218 ? 1.1505 0.6429 0.6912 -0.4606 0.2857 -0.2050 218 SER A OG 1663 N N . GLY A 219 ? 1.1222 0.6479 0.6088 -0.4243 0.1969 -0.1565 219 GLY A N 1664 C CA . GLY A 219 ? 1.1259 0.6660 0.5966 -0.4159 0.1617 -0.1444 219 GLY A CA 1665 C C . GLY A 219 ? 1.0742 0.6482 0.5951 -0.3898 0.1481 -0.1330 219 GLY A C 1666 O O . GLY A 219 ? 1.0447 0.6256 0.6047 -0.3785 0.1658 -0.1319 219 GLY A O 1667 N N . ARG A 220 ? 1.0692 0.6645 0.5895 -0.3806 0.1161 -0.1252 220 ARG A N 1668 C CA . ARG A 220 ? 1.0246 0.6526 0.5896 -0.3570 0.1021 -0.1158 220 ARG A CA 1669 C C . ARG A 220 ? 1.0391 0.6709 0.5900 -0.3458 0.0721 -0.1050 220 ARG A C 1670 O O . ARG A 220 ? 1.0731 0.6908 0.5832 -0.3560 0.0536 -0.1047 220 ARG A O 1671 C CB . ARG A 220 ? 0.9985 0.6601 0.5958 -0.3556 0.0948 -0.1213 220 ARG A CB 1672 C CG . ARG A 220 ? 0.9825 0.6407 0.5976 -0.3653 0.1221 -0.1306 220 ARG A CG 1673 C CD . ARG A 220 ? 0.9403 0.6005 0.5926 -0.3512 0.1415 -0.1249 220 ARG A CD 1674 N NE . ARG A 220 ? 0.9293 0.5873 0.6018 -0.3586 0.1627 -0.1322 220 ARG A NE 1675 C CZ . ARG A 220 ? 0.9604 0.5902 0.6250 -0.3698 0.1885 -0.1401 220 ARG A CZ 1676 N NH1 . ARG A 220 ? 0.9941 0.5958 0.6300 -0.3768 0.1992 -0.1432 220 ARG A NH1 1677 N NH2 . ARG A 220 ? 0.9579 0.5865 0.6443 -0.3748 0.2045 -0.1458 220 ARG A NH2 1678 N N . ILE A 221 ? 1.0064 0.6561 0.5910 -0.3249 0.0667 -0.0961 221 ILE A N 1679 C CA . ILE A 221 ? 1.0141 0.6723 0.5967 -0.3109 0.0373 -0.0867 221 ILE A CA 1680 C C . ILE A 221 ? 0.9683 0.6709 0.6019 -0.2935 0.0231 -0.0865 221 ILE A C 1681 O O . ILE A 221 ? 0.9304 0.6488 0.6006 -0.2829 0.0373 -0.0849 221 ILE A O 1682 C CB . ILE A 221 ? 1.0197 0.6543 0.5907 -0.3033 0.0442 -0.0772 221 ILE A CB 1683 C CG1 . ILE A 221 ? 1.0736 0.6638 0.5877 -0.3231 0.0545 -0.0782 221 ILE A CG1 1684 C CG2 . ILE A 221 ? 1.0124 0.6582 0.5919 -0.2855 0.0155 -0.0674 221 ILE A CG2 1685 C CD1 . ILE A 221 ? 1.0813 0.6460 0.5825 -0.3201 0.0672 -0.0715 221 ILE A CD1 1686 N N . ASP A 222 ? 0.9804 0.7037 0.6167 -0.2918 -0.0047 -0.0892 222 ASP A N 1687 C CA . ASP A 222 ? 0.9450 0.7110 0.6290 -0.2751 -0.0207 -0.0905 222 ASP A CA 1688 C C . ASP A 222 ? 0.9307 0.6955 0.6240 -0.2561 -0.0334 -0.0804 222 ASP A C 1689 O O . ASP A 222 ? 0.9660 0.7028 0.6246 -0.2562 -0.0467 -0.0730 222 ASP A O 1690 C CB . ASP A 222 ? 0.9648 0.7539 0.6516 -0.2778 -0.0489 -0.0980 222 ASP A CB 1691 C CG . ASP A 222 ? 0.9762 0.7773 0.6656 -0.2950 -0.0380 -0.1104 222 ASP A CG 1692 O OD1 . ASP A 222 ? 1.0032 0.7768 0.6646 -0.3112 -0.0161 -0.1124 222 ASP A OD1 1693 O OD2 . ASP A 222 ? 0.9556 0.7939 0.6761 -0.2931 -0.0509 -0.1194 222 ASP A OD2 1694 N N . PHE A 223 ? 0.8871 0.6806 0.6248 -0.2415 -0.0290 -0.0802 223 PHE A N 1695 C CA . PHE A 223 ? 0.8780 0.6769 0.6317 -0.2229 -0.0425 -0.0732 223 PHE A CA 1696 C C . PHE A 223 ? 0.8552 0.6982 0.6520 -0.2109 -0.0632 -0.0805 223 PHE A C 1697 O O . PHE A 223 ? 0.8358 0.7101 0.6650 -0.2127 -0.0532 -0.0888 223 PHE A O 1698 C CB . PHE A 223 ? 0.8457 0.6412 0.6157 -0.2162 -0.0187 -0.0680 223 PHE A CB 1699 C CG . PHE A 223 ? 0.8648 0.6184 0.5981 -0.2245 -0.0007 -0.0616 223 PHE A CG 1700 C CD1 . PHE A 223 ? 0.8947 0.6189 0.5976 -0.2218 -0.0110 -0.0536 223 PHE A CD1 1701 C CD2 . PHE A 223 ? 0.8663 0.6092 0.5967 -0.2354 0.0272 -0.0643 223 PHE A CD2 1702 C CE1 . PHE A 223 ? 0.9177 0.6045 0.5872 -0.2316 0.0079 -0.0497 223 PHE A CE1 1703 C CE2 . PHE A 223 ? 0.8842 0.5913 0.5856 -0.2435 0.0453 -0.0613 223 PHE A CE2 1704 C CZ . PHE A 223 ? 0.9117 0.5917 0.5822 -0.2424 0.0366 -0.0546 223 PHE A CZ 1705 N N . HIS A 224 ? 0.8773 0.7209 0.6740 -0.1993 -0.0917 -0.0780 224 HIS A N 1706 C CA . HIS A 224 ? 0.8604 0.7453 0.7009 -0.1863 -0.1140 -0.0868 224 HIS A CA 1707 C C . HIS A 224 ? 0.8421 0.7295 0.7037 -0.1666 -0.1237 -0.0817 224 HIS A C 1708 O O . HIS A 224 ? 0.8467 0.6979 0.6789 -0.1637 -0.1229 -0.0699 224 HIS A O 1709 C CB . HIS A 224 ? 0.9088 0.7936 0.7349 -0.1887 -0.1451 -0.0901 224 HIS A CB 1710 C CG . HIS A 224 ? 0.9417 0.8227 0.7438 -0.2091 -0.1388 -0.0961 224 HIS A CG 1711 N ND1 . HIS A 224 ? 0.9815 0.8198 0.7285 -0.2246 -0.1318 -0.0889 224 HIS A ND1 1712 C CD2 . HIS A 224 ? 0.9334 0.8478 0.7587 -0.2178 -0.1378 -0.1099 224 HIS A CD2 1713 C CE1 . HIS A 224 ? 0.9925 0.8379 0.7305 -0.2414 -0.1267 -0.0981 224 HIS A CE1 1714 N NE2 . HIS A 224 ? 0.9705 0.8615 0.7553 -0.2376 -0.1304 -0.1105 224 HIS A NE2 1715 N N . TRP A 225 ? 0.8076 0.7372 0.7196 -0.1544 -0.1328 -0.0919 225 TRP A N 1716 C CA . TRP A 225 ? 0.7880 0.7239 0.7259 -0.1361 -0.1394 -0.0899 225 TRP A CA 1717 C C . TRP A 225 ? 0.7798 0.7573 0.7682 -0.1217 -0.1623 -0.1033 225 TRP A C 1718 O O . TRP A 225 ? 0.7595 0.7737 0.7756 -0.1267 -0.1646 -0.1173 225 TRP A O 1719 C CB . TRP A 225 ? 0.7471 0.6904 0.6998 -0.1365 -0.1094 -0.0887 225 TRP A CB 1720 C CG . TRP A 225 ? 0.7083 0.6934 0.6963 -0.1427 -0.0952 -0.1011 225 TRP A CG 1721 C CD1 . TRP A 225 ? 0.6991 0.6864 0.6768 -0.1590 -0.0775 -0.1034 225 TRP A CD1 1722 C CD2 . TRP A 225 ? 0.6760 0.7049 0.7136 -0.1342 -0.0967 -0.1137 225 TRP A CD2 1723 N NE1 . TRP A 225 ? 0.6689 0.6967 0.6840 -0.1618 -0.0683 -0.1151 225 TRP A NE1 1724 C CE2 . TRP A 225 ? 0.6502 0.7052 0.7021 -0.1475 -0.0792 -0.1222 225 TRP A CE2 1725 C CE3 . TRP A 225 ? 0.6645 0.7118 0.7357 -0.1175 -0.1101 -0.1194 225 TRP A CE3 1726 C CZ2 . TRP A 225 ? 0.6216 0.7207 0.7170 -0.1464 -0.0740 -0.1362 225 TRP A CZ2 1727 C CZ3 . TRP A 225 ? 0.6315 0.7247 0.7493 -0.1156 -0.1044 -0.1349 225 TRP A CZ3 1728 C CH2 . TRP A 225 ? 0.6155 0.7343 0.7436 -0.1309 -0.0863 -0.1431 225 TRP A CH2 1729 N N . LEU A 226 ? 0.8004 0.7716 0.8021 -0.1043 -0.1779 -0.1001 226 LEU A N 1730 C CA . LEU A 226 ? 0.7842 0.7960 0.8420 -0.0884 -0.1954 -0.1146 226 LEU A CA 1731 C C . LEU A 226 ? 0.7760 0.7825 0.8522 -0.0727 -0.1934 -0.1118 226 LEU A C 1732 O O . LEU A 226 ? 0.7873 0.7524 0.8280 -0.0718 -0.1881 -0.0965 226 LEU A O 1733 C CB . LEU A 226 ? 0.8197 0.8341 0.8829 -0.0807 -0.2329 -0.1183 226 LEU A CB 1734 C CG . LEU A 226 ? 0.8700 0.8440 0.9078 -0.0678 -0.2639 -0.1047 226 LEU A CG 1735 C CD1 . LEU A 226 ? 0.9095 0.8274 0.8757 -0.0815 -0.2594 -0.0852 226 LEU A CD1 1736 C CD2 . LEU A 226 ? 0.8621 0.8314 0.9250 -0.0487 -0.2683 -0.1031 226 LEU A CD2 1737 N N . MET A 227 ? 0.7524 0.8020 0.8849 -0.0617 -0.1967 -0.1282 227 MET A N 1738 C CA . MET A 227 ? 0.7415 0.7916 0.8992 -0.0459 -0.1972 -0.1296 227 MET A CA 1739 C C . MET A 227 ? 0.7691 0.8126 0.9447 -0.0270 -0.2333 -0.1315 227 MET A C 1740 O O . MET A 227 ? 0.7618 0.8409 0.9786 -0.0204 -0.2521 -0.1474 227 MET A O 1741 C CB . MET A 227 ? 0.7014 0.8017 0.9102 -0.0461 -0.1783 -0.1482 227 MET A CB 1742 C CG . MET A 227 ? 0.6793 0.7862 0.8728 -0.0638 -0.1446 -0.1456 227 MET A CG 1743 S SD . MET A 227 ? 0.6849 0.7484 0.8377 -0.0659 -0.1234 -0.1257 227 MET A SD 1744 C CE . MET A 227 ? 0.6715 0.7565 0.8680 -0.0509 -0.1216 -0.1363 227 MET A CE 1745 N N . LEU A 228 ? 0.7989 0.7959 0.9440 -0.0187 -0.2434 -0.1154 228 LEU A N 1746 C CA . LEU A 228 ? 0.8364 0.8167 0.9915 -0.0004 -0.2793 -0.1131 228 LEU A CA 1747 C C . LEU A 228 ? 0.8219 0.8171 1.0243 0.0173 -0.2794 -0.1231 228 LEU A C 1748 O O . LEU A 228 ? 0.8207 0.7945 1.0086 0.0171 -0.2609 -0.1155 228 LEU A O 1749 C CB . LEU A 228 ? 0.8852 0.8005 0.9739 -0.0036 -0.2916 -0.0888 228 LEU A CB 1750 C CG . LEU A 228 ? 0.9353 0.8235 1.0217 0.0131 -0.3333 -0.0819 228 LEU A CG 1751 C CD1 . LEU A 228 ? 0.9446 0.8634 1.0572 0.0170 -0.3623 -0.0928 228 LEU A CD1 1752 C CD2 . LEU A 228 ? 0.9887 0.8089 1.0005 0.0050 -0.3400 -0.0569 228 LEU A CD2 1753 N N . ASN A 229 ? 0.8192 0.8522 1.0800 0.0322 -0.3000 -0.1416 229 ASN A N 1754 C CA . ASN A 229 ? 0.8096 0.8624 1.1235 0.0492 -0.3005 -0.1558 229 ASN A CA 1755 C C . ASN A 229 ? 0.8544 0.8561 1.1499 0.0647 -0.3196 -0.1407 229 ASN A C 1756 O O . ASN A 229 ? 0.8892 0.8439 1.1378 0.0652 -0.3419 -0.1211 229 ASN A O 1757 C CB . ASN A 229 ? 0.7989 0.9052 1.1830 0.0612 -0.3196 -0.1815 229 ASN A CB 1758 C CG . ASN A 229 ? 0.7525 0.9157 1.1668 0.0460 -0.2942 -0.2018 229 ASN A CG 1759 O OD1 . ASN A 229 ? 0.7214 0.8939 1.1265 0.0327 -0.2605 -0.2026 229 ASN A OD1 1760 N ND2 . ASN A 229 ? 0.7539 0.9553 1.2048 0.0474 -0.3111 -0.2185 229 ASN A ND2 1761 N N . PRO A 230 ? 0.8535 0.8627 1.1838 0.0759 -0.3103 -0.1499 230 PRO A N 1762 C CA . PRO A 230 ? 0.9054 0.8689 1.2270 0.0919 -0.3282 -0.1387 230 PRO A CA 1763 C C . PRO A 230 ? 0.9678 0.9142 1.3016 0.1103 -0.3738 -0.1357 230 PRO A C 1764 O O . PRO A 230 ? 0.9474 0.9380 1.3386 0.1211 -0.3906 -0.1556 230 PRO A O 1765 C CB . PRO A 230 ? 0.8680 0.8642 1.2465 0.1011 -0.3112 -0.1594 230 PRO A CB 1766 C CG . PRO A 230 ? 0.8134 0.8497 1.1954 0.0821 -0.2739 -0.1693 230 PRO A CG 1767 C CD . PRO A 230 ? 0.8079 0.8657 1.1811 0.0710 -0.2792 -0.1705 230 PRO A CD 1768 N N . ASN A 231 ? 1.0543 0.9367 1.3338 0.1128 -0.3933 -0.1109 231 ASN A N 1769 C CA . ASN A 231 ? 1.1471 1.0008 1.4239 0.1288 -0.4400 -0.1018 231 ASN A CA 1770 C C . ASN A 231 ? 1.1349 1.0013 1.3975 0.1220 -0.4616 -0.0998 231 ASN A C 1771 O O . ASN A 231 ? 1.1816 1.0275 1.4423 0.1346 -0.5030 -0.0925 231 ASN A O 1772 C CB . ASN A 231 ? 1.2037 1.0800 1.5566 0.1561 -0.4625 -0.1205 231 ASN A CB 1773 C CG . ASN A 231 ? 1.3022 1.1384 1.6517 0.1665 -0.4579 -0.1137 231 ASN A CG 1774 O OD1 . ASN A 231 ? 1.3190 1.1008 1.6034 0.1553 -0.4470 -0.0911 231 ASN A OD1 1775 N ND2 . ASN A 231 ? 1.4057 1.2693 1.8276 0.1873 -0.4652 -0.1349 231 ASN A ND2 1776 N N . ASP A 232 ? 1.0701 0.9677 1.3212 0.1017 -0.4350 -0.1057 232 ASP A N 1777 C CA . ASP A 232 ? 1.0724 0.9804 1.3048 0.0917 -0.4511 -0.1040 232 ASP A CA 1778 C C . ASP A 232 ? 1.1039 0.9498 1.2465 0.0746 -0.4524 -0.0759 232 ASP A C 1779 O O . ASP A 232 ? 1.1048 0.9158 1.2042 0.0639 -0.4263 -0.0628 232 ASP A O 1780 C CB . ASP A 232 ? 1.0104 0.9784 1.2718 0.0768 -0.4212 -0.1240 232 ASP A CB 1781 C CG . ASP A 232 ? 1.0216 1.0125 1.2823 0.0693 -0.4402 -0.1291 232 ASP A CG 1782 O OD1 . ASP A 232 ? 1.0676 1.0325 1.3096 0.0767 -0.4789 -0.1185 232 ASP A OD1 1783 O OD2 . ASP A 232 ? 0.9841 1.0188 1.2623 0.0551 -0.4166 -0.1439 232 ASP A OD2 1784 N N . THR A 233 ? 1.1325 0.9660 1.2482 0.0711 -0.4826 -0.0681 233 THR A N 1785 C CA . THR A 233 ? 1.1742 0.9495 1.2032 0.0530 -0.4864 -0.0434 233 THR A CA 1786 C C . THR A 233 ? 1.1629 0.9621 1.1714 0.0314 -0.4742 -0.0484 233 THR A C 1787 O O . THR A 233 ? 1.1439 0.9935 1.1992 0.0352 -0.4859 -0.0663 233 THR A O 1788 C CB . THR A 233 ? 1.2437 0.9724 1.2451 0.0649 -0.5361 -0.0262 233 THR A CB 1789 O OG1 . THR A 233 ? 1.2538 0.9625 1.2826 0.0871 -0.5497 -0.0236 233 THR A OG1 1790 C CG2 . THR A 233 ? 1.2964 0.9594 1.2014 0.0435 -0.5369 -0.0002 233 THR A CG2 1791 N N . VAL A 234 ? 1.1708 0.9336 1.1111 0.0085 -0.4498 -0.0339 234 VAL A N 1792 C CA . VAL A 234 ? 1.1569 0.9321 1.0684 -0.0140 -0.4364 -0.0366 234 VAL A CA 1793 C C . VAL A 234 ? 1.2161 0.9316 1.0445 -0.0299 -0.4519 -0.0151 234 VAL A C 1794 O O . VAL A 234 ? 1.2334 0.8944 1.0122 -0.0335 -0.4485 0.0028 234 VAL A O 1795 C CB . VAL A 234 ? 1.1054 0.8994 1.0172 -0.0299 -0.3863 -0.0434 234 VAL A CB 1796 C CG1 . VAL A 234 ? 1.1155 0.8616 0.9824 -0.0366 -0.3618 -0.0277 234 VAL A CG1 1797 C CG2 . VAL A 234 ? 1.1055 0.9102 0.9901 -0.0523 -0.3735 -0.0470 234 VAL A CG2 1798 N N . THR A 235 ? 1.2372 0.9634 1.0494 -0.0412 -0.4679 -0.0181 235 THR A N 1799 C CA . THR A 235 ? 1.3074 0.9799 1.0395 -0.0583 -0.4850 0.0005 235 THR A CA 1800 C C . THR A 235 ? 1.3060 0.9859 1.0036 -0.0856 -0.4600 -0.0045 235 THR A C 1801 O O . THR A 235 ? 1.2583 0.9909 0.9993 -0.0879 -0.4509 -0.0231 235 THR A O 1802 C CB . THR A 235 ? 1.3617 1.0278 1.0962 -0.0453 -0.5404 0.0054 235 THR A CB 1803 O OG1 . THR A 235 ? 1.3625 1.0297 1.1436 -0.0171 -0.5635 0.0061 235 THR A OG1 1804 C CG2 . THR A 235 ? 1.4427 1.0421 1.0855 -0.0628 -0.5602 0.0287 235 THR A CG2 1805 N N . PHE A 236 ? 1.3547 0.9802 0.9741 -0.1071 -0.4482 0.0112 236 PHE A N 1806 C CA . PHE A 236 ? 1.3617 0.9846 0.9408 -0.1346 -0.4229 0.0075 236 PHE A CA 1807 C C . PHE A 236 ? 1.4460 1.0281 0.9553 -0.1510 -0.4521 0.0197 236 PHE A C 1808 O O . PHE A 236 ? 1.5079 1.0309 0.9523 -0.1602 -0.4569 0.0381 236 PHE A O 1809 C CB . PHE A 236 ? 1.3481 0.9433 0.8949 -0.1494 -0.3769 0.0123 236 PHE A CB 1810 C CG . PHE A 236 ? 1.2712 0.9057 0.8790 -0.1380 -0.3448 0.0004 236 PHE A CG 1811 C CD1 . PHE A 236 ? 1.2207 0.9023 0.8664 -0.1438 -0.3207 -0.0164 236 PHE A CD1 1812 C CD2 . PHE A 236 ? 1.2565 0.8788 0.8808 -0.1230 -0.3387 0.0064 236 PHE A CD2 1813 C CE1 . PHE A 236 ? 1.1523 0.8675 0.8490 -0.1349 -0.2927 -0.0259 236 PHE A CE1 1814 C CE2 . PHE A 236 ? 1.1938 0.8521 0.8710 -0.1141 -0.3101 -0.0044 236 PHE A CE2 1815 C CZ . PHE A 236 ? 1.1435 0.8479 0.8557 -0.1202 -0.2877 -0.0200 236 PHE A CZ 1816 N N . SER A 237 ? 1.4523 1.0655 0.9733 -0.1562 -0.4711 0.0091 237 SER A N 1817 C CA . SER A 237 ? 1.5271 1.1066 0.9795 -0.1766 -0.4943 0.0181 237 SER A CA 1818 C C . SER A 237 ? 1.5161 1.0978 0.9370 -0.2057 -0.4557 0.0087 237 SER A C 1819 O O . SER A 237 ? 1.4521 1.0841 0.9210 -0.2067 -0.4381 -0.0099 237 SER A O 1820 C CB . SER A 237 ? 1.5473 1.1588 1.0308 -0.1648 -0.5428 0.0118 237 SER A CB 1821 O OG . SER A 237 ? 1.5135 1.1742 1.0258 -0.1758 -0.5314 -0.0085 237 SER A OG 1822 N N . PHE A 238 ? 1.5685 1.0948 0.9095 -0.2299 -0.4417 0.0209 238 PHE A N 1823 C CA . PHE A 238 ? 1.5597 1.0826 0.8703 -0.2577 -0.4011 0.0115 238 PHE A CA 1824 C C . PHE A 238 ? 1.6384 1.1088 0.8575 -0.2874 -0.4076 0.0210 238 PHE A C 1825 O O . PHE A 238 ? 1.6932 1.1109 0.8554 -0.2916 -0.4240 0.0394 238 PHE A O 1826 C CB . PHE A 238 ? 1.5181 1.0368 0.8426 -0.2581 -0.3525 0.0093 238 PHE A CB 1827 C CG . PHE A 238 ? 1.5507 1.0227 0.8451 -0.2524 -0.3512 0.0265 238 PHE A CG 1828 C CD1 . PHE A 238 ? 1.5330 1.0156 0.8722 -0.2241 -0.3705 0.0321 238 PHE A CD1 1829 C CD2 . PHE A 238 ? 1.5936 1.0117 0.8166 -0.2763 -0.3286 0.0352 238 PHE A CD2 1830 C CE1 . PHE A 238 ? 1.5569 0.9954 0.8686 -0.2197 -0.3685 0.0474 238 PHE A CE1 1831 C CE2 . PHE A 238 ? 1.6208 0.9959 0.8161 -0.2729 -0.3258 0.0500 238 PHE A CE2 1832 C CZ . PHE A 238 ? 1.6007 0.9852 0.8396 -0.2444 -0.3461 0.0567 238 PHE A CZ 1833 N N . ASN A 239 ? 1.6382 1.1230 0.8429 -0.3093 -0.3938 0.0077 239 ASN A N 1834 C CA . ASN A 239 ? 1.7131 1.1546 0.8333 -0.3414 -0.3949 0.0120 239 ASN A CA 1835 C C . ASN A 239 ? 1.6995 1.1159 0.7861 -0.3655 -0.3411 0.0061 239 ASN A C 1836 O O . ASN A 239 ? 1.7555 1.1338 0.7710 -0.3951 -0.3325 0.0071 239 ASN A O 1837 C CB . ASN A 239 ? 1.7284 1.2027 0.8549 -0.3515 -0.4152 -0.0012 239 ASN A CB 1838 C CG . ASN A 239 ? 1.8275 1.2578 0.8665 -0.3787 -0.4391 0.0074 239 ASN A CG 1839 O OD1 . ASN A 239 ? 1.8916 1.2648 0.8586 -0.3967 -0.4297 0.0205 239 ASN A OD1 1840 N ND2 . ASN A 239 ? 1.8472 1.3046 0.8912 -0.3835 -0.4697 -0.0007 239 ASN A ND2 1841 N N . GLY A 240 ? 1.6253 1.0636 0.7642 -0.3529 -0.3055 -0.0007 240 GLY A N 1842 C CA . GLY A 240 ? 1.6061 1.0270 0.7275 -0.3713 -0.2544 -0.0080 240 GLY A CA 1843 C C . GLY A 240 ? 1.5156 0.9855 0.7099 -0.3603 -0.2233 -0.0240 240 GLY A C 1844 O O . GLY A 240 ? 1.4738 0.9904 0.7301 -0.3394 -0.2397 -0.0292 240 GLY A O 1845 N N . ALA A 241 ? 1.4933 0.9515 0.6797 -0.3752 -0.1785 -0.0320 241 ALA A N 1846 C CA . ALA A 241 ? 1.4191 0.9161 0.6668 -0.3681 -0.1462 -0.0460 241 ALA A CA 1847 C C . ALA A 241 ? 1.3526 0.8810 0.6657 -0.3378 -0.1493 -0.0420 241 ALA A C 1848 O O . ALA A 241 ? 1.3050 0.8783 0.6770 -0.3257 -0.1444 -0.0515 241 ALA A O 1849 C CB . ALA A 241 ? 1.4088 0.9400 0.6764 -0.3759 -0.1514 -0.0606 241 ALA A CB 1850 N N . PHE A 242 ? 1.3584 0.8613 0.6582 -0.3275 -0.1557 -0.0283 242 PHE A N 1851 C CA . PHE A 242 ? 1.3080 0.8363 0.6626 -0.2989 -0.1657 -0.0233 242 PHE A CA 1852 C C . PHE A 242 ? 1.2847 0.7921 0.6394 -0.2960 -0.1359 -0.0182 242 PHE A C 1853 O O . PHE A 242 ? 1.3220 0.7830 0.6222 -0.3093 -0.1299 -0.0099 242 PHE A O 1854 C CB . PHE A 242 ? 1.3446 0.8638 0.6872 -0.2860 -0.2122 -0.0112 242 PHE A CB 1855 C CG . PHE A 242 ? 1.3038 0.8406 0.6954 -0.2577 -0.2241 -0.0056 242 PHE A CG 1856 C CD1 . PHE A 242 ? 1.2457 0.8369 0.7088 -0.2381 -0.2301 -0.0157 242 PHE A CD1 1857 C CD2 . PHE A 242 ? 1.3336 0.8314 0.6982 -0.2524 -0.2289 0.0089 242 PHE A CD2 1858 C CE1 . PHE A 242 ? 1.2160 0.8238 0.7242 -0.2134 -0.2398 -0.0125 242 PHE A CE1 1859 C CE2 . PHE A 242 ? 1.3017 0.8149 0.7117 -0.2271 -0.2392 0.0128 242 PHE A CE2 1860 C CZ . PHE A 242 ? 1.2408 0.8096 0.7232 -0.2074 -0.2446 0.0017 242 PHE A CZ 1861 N N . ILE A 243 ? 1.2102 0.7523 0.6246 -0.2805 -0.1168 -0.0241 243 ILE A N 1862 C CA . ILE A 243 ? 1.1836 0.7147 0.6094 -0.2747 -0.0908 -0.0206 243 ILE A CA 1863 C C . ILE A 243 ? 1.1632 0.7056 0.6203 -0.2500 -0.1125 -0.0123 243 ILE A C 1864 O O . ILE A 243 ? 1.1211 0.7066 0.6352 -0.2322 -0.1190 -0.0176 243 ILE A O 1865 C CB . ILE A 243 ? 1.1293 0.6905 0.6006 -0.2734 -0.0570 -0.0318 243 ILE A CB 1866 C CG1 . ILE A 243 ? 1.1537 0.7049 0.6000 -0.2966 -0.0352 -0.0419 243 ILE A CG1 1867 C CG2 . ILE A 243 ? 1.1051 0.6577 0.5908 -0.2666 -0.0326 -0.0286 243 ILE A CG2 1868 C CD1 . ILE A 243 ? 1.2041 0.7063 0.5905 -0.3184 -0.0174 -0.0402 243 ILE A CD1 1869 N N . ALA A 244 ? 1.1979 0.7000 0.6166 -0.2505 -0.1222 0.0001 244 ALA A N 1870 C CA . ALA A 244 ? 1.1897 0.6942 0.6295 -0.2284 -0.1490 0.0089 244 ALA A CA 1871 C C . ALA A 244 ? 1.1329 0.6516 0.6145 -0.2138 -0.1285 0.0081 244 ALA A C 1872 O O . ALA A 244 ? 1.1336 0.6337 0.6006 -0.2240 -0.0978 0.0077 244 ALA A O 1873 C CB . ALA A 244 ? 1.2627 0.7128 0.6390 -0.2362 -0.1707 0.0239 244 ALA A CB 1874 N N . PRO A 245 ? 1.0886 0.6404 0.6228 -0.1905 -0.1457 0.0066 245 PRO A N 1875 C CA . PRO A 245 ? 1.0469 0.6103 0.6171 -0.1774 -0.1289 0.0061 245 PRO A CA 1876 C C . PRO A 245 ? 1.0844 0.6012 0.6184 -0.1777 -0.1321 0.0184 245 PRO A C 1877 O O . PRO A 245 ? 1.1294 0.6177 0.6337 -0.1752 -0.1619 0.0283 245 PRO A O 1878 C CB . PRO A 245 ? 1.0074 0.6160 0.6378 -0.1547 -0.1501 0.0000 245 PRO A CB 1879 C CG . PRO A 245 ? 1.0489 0.6520 0.6641 -0.1523 -0.1873 0.0030 245 PRO A CG 1880 C CD . PRO A 245 ? 1.0874 0.6660 0.6494 -0.1758 -0.1819 0.0045 245 PRO A CD 1881 N N . ASP A 246 ? 1.0678 0.5766 0.6047 -0.1811 -0.1023 0.0177 246 ASP A N 1882 C CA . ASP A 246 ? 1.0947 0.5645 0.6061 -0.1807 -0.1014 0.0272 246 ASP A CA 1883 C C . ASP A 246 ? 1.0591 0.5539 0.6228 -0.1576 -0.1083 0.0258 246 ASP A C 1884 O O . ASP A 246 ? 1.0892 0.5572 0.6407 -0.1496 -0.1262 0.0345 246 ASP A O 1885 C CB . ASP A 246 ? 1.0985 0.5456 0.5844 -0.1989 -0.0642 0.0253 246 ASP A CB 1886 C CG . ASP A 246 ? 1.1380 0.5406 0.5902 -0.2029 -0.0616 0.0345 246 ASP A CG 1887 O OD1 . ASP A 246 ? 1.2016 0.5633 0.6068 -0.2076 -0.0852 0.0461 246 ASP A OD1 1888 O OD2 . ASP A 246 ? 1.1142 0.5218 0.5863 -0.2017 -0.0370 0.0305 246 ASP A OD2 1889 N N . ARG A 247 ? 0.9966 0.5406 0.6164 -0.1481 -0.0936 0.0147 247 ARG A N 1890 C CA . ARG A 247 ? 0.9601 0.5323 0.6309 -0.1284 -0.0971 0.0107 247 ARG A CA 1891 C C . ARG A 247 ? 0.9067 0.5330 0.6320 -0.1150 -0.1083 0.0001 247 ARG A C 1892 O O . ARG A 247 ? 0.8842 0.5321 0.6145 -0.1223 -0.1035 -0.0056 247 ARG A O 1893 C CB . ARG A 247 ? 0.9379 0.5179 0.6253 -0.1312 -0.0646 0.0068 247 ARG A CB 1894 C CG . ARG A 247 ? 0.9866 0.5185 0.6298 -0.1435 -0.0500 0.0143 247 ARG A CG 1895 C CD . ARG A 247 ? 0.9595 0.5056 0.6206 -0.1497 -0.0155 0.0076 247 ARG A CD 1896 N NE . ARG A 247 ? 0.9541 0.5009 0.6355 -0.1415 -0.0080 0.0071 247 ARG A NE 1897 C CZ . ARG A 247 ? 0.9203 0.4895 0.6309 -0.1415 0.0166 0.0003 247 ARG A CZ 1898 N NH1 . ARG A 247 ? 0.8871 0.4795 0.6124 -0.1479 0.0355 -0.0058 247 ARG A NH1 1899 N NH2 . ARG A 247 ? 0.9130 0.4809 0.6390 -0.1350 0.0212 -0.0004 247 ARG A NH2 1900 N N . ALA A 248 ? 0.8802 0.5273 0.6462 -0.0966 -0.1218 -0.0036 248 ALA A N 1901 C CA . ALA A 248 ? 0.8333 0.5337 0.6554 -0.0842 -0.1296 -0.0161 248 ALA A CA 1902 C C . ALA A 248 ? 0.7799 0.5107 0.6417 -0.0793 -0.1062 -0.0238 248 ALA A C 1903 O O . ALA A 248 ? 0.7806 0.4916 0.6348 -0.0785 -0.0946 -0.0196 248 ALA A O 1904 C CB . ALA A 248 ? 0.8543 0.5576 0.6968 -0.0668 -0.1638 -0.0171 248 ALA A CB 1905 N N . SER A 249 ? 0.7359 0.5146 0.6385 -0.0772 -0.0997 -0.0353 249 SER A N 1906 C CA . SER A 249 ? 0.6894 0.4994 0.6279 -0.0742 -0.0789 -0.0426 249 SER A CA 1907 C C . SER A 249 ? 0.6597 0.5059 0.6477 -0.0589 -0.0919 -0.0543 249 SER A C 1908 O O . SER A 249 ? 0.6645 0.5302 0.6716 -0.0530 -0.1115 -0.0613 249 SER A O 1909 C CB . SER A 249 ? 0.6590 0.4938 0.6041 -0.0857 -0.0589 -0.0465 249 SER A CB 1910 O OG . SER A 249 ? 0.6830 0.4849 0.5862 -0.0995 -0.0463 -0.0380 249 SER A OG 1911 N N . PHE A 250 ? 0.6348 0.4911 0.6448 -0.0532 -0.0803 -0.0579 250 PHE A N 1912 C CA . PHE A 250 ? 0.6105 0.5044 0.6701 -0.0408 -0.0868 -0.0719 250 PHE A CA 1913 C C . PHE A 250 ? 0.5752 0.5035 0.6589 -0.0463 -0.0625 -0.0792 250 PHE A C 1914 O O . PHE A 250 ? 0.5733 0.4879 0.6382 -0.0542 -0.0433 -0.0719 250 PHE A O 1915 C CB . PHE A 250 ? 0.6284 0.4991 0.6921 -0.0279 -0.0994 -0.0704 250 PHE A CB 1916 C CG . PHE A 250 ? 0.6693 0.5098 0.7160 -0.0199 -0.1288 -0.0641 250 PHE A CG 1917 C CD1 . PHE A 250 ? 0.7084 0.4988 0.7005 -0.0279 -0.1332 -0.0477 250 PHE A CD1 1918 C CD2 . PHE A 250 ? 0.6698 0.5322 0.7551 -0.0050 -0.1526 -0.0750 250 PHE A CD2 1919 C CE1 . PHE A 250 ? 0.7553 0.5155 0.7269 -0.0219 -0.1626 -0.0402 250 PHE A CE1 1920 C CE2 . PHE A 250 ? 0.7131 0.5472 0.7835 0.0033 -0.1831 -0.0681 250 PHE A CE2 1921 C CZ . PHE A 250 ? 0.7556 0.5372 0.7666 -0.0054 -0.1890 -0.0496 250 PHE A CZ 1922 N N . LEU A 251 ? 0.5522 0.5256 0.6774 -0.0431 -0.0636 -0.0941 251 LEU A N 1923 C CA . LEU A 251 ? 0.5224 0.5297 0.6674 -0.0506 -0.0423 -0.1009 251 LEU A CA 1924 C C . LEU A 251 ? 0.5182 0.5326 0.6837 -0.0440 -0.0356 -0.1068 251 LEU A C 1925 O O . LEU A 251 ? 0.5293 0.5487 0.7193 -0.0319 -0.0489 -0.1160 251 LEU A O 1926 C CB . LEU A 251 ? 0.5010 0.5527 0.6772 -0.0538 -0.0439 -0.1152 251 LEU A CB 1927 C CG . LEU A 251 ? 0.5134 0.5637 0.6766 -0.0596 -0.0534 -0.1133 251 LEU A CG 1928 C CD1 . LEU A 251 ? 0.4887 0.5850 0.6818 -0.0670 -0.0479 -0.1281 251 LEU A CD1 1929 C CD2 . LEU A 251 ? 0.5252 0.5427 0.6447 -0.0706 -0.0429 -0.0972 251 LEU A CD2 1930 N N . ARG A 252 ? 0.5055 0.5210 0.6628 -0.0519 -0.0156 -0.1022 252 ARG A N 1931 C CA . ARG A 252 ? 0.5011 0.5187 0.6709 -0.0481 -0.0074 -0.1061 252 ARG A CA 1932 C C . ARG A 252 ? 0.4847 0.5466 0.6947 -0.0469 -0.0035 -0.1237 252 ARG A C 1933 O O . ARG A 252 ? 0.4864 0.5511 0.7152 -0.0395 -0.0046 -0.1321 252 ARG A O 1934 C CB . ARG A 252 ? 0.4977 0.5033 0.6461 -0.0576 0.0115 -0.0957 252 ARG A CB 1935 C CG . ARG A 252 ? 0.5266 0.4859 0.6376 -0.0591 0.0117 -0.0814 252 ARG A CG 1936 C CD . ARG A 252 ? 0.5266 0.4795 0.6245 -0.0679 0.0310 -0.0743 252 ARG A CD 1937 N NE . ARG A 252 ? 0.5534 0.4636 0.6164 -0.0716 0.0338 -0.0631 252 ARG A NE 1938 C CZ . ARG A 252 ? 0.5791 0.4580 0.6273 -0.0688 0.0327 -0.0600 252 ARG A CZ 1939 N NH1 . ARG A 252 ? 0.5783 0.4626 0.6453 -0.0608 0.0281 -0.0670 252 ARG A NH1 1940 N NH2 . ARG A 252 ? 0.6064 0.4471 0.6201 -0.0753 0.0374 -0.0508 252 ARG A NH2 1941 N N . GLY A 253 ? 0.4706 0.5661 0.6925 -0.0559 0.0026 -0.1301 253 GLY A N 1942 C CA . GLY A 253 ? 0.4564 0.5948 0.7116 -0.0594 0.0105 -0.1472 253 GLY A CA 1943 C C . GLY A 253 ? 0.4497 0.6186 0.7076 -0.0735 0.0201 -0.1506 253 GLY A C 1944 O O . GLY A 253 ? 0.4534 0.6326 0.7173 -0.0749 0.0126 -0.1551 253 GLY A O 1945 N N . LYS A 254 ? 0.4428 0.6254 0.6955 -0.0847 0.0359 -0.1486 254 LYS A N 1946 C CA . LYS A 254 ? 0.4435 0.6520 0.6952 -0.1000 0.0458 -0.1505 254 LYS A CA 1947 C C . LYS A 254 ? 0.4155 0.6082 0.6381 -0.1094 0.0564 -0.1326 254 LYS A C 1948 O O . LYS A 254 ? 0.3976 0.5766 0.6117 -0.1070 0.0610 -0.1252 254 LYS A O 1949 C CB . LYS A 254 ? 0.4629 0.7116 0.7416 -0.1070 0.0539 -0.1695 254 LYS A CB 1950 C CG . LYS A 254 ? 0.5008 0.7746 0.8157 -0.1005 0.0456 -0.1914 254 LYS A CG 1951 C CD . LYS A 254 ? 0.5163 0.8263 0.8589 -0.1065 0.0559 -0.2121 254 LYS A CD 1952 C CE . LYS A 254 ? 0.5415 0.8790 0.9269 -0.0994 0.0486 -0.2370 254 LYS A CE 1953 N NZ . LYS A 254 ? 0.5607 0.9231 0.9550 -0.1098 0.0494 -0.2458 254 LYS A NZ 1954 N N . SER A 255 ? 0.3919 0.5870 0.6019 -0.1200 0.0599 -0.1265 255 SER A N 1955 C CA . SER A 255 ? 0.3874 0.5719 0.5752 -0.1297 0.0694 -0.1112 255 SER A CA 1956 C C . SER A 255 ? 0.3978 0.5986 0.5814 -0.1444 0.0745 -0.1120 255 SER A C 1957 O O . SER A 255 ? 0.3886 0.6114 0.5875 -0.1480 0.0720 -0.1259 255 SER A O 1958 C CB . SER A 255 ? 0.3899 0.5357 0.5553 -0.1236 0.0674 -0.0953 255 SER A CB 1959 O OG . SER A 255 ? 0.3923 0.5250 0.5519 -0.1208 0.0592 -0.0956 255 SER A OG 1960 N N . MET A 256 ? 0.4184 0.6082 0.5827 -0.1532 0.0814 -0.0976 256 MET A N 1961 C CA . MET A 256 ? 0.4527 0.6457 0.6063 -0.1668 0.0856 -0.0939 256 MET A CA 1962 C C . MET A 256 ? 0.4460 0.6050 0.5787 -0.1652 0.0865 -0.0763 256 MET A C 1963 O O . MET A 256 ? 0.4384 0.5791 0.5648 -0.1585 0.0875 -0.0660 256 MET A O 1964 C CB . MET A 256 ? 0.5035 0.7172 0.6535 -0.1820 0.0937 -0.0939 256 MET A CB 1965 C CG . MET A 256 ? 0.5592 0.7945 0.7113 -0.1978 0.0981 -0.1040 256 MET A CG 1966 S SD . MET A 256 ? 0.6458 0.8840 0.7746 -0.2202 0.1074 -0.0932 256 MET A SD 1967 C CE . MET A 256 ? 0.6055 0.8346 0.7254 -0.2154 0.1065 -0.0793 256 MET A CE 1968 N N . GLY A 257 ? 0.4374 0.5890 0.5614 -0.1722 0.0871 -0.0745 257 GLY A N 1969 C CA . GLY A 257 ? 0.4400 0.5595 0.5458 -0.1721 0.0894 -0.0601 257 GLY A CA 1970 C C . GLY A 257 ? 0.4395 0.5569 0.5336 -0.1866 0.0961 -0.0518 257 GLY A C 1971 O O . GLY A 257 ? 0.4420 0.5792 0.5381 -0.1988 0.0982 -0.0596 257 GLY A O 1972 N N . ILE A 258 ? 0.4324 0.5253 0.5154 -0.1854 0.0993 -0.0366 258 ILE A N 1973 C CA . ILE A 258 ? 0.4421 0.5248 0.5126 -0.1974 0.1040 -0.0261 258 ILE A CA 1974 C C . ILE A 258 ? 0.4548 0.5031 0.5162 -0.1940 0.1067 -0.0162 258 ILE A C 1975 O O . ILE A 258 ? 0.4533 0.4853 0.5168 -0.1827 0.1061 -0.0157 258 ILE A O 1976 C CB . ILE A 258 ? 0.4464 0.5348 0.5143 -0.2013 0.1043 -0.0160 258 ILE A CB 1977 C CG1 . ILE A 258 ? 0.4361 0.5095 0.5094 -0.1876 0.1023 -0.0074 258 ILE A CG1 1978 C CG2 . ILE A 258 ? 0.4408 0.5635 0.5155 -0.2079 0.1039 -0.0274 258 ILE A CG2 1979 C CD1 . ILE A 258 ? 0.4456 0.5183 0.5152 -0.1911 0.1004 0.0058 258 ILE A CD1 1980 N N . GLN A 259 ? 0.4692 0.5058 0.5200 -0.2053 0.1106 -0.0092 259 GLN A N 1981 C CA . GLN A 259 ? 0.4824 0.4858 0.5264 -0.2036 0.1145 0.0005 259 GLN A CA 1982 C C . GLN A 259 ? 0.4998 0.4922 0.5413 -0.2057 0.1143 0.0162 259 GLN A C 1983 O O . GLN A 259 ? 0.5186 0.5232 0.5529 -0.2171 0.1131 0.0200 259 GLN A O 1984 C CB . GLN A 259 ? 0.4911 0.4867 0.5255 -0.2151 0.1186 -0.0043 259 GLN A CB 1985 C CG . GLN A 259 ? 0.4760 0.4854 0.5136 -0.2137 0.1156 -0.0198 259 GLN A CG 1986 C CD . GLN A 259 ? 0.4860 0.4877 0.5149 -0.2251 0.1190 -0.0254 259 GLN A CD 1987 O OE1 . GLN A 259 ? 0.4892 0.5000 0.5140 -0.2394 0.1224 -0.0267 259 GLN A OE1 1988 N NE2 . GLN A 259 ? 0.4886 0.4734 0.5129 -0.2204 0.1187 -0.0295 259 GLN A NE2 1989 N N . SER A 260 ? 0.5085 0.4779 0.5558 -0.1955 0.1151 0.0247 260 SER A N 1990 C CA . SER A 260 ? 0.5287 0.4887 0.5782 -0.1944 0.1115 0.0398 260 SER A CA 1991 C C . SER A 260 ? 0.5350 0.4656 0.5946 -0.1844 0.1141 0.0468 260 SER A C 1992 O O . SER A 260 ? 0.5263 0.4484 0.5935 -0.1758 0.1192 0.0391 260 SER A O 1993 C CB . SER A 260 ? 0.5207 0.5036 0.5781 -0.1890 0.1052 0.0406 260 SER A CB 1994 O OG . SER A 260 ? 0.5381 0.5140 0.5964 -0.1887 0.0989 0.0556 260 SER A OG 1995 N N . GLY A 261 ? 0.5566 0.4711 0.6163 -0.1861 0.1104 0.0611 261 GLY A N 1996 C CA . GLY A 261 ? 0.5718 0.4604 0.6478 -0.1753 0.1116 0.0676 261 GLY A CA 1997 C C . GLY A 261 ? 0.5731 0.4660 0.6638 -0.1664 0.1015 0.0788 261 GLY A C 1998 O O . GLY A 261 ? 0.5973 0.4692 0.7036 -0.1586 0.0996 0.0866 261 GLY A O 1999 N N . VAL A 262 ? 0.5559 0.4765 0.6439 -0.1675 0.0948 0.0785 262 VAL A N 2000 C CA . VAL A 262 ? 0.5567 0.4849 0.6571 -0.1604 0.0837 0.0884 262 VAL A CA 2001 C C . VAL A 262 ? 0.5352 0.4852 0.6510 -0.1509 0.0848 0.0778 262 VAL A C 2002 O O . VAL A 262 ? 0.5058 0.4675 0.6175 -0.1516 0.0921 0.0644 262 VAL A O 2003 C CB . VAL A 262 ? 0.5720 0.5102 0.6525 -0.1730 0.0728 0.1008 262 VAL A CB 2004 C CG1 . VAL A 262 ? 0.6048 0.5152 0.6700 -0.1823 0.0711 0.1137 262 VAL A CG1 2005 C CG2 . VAL A 262 ? 0.5571 0.5240 0.6205 -0.1848 0.0761 0.0902 262 VAL A CG2 2006 N N . GLN A 263 ? 0.5426 0.4969 0.6766 -0.1420 0.0765 0.0842 263 GLN A N 2007 C CA . GLN A 263 ? 0.5346 0.5053 0.6869 -0.1325 0.0786 0.0744 263 GLN A CA 2008 C C . GLN A 263 ? 0.5107 0.5107 0.6513 -0.1388 0.0760 0.0684 263 GLN A C 2009 O O . GLN A 263 ? 0.5177 0.5291 0.6404 -0.1498 0.0694 0.0745 263 GLN A O 2010 C CB . GLN A 263 ? 0.5556 0.5253 0.7340 -0.1219 0.0695 0.0819 263 GLN A CB 2011 C CG . GLN A 263 ? 0.6026 0.5444 0.8009 -0.1134 0.0722 0.0856 263 GLN A CG 2012 C CD . GLN A 263 ? 0.6519 0.5881 0.8657 -0.1078 0.0556 0.1016 263 GLN A CD 2013 O OE1 . GLN A 263 ? 0.6674 0.6228 0.8940 -0.1034 0.0446 0.1044 263 GLN A OE1 2014 N NE2 . GLN A 263 ? 0.6863 0.5953 0.8991 -0.1081 0.0526 0.1122 263 GLN A NE2 2015 N N . VAL A 264 ? 0.4879 0.4987 0.6390 -0.1326 0.0822 0.0557 264 VAL A N 2016 C CA . VAL A 264 ? 0.4773 0.5149 0.6240 -0.1358 0.0807 0.0479 264 VAL A CA 2017 C C . VAL A 264 ? 0.4722 0.5257 0.6303 -0.1339 0.0702 0.0542 264 VAL A C 2018 O O . VAL A 264 ? 0.4826 0.5276 0.6603 -0.1253 0.0663 0.0599 264 VAL A O 2019 C CB . VAL A 264 ? 0.4647 0.5022 0.6180 -0.1295 0.0907 0.0331 264 VAL A CB 2020 C CG1 . VAL A 264 ? 0.4606 0.5233 0.6150 -0.1306 0.0891 0.0244 264 VAL A CG1 2021 C CG2 . VAL A 264 ? 0.4661 0.4909 0.6046 -0.1329 0.0978 0.0272 264 VAL A CG2 2022 N N . ASP A 265 ? 0.4593 0.5368 0.6062 -0.1424 0.0654 0.0522 265 ASP A N 2023 C CA . ASP A 265 ? 0.4472 0.5427 0.6006 -0.1431 0.0546 0.0572 265 ASP A CA 2024 C C . ASP A 265 ? 0.4154 0.5379 0.5645 -0.1487 0.0576 0.0442 265 ASP A C 2025 O O . ASP A 265 ? 0.4142 0.5475 0.5453 -0.1597 0.0600 0.0397 265 ASP A O 2026 C CB . ASP A 265 ? 0.4737 0.5658 0.6101 -0.1528 0.0418 0.0743 265 ASP A CB 2027 C CG . ASP A 265 ? 0.4876 0.5949 0.6295 -0.1533 0.0271 0.0823 265 ASP A CG 2028 O OD1 . ASP A 265 ? 0.4688 0.5939 0.6274 -0.1480 0.0283 0.0724 265 ASP A OD1 2029 O OD2 . ASP A 265 ? 0.5086 0.6090 0.6369 -0.1598 0.0136 0.0989 265 ASP A OD2 2030 N N . ALA A 266 ? 0.3886 0.5219 0.5563 -0.1415 0.0584 0.0366 266 ALA A N 2031 C CA . ALA A 266 ? 0.3689 0.5254 0.5358 -0.1456 0.0621 0.0228 266 ALA A CA 2032 C C . ALA A 266 ? 0.3748 0.5547 0.5377 -0.1542 0.0514 0.0266 266 ALA A C 2033 O O . ALA A 266 ? 0.3588 0.5591 0.5242 -0.1577 0.0540 0.0148 266 ALA A O 2034 C CB . ALA A 266 ? 0.3513 0.5040 0.5375 -0.1351 0.0709 0.0110 266 ALA A CB 2035 N N . ASN A 267 ? 0.3970 0.5721 0.5525 -0.1580 0.0387 0.0432 267 ASN A N 2036 C CA . ASN A 267 ? 0.4073 0.6014 0.5531 -0.1680 0.0255 0.0500 267 ASN A CA 2037 C C . ASN A 267 ? 0.4354 0.6369 0.5483 -0.1867 0.0240 0.0533 267 ASN A C 2038 O O . ASN A 267 ? 0.4420 0.6627 0.5406 -0.1992 0.0168 0.0541 267 ASN A O 2039 C CB . ASN A 267 ? 0.4186 0.6015 0.5762 -0.1607 0.0094 0.0675 267 ASN A CB 2040 C CG . ASN A 267 ? 0.4328 0.6311 0.5751 -0.1720 -0.0082 0.0783 267 ASN A CG 2041 O OD1 . ASN A 267 ? 0.4573 0.6448 0.5755 -0.1815 -0.0185 0.0942 267 ASN A OD1 2042 N ND2 . ASN A 267 ? 0.4183 0.6408 0.5719 -0.1726 -0.0116 0.0698 267 ASN A ND2 2043 N N . CYS A 268 ? 0.4599 0.6469 0.5599 -0.1902 0.0315 0.0542 268 CYS A N 2044 C CA . CYS A 268 ? 0.4923 0.6871 0.5627 -0.2095 0.0335 0.0541 268 CYS A CA 2045 C C . CYS A 268 ? 0.4783 0.6825 0.5506 -0.2116 0.0493 0.0347 268 CYS A C 2046 O O . CYS A 268 ? 0.4577 0.6512 0.5473 -0.1982 0.0568 0.0276 268 CYS A O 2047 C CB . CYS A 268 ? 0.5363 0.7068 0.5868 -0.2158 0.0264 0.0734 268 CYS A CB 2048 S SG . CYS A 268 ? 0.5457 0.6838 0.6092 -0.2019 0.0332 0.0773 268 CYS A SG 2049 N N . GLU A 269 ? 0.5016 0.6924 0.9135 -0.3091 0.0183 0.0530 269 GLU A N 2050 C CA . GLU A 269 ? 0.5398 0.6468 0.9050 -0.2956 0.0362 0.0442 269 GLU A CA 2051 C C . GLU A 269 ? 0.4984 0.5933 0.8510 -0.2598 0.0267 0.0480 269 GLU A C 2052 O O . GLU A 269 ? 0.4821 0.6091 0.8400 -0.2593 0.0066 0.0481 269 GLU A O 2053 C CB . GLU A 269 ? 0.6281 0.6851 0.9483 -0.3315 0.0433 0.0252 269 GLU A CB 2054 C CG . GLU A 269 ? 0.6951 0.6640 0.9673 -0.3183 0.0704 0.0198 269 GLU A CG 2055 C CD . GLU A 269 ? 0.7965 0.7047 1.0165 -0.3528 0.0832 0.0016 269 GLU A CD 2056 O OE1 . GLU A 269 ? 0.8434 0.7783 1.0667 -0.3962 0.0729 -0.0091 269 GLU A OE1 2057 O OE2 . GLU A 269 ? 0.8627 0.6963 1.0357 -0.3365 0.1050 -0.0014 269 GLU A OE2 2058 N N . GLY A 270 ? 0.4843 0.5363 0.8202 -0.2305 0.0414 0.0518 270 GLY A N 2059 C CA . GLY A 270 ? 0.4675 0.5057 0.7881 -0.2010 0.0345 0.0541 270 GLY A CA 2060 C C . GLY A 270 ? 0.4721 0.4559 0.7622 -0.1798 0.0539 0.0546 270 GLY A C 2061 O O . GLY A 270 ? 0.4845 0.4467 0.7718 -0.1803 0.0725 0.0567 270 GLY A O 2062 N N . ASP A 271 ? 0.4663 0.4318 0.7340 -0.1606 0.0500 0.0542 271 ASP A N 2063 C CA . ASP A 271 ? 0.4749 0.4016 0.7154 -0.1364 0.0660 0.0580 271 ASP A CA 2064 C C . ASP A 271 ? 0.4262 0.3740 0.6749 -0.1094 0.0567 0.0655 271 ASP A C 2065 O O . ASP A 271 ? 0.4248 0.3540 0.6545 -0.0892 0.0666 0.0702 271 ASP A O 2066 C CB . ASP A 271 ? 0.5238 0.4026 0.7206 -0.1396 0.0759 0.0513 271 ASP A CB 2067 C CG . ASP A 271 ? 0.5840 0.4221 0.7582 -0.1651 0.0938 0.0430 271 ASP A CG 2068 O OD1 . ASP A 271 ? 0.6091 0.4414 0.7928 -0.1700 0.1079 0.0456 271 ASP A OD1 2069 O OD2 . ASP A 271 ? 0.6422 0.4494 0.7851 -0.1813 0.0959 0.0334 271 ASP A OD2 2070 N N . CYS A 272 ? 0.3904 0.3777 0.6655 -0.1097 0.0392 0.0675 272 CYS A N 2071 C CA . CYS A 272 ? 0.3700 0.3727 0.6496 -0.0896 0.0320 0.0727 272 CYS A CA 2072 C C . CYS A 272 ? 0.3471 0.3765 0.6546 -0.0850 0.0308 0.0793 272 CYS A C 2073 O O . CYS A 272 ? 0.3425 0.3999 0.6734 -0.0942 0.0228 0.0814 272 CYS A O 2074 C CB . CYS A 272 ? 0.3629 0.3771 0.6390 -0.0907 0.0165 0.0699 272 CYS A CB 2075 S SG . CYS A 272 ? 0.3527 0.3797 0.6291 -0.0716 0.0104 0.0745 272 CYS A SG 2076 N N . TYR A 273 ? 0.3363 0.3584 0.6391 -0.0696 0.0396 0.0837 273 TYR A N 2077 C CA . TYR A 273 ? 0.3277 0.3632 0.6491 -0.0634 0.0448 0.0903 273 TYR A CA 2078 C C . TYR A 273 ? 0.3256 0.3611 0.6373 -0.0490 0.0429 0.0921 273 TYR A C 2079 O O . TYR A 273 ? 0.3302 0.3559 0.6208 -0.0434 0.0414 0.0890 273 TYR A O 2080 C CB . TYR A 273 ? 0.3395 0.3584 0.6579 -0.0613 0.0616 0.0930 273 TYR A CB 2081 C CG . TYR A 273 ? 0.3473 0.3587 0.6711 -0.0791 0.0687 0.0904 273 TYR A CG 2082 C CD1 . TYR A 273 ? 0.3418 0.3813 0.6944 -0.0954 0.0645 0.0923 273 TYR A CD1 2083 C CD2 . TYR A 273 ? 0.3687 0.3453 0.6667 -0.0801 0.0817 0.0872 273 TYR A CD2 2084 C CE1 . TYR A 273 ? 0.3615 0.3957 0.7174 -0.1179 0.0713 0.0883 273 TYR A CE1 2085 C CE2 . TYR A 273 ? 0.3945 0.3549 0.6908 -0.1000 0.0919 0.0833 273 TYR A CE2 2086 C CZ . TYR A 273 ? 0.3867 0.3765 0.7123 -0.1219 0.0858 0.0825 273 TYR A CZ 2087 O OH . TYR A 273 ? 0.4084 0.3845 0.7313 -0.1480 0.0955 0.0768 273 TYR A OH 2088 N N . HIS A 274 ? 0.3271 0.3741 0.6526 -0.0438 0.0446 0.0976 274 HIS A N 2089 C CA . HIS A 274 ? 0.3380 0.3750 0.6481 -0.0331 0.0482 0.0983 274 HIS A CA 2090 C C . HIS A 274 ? 0.3496 0.3867 0.6710 -0.0249 0.0612 0.1067 274 HIS A C 2091 O O . HIS A 274 ? 0.3532 0.4047 0.6980 -0.0278 0.0655 0.1126 274 HIS A O 2092 C CB . HIS A 274 ? 0.3326 0.3735 0.6374 -0.0336 0.0387 0.0962 274 HIS A CB 2093 C CG . HIS A 274 ? 0.3371 0.3967 0.6635 -0.0322 0.0360 0.1035 274 HIS A CG 2094 N ND1 . HIS A 274 ? 0.3593 0.4145 0.6828 -0.0217 0.0427 0.1098 274 HIS A ND1 2095 C CD2 . HIS A 274 ? 0.3438 0.4284 0.6927 -0.0394 0.0284 0.1065 274 HIS A CD2 2096 C CE1 . HIS A 274 ? 0.3491 0.4305 0.6952 -0.0185 0.0395 0.1190 274 HIS A CE1 2097 N NE2 . HIS A 274 ? 0.3436 0.4469 0.7066 -0.0310 0.0290 0.1165 274 HIS A NE2 2098 N N . SER A 275 ? 0.3605 0.3813 0.6639 -0.0162 0.0688 0.1074 275 SER A N 2099 C CA . SER A 275 ? 0.3882 0.4027 0.6968 -0.0054 0.0848 0.1164 275 SER A CA 2100 C C . SER A 275 ? 0.3772 0.4149 0.7143 0.0002 0.0871 0.1284 275 SER A C 2101 O O . SER A 275 ? 0.4003 0.4489 0.7562 0.0068 0.0983 0.1389 275 SER A O 2102 C CB . SER A 275 ? 0.4098 0.3936 0.6842 0.0012 0.0950 0.1132 275 SER A CB 2103 O OG . SER A 275 ? 0.4237 0.3966 0.6818 -0.0005 0.0920 0.1096 275 SER A OG 2104 N N . GLY A 276 ? 0.3694 0.4192 0.7106 -0.0017 0.0767 0.1285 276 GLY A N 2105 C CA . GLY A 276 ? 0.3591 0.4400 0.7272 0.0057 0.0768 0.1420 276 GLY A CA 2106 C C . GLY A 276 ? 0.3399 0.4635 0.7420 -0.0074 0.0650 0.1447 276 GLY A C 2107 O O . GLY A 276 ? 0.3372 0.4990 0.7656 -0.0025 0.0638 0.1578 276 GLY A O 2108 N N . GLY A 277 ? 0.3242 0.4426 0.7235 -0.0242 0.0573 0.1331 277 GLY A N 2109 C CA . GLY A 277 ? 0.3172 0.4672 0.7411 -0.0423 0.0485 0.1326 277 GLY A CA 2110 C C . GLY A 277 ? 0.3124 0.4479 0.7205 -0.0598 0.0373 0.1182 277 GLY A C 2111 O O . GLY A 277 ? 0.3178 0.4196 0.7011 -0.0584 0.0412 0.1099 277 GLY A O 2112 N N . THR A 278 ? 0.3048 0.4678 0.7256 -0.0753 0.0244 0.1165 278 THR A N 2113 C CA . THR A 278 ? 0.3102 0.4567 0.7138 -0.0937 0.0166 0.1033 278 THR A CA 2114 C C . THR A 278 ? 0.3054 0.4642 0.7028 -0.0961 0.0004 0.1004 278 THR A C 2115 O O . THR A 278 ? 0.2914 0.4894 0.7088 -0.0951 -0.0081 0.1086 278 THR A O 2116 C CB . THR A 278 ? 0.3207 0.4827 0.7386 -0.1189 0.0180 0.1006 278 THR A CB 2117 O OG1 . THR A 278 ? 0.3232 0.4803 0.7523 -0.1158 0.0344 0.1063 278 THR A OG1 2118 C CG2 . THR A 278 ? 0.3409 0.4672 0.7293 -0.1366 0.0174 0.0862 278 THR A CG2 2119 N N . ILE A 279 ? 0.3201 0.4475 0.6893 -0.0973 -0.0029 0.0904 279 ILE A N 2120 C CA . ILE A 279 ? 0.3215 0.4547 0.6807 -0.1001 -0.0167 0.0868 279 ILE A CA 2121 C C . ILE A 279 ? 0.3505 0.4789 0.6992 -0.1242 -0.0219 0.0769 279 ILE A C 2122 O O . ILE A 279 ? 0.3692 0.4598 0.6930 -0.1287 -0.0142 0.0688 279 ILE A O 2123 C CB . ILE A 279 ? 0.3153 0.4187 0.6492 -0.0869 -0.0156 0.0830 279 ILE A CB 2124 C CG1 . ILE A 279 ? 0.3036 0.4054 0.6410 -0.0691 -0.0086 0.0899 279 ILE A CG1 2125 C CG2 . ILE A 279 ? 0.3183 0.4256 0.6411 -0.0890 -0.0281 0.0799 279 ILE A CG2 2126 C CD1 . ILE A 279 ? 0.3036 0.3820 0.6177 -0.0610 -0.0068 0.0858 279 ILE A CD1 2127 N N . ILE A 280 ? 0.3663 0.5334 0.7317 -0.1396 -0.0335 0.0784 280 ILE A N 2128 C CA . ILE A 280 ? 0.4062 0.5682 0.7559 -0.1677 -0.0397 0.0668 280 ILE A CA 2129 C C . ILE A 280 ? 0.4192 0.5863 0.7533 -0.1660 -0.0543 0.0641 280 ILE A C 2130 O O . ILE A 280 ? 0.4157 0.6265 0.7690 -0.1588 -0.0661 0.0733 280 ILE A O 2131 C CB . ILE A 280 ? 0.4147 0.6242 0.7915 -0.1925 -0.0452 0.0690 280 ILE A CB 2132 C CG1 . ILE A 280 ? 0.4138 0.6172 0.8063 -0.1951 -0.0287 0.0723 280 ILE A CG1 2133 C CG2 . ILE A 280 ? 0.4506 0.6522 0.8039 -0.2269 -0.0527 0.0542 280 ILE A CG2 2134 C CD1 . ILE A 280 ? 0.4258 0.6804 0.8483 -0.2215 -0.0323 0.0755 280 ILE A CD1 2135 N N . SER A 281 ? 0.4517 0.5738 0.7495 -0.1703 -0.0515 0.0532 281 SER A N 2136 C CA . SER A 281 ? 0.4602 0.5786 0.7390 -0.1644 -0.0622 0.0512 281 SER A CA 2137 C C . SER A 281 ? 0.4958 0.5595 0.7317 -0.1715 -0.0542 0.0394 281 SER A C 2138 O O . SER A 281 ? 0.4923 0.5178 0.7136 -0.1683 -0.0377 0.0369 281 SER A O 2139 C CB . SER A 281 ? 0.4347 0.5559 0.7219 -0.1347 -0.0612 0.0611 281 SER A CB 2140 O OG . SER A 281 ? 0.4325 0.5542 0.7051 -0.1278 -0.0705 0.0612 281 SER A OG 2141 N N . ASN A 282 ? 0.5335 0.5928 0.7468 -0.1784 -0.0640 0.0339 282 ASN A N 2142 C CA . ASN A 282 ? 0.5811 0.5864 0.7503 -0.1772 -0.0546 0.0259 282 ASN A CA 2143 C C . ASN A 282 ? 0.5529 0.5560 0.7156 -0.1527 -0.0581 0.0322 282 ASN A C 2144 O O . ASN A 282 ? 0.5631 0.5284 0.6913 -0.1482 -0.0512 0.0284 282 ASN A O 2145 C CB . ASN A 282 ? 0.6547 0.6449 0.7926 -0.2076 -0.0594 0.0126 282 ASN A CB 2146 C CG . ASN A 282 ? 0.7115 0.6987 0.8511 -0.2377 -0.0534 0.0045 282 ASN A CG 2147 O OD1 . ASN A 282 ? 0.7438 0.6952 0.8762 -0.2349 -0.0340 0.0039 282 ASN A OD1 2148 N ND2 . ASN A 282 ? 0.7318 0.7598 0.8808 -0.2670 -0.0694 -0.0009 282 ASN A ND2 2149 N N . LEU A 283 ? 0.5057 0.5460 0.6989 -0.1367 -0.0662 0.0425 283 LEU A N 2150 C CA . LEU A 283 ? 0.4834 0.5207 0.6707 -0.1164 -0.0676 0.0481 283 LEU A CA 2151 C C . LEU A 283 ? 0.4710 0.4810 0.6501 -0.1009 -0.0528 0.0507 283 LEU A C 2152 O O . LEU A 283 ? 0.4702 0.4768 0.6596 -0.0996 -0.0439 0.0519 283 LEU A O 2153 C CB . LEU A 283 ? 0.4538 0.5302 0.6700 -0.1045 -0.0759 0.0583 283 LEU A CB 2154 C CG . LEU A 283 ? 0.4758 0.5943 0.7070 -0.1142 -0.0904 0.0613 283 LEU A CG 2155 C CD1 . LEU A 283 ? 0.4591 0.6053 0.7089 -0.0937 -0.0931 0.0746 283 LEU A CD1 2156 C CD2 . LEU A 283 ? 0.5069 0.6207 0.7106 -0.1300 -0.1007 0.0529 283 LEU A CD2 2157 N N . PRO A 284 ? 0.4660 0.4606 0.6265 -0.0888 -0.0498 0.0527 284 PRO A N 2158 C CA . PRO A 284 ? 0.4557 0.4348 0.6092 -0.0745 -0.0365 0.0571 284 PRO A CA 2159 C C . PRO A 284 ? 0.4131 0.4160 0.5925 -0.0650 -0.0359 0.0636 284 PRO A C 2160 O O . PRO A 284 ? 0.4087 0.4086 0.5868 -0.0567 -0.0264 0.0672 284 PRO A O 2161 C CB . PRO A 284 ? 0.4703 0.4352 0.6004 -0.0655 -0.0347 0.0591 284 PRO A CB 2162 C CG . PRO A 284 ? 0.4692 0.4509 0.6046 -0.0699 -0.0487 0.0581 284 PRO A CG 2163 C CD . PRO A 284 ? 0.4683 0.4628 0.6137 -0.0868 -0.0579 0.0525 284 PRO A CD 2164 N N . PHE A 285 ? 0.3798 0.4051 0.5788 -0.0657 -0.0445 0.0658 285 PHE A N 2165 C CA . PHE A 285 ? 0.3544 0.3927 0.5691 -0.0588 -0.0414 0.0704 285 PHE A CA 2166 C C . PHE A 285 ? 0.3438 0.3977 0.5801 -0.0611 -0.0435 0.0726 285 PHE A C 2167 O O . PHE A 285 ? 0.3500 0.4160 0.5941 -0.0668 -0.0505 0.0727 285 PHE A O 2168 C CB . PHE A 285 ? 0.3436 0.3844 0.5533 -0.0528 -0.0427 0.0736 285 PHE A CB 2169 C CG . PHE A 285 ? 0.3513 0.3812 0.5415 -0.0491 -0.0406 0.0738 285 PHE A CG 2170 C CD1 . PHE A 285 ? 0.3489 0.3757 0.5315 -0.0445 -0.0324 0.0757 285 PHE A CD1 2171 C CD2 . PHE A 285 ? 0.3639 0.3886 0.5421 -0.0475 -0.0457 0.0741 285 PHE A CD2 2172 C CE1 . PHE A 285 ? 0.3590 0.3780 0.5238 -0.0375 -0.0279 0.0790 285 PHE A CE1 2173 C CE2 . PHE A 285 ? 0.3732 0.3856 0.5317 -0.0422 -0.0416 0.0754 285 PHE A CE2 2174 C CZ . PHE A 285 ? 0.3756 0.3852 0.5280 -0.0367 -0.0320 0.0784 285 PHE A CZ 2175 N N . GLN A 286 ? 0.3311 0.3870 0.5755 -0.0568 -0.0368 0.0750 286 GLN A N 2176 C CA . GLN A 286 ? 0.3275 0.3938 0.5890 -0.0546 -0.0346 0.0793 286 GLN A CA 2177 C C . GLN A 286 ? 0.3261 0.3847 0.5837 -0.0490 -0.0265 0.0816 286 GLN A C 2178 O O . GLN A 286 ? 0.3397 0.3903 0.5858 -0.0513 -0.0225 0.0782 286 GLN A O 2179 C CB . GLN A 286 ? 0.3284 0.3970 0.6005 -0.0589 -0.0308 0.0783 286 GLN A CB 2180 C CG . GLN A 286 ? 0.3336 0.3897 0.5966 -0.0574 -0.0226 0.0758 286 GLN A CG 2181 C CD . GLN A 286 ? 0.3316 0.3870 0.5993 -0.0532 -0.0146 0.0781 286 GLN A CD 2182 O OE1 . GLN A 286 ? 0.3363 0.3945 0.6115 -0.0496 -0.0124 0.0822 286 GLN A OE1 2183 N NE2 . GLN A 286 ? 0.3352 0.3855 0.5946 -0.0520 -0.0087 0.0766 286 GLN A NE2 2184 N N . ASN A 287 ? 0.3284 0.3900 0.5929 -0.0420 -0.0227 0.0881 287 ASN A N 2185 C CA . ASN A 287 ? 0.3513 0.3947 0.6047 -0.0377 -0.0105 0.0899 287 ASN A CA 2186 C C . ASN A 287 ? 0.3691 0.4109 0.6311 -0.0316 -0.0007 0.0950 287 ASN A C 2187 O O . ASN A 287 ? 0.3888 0.4139 0.6415 -0.0232 0.0119 0.1004 287 ASN A O 2188 C CB . ASN A 287 ? 0.3661 0.4028 0.6106 -0.0299 -0.0081 0.0955 287 ASN A CB 2189 C CG . ASN A 287 ? 0.3974 0.4042 0.6224 -0.0274 0.0088 0.0964 287 ASN A CG 2190 O OD1 . ASN A 287 ? 0.4240 0.4216 0.6455 -0.0138 0.0193 0.1061 287 ASN A OD1 2191 N ND2 . ASN A 287 ? 0.4062 0.3977 0.6155 -0.0408 0.0128 0.0871 287 ASN A ND2 2192 N N . ILE A 288 ? 0.3636 0.4181 0.6402 -0.0348 -0.0036 0.0941 288 ILE A N 2193 C CA . ILE A 288 ? 0.3711 0.4270 0.6583 -0.0283 0.0063 0.1002 288 ILE A CA 2194 C C . ILE A 288 ? 0.3746 0.4083 0.6461 -0.0314 0.0162 0.0945 288 ILE A C 2195 O O . ILE A 288 ? 0.3925 0.4088 0.6549 -0.0247 0.0296 0.0981 288 ILE A O 2196 C CB . ILE A 288 ? 0.3591 0.4424 0.6714 -0.0316 -0.0003 0.1034 288 ILE A CB 2197 C CG1 . ILE A 288 ? 0.3614 0.4737 0.6884 -0.0294 -0.0101 0.1107 288 ILE A CG1 2198 C CG2 . ILE A 288 ? 0.3664 0.4524 0.6908 -0.0248 0.0115 0.1106 288 ILE A CG2 2199 C CD1 . ILE A 288 ? 0.3547 0.4940 0.6996 -0.0427 -0.0208 0.1087 288 ILE A CD1 2200 N N . ASP A 289 ? 0.3759 0.4101 0.6413 -0.0402 0.0109 0.0865 289 ASP A N 2201 C CA . ASP A 289 ? 0.3731 0.3956 0.6246 -0.0429 0.0183 0.0822 289 ASP A CA 2202 C C . ASP A 289 ? 0.3507 0.3812 0.5929 -0.0497 0.0114 0.0763 289 ASP A C 2203 O O . ASP A 289 ? 0.3438 0.3841 0.5944 -0.0486 0.0068 0.0770 289 ASP A O 2204 C CB . ASP A 289 ? 0.3790 0.4048 0.6443 -0.0375 0.0246 0.0868 289 ASP A CB 2205 C CG . ASP A 289 ? 0.3962 0.4062 0.6437 -0.0371 0.0349 0.0840 289 ASP A CG 2206 O OD1 . ASP A 289 ? 0.3792 0.3841 0.6053 -0.0443 0.0335 0.0772 289 ASP A OD1 2207 O OD2 . ASP A 289 ? 0.4302 0.4363 0.6854 -0.0301 0.0443 0.0894 289 ASP A OD2 2208 N N . SER A 290 ? 0.3529 0.3790 0.5756 -0.0569 0.0127 0.0713 290 SER A N 2209 C CA . SER A 290 ? 0.3464 0.3901 0.5614 -0.0616 0.0067 0.0688 290 SER A CA 2210 C C . SER A 290 ? 0.3372 0.3906 0.5509 -0.0564 0.0091 0.0707 290 SER A C 2211 O O . SER A 290 ? 0.3366 0.4086 0.5462 -0.0543 0.0057 0.0727 290 SER A O 2212 C CB . SER A 290 ? 0.3618 0.4056 0.5572 -0.0749 0.0074 0.0630 290 SER A CB 2213 O OG . SER A 290 ? 0.3870 0.4188 0.5657 -0.0808 0.0151 0.0588 290 SER A OG 2214 N N . ARG A 291 ? 0.3387 0.3799 0.5545 -0.0520 0.0168 0.0719 291 ARG A N 2215 C CA . ARG A 291 ? 0.3413 0.3876 0.5535 -0.0452 0.0215 0.0747 291 ARG A CA 2216 C C . ARG A 291 ? 0.3396 0.3796 0.5689 -0.0371 0.0256 0.0797 291 ARG A C 2217 O O . ARG A 291 ? 0.3593 0.3960 0.5863 -0.0303 0.0333 0.0829 291 ARG A O 2218 C CB . ARG A 291 ? 0.3513 0.3859 0.5480 -0.0473 0.0295 0.0721 291 ARG A CB 2219 C CG . ARG A 291 ? 0.3636 0.4042 0.5360 -0.0610 0.0265 0.0650 291 ARG A CG 2220 C CD . ARG A 291 ? 0.3864 0.4091 0.5351 -0.0658 0.0356 0.0605 291 ARG A CD 2221 N NE . ARG A 291 ? 0.3854 0.4149 0.5320 -0.0548 0.0398 0.0652 291 ARG A NE 2222 C CZ . ARG A 291 ? 0.3884 0.3993 0.5445 -0.0425 0.0501 0.0704 291 ARG A CZ 2223 N NH1 . ARG A 291 ? 0.3894 0.3802 0.5604 -0.0390 0.0563 0.0728 291 ARG A NH1 2224 N NH2 . ARG A 291 ? 0.3922 0.4082 0.5434 -0.0325 0.0552 0.0749 291 ARG A NH2 2225 N N . ALA A 292 ? 0.3280 0.3666 0.5721 -0.0396 0.0209 0.0799 292 ALA A N 2226 C CA . ALA A 292 ? 0.3280 0.3625 0.5855 -0.0389 0.0236 0.0824 292 ALA A CA 2227 C C . ALA A 292 ? 0.3312 0.3612 0.5761 -0.0334 0.0287 0.0841 292 ALA A C 2228 O O . ALA A 292 ? 0.3257 0.3632 0.5575 -0.0297 0.0255 0.0846 292 ALA A O 2229 C CB . ALA A 292 ? 0.3316 0.3705 0.6005 -0.0456 0.0148 0.0811 292 ALA A CB 2230 N N . VAL A 293 ? 0.3336 0.3512 0.5817 -0.0320 0.0386 0.0863 293 VAL A N 2231 C CA . VAL A 293 ? 0.3489 0.3536 0.5801 -0.0237 0.0489 0.0898 293 VAL A CA 2232 C C . VAL A 293 ? 0.3617 0.3448 0.5939 -0.0322 0.0557 0.0877 293 VAL A C 2233 O O . VAL A 293 ? 0.3520 0.3387 0.6027 -0.0461 0.0510 0.0841 293 VAL A O 2234 C CB . VAL A 293 ? 0.3662 0.3690 0.5883 -0.0117 0.0604 0.0952 293 VAL A CB 2235 C CG1 . VAL A 293 ? 0.3621 0.3877 0.5735 -0.0060 0.0535 0.0962 293 VAL A CG1 2236 C CG2 . VAL A 293 ? 0.3668 0.3636 0.6048 -0.0163 0.0663 0.0951 293 VAL A CG2 2237 N N . GLY A 294 ? 0.3877 0.3492 0.5973 -0.0239 0.0682 0.0909 294 GLY A N 2238 C CA . GLY A 294 ? 0.4251 0.3549 0.6235 -0.0342 0.0784 0.0873 294 GLY A CA 2239 C C . GLY A 294 ? 0.4372 0.3590 0.6191 -0.0348 0.0734 0.0848 294 GLY A C 2240 O O . GLY A 294 ? 0.4307 0.3645 0.6022 -0.0189 0.0714 0.0906 294 GLY A O 2241 N N . LYS A 295 ? 0.4536 0.3588 0.6327 -0.0543 0.0710 0.0765 295 LYS A N 2242 C CA . LYS A 295 ? 0.4727 0.3667 0.6335 -0.0567 0.0661 0.0729 295 LYS A CA 2243 C C . LYS A 295 ? 0.4446 0.3702 0.6294 -0.0700 0.0436 0.0674 295 LYS A C 2244 O O . LYS A 295 ? 0.4693 0.4012 0.6676 -0.0902 0.0367 0.0610 295 LYS A O 2245 C CB . LYS A 295 ? 0.5318 0.3776 0.6624 -0.0704 0.0817 0.0665 295 LYS A CB 2246 C CG . LYS A 295 ? 0.5684 0.3744 0.6685 -0.0530 0.1092 0.0742 295 LYS A CG 2247 C CD . LYS A 295 ? 0.6406 0.3888 0.7070 -0.0712 0.1293 0.0662 295 LYS A CD 2248 C CE . LYS A 295 ? 0.6857 0.3913 0.7211 -0.0502 0.1606 0.0762 295 LYS A CE 2249 N NZ . LYS A 295 ? 0.7853 0.4217 0.7776 -0.0679 0.1856 0.0680 295 LYS A NZ 2250 N N . CYS A 296 ? 0.4199 0.3683 0.6098 -0.0583 0.0332 0.0710 296 CYS A N 2251 C CA . CYS A 296 ? 0.3915 0.3698 0.6041 -0.0648 0.0154 0.0689 296 CYS A CA 2252 C C . CYS A 296 ? 0.3905 0.3705 0.5918 -0.0623 0.0071 0.0680 296 CYS A C 2253 O O . CYS A 296 ? 0.3751 0.3439 0.5564 -0.0504 0.0142 0.0718 296 CYS A O 2254 C CB . CYS A 296 ? 0.3704 0.3719 0.5989 -0.0548 0.0133 0.0739 296 CYS A CB 2255 S SG . CYS A 296 ? 0.3688 0.3715 0.6127 -0.0555 0.0223 0.0762 296 CYS A SG 2256 N N . PRO A 297 ? 0.3835 0.3806 0.5980 -0.0710 -0.0069 0.0650 297 PRO A N 2257 C CA . PRO A 297 ? 0.3801 0.3838 0.5883 -0.0656 -0.0146 0.0660 297 PRO A CA 2258 C C . PRO A 297 ? 0.3712 0.3897 0.5840 -0.0536 -0.0129 0.0715 297 PRO A C 2259 O O . PRO A 297 ? 0.3753 0.4027 0.5995 -0.0516 -0.0098 0.0733 297 PRO A O 2260 C CB . PRO A 297 ? 0.3699 0.3935 0.5952 -0.0739 -0.0277 0.0647 297 PRO A CB 2261 C CG . PRO A 297 ? 0.3758 0.4048 0.6137 -0.0870 -0.0281 0.0622 297 PRO A CG 2262 C CD . PRO A 297 ? 0.3779 0.3936 0.6151 -0.0835 -0.0148 0.0633 297 PRO A CD 2263 N N . ARG A 298 ? 0.3662 0.3877 0.5686 -0.0475 -0.0144 0.0738 298 ARG A N 2264 C CA . ARG A 298 ? 0.3626 0.4032 0.5683 -0.0418 -0.0136 0.0780 298 ARG A CA 2265 C C . ARG A 298 ? 0.3298 0.3801 0.5491 -0.0483 -0.0199 0.0757 298 ARG A C 2266 O O . ARG A 298 ? 0.3119 0.3592 0.5340 -0.0513 -0.0258 0.0743 298 ARG A O 2267 C CB . ARG A 298 ? 0.3896 0.4351 0.5826 -0.0351 -0.0126 0.0823 298 ARG A CB 2268 C CG . ARG A 298 ? 0.4355 0.4793 0.6132 -0.0216 -0.0015 0.0899 298 ARG A CG 2269 C CD . ARG A 298 ? 0.4927 0.5023 0.6531 -0.0191 0.0072 0.0882 298 ARG A CD 2270 N NE . ARG A 298 ? 0.5378 0.5256 0.6877 -0.0272 0.0022 0.0818 298 ARG A NE 2271 C CZ . ARG A 298 ? 0.5688 0.5272 0.7058 -0.0366 0.0049 0.0750 298 ARG A CZ 2272 N NH1 . ARG A 298 ? 0.5765 0.5197 0.7105 -0.0385 0.0145 0.0739 298 ARG A NH1 2273 N NH2 . ARG A 298 ? 0.5866 0.5310 0.7118 -0.0459 -0.0016 0.0687 298 ARG A NH2 2274 N N . TYR A 299 ? 0.3112 0.3710 0.5344 -0.0495 -0.0169 0.0760 299 TYR A N 2275 C CA . TYR A 299 ? 0.3023 0.3616 0.5296 -0.0549 -0.0175 0.0741 299 TYR A CA 2276 C C . TYR A 299 ? 0.3088 0.3716 0.5281 -0.0585 -0.0191 0.0739 299 TYR A C 2277 O O . TYR A 299 ? 0.3183 0.3956 0.5314 -0.0595 -0.0187 0.0755 299 TYR A O 2278 C CB . TYR A 299 ? 0.3009 0.3624 0.5265 -0.0578 -0.0119 0.0727 299 TYR A CB 2279 C CG . TYR A 299 ? 0.2980 0.3473 0.5196 -0.0633 -0.0079 0.0704 299 TYR A CG 2280 C CD1 . TYR A 299 ? 0.3023 0.3398 0.5321 -0.0583 -0.0045 0.0729 299 TYR A CD1 2281 C CD2 . TYR A 299 ? 0.3107 0.3600 0.5183 -0.0734 -0.0054 0.0669 299 TYR A CD2 2282 C CE1 . TYR A 299 ? 0.3222 0.3420 0.5431 -0.0588 0.0038 0.0732 299 TYR A CE1 2283 C CE2 . TYR A 299 ? 0.3384 0.3651 0.5343 -0.0790 0.0028 0.0643 299 TYR A CE2 2284 C CZ . TYR A 299 ? 0.3415 0.3504 0.5426 -0.0693 0.0087 0.0682 299 TYR A CZ 2285 O OH . TYR A 299 ? 0.3653 0.3457 0.5500 -0.0703 0.0215 0.0680 299 TYR A OH 2286 N N . VAL A 300 ? 0.3173 0.3694 0.5371 -0.0595 -0.0195 0.0737 300 VAL A N 2287 C CA . VAL A 300 ? 0.3204 0.3688 0.5306 -0.0638 -0.0176 0.0735 300 VAL A CA 2288 C C . VAL A 300 ? 0.3464 0.3757 0.5507 -0.0662 -0.0094 0.0729 300 VAL A C 2289 O O . VAL A 300 ? 0.3518 0.3742 0.5629 -0.0596 -0.0071 0.0753 300 VAL A O 2290 C CB . VAL A 300 ? 0.3192 0.3656 0.5277 -0.0576 -0.0229 0.0764 300 VAL A CB 2291 C CG1 . VAL A 300 ? 0.3170 0.3721 0.5235 -0.0538 -0.0266 0.0775 300 VAL A CG1 2292 C CG2 . VAL A 300 ? 0.3249 0.3654 0.5400 -0.0510 -0.0265 0.0788 300 VAL A CG2 2293 N N . LYS A 301 ? 0.3739 0.3933 0.5639 -0.0754 -0.0027 0.0705 301 LYS A N 2294 C CA . LYS A 301 ? 0.4128 0.4026 0.5877 -0.0783 0.0106 0.0696 301 LYS A CA 2295 C C . LYS A 301 ? 0.4210 0.3949 0.5948 -0.0634 0.0147 0.0773 301 LYS A C 2296 O O . LYS A 301 ? 0.4491 0.3975 0.6119 -0.0572 0.0280 0.0808 301 LYS A O 2297 C CB . LYS A 301 ? 0.4564 0.4369 0.6116 -0.0977 0.0188 0.0632 301 LYS A CB 2298 C CG . LYS A 301 ? 0.4819 0.4814 0.6331 -0.1155 0.0165 0.0560 301 LYS A CG 2299 C CD . LYS A 301 ? 0.5308 0.5271 0.6626 -0.1403 0.0237 0.0491 301 LYS A CD 2300 C CE . LYS A 301 ? 0.5468 0.5546 0.6836 -0.1400 0.0214 0.0534 301 LYS A CE 2301 N NZ . LYS A 301 ? 0.5792 0.5981 0.7033 -0.1675 0.0265 0.0475 301 LYS A NZ 2302 N N . GLN A 302 ? 0.4000 0.3878 0.5813 -0.0562 0.0050 0.0811 302 GLN A N 2303 C CA . GLN A 302 ? 0.4119 0.3913 0.5903 -0.0415 0.0072 0.0895 302 GLN A CA 2304 C C . GLN A 302 ? 0.4163 0.4108 0.6115 -0.0285 0.0017 0.0961 302 GLN A C 2305 O O . GLN A 302 ? 0.4024 0.4172 0.6131 -0.0320 -0.0091 0.0932 302 GLN A O 2306 C CB . GLN A 302 ? 0.4026 0.3924 0.5802 -0.0391 -0.0019 0.0908 302 GLN A CB 2307 C CG . GLN A 302 ? 0.4042 0.3870 0.5692 -0.0512 0.0036 0.0867 302 GLN A CG 2308 C CD . GLN A 302 ? 0.3864 0.3930 0.5598 -0.0605 -0.0050 0.0819 302 GLN A CD 2309 O OE1 . GLN A 302 ? 0.3662 0.3848 0.5493 -0.0632 -0.0093 0.0790 302 GLN A OE1 2310 N NE2 . GLN A 302 ? 0.3802 0.3939 0.5489 -0.0632 -0.0054 0.0831 302 GLN A NE2 2311 N N . ARG A 303 ? 0.4496 0.4355 0.6410 -0.0131 0.0108 0.1065 303 ARG A N 2312 C CA . ARG A 303 ? 0.4687 0.4799 0.6793 0.0000 0.0054 0.1159 303 ARG A CA 2313 C C . ARG A 303 ? 0.4473 0.4899 0.6690 0.0023 -0.0127 0.1183 303 ARG A C 2314 O O . ARG A 303 ? 0.4395 0.5124 0.6804 0.0017 -0.0237 0.1205 303 ARG A O 2315 C CB . ARG A 303 ? 0.5307 0.5273 0.7330 0.0201 0.0236 0.1300 303 ARG A CB 2316 C CG . ARG A 303 ? 0.5975 0.5895 0.7867 0.0365 0.0285 0.1411 303 ARG A CG 2317 C CD . ARG A 303 ? 0.6731 0.6578 0.8560 0.0632 0.0476 0.1599 303 ARG A CD 2318 N NE . ARG A 303 ? 0.6820 0.7207 0.8904 0.0799 0.0348 0.1750 303 ARG A NE 2319 C CZ . ARG A 303 ? 0.7014 0.7728 0.9344 0.0848 0.0317 0.1822 303 ARG A CZ 2320 N NH1 . ARG A 303 ? 0.7109 0.7624 0.9454 0.0771 0.0412 0.1760 303 ARG A NH1 2321 N NH2 . ARG A 303 ? 0.7066 0.8350 0.9630 0.0966 0.0187 0.1962 303 ARG A NH2 2322 N N . SER A 304 ? 0.4410 0.4750 0.6481 0.0025 -0.0151 0.1171 304 SER A N 2323 C CA . SER A 304 ? 0.4348 0.4924 0.6438 0.0059 -0.0302 0.1199 304 SER A CA 2324 C C . SER A 304 ? 0.4312 0.4735 0.6228 0.0001 -0.0328 0.1135 304 SER A C 2325 O O . SER A 304 ? 0.4458 0.4625 0.6223 0.0013 -0.0202 0.1138 304 SER A O 2326 C CB . SER A 304 ? 0.4556 0.5274 0.6638 0.0271 -0.0265 0.1360 304 SER A CB 2327 O OG . SER A 304 ? 0.4588 0.5605 0.6681 0.0288 -0.0433 0.1387 304 SER A OG 2328 N N . LEU A 305 ? 0.4185 0.4744 0.6100 -0.0074 -0.0474 0.1078 305 LEU A N 2329 C CA . LEU A 305 ? 0.4240 0.4669 0.5975 -0.0098 -0.0496 0.1037 305 LEU A CA 2330 C C . LEU A 305 ? 0.4373 0.4966 0.6042 -0.0110 -0.0649 0.1027 305 LEU A C 2331 O O . LEU A 305 ? 0.4322 0.4966 0.6007 -0.0234 -0.0731 0.0948 305 LEU A O 2332 C CB . LEU A 305 ? 0.4077 0.4396 0.5801 -0.0214 -0.0469 0.0949 305 LEU A CB 2333 C CG . LEU A 305 ? 0.4003 0.4211 0.5753 -0.0258 -0.0341 0.0938 305 LEU A CG 2334 C CD1 . LEU A 305 ? 0.3819 0.4066 0.5601 -0.0351 -0.0345 0.0878 305 LEU A CD1 2335 C CD2 . LEU A 305 ? 0.4049 0.4094 0.5657 -0.0229 -0.0235 0.0975 305 LEU A CD2 2336 N N . LEU A 306 ? 0.4538 0.5190 0.6095 0.0009 -0.0673 0.1107 306 LEU A N 2337 C CA . LEU A 306 ? 0.4640 0.5510 0.6111 -0.0014 -0.0832 0.1104 306 LEU A CA 2338 C C . LEU A 306 ? 0.4772 0.5417 0.5973 -0.0073 -0.0861 0.1023 306 LEU A C 2339 O O . LEU A 306 ? 0.4791 0.5202 0.5853 0.0012 -0.0760 0.1049 306 LEU A O 2340 C CB . LEU A 306 ? 0.4785 0.5878 0.6241 0.0173 -0.0846 0.1251 306 LEU A CB 2341 C CG . LEU A 306 ? 0.4742 0.6043 0.6423 0.0296 -0.0776 0.1373 306 LEU A CG 2342 C CD1 . LEU A 306 ? 0.4923 0.6418 0.6536 0.0542 -0.0750 0.1556 306 LEU A CD1 2343 C CD2 . LEU A 306 ? 0.4626 0.6276 0.6547 0.0159 -0.0894 0.1341 306 LEU A CD2 2344 N N . LEU A 307 ? 0.4737 0.5427 0.5841 -0.0227 -0.0978 0.0928 307 LEU A N 2345 C CA . LEU A 307 ? 0.4859 0.5273 0.5642 -0.0285 -0.0984 0.0847 307 LEU A CA 2346 C C . LEU A 307 ? 0.5154 0.5716 0.5718 -0.0288 -0.1119 0.0856 307 LEU A C 2347 O O . LEU A 307 ? 0.5260 0.6154 0.5890 -0.0401 -0.1263 0.0840 307 LEU A O 2348 C CB . LEU A 307 ? 0.4908 0.5170 0.5634 -0.0467 -0.0985 0.0726 307 LEU A CB 2349 C CG . LEU A 307 ? 0.5225 0.5095 0.5567 -0.0512 -0.0932 0.0646 307 LEU A CG 2350 C CD1 . LEU A 307 ? 0.5141 0.4768 0.5473 -0.0384 -0.0761 0.0689 307 LEU A CD1 2351 C CD2 . LEU A 307 ? 0.5447 0.5188 0.5654 -0.0728 -0.0957 0.0522 307 LEU A CD2 2352 N N . ALA A 308 ? 0.5266 0.5625 0.5572 -0.0170 -0.1075 0.0889 308 ALA A N 2353 C CA . ALA A 308 ? 0.5510 0.5988 0.5550 -0.0161 -0.1200 0.0897 308 ALA A CA 2354 C C . ALA A 308 ? 0.5752 0.6143 0.5526 -0.0409 -0.1308 0.0743 308 ALA A C 2355 O O . ALA A 308 ? 0.5739 0.5724 0.5334 -0.0497 -0.1211 0.0645 308 ALA A O 2356 C CB . ALA A 308 ? 0.5694 0.5893 0.5477 0.0016 -0.1100 0.0958 308 ALA A CB 2357 N N . THR A 309 ? 0.5863 0.6644 0.5597 -0.0526 -0.1495 0.0730 309 THR A N 2358 C CA . THR A 309 ? 0.6272 0.6970 0.5671 -0.0815 -0.1608 0.0566 309 THR A CA 2359 C C . THR A 309 ? 0.6625 0.7492 0.5684 -0.0813 -0.1751 0.0577 309 THR A C 2360 O O . THR A 309 ? 0.6983 0.7931 0.5760 -0.1086 -0.1893 0.0449 309 THR A O 2361 C CB . THR A 309 ? 0.6160 0.7243 0.5816 -0.1069 -0.1723 0.0505 309 THR A CB 2362 O OG1 . THR A 309 ? 0.5986 0.7754 0.5985 -0.0969 -0.1854 0.0655 309 THR A OG1 2363 C CG2 . THR A 309 ? 0.5850 0.6702 0.5765 -0.1078 -0.1573 0.0482 309 THR A CG2 2364 N N . GLY A 310 ? 0.6549 0.7447 0.5601 -0.0519 -0.1703 0.0725 310 GLY A N 2365 C CA . GLY A 310 ? 0.6898 0.7951 0.5618 -0.0455 -0.1819 0.0765 310 GLY A CA 2366 C C . GLY A 310 ? 0.6948 0.7630 0.5502 -0.0157 -0.1653 0.0869 310 GLY A C 2367 O O . GLY A 310 ? 0.6747 0.7155 0.5503 -0.0013 -0.1464 0.0922 310 GLY A O 2368 N N . MET A 311 ? 0.7343 0.8038 0.5519 -0.0082 -0.1723 0.0896 311 MET A N 2369 C CA . MET A 311 ? 0.7413 0.7765 0.5393 0.0200 -0.1561 0.1003 311 MET A CA 2370 C C . MET A 311 ? 0.7140 0.7763 0.5461 0.0499 -0.1477 0.1218 311 MET A C 2371 O O . MET A 311 ? 0.6939 0.8050 0.5594 0.0514 -0.1562 0.1298 311 MET A O 2372 C CB . MET A 311 ? 0.7942 0.8252 0.5390 0.0200 -0.1666 0.0976 311 MET A CB 2373 C CG . MET A 311 ? 0.8036 0.9034 0.5511 0.0265 -0.1878 0.1091 311 MET A CG 2374 S SD . MET A 311 ? 0.8696 0.9645 0.5493 0.0258 -0.2007 0.1054 311 MET A SD 2375 C CE . MET A 311 ? 0.9066 0.9800 0.5491 -0.0252 -0.2150 0.0747 311 MET A CE 2376 N N . LYS A 312 ? 0.7262 0.7541 0.5468 0.0736 -0.1287 0.1318 312 LYS A N 2377 C CA . LYS A 312 ? 0.7245 0.7650 0.5648 0.1024 -0.1159 0.1522 312 LYS A CA 2378 C C . LYS A 312 ? 0.7533 0.8458 0.5842 0.1176 -0.1312 0.1660 312 LYS A C 2379 O O . LYS A 312 ? 0.7925 0.8931 0.5862 0.1151 -0.1449 0.1629 312 LYS A O 2380 C CB . LYS A 312 ? 0.7438 0.7346 0.5654 0.1208 -0.0921 0.1588 312 LYS A CB 2381 C CG . LYS A 312 ? 0.7531 0.7440 0.5838 0.1497 -0.0742 0.1792 312 LYS A CG 2382 C CD . LYS A 312 ? 0.7822 0.7259 0.5877 0.1643 -0.0523 0.1848 312 LYS A CD 2383 C CE . LYS A 312 ? 0.8064 0.7442 0.6096 0.1935 -0.0327 0.2055 312 LYS A CE 2384 N NZ . LYS A 312 ? 0.7856 0.7183 0.6230 0.1925 -0.0166 0.2095 312 LYS A NZ 2385 N N . ASN A 313 ? 0.7372 0.8654 0.5992 0.1347 -0.1277 0.1824 313 ASN A N 2386 C CA . ASN A 313 ? 0.7551 0.9416 0.6127 0.1547 -0.1400 0.2006 313 ASN A CA 2387 C C . ASN A 313 ? 0.7879 0.9518 0.6201 0.1914 -0.1210 0.2202 313 ASN A C 2388 O O . ASN A 313 ? 0.7735 0.9015 0.6164 0.2100 -0.0941 0.2305 313 ASN A O 2389 C CB . ASN A 313 ? 0.7283 0.9642 0.6288 0.1613 -0.1415 0.2131 313 ASN A CB 2390 C CG . ASN A 313 ? 0.7459 1.0620 0.6469 0.1751 -0.1610 0.2306 313 ASN A CG 2391 O OD1 . ASN A 313 ? 0.7623 1.1168 0.6465 0.1540 -0.1873 0.2209 313 ASN A OD1 2392 N ND2 . ASN A 313 ? 0.7440 1.0867 0.6618 0.2105 -0.1470 0.2573 313 ASN A ND2 2393 N N . VAL A 314 ? 0.8289 1.0117 0.6241 0.1997 -0.1341 0.2244 314 VAL A N 2394 C CA . VAL A 314 ? 0.8679 1.0312 0.6332 0.2358 -0.1170 0.2438 314 VAL A CA 2395 C C . VAL A 314 ? 0.9043 1.1421 0.6603 0.2578 -0.1346 0.2641 314 VAL A C 2396 O O . VAL A 314 ? 0.9320 1.1967 0.6553 0.2500 -0.1566 0.2591 314 VAL A O 2397 C CB . VAL A 314 ? 0.8958 1.0054 0.6174 0.2296 -0.1130 0.2315 314 VAL A CB 2398 C CG1 . VAL A 314 ? 0.9257 0.9994 0.6226 0.2666 -0.0865 0.2513 314 VAL A CG1 2399 C CG2 . VAL A 314 ? 0.8719 0.9281 0.6041 0.2017 -0.1040 0.2098 314 VAL A CG2 2400 N N . PRO A 315 ? 0.9058 1.1785 0.6883 0.2859 -0.1240 0.2880 315 PRO A N 2401 C CA . PRO A 315 ? 0.9390 1.2956 0.7197 0.3101 -0.1400 0.3116 315 PRO A CA 2402 C C . PRO A 315 ? 0.9994 1.3507 0.7372 0.3497 -0.1294 0.3333 315 PRO A C 2403 O O . PRO A 315 ? 1.0154 1.2915 0.7299 0.3641 -0.1021 0.3341 315 PRO A O 2404 C CB . PRO A 315 ? 0.9143 1.2941 0.7359 0.3315 -0.1236 0.3316 315 PRO A CB 2405 C CG . PRO A 315 ? 0.8957 1.1854 0.7224 0.3333 -0.0890 0.3253 315 PRO A CG 2406 C CD . PRO A 315 ? 0.8846 1.1166 0.6950 0.2989 -0.0933 0.2957 315 PRO A CD 2407 N N . GLU A 316 ? 1.0412 1.4764 0.7692 0.3664 -0.1510 0.3515 316 GLU A N 2408 C CA . GLU A 316 ? 1.1081 1.5515 0.7947 0.4085 -0.1428 0.3761 316 GLU A CA 2409 C C . GLU A 316 ? 1.1243 1.5135 0.8071 0.4573 -0.0978 0.4032 316 GLU A C 2410 O O . GLU A 316 ? 1.1062 1.5033 0.8205 0.4750 -0.0799 0.4190 316 GLU A O 2411 C CB . GLU A 316 ? 1.1399 1.7008 0.8267 0.4220 -0.1729 0.3968 316 GLU A CB 2412 C CG . GLU A 316 ? 1.1850 1.7785 0.8275 0.4025 -0.2050 0.3842 316 GLU A CG 2413 C CD . GLU A 316 ? 1.2417 1.8005 0.8324 0.4437 -0.1872 0.4023 316 GLU A CD 2414 O OE1 . GLU A 316 ? 1.2602 1.7226 0.8379 0.4595 -0.1521 0.4016 316 GLU A OE1 2415 O OE2 . GLU A 316 ? 1.2759 1.9064 0.8385 0.4597 -0.2082 0.4178 316 GLU A OE2 2416 N N . ILE A 317 ? 1.1613 1.4933 0.8058 0.4797 -0.0762 0.4098 317 ILE A N 2417 N N . GLY B 1 ? 0.9098 1.0325 0.5792 -0.2067 -0.2161 0.3725 1 GLY B N 2418 C CA . GLY B 1 ? 0.8915 1.0376 0.5639 -0.1958 -0.1970 0.3657 1 GLY B CA 2419 C C . GLY B 1 ? 0.8824 1.0861 0.5688 -0.1963 -0.1891 0.3933 1 GLY B C 2420 O O . GLY B 1 ? 0.8859 1.1176 0.5821 -0.2061 -0.1947 0.4192 1 GLY B O 2421 N N . LEU B 2 ? 0.8706 1.0938 0.5557 -0.1835 -0.1752 0.3890 2 LEU B N 2422 C CA . LEU B 2 ? 0.8672 1.1534 0.5649 -0.1776 -0.1661 0.4152 2 LEU B CA 2423 C C . LEU B 2 ? 0.8729 1.1967 0.5597 -0.1575 -0.1500 0.4208 2 LEU B C 2424 O O . LEU B 2 ? 0.8717 1.2567 0.5713 -0.1538 -0.1436 0.4507 2 LEU B O 2425 C CB . LEU B 2 ? 0.8612 1.1532 0.5524 -0.1623 -0.1564 0.4056 2 LEU B CB 2426 C CG . LEU B 2 ? 0.8598 1.1251 0.5602 -0.1775 -0.1718 0.4046 2 LEU B CG 2427 C CD1 . LEU B 2 ? 0.8602 1.1330 0.5480 -0.1565 -0.1595 0.3941 2 LEU B CD1 2428 C CD2 . LEU B 2 ? 0.8653 1.1607 0.5973 -0.2049 -0.1927 0.4397 2 LEU B CD2 2429 N N . PHE B 3 ? 0.8782 1.1686 0.5413 -0.1440 -0.1443 0.3937 3 PHE B N 2430 C CA . PHE B 3 ? 0.8929 1.2069 0.5356 -0.1200 -0.1318 0.3933 3 PHE B CA 2431 C C . PHE B 3 ? 0.9039 1.2202 0.5482 -0.1274 -0.1388 0.4036 3 PHE B C 2432 O O . PHE B 3 ? 0.9294 1.2637 0.5541 -0.1067 -0.1304 0.4047 3 PHE B O 2433 C CB . PHE B 3 ? 0.9002 1.1759 0.5112 -0.0991 -0.1243 0.3583 3 PHE B CB 2434 C CG . PHE B 3 ? 0.9009 1.1754 0.5005 -0.0860 -0.1163 0.3515 3 PHE B CG 2435 C CD1 . PHE B 3 ? 0.8910 1.1316 0.4987 -0.1006 -0.1211 0.3396 3 PHE B CD1 2436 C CD2 . PHE B 3 ? 0.9183 1.2257 0.4948 -0.0551 -0.1042 0.3582 3 PHE B CD2 2437 C CE1 . PHE B 3 ? 0.8996 1.1361 0.4933 -0.0872 -0.1145 0.3339 3 PHE B CE1 2438 C CE2 . PHE B 3 ? 0.9266 1.2306 0.4879 -0.0394 -0.0983 0.3517 3 PHE B CE2 2439 C CZ . PHE B 3 ? 0.9189 1.1864 0.4895 -0.0569 -0.1038 0.3396 3 PHE B CZ 2440 N N . GLY B 4 ? 0.9054 1.1989 0.5669 -0.1540 -0.1560 0.4109 4 GLY B N 2441 C CA . GLY B 4 ? 0.9170 1.2146 0.5799 -0.1640 -0.1655 0.4292 4 GLY B CA 2442 C C . GLY B 4 ? 0.9269 1.2020 0.5674 -0.1485 -0.1651 0.4080 4 GLY B C 2443 O O . GLY B 4 ? 0.9487 1.2369 0.5830 -0.1480 -0.1680 0.4251 4 GLY B O 2444 N N . ALA B 5 ? 0.9213 1.1636 0.5501 -0.1375 -0.1629 0.3727 5 ALA B N 2445 C CA . ALA B 5 ? 0.9294 1.1515 0.5416 -0.1255 -0.1663 0.3508 5 ALA B CA 2446 C C . ALA B 5 ? 0.9307 1.1151 0.5515 -0.1384 -0.1813 0.3346 5 ALA B C 2447 O O . ALA B 5 ? 0.9416 1.1173 0.5585 -0.1405 -0.1930 0.3398 5 ALA B O 2448 C CB . ALA B 5 ? 0.9303 1.1444 0.5235 -0.1060 -0.1568 0.3251 5 ALA B CB 2449 N N . ILE B 6 ? 0.9264 1.0891 0.5554 -0.1438 -0.1805 0.3162 6 ILE B N 2450 C CA . ILE B 6 ? 0.9292 1.0618 0.5641 -0.1502 -0.1923 0.3015 6 ILE B CA 2451 C C . ILE B 6 ? 0.9467 1.0634 0.5839 -0.1641 -0.2078 0.3219 6 ILE B C 2452 O O . ILE B 6 ? 0.9418 1.0593 0.5857 -0.1749 -0.2083 0.3359 6 ILE B O 2453 C CB . ILE B 6 ? 0.9188 1.0364 0.5596 -0.1508 -0.1848 0.2803 6 ILE B CB 2454 C CG1 . ILE B 6 ? 0.9190 1.0433 0.5548 -0.1423 -0.1746 0.2613 6 ILE B CG1 2455 C CG2 . ILE B 6 ? 0.9222 1.0172 0.5671 -0.1515 -0.1948 0.2682 6 ILE B CG2 2456 C CD1 . ILE B 6 ? 0.9121 1.0226 0.5513 -0.1464 -0.1654 0.2461 6 ILE B CD1 2457 N N . ALA B 7 ? 0.9683 1.0665 0.5969 -0.1634 -0.2236 0.3231 7 ALA B N 2458 C CA . ALA B 7 ? 1.0007 1.0730 0.6219 -0.1773 -0.2444 0.3446 7 ALA B CA 2459 C C . ALA B 7 ? 1.0153 1.1170 0.6430 -0.1921 -0.2429 0.3797 7 ALA B C 2460 O O . ALA B 7 ? 1.0304 1.1207 0.6619 -0.2122 -0.2573 0.4028 7 ALA B O 2461 C CB . ALA B 7 ? 1.0084 1.0459 0.6280 -0.1833 -0.2548 0.3384 7 ALA B CB 2462 N N . GLY B 8 ? 1.0192 1.1601 0.6470 -0.1812 -0.2265 0.3844 8 GLY B N 2463 C CA . GLY B 8 ? 1.0323 1.2156 0.6661 -0.1886 -0.2195 0.4195 8 GLY B CA 2464 C C . GLY B 8 ? 1.0558 1.2519 0.6725 -0.1763 -0.2172 0.4271 8 GLY B C 2465 O O . GLY B 8 ? 1.0904 1.2554 0.6937 -0.1812 -0.2344 0.4303 8 GLY B O 2466 N N . PHE B 9 ? 1.0528 1.2895 0.6634 -0.1567 -0.1975 0.4290 9 PHE B N 2467 C CA . PHE B 9 ? 1.0785 1.3273 0.6670 -0.1405 -0.1948 0.4368 9 PHE B CA 2468 C C . PHE B 9 ? 1.0815 1.2973 0.6524 -0.1222 -0.2016 0.3997 9 PHE B C 2469 O O . PHE B 9 ? 1.0954 1.3107 0.6450 -0.1082 -0.2044 0.4013 9 PHE B O 2470 C CB . PHE B 9 ? 1.0848 1.3892 0.6657 -0.1210 -0.1728 0.4557 9 PHE B CB 2471 C CG . PHE B 9 ? 1.0823 1.3867 0.6459 -0.0918 -0.1608 0.4240 9 PHE B CG 2472 C CD1 . PHE B 9 ? 1.0641 1.3702 0.6383 -0.0914 -0.1533 0.4105 9 PHE B CD1 2473 C CD2 . PHE B 9 ? 1.1103 1.4073 0.6420 -0.0645 -0.1599 0.4082 9 PHE B CD2 2474 C CE1 . PHE B 9 ? 1.0708 1.3668 0.6226 -0.0666 -0.1460 0.3827 9 PHE B CE1 2475 C CE2 . PHE B 9 ? 1.1151 1.4019 0.6250 -0.0399 -0.1547 0.3795 9 PHE B CE2 2476 C CZ . PHE B 9 ? 1.0946 1.3789 0.6137 -0.0419 -0.1481 0.3672 9 PHE B CZ 2477 N N . ILE B 10 ? 1.0684 1.2607 0.6493 -0.1226 -0.2043 0.3681 10 ILE B N 2478 C CA . ILE B 10 ? 1.0730 1.2383 0.6479 -0.1132 -0.2153 0.3376 10 ILE B CA 2479 C C . ILE B 10 ? 1.0812 1.2139 0.6608 -0.1266 -0.2333 0.3390 10 ILE B C 2480 O O . ILE B 10 ? 1.0744 1.1944 0.6668 -0.1409 -0.2357 0.3417 10 ILE B O 2481 C CB . ILE B 10 ? 1.0576 1.2194 0.6415 -0.1075 -0.2090 0.3058 10 ILE B CB 2482 C CG1 . ILE B 10 ? 1.0700 1.2489 0.6365 -0.0900 -0.1974 0.3005 10 ILE B CG1 2483 C CG2 . ILE B 10 ? 1.0594 1.2046 0.6469 -0.1023 -0.2217 0.2794 10 ILE B CG2 2484 C CD1 . ILE B 10 ? 1.0715 1.2750 0.6359 -0.0887 -0.1818 0.3218 10 ILE B CD1 2485 N N . GLU B 11 ? 1.1089 1.2239 0.6720 -0.1185 -0.2477 0.3364 11 GLU B N 2486 C CA . GLU B 11 ? 1.1321 1.2081 0.6862 -0.1248 -0.2687 0.3393 11 GLU B CA 2487 C C . GLU B 11 ? 1.1047 1.1636 0.6710 -0.1221 -0.2726 0.3133 11 GLU B C 2488 O O . GLU B 11 ? 1.1197 1.1492 0.6828 -0.1320 -0.2834 0.3197 11 GLU B O 2489 C CB . GLU B 11 ? 1.1733 1.2345 0.7029 -0.1090 -0.2825 0.3356 11 GLU B CB 2490 C CG . GLU B 11 ? 1.2216 1.2339 0.7290 -0.1106 -0.3076 0.3404 11 GLU B CG 2491 C CD . GLU B 11 ? 1.2594 1.2501 0.7502 -0.1326 -0.3182 0.3797 11 GLU B CD 2492 O OE1 . GLU B 11 ? 1.2542 1.2563 0.7624 -0.1549 -0.3119 0.3996 11 GLU B OE1 2493 O OE2 . GLU B 11 ? 1.2979 1.2607 0.7584 -0.1289 -0.3341 0.3920 11 GLU B OE2 2494 N N . ASN B 12 ? 1.0724 1.1499 0.6510 -0.1086 -0.2651 0.2856 12 ASN B N 2495 C CA . ASN B 12 ? 1.0527 1.1259 0.6455 -0.1038 -0.2654 0.2630 12 ASN B CA 2496 C C . ASN B 12 ? 1.0194 1.1243 0.6336 -0.0989 -0.2530 0.2403 12 ASN B C 2497 O O . ASN B 12 ? 1.0145 1.1358 0.6263 -0.0963 -0.2485 0.2386 12 ASN B O 2498 C CB . ASN B 12 ? 1.0838 1.1315 0.6598 -0.0884 -0.2854 0.2552 12 ASN B CB 2499 C CG . ASN B 12 ? 1.0986 1.1530 0.6620 -0.0732 -0.2951 0.2501 12 ASN B CG 2500 O OD1 . ASN B 12 ? 1.1355 1.1616 0.6706 -0.0702 -0.3104 0.2648 12 ASN B OD1 2501 N ND2 . ASN B 12 ? 1.0780 1.1667 0.6603 -0.0648 -0.2887 0.2302 12 ASN B ND2 2502 N N . GLY B 13 ? 1.0033 1.1142 0.6350 -0.0976 -0.2490 0.2244 13 GLY B N 2503 C CA . GLY B 13 ? 0.9845 1.1249 0.6397 -0.0985 -0.2403 0.2057 13 GLY B CA 2504 C C . GLY B 13 ? 0.9937 1.1542 0.6571 -0.0843 -0.2524 0.1908 13 GLY B C 2505 O O . GLY B 13 ? 1.0099 1.1581 0.6574 -0.0696 -0.2665 0.1926 13 GLY B O 2506 N N . TRP B 14 ? 0.9855 1.1750 0.6723 -0.0896 -0.2493 0.1765 14 TRP B N 2507 C CA . TRP B 14 ? 0.9947 1.2141 0.6980 -0.0794 -0.2617 0.1622 14 TRP B CA 2508 C C . TRP B 14 ? 0.9812 1.2361 0.7185 -0.0807 -0.2548 0.1539 14 TRP B C 2509 O O . TRP B 14 ? 0.9736 1.2411 0.7314 -0.0989 -0.2423 0.1528 14 TRP B O 2510 C CB . TRP B 14 ? 1.0034 1.2316 0.7092 -0.0866 -0.2684 0.1539 14 TRP B CB 2511 C CG . TRP B 14 ? 1.0249 1.2251 0.6941 -0.0793 -0.2731 0.1626 14 TRP B CG 2512 C CD1 . TRP B 14 ? 1.0428 1.2238 0.6849 -0.0656 -0.2790 0.1749 14 TRP B CD1 2513 C CD2 . TRP B 14 ? 1.0367 1.2250 0.6882 -0.0830 -0.2727 0.1614 14 TRP B CD2 2514 N NE1 . TRP B 14 ? 1.0576 1.2243 0.6712 -0.0615 -0.2788 0.1839 14 TRP B NE1 2515 C CE2 . TRP B 14 ? 1.0583 1.2289 0.6747 -0.0686 -0.2750 0.1745 14 TRP B CE2 2516 C CE3 . TRP B 14 ? 1.0403 1.2272 0.6971 -0.0958 -0.2721 0.1514 14 TRP B CE3 2517 C CZ2 . TRP B 14 ? 1.0805 1.2386 0.6670 -0.0613 -0.2740 0.1771 14 TRP B CZ2 2518 C CZ3 . TRP B 14 ? 1.0664 1.2303 0.6882 -0.0884 -0.2750 0.1515 14 TRP B CZ3 2519 C CH2 . TRP B 14 ? 1.0859 1.2388 0.6728 -0.0687 -0.2747 0.1640 14 TRP B CH2 2520 N N . GLU B 15 ? 0.9900 1.2613 0.7301 -0.0592 -0.2627 0.1495 15 GLU B N 2521 C CA . GLU B 15 ? 0.9837 1.3011 0.7562 -0.0534 -0.2549 0.1436 15 GLU B CA 2522 C C . GLU B 15 ? 0.9804 1.3545 0.7953 -0.0645 -0.2597 0.1345 15 GLU B C 2523 O O . GLU B 15 ? 0.9707 1.3940 0.8229 -0.0710 -0.2495 0.1341 15 GLU B O 2524 C CB . GLU B 15 ? 1.0050 1.3199 0.7587 -0.0194 -0.2633 0.1416 15 GLU B CB 2525 C CG . GLU B 15 ? 1.0251 1.2782 0.7360 -0.0121 -0.2634 0.1514 15 GLU B CG 2526 C CD . GLU B 15 ? 1.0648 1.2945 0.7410 0.0233 -0.2799 0.1487 15 GLU B CD 2527 O OE1 . GLU B 15 ? 1.0731 1.3467 0.7632 0.0488 -0.2823 0.1386 15 GLU B OE1 2528 O OE2 . GLU B 15 ? 1.0928 1.2594 0.7260 0.0259 -0.2920 0.1577 15 GLU B OE2 2529 N N . GLY B 16 ? 0.9953 1.3629 0.8036 -0.0675 -0.2764 0.1288 16 GLY B N 2530 C CA . GLY B 16 ? 0.9963 1.4071 0.8402 -0.0821 -0.2878 0.1199 16 GLY B CA 2531 C C . GLY B 16 ? 0.9925 1.3953 0.8493 -0.1163 -0.2809 0.1219 16 GLY B C 2532 O O . GLY B 16 ? 0.9947 1.4356 0.8880 -0.1362 -0.2891 0.1178 16 GLY B O 2533 N N . LEU B 17 ? 0.9890 1.3416 0.8149 -0.1236 -0.2682 0.1290 17 LEU B N 2534 C CA . LEU B 17 ? 0.9884 1.3212 0.8143 -0.1510 -0.2629 0.1301 17 LEU B CA 2535 C C . LEU B 17 ? 0.9728 1.3337 0.8311 -0.1687 -0.2448 0.1365 17 LEU B C 2536 O O . LEU B 17 ? 0.9651 1.3023 0.8090 -0.1689 -0.2262 0.1442 17 LEU B O 2537 C CB . LEU B 17 ? 0.9900 1.2658 0.7704 -0.1474 -0.2554 0.1361 17 LEU B CB 2538 C CG . LEU B 17 ? 1.0025 1.2473 0.7686 -0.1677 -0.2535 0.1351 17 LEU B CG 2539 C CD1 . LEU B 17 ? 1.0315 1.2689 0.7908 -0.1739 -0.2780 0.1235 17 LEU B CD1 2540 C CD2 . LEU B 17 ? 0.9995 1.2021 0.7254 -0.1584 -0.2417 0.1437 17 LEU B CD2 2541 N N . ILE B 18 ? 0.9758 1.3901 0.8787 -0.1840 -0.2509 0.1348 18 ILE B N 2542 C CA . ILE B 18 ? 0.9686 1.4186 0.9062 -0.2040 -0.2333 0.1445 18 ILE B CA 2543 C C . ILE B 18 ? 0.9863 1.4120 0.9258 -0.2421 -0.2383 0.1466 18 ILE B C 2544 O O . ILE B 18 ? 0.9831 1.4272 0.9450 -0.2640 -0.2237 0.1572 18 ILE B O 2545 C CB . ILE B 18 ? 0.9641 1.5004 0.9547 -0.1983 -0.2331 0.1474 18 ILE B CB 2546 C CG1 . ILE B 18 ? 0.9772 1.5475 0.9916 -0.2012 -0.2616 0.1382 18 ILE B CG1 2547 C CG2 . ILE B 18 ? 0.9538 1.5036 0.9322 -0.1578 -0.2213 0.1478 18 ILE B CG2 2548 C CD1 . ILE B 18 ? 1.0041 1.5545 1.0249 -0.2393 -0.2823 0.1355 18 ILE B CD1 2549 N N . ASP B 19 ? 1.0121 1.3915 0.9220 -0.2475 -0.2598 0.1371 19 ASP B N 2550 C CA . ASP B 19 ? 1.0450 1.3857 0.9431 -0.2795 -0.2725 0.1360 19 ASP B CA 2551 C C . ASP B 19 ? 1.0325 1.3182 0.8940 -0.2837 -0.2536 0.1417 19 ASP B C 2552 O O . ASP B 19 ? 1.0503 1.3199 0.9147 -0.3129 -0.2528 0.1474 19 ASP B O 2553 C CB . ASP B 19 ? 1.0854 1.3835 0.9484 -0.2735 -0.3026 0.1220 19 ASP B CB 2554 C CG . ASP B 19 ? 1.1041 1.4491 1.0026 -0.2781 -0.3289 0.1152 19 ASP B CG 2555 O OD1 . ASP B 19 ? 1.1299 1.5108 1.0715 -0.3115 -0.3404 0.1200 19 ASP B OD1 2556 O OD2 . ASP B 19 ? 1.1090 1.4554 0.9923 -0.2497 -0.3395 0.1064 19 ASP B OD2 2557 N N . GLY B 20 ? 1.0069 1.2632 0.8331 -0.2555 -0.2406 0.1412 20 GLY B N 2558 C CA . GLY B 20 ? 0.9992 1.2070 0.7897 -0.2543 -0.2240 0.1461 20 GLY B CA 2559 C C . GLY B 20 ? 0.9659 1.1666 0.7371 -0.2256 -0.2091 0.1503 20 GLY B C 2560 O O . GLY B 20 ? 0.9460 1.1763 0.7313 -0.2083 -0.2099 0.1505 20 GLY B O 2561 N N . TRP B 21 ? 0.9612 1.1208 0.6987 -0.2210 -0.1979 0.1543 21 TRP B N 2562 C CA . TRP B 21 ? 0.9336 1.0857 0.6549 -0.1996 -0.1863 0.1615 21 TRP B CA 2563 C C . TRP B 21 ? 0.9364 1.0776 0.6325 -0.1810 -0.1978 0.1606 21 TRP B C 2564 O O . TRP B 21 ? 0.9225 1.0755 0.6200 -0.1665 -0.1973 0.1665 21 TRP B O 2565 C CB . TRP B 21 ? 0.9323 1.0517 0.6302 -0.2015 -0.1714 0.1675 21 TRP B CB 2566 C CG . TRP B 21 ? 0.9214 1.0495 0.6380 -0.2138 -0.1560 0.1719 21 TRP B CG 2567 C CD1 . TRP B 21 ? 0.9228 1.0811 0.6718 -0.2308 -0.1541 0.1717 21 TRP B CD1 2568 C CD2 . TRP B 21 ? 0.9095 1.0189 0.6125 -0.2090 -0.1402 0.1788 21 TRP B CD2 2569 N NE1 . TRP B 21 ? 0.9170 1.0767 0.6707 -0.2349 -0.1357 0.1790 21 TRP B NE1 2570 C CE2 . TRP B 21 ? 0.9115 1.0370 0.6348 -0.2210 -0.1281 0.1819 21 TRP B CE2 2571 C CE3 . TRP B 21 ? 0.9041 0.9888 0.5810 -0.1957 -0.1359 0.1843 21 TRP B CE3 2572 C CZ2 . TRP B 21 ? 0.9085 1.0185 0.6206 -0.2172 -0.1121 0.1879 21 TRP B CZ2 2573 C CZ3 . TRP B 21 ? 0.9034 0.9738 0.5730 -0.1944 -0.1226 0.1896 21 TRP B CZ3 2574 C CH2 . TRP B 21 ? 0.9055 0.9847 0.5895 -0.2037 -0.1111 0.1902 21 TRP B CH2 2575 N N . TYR B 22 ? 0.9647 1.0798 0.6332 -0.1805 -0.2091 0.1541 22 TYR B N 2576 C CA . TYR B 22 ? 0.9783 1.0829 0.6156 -0.1590 -0.2178 0.1546 22 TYR B CA 2577 C C . TYR B 22 ? 1.0149 1.1155 0.6458 -0.1591 -0.2412 0.1412 22 TYR B C 2578 O O . TYR B 22 ? 1.0328 1.1266 0.6746 -0.1792 -0.2526 0.1320 22 TYR B O 2579 C CB . TYR B 22 ? 0.9903 1.0635 0.5863 -0.1471 -0.2100 0.1596 22 TYR B CB 2580 C CG . TYR B 22 ? 0.9649 1.0371 0.5669 -0.1514 -0.1906 0.1703 22 TYR B CG 2581 C CD1 . TYR B 22 ? 0.9368 1.0258 0.5440 -0.1419 -0.1808 0.1854 22 TYR B CD1 2582 C CD2 . TYR B 22 ? 0.9710 1.0219 0.5714 -0.1664 -0.1847 0.1662 22 TYR B CD2 2583 C CE1 . TYR B 22 ? 0.9208 1.0064 0.5325 -0.1460 -0.1674 0.1943 22 TYR B CE1 2584 C CE2 . TYR B 22 ? 0.9533 1.0007 0.5557 -0.1678 -0.1684 0.1748 22 TYR B CE2 2585 C CZ . TYR B 22 ? 0.9261 0.9913 0.5345 -0.1569 -0.1606 0.1879 22 TYR B CZ 2586 O OH . TYR B 22 ? 0.9078 0.9672 0.5170 -0.1584 -0.1485 0.1958 22 TYR B OH 2587 N N . GLY B 23 ? 1.0284 1.1317 0.6404 -0.1381 -0.2499 0.1416 23 GLY B N 2588 C CA . GLY B 23 ? 1.0706 1.1684 0.6728 -0.1342 -0.2748 0.1281 23 GLY B CA 2589 C C . GLY B 23 ? 1.0947 1.1864 0.6611 -0.1049 -0.2814 0.1305 23 GLY B C 2590 O O . GLY B 23 ? 1.0808 1.1773 0.6321 -0.0892 -0.2655 0.1461 23 GLY B O 2591 N N . PHE B 24 ? 1.1414 1.2237 0.6946 -0.0990 -0.3063 0.1166 24 PHE B N 2592 C CA . PHE B 24 ? 1.1766 1.2512 0.6916 -0.0691 -0.3158 0.1170 24 PHE B CA 2593 C C . PHE B 24 ? 1.1730 1.2754 0.7157 -0.0690 -0.3316 0.1106 24 PHE B C 2594 O O . PHE B 24 ? 1.1613 1.2799 0.7403 -0.0893 -0.3469 0.0986 24 PHE B O 2595 C CB . PHE B 24 ? 1.2406 1.2689 0.7012 -0.0541 -0.3368 0.1030 24 PHE B CB 2596 C CG . PHE B 24 ? 1.2641 1.2564 0.6973 -0.0580 -0.3306 0.1018 24 PHE B CG 2597 C CD1 . PHE B 24 ? 1.2712 1.2473 0.7257 -0.0900 -0.3408 0.0920 24 PHE B CD1 2598 C CD2 . PHE B 24 ? 1.2816 1.2578 0.6660 -0.0285 -0.3152 0.1118 24 PHE B CD2 2599 C CE1 . PHE B 24 ? 1.2999 1.2343 0.7222 -0.0924 -0.3373 0.0905 24 PHE B CE1 2600 C CE2 . PHE B 24 ? 1.3093 1.2505 0.6634 -0.0271 -0.3110 0.1093 24 PHE B CE2 2601 C CZ . PHE B 24 ? 1.3196 1.2346 0.6897 -0.0589 -0.3229 0.0977 24 PHE B CZ 2602 N N . ARG B 25 ? 1.1875 1.2980 0.7129 -0.0462 -0.3281 0.1205 25 ARG B N 2603 C CA . ARG B 25 ? 1.2053 1.3337 0.7418 -0.0372 -0.3457 0.1138 25 ARG B CA 2604 C C . ARG B 25 ? 1.2512 1.3575 0.7329 -0.0054 -0.3549 0.1157 25 ARG B C 2605 O O . ARG B 25 ? 1.2558 1.3604 0.7123 0.0100 -0.3372 0.1358 25 ARG B O 2606 C CB . ARG B 25 ? 1.1720 1.3283 0.7393 -0.0402 -0.3326 0.1263 25 ARG B CB 2607 C CG . ARG B 25 ? 1.1832 1.3548 0.7554 -0.0256 -0.3501 0.1203 25 ARG B CG 2608 C CD . ARG B 25 ? 1.1599 1.3504 0.7572 -0.0273 -0.3404 0.1299 25 ARG B CD 2609 N NE . ARG B 25 ? 1.1356 1.3570 0.7822 -0.0461 -0.3368 0.1220 25 ARG B NE 2610 C CZ . ARG B 25 ? 1.1169 1.3528 0.7836 -0.0464 -0.3270 0.1282 25 ARG B CZ 2611 N NH1 . ARG B 25 ? 1.1240 1.3387 0.7654 -0.0331 -0.3233 0.1421 25 ARG B NH1 2612 N NH2 . ARG B 25 ? 1.0951 1.3642 0.8041 -0.0600 -0.3220 0.1220 25 ARG B NH2 2613 N N . HIS B 26 ? 1.2976 1.3888 0.7610 0.0038 -0.3833 0.0967 26 HIS B N 2614 C CA . HIS B 26 ? 1.3500 1.4134 0.7516 0.0384 -0.3939 0.0960 26 HIS B CA 2615 C C . HIS B 26 ? 1.3725 1.4463 0.7707 0.0553 -0.4113 0.0916 26 HIS B C 2616 O O . HIS B 26 ? 1.3470 1.4497 0.7911 0.0413 -0.4206 0.0847 26 HIS B O 2617 C CB . HIS B 26 ? 1.4032 1.4244 0.7654 0.0448 -0.4179 0.0764 26 HIS B CB 2618 C CG . HIS B 26 ? 1.4136 1.4360 0.8090 0.0210 -0.4512 0.0537 26 HIS B CG 2619 N ND1 . HIS B 26 ? 1.4400 1.4686 0.8366 0.0306 -0.4802 0.0402 26 HIS B ND1 2620 C CD2 . HIS B 26 ? 1.4054 1.4268 0.8358 -0.0137 -0.4609 0.0445 26 HIS B CD2 2621 C CE1 . HIS B 26 ? 1.4437 1.4812 0.8796 0.0014 -0.5069 0.0243 26 HIS B CE1 2622 N NE2 . HIS B 26 ? 1.4251 1.4581 0.8822 -0.0272 -0.4953 0.0278 26 HIS B NE2 2623 N N . GLN B 27 ? 1.4244 1.4756 0.7638 0.0892 -0.4146 0.0967 27 GLN B N 2624 C CA . GLN B 27 ? 1.4612 1.5114 0.7815 0.1116 -0.4334 0.0919 27 GLN B CA 2625 C C . GLN B 27 ? 1.5312 1.5415 0.7813 0.1459 -0.4517 0.0818 27 GLN B C 2626 O O . GLN B 27 ? 1.5517 1.5442 0.7552 0.1656 -0.4345 0.0947 27 GLN B O 2627 C CB . GLN B 27 ? 1.4501 1.5142 0.7651 0.1206 -0.4112 0.1190 27 GLN B CB 2628 C CG . GLN B 27 ? 1.4873 1.5455 0.7774 0.1450 -0.4294 0.1165 27 GLN B CG 2629 C CD . GLN B 27 ? 1.4682 1.5500 0.8070 0.1325 -0.4483 0.1003 27 GLN B CD 2630 O OE1 . GLN B 27 ? 1.4972 1.5792 0.8356 0.1425 -0.4783 0.0777 27 GLN B OE1 2631 N NE2 . GLN B 27 ? 1.4266 1.5297 0.8056 0.1131 -0.4321 0.1120 27 GLN B NE2 2632 N N . ASN B 28 ? 1.5675 1.5654 0.8084 0.1556 -0.4877 0.0588 28 ASN B N 2633 C CA . ASN B 28 ? 1.6454 1.5972 0.8139 0.1907 -0.5122 0.0449 28 ASN B CA 2634 C C . ASN B 28 ? 1.6817 1.6292 0.8438 0.2047 -0.5493 0.0255 28 ASN B C 2635 O O . ASN B 28 ? 1.6462 1.6293 0.8525 0.1947 -0.5497 0.0277 28 ASN B O 2636 C CB . ASN B 28 ? 1.6775 1.5932 0.8302 0.1805 -0.5288 0.0274 28 ASN B CB 2637 C CG . ASN B 28 ? 1.6604 1.5881 0.8753 0.1387 -0.5579 0.0065 28 ASN B CG 2638 O OD1 . ASN B 28 ? 1.6178 1.5908 0.8936 0.1189 -0.5617 0.0053 28 ASN B OD1 2639 N ND2 . ASN B 28 ? 1.6984 1.5859 0.8959 0.1260 -0.5790 -0.0085 28 ASN B ND2 2640 N N . ALA B 29 ? 1.7559 1.6572 0.8584 0.2313 -0.5820 0.0059 29 ALA B N 2641 C CA . ALA B 29 ? 1.7997 1.6929 0.8920 0.2461 -0.6227 -0.0150 29 ALA B CA 2642 C C . ALA B 29 ? 1.7582 1.6935 0.9351 0.2054 -0.6470 -0.0311 29 ALA B C 2643 O O . ALA B 29 ? 1.7469 1.7118 0.9487 0.2107 -0.6601 -0.0357 29 ALA B O 2644 C CB . ALA B 29 ? 1.8951 1.7233 0.9077 0.2778 -0.6586 -0.0359 29 ALA B CB 2645 N N . GLN B 30 ? 1.7364 1.6769 0.9560 0.1664 -0.6522 -0.0377 30 GLN B N 2646 C CA . GLN B 30 ? 1.6974 1.6880 1.0024 0.1249 -0.6722 -0.0483 30 GLN B CA 2647 C C . GLN B 30 ? 1.6096 1.6672 0.9848 0.1067 -0.6381 -0.0311 30 GLN B C 2648 O O . GLN B 30 ? 1.5789 1.6905 1.0223 0.0839 -0.6515 -0.0375 30 GLN B O 2649 C CB . GLN B 30 ? 1.7101 1.6824 1.0357 0.0862 -0.6892 -0.0573 30 GLN B CB 2650 C CG . GLN B 30 ? 1.8027 1.7081 1.0698 0.0958 -0.7398 -0.0803 30 GLN B CG 2651 C CD . GLN B 30 ? 1.8577 1.6871 1.0401 0.1186 -0.7323 -0.0797 30 GLN B CD 2652 O OE1 . GLN B 30 ? 1.8391 1.6649 0.9863 0.1461 -0.6907 -0.0620 30 GLN B OE1 2653 N NE2 . GLN B 30 ? 1.9311 1.6994 1.0787 0.1078 -0.7748 -0.0984 30 GLN B NE2 2654 N N . GLY B 31 ? 1.5752 1.6304 0.9328 0.1179 -0.5960 -0.0088 31 GLY B N 2655 C CA . GLY B 31 ? 1.5115 1.6156 0.9209 0.1059 -0.5668 0.0073 31 GLY B CA 2656 C C . GLY B 31 ? 1.4650 1.5750 0.8974 0.0808 -0.5311 0.0240 31 GLY B C 2657 O O . GLY B 31 ? 1.4810 1.5541 0.8734 0.0845 -0.5190 0.0301 31 GLY B O 2658 N N . GLU B 32 ? 1.4261 1.6022 0.9169 0.0030 -0.4449 0.0864 32 GLU B N 2659 C CA . GLU B 32 ? 1.3768 1.5261 0.8976 0.0058 -0.4130 0.0717 32 GLU B CA 2660 C C . GLU B 32 ? 1.2970 1.5480 0.9025 0.0079 -0.3980 0.0603 32 GLU B C 2661 O O . GLU B 32 ? 1.2841 1.6391 0.9296 0.0297 -0.4172 0.0729 32 GLU B O 2662 C CB . GLU B 32 ? 1.4386 1.4990 0.9136 0.0571 -0.4275 0.0822 32 GLU B CB 2663 C CG . GLU B 32 ? 1.4005 1.4342 0.9026 0.0650 -0.4010 0.0688 32 GLU B CG 2664 C CD . GLU B 32 ? 1.4969 1.3881 0.9124 0.0820 -0.4216 0.0805 32 GLU B CD 2665 O OE1 . GLU B 32 ? 1.5623 1.3740 0.9094 0.0338 -0.4348 0.0993 32 GLU B OE1 2666 O OE2 . GLU B 32 ? 1.5210 1.3776 0.9264 0.1396 -0.4283 0.0738 32 GLU B OE2 2667 N N . GLY B 33 ? 1.2489 1.4807 0.8788 -0.0185 -0.3661 0.0419 33 GLY B N 2668 C CA . GLY B 33 ? 1.1875 1.4948 0.8863 -0.0254 -0.3531 0.0344 33 GLY B CA 2669 C C . GLY B 33 ? 1.1465 1.4037 0.8592 -0.0250 -0.3204 0.0185 33 GLY B C 2670 O O . GLY B 33 ? 1.1563 1.3371 0.8298 -0.0396 -0.3049 0.0115 33 GLY B O 2671 N N . THR B 34 ? 1.1006 1.4190 0.8703 -0.0108 -0.3105 0.0178 34 THR B N 2672 C CA . THR B 34 ? 1.0657 1.3432 0.8516 -0.0065 -0.2822 0.0046 34 THR B CA 2673 C C . THR B 34 ? 1.0123 1.3507 0.8501 -0.0381 -0.2724 -0.0004 34 THR B C 2674 O O . THR B 34 ? 0.9969 1.4420 0.8754 -0.0426 -0.2876 0.0165 34 THR B O 2675 C CB . THR B 34 ? 1.0891 1.3483 0.8679 0.0570 -0.2836 0.0101 34 THR B CB 2676 O OG1 . THR B 34 ? 1.0657 1.4339 0.9020 0.0865 -0.2792 0.0151 34 THR B OG1 2677 C CG2 . THR B 34 ? 1.1705 1.3895 0.8899 0.1004 -0.3139 0.0233 34 THR B CG2 2678 N N . ALA B 35 ? 0.9888 1.2680 0.8207 -0.0617 -0.2508 -0.0180 35 ALA B N 2679 C CA . ALA B 35 ? 0.9668 1.2708 0.8274 -0.0949 -0.2479 -0.0221 35 ALA B CA 2680 C C . ALA B 35 ? 0.9379 1.1857 0.8026 -0.0878 -0.2193 -0.0379 35 ALA B C 2681 O O . ALA B 35 ? 0.9443 1.1348 0.7820 -0.0733 -0.2030 -0.0465 35 ALA B O 2682 C CB . ALA B 35 ? 1.0200 1.2894 0.8355 -0.1455 -0.2709 -0.0287 35 ALA B CB 2683 N N . ALA B 36 ? 0.9152 1.1917 0.8128 -0.1045 -0.2162 -0.0359 36 ALA B N 2684 C CA . ALA B 36 ? 0.8870 1.1200 0.7930 -0.0965 -0.1916 -0.0482 36 ALA B CA 2685 C C . ALA B 36 ? 0.9325 1.0875 0.7935 -0.1212 -0.1924 -0.0672 36 ALA B C 2686 O O . ALA B 36 ? 0.9858 1.1154 0.8089 -0.1569 -0.2199 -0.0683 36 ALA B O 2687 C CB . ALA B 36 ? 0.8459 1.1506 0.8039 -0.0931 -0.1872 -0.0348 36 ALA B CB 2688 N N . ASP B 37 ? 0.9216 1.0348 0.7754 -0.0995 -0.1675 -0.0802 37 ASP B N 2689 C CA . ASP B 37 ? 0.9713 1.0147 0.7761 -0.0984 -0.1654 -0.1003 37 ASP B CA 2690 C C . ASP B 37 ? 0.9674 0.9998 0.7948 -0.1114 -0.1656 -0.0984 37 ASP B C 2691 O O . ASP B 37 ? 0.9119 0.9748 0.7855 -0.0959 -0.1435 -0.0927 37 ASP B O 2692 C CB . ASP B 37 ? 0.9643 1.0043 0.7518 -0.0629 -0.1375 -0.1085 37 ASP B CB 2693 C CG . ASP B 37 ? 1.0286 1.0104 0.7536 -0.0366 -0.1340 -0.1316 37 ASP B CG 2694 O OD1 . ASP B 37 ? 1.1171 1.0304 0.7648 -0.0350 -0.1571 -0.1493 37 ASP B OD1 2695 O OD2 . ASP B 37 ? 1.0059 1.0037 0.7473 -0.0126 -0.1122 -0.1325 37 ASP B OD2 2696 N N . TYR B 38 ? 1.0428 1.0195 0.8243 -0.1461 -0.1967 -0.1006 38 TYR B N 2697 C CA . TYR B 38 ? 1.0548 1.0138 0.8444 -0.1727 -0.2064 -0.0923 38 TYR B CA 2698 C C . TYR B 38 ? 1.0450 0.9474 0.8171 -0.1328 -0.1846 -0.1108 38 TYR B C 2699 O O . TYR B 38 ? 0.9835 0.9240 0.8080 -0.1310 -0.1675 -0.1013 38 TYR B O 2700 C CB . TYR B 38 ? 1.1826 1.0643 0.8960 -0.2327 -0.2588 -0.0853 38 TYR B CB 2701 C CG . TYR B 38 ? 1.2263 1.0893 0.9368 -0.2803 -0.2798 -0.0659 38 TYR B CG 2702 C CD1 . TYR B 38 ? 1.1699 1.1687 0.9603 -0.3252 -0.2812 -0.0271 38 TYR B CD1 2703 C CD2 . TYR B 38 ? 1.3394 1.0543 0.9582 -0.2753 -0.3003 -0.0840 38 TYR B CD2 2704 C CE1 . TYR B 38 ? 1.2069 1.2048 0.9932 -0.3770 -0.3009 -0.0025 38 TYR B CE1 2705 C CE2 . TYR B 38 ? 1.3864 1.0723 0.9921 -0.3264 -0.3252 -0.0619 38 TYR B CE2 2706 C CZ . TYR B 38 ? 1.3149 1.1476 1.0079 -0.3840 -0.3248 -0.0189 38 TYR B CZ 2707 O OH . TYR B 38 ? 1.3612 1.1820 1.0407 -0.4425 -0.3497 0.0098 38 TYR B OH 2708 N N . LYS B 39 ? 1.1133 0.9357 0.8076 -0.0940 -0.1854 -0.1365 39 LYS B N 2709 C CA . LYS B 39 ? 1.1336 0.9095 0.7961 -0.0458 -0.1705 -0.1533 39 LYS B CA 2710 C C . LYS B 39 ? 1.0119 0.8899 0.7642 -0.0239 -0.1288 -0.1409 39 LYS B C 2711 O O . LYS B 39 ? 0.9872 0.8606 0.7590 -0.0181 -0.1219 -0.1377 39 LYS B O 2712 C CB . LYS B 39 ? 1.2403 0.9508 0.8025 0.0145 -0.1720 -0.1823 39 LYS B CB 2713 C CG . LYS B 39 ? 1.3975 0.9568 0.8372 0.0476 -0.2032 -0.2070 39 LYS B CG 2714 C CD . LYS B 39 ? 1.5290 0.9482 0.8746 -0.0150 -0.2653 -0.2072 39 LYS B CD 2715 C CE . LYS B 39 ? 1.7387 0.9536 0.9123 0.0243 -0.3110 -0.2365 39 LYS B CE 2716 N NZ . LYS B 39 ? 1.8626 1.0087 0.9156 0.1112 -0.3114 -0.2745 39 LYS B NZ 2717 N N . SER B 40 ? 0.9395 0.8966 0.7335 -0.0182 -0.1082 -0.1311 40 SER B N 2718 C CA . SER B 40 ? 0.8482 0.8806 0.7036 -0.0122 -0.0817 -0.1138 40 SER B CA 2719 C C . SER B 40 ? 0.7899 0.8375 0.7004 -0.0399 -0.0840 -0.0998 40 SER B C 2720 O O . SER B 40 ? 0.7513 0.8121 0.6884 -0.0360 -0.0725 -0.0931 40 SER B O 2721 C CB . SER B 40 ? 0.8266 0.9128 0.6888 -0.0142 -0.0732 -0.1009 40 SER B CB 2722 O OG . SER B 40 ? 0.8172 0.8947 0.6846 -0.0372 -0.0903 -0.0972 40 SER B OG 2723 N N . THR B 41 ? 0.7768 0.8344 0.7003 -0.0623 -0.0989 -0.0938 41 THR B N 2724 C CA . THR B 41 ? 0.7373 0.8314 0.7041 -0.0736 -0.0996 -0.0808 41 THR B CA 2725 C C . THR B 41 ? 0.7453 0.8197 0.7166 -0.0863 -0.1009 -0.0806 41 THR B C 2726 O O . THR B 41 ? 0.7165 0.8105 0.7159 -0.0797 -0.0889 -0.0743 41 THR B O 2727 C CB . THR B 41 ? 0.7407 0.8814 0.7191 -0.0894 -0.1169 -0.0702 41 THR B CB 2728 O OG1 . THR B 41 ? 0.7321 0.8880 0.7064 -0.0694 -0.1164 -0.0679 41 THR B OG1 2729 C CG2 . THR B 41 ? 0.7101 0.9191 0.7286 -0.0924 -0.1157 -0.0543 41 THR B CG2 2730 N N . GLN B 42 ? 0.8112 0.8283 0.7380 -0.1047 -0.1210 -0.0877 42 GLN B N 2731 C CA . GLN B 42 ? 0.8461 0.8234 0.7580 -0.1266 -0.1337 -0.0831 42 GLN B CA 2732 C C . GLN B 42 ? 0.8415 0.7869 0.7489 -0.0918 -0.1161 -0.0933 42 GLN B C 2733 O O . GLN B 42 ? 0.8217 0.7710 0.7481 -0.1024 -0.1139 -0.0840 42 GLN B O 2734 C CB . GLN B 42 ? 0.9576 0.8427 0.7898 -0.1608 -0.1746 -0.0862 42 GLN B CB 2735 C CG . GLN B 42 ? 1.0159 0.8617 0.8238 -0.2114 -0.2031 -0.0676 42 GLN B CG 2736 C CD . GLN B 42 ? 0.9537 0.9321 0.8364 -0.2559 -0.1994 -0.0327 42 GLN B CD 2737 O OE1 . GLN B 42 ? 0.9013 0.9828 0.8330 -0.2536 -0.1893 -0.0228 42 GLN B OE1 2738 N NE2 . GLN B 42 ? 0.9677 0.9524 0.8538 -0.2896 -0.2079 -0.0124 42 GLN B NE2 2739 N N . SER B 43 ? 0.8579 0.7904 0.7411 -0.0501 -0.1035 -0.1082 43 SER B N 2740 C CA . SER B 43 ? 0.8487 0.7884 0.7339 -0.0127 -0.0862 -0.1114 43 SER B CA 2741 C C . SER B 43 ? 0.7672 0.7765 0.7193 -0.0233 -0.0667 -0.0934 43 SER B C 2742 O O . SER B 43 ? 0.7513 0.7609 0.7145 -0.0169 -0.0620 -0.0886 43 SER B O 2743 C CB . SER B 43 ? 0.8845 0.8457 0.7372 0.0350 -0.0736 -0.1222 43 SER B CB 2744 O OG . SER B 43 ? 0.9133 0.8944 0.7566 0.0799 -0.0617 -0.1235 43 SER B OG 2745 N N . ALA B 44 ? 0.7175 0.7688 0.6982 -0.0374 -0.0614 -0.0839 44 ALA B N 2746 C CA . ALA B 44 ? 0.6725 0.7504 0.6830 -0.0460 -0.0547 -0.0696 44 ALA B CA 2747 C C . ALA B 44 ? 0.6568 0.7292 0.6832 -0.0570 -0.0581 -0.0673 44 ALA B C 2748 O O . ALA B 44 ? 0.6495 0.7208 0.6847 -0.0573 -0.0538 -0.0614 44 ALA B O 2749 C CB . ALA B 44 ? 0.6728 0.7618 0.6782 -0.0507 -0.0586 -0.0621 44 ALA B CB 2750 N N . ILE B 45 ? 0.6570 0.7412 0.6856 -0.0692 -0.0671 -0.0675 45 ILE B N 2751 C CA . ILE B 45 ? 0.6436 0.7614 0.6897 -0.0828 -0.0693 -0.0572 45 ILE B CA 2752 C C . ILE B 45 ? 0.6609 0.7459 0.6998 -0.0989 -0.0728 -0.0542 45 ILE B C 2753 O O . ILE B 45 ? 0.6383 0.7450 0.6909 -0.0994 -0.0659 -0.0461 45 ILE B O 2754 C CB . ILE B 45 ? 0.6517 0.8185 0.7035 -0.1059 -0.0834 -0.0470 45 ILE B CB 2755 C CG1 . ILE B 45 ? 0.6391 0.8547 0.7009 -0.0771 -0.0792 -0.0467 45 ILE B CG1 2756 C CG2 . ILE B 45 ? 0.6530 0.8805 0.7216 -0.1355 -0.0887 -0.0255 45 ILE B CG2 2757 C CD1 . ILE B 45 ? 0.6459 0.9360 0.7199 -0.0960 -0.0936 -0.0322 45 ILE B CD1 2758 N N . ASP B 46 ? 0.7130 0.7346 0.7157 -0.1053 -0.0867 -0.0620 46 ASP B N 2759 C CA . ASP B 46 ? 0.7616 0.7252 0.7357 -0.1140 -0.0987 -0.0600 46 ASP B CA 2760 C C . ASP B 46 ? 0.7310 0.7024 0.7237 -0.0855 -0.0808 -0.0616 46 ASP B C 2761 O O . ASP B 46 ? 0.7399 0.7025 0.7343 -0.0969 -0.0835 -0.0523 46 ASP B O 2762 C CB . ASP B 46 ? 0.8546 0.7174 0.7546 -0.1064 -0.1240 -0.0743 46 ASP B CB 2763 C CG . ASP B 46 ? 0.9193 0.7464 0.7786 -0.1565 -0.1576 -0.0656 46 ASP B CG 2764 O OD1 . ASP B 46 ? 0.8784 0.7858 0.7794 -0.2015 -0.1596 -0.0415 46 ASP B OD1 2765 O OD2 . ASP B 46 ? 1.0239 0.7471 0.8010 -0.1488 -0.1848 -0.0808 46 ASP B OD2 2766 N N . GLN B 47 ? 0.7082 0.7049 0.7125 -0.0566 -0.0661 -0.0676 47 GLN B N 2767 C CA . GLN B 47 ? 0.6889 0.7120 0.7108 -0.0418 -0.0549 -0.0602 47 GLN B CA 2768 C C . GLN B 47 ? 0.6526 0.6959 0.6971 -0.0603 -0.0508 -0.0494 47 GLN B C 2769 O O . GLN B 47 ? 0.6411 0.6822 0.6892 -0.0624 -0.0507 -0.0418 47 GLN B O 2770 C CB . GLN B 47 ? 0.6793 0.7495 0.7059 -0.0229 -0.0453 -0.0572 47 GLN B CB 2771 C CG . GLN B 47 ? 0.7329 0.7983 0.7255 0.0185 -0.0449 -0.0693 47 GLN B CG 2772 C CD . GLN B 47 ? 0.7218 0.8728 0.7242 0.0341 -0.0315 -0.0586 47 GLN B CD 2773 O OE1 . GLN B 47 ? 0.7127 0.9437 0.7372 0.0394 -0.0237 -0.0377 47 GLN B OE1 2774 N NE2 . GLN B 47 ? 0.7373 0.8851 0.7227 0.0347 -0.0311 -0.0669 47 GLN B NE2 2775 N N . ILE B 48 ? 0.6440 0.7007 0.6914 -0.0652 -0.0498 -0.0501 48 ILE B N 2776 C CA . ILE B 48 ? 0.6474 0.7058 0.6884 -0.0629 -0.0493 -0.0460 48 ILE B CA 2777 C C . ILE B 48 ? 0.6470 0.7239 0.6948 -0.0696 -0.0466 -0.0418 48 ILE B C 2778 O O . ILE B 48 ? 0.6646 0.7339 0.7026 -0.0672 -0.0453 -0.0379 48 ILE B O 2779 C CB . ILE B 48 ? 0.6663 0.7267 0.6896 -0.0466 -0.0526 -0.0503 48 ILE B CB 2780 C CG1 . ILE B 48 ? 0.6957 0.7116 0.6848 -0.0497 -0.0649 -0.0453 48 ILE B CG1 2781 C CG2 . ILE B 48 ? 0.6886 0.7678 0.6959 -0.0223 -0.0503 -0.0519 48 ILE B CG2 2782 C CD1 . ILE B 48 ? 0.6845 0.7193 0.6873 -0.0658 -0.0642 -0.0386 48 ILE B CD1 2783 N N . THR B 49 ? 0.6441 0.7478 0.7019 -0.0857 -0.0500 -0.0379 49 THR B N 2784 C CA . THR B 49 ? 0.6549 0.7965 0.7174 -0.1082 -0.0518 -0.0226 49 THR B CA 2785 C C . THR B 49 ? 0.6662 0.7568 0.7163 -0.1233 -0.0586 -0.0178 49 THR B C 2786 O O . THR B 49 ? 0.6715 0.7868 0.7205 -0.1357 -0.0568 -0.0047 49 THR B O 2787 C CB . THR B 49 ? 0.6800 0.8578 0.7459 -0.1445 -0.0661 -0.0086 49 THR B CB 2788 O OG1 . THR B 49 ? 0.7285 0.8251 0.7684 -0.1551 -0.0829 -0.0191 49 THR B OG1 2789 C CG2 . THR B 49 ? 0.6587 0.9230 0.7438 -0.1257 -0.0585 -0.0060 49 THR B CG2 2790 N N . GLY B 50 ? 0.6690 0.6976 0.7050 -0.1147 -0.0661 -0.0274 50 GLY B N 2791 C CA . GLY B 50 ? 0.6907 0.6721 0.7092 -0.1116 -0.0740 -0.0244 50 GLY B CA 2792 C C . GLY B 50 ? 0.6581 0.6605 0.6917 -0.0993 -0.0629 -0.0208 50 GLY B C 2793 O O . GLY B 50 ? 0.6701 0.6542 0.6945 -0.1049 -0.0688 -0.0122 50 GLY B O 2794 N N . LYS B 51 ? 0.6235 0.6499 0.6672 -0.0876 -0.0539 -0.0251 51 LYS B N 2795 C CA . LYS B 51 ? 0.6200 0.6440 0.6545 -0.0876 -0.0545 -0.0194 51 LYS B CA 2796 C C . LYS B 51 ? 0.6324 0.6635 0.6512 -0.0891 -0.0508 -0.0176 51 LYS B C 2797 O O . LYS B 51 ? 0.6442 0.6627 0.6491 -0.0943 -0.0544 -0.0109 51 LYS B O 2798 C CB . LYS B 51 ? 0.6234 0.6390 0.6416 -0.0843 -0.0587 -0.0213 51 LYS B CB 2799 C CG . LYS B 51 ? 0.6192 0.6547 0.6492 -0.0919 -0.0637 -0.0111 51 LYS B CG 2800 C CD . LYS B 51 ? 0.6556 0.6626 0.6485 -0.1085 -0.0798 -0.0033 51 LYS B CD 2801 C CE . LYS B 51 ? 0.6516 0.7080 0.6565 -0.1322 -0.0877 0.0201 51 LYS B CE 2802 N NZ . LYS B 51 ? 0.7197 0.7261 0.6674 -0.1714 -0.1183 0.0391 51 LYS B NZ 2803 N N . LEU B 52 ? 0.6356 0.7026 0.6552 -0.0805 -0.0433 -0.0215 52 LEU B N 2804 C CA . LEU B 52 ? 0.6529 0.7677 0.6579 -0.0690 -0.0346 -0.0170 52 LEU B CA 2805 C C . LEU B 52 ? 0.6565 0.7943 0.6698 -0.1001 -0.0357 0.0013 52 LEU B C 2806 O O . LEU B 52 ? 0.6778 0.8220 0.6688 -0.0933 -0.0321 0.0055 52 LEU B O 2807 C CB . LEU B 52 ? 0.6499 0.8395 0.6667 -0.0537 -0.0264 -0.0161 52 LEU B CB 2808 C CG . LEU B 52 ? 0.6833 0.8543 0.6634 -0.0023 -0.0259 -0.0336 52 LEU B CG 2809 C CD1 . LEU B 52 ? 0.6743 0.9180 0.6782 0.0098 -0.0217 -0.0312 52 LEU B CD1 2810 C CD2 . LEU B 52 ? 0.7409 0.9144 0.6636 0.0460 -0.0214 -0.0406 52 LEU B CD2 2811 N N . ASN B 53 ? 0.6615 0.7950 0.6909 -0.1357 -0.0465 0.0129 53 ASN B N 2812 C CA . ASN B 53 ? 0.6999 0.8336 0.7188 -0.1769 -0.0587 0.0363 53 ASN B CA 2813 C C . ASN B 53 ? 0.7125 0.7855 0.7149 -0.1710 -0.0641 0.0350 53 ASN B C 2814 O O . ASN B 53 ? 0.7272 0.8111 0.7145 -0.1932 -0.0684 0.0531 53 ASN B O 2815 C CB . ASN B 53 ? 0.7454 0.8298 0.7499 -0.2166 -0.0845 0.0462 53 ASN B CB 2816 C CG . ASN B 53 ? 0.7489 0.9001 0.7686 -0.2353 -0.0857 0.0539 53 ASN B CG 2817 O OD1 . ASN B 53 ? 0.7227 0.9896 0.7680 -0.2255 -0.0670 0.0630 53 ASN B OD1 2818 N ND2 . ASN B 53 ? 0.7949 0.8748 0.7903 -0.2549 -0.1096 0.0500 53 ASN B ND2 2819 N N . ARG B 54 ? 0.7071 0.7326 0.7134 -0.1442 -0.0651 0.0185 54 ARG B N 2820 C CA . ARG B 54 ? 0.7362 0.7275 0.7338 -0.1372 -0.0721 0.0215 54 ARG B CA 2821 C C . ARG B 54 ? 0.7309 0.7385 0.7122 -0.1313 -0.0650 0.0217 54 ARG B C 2822 O O . ARG B 54 ? 0.7349 0.7281 0.7011 -0.1401 -0.0722 0.0321 54 ARG B O 2823 C CB . ARG B 54 ? 0.7418 0.7190 0.7529 -0.1141 -0.0753 0.0131 54 ARG B CB 2824 C CG . ARG B 54 ? 0.7912 0.7505 0.7974 -0.1016 -0.0881 0.0225 54 ARG B CG 2825 C CD . ARG B 54 ? 0.7917 0.7928 0.8147 -0.0964 -0.0883 0.0301 54 ARG B CD 2826 N NE . ARG B 54 ? 0.7890 0.8145 0.8230 -0.0985 -0.0812 0.0237 54 ARG B NE 2827 C CZ . ARG B 54 ? 0.7974 0.8418 0.8267 -0.1167 -0.0893 0.0347 54 ARG B CZ 2828 N NH1 . ARG B 54 ? 0.8158 0.8672 0.8343 -0.1358 -0.1046 0.0529 54 ARG B NH1 2829 N NH2 . ARG B 54 ? 0.7861 0.8343 0.8120 -0.1226 -0.0884 0.0310 54 ARG B NH2 2830 N N . LEU B 55 ? 0.7319 0.7535 0.7006 -0.1116 -0.0560 0.0090 55 LEU B N 2831 C CA . LEU B 55 ? 0.7823 0.7823 0.7015 -0.0949 -0.0580 0.0030 55 LEU B CA 2832 C C . LEU B 55 ? 0.8157 0.8696 0.7103 -0.0780 -0.0431 0.0049 55 LEU B C 2833 O O . LEU B 55 ? 0.8406 0.8785 0.6896 -0.0684 -0.0453 0.0050 55 LEU B O 2834 C CB . LEU B 55 ? 0.8101 0.7661 0.6940 -0.0737 -0.0661 -0.0124 55 LEU B CB 2835 C CG . LEU B 55 ? 0.7977 0.7250 0.6984 -0.0973 -0.0825 -0.0054 55 LEU B CG 2836 C CD1 . LEU B 55 ? 0.8505 0.7240 0.7014 -0.0880 -0.0972 -0.0145 55 LEU B CD1 2837 C CD2 . LEU B 55 ? 0.8188 0.7286 0.7106 -0.1237 -0.1002 0.0112 55 LEU B CD2 2838 N N . ILE B 56 ? 0.8232 0.9548 0.7446 -0.0739 -0.0288 0.0095 56 ILE B N 2839 C CA . ILE B 56 ? 0.8705 1.1049 0.7784 -0.0573 -0.0114 0.0209 56 ILE B CA 2840 C C . ILE B 56 ? 0.8989 1.1696 0.8274 -0.1131 -0.0157 0.0520 56 ILE B C 2841 O O . ILE B 56 ? 0.8969 1.2255 0.8570 -0.1573 -0.0197 0.0768 56 ILE B O 2842 C CB . ILE B 56 ? 0.8538 1.1885 0.7836 -0.0334 0.0025 0.0225 56 ILE B CB 2843 C CG1 . ILE B 56 ? 0.9003 1.1907 0.7752 0.0407 0.0041 -0.0086 56 ILE B CG1 2844 C CG2 . ILE B 56 ? 0.8637 1.3613 0.8030 -0.0354 0.0203 0.0517 56 ILE B CG2 2845 C CD1 . ILE B 56 ? 0.9079 1.0569 0.7642 0.0340 -0.0175 -0.0281 56 ILE B CD1 2846 N N . GLU B 57 ? 0.9687 1.1868 0.8666 -0.1174 -0.0227 0.0528 57 GLU B N 2847 C CA . GLU B 57 ? 1.0134 1.2548 0.9103 -0.1636 -0.0295 0.0828 57 GLU B CA 2848 C C . GLU B 57 ? 1.0638 1.2806 0.9088 -0.1392 -0.0272 0.0761 57 GLU B C 2849 O O . GLU B 57 ? 1.0769 1.2121 0.8887 -0.1071 -0.0345 0.0506 57 GLU B O 2850 C CB . GLU B 57 ? 1.0278 1.1813 0.9436 -0.2073 -0.0559 0.0928 57 GLU B CB 2851 C CG . GLU B 57 ? 1.0403 1.0988 0.9473 -0.1918 -0.0697 0.0785 57 GLU B CG 2852 C CD . GLU B 57 ? 1.0831 1.1193 0.9614 -0.2103 -0.0814 0.0962 57 GLU B CD 2853 O OE1 . GLU B 57 ? 1.1358 1.2034 1.0006 -0.2475 -0.0861 0.1235 57 GLU B OE1 2854 O OE2 . GLU B 57 ? 1.0869 1.0787 0.9528 -0.1953 -0.0900 0.0881 57 GLU B OE2 2855 N N . LYS B 58 ? 1.0992 1.3870 0.9278 -0.1614 -0.0214 0.1030 58 LYS B N 2856 C CA . LYS B 58 ? 1.1506 1.4185 0.9218 -0.1421 -0.0205 0.0995 58 LYS B CA 2857 C C . LYS B 58 ? 1.1630 1.3822 0.9398 -0.2011 -0.0432 0.1269 58 LYS B C 2858 O O . LYS B 58 ? 1.1545 1.3917 0.9587 -0.2553 -0.0553 0.1570 58 LYS B O 2859 C CB . LYS B 58 ? 1.1856 1.5956 0.9230 -0.1085 0.0076 0.1104 58 LYS B CB 2860 C CG . LYS B 58 ? 1.2491 1.6275 0.8995 -0.0589 0.0115 0.0925 58 LYS B CG 2861 C CD . LYS B 58 ? 1.2799 1.8211 0.9069 -0.0537 0.0361 0.1231 58 LYS B CD 2862 C CE . LYS B 58 ? 1.2667 1.9936 0.9139 -0.0113 0.0676 0.1334 58 LYS B CE 2863 N NZ . LYS B 58 ? 1.2874 2.2169 0.9204 -0.0140 0.0929 0.1750 58 LYS B NZ 2864 N N . THR B 59 ? 1.1983 1.3434 0.9357 -0.1916 -0.0557 0.1182 59 THR B N 2865 C CA . THR B 59 ? 1.2125 1.3027 0.9497 -0.2353 -0.0807 0.1420 59 THR B CA 2866 C C . THR B 59 ? 1.2480 1.4097 0.9552 -0.2688 -0.0764 0.1766 59 THR B C 2867 O O . THR B 59 ? 1.2662 1.5187 0.9395 -0.2424 -0.0516 0.1757 59 THR B O 2868 C CB . THR B 59 ? 1.2382 1.2414 0.9483 -0.2198 -0.0999 0.1270 59 THR B CB 2869 O OG1 . THR B 59 ? 1.2856 1.2957 0.9252 -0.1943 -0.0923 0.1166 59 THR B OG1 2870 C CG2 . THR B 59 ? 1.2020 1.1574 0.9383 -0.1983 -0.1067 0.1028 59 THR B CG2 2871 N N . ASN B 60 ? 0.8850 0.7462 0.7896 -0.2378 -0.0133 -0.0368 60 ASN B N 2872 C CA . ASN B 60 ? 0.9129 0.7588 0.7934 -0.2660 -0.0131 -0.0334 60 ASN B CA 2873 C C . ASN B 60 ? 0.8578 0.6932 0.7548 -0.2408 -0.0086 -0.0281 60 ASN B C 2874 O O . ASN B 60 ? 0.8979 0.6997 0.7655 -0.2582 -0.0076 -0.0246 60 ASN B O 2875 C CB . ASN B 60 ? 1.0199 0.7792 0.8274 -0.2945 -0.0137 -0.0376 60 ASN B CB 2876 C CG . ASN B 60 ? 1.0846 0.8406 0.8605 -0.3418 -0.0159 -0.0343 60 ASN B CG 2877 O OD1 . ASN B 60 ? 1.0926 0.8908 0.8645 -0.3805 -0.0208 -0.0353 60 ASN B OD1 2878 N ND2 . ASN B 60 ? 1.1312 0.8384 0.8825 -0.3406 -0.0127 -0.0296 60 ASN B ND2 2879 N N . GLN B 61 ? 0.7537 0.6157 0.6935 -0.2028 -0.0064 -0.0269 61 GLN B N 2880 C CA . GLN B 61 ? 0.7139 0.5656 0.6675 -0.1789 -0.0033 -0.0223 61 GLN B CA 2881 C C . GLN B 61 ? 0.6248 0.5377 0.6119 -0.1852 -0.0025 -0.0185 61 GLN B C 2882 O O . GLN B 61 ? 0.5466 0.5204 0.5734 -0.1761 -0.0025 -0.0191 61 GLN B O 2883 C CB . GLN B 61 ? 0.7048 0.5567 0.6845 -0.1400 -0.0014 -0.0230 61 GLN B CB 2884 C CG . GLN B 61 ? 0.7116 0.5673 0.7119 -0.1171 0.0002 -0.0180 61 GLN B CG 2885 C CD . GLN B 61 ? 0.7940 0.5873 0.7618 -0.1045 0.0008 -0.0151 61 GLN B CD 2886 O OE1 . GLN B 61 ? 0.8542 0.6012 0.7800 -0.1225 0.0000 -0.0133 61 GLN B OE1 2887 N NE2 . GLN B 61 ? 0.7890 0.5811 0.7743 -0.0732 0.0021 -0.0138 61 GLN B NE2 2888 N N . GLN B 62 ? 0.6256 0.5190 0.5930 -0.1990 -0.0012 -0.0143 62 GLN B N 2889 C CA . GLN B 62 ? 0.5977 0.5460 0.5910 -0.2059 0.0015 -0.0114 62 GLN B CA 2890 C C . GLN B 62 ? 0.5441 0.4972 0.5625 -0.1746 0.0038 -0.0092 62 GLN B C 2891 O O . GLN B 62 ? 0.5545 0.4585 0.5562 -0.1595 0.0026 -0.0066 62 GLN B O 2892 C CB . GLN B 62 ? 0.6537 0.5831 0.6101 -0.2424 0.0023 -0.0078 62 GLN B CB 2893 C CG . GLN B 62 ? 0.6449 0.6367 0.6270 -0.2509 0.0070 -0.0054 62 GLN B CG 2894 C CD . GLN B 62 ? 0.7091 0.7110 0.6626 -0.2966 0.0082 -0.0028 62 GLN B CD 2895 O OE1 . GLN B 62 ? 0.7763 0.7526 0.7037 -0.3115 0.0106 0.0021 62 GLN B OE1 2896 N NE2 . GLN B 62 ? 0.7256 0.7665 0.6817 -0.3220 0.0060 -0.0052 62 GLN B NE2 2897 N N . PHE B 63 ? 0.4906 0.5035 0.5470 -0.1647 0.0068 -0.0102 63 PHE B N 2898 C CA . PHE B 63 ? 0.4612 0.4805 0.5356 -0.1424 0.0094 -0.0090 63 PHE B CA 2899 C C . PHE B 63 ? 0.4542 0.5145 0.5353 -0.1556 0.0149 -0.0083 63 PHE B C 2900 O O . PHE B 63 ? 0.4370 0.5467 0.5294 -0.1705 0.0176 -0.0099 63 PHE B O 2901 C CB . PHE B 63 ? 0.4141 0.4564 0.5214 -0.1137 0.0094 -0.0120 63 PHE B CB 2902 C CG . PHE B 63 ? 0.4246 0.4295 0.5271 -0.0978 0.0058 -0.0120 63 PHE B CG 2903 C CD1 . PHE B 63 ? 0.4444 0.4448 0.5425 -0.1011 0.0037 -0.0144 63 PHE B CD1 2904 C CD2 . PHE B 63 ? 0.4312 0.4100 0.5331 -0.0803 0.0047 -0.0095 63 PHE B CD2 2905 C CE1 . PHE B 63 ? 0.4397 0.4084 0.5320 -0.0857 0.0023 -0.0151 63 PHE B CE1 2906 C CE2 . PHE B 63 ? 0.4363 0.3905 0.5365 -0.0648 0.0027 -0.0093 63 PHE B CE2 2907 C CZ . PHE B 63 ? 0.4425 0.3905 0.5374 -0.0667 0.0024 -0.0125 63 PHE B CZ 2908 N N . GLU B 64 ? 0.4637 0.5079 0.5378 -0.1498 0.0166 -0.0059 64 GLU B N 2909 C CA . GLU B 64 ? 0.4758 0.5548 0.5526 -0.1601 0.0234 -0.0059 64 GLU B CA 2910 C C . GLU B 64 ? 0.4348 0.5368 0.5366 -0.1333 0.0274 -0.0099 64 GLU B C 2911 O O . GLU B 64 ? 0.3945 0.4758 0.5053 -0.1111 0.0236 -0.0108 64 GLU B O 2912 C CB . GLU B 64 ? 0.5402 0.5792 0.5814 -0.1774 0.0226 0.0001 64 GLU B CB 2913 C CG . GLU B 64 ? 0.6119 0.5871 0.6153 -0.1898 0.0157 0.0055 64 GLU B CG 2914 C CD . GLU B 64 ? 0.6723 0.6504 0.6588 -0.2197 0.0158 0.0050 64 GLU B CD 2915 O OE1 . GLU B 64 ? 0.7306 0.7565 0.7219 -0.2437 0.0213 0.0043 64 GLU B OE1 2916 O OE2 . GLU B 64 ? 0.7369 0.6711 0.7037 -0.2201 0.0107 0.0049 64 GLU B OE2 2917 N N . LEU B 65 ? 0.4236 0.5666 0.5323 -0.1372 0.0359 -0.0124 65 LEU B N 2918 C CA . LEU B 65 ? 0.4142 0.5662 0.5322 -0.1161 0.0413 -0.0168 65 LEU B CA 2919 C C . LEU B 65 ? 0.4213 0.5234 0.5199 -0.1122 0.0358 -0.0137 65 LEU B C 2920 O O . LEU B 65 ? 0.4267 0.5021 0.5000 -0.1299 0.0327 -0.0077 65 LEU B O 2921 C CB . LEU B 65 ? 0.4253 0.6234 0.5434 -0.1258 0.0528 -0.0196 65 LEU B CB 2922 C CG . LEU B 65 ? 0.4107 0.6700 0.5561 -0.1079 0.0623 -0.0259 65 LEU B CG 2923 C CD1 . LEU B 65 ? 0.3944 0.6691 0.5630 -0.0927 0.0571 -0.0263 65 LEU B CD1 2924 C CD2 . LEU B 65 ? 0.4298 0.7470 0.5767 -0.1292 0.0720 -0.0255 65 LEU B CD2 2925 N N . ILE B 66 ? 0.4257 0.5152 0.5335 -0.0902 0.0337 -0.0167 66 ILE B N 2926 C CA . ILE B 66 ? 0.4479 0.5063 0.5398 -0.0874 0.0294 -0.0146 66 ILE B CA 2927 C C . ILE B 66 ? 0.4271 0.4959 0.5178 -0.0770 0.0364 -0.0220 66 ILE B C 2928 O O . ILE B 66 ? 0.4243 0.4710 0.4997 -0.0777 0.0327 -0.0211 66 ILE B O 2929 C CB . ILE B 66 ? 0.4645 0.4911 0.5583 -0.0774 0.0187 -0.0101 66 ILE B CB 2930 C CG1 . ILE B 66 ? 0.4643 0.4985 0.5800 -0.0636 0.0179 -0.0130 66 ILE B CG1 2931 C CG2 . ILE B 66 ? 0.4921 0.4896 0.5673 -0.0879 0.0116 -0.0013 66 ILE B CG2 2932 C CD1 . ILE B 66 ? 0.4738 0.5241 0.6015 -0.0491 0.0234 -0.0202 66 ILE B CD1 2933 N N . ASP B 67 ? 0.4127 0.5142 0.5166 -0.0666 0.0463 -0.0291 67 ASP B N 2934 C CA . ASP B 67 ? 0.4157 0.5235 0.5109 -0.0557 0.0559 -0.0373 67 ASP B CA 2935 C C . ASP B 67 ? 0.4303 0.5869 0.5331 -0.0546 0.0692 -0.0419 67 ASP B C 2936 O O . ASP B 67 ? 0.4429 0.6294 0.5554 -0.0694 0.0698 -0.0374 67 ASP B O 2937 C CB . ASP B 67 ? 0.4158 0.5020 0.5131 -0.0341 0.0546 -0.0427 67 ASP B CB 2938 C CG . ASP B 67 ? 0.3921 0.4933 0.5125 -0.0184 0.0539 -0.0428 67 ASP B CG 2939 O OD1 . ASP B 67 ? 0.3840 0.5222 0.5212 -0.0205 0.0565 -0.0409 67 ASP B OD1 2940 O OD2 . ASP B 67 ? 0.3789 0.4546 0.4981 -0.0056 0.0502 -0.0443 67 ASP B OD2 2941 N N . ASN B 68 ? 0.4497 0.6148 0.5455 -0.0379 0.0804 -0.0507 68 ASN B N 2942 C CA . ASN B 68 ? 0.4599 0.6749 0.5587 -0.0366 0.0953 -0.0553 68 ASN B CA 2943 C C . ASN B 68 ? 0.4828 0.7120 0.5866 -0.0023 0.1065 -0.0650 68 ASN B C 2944 O O . ASN B 68 ? 0.5084 0.6939 0.5923 0.0136 0.1072 -0.0714 68 ASN B O 2945 C CB . ASN B 68 ? 0.4784 0.6838 0.5490 -0.0556 0.1003 -0.0561 68 ASN B CB 2946 C CG . ASN B 68 ? 0.4898 0.7532 0.5630 -0.0616 0.1163 -0.0592 68 ASN B CG 2947 O OD1 . ASN B 68 ? 0.5007 0.8127 0.5952 -0.0421 0.1264 -0.0638 68 ASN B OD1 2948 N ND2 . ASN B 68 ? 0.5061 0.7677 0.5567 -0.0883 0.1187 -0.0558 68 ASN B ND2 2949 N N . GLU B 69 ? 0.4822 0.7727 0.6097 0.0083 0.1150 -0.0655 69 GLU B N 2950 C CA . GLU B 69 ? 0.5077 0.8192 0.6448 0.0464 0.1242 -0.0720 69 GLU B CA 2951 C C . GLU B 69 ? 0.5389 0.8835 0.6652 0.0612 0.1437 -0.0812 69 GLU B C 2952 O O . GLU B 69 ? 0.5668 0.9170 0.6908 0.0984 0.1538 -0.0884 69 GLU B O 2953 C CB . GLU B 69 ? 0.4937 0.8626 0.6667 0.0504 0.1202 -0.0654 69 GLU B CB 2954 C CG . GLU B 69 ? 0.5147 0.9079 0.7018 0.0923 0.1254 -0.0683 69 GLU B CG 2955 C CD . GLU B 69 ? 0.4945 0.9384 0.7150 0.0904 0.1164 -0.0597 69 GLU B CD 2956 O OE1 . GLU B 69 ? 0.4694 0.8875 0.6929 0.0668 0.1021 -0.0531 69 GLU B OE1 2957 O OE2 . GLU B 69 ? 0.4856 0.9974 0.7283 0.1128 0.1236 -0.0594 69 GLU B OE2 2958 N N . PHE B 70 ? 0.5440 0.9093 0.6609 0.0333 0.1495 -0.0805 70 PHE B N 2959 C CA . PHE B 70 ? 0.5713 0.9715 0.6756 0.0429 0.1695 -0.0893 70 PHE B CA 2960 C C . PHE B 70 ? 0.6087 0.9486 0.6699 0.0322 0.1720 -0.0956 70 PHE B C 2961 O O . PHE B 70 ? 0.6470 0.9936 0.6873 0.0475 0.1890 -0.1061 70 PHE B O 2962 C CB . PHE B 70 ? 0.5518 1.0310 0.6748 0.0155 0.1766 -0.0837 70 PHE B CB 2963 C CG . PHE B 70 ? 0.5175 1.0704 0.6822 0.0198 0.1746 -0.0773 70 PHE B CG 2964 C CD1 . PHE B 70 ? 0.5055 1.0640 0.6907 0.0568 0.1711 -0.0781 70 PHE B CD1 2965 C CD2 . PHE B 70 ? 0.5072 1.1240 0.6873 -0.0163 0.1757 -0.0697 70 PHE B CD2 2966 C CE1 . PHE B 70 ? 0.4790 1.1103 0.7017 0.0591 0.1678 -0.0713 70 PHE B CE1 2967 C CE2 . PHE B 70 ? 0.4862 1.1757 0.7027 -0.0173 0.1727 -0.0636 70 PHE B CE2 2968 C CZ . PHE B 70 ? 0.4714 1.1710 0.7108 0.0212 0.1684 -0.0644 70 PHE B CZ 2969 N N . ASN B 71 ? 0.6116 0.8959 0.6587 0.0066 0.1553 -0.0891 71 ASN B N 2970 C CA . ASN B 71 ? 0.6558 0.8899 0.6635 -0.0098 0.1540 -0.0922 71 ASN B CA 2971 C C . ASN B 71 ? 0.6333 0.8029 0.6322 -0.0168 0.1344 -0.0873 71 ASN B C 2972 O O . ASN B 71 ? 0.6064 0.7652 0.6102 -0.0417 0.1202 -0.0762 71 ASN B O 2973 C CB . ASN B 71 ? 0.6837 0.9440 0.6839 -0.0457 0.1554 -0.0850 71 ASN B CB 2974 C CG . ASN B 71 ? 0.7491 0.9920 0.7091 -0.0533 0.1660 -0.0924 71 ASN B CG 2975 O OD1 . ASN B 71 ? 0.7865 0.9712 0.7162 -0.0518 0.1600 -0.0968 71 ASN B OD1 2976 N ND2 . ASN B 71 ? 0.7721 1.0684 0.7299 -0.0643 0.1820 -0.0937 71 ASN B ND2 2977 N N . GLU B 72 ? 0.6469 0.7734 0.6304 0.0058 0.1345 -0.0954 72 GLU B N 2978 C CA . GLU B 72 ? 0.6338 0.7093 0.6141 0.0015 0.1172 -0.0910 72 GLU B CA 2979 C C . GLU B 72 ? 0.6043 0.6545 0.5698 -0.0296 0.1032 -0.0830 72 GLU B C 2980 O O . GLU B 72 ? 0.6122 0.6522 0.5485 -0.0427 0.1070 -0.0861 72 GLU B O 2981 C CB . GLU B 72 ? 0.6993 0.7240 0.6506 0.0229 0.1210 -0.1020 72 GLU B CB 2982 C CG . GLU B 72 ? 0.7102 0.6981 0.6682 0.0236 0.1058 -0.0967 72 GLU B CG 2983 C CD . GLU B 72 ? 0.7853 0.7105 0.7036 0.0337 0.1069 -0.1063 72 GLU B CD 2984 O OE1 . GLU B 72 ? 0.8448 0.7458 0.7246 0.0379 0.1181 -0.1177 72 GLU B OE1 2985 O OE2 . GLU B 72 ? 0.8046 0.7014 0.7259 0.0357 0.0970 -0.1027 72 GLU B OE2 2986 N N . VAL B 73 ? 0.5693 0.6109 0.5540 -0.0393 0.0871 -0.0722 73 VAL B N 2987 C CA . VAL B 73 ? 0.5663 0.5842 0.5386 -0.0623 0.0723 -0.0633 73 VAL B CA 2988 C C . VAL B 73 ? 0.5901 0.5652 0.5338 -0.0637 0.0668 -0.0688 73 VAL B C 2989 O O . VAL B 73 ? 0.5844 0.5391 0.5188 -0.0476 0.0726 -0.0783 73 VAL B O 2990 C CB . VAL B 73 ? 0.5323 0.5521 0.5311 -0.0677 0.0578 -0.0511 73 VAL B CB 2991 C CG1 . VAL B 73 ? 0.5145 0.5704 0.5350 -0.0712 0.0623 -0.0463 73 VAL B CG1 2992 C CG2 . VAL B 73 ? 0.5223 0.5252 0.5347 -0.0531 0.0522 -0.0527 73 VAL B CG2 2993 N N . GLU B 74 ? 0.6161 0.5766 0.5426 -0.0840 0.0550 -0.0620 74 GLU B N 2994 C CA . GLU B 74 ? 0.6596 0.5857 0.5588 -0.0929 0.0462 -0.0649 74 GLU B CA 2995 C C . GLU B 74 ? 0.6463 0.5553 0.5583 -0.0837 0.0402 -0.0659 74 GLU B C 2996 O O . GLU B 74 ? 0.6055 0.5304 0.5506 -0.0770 0.0350 -0.0583 74 GLU B O 2997 C CB . GLU B 74 ? 0.6708 0.5974 0.5623 -0.1140 0.0299 -0.0523 74 GLU B CB 2998 C CG . GLU B 74 ? 0.7214 0.6228 0.5830 -0.1290 0.0192 -0.0541 74 GLU B CG 2999 C CD . GLU B 74 ? 0.7187 0.6169 0.5981 -0.1305 0.0050 -0.0480 74 GLU B CD 3000 O OE1 . GLU B 74 ? 0.6837 0.6025 0.5980 -0.1239 -0.0023 -0.0371 74 GLU B OE1 3001 O OE2 . GLU B 74 ? 0.7473 0.6213 0.6024 -0.1402 0.0016 -0.0546 74 GLU B OE2 3002 N N . LYS B 75 ? 0.6948 0.5678 0.5754 -0.0858 0.0412 -0.0752 75 LYS B N 3003 C CA . LYS B 75 ? 0.7077 0.5571 0.5907 -0.0775 0.0392 -0.0781 75 LYS B CA 3004 C C . LYS B 75 ? 0.6500 0.5112 0.5592 -0.0885 0.0223 -0.0655 75 LYS B C 3005 O O . LYS B 75 ? 0.6218 0.4891 0.5566 -0.0768 0.0218 -0.0623 75 LYS B O 3006 C CB . LYS B 75 ? 0.8035 0.6019 0.6360 -0.0830 0.0433 -0.0908 75 LYS B CB 3007 C CG . LYS B 75 ? 0.8702 0.6335 0.6925 -0.0648 0.0502 -0.0980 75 LYS B CG 3008 C CD . LYS B 75 ? 0.9074 0.6749 0.7303 -0.0325 0.0692 -0.1071 75 LYS B CD 3009 C CE . LYS B 75 ? 0.9668 0.6986 0.7797 -0.0097 0.0745 -0.1117 75 LYS B CE 3010 N NZ . LYS B 75 ? 1.0101 0.7487 0.8210 0.0265 0.0929 -0.1204 75 LYS B NZ 3011 N N . GLN B 76 ? 0.6383 0.5062 0.5410 -0.1096 0.0087 -0.0579 76 GLN B N 3012 C CA . GLN B 76 ? 0.6008 0.4879 0.5293 -0.1176 -0.0065 -0.0457 76 GLN B CA 3013 C C . GLN B 76 ? 0.5402 0.4570 0.5107 -0.1021 -0.0066 -0.0367 76 GLN B C 3014 O O . GLN B 76 ? 0.4992 0.4217 0.4919 -0.0954 -0.0089 -0.0335 76 GLN B O 3015 C CB . GLN B 76 ? 0.6120 0.5123 0.5297 -0.1388 -0.0216 -0.0372 76 GLN B CB 3016 C CG . GLN B 76 ? 0.6008 0.5284 0.5454 -0.1445 -0.0364 -0.0248 76 GLN B CG 3017 C CD . GLN B 76 ? 0.6201 0.5645 0.5512 -0.1662 -0.0526 -0.0169 76 GLN B CD 3018 O OE1 . GLN B 76 ? 0.6339 0.5855 0.5535 -0.1701 -0.0572 -0.0122 76 GLN B OE1 3019 N NE2 . GLN B 76 ? 0.6304 0.5844 0.5623 -0.1822 -0.0620 -0.0144 76 GLN B NE2 3020 N N . ILE B 77 ? 0.5303 0.4625 0.5070 -0.0985 -0.0038 -0.0329 77 ILE B N 3021 C CA . ILE B 77 ? 0.4989 0.4512 0.5069 -0.0875 -0.0039 -0.0252 77 ILE B CA 3022 C C . ILE B 77 ? 0.4696 0.4223 0.4929 -0.0715 0.0073 -0.0323 77 ILE B C 3023 O O . ILE B 77 ? 0.4341 0.3968 0.4821 -0.0636 0.0049 -0.0277 77 ILE B O 3024 C CB . ILE B 77 ? 0.5150 0.4765 0.5181 -0.0919 -0.0036 -0.0190 77 ILE B CB 3025 C CG1 . ILE B 77 ? 0.5041 0.4762 0.5309 -0.0847 -0.0072 -0.0096 77 ILE B CG1 3026 C CG2 . ILE B 77 ? 0.5287 0.4912 0.5179 -0.0911 0.0114 -0.0284 77 ILE B CG2 3027 C CD1 . ILE B 77 ? 0.5126 0.4886 0.5510 -0.0824 -0.0211 0.0011 77 ILE B CD1 3028 N N . GLY B 78 ? 0.4850 0.4273 0.4916 -0.0652 0.0194 -0.0434 78 GLY B N 3029 C CA . GLY B 78 ? 0.4677 0.4122 0.4861 -0.0466 0.0294 -0.0494 78 GLY B CA 3030 C C . GLY B 78 ? 0.4601 0.3882 0.4846 -0.0412 0.0247 -0.0489 78 GLY B C 3031 O O . GLY B 78 ? 0.4370 0.3772 0.4843 -0.0292 0.0260 -0.0465 78 GLY B O 3032 N N . ASN B 79 ? 0.4731 0.3743 0.4747 -0.0531 0.0190 -0.0506 79 ASN B N 3033 C CA . ASN B 79 ? 0.4744 0.3597 0.4777 -0.0549 0.0137 -0.0486 79 ASN B CA 3034 C C . ASN B 79 ? 0.4335 0.3470 0.4700 -0.0586 0.0039 -0.0372 79 ASN B C 3035 O O . ASN B 79 ? 0.4163 0.3293 0.4659 -0.0519 0.0038 -0.0351 79 ASN B O 3036 C CB . ASN B 79 ? 0.5139 0.3646 0.4800 -0.0733 0.0095 -0.0531 79 ASN B CB 3037 C CG . ASN B 79 ? 0.5660 0.3718 0.4924 -0.0637 0.0211 -0.0661 79 ASN B CG 3038 O OD1 . ASN B 79 ? 0.5732 0.3761 0.5045 -0.0393 0.0316 -0.0704 79 ASN B OD1 3039 N ND2 . ASN B 79 ? 0.6166 0.3870 0.5011 -0.0819 0.0191 -0.0723 79 ASN B ND2 3040 N N . VAL B 80 ? 0.4174 0.3535 0.4647 -0.0670 -0.0037 -0.0297 80 VAL B N 3041 C CA . VAL B 80 ? 0.3946 0.3555 0.4709 -0.0642 -0.0108 -0.0197 80 VAL B CA 3042 C C . VAL B 80 ? 0.3758 0.3454 0.4721 -0.0486 -0.0042 -0.0198 80 VAL B C 3043 O O . VAL B 80 ? 0.3691 0.3455 0.4825 -0.0426 -0.0053 -0.0167 80 VAL B O 3044 C CB . VAL B 80 ? 0.3919 0.3703 0.4710 -0.0708 -0.0199 -0.0109 80 VAL B CB 3045 C CG1 . VAL B 80 ? 0.3735 0.3716 0.4785 -0.0611 -0.0245 -0.0017 80 VAL B CG1 3046 C CG2 . VAL B 80 ? 0.4136 0.3934 0.4771 -0.0881 -0.0293 -0.0088 80 VAL B CG2 3047 N N . ILE B 81 ? 0.3819 0.3540 0.4744 -0.0443 0.0027 -0.0234 81 ILE B N 3048 C CA . ILE B 81 ? 0.3568 0.3424 0.4659 -0.0344 0.0082 -0.0236 81 ILE B CA 3049 C C . ILE B 81 ? 0.3729 0.3553 0.4891 -0.0220 0.0128 -0.0276 81 ILE B C 3050 O O . ILE B 81 ? 0.3510 0.3433 0.4841 -0.0165 0.0117 -0.0245 81 ILE B O 3051 C CB . ILE B 81 ? 0.3617 0.3570 0.4631 -0.0359 0.0159 -0.0272 81 ILE B CB 3052 C CG1 . ILE B 81 ? 0.3604 0.3569 0.4544 -0.0484 0.0106 -0.0204 81 ILE B CG1 3053 C CG2 . ILE B 81 ? 0.3516 0.3674 0.4686 -0.0273 0.0225 -0.0291 81 ILE B CG2 3054 C CD1 . ILE B 81 ? 0.3740 0.3773 0.4527 -0.0557 0.0180 -0.0235 81 ILE B CD1 3055 N N . ASN B 82 ? 0.4055 0.3698 0.5039 -0.0171 0.0179 -0.0346 82 ASN B N 3056 C CA . ASN B 82 ? 0.4339 0.3870 0.5312 -0.0029 0.0219 -0.0376 82 ASN B CA 3057 C C . ASN B 82 ? 0.4148 0.3570 0.5166 -0.0074 0.0152 -0.0325 82 ASN B C 3058 O O . ASN B 82 ? 0.3961 0.3411 0.5077 0.0023 0.0158 -0.0306 82 ASN B O 3059 C CB . ASN B 82 ? 0.5048 0.4284 0.5720 0.0045 0.0290 -0.0462 82 ASN B CB 3060 C CG . ASN B 82 ? 0.5703 0.5123 0.6370 0.0184 0.0396 -0.0522 82 ASN B CG 3061 O OD1 . ASN B 82 ? 0.5169 0.4949 0.6037 0.0156 0.0408 -0.0494 82 ASN B OD1 3062 N ND2 . ASN B 82 ? 0.6965 0.6124 0.7367 0.0332 0.0481 -0.0605 82 ASN B ND2 3063 N N . TRP B 83 ? 0.4302 0.3637 0.5236 -0.0233 0.0087 -0.0300 83 TRP B N 3064 C CA . TRP B 83 ? 0.4301 0.3623 0.5286 -0.0317 0.0029 -0.0246 83 TRP B CA 3065 C C . TRP B 83 ? 0.3811 0.3411 0.5081 -0.0262 0.0008 -0.0184 83 TRP B C 3066 O O . TRP B 83 ? 0.3674 0.3275 0.5013 -0.0223 0.0011 -0.0162 83 TRP B O 3067 C CB . TRP B 83 ? 0.4537 0.3856 0.5413 -0.0515 -0.0042 -0.0223 83 TRP B CB 3068 C CG . TRP B 83 ? 0.4591 0.4058 0.5565 -0.0639 -0.0108 -0.0154 83 TRP B CG 3069 C CD1 . TRP B 83 ? 0.4879 0.4171 0.5703 -0.0755 -0.0115 -0.0151 83 TRP B CD1 3070 C CD2 . TRP B 83 ? 0.4460 0.4297 0.5672 -0.0664 -0.0173 -0.0073 83 TRP B CD2 3071 N NE1 . TRP B 83 ? 0.4874 0.4487 0.5870 -0.0873 -0.0174 -0.0074 83 TRP B NE1 3072 C CE2 . TRP B 83 ? 0.4616 0.4582 0.5864 -0.0791 -0.0209 -0.0027 83 TRP B CE2 3073 C CE3 . TRP B 83 ? 0.4376 0.4430 0.5745 -0.0583 -0.0200 -0.0031 83 TRP B CE3 3074 C CZ2 . TRP B 83 ? 0.4556 0.4942 0.6042 -0.0802 -0.0263 0.0057 83 TRP B CZ2 3075 C CZ3 . TRP B 83 ? 0.4429 0.4801 0.5987 -0.0573 -0.0261 0.0054 83 TRP B CZ3 3076 C CH2 . TRP B 83 ? 0.4482 0.5060 0.6121 -0.0666 -0.0288 0.0096 83 TRP B CH2 3077 N N . THR B 84 ? 0.3669 0.3449 0.5052 -0.0259 -0.0009 -0.0159 84 THR B N 3078 C CA . THR B 84 ? 0.3479 0.3426 0.5050 -0.0202 -0.0021 -0.0114 84 THR B CA 3079 C C . THR B 84 ? 0.3513 0.3480 0.5146 -0.0103 0.0030 -0.0141 84 THR B C 3080 O O . THR B 84 ? 0.3408 0.3420 0.5133 -0.0065 0.0026 -0.0120 84 THR B O 3081 C CB . THR B 84 ? 0.3403 0.3420 0.4982 -0.0223 -0.0048 -0.0081 84 THR B CB 3082 O OG1 . THR B 84 ? 0.3281 0.3330 0.4807 -0.0300 -0.0112 -0.0040 84 THR B OG1 3083 C CG2 . THR B 84 ? 0.3322 0.3393 0.5007 -0.0159 -0.0057 -0.0040 84 THR B CG2 3084 N N . ARG B 85 ? 0.3620 0.3600 0.5204 -0.0063 0.0077 -0.0187 85 ARG B N 3085 C CA . ARG B 85 ? 0.3539 0.3636 0.5202 0.0030 0.0113 -0.0203 85 ARG B CA 3086 C C . ARG B 85 ? 0.3470 0.3460 0.5113 0.0115 0.0112 -0.0198 85 ARG B C 3087 O O . ARG B 85 ? 0.3154 0.3225 0.4885 0.0147 0.0099 -0.0174 85 ARG B O 3088 C CB . ARG B 85 ? 0.3819 0.4036 0.5447 0.0078 0.0173 -0.0249 85 ARG B CB 3089 C CG . ARG B 85 ? 0.3919 0.4388 0.5664 0.0168 0.0199 -0.0253 85 ARG B CG 3090 C CD . ARG B 85 ? 0.4143 0.4813 0.5873 0.0253 0.0273 -0.0298 85 ARG B CD 3091 N NE . ARG B 85 ? 0.4372 0.5163 0.6079 0.0109 0.0296 -0.0306 85 ARG B NE 3092 C CZ . ARG B 85 ? 0.4513 0.5235 0.6085 0.0094 0.0345 -0.0345 85 ARG B CZ 3093 N NH1 . ARG B 85 ? 0.4772 0.5273 0.6195 0.0218 0.0383 -0.0395 85 ARG B NH1 3094 N NH2 . ARG B 85 ? 0.4381 0.5213 0.5916 -0.0060 0.0359 -0.0335 85 ARG B NH2 3095 N N . ASP B 86 ? 0.3591 0.3348 0.5066 0.0136 0.0125 -0.0221 86 ASP B N 3096 C CA . ASP B 86 ? 0.3692 0.3246 0.5066 0.0191 0.0121 -0.0205 86 ASP B CA 3097 C C . ASP B 86 ? 0.3507 0.3097 0.4963 0.0095 0.0079 -0.0150 86 ASP B C 3098 O O . ASP B 86 ? 0.3396 0.2962 0.4854 0.0148 0.0076 -0.0122 86 ASP B O 3099 C CB . ASP B 86 ? 0.4138 0.3325 0.5224 0.0173 0.0138 -0.0240 86 ASP B CB 3100 C CG . ASP B 86 ? 0.4379 0.3482 0.5334 0.0337 0.0204 -0.0304 86 ASP B CG 3101 O OD1 . ASP B 86 ? 0.4338 0.3738 0.5461 0.0472 0.0234 -0.0309 86 ASP B OD1 3102 O OD2 . ASP B 86 ? 0.4770 0.3518 0.5432 0.0327 0.0230 -0.0351 86 ASP B OD2 3103 N N . SER B 87 ? 0.3381 0.3065 0.4905 -0.0028 0.0049 -0.0130 87 SER B N 3104 C CA . SER B 87 ? 0.3315 0.3118 0.4942 -0.0086 0.0027 -0.0080 87 SER B CA 3105 C C . SER B 87 ? 0.3257 0.3208 0.5019 -0.0004 0.0038 -0.0072 87 SER B C 3106 O O . SER B 87 ? 0.3177 0.3145 0.4954 0.0003 0.0045 -0.0048 87 SER B O 3107 C CB . SER B 87 ? 0.3211 0.3165 0.4909 -0.0180 -0.0009 -0.0053 87 SER B CB 3108 O OG . SER B 87 ? 0.3303 0.3143 0.4852 -0.0303 -0.0033 -0.0059 87 SER B OG 3109 N N . ILE B 88 ? 0.3168 0.3205 0.4987 0.0029 0.0042 -0.0093 88 ILE B N 3110 C CA . ILE B 88 ? 0.3113 0.3241 0.4991 0.0064 0.0048 -0.0097 88 ILE B CA 3111 C C . ILE B 88 ? 0.3079 0.3228 0.4939 0.0130 0.0054 -0.0101 88 ILE B C 3112 O O . ILE B 88 ? 0.3080 0.3262 0.4949 0.0138 0.0049 -0.0088 88 ILE B O 3113 C CB . ILE B 88 ? 0.3136 0.3316 0.5014 0.0030 0.0048 -0.0114 88 ILE B CB 3114 C CG1 . ILE B 88 ? 0.3219 0.3344 0.5080 -0.0004 0.0029 -0.0090 88 ILE B CG1 3115 C CG2 . ILE B 88 ? 0.3142 0.3385 0.5018 0.0011 0.0049 -0.0125 88 ILE B CG2 3116 C CD1 . ILE B 88 ? 0.3211 0.3320 0.5095 0.0038 0.0026 -0.0064 88 ILE B CD1 3117 N N . THR B 89 ? 0.3124 0.3258 0.4942 0.0196 0.0065 -0.0118 89 THR B N 3118 C CA . THR B 89 ? 0.3182 0.3348 0.4974 0.0309 0.0062 -0.0105 89 THR B CA 3119 C C . THR B 89 ? 0.3393 0.3389 0.5096 0.0311 0.0047 -0.0064 89 THR B C 3120 O O . THR B 89 ? 0.3368 0.3436 0.5072 0.0354 0.0026 -0.0037 89 THR B O 3121 C CB . THR B 89 ? 0.3369 0.3475 0.5080 0.0434 0.0089 -0.0128 89 THR B CB 3122 O OG1 . THR B 89 ? 0.3449 0.3815 0.5259 0.0436 0.0113 -0.0161 89 THR B OG1 3123 C CG2 . THR B 89 ? 0.3550 0.3624 0.5189 0.0606 0.0079 -0.0097 89 THR B CG2 3124 N N . GLU B 90 ? 0.3463 0.3260 0.5075 0.0236 0.0053 -0.0055 90 GLU B N 3125 C CA . GLU B 90 ? 0.3779 0.3421 0.5278 0.0188 0.0048 -0.0010 90 GLU B CA 3126 C C . GLU B 90 ? 0.3531 0.3355 0.5138 0.0139 0.0051 0.0006 90 GLU B C 3127 O O . GLU B 90 ? 0.3506 0.3294 0.5039 0.0149 0.0048 0.0040 90 GLU B O 3128 C CB . GLU B 90 ? 0.4173 0.3633 0.5554 0.0060 0.0053 -0.0006 90 GLU B CB 3129 C CG . GLU B 90 ? 0.4941 0.4084 0.6066 0.0005 0.0051 0.0035 90 GLU B CG 3130 C CD . GLU B 90 ? 0.5514 0.4340 0.6414 0.0168 0.0050 0.0035 90 GLU B CD 3131 O OE1 . GLU B 90 ? 0.5737 0.4613 0.6683 0.0319 0.0060 -0.0007 90 GLU B OE1 3132 O OE2 . GLU B 90 ? 0.6535 0.5059 0.7189 0.0154 0.0042 0.0085 90 GLU B OE2 3133 N N . VAL B 91 ? 0.3246 0.3229 0.4985 0.0102 0.0060 -0.0017 91 VAL B N 3134 C CA . VAL B 91 ? 0.3188 0.3283 0.4977 0.0094 0.0078 -0.0019 91 VAL B CA 3135 C C . VAL B 91 ? 0.3311 0.3448 0.5069 0.0134 0.0062 -0.0031 91 VAL B C 3136 O O . VAL B 91 ? 0.3392 0.3529 0.5086 0.0127 0.0071 -0.0017 91 VAL B O 3137 C CB . VAL B 91 ? 0.3079 0.3255 0.4955 0.0089 0.0089 -0.0039 91 VAL B CB 3138 C CG1 . VAL B 91 ? 0.3135 0.3331 0.4989 0.0119 0.0118 -0.0058 91 VAL B CG1 3139 C CG2 . VAL B 91 ? 0.3063 0.3303 0.4988 0.0043 0.0093 -0.0011 91 VAL B CG2 3140 N N . TRP B 92 ? 0.3200 0.3410 0.4994 0.0156 0.0039 -0.0054 92 TRP B N 3141 C CA . TRP B 92 ? 0.3177 0.3511 0.4952 0.0158 0.0010 -0.0060 92 TRP B CA 3142 C C . TRP B 92 ? 0.3238 0.3586 0.4954 0.0235 -0.0022 -0.0014 92 TRP B C 3143 O O . TRP B 92 ? 0.3174 0.3603 0.4836 0.0218 -0.0051 -0.0001 92 TRP B O 3144 C CB . TRP B 92 ? 0.3146 0.3642 0.4985 0.0133 -0.0006 -0.0086 92 TRP B CB 3145 C CG . TRP B 92 ? 0.3231 0.3654 0.5042 0.0035 0.0012 -0.0121 92 TRP B CG 3146 C CD1 . TRP B 92 ? 0.3128 0.3501 0.4962 0.0011 0.0027 -0.0132 92 TRP B CD1 3147 C CD2 . TRP B 92 ? 0.3379 0.3698 0.5071 -0.0040 0.0016 -0.0146 92 TRP B CD2 3148 N NE1 . TRP B 92 ? 0.3352 0.3586 0.5087 -0.0063 0.0035 -0.0150 92 TRP B NE1 3149 C CE2 . TRP B 92 ? 0.3489 0.3661 0.5122 -0.0089 0.0034 -0.0166 92 TRP B CE2 3150 C CE3 . TRP B 92 ? 0.3478 0.3774 0.5062 -0.0069 0.0008 -0.0155 92 TRP B CE3 3151 C CZ2 . TRP B 92 ? 0.3682 0.3628 0.5126 -0.0144 0.0049 -0.0197 92 TRP B CZ2 3152 C CZ3 . TRP B 92 ? 0.3673 0.3769 0.5076 -0.0141 0.0029 -0.0198 92 TRP B CZ3 3153 C CH2 . TRP B 92 ? 0.3792 0.3691 0.5116 -0.0168 0.0052 -0.0221 92 TRP B CH2 3154 N N . SER B 93 ? 0.3337 0.3565 0.5017 0.0320 -0.0020 0.0014 93 SER B N 3155 C CA . SER B 93 ? 0.3541 0.3686 0.5100 0.0429 -0.0053 0.0071 93 SER B CA 3156 C C . SER B 93 ? 0.3704 0.3709 0.5134 0.0358 -0.0049 0.0110 93 SER B C 3157 O O . SER B 93 ? 0.3854 0.3874 0.5186 0.0403 -0.0090 0.0158 93 SER B O 3158 C CB . SER B 93 ? 0.3759 0.3669 0.5214 0.0533 -0.0039 0.0082 93 SER B CB 3159 O OG . SER B 93 ? 0.3777 0.3855 0.5338 0.0624 -0.0028 0.0043 93 SER B OG 3160 N N . TYR B 94 ? 0.3633 0.3547 0.5064 0.0247 -0.0001 0.0095 94 TYR B N 3161 C CA . TYR B 94 ? 0.3796 0.3664 0.5135 0.0161 0.0027 0.0122 94 TYR B CA 3162 C C . TYR B 94 ? 0.3695 0.3725 0.5056 0.0139 0.0031 0.0090 94 TYR B C 3163 O O . TYR B 94 ? 0.3774 0.3785 0.5002 0.0124 0.0021 0.0122 94 TYR B O 3164 C CB . TYR B 94 ? 0.3897 0.3760 0.5286 0.0059 0.0082 0.0111 94 TYR B CB 3165 C CG . TYR B 94 ? 0.4143 0.4090 0.5496 -0.0024 0.0136 0.0126 94 TYR B CG 3166 C CD1 . TYR B 94 ? 0.4615 0.4440 0.5794 -0.0115 0.0150 0.0189 94 TYR B CD1 3167 C CD2 . TYR B 94 ? 0.4241 0.4365 0.5696 -0.0009 0.0183 0.0077 94 TYR B CD2 3168 C CE1 . TYR B 94 ? 0.4776 0.4740 0.5926 -0.0201 0.0216 0.0203 94 TYR B CE1 3169 C CE2 . TYR B 94 ? 0.4439 0.4673 0.5856 -0.0051 0.0254 0.0081 94 TYR B CE2 3170 C CZ . TYR B 94 ? 0.4750 0.4948 0.6037 -0.0153 0.0274 0.0144 94 TYR B CZ 3171 O OH . TYR B 94 ? 0.5131 0.5499 0.6384 -0.0206 0.0359 0.0150 94 TYR B OH 3172 N N . ASN B 95 ? 0.3513 0.3649 0.4986 0.0124 0.0046 0.0027 95 ASN B N 3173 C CA . ASN B 95 ? 0.3581 0.3768 0.4994 0.0084 0.0055 -0.0017 95 ASN B CA 3174 C C . ASN B 95 ? 0.3609 0.3884 0.4936 0.0079 -0.0016 0.0004 95 ASN B C 3175 O O . ASN B 95 ? 0.3651 0.3911 0.4834 0.0032 -0.0014 -0.0001 95 ASN B O 3176 C CB . ASN B 95 ? 0.3573 0.3765 0.5047 0.0063 0.0067 -0.0079 95 ASN B CB 3177 C CG . ASN B 95 ? 0.3756 0.3891 0.5286 0.0089 0.0132 -0.0095 95 ASN B CG 3178 O OD1 . ASN B 95 ? 0.3704 0.3865 0.5248 0.0101 0.0175 -0.0068 95 ASN B OD1 3179 N ND2 . ASN B 95 ? 0.3797 0.3884 0.5353 0.0091 0.0134 -0.0129 95 ASN B ND2 3180 N N . ALA B 96 ? 0.3590 0.3992 0.5002 0.0136 -0.0077 0.0029 96 ALA B N 3181 C CA . ALA B 96 ? 0.3758 0.4363 0.5133 0.0153 -0.0160 0.0065 96 ALA B CA 3182 C C . ALA B 96 ? 0.3980 0.4500 0.5201 0.0210 -0.0192 0.0142 96 ALA B C 3183 O O . ALA B 96 ? 0.4080 0.4702 0.5187 0.0161 -0.0244 0.0160 96 ALA B O 3184 C CB . ALA B 96 ? 0.3630 0.4456 0.5155 0.0249 -0.0202 0.0083 96 ALA B CB 3185 N N . GLU B 97 ? 0.4140 0.4443 0.5315 0.0290 -0.0167 0.0191 97 GLU B N 3186 C CA . GLU B 97 ? 0.4422 0.4547 0.5389 0.0331 -0.0194 0.0279 97 GLU B CA 3187 C C . GLU B 97 ? 0.4418 0.4484 0.5242 0.0193 -0.0149 0.0268 97 GLU B C 3188 O O . GLU B 97 ? 0.4565 0.4623 0.5209 0.0185 -0.0196 0.0325 97 GLU B O 3189 C CB . GLU B 97 ? 0.4692 0.4506 0.5576 0.0381 -0.0160 0.0319 97 GLU B CB 3190 C CG . GLU B 97 ? 0.5169 0.4691 0.5762 0.0423 -0.0193 0.0424 97 GLU B CG 3191 C CD . GLU B 97 ? 0.5562 0.5011 0.6069 0.0654 -0.0272 0.0496 97 GLU B CD 3192 O OE1 . GLU B 97 ? 0.5605 0.5017 0.6197 0.0775 -0.0260 0.0466 97 GLU B OE1 3193 O OE2 . GLU B 97 ? 0.6037 0.5463 0.6370 0.0736 -0.0344 0.0585 97 GLU B OE2 3194 N N . LEU B 98 ? 0.4093 0.4136 0.4987 0.0103 -0.0057 0.0198 98 LEU B N 3195 C CA . LEU B 98 ? 0.4186 0.4203 0.4955 0.0006 0.0015 0.0175 98 LEU B CA 3196 C C . LEU B 98 ? 0.4130 0.4245 0.4812 -0.0041 -0.0005 0.0118 98 LEU B C 3197 O O . LEU B 98 ? 0.4248 0.4330 0.4728 -0.0100 0.0011 0.0127 98 LEU B O 3198 C CB . LEU B 98 ? 0.4230 0.4260 0.5121 -0.0028 0.0120 0.0121 98 LEU B CB 3199 C CG . LEU B 98 ? 0.4588 0.4660 0.5382 -0.0085 0.0223 0.0086 98 LEU B CG 3200 C CD1 . LEU B 98 ? 0.4852 0.4862 0.5449 -0.0161 0.0239 0.0167 98 LEU B CD1 3201 C CD2 . LEU B 98 ? 0.4570 0.4747 0.5534 -0.0066 0.0314 0.0043 98 LEU B CD2 3202 N N . LEU B 99 ? 0.3972 0.4184 0.4763 -0.0044 -0.0036 0.0057 99 LEU B N 3203 C CA . LEU B 99 ? 0.4107 0.4361 0.4760 -0.0139 -0.0061 -0.0007 99 LEU B CA 3204 C C . LEU B 99 ? 0.4221 0.4601 0.4732 -0.0168 -0.0167 0.0059 99 LEU B C 3205 O O . LEU B 99 ? 0.4338 0.4665 0.4617 -0.0256 -0.0162 0.0037 99 LEU B O 3206 C CB . LEU B 99 ? 0.4070 0.4404 0.4840 -0.0177 -0.0092 -0.0063 99 LEU B CB 3207 C CG . LEU B 99 ? 0.4294 0.4650 0.4880 -0.0333 -0.0137 -0.0126 99 LEU B CG 3208 C CD1 . LEU B 99 ? 0.4485 0.4534 0.4827 -0.0390 -0.0036 -0.0225 99 LEU B CD1 3209 C CD2 . LEU B 99 ? 0.4236 0.4745 0.4960 -0.0394 -0.0186 -0.0144 99 LEU B CD2 3210 N N . VAL B 100 ? 0.4147 0.4697 0.4781 -0.0074 -0.0262 0.0142 100 VAL B N 3211 C CA . VAL B 100 ? 0.4401 0.5142 0.4931 -0.0058 -0.0384 0.0225 100 VAL B CA 3212 C C . VAL B 100 ? 0.4688 0.5240 0.4978 -0.0044 -0.0379 0.0301 100 VAL B C 3213 O O . VAL B 100 ? 0.4933 0.5569 0.5026 -0.0110 -0.0450 0.0334 100 VAL B O 3214 C CB . VAL B 100 ? 0.4336 0.5322 0.5064 0.0109 -0.0472 0.0303 100 VAL B CB 3215 C CG1 . VAL B 100 ? 0.4619 0.5850 0.5251 0.0177 -0.0608 0.0411 100 VAL B CG1 3216 C CG2 . VAL B 100 ? 0.4185 0.5424 0.5124 0.0049 -0.0476 0.0231 100 VAL B CG2 3217 N N . ALA B 101 ? 0.4749 0.5052 0.5027 0.0010 -0.0298 0.0332 101 ALA B N 3218 C CA . ALA B 101 ? 0.5129 0.5230 0.5150 -0.0014 -0.0281 0.0412 101 ALA B CA 3219 C C . ALA B 101 ? 0.5334 0.5404 0.5165 -0.0168 -0.0200 0.0341 101 ALA B C 3220 O O . ALA B 101 ? 0.5601 0.5648 0.5173 -0.0224 -0.0241 0.0394 101 ALA B O 3221 C CB . ALA B 101 ? 0.5148 0.5001 0.5181 0.0017 -0.0207 0.0452 101 ALA B CB 3222 N N . MET B 102 ? 0.5288 0.5346 0.5222 -0.0217 -0.0083 0.0223 102 MET B N 3223 C CA . MET B 102 ? 0.5649 0.5653 0.5385 -0.0316 0.0019 0.0138 102 MET B CA 3224 C C . MET B 102 ? 0.5640 0.5697 0.5189 -0.0406 -0.0056 0.0081 102 MET B C 3225 O O . MET B 102 ? 0.5862 0.5855 0.5118 -0.0495 -0.0032 0.0066 102 MET B O 3226 C CB . MET B 102 ? 0.5842 0.5814 0.5722 -0.0289 0.0167 0.0039 102 MET B CB 3227 C CG . MET B 102 ? 0.6241 0.6192 0.6197 -0.0277 0.0176 -0.0074 102 MET B CG 3228 S SD . MET B 102 ? 0.7492 0.7270 0.7101 -0.0347 0.0270 -0.0211 102 MET B SD 3229 C CE . MET B 102 ? 0.7117 0.6766 0.6789 -0.0343 0.0253 -0.0311 102 MET B CE 3230 N N . GLU B 103 ? 0.5275 0.5459 0.4961 -0.0413 -0.0148 0.0054 103 GLU B N 3231 C CA . GLU B 103 ? 0.5490 0.5771 0.4982 -0.0553 -0.0245 0.0015 103 GLU B CA 3232 C C . GLU B 103 ? 0.5576 0.6005 0.4901 -0.0570 -0.0374 0.0134 103 GLU B C 3233 O O . GLU B 103 ? 0.5776 0.6186 0.4795 -0.0713 -0.0405 0.0104 103 GLU B O 3234 C CB . GLU B 103 ? 0.5386 0.5869 0.5078 -0.0585 -0.0333 -0.0006 103 GLU B CB 3235 C CG . GLU B 103 ? 0.5391 0.5697 0.5182 -0.0591 -0.0229 -0.0116 103 GLU B CG 3236 C CD . GLU B 103 ? 0.5785 0.5854 0.5264 -0.0762 -0.0187 -0.0248 103 GLU B CD 3237 O OE1 . GLU B 103 ? 0.6132 0.6095 0.5282 -0.0868 -0.0188 -0.0282 103 GLU B OE1 3238 O OE2 . GLU B 103 ? 0.5986 0.5921 0.5504 -0.0792 -0.0149 -0.0320 103 GLU B OE2 3239 N N . ASN B 104 ? 0.5311 0.5848 0.4796 -0.0418 -0.0450 0.0270 104 ASN B N 3240 C CA . ASN B 104 ? 0.5561 0.6212 0.4882 -0.0379 -0.0585 0.0410 104 ASN B CA 3241 C C . ASN B 104 ? 0.5869 0.6276 0.4848 -0.0452 -0.0521 0.0438 104 ASN B C 3242 O O . ASN B 104 ? 0.6190 0.6671 0.4906 -0.0526 -0.0618 0.0494 104 ASN B O 3243 C CB . ASN B 104 ? 0.5457 0.6166 0.4967 -0.0151 -0.0659 0.0545 104 ASN B CB 3244 C CG . ASN B 104 ? 0.5285 0.6363 0.5095 -0.0067 -0.0751 0.0544 104 ASN B CG 3245 O OD1 . ASN B 104 ? 0.5253 0.6567 0.5125 -0.0218 -0.0776 0.0455 104 ASN B OD1 3246 N ND2 . ASN B 104 ? 0.5306 0.6419 0.5269 0.0165 -0.0794 0.0641 104 ASN B ND2 3247 N N . GLN B 105 ? 0.5670 0.6274 0.5086 -0.0124 -0.1571 0.0416 105 GLN B N 3248 C CA . GLN B 105 ? 0.5721 0.6457 0.5190 -0.0173 -0.1479 0.0418 105 GLN B CA 3249 C C . GLN B 105 ? 0.5862 0.6656 0.5120 -0.0205 -0.1452 0.0351 105 GLN B C 3250 O O . GLN B 105 ? 0.5978 0.6888 0.5130 -0.0270 -0.1385 0.0422 105 GLN B O 3251 C CB . GLN B 105 ? 0.5671 0.6410 0.5384 -0.0132 -0.1457 0.0303 105 GLN B CB 3252 C CG . GLN B 105 ? 0.5735 0.6643 0.5578 -0.0209 -0.1333 0.0322 105 GLN B CG 3253 C CD . GLN B 105 ? 0.5806 0.6700 0.5761 -0.0271 -0.1298 0.0482 105 GLN B CD 3254 O OE1 . GLN B 105 ? 0.5799 0.6572 0.5873 -0.0223 -0.1375 0.0513 105 GLN B OE1 3255 N NE2 . GLN B 105 ? 0.5954 0.6943 0.5844 -0.0377 -0.1184 0.0582 105 GLN B NE2 3256 N N . HIS B 106 ? 0.5894 0.6570 0.5054 -0.0154 -0.1514 0.0216 106 HIS B N 3257 C CA . HIS B 106 ? 0.6031 0.6711 0.4976 -0.0169 -0.1511 0.0127 106 HIS B CA 3258 C C . HIS B 106 ? 0.6084 0.6794 0.4808 -0.0247 -0.1528 0.0224 106 HIS B C 3259 O O . HIS B 106 ? 0.6223 0.7012 0.4791 -0.0284 -0.1495 0.0207 106 HIS B O 3260 C CB . HIS B 106 ? 0.6083 0.6552 0.4940 -0.0091 -0.1598 -0.0034 106 HIS B CB 3261 C CG . HIS B 106 ? 0.6299 0.6724 0.4930 -0.0088 -0.1614 -0.0147 106 HIS B CG 3262 N ND1 . HIS B 106 ? 0.6469 0.6731 0.4830 -0.0135 -0.1681 -0.0148 106 HIS B ND1 3263 C CD2 . HIS B 106 ? 0.6429 0.6952 0.5066 -0.0046 -0.1570 -0.0272 106 HIS B CD2 3264 C CE1 . HIS B 106 ? 0.6666 0.6892 0.4856 -0.0116 -0.1693 -0.0266 106 HIS B CE1 3265 N NE2 . HIS B 106 ? 0.6689 0.7081 0.5041 -0.0052 -0.1625 -0.0347 106 HIS B NE2 3266 N N . THR B 107 ? 0.6017 0.6683 0.4740 -0.0267 -0.1583 0.0310 107 THR B N 3267 C CA . THR B 107 ? 0.5992 0.6727 0.4563 -0.0338 -0.1617 0.0385 107 THR B CA 3268 C C . THR B 107 ? 0.6118 0.7020 0.4671 -0.0370 -0.1578 0.0506 107 THR B C 3269 O O . THR B 107 ? 0.6238 0.7207 0.4609 -0.0418 -0.1597 0.0520 107 THR B O 3270 C CB . THR B 107 ? 0.5853 0.6558 0.4486 -0.0345 -0.1670 0.0433 107 THR B CB 3271 O OG1 . THR B 107 ? 0.5918 0.6425 0.4455 -0.0345 -0.1704 0.0328 107 THR B OG1 3272 C CG2 . THR B 107 ? 0.5897 0.6753 0.4464 -0.0410 -0.1708 0.0508 107 THR B CG2 3273 N N . ILE B 108 ? 0.6115 0.7051 0.4829 -0.0345 -0.1534 0.0593 108 ILE B N 3274 C CA . ILE B 108 ? 0.6278 0.7301 0.4928 -0.0377 -0.1498 0.0727 108 ILE B CA 3275 C C . ILE B 108 ? 0.6421 0.7499 0.4932 -0.0417 -0.1402 0.0685 108 ILE B C 3276 O O . ILE B 108 ? 0.6451 0.7582 0.4748 -0.0455 -0.1395 0.0749 108 ILE B O 3277 C CB . ILE B 108 ? 0.6274 0.7259 0.5115 -0.0352 -0.1481 0.0833 108 ILE B CB 3278 C CG1 . ILE B 108 ? 0.6240 0.7207 0.5164 -0.0302 -0.1583 0.0886 108 ILE B CG1 3279 C CG2 . ILE B 108 ? 0.6411 0.7412 0.5144 -0.0400 -0.1419 0.0968 108 ILE B CG2 3280 C CD1 . ILE B 108 ? 0.6214 0.7095 0.5349 -0.0249 -0.1591 0.0934 108 ILE B CD1 3281 N N . ASP B 109 ? 0.6385 0.7460 0.5015 -0.0397 -0.1333 0.0563 109 ASP B N 3282 C CA . ASP B 109 ? 0.6569 0.7735 0.5102 -0.0420 -0.1229 0.0480 109 ASP B CA 3283 C C . ASP B 109 ? 0.6768 0.7921 0.5042 -0.0418 -0.1280 0.0389 109 ASP B C 3284 O O . ASP B 109 ? 0.7023 0.8252 0.5098 -0.0449 -0.1219 0.0383 109 ASP B O 3285 C CB . ASP B 109 ? 0.6456 0.7653 0.5227 -0.0374 -0.1172 0.0331 109 ASP B CB 3286 C CG . ASP B 109 ? 0.6388 0.7626 0.5416 -0.0404 -0.1099 0.0405 109 ASP B CG 3287 O OD1 . ASP B 109 ? 0.6544 0.7781 0.5508 -0.0473 -0.1057 0.0576 109 ASP B OD1 3288 O OD2 . ASP B 109 ? 0.6326 0.7577 0.5608 -0.0357 -0.1095 0.0289 109 ASP B OD2 3289 N N . LEU B 110 ? 0.6752 0.7788 0.5006 -0.0389 -0.1391 0.0319 110 LEU B N 3290 C CA . LEU B 110 ? 0.6982 0.7959 0.4992 -0.0404 -0.1458 0.0230 110 LEU B CA 3291 C C . LEU B 110 ? 0.7067 0.8119 0.4879 -0.0466 -0.1495 0.0338 110 LEU B C 3292 O O . LEU B 110 ? 0.7285 0.8351 0.4865 -0.0484 -0.1502 0.0279 110 LEU B O 3293 C CB . LEU B 110 ? 0.7008 0.7808 0.5029 -0.0391 -0.1560 0.0160 110 LEU B CB 3294 C CG . LEU B 110 ? 0.7219 0.7884 0.4994 -0.0425 -0.1644 0.0061 110 LEU B CG 3295 C CD1 . LEU B 110 ? 0.7286 0.7707 0.5058 -0.0381 -0.1701 -0.0056 110 LEU B CD1 3296 C CD2 . LEU B 110 ? 0.7227 0.7945 0.4925 -0.0517 -0.1712 0.0153 110 LEU B CD2 3297 N N . ALA B 111 ? 0.6915 0.8011 0.4815 -0.0483 -0.1534 0.0482 111 ALA B N 3298 C CA . ALA B 111 ? 0.7019 0.8195 0.4754 -0.0518 -0.1596 0.0582 111 ALA B CA 3299 C C . ALA B 111 ? 0.7278 0.8503 0.4837 -0.0527 -0.1514 0.0660 111 ALA B C 3300 O O . ALA B 111 ? 0.7500 0.8755 0.4804 -0.0547 -0.1556 0.0676 111 ALA B O 3301 C CB . ALA B 111 ? 0.6896 0.8112 0.4793 -0.0505 -0.1669 0.0697 111 ALA B CB 3302 N N . ASP B 112 ? 0.7274 0.8499 0.4959 -0.0521 -0.1396 0.0707 112 ASP B N 3303 C CA . ASP B 112 ? 0.7530 0.8785 0.5049 -0.0555 -0.1277 0.0783 112 ASP B CA 3304 C C . ASP B 112 ? 0.7720 0.9025 0.5034 -0.0562 -0.1212 0.0642 112 ASP B C 3305 O O . ASP B 112 ? 0.7865 0.9184 0.4877 -0.0586 -0.1191 0.0683 112 ASP B O 3306 C CB . ASP B 112 ? 0.7479 0.8734 0.5236 -0.0572 -0.1152 0.0823 112 ASP B CB 3307 C CG . ASP B 112 ? 0.7797 0.9053 0.5384 -0.0642 -0.1016 0.0947 112 ASP B CG 3308 O OD1 . ASP B 112 ? 0.8032 0.9242 0.5297 -0.0662 -0.1045 0.1052 112 ASP B OD1 3309 O OD2 . ASP B 112 ? 0.7746 0.9040 0.5517 -0.0686 -0.0878 0.0938 112 ASP B OD2 3310 N N . SER B 113 ? 0.7596 0.8907 0.5054 -0.0525 -0.1195 0.0468 113 SER B N 3311 C CA . SER B 113 ? 0.7765 0.9108 0.5054 -0.0502 -0.1154 0.0298 113 SER B CA 3312 C C . SER B 113 ? 0.7992 0.9287 0.4958 -0.0513 -0.1265 0.0279 113 SER B C 3313 O O . SER B 113 ? 0.8224 0.9563 0.4926 -0.0518 -0.1206 0.0241 113 SER B O 3314 C CB . SER B 113 ? 0.7569 0.8858 0.5048 -0.0433 -0.1185 0.0113 113 SER B CB 3315 O OG . SER B 113 ? 0.7812 0.9075 0.5090 -0.0391 -0.1203 -0.0060 113 SER B OG 3316 N N . GLU B 114 ? 0.7888 0.9104 0.4879 -0.0524 -0.1419 0.0295 114 GLU B N 3317 C CA . GLU B 114 ? 0.8056 0.9236 0.4791 -0.0550 -0.1544 0.0253 114 GLU B CA 3318 C C . GLU B 114 ? 0.8335 0.9578 0.4820 -0.0571 -0.1556 0.0377 114 GLU B C 3319 O O . GLU B 114 ? 0.8703 0.9934 0.4896 -0.0575 -0.1603 0.0312 114 GLU B O 3320 C CB . GLU B 114 ? 0.7908 0.9030 0.4767 -0.0585 -0.1687 0.0254 114 GLU B CB 3321 C CG . GLU B 114 ? 0.7877 0.8854 0.4842 -0.0573 -0.1706 0.0115 114 GLU B CG 3322 C CD . GLU B 114 ? 0.8110 0.8964 0.4834 -0.0563 -0.1744 -0.0060 114 GLU B CD 3323 O OE1 . GLU B 114 ? 0.8443 0.9307 0.4936 -0.0603 -0.1816 -0.0080 114 GLU B OE1 3324 O OE2 . GLU B 114 ? 0.8168 0.8898 0.4925 -0.0505 -0.1718 -0.0188 114 GLU B OE2 3325 N N . MET B 115 ? 0.8221 0.9498 0.4791 -0.0576 -0.1528 0.0551 115 MET B N 3326 C CA . MET B 115 ? 0.8485 0.9766 0.4776 -0.0583 -0.1538 0.0687 115 MET B CA 3327 C C . MET B 115 ? 0.8765 1.0052 0.4784 -0.0592 -0.1380 0.0650 115 MET B C 3328 O O . MET B 115 ? 0.9140 1.0404 0.4797 -0.0591 -0.1416 0.0657 115 MET B O 3329 C CB . MET B 115 ? 0.8411 0.9667 0.4836 -0.0578 -0.1529 0.0877 115 MET B CB 3330 C CG . MET B 115 ? 0.8741 0.9927 0.4836 -0.0578 -0.1543 0.1042 115 MET B CG 3331 S SD . MET B 115 ? 0.8840 1.0033 0.4808 -0.0525 -0.1807 0.1103 115 MET B SD 3332 C CE . MET B 115 ? 0.9118 1.0336 0.4720 -0.0536 -0.1867 0.0963 115 MET B CE 3333 N N . ASP B 116 ? 0.8596 0.9929 0.4792 -0.0599 -0.1207 0.0599 116 ASP B N 3334 C CA . ASP B 116 ? 0.8894 1.0288 0.4890 -0.0616 -0.1019 0.0549 116 ASP B CA 3335 C C . ASP B 116 ? 0.9019 1.0428 0.4785 -0.0574 -0.1053 0.0356 116 ASP B C 3336 O O . ASP B 116 ? 0.9357 1.0773 0.4760 -0.0580 -0.0992 0.0350 116 ASP B O 3337 C CB . ASP B 116 ? 0.8716 1.0211 0.5040 -0.0629 -0.0840 0.0494 116 ASP B CB 3338 C CG . ASP B 116 ? 0.9045 1.0656 0.5206 -0.0674 -0.0610 0.0463 116 ASP B CG 3339 O OD1 . ASP B 116 ? 0.9293 1.0852 0.5181 -0.0744 -0.0530 0.0631 116 ASP B OD1 3340 O OD2 . ASP B 116 ? 0.9048 1.0798 0.5345 -0.0636 -0.0509 0.0265 116 ASP B OD2 3341 N N . LYS B 117 ? 0.8711 1.0088 0.4654 -0.0531 -0.1158 0.0200 117 LYS B N 3342 C CA . LYS B 117 ? 0.8843 1.0174 0.4575 -0.0487 -0.1226 0.0006 117 LYS B CA 3343 C C . LYS B 117 ? 0.9132 1.0402 0.4490 -0.0506 -0.1359 0.0047 117 LYS B C 3344 O O . LYS B 117 ? 0.9410 1.0670 0.4453 -0.0478 -0.1342 -0.0065 117 LYS B O 3345 C CB . LYS B 117 ? 0.8576 0.9801 0.4527 -0.0457 -0.1349 -0.0126 117 LYS B CB 3346 C CG . LYS B 117 ? 0.8397 0.9662 0.4624 -0.0396 -0.1241 -0.0247 117 LYS B CG 3347 C CD . LYS B 117 ? 0.8125 0.9273 0.4639 -0.0387 -0.1340 -0.0256 117 LYS B CD 3348 C CE . LYS B 117 ? 0.8187 0.9122 0.4577 -0.0368 -0.1501 -0.0400 117 LYS B CE 3349 N NZ . LYS B 117 ? 0.7901 0.8700 0.4523 -0.0321 -0.1542 -0.0474 117 LYS B NZ 3350 N N . LEU B 118 ? 0.9018 1.0259 0.4417 -0.0544 -0.1497 0.0193 118 LEU B N 3351 C CA . LEU B 118 ? 0.9277 1.0484 0.4362 -0.0554 -0.1649 0.0235 118 LEU B CA 3352 C C . LEU B 118 ? 0.9688 1.0895 0.4404 -0.0547 -0.1549 0.0343 118 LEU B C 3353 O O . LEU B 118 ? 1.0029 1.1196 0.4364 -0.0528 -0.1601 0.0284 118 LEU B O 3354 C CB . LEU B 118 ? 0.9052 1.0275 0.4328 -0.0580 -0.1817 0.0352 118 LEU B CB 3355 C CG . LEU B 118 ? 0.9301 1.0525 0.4309 -0.0578 -0.2004 0.0392 118 LEU B CG 3356 C CD1 . LEU B 118 ? 0.9476 1.0657 0.4295 -0.0593 -0.2117 0.0202 118 LEU B CD1 3357 C CD2 . LEU B 118 ? 0.9080 1.0379 0.4350 -0.0588 -0.2156 0.0490 118 LEU B CD2 3358 N N . TYR B 119 ? 0.9686 1.0911 0.4488 -0.0569 -0.1407 0.0504 119 TYR B N 3359 C CA . TYR B 119 ? 1.0117 1.1298 0.4542 -0.0587 -0.1283 0.0631 119 TYR B CA 3360 C C . TYR B 119 ? 1.0396 1.1629 0.4561 -0.0579 -0.1112 0.0481 119 TYR B C 3361 O O . TYR B 119 ? 1.0865 1.2036 0.4567 -0.0570 -0.1108 0.0498 119 TYR B O 3362 C CB . TYR B 119 ? 1.0041 1.1209 0.4646 -0.0637 -0.1137 0.0811 119 TYR B CB 3363 C CG . TYR B 119 ? 1.0568 1.1637 0.4753 -0.0685 -0.0993 0.0967 119 TYR B CG 3364 C CD1 . TYR B 119 ? 1.0973 1.1869 0.4773 -0.0665 -0.1139 0.1128 119 TYR B CD1 3365 C CD2 . TYR B 119 ? 1.0722 1.1867 0.4883 -0.0753 -0.0713 0.0948 119 TYR B CD2 3366 C CE1 . TYR B 119 ? 1.1516 1.2256 0.4857 -0.0714 -0.1011 0.1285 119 TYR B CE1 3367 C CE2 . TYR B 119 ? 1.1235 1.2268 0.4975 -0.0825 -0.0557 0.1101 119 TYR B CE2 3368 C CZ . TYR B 119 ? 1.1669 1.2468 0.4966 -0.0807 -0.0708 0.1279 119 TYR B CZ 3369 O OH . TYR B 119 ? 1.2282 1.2904 0.5085 -0.0882 -0.0560 0.1446 119 TYR B OH 3370 N N . GLU B 120 ? 1.0176 1.1523 0.4633 -0.0567 -0.0983 0.0324 120 GLU B N 3371 C CA . GLU B 120 ? 1.0444 1.1889 0.4728 -0.0540 -0.0809 0.0149 120 GLU B CA 3372 C C . GLU B 120 ? 1.0657 1.2035 0.4634 -0.0471 -0.0955 -0.0026 120 GLU B C 3373 O O . GLU B 120 ? 1.1038 1.2437 0.4640 -0.0448 -0.0855 -0.0102 120 GLU B O 3374 C CB . GLU B 120 ? 1.0168 1.1762 0.4888 -0.0516 -0.0676 -0.0001 120 GLU B CB 3375 C CG . GLU B 120 ? 1.0059 1.1750 0.5077 -0.0592 -0.0496 0.0135 120 GLU B CG 3376 C CD . GLU B 120 ? 1.0490 1.2260 0.5236 -0.0672 -0.0245 0.0219 120 GLU B CD 3377 O OE1 . GLU B 120 ? 1.0760 1.2678 0.5377 -0.0645 -0.0088 0.0047 120 GLU B OE1 3378 O OE2 . GLU B 120 ? 1.0630 1.2301 0.5273 -0.0762 -0.0203 0.0453 120 GLU B OE2 3379 N N . ARG B 121 ? 1.0400 1.1689 0.4523 -0.0449 -0.1183 -0.0094 121 ARG B N 3380 C CA . ARG B 121 ? 1.0642 1.1830 0.4485 -0.0406 -0.1356 -0.0253 121 ARG B CA 3381 C C . ARG B 121 ? 1.1157 1.2286 0.4501 -0.0409 -0.1409 -0.0170 121 ARG B C 3382 O O . ARG B 121 ? 1.1501 1.2599 0.4480 -0.0361 -0.1398 -0.0309 121 ARG B O 3383 C CB . ARG B 121 ? 1.0348 1.1441 0.4418 -0.0432 -0.1595 -0.0275 121 ARG B CB 3384 C CG . ARG B 121 ? 1.0584 1.1551 0.4393 -0.0418 -0.1792 -0.0437 121 ARG B CG 3385 C CD . ARG B 121 ? 1.0507 1.1437 0.4380 -0.0486 -0.2026 -0.0358 121 ARG B CD 3386 N NE . ARG B 121 ? 1.0132 1.1052 0.4432 -0.0539 -0.2079 -0.0347 121 ARG B NE 3387 C CZ . ARG B 121 ? 0.9995 1.0929 0.4465 -0.0613 -0.2250 -0.0296 121 ARG B CZ 3388 N NH1 . ARG B 121 ? 1.0146 1.1119 0.4430 -0.0633 -0.2410 -0.0259 121 ARG B NH1 3389 N NH2 . ARG B 121 ? 0.9649 1.0567 0.4476 -0.0664 -0.2260 -0.0291 121 ARG B NH2 3390 N N . VAL B 122 ? 1.1225 1.2322 0.4540 -0.0451 -0.1481 0.0049 122 VAL B N 3391 C CA . VAL B 122 ? 1.1742 1.2745 0.4572 -0.0440 -0.1576 0.0145 122 VAL B CA 3392 C C . VAL B 122 ? 1.2223 1.3223 0.4641 -0.0436 -0.1336 0.0172 122 VAL B C 3393 O O . VAL B 122 ? 1.2645 1.3573 0.4589 -0.0395 -0.1373 0.0099 122 VAL B O 3394 C CB . VAL B 122 ? 1.1689 1.2646 0.4594 -0.0463 -0.1712 0.0373 122 VAL B CB 3395 C CG1 . VAL B 122 ? 1.2243 1.3068 0.4594 -0.0430 -0.1810 0.0481 122 VAL B CG1 3396 C CG2 . VAL B 122 ? 1.1320 1.2320 0.4599 -0.0471 -0.1949 0.0322 122 VAL B CG2 3397 N N . LYS B 123 ? 1.2189 1.3270 0.4782 -0.0488 -0.1086 0.0267 123 LYS B N 3398 C CA . LYS B 123 ? 1.2693 1.3808 0.4937 -0.0515 -0.0812 0.0282 123 LYS B CA 3399 C C . LYS B 123 ? 1.2920 1.4118 0.4975 -0.0444 -0.0746 0.0016 123 LYS B C 3400 O O . LYS B 123 ? 1.3422 1.4571 0.4954 -0.0426 -0.0667 -0.0008 123 LYS B O 3401 C CB . LYS B 123 ? 1.2520 1.3772 0.5116 -0.0596 -0.0543 0.0357 123 LYS B CB 3402 C CG . LYS B 123 ? 1.3051 1.4350 0.5290 -0.0666 -0.0233 0.0404 123 LYS B CG 3403 C CD . LYS B 123 ? 1.2883 1.4462 0.5513 -0.0695 0.0044 0.0247 123 LYS B CD 3404 C CE . LYS B 123 ? 1.2563 1.4200 0.5679 -0.0789 0.0134 0.0387 123 LYS B CE 3405 N NZ . LYS B 123 ? 1.2992 1.4494 0.5816 -0.0927 0.0294 0.0651 123 LYS B NZ 3406 N N . ARG B 124 ? 1.2550 1.3848 0.5002 -0.0393 -0.0786 -0.0189 124 ARG B N 3407 C CA . ARG B 124 ? 1.2788 1.4148 0.5107 -0.0302 -0.0740 -0.0467 124 ARG B CA 3408 C C . ARG B 124 ? 1.3181 1.4370 0.5033 -0.0242 -0.0961 -0.0560 124 ARG B C 3409 O O . ARG B 124 ? 1.3603 1.4810 0.5124 -0.0170 -0.0886 -0.0741 124 ARG B O 3410 C CB . ARG B 124 ? 1.2379 1.3810 0.5199 -0.0249 -0.0782 -0.0654 124 ARG B CB 3411 C CG . ARG B 124 ? 1.2070 1.3697 0.5349 -0.0287 -0.0562 -0.0616 124 ARG B CG 3412 C CD . ARG B 124 ? 1.1860 1.3582 0.5493 -0.0188 -0.0551 -0.0874 124 ARG B CD 3413 N NE . ARG B 124 ? 1.1626 1.3585 0.5666 -0.0215 -0.0321 -0.0872 124 ARG B NE 3414 C CZ . ARG B 124 ? 1.1154 1.3125 0.5632 -0.0264 -0.0344 -0.0761 124 ARG B CZ 3415 N NH1 . ARG B 124 ? 1.0908 1.2680 0.5485 -0.0291 -0.0572 -0.0638 124 ARG B NH1 3416 N NH2 . ARG B 124 ? 1.0992 1.3194 0.5821 -0.0289 -0.0134 -0.0785 124 ARG B NH2 3417 N N . GLN B 125 ? 1.3064 1.4105 0.4900 -0.0267 -0.1232 -0.0452 125 GLN B N 3418 C CA . GLN B 125 ? 1.3426 1.4312 0.4834 -0.0224 -0.1467 -0.0529 125 GLN B CA 3419 C C . GLN B 125 ? 1.4020 1.4835 0.4809 -0.0211 -0.1392 -0.0430 125 GLN B C 3420 O O . GLN B 125 ? 1.4543 1.5282 0.4888 -0.0143 -0.1440 -0.0582 125 GLN B O 3421 C CB . GLN B 125 ? 1.3178 1.3982 0.4781 -0.0266 -0.1767 -0.0437 125 GLN B CB 3422 C CG . GLN B 125 ? 1.2684 1.3500 0.4788 -0.0290 -0.1881 -0.0549 125 GLN B CG 3423 C CD . GLN B 125 ? 1.2430 1.3227 0.4774 -0.0354 -0.2123 -0.0439 125 GLN B CD 3424 O OE1 . GLN B 125 ? 1.2041 1.2911 0.4787 -0.0401 -0.2090 -0.0306 125 GLN B OE1 3425 N NE2 . GLN B 125 ? 1.2677 1.3394 0.4789 -0.0355 -0.2368 -0.0507 125 GLN B NE2 3426 N N . LEU B 126 ? 1.4052 1.4855 0.4778 -0.0275 -0.1280 -0.0175 126 LEU B N 3427 C CA . LEU B 126 ? 1.4674 1.5327 0.4761 -0.0272 -0.1256 -0.0032 126 LEU B CA 3428 C C . LEU B 126 ? 1.5093 1.5793 0.4750 -0.0261 -0.0957 -0.0118 126 LEU B C 3429 O O . LEU B 126 ? 1.5775 1.6324 0.4803 -0.0223 -0.0986 -0.0107 126 LEU B O 3430 C CB . LEU B 126 ? 1.4683 1.5247 0.4802 -0.0343 -0.1244 0.0273 126 LEU B CB 3431 C CG . LEU B 126 ? 1.4281 1.4825 0.4809 -0.0341 -0.1535 0.0357 126 LEU B CG 3432 C CD1 . LEU B 126 ? 1.4411 1.4821 0.4860 -0.0376 -0.1551 0.0646 126 LEU B CD1 3433 C CD2 . LEU B 126 ? 1.4413 1.4891 0.4785 -0.0271 -0.1873 0.0228 126 LEU B CD2 3434 N N . ARG B 127 ? 1.4789 1.5706 0.4777 -0.0291 -0.0672 -0.0209 127 ARG B N 3435 C CA . ARG B 127 ? 1.5191 1.6238 0.4879 -0.0266 -0.0383 -0.0365 127 ARG B CA 3436 C C . ARG B 127 ? 1.5960 1.6862 0.4921 -0.0308 -0.0232 -0.0215 127 ARG B C 3437 O O . ARG B 127 ? 1.6510 1.7306 0.4916 -0.0226 -0.0293 -0.0333 127 ARG B O 3438 C CB . ARG B 127 ? 1.5276 1.6336 0.4881 -0.0131 -0.0521 -0.0683 127 ARG B CB 3439 C CG . ARG B 127 ? 1.4700 1.5900 0.4935 -0.0083 -0.0577 -0.0881 127 ARG B CG 3440 C CD . ARG B 127 ? 1.4912 1.6157 0.5006 0.0053 -0.0575 -0.1216 127 ARG B CD 3441 N NE . ARG B 127 ? 1.5347 1.6766 0.5115 0.0078 -0.0248 -0.1306 127 ARG B NE 3442 C CZ . ARG B 127 ? 1.5600 1.7117 0.5230 0.0209 -0.0174 -0.1608 127 ARG B CZ 3443 N NH1 . ARG B 127 ? 1.5439 1.6851 0.5216 0.0329 -0.0415 -0.1843 127 ARG B NH1 3444 N NH2 . ARG B 127 ? 1.6021 1.7734 0.5358 0.0217 0.0152 -0.1679 127 ARG B NH2 3445 N N . GLU B 128 ? 1.6023 1.6887 0.4950 -0.0437 -0.0044 0.0045 128 GLU B N 3446 C CA . GLU B 128 ? 1.6739 1.7429 0.4947 -0.0504 0.0145 0.0213 128 GLU B CA 3447 C C . GLU B 128 ? 1.7229 1.7546 0.4811 -0.0445 -0.0160 0.0364 128 GLU B C 3448 O O . GLU B 128 ? 1.8000 1.8099 0.4892 -0.0484 -0.0046 0.0511 128 GLU B O 3449 C CB . GLU B 128 ? 1.7154 1.8032 0.5047 -0.0480 0.0446 -0.0008 128 GLU B CB 3450 C CG . GLU B 128 ? 1.7759 1.8623 0.5213 -0.0630 0.0837 0.0157 128 GLU B CG 3451 C CD . GLU B 128 ? 1.7357 1.8411 0.5365 -0.0799 0.1099 0.0287 128 GLU B CD 3452 O OE1 . GLU B 128 ? 1.6619 1.7949 0.5372 -0.0771 0.1082 0.0139 128 GLU B OE1 3453 O OE2 . GLU B 128 ? 1.7795 1.8693 0.5467 -0.0962 0.1313 0.0538 128 GLU B OE2 3454 N N . ASN B 129 ? 1.6880 1.7124 0.4693 -0.0354 -0.0547 0.0323 129 ASN B N 3455 C CA . ASN B 129 ? 1.7245 1.7180 0.4613 -0.0295 -0.0878 0.0470 129 ASN B CA 3456 C C . ASN B 129 ? 1.7088 1.6886 0.4666 -0.0360 -0.0967 0.0760 129 ASN B C 3457 O O . ASN B 129 ? 1.7425 1.6968 0.4668 -0.0303 -0.1240 0.0904 129 ASN B O 3458 C CB . ASN B 129 ? 1.6976 1.6929 0.4512 -0.0178 -0.1257 0.0266 129 ASN B CB 3459 C CG . ASN B 129 ? 1.7147 1.7191 0.4481 -0.0098 -0.1215 -0.0037 129 ASN B CG 3460 O OD1 . ASN B 129 ? 1.7274 1.7455 0.4515 -0.0118 -0.0888 -0.0136 129 ASN B OD1 3461 N ND2 . ASN B 129 ? 1.7151 1.7128 0.4436 -0.0007 -0.1552 -0.0200 129 ASN B ND2 3462 N N . ALA B 130 ? 1.6629 1.6596 0.4768 -0.0463 -0.0757 0.0829 130 ALA B N 3463 C CA . ALA B 130 ? 1.6436 1.6273 0.4801 -0.0526 -0.0812 0.1092 130 ALA B CA 3464 C C . ALA B 130 ? 1.6285 1.6234 0.4924 -0.0680 -0.0438 0.1194 130 ALA B C 3465 O O . ALA B 130 ? 1.6094 1.6303 0.4920 -0.0726 -0.0158 0.1026 130 ALA B O 3466 C CB . ALA B 130 ? 1.5741 1.5692 0.4743 -0.0464 -0.1116 0.1037 130 ALA B CB 3467 N N . GLU B 131 ? 1.6378 1.6129 0.5047 -0.0752 -0.0446 0.1457 131 GLU B N 3468 C CA . GLU B 131 ? 1.6259 1.6090 0.5244 -0.0912 -0.0132 0.1569 131 GLU B CA 3469 C C . GLU B 131 ? 1.5762 1.5582 0.5335 -0.0913 -0.0299 0.1684 131 GLU B C 3470 O O . GLU B 131 ? 1.5639 1.5321 0.5232 -0.0802 -0.0639 0.1739 131 GLU B O 3471 C CB . GLU B 131 ? 1.7074 1.6600 0.5377 -0.1044 0.0101 0.1806 131 GLU B CB 3472 C CG . GLU B 131 ? 1.7663 1.7242 0.5403 -0.1074 0.0356 0.1691 131 GLU B CG 3473 C CD . GLU B 131 ? 1.8411 1.7747 0.5571 -0.1261 0.0687 0.1915 131 GLU B CD 3474 O OE1 . GLU B 131 ? 1.8590 1.7624 0.5676 -0.1356 0.0667 0.2185 131 GLU B OE1 3475 O OE2 . GLU B 131 ? 1.8814 1.8249 0.5572 -0.1319 0.0972 0.1817 131 GLU B OE2 3476 N N . GLU B 132 ? 1.5490 1.5476 0.5550 -0.1035 -0.0059 0.1702 132 GLU B N 3477 C CA . GLU B 132 ? 1.5009 1.4996 0.5641 -0.1040 -0.0184 0.1795 132 GLU B CA 3478 C C . GLU B 132 ? 1.5462 1.5054 0.5767 -0.1098 -0.0233 0.2104 132 GLU B C 3479 O O . GLU B 132 ? 1.5945 1.5368 0.5904 -0.1250 0.0027 0.2256 132 GLU B O 3480 C CB . GLU B 132 ? 1.4511 1.4812 0.5786 -0.1139 0.0070 0.1684 132 GLU B CB 3481 C CG . GLU B 132 ? 1.3950 1.4596 0.5720 -0.1041 0.0016 0.1388 132 GLU B CG 3482 C CD . GLU B 132 ? 1.3432 1.4342 0.5883 -0.1104 0.0181 0.1295 132 GLU B CD 3483 O OE1 . GLU B 132 ? 1.3647 1.4601 0.6145 -0.1251 0.0460 0.1372 132 GLU B OE1 3484 O OE2 . GLU B 132 ? 1.2883 1.3949 0.5813 -0.1012 0.0029 0.1138 132 GLU B OE2 3485 N N . ASP B 133 ? 1.5356 1.4798 0.5777 -0.0980 -0.0568 0.2187 133 ASP B N 3486 C CA . ASP B 133 ? 1.5735 1.4797 0.5944 -0.0997 -0.0670 0.2460 133 ASP B CA 3487 C C . ASP B 133 ? 1.5359 1.4467 0.6054 -0.1137 -0.0467 0.2537 133 ASP B C 3488 O O . ASP B 133 ? 1.5835 1.4653 0.6226 -0.1274 -0.0302 0.2746 133 ASP B O 3489 C CB . ASP B 133 ? 1.5592 1.4583 0.5931 -0.0809 -0.1087 0.2469 133 ASP B CB 3490 C CG . ASP B 133 ? 1.5926 1.4536 0.6114 -0.0787 -0.1232 0.2722 133 ASP B CG 3491 O OD1 . ASP B 133 ? 1.6607 1.4819 0.6164 -0.0858 -0.1144 0.2930 133 ASP B OD1 3492 O OD2 . ASP B 133 ? 1.5516 1.4208 0.6198 -0.0696 -0.1435 0.2708 133 ASP B OD2 3493 N N . GLY B 134 ? 1.4552 1.4002 0.5977 -0.1107 -0.0485 0.2367 134 GLY B N 3494 C CA . GLY B 134 ? 1.4128 1.3657 0.6075 -0.1218 -0.0326 0.2403 134 GLY B CA 3495 C C . GLY B 134 ? 1.3680 1.3141 0.6040 -0.1117 -0.0587 0.2461 134 GLY B C 3496 O O . GLY B 134 ? 1.3344 1.2855 0.6153 -0.1186 -0.0497 0.2481 134 GLY B O 3497 N N . THR B 135 ? 1.3701 1.3065 0.5920 -0.0950 -0.0909 0.2474 135 THR B N 3498 C CA . THR B 135 ? 1.3287 1.2643 0.5907 -0.0830 -0.1170 0.2495 135 THR B CA 3499 C C . THR B 135 ? 1.2730 1.2436 0.5772 -0.0716 -0.1335 0.2263 135 THR B C 3500 O O . THR B 135 ? 1.2446 1.2197 0.5776 -0.0602 -0.1573 0.2248 135 THR B O 3501 C CB . THR B 135 ? 1.3810 1.2791 0.5979 -0.0716 -0.1438 0.2687 135 THR B CB 3502 O OG1 . THR B 135 ? 1.3978 1.2988 0.5796 -0.0601 -0.1630 0.2610 135 THR B OG1 3503 C CG2 . THR B 135 ? 1.4511 1.3055 0.6137 -0.0838 -0.1285 0.2935 135 THR B CG2 3504 N N . GLY B 136 ? 1.2611 1.2559 0.5686 -0.0754 -0.1200 0.2077 136 GLY B N 3505 C CA . GLY B 136 ? 1.2171 1.2387 0.5536 -0.0668 -0.1350 0.1860 136 GLY B CA 3506 C C . GLY B 136 ? 1.2550 1.2692 0.5479 -0.0574 -0.1571 0.1841 136 GLY B C 3507 O O . GLY B 136 ? 1.2374 1.2598 0.5480 -0.0475 -0.1831 0.1782 136 GLY B O 3508 N N . CYS B 137 ? 1.6986 1.4858 0.6477 -0.0174 -0.1811 -0.0339 137 CYS B N 3509 C CA . CYS B 137 ? 1.6654 1.4886 0.6620 0.0111 -0.1892 -0.0244 137 CYS B CA 3510 C C . CYS B 137 ? 1.6195 1.4827 0.6270 0.0198 -0.2186 -0.0195 137 CYS B C 3511 O O . CYS B 137 ? 1.6181 1.4778 0.6055 0.0118 -0.2252 -0.0187 137 CYS B O 3512 C CB . CYS B 137 ? 1.6903 1.4987 0.7101 0.0282 -0.1614 -0.0137 137 CYS B CB 3513 S SG . CYS B 137 ? 1.6757 1.5242 0.7570 0.0546 -0.1645 0.0037 137 CYS B SG 3514 N N . PHE B 138 ? 1.5836 1.4825 0.6210 0.0338 -0.2343 -0.0168 138 PHE B N 3515 C CA . PHE B 138 ? 1.5578 1.4892 0.6002 0.0392 -0.2572 -0.0167 138 PHE B CA 3516 C C . PHE B 138 ? 1.5501 1.5110 0.6146 0.0556 -0.2629 -0.0057 138 PHE B C 3517 O O . PHE B 138 ? 1.5389 1.5191 0.6285 0.0613 -0.2670 -0.0016 138 PHE B O 3518 C CB . PHE B 138 ? 1.5386 1.4853 0.5894 0.0335 -0.2721 -0.0263 138 PHE B CB 3519 C CG . PHE B 138 ? 1.5429 1.4740 0.5777 0.0163 -0.2728 -0.0296 138 PHE B CG 3520 C CD1 . PHE B 138 ? 1.5400 1.4745 0.5649 0.0101 -0.2805 -0.0260 138 PHE B CD1 3521 C CD2 . PHE B 138 ? 1.5501 1.4668 0.5824 0.0052 -0.2660 -0.0321 138 PHE B CD2 3522 C CE1 . PHE B 138 ? 1.5426 1.4713 0.5599 -0.0080 -0.2842 -0.0209 138 PHE B CE1 3523 C CE2 . PHE B 138 ? 1.5563 1.4657 0.5736 -0.0144 -0.2700 -0.0296 138 PHE B CE2 3524 C CZ . PHE B 138 ? 1.5529 1.4709 0.5650 -0.0216 -0.2806 -0.0220 138 PHE B CZ 3525 N N . GLU B 139 ? 1.5539 1.5219 0.6098 0.0610 -0.2649 0.0020 139 GLU B N 3526 C CA . GLU B 139 ? 1.5536 1.5563 0.6255 0.0724 -0.2741 0.0162 139 GLU B CA 3527 C C . GLU B 139 ? 1.5458 1.5765 0.6092 0.0677 -0.2956 0.0052 139 GLU B C 3528 O O . GLU B 139 ? 1.5437 1.5687 0.5863 0.0628 -0.2992 -0.0058 139 GLU B O 3529 C CB . GLU B 139 ? 1.5630 1.5631 0.6286 0.0794 -0.2664 0.0304 139 GLU B CB 3530 C CG . GLU B 139 ? 1.5801 1.5585 0.6658 0.0871 -0.2412 0.0462 139 GLU B CG 3531 C CD . GLU B 139 ? 1.5921 1.5618 0.6733 0.0926 -0.2304 0.0591 139 GLU B CD 3532 O OE1 . GLU B 139 ? 1.5807 1.5717 0.6477 0.0934 -0.2456 0.0611 139 GLU B OE1 3533 O OE2 . GLU B 139 ? 1.6115 1.5496 0.7036 0.0955 -0.2033 0.0668 139 GLU B OE2 3534 N N . ILE B 140 ? 1.5482 1.6076 0.6294 0.0674 -0.3075 0.0092 140 ILE B N 3535 C CA . ILE B 140 ? 1.5575 1.6376 0.6269 0.0573 -0.3250 -0.0056 140 ILE B CA 3536 C C . ILE B 140 ? 1.5824 1.6967 0.6401 0.0557 -0.3379 0.0064 140 ILE B C 3537 O O . ILE B 140 ? 1.5843 1.7267 0.6644 0.0597 -0.3436 0.0314 140 ILE B O 3538 C CB . ILE B 140 ? 1.5500 1.6409 0.6427 0.0514 -0.3326 -0.0098 140 ILE B CB 3539 C CG1 . ILE B 140 ? 1.5365 1.5964 0.6418 0.0533 -0.3180 -0.0157 140 ILE B CG1 3540 C CG2 . ILE B 140 ? 1.5581 1.6592 0.6345 0.0369 -0.3461 -0.0313 140 ILE B CG2 3541 C CD1 . ILE B 140 ? 1.5295 1.5987 0.6631 0.0502 -0.3219 -0.0158 140 ILE B CD1 3542 N N . PHE B 141 ? 1.6079 1.7210 0.6325 0.0489 -0.3409 -0.0086 141 PHE B N 3543 C CA . PHE B 141 ? 1.6444 1.7875 0.6464 0.0435 -0.3517 0.0007 141 PHE B CA 3544 C C . PHE B 141 ? 1.6671 1.8445 0.6637 0.0255 -0.3723 -0.0005 141 PHE B C 3545 O O . PHE B 141 ? 1.6896 1.9068 0.6888 0.0210 -0.3869 0.0247 141 PHE B O 3546 C CB . PHE B 141 ? 1.6683 1.7945 0.6337 0.0407 -0.3431 -0.0168 141 PHE B CB 3547 C CG . PHE B 141 ? 1.6602 1.7613 0.6307 0.0547 -0.3273 -0.0098 141 PHE B CG 3548 C CD1 . PHE B 141 ? 1.6623 1.7711 0.6446 0.0660 -0.3242 0.0158 141 PHE B CD1 3549 C CD2 . PHE B 141 ? 1.6579 1.7289 0.6258 0.0548 -0.3151 -0.0258 141 PHE B CD2 3550 C CE1 . PHE B 141 ? 1.6601 1.7437 0.6445 0.0744 -0.3103 0.0208 141 PHE B CE1 3551 C CE2 . PHE B 141 ? 1.6513 1.7037 0.6242 0.0627 -0.3044 -0.0161 141 PHE B CE2 3552 C CZ . PHE B 141 ? 1.6524 1.7093 0.6300 0.0711 -0.3025 0.0049 141 PHE B CZ 3553 N N . HIS B 142 ? 1.6703 1.8346 0.6612 0.0128 -0.3742 -0.0268 142 HIS B N 3554 C CA . HIS B 142 ? 1.6961 1.8894 0.6796 -0.0097 -0.3945 -0.0311 142 HIS B CA 3555 C C . HIS B 142 ? 1.6746 1.8926 0.7074 -0.0057 -0.4053 -0.0063 142 HIS B C 3556 O O . HIS B 142 ? 1.6361 1.8378 0.7042 0.0142 -0.3915 0.0058 142 HIS B O 3557 C CB . HIS B 142 ? 1.7165 1.8821 0.6775 -0.0261 -0.3883 -0.0698 142 HIS B CB 3558 C CG . HIS B 142 ? 1.6879 1.8298 0.6853 -0.0182 -0.3797 -0.0791 142 HIS B CG 3559 N ND1 . HIS B 142 ? 1.6837 1.8424 0.7093 -0.0265 -0.3928 -0.0749 142 HIS B ND1 3560 C CD2 . HIS B 142 ? 1.6612 1.7675 0.6722 -0.0049 -0.3604 -0.0894 142 HIS B CD2 3561 C CE1 . HIS B 142 ? 1.6565 1.7886 0.7092 -0.0171 -0.3802 -0.0838 142 HIS B CE1 3562 N NE2 . HIS B 142 ? 1.6435 1.7453 0.6871 -0.0052 -0.3616 -0.0918 142 HIS B NE2 3563 N N . LYS B 143 ? 1.6996 1.9559 0.7332 -0.0272 -0.4287 0.0015 143 LYS B N 3564 C CA . LYS B 143 ? 1.6860 1.9739 0.7734 -0.0247 -0.4403 0.0316 143 LYS B CA 3565 C C . LYS B 143 ? 1.6642 1.9254 0.7722 -0.0253 -0.4334 0.0095 143 LYS B C 3566 O O . LYS B 143 ? 1.6854 1.9358 0.7673 -0.0460 -0.4392 -0.0210 143 LYS B O 3567 C CB . LYS B 143 ? 1.7241 2.0714 0.8074 -0.0521 -0.4725 0.0546 143 LYS B CB 3568 C CG . LYS B 143 ? 1.7571 2.1367 0.8094 -0.0594 -0.4835 0.0752 143 LYS B CG 3569 C CD . LYS B 143 ? 1.7399 2.1550 0.8477 -0.0372 -0.4827 0.1298 143 LYS B CD 3570 C CE . LYS B 143 ? 1.7040 2.0722 0.8354 -0.0012 -0.4484 0.1281 143 LYS B CE 3571 N NZ . LYS B 143 ? 1.7003 2.0954 0.8722 0.0178 -0.4419 0.1760 143 LYS B NZ 3572 N N . CYS B 144 ? 1.6260 1.8735 0.7794 -0.0035 -0.4178 0.0242 144 CYS B N 3573 C CA . CYS B 144 ? 1.6074 1.8300 0.7820 -0.0020 -0.4091 0.0072 144 CYS B CA 3574 C C . CYS B 144 ? 1.5922 1.8426 0.8245 0.0031 -0.4133 0.0387 144 CYS B C 3575 O O . CYS B 144 ? 1.5739 1.8160 0.8397 0.0243 -0.3941 0.0614 144 CYS B O 3576 C CB . CYS B 144 ? 1.5856 1.7593 0.7536 0.0160 -0.3824 -0.0077 144 CYS B CB 3577 S SG . CYS B 144 ? 1.5719 1.7143 0.7573 0.0155 -0.3711 -0.0290 144 CYS B SG 3578 N N . ASP B 145 ? 1.6013 1.8832 0.8457 -0.0182 -0.4362 0.0403 145 ASP B N 3579 C CA . ASP B 145 ? 1.5889 1.9036 0.8951 -0.0159 -0.4426 0.0739 145 ASP B CA 3580 C C . ASP B 145 ? 1.5604 1.8396 0.8949 -0.0019 -0.4205 0.0627 145 ASP B C 3581 O O . ASP B 145 ? 1.5528 1.7874 0.8583 0.0025 -0.4046 0.0306 145 ASP B O 3582 C CB . ASP B 145 ? 1.6165 1.9798 0.9240 -0.0489 -0.4781 0.0806 145 ASP B CB 3583 C CG . ASP B 145 ? 1.6293 1.9677 0.9111 -0.0702 -0.4830 0.0380 145 ASP B CG 3584 O OD1 . ASP B 145 ? 1.6267 1.9158 0.8750 -0.0637 -0.4635 0.0009 145 ASP B OD1 3585 O OD2 . ASP B 145 ? 1.6425 2.0126 0.9424 -0.0947 -0.5060 0.0444 145 ASP B OD2 3586 N N . ASP B 146 ? 1.5464 1.8489 0.9405 0.0041 -0.4192 0.0932 146 ASP B N 3587 C CA . ASP B 146 ? 1.5251 1.7972 0.9476 0.0166 -0.3967 0.0868 146 ASP B CA 3588 C C . ASP B 146 ? 1.5240 1.7740 0.9215 0.0008 -0.4034 0.0478 146 ASP B C 3589 O O . ASP B 146 ? 1.5094 1.7199 0.9014 0.0107 -0.3820 0.0302 146 ASP B O 3590 C CB . ASP B 146 ? 1.5195 1.8271 1.0151 0.0225 -0.3964 0.1286 146 ASP B CB 3591 C CG . ASP B 146 ? 1.5184 1.8339 1.0540 0.0460 -0.3738 0.1695 146 ASP B CG 3592 O OD1 . ASP B 146 ? 1.5166 1.7999 1.0208 0.0591 -0.3538 0.1607 146 ASP B OD1 3593 O OD2 . ASP B 146 ? 1.5200 1.8737 1.1237 0.0513 -0.3742 0.2129 146 ASP B OD2 3594 N N . ASP B 147 ? 1.5419 1.8167 0.9235 -0.0260 -0.4316 0.0356 147 ASP B N 3595 C CA . ASP B 147 ? 1.5486 1.7986 0.9069 -0.0425 -0.4340 -0.0030 147 ASP B CA 3596 C C . ASP B 147 ? 1.5428 1.7472 0.8548 -0.0342 -0.4152 -0.0335 147 ASP B C 3597 O O . ASP B 147 ? 1.5296 1.7021 0.8430 -0.0305 -0.4004 -0.0530 147 ASP B O 3598 C CB . ASP B 147 ? 1.5854 1.8647 0.9233 -0.0777 -0.4642 -0.0136 147 ASP B CB 3599 C CG . ASP B 147 ? 1.5981 1.8549 0.9322 -0.0966 -0.4641 -0.0471 147 ASP B CG 3600 O OD1 . ASP B 147 ? 1.5869 1.7998 0.9079 -0.0862 -0.4417 -0.0735 147 ASP B OD1 3601 O OD2 . ASP B 147 ? 1.6230 1.9081 0.9710 -0.1236 -0.4867 -0.0443 147 ASP B OD2 3602 N N . CYS B 148 ? 1.5535 1.7592 0.8300 -0.0318 -0.4163 -0.0326 148 CYS B N 3603 C CA . CYS B 148 ? 1.5525 1.7211 0.7894 -0.0240 -0.3999 -0.0550 148 CYS B CA 3604 C C . CYS B 148 ? 1.5203 1.6595 0.7694 -0.0013 -0.3759 -0.0480 148 CYS B C 3605 O O . CYS B 148 ? 1.5102 1.6190 0.7467 0.0009 -0.3630 -0.0657 148 CYS B O 3606 C CB . CYS B 148 ? 1.5790 1.7613 0.7790 -0.0270 -0.4077 -0.0505 148 CYS B CB 3607 S SG . CYS B 148 ? 1.5845 1.7290 0.7463 -0.0125 -0.3868 -0.0646 148 CYS B SG 3608 N N . MET B 149 ? 1.5021 1.6503 0.7764 0.0131 -0.3684 -0.0206 149 MET B N 3609 C CA . MET B 149 ? 1.4820 1.5978 0.7590 0.0290 -0.3429 -0.0160 149 MET B CA 3610 C C . MET B 149 ? 1.4665 1.5643 0.7590 0.0266 -0.3343 -0.0264 149 MET B C 3611 O O . MET B 149 ? 1.4619 1.5303 0.7360 0.0285 -0.3203 -0.0358 149 MET B O 3612 C CB . MET B 149 ? 1.4835 1.6077 0.7901 0.0434 -0.3298 0.0146 149 MET B CB 3613 C CG . MET B 149 ? 1.4923 1.6322 0.7898 0.0491 -0.3330 0.0310 149 MET B CG 3614 S SD . MET B 149 ? 1.4943 1.5951 0.7415 0.0544 -0.3175 0.0154 149 MET B SD 3615 C CE . MET B 149 ? 1.5041 1.6314 0.7603 0.0637 -0.3196 0.0445 149 MET B CE 3616 N N . ALA B 150 ? 1.4594 1.5784 0.7870 0.0205 -0.3443 -0.0214 150 ALA B N 3617 C CA . ALA B 150 ? 1.4459 1.5525 0.7942 0.0179 -0.3373 -0.0287 150 ALA B CA 3618 C C . ALA B 150 ? 1.4416 1.5299 0.7693 0.0086 -0.3388 -0.0540 150 ALA B C 3619 O O . ALA B 150 ? 1.4322 1.5021 0.7660 0.0100 -0.3267 -0.0566 150 ALA B O 3620 C CB . ALA B 150 ? 1.4462 1.5830 0.8387 0.0110 -0.3507 -0.0177 150 ALA B CB 3621 N N . SER B 151 ? 1.4483 1.5421 0.7537 -0.0017 -0.3512 -0.0698 151 SER B N 3622 C CA . SER B 151 ? 1.4468 1.5206 0.7390 -0.0088 -0.3463 -0.0919 151 SER B CA 3623 C C . SER B 151 ? 1.4300 1.4811 0.7034 0.0007 -0.3316 -0.0889 151 SER B C 3624 O O . SER B 151 ? 1.4255 1.4625 0.7087 -0.0010 -0.3227 -0.0936 151 SER B O 3625 C CB . SER B 151 ? 1.4724 1.5512 0.7376 -0.0227 -0.3564 -0.1106 151 SER B CB 3626 O OG . SER B 151 ? 1.4760 1.5535 0.7070 -0.0163 -0.3556 -0.1071 151 SER B OG 3627 N N . ILE B 152 ? 1.4229 1.4729 0.6733 0.0090 -0.3293 -0.0781 152 ILE B N 3628 C CA . ILE B 152 ? 1.4160 1.4460 0.6456 0.0135 -0.3177 -0.0731 152 ILE B CA 3629 C C . ILE B 152 ? 1.4055 1.4244 0.6478 0.0132 -0.3072 -0.0632 152 ILE B C 3630 O O . ILE B 152 ? 1.3946 1.4040 0.6359 0.0081 -0.3026 -0.0614 152 ILE B O 3631 C CB . ILE B 152 ? 1.4210 1.4493 0.6243 0.0206 -0.3156 -0.0642 152 ILE B CB 3632 C CG1 . ILE B 152 ? 1.4314 1.4709 0.6160 0.0192 -0.3254 -0.0724 152 ILE B CG1 3633 C CG2 . ILE B 152 ? 1.4213 1.4272 0.6024 0.0203 -0.3038 -0.0583 152 ILE B CG2 3634 C CD1 . ILE B 152 ? 1.4364 1.4811 0.6033 0.0268 -0.3251 -0.0601 152 ILE B CD1 3635 N N . ARG B 153 ? 1.4080 1.4303 0.6643 0.0175 -0.3024 -0.0539 153 ARG B N 3636 C CA . ARG B 153 ? 1.4126 1.4220 0.6756 0.0159 -0.2886 -0.0453 153 ARG B CA 3637 C C . ARG B 153 ? 1.4050 1.4190 0.6938 0.0091 -0.2914 -0.0475 153 ARG B C 3638 O O . ARG B 153 ? 1.4090 1.4127 0.6918 0.0029 -0.2828 -0.0400 153 ARG B O 3639 C CB . ARG B 153 ? 1.4181 1.4315 0.7020 0.0241 -0.2792 -0.0340 153 ARG B CB 3640 C CG . ARG B 153 ? 1.4314 1.4357 0.6987 0.0326 -0.2678 -0.0256 153 ARG B CG 3641 C CD . ARG B 153 ? 1.4438 1.4421 0.7364 0.0414 -0.2464 -0.0101 153 ARG B CD 3642 N NE . ARG B 153 ? 1.4336 1.4655 0.7765 0.0462 -0.2590 0.0011 153 ARG B NE 3643 C CZ . ARG B 153 ? 1.4340 1.4930 0.8043 0.0536 -0.2671 0.0175 153 ARG B CZ 3644 N NH1 . ARG B 153 ? 1.4436 1.4990 0.7990 0.0604 -0.2614 0.0250 153 ARG B NH1 3645 N NH2 . ARG B 153 ? 1.4254 1.5187 0.8412 0.0522 -0.2823 0.0299 153 ARG B NH2 3646 N N . ASN B 154 ? 1.4049 1.4343 0.7211 0.0077 -0.3028 -0.0568 154 ASN B N 3647 C CA . ASN B 154 ? 1.4010 1.4336 0.7506 0.0021 -0.3028 -0.0590 154 ASN B CA 3648 C C . ASN B 154 ? 1.3992 1.4262 0.7510 -0.0024 -0.3022 -0.0663 154 ASN B C 3649 O O . ASN B 154 ? 1.3955 1.4235 0.7815 -0.0062 -0.2991 -0.0682 154 ASN B O 3650 C CB . ASN B 154 ? 1.4066 1.4553 0.7890 -0.0003 -0.3120 -0.0653 154 ASN B CB 3651 C CG . ASN B 154 ? 1.4088 1.4673 0.8063 0.0058 -0.3096 -0.0504 154 ASN B CG 3652 O OD1 . ASN B 154 ? 1.4130 1.4594 0.7991 0.0116 -0.2948 -0.0382 154 ASN B OD1 3653 N ND2 . ASN B 154 ? 1.4137 1.4936 0.8372 0.0023 -0.3223 -0.0503 154 ASN B ND2 3654 N N . ASN B 155 ? 1.4040 1.4243 0.7251 -0.0010 -0.3022 -0.0682 155 ASN B N 3655 C CA . ASN B 155 ? 1.4058 1.4201 0.7330 -0.0031 -0.2971 -0.0693 155 ASN B CA 3656 C C . ASN B 155 ? 1.4227 1.4330 0.7658 -0.0057 -0.2946 -0.0904 155 ASN B C 3657 O O . ASN B 155 ? 1.4267 1.4287 0.7926 -0.0065 -0.2826 -0.0906 155 ASN B O 3658 C CB . ASN B 155 ? 1.3953 1.4122 0.7498 -0.0071 -0.2908 -0.0490 155 ASN B CB 3659 C CG . ASN B 155 ? 1.3946 1.4112 0.7469 -0.0093 -0.2871 -0.0338 155 ASN B CG 3660 O OD1 . ASN B 155 ? 1.3914 1.4157 0.7481 -0.0167 -0.2878 -0.0099 155 ASN B OD1 3661 N ND2 . ASN B 155 ? 1.4010 1.4109 0.7463 -0.0049 -0.2835 -0.0451 155 ASN B ND2 3662 N N . THR B 156 ? 1.4383 1.4542 0.7696 -0.0093 -0.3040 -0.1063 156 THR B N 3663 C CA . THR B 156 ? 1.4647 1.4738 0.7986 -0.0197 -0.3022 -0.1306 156 THR B CA 3664 C C . THR B 156 ? 1.4868 1.4949 0.7763 -0.0234 -0.3070 -0.1445 156 THR B C 3665 O O . THR B 156 ? 1.5189 1.5221 0.7949 -0.0375 -0.3079 -0.1668 156 THR B O 3666 C CB . THR B 156 ? 1.4717 1.4926 0.8259 -0.0296 -0.3129 -0.1375 156 THR B CB 3667 O OG1 . THR B 156 ? 1.4704 1.5127 0.8065 -0.0288 -0.3302 -0.1290 156 THR B OG1 3668 C CG2 . THR B 156 ? 1.4504 1.4734 0.8490 -0.0253 -0.3072 -0.1225 156 THR B CG2 3669 N N . TYR B 157 ? 1.4757 1.4871 0.7397 -0.0135 -0.3092 -0.1315 157 TYR B N 3670 C CA . TYR B 157 ? 1.4905 1.5048 0.7137 -0.0152 -0.3144 -0.1392 157 TYR B CA 3671 C C . TYR B 157 ? 1.5148 1.5080 0.7272 -0.0175 -0.2969 -0.1539 157 TYR B C 3672 O O . TYR B 157 ? 1.4993 1.4820 0.7267 -0.0085 -0.2834 -0.1423 157 TYR B O 3673 C CB . TYR B 157 ? 1.4700 1.4919 0.6754 -0.0032 -0.3192 -0.1189 157 TYR B CB 3674 C CG . TYR B 157 ? 1.4804 1.5053 0.6488 -0.0019 -0.3219 -0.1213 157 TYR B CG 3675 C CD1 . TYR B 157 ? 1.4932 1.5392 0.6438 -0.0060 -0.3368 -0.1192 157 TYR B CD1 3676 C CD2 . TYR B 157 ? 1.4805 1.4910 0.6362 0.0032 -0.3100 -0.1206 157 TYR B CD2 3677 C CE1 . TYR B 157 ? 1.5054 1.5573 0.6230 -0.0052 -0.3395 -0.1182 157 TYR B CE1 3678 C CE2 . TYR B 157 ? 1.4942 1.5077 0.6172 0.0051 -0.3111 -0.1215 157 TYR B CE2 3679 C CZ . TYR B 157 ? 1.5054 1.5390 0.6074 0.0008 -0.3258 -0.1211 157 TYR B CZ 3680 O OH . TYR B 157 ? 1.5145 1.5540 0.5848 0.0022 -0.3271 -0.1189 157 TYR B OH 3681 N N . ASP B 158 ? 1.5575 1.5449 0.7436 -0.0317 -0.2959 -0.1777 158 ASP B N 3682 C CA . ASP B 158 ? 1.5939 1.5551 0.7655 -0.0353 -0.2726 -0.1956 158 ASP B CA 3683 C C . ASP B 158 ? 1.6081 1.5750 0.7356 -0.0318 -0.2761 -0.1928 158 ASP B C 3684 O O . ASP B 158 ? 1.6289 1.6102 0.7175 -0.0444 -0.2913 -0.2014 158 ASP B O 3685 C CB . ASP B 158 ? 1.6454 1.5887 0.8054 -0.0583 -0.2640 -0.2282 158 ASP B CB 3686 C CG . ASP B 158 ? 1.6883 1.5933 0.8397 -0.0621 -0.2286 -0.2495 158 ASP B CG 3687 O OD1 . ASP B 158 ? 1.6753 1.5725 0.8369 -0.0448 -0.2123 -0.2348 158 ASP B OD1 3688 O OD2 . ASP B 158 ? 1.7410 1.6217 0.8761 -0.0841 -0.2148 -0.2810 158 ASP B OD2 3689 N N . HIS B 159 ? 1.5940 1.5532 0.7302 -0.0163 -0.2632 -0.1772 159 HIS B N 3690 C CA . HIS B 159 ? 1.6037 1.5683 0.7048 -0.0104 -0.2650 -0.1704 159 HIS B CA 3691 C C . HIS B 159 ? 1.6607 1.6093 0.7210 -0.0228 -0.2504 -0.1958 159 HIS B C 3692 O O . HIS B 159 ? 1.6725 1.6338 0.6925 -0.0251 -0.2599 -0.1945 159 HIS B O 3693 C CB . HIS B 159 ? 1.5773 1.5372 0.7018 0.0055 -0.2540 -0.1467 159 HIS B CB 3694 C CG . HIS B 159 ? 1.6002 1.5361 0.7425 0.0083 -0.2235 -0.1515 159 HIS B CG 3695 N ND1 . HIS B 159 ? 1.6108 1.5290 0.7940 0.0061 -0.2029 -0.1578 159 HIS B ND1 3696 C CD2 . HIS B 159 ? 1.6173 1.5432 0.7483 0.0146 -0.2061 -0.1481 159 HIS B CD2 3697 C CE1 . HIS B 159 ? 1.6334 1.5304 0.8326 0.0116 -0.1719 -0.1573 159 HIS B CE1 3698 N NE2 . HIS B 159 ? 1.6376 1.5392 0.8048 0.0168 -0.1735 -0.1516 159 HIS B NE2 3699 N N . SER B 160 ? 1.7010 1.6198 0.7712 -0.0319 -0.2245 -0.2185 160 SER B N 3700 C CA . SER B 160 ? 1.7695 1.6618 0.7968 -0.0465 -0.2011 -0.2472 160 SER B CA 3701 C C . SER B 160 ? 1.8212 1.7270 0.7891 -0.0738 -0.2225 -0.2683 160 SER B C 3702 O O . SER B 160 ? 1.8727 1.7681 0.7869 -0.0878 -0.2126 -0.2855 160 SER B O 3703 C CB . SER B 160 ? 1.7999 1.6501 0.8573 -0.0508 -0.1616 -0.2674 160 SER B CB 3704 O OG . SER B 160 ? 1.8004 1.6487 0.8766 -0.0646 -0.1694 -0.2806 160 SER B OG 3705 N N . LYS B 161 ? 1.8137 1.7453 0.7922 -0.0831 -0.2517 -0.2639 161 LYS B N 3706 C CA . LYS B 161 ? 1.8626 1.8172 0.7944 -0.1121 -0.2777 -0.2754 161 LYS B CA 3707 C C . LYS B 161 ? 1.8531 1.8445 0.7531 -0.1081 -0.3013 -0.2526 161 LYS B C 3708 O O . LYS B 161 ? 1.9053 1.9068 0.7493 -0.1325 -0.3097 -0.2637 161 LYS B O 3709 C CB . LYS B 161 ? 1.8482 1.8258 0.8132 -0.1199 -0.3027 -0.2683 161 LYS B CB 3710 C CG . LYS B 161 ? 1.8704 1.8147 0.8681 -0.1271 -0.2815 -0.2903 161 LYS B CG 3711 C CD . LYS B 161 ? 1.8765 1.8440 0.8922 -0.1451 -0.3076 -0.2895 161 LYS B CD 3712 C CE . LYS B 161 ? 1.8725 1.8123 0.9395 -0.1422 -0.2875 -0.3002 161 LYS B CE 3713 N NZ . LYS B 161 ? 1.8939 1.8478 0.9691 -0.1683 -0.3079 -0.3088 161 LYS B NZ 3714 N N . TYR B 162 ? 1.7904 1.8008 0.7250 -0.0798 -0.3106 -0.2203 162 TYR B N 3715 C CA . TYR B 162 ? 1.7779 1.8221 0.6953 -0.0722 -0.3300 -0.1941 162 TYR B CA 3716 C C . TYR B 162 ? 1.7702 1.7994 0.6723 -0.0555 -0.3109 -0.1887 162 TYR B C 3717 O O . TYR B 162 ? 1.7525 1.8055 0.6465 -0.0456 -0.3228 -0.1653 162 TYR B O 3718 C CB . TYR B 162 ? 1.7293 1.7986 0.6927 -0.0533 -0.3476 -0.1628 162 TYR B CB 3719 C CG . TYR B 162 ? 1.7309 1.8182 0.7207 -0.0650 -0.3653 -0.1610 162 TYR B CG 3720 C CD1 . TYR B 162 ? 1.7173 1.7838 0.7435 -0.0614 -0.3551 -0.1708 162 TYR B CD1 3721 C CD2 . TYR B 162 ? 1.7450 1.8746 0.7293 -0.0796 -0.3929 -0.1442 162 TYR B CD2 3722 C CE1 . TYR B 162 ? 1.7138 1.7972 0.7671 -0.0713 -0.3704 -0.1676 162 TYR B CE1 3723 C CE2 . TYR B 162 ? 1.7425 1.8918 0.7576 -0.0902 -0.4093 -0.1381 162 TYR B CE2 3724 C CZ . TYR B 162 ? 1.7273 1.8516 0.7754 -0.0856 -0.3973 -0.1516 162 TYR B CZ 3725 O OH . TYR B 162 ? 1.7269 1.8709 0.8081 -0.0956 -0.4126 -0.1444 162 TYR B OH 3726 N N . ARG B 163 ? 1.7835 1.7741 0.6875 -0.0520 -0.2795 -0.2072 163 ARG B N 3727 C CA . ARG B 163 ? 1.7750 1.7524 0.6803 -0.0329 -0.2601 -0.1959 163 ARG B CA 3728 C C . ARG B 163 ? 1.8110 1.8001 0.6633 -0.0399 -0.2621 -0.1953 163 ARG B C 3729 O O . ARG B 163 ? 1.7852 1.7930 0.6406 -0.0244 -0.2709 -0.1699 163 ARG B O 3730 C CB . ARG B 163 ? 1.7911 1.7274 0.7179 -0.0282 -0.2225 -0.2111 163 ARG B CB 3731 C CG . ARG B 163 ? 1.7757 1.7037 0.7166 -0.0079 -0.2038 -0.1920 163 ARG B CG 3732 C CD . ARG B 163 ? 1.7812 1.6763 0.7648 0.0009 -0.1670 -0.1943 163 ARG B CD 3733 N NE . ARG B 163 ? 1.7492 1.6499 0.7665 0.0213 -0.1605 -0.1625 163 ARG B NE 3734 C CZ . ARG B 163 ? 1.7517 1.6333 0.8139 0.0321 -0.1291 -0.1510 163 ARG B CZ 3735 N NH1 . ARG B 163 ? 1.7885 1.6382 0.8703 0.0274 -0.0955 -0.1702 163 ARG B NH1 3736 N NH2 . ARG B 163 ? 1.7196 1.6141 0.8113 0.0466 -0.1301 -0.1176 163 ARG B NH2 3737 N N . GLU B 164 ? 1.8787 1.8553 0.6803 -0.0656 -0.2527 -0.2236 164 GLU B N 3738 C CA . GLU B 164 ? 1.9259 1.9103 0.6692 -0.0764 -0.2502 -0.2256 164 GLU B CA 3739 C C . GLU B 164 ? 1.8992 1.9355 0.6353 -0.0741 -0.2866 -0.1930 164 GLU B C 3740 O O . GLU B 164 ? 1.8880 1.9351 0.6166 -0.0600 -0.2845 -0.1733 164 GLU B O 3741 C CB . GLU B 164 ? 2.0157 1.9795 0.6951 -0.1140 -0.2382 -0.2641 164 GLU B CB 3742 C CG . GLU B 164 ? 2.0570 1.9609 0.7404 -0.1169 -0.1911 -0.2983 164 GLU B CG 3743 C CD . GLU B 164 ? 2.0651 1.9401 0.7537 -0.0953 -0.1522 -0.2943 164 GLU B CD 3744 O OE1 . GLU B 164 ? 2.0005 1.8826 0.7483 -0.0629 -0.1511 -0.2648 164 GLU B OE1 3745 O OE2 . GLU B 164 ? 2.1410 1.9854 0.7735 -0.1130 -0.1215 -0.3204 164 GLU B OE2 3746 N N . GLU B 165 ? 1.8860 1.9548 0.6320 -0.0868 -0.3175 -0.1842 165 GLU B N 3747 C CA . GLU B 165 ? 1.8648 1.9857 0.6174 -0.0839 -0.3495 -0.1474 165 GLU B CA 3748 C C . GLU B 165 ? 1.8022 1.9281 0.6053 -0.0485 -0.3483 -0.1158 165 GLU B C 3749 O O . GLU B 165 ? 1.7946 1.9478 0.5958 -0.0399 -0.3576 -0.0879 165 GLU B O 3750 C CB . GLU B 165 ? 1.8681 2.0244 0.6324 -0.1044 -0.3806 -0.1395 165 GLU B CB 3751 C CG . GLU B 165 ? 1.8482 1.9820 0.6498 -0.1041 -0.3763 -0.1571 165 GLU B CG 3752 C CD . GLU B 165 ? 1.8430 2.0174 0.6683 -0.1193 -0.4078 -0.1402 165 GLU B CD 3753 O OE1 . GLU B 165 ? 1.8152 2.0327 0.6671 -0.1095 -0.4284 -0.1011 165 GLU B OE1 3754 O OE2 . GLU B 165 ? 1.8662 2.0287 0.6890 -0.1406 -0.4097 -0.1640 165 GLU B OE2 3755 N N . ALA B 166 ? 1.7608 1.8602 0.6072 -0.0310 -0.3361 -0.1197 166 ALA B N 3756 C CA . ALA B 166 ? 1.7102 1.8068 0.5956 -0.0041 -0.3325 -0.0951 166 ALA B CA 3757 C C . ALA B 166 ? 1.7145 1.7932 0.5872 0.0083 -0.3132 -0.0922 166 ALA B C 3758 O O . ALA B 166 ? 1.6942 1.7843 0.5752 0.0220 -0.3159 -0.0679 166 ALA B O 3759 C CB . ALA B 166 ? 1.6754 1.7508 0.6019 0.0042 -0.3265 -0.1001 166 ALA B CB 3760 N N . MET B 167 ? 1.7422 1.7913 0.6001 0.0036 -0.2907 -0.1156 167 MET B N 3761 C CA . MET B 167 ? 1.7553 1.7876 0.6032 0.0139 -0.2687 -0.1127 167 MET B CA 3762 C C . MET B 167 ? 1.7832 1.8394 0.5937 0.0115 -0.2758 -0.0994 167 MET B C 3763 O O . MET B 167 ? 1.7603 1.8208 0.5817 0.0274 -0.2726 -0.0776 167 MET B O 3764 C CB . MET B 167 ? 1.7965 1.7942 0.6303 0.0053 -0.2388 -0.1413 167 MET B CB 3765 C CG . MET B 167 ? 1.7696 1.7417 0.6539 0.0156 -0.2217 -0.1429 167 MET B CG 3766 S SD . MET B 167 ? 1.7398 1.7039 0.6600 0.0380 -0.2049 -0.1148 167 MET B SD 3767 C CE . MET B 167 ? 1.7338 1.6697 0.7075 0.0417 -0.1781 -0.1189 167 MET B CE 3768 N N . GLN B 168 ? 1.8319 1.9053 0.5978 -0.0112 -0.2863 -0.1113 168 GLN B N 3769 C CA . GLN B 168 ? 1.8674 1.9700 0.5932 -0.0186 -0.2955 -0.0964 168 GLN B CA 3770 C C . GLN B 168 ? 1.8234 1.9624 0.5825 -0.0027 -0.3173 -0.0566 168 GLN B C 3771 O O . GLN B 168 ? 1.8268 1.9788 0.5799 0.0073 -0.3148 -0.0352 168 GLN B O 3772 C CB . GLN B 168 ? 1.9338 2.0546 0.6049 -0.0535 -0.3093 -0.1134 168 GLN B CB 3773 C CG . GLN B 168 ? 1.9985 2.0764 0.6248 -0.0745 -0.2811 -0.1570 168 GLN B CG 3774 C CD . GLN B 168 ? 2.0665 2.1335 0.6317 -0.0853 -0.2594 -0.1668 168 GLN B CD 3775 O OE1 . GLN B 168 ? 2.0942 2.1175 0.6570 -0.0757 -0.2211 -0.1848 168 GLN B OE1 3776 N NE2 . GLN B 168 ? 2.1011 2.2095 0.6192 -0.1061 -0.2824 -0.1519 168 GLN B NE2 3777 N N . ASN B 169 ? 1.7854 1.9377 0.5829 0.0003 -0.3344 -0.0464 169 ASN B N 3778 C CA . ASN B 169 ? 1.7501 1.9309 0.5856 0.0153 -0.3484 -0.0094 169 ASN B CA 3779 C C . ASN B 169 ? 1.7119 1.8685 0.5809 0.0403 -0.3327 0.0033 169 ASN B C 3780 O O . ASN B 169 ? 1.6893 1.8593 0.5899 0.0528 -0.3369 0.0309 169 ASN B O 3781 C CB . ASN B 169 ? 1.7316 1.9304 0.5998 0.0104 -0.3660 -0.0025 169 ASN B CB 3782 C CG . ASN B 169 ? 1.7721 2.0097 0.6132 -0.0175 -0.3895 -0.0014 169 ASN B CG 3783 O OD1 . ASN B 169 ? 1.8120 2.0712 0.6088 -0.0338 -0.3960 0.0017 169 ASN B OD1 3784 N ND2 . ASN B 169 ? 1.7618 2.0101 0.6279 -0.0261 -0.4031 -0.0026 169 ASN B ND2 3785 N N . ARG B 170 ? 1.7080 1.8290 0.5726 0.0454 -0.3134 -0.0148 170 ARG B N 3786 C CA . ARG B 170 ? 1.6775 1.7782 0.5663 0.0624 -0.3008 -0.0019 170 ARG B CA 3787 C C . ARG B 170 ? 1.6781 1.7984 0.5721 0.0726 -0.3034 0.0280 170 ARG B C 3788 O O . ARG B 170 ? 1.6649 1.7693 0.5752 0.0836 -0.2934 0.0398 170 ARG B O 3789 C CB . ARG B 170 ? 1.6831 1.7576 0.5617 0.0638 -0.2807 -0.0158 170 ARG B CB 3790 C CG . ARG B 170 ? 1.7211 1.8021 0.5587 0.0581 -0.2711 -0.0218 170 ARG B CG 3791 C CD . ARG B 170 ? 1.7177 1.8044 0.5548 0.0704 -0.2636 0.0013 170 ARG B CD 3792 N NE . ARG B 170 ? 1.7546 1.8621 0.5475 0.0624 -0.2631 0.0033 170 ARG B NE 3793 C CZ . ARG B 170 ? 1.7582 1.9008 0.5436 0.0624 -0.2786 0.0279 170 ARG B CZ 3794 N NH1 . ARG B 170 ? 1.7238 1.8808 0.5474 0.0727 -0.2916 0.0524 170 ARG B NH1 3795 N NH2 . ARG B 170 ? 1.8011 1.9640 0.5407 0.0509 -0.2783 0.0297 170 ARG B NH2 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ASP 1 1 1 ASP ASP A . n A 1 2 LYS 2 2 2 LYS LYS A . n A 1 3 ILE 3 3 3 ILE ILE A . n A 1 4 CYS 4 4 4 CYS CYS A . n A 1 5 LEU 5 5 5 LEU LEU A . n A 1 6 GLY 6 6 6 GLY GLY A . n A 1 7 HIS 7 7 7 HIS HIS A . n A 1 8 HIS 8 8 8 HIS HIS A . n A 1 9 ALA 9 9 9 ALA ALA A . n A 1 10 LEU 10 10 10 LEU LEU A . n A 1 11 SER 11 11 11 SER SER A . n A 1 12 ASN 12 12 12 ASN ASN A . n A 1 13 GLY 13 13 13 GLY GLY A . n A 1 14 THR 14 14 14 THR THR A . n A 1 15 LYS 15 15 15 LYS LYS A . n A 1 16 VAL 16 16 16 VAL VAL A . n A 1 17 ASN 17 17 17 ASN ASN A . n A 1 18 THR 18 18 18 THR THR A . n A 1 19 LEU 19 19 19 LEU LEU A . n A 1 20 THR 20 20 20 THR THR A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 GLY 23 23 23 GLY GLY A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 GLU 25 25 25 GLU GLU A . n A 1 26 VAL 26 26 26 VAL VAL A . n A 1 27 VAL 27 27 27 VAL VAL A . n A 1 28 ASN 28 28 28 ASN ASN A . n A 1 29 ALA 29 29 29 ALA ALA A . n A 1 30 THR 30 30 30 THR THR A . n A 1 31 GLU 31 31 31 GLU GLU A . n A 1 32 THR 32 32 32 THR THR A . n A 1 33 VAL 33 33 33 VAL VAL A . n A 1 34 GLU 34 34 34 GLU GLU A . n A 1 35 ARG 35 35 35 ARG ARG A . n A 1 36 THR 36 36 36 THR THR A . n A 1 37 ASN 37 37 37 ASN ASN A . n A 1 38 ILE 38 38 38 ILE ILE A . n A 1 39 PRO 39 39 39 PRO PRO A . n A 1 40 ARG 40 40 40 ARG ARG A . n A 1 41 ILE 41 41 41 ILE ILE A . n A 1 42 CYS 42 42 42 CYS CYS A . n A 1 43 SER 43 43 43 SER SER A . n A 1 44 LYS 44 44 44 LYS LYS A . n A 1 45 GLY 45 45 45 GLY GLY A . n A 1 46 LYS 46 46 46 LYS LYS A . n A 1 47 ARG 47 47 47 ARG ARG A . n A 1 48 THR 48 48 48 THR THR A . n A 1 49 VAL 49 49 49 VAL VAL A . n A 1 50 ASP 50 50 50 ASP ASP A . n A 1 51 LEU 51 51 51 LEU LEU A . n A 1 52 GLY 52 52 52 GLY GLY A . n A 1 53 GLN 53 53 53 GLN GLN A . n A 1 54 CYS 54 54 54 CYS CYS A . n A 1 55 GLY 55 55 55 GLY GLY A . n A 1 56 LEU 56 56 56 LEU LEU A . n A 1 57 LEU 57 57 57 LEU LEU A . n A 1 58 GLY 58 58 58 GLY GLY A . n A 1 59 THR 59 59 59 THR THR A . n A 1 60 ILE 60 60 60 ILE ILE A . n A 1 61 THR 61 61 61 THR THR A . n A 1 62 GLY 62 62 62 GLY GLY A . n A 1 63 PRO 63 63 63 PRO PRO A . n A 1 64 PRO 64 64 64 PRO PRO A . n A 1 65 GLN 65 65 65 GLN GLN A . n A 1 66 CYS 66 66 66 CYS CYS A . n A 1 67 ASP 67 67 67 ASP ASP A . n A 1 68 GLN 68 68 68 GLN GLN A . n A 1 69 PHE 69 69 69 PHE PHE A . n A 1 70 LEU 70 70 70 LEU LEU A . n A 1 71 GLU 71 71 71 GLU GLU A . n A 1 72 PHE 72 72 72 PHE PHE A . n A 1 73 SER 73 73 73 SER SER A . n A 1 74 ALA 74 74 74 ALA ALA A . n A 1 75 ASP 75 75 75 ASP ASP A . n A 1 76 LEU 76 76 76 LEU LEU A . n A 1 77 ILE 77 77 77 ILE ILE A . n A 1 78 ILE 78 78 78 ILE ILE A . n A 1 79 GLU 79 79 79 GLU GLU A . n A 1 80 ARG 80 80 80 ARG ARG A . n A 1 81 ARG 81 81 81 ARG ARG A . n A 1 82 GLU 82 82 82 GLU GLU A . n A 1 83 GLY 83 83 83 GLY GLY A . n A 1 84 SER 84 84 84 SER SER A . n A 1 85 ASP 85 85 85 ASP ASP A . n A 1 86 VAL 86 86 86 VAL VAL A . n A 1 87 CYS 87 87 87 CYS CYS A . n A 1 88 TYR 88 88 88 TYR TYR A . n A 1 89 PRO 89 89 89 PRO PRO A . n A 1 90 GLY 90 90 90 GLY GLY A . n A 1 91 LYS 91 91 91 LYS LYS A . n A 1 92 PHE 92 92 92 PHE PHE A . n A 1 93 VAL 93 93 93 VAL VAL A . n A 1 94 ASN 94 94 94 ASN ASN A . n A 1 95 GLU 95 95 95 GLU GLU A . n A 1 96 GLU 96 96 96 GLU GLU A . n A 1 97 ALA 97 97 97 ALA ALA A . n A 1 98 LEU 98 98 98 LEU LEU A . n A 1 99 ARG 99 99 99 ARG ARG A . n A 1 100 GLN 100 100 100 GLN GLN A . n A 1 101 ILE 101 101 101 ILE ILE A . n A 1 102 LEU 102 102 102 LEU LEU A . n A 1 103 ARG 103 103 103 ARG ARG A . n A 1 104 GLU 104 104 104 GLU GLU A . n A 1 105 SER 105 105 105 SER SER A . n A 1 106 GLY 106 106 106 GLY GLY A . n A 1 107 GLY 107 107 107 GLY GLY A . n A 1 108 ILE 108 108 108 ILE ILE A . n A 1 109 ASP 109 109 109 ASP ASP A . n A 1 110 LYS 110 110 110 LYS LYS A . n A 1 111 GLU 111 111 111 GLU GLU A . n A 1 112 ALA 112 112 112 ALA ALA A . n A 1 113 MET 113 113 113 MET MET A . n A 1 114 GLY 114 114 114 GLY GLY A . n A 1 115 PHE 115 115 115 PHE PHE A . n A 1 116 THR 116 116 116 THR THR A . n A 1 117 TYR 117 117 117 TYR TYR A . n A 1 118 SER 118 118 118 SER SER A . n A 1 119 GLY 119 119 119 GLY GLY A . n A 1 120 ILE 120 120 120 ILE ILE A . n A 1 121 ARG 121 121 121 ARG ARG A . n A 1 122 THR 122 122 122 THR THR A . n A 1 123 ASN 123 123 123 ASN ASN A . n A 1 124 GLY 124 124 124 GLY GLY A . n A 1 125 THR 125 125 125 THR THR A . n A 1 126 THR 126 126 126 THR THR A . n A 1 127 SER 127 127 127 SER SER A . n A 1 128 ALA 128 128 128 ALA ALA A . n A 1 129 CYS 129 129 129 CYS CYS A . n A 1 130 ARG 130 130 130 ARG ARG A . n A 1 131 ARG 131 131 131 ARG ARG A . n A 1 132 SER 132 132 132 SER SER A . n A 1 133 GLY 133 133 133 GLY GLY A . n A 1 134 SER 134 134 134 SER SER A . n A 1 135 SER 135 135 135 SER SER A . n A 1 136 PHE 136 136 136 PHE PHE A . n A 1 137 TYR 137 137 137 TYR TYR A . n A 1 138 ALA 138 138 138 ALA ALA A . n A 1 139 GLU 139 139 139 GLU GLU A . n A 1 140 MET 140 140 140 MET MET A . n A 1 141 LYS 141 141 141 LYS LYS A . n A 1 142 TRP 142 142 142 TRP TRP A . n A 1 143 LEU 143 143 143 LEU LEU A . n A 1 144 LEU 144 144 144 LEU LEU A . n A 1 145 SER 145 145 145 SER SER A . n A 1 146 ASN 146 146 146 ASN ASN A . n A 1 147 THR 147 147 147 THR THR A . n A 1 148 ASP 148 148 148 ASP ASP A . n A 1 149 ASN 149 149 149 ASN ASN A . n A 1 150 ALA 150 150 150 ALA ALA A . n A 1 151 ALA 151 151 151 ALA ALA A . n A 1 152 PHE 152 152 152 PHE PHE A . n A 1 153 PRO 153 153 153 PRO PRO A . n A 1 154 GLN 154 154 154 GLN GLN A . n A 1 155 MET 155 155 155 MET MET A . n A 1 156 THR 156 156 156 THR THR A . n A 1 157 LYS 157 157 157 LYS LYS A . n A 1 158 SER 158 158 158 SER SER A . n A 1 159 TYR 159 159 159 TYR TYR A . n A 1 160 LYS 160 160 160 LYS LYS A . n A 1 161 ASN 161 161 161 ASN ASN A . n A 1 162 THR 162 162 162 THR THR A . n A 1 163 ARG 163 163 163 ARG ARG A . n A 1 164 LYS 164 164 164 LYS LYS A . n A 1 165 SER 165 165 165 SER SER A . n A 1 166 PRO 166 166 166 PRO PRO A . n A 1 167 ALA 167 167 167 ALA ALA A . n A 1 168 LEU 168 168 168 LEU LEU A . n A 1 169 ILE 169 169 169 ILE ILE A . n A 1 170 VAL 170 170 170 VAL VAL A . n A 1 171 TRP 171 171 171 TRP TRP A . n A 1 172 GLY 172 172 172 GLY GLY A . n A 1 173 ILE 173 173 173 ILE ILE A . n A 1 174 HIS 174 174 174 HIS HIS A . n A 1 175 HIS 175 175 175 HIS HIS A . n A 1 176 SER 176 176 176 SER SER A . n A 1 177 VAL 177 177 177 VAL VAL A . n A 1 178 SER 178 178 178 SER SER A . n A 1 179 THR 179 179 179 THR THR A . n A 1 180 ALA 180 180 180 ALA ALA A . n A 1 181 GLU 181 181 181 GLU GLU A . n A 1 182 GLN 182 182 182 GLN GLN A . n A 1 183 THR 183 183 183 THR THR A . n A 1 184 LYS 184 184 184 LYS LYS A . n A 1 185 LEU 185 185 185 LEU LEU A . n A 1 186 TYR 186 186 186 TYR TYR A . n A 1 187 GLY 187 187 187 GLY GLY A . n A 1 188 SER 188 188 188 SER SER A . n A 1 189 GLY 189 189 189 GLY GLY A . n A 1 190 ASN 190 190 190 ASN ASN A . n A 1 191 LYS 191 191 191 LYS LYS A . n A 1 192 LEU 192 192 192 LEU LEU A . n A 1 193 VAL 193 193 193 VAL VAL A . n A 1 194 THR 194 194 194 THR THR A . n A 1 195 VAL 195 195 195 VAL VAL A . n A 1 196 GLY 196 196 196 GLY GLY A . n A 1 197 SER 197 197 197 SER SER A . n A 1 198 SER 198 198 198 SER SER A . n A 1 199 ASN 199 199 199 ASN ASN A . n A 1 200 TYR 200 200 200 TYR TYR A . n A 1 201 GLN 201 201 201 GLN GLN A . n A 1 202 GLN 202 202 202 GLN GLN A . n A 1 203 SER 203 203 203 SER SER A . n A 1 204 PHE 204 204 204 PHE PHE A . n A 1 205 VAL 205 205 205 VAL VAL A . n A 1 206 PRO 206 206 206 PRO PRO A . n A 1 207 SER 207 207 207 SER SER A . n A 1 208 PRO 208 208 208 PRO PRO A . n A 1 209 GLY 209 209 209 GLY GLY A . n A 1 210 ALA 210 210 210 ALA ALA A . n A 1 211 ARG 211 211 211 ARG ARG A . n A 1 212 PRO 212 212 212 PRO PRO A . n A 1 213 GLN 213 213 213 GLN GLN A . n A 1 214 VAL 214 214 214 VAL VAL A . n A 1 215 ASN 215 215 215 ASN ASN A . n A 1 216 GLY 216 216 216 GLY GLY A . n A 1 217 LEU 217 217 217 LEU LEU A . n A 1 218 SER 218 218 218 SER SER A . n A 1 219 GLY 219 219 219 GLY GLY A . n A 1 220 ARG 220 220 220 ARG ARG A . n A 1 221 ILE 221 221 221 ILE ILE A . n A 1 222 ASP 222 222 222 ASP ASP A . n A 1 223 PHE 223 223 223 PHE PHE A . n A 1 224 HIS 224 224 224 HIS HIS A . n A 1 225 TRP 225 225 225 TRP TRP A . n A 1 226 LEU 226 226 226 LEU LEU A . n A 1 227 MET 227 227 227 MET MET A . n A 1 228 LEU 228 228 228 LEU LEU A . n A 1 229 ASN 229 229 229 ASN ASN A . n A 1 230 PRO 230 230 230 PRO PRO A . n A 1 231 ASN 231 231 231 ASN ASN A . n A 1 232 ASP 232 232 232 ASP ASP A . n A 1 233 THR 233 233 233 THR THR A . n A 1 234 VAL 234 234 234 VAL VAL A . n A 1 235 THR 235 235 235 THR THR A . n A 1 236 PHE 236 236 236 PHE PHE A . n A 1 237 SER 237 237 237 SER SER A . n A 1 238 PHE 238 238 238 PHE PHE A . n A 1 239 ASN 239 239 239 ASN ASN A . n A 1 240 GLY 240 240 240 GLY GLY A . n A 1 241 ALA 241 241 241 ALA ALA A . n A 1 242 PHE 242 242 242 PHE PHE A . n A 1 243 ILE 243 243 243 ILE ILE A . n A 1 244 ALA 244 244 244 ALA ALA A . n A 1 245 PRO 245 245 245 PRO PRO A . n A 1 246 ASP 246 246 246 ASP ASP A . n A 1 247 ARG 247 247 247 ARG ARG A . n A 1 248 ALA 248 248 248 ALA ALA A . n A 1 249 SER 249 249 249 SER SER A . n A 1 250 PHE 250 250 250 PHE PHE A . n A 1 251 LEU 251 251 251 LEU LEU A . n A 1 252 ARG 252 252 252 ARG ARG A . n A 1 253 GLY 253 253 253 GLY GLY A . n A 1 254 LYS 254 254 254 LYS LYS A . n A 1 255 SER 255 255 255 SER SER A . n A 1 256 MET 256 256 256 MET MET A . n A 1 257 GLY 257 257 257 GLY GLY A . n A 1 258 ILE 258 258 258 ILE ILE A . n A 1 259 GLN 259 259 259 GLN GLN A . n A 1 260 SER 260 260 260 SER SER A . n A 1 261 GLY 261 261 261 GLY GLY A . n A 1 262 VAL 262 262 262 VAL VAL A . n A 1 263 GLN 263 263 263 GLN GLN A . n A 1 264 VAL 264 264 264 VAL VAL A . n A 1 265 ASP 265 265 265 ASP ASP A . n A 1 266 ALA 266 266 266 ALA ALA A . n A 1 267 ASN 267 267 267 ASN ASN A . n A 1 268 CYS 268 268 268 CYS CYS A . n A 1 269 GLU 269 269 269 GLU GLU A . n A 1 270 GLY 270 270 270 GLY GLY A . n A 1 271 ASP 271 271 271 ASP ASP A . n A 1 272 CYS 272 272 272 CYS CYS A . n A 1 273 TYR 273 273 273 TYR TYR A . n A 1 274 HIS 274 274 274 HIS HIS A . n A 1 275 SER 275 275 275 SER SER A . n A 1 276 GLY 276 276 276 GLY GLY A . n A 1 277 GLY 277 277 277 GLY GLY A . n A 1 278 THR 278 278 278 THR THR A . n A 1 279 ILE 279 279 279 ILE ILE A . n A 1 280 ILE 280 280 280 ILE ILE A . n A 1 281 SER 281 281 281 SER SER A . n A 1 282 ASN 282 282 282 ASN ASN A . n A 1 283 LEU 283 283 283 LEU LEU A . n A 1 284 PRO 284 284 284 PRO PRO A . n A 1 285 PHE 285 285 285 PHE PHE A . n A 1 286 GLN 286 286 286 GLN GLN A . n A 1 287 ASN 287 287 287 ASN ASN A . n A 1 288 ILE 288 288 288 ILE ILE A . n A 1 289 ASP 289 289 289 ASP ASP A . n A 1 290 SER 290 290 290 SER SER A . n A 1 291 ARG 291 291 291 ARG ARG A . n A 1 292 ALA 292 292 292 ALA ALA A . n A 1 293 VAL 293 293 293 VAL VAL A . n A 1 294 GLY 294 294 294 GLY GLY A . n A 1 295 LYS 295 295 295 LYS LYS A . n A 1 296 CYS 296 296 296 CYS CYS A . n A 1 297 PRO 297 297 297 PRO PRO A . n A 1 298 ARG 298 298 298 ARG ARG A . n A 1 299 TYR 299 299 299 TYR TYR A . n A 1 300 VAL 300 300 300 VAL VAL A . n A 1 301 LYS 301 301 301 LYS LYS A . n A 1 302 GLN 302 302 302 GLN GLN A . n A 1 303 ARG 303 303 303 ARG ARG A . n A 1 304 SER 304 304 304 SER SER A . n A 1 305 LEU 305 305 305 LEU LEU A . n A 1 306 LEU 306 306 306 LEU LEU A . n A 1 307 LEU 307 307 307 LEU LEU A . n A 1 308 ALA 308 308 308 ALA ALA A . n A 1 309 THR 309 309 309 THR THR A . n A 1 310 GLY 310 310 310 GLY GLY A . n A 1 311 MET 311 311 311 MET MET A . n A 1 312 LYS 312 312 312 LYS LYS A . n A 1 313 ASN 313 313 313 ASN ASN A . n A 1 314 VAL 314 314 314 VAL VAL A . n A 1 315 PRO 315 315 315 PRO PRO A . n A 1 316 GLU 316 316 316 GLU GLU A . n A 1 317 ILE 317 317 317 ILE ILE A . n A 1 318 PRO 318 318 ? ? ? A . n A 1 319 LYS 319 319 ? ? ? A . n A 1 320 GLY 320 320 ? ? ? A . n A 1 321 ARG 321 321 ? ? ? 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 ASN 12 12 12 ASN ASN 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 GLU 15 15 15 GLU GLU B . n B 2 16 GLY 16 16 16 GLY GLY B . n B 2 17 LEU 17 17 17 LEU LEU B . n B 2 18 ILE 18 18 18 ILE ILE 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 PHE 24 24 24 PHE PHE B . n B 2 25 ARG 25 25 25 ARG ARG B . n B 2 26 HIS 26 26 26 HIS HIS B . n B 2 27 GLN 27 27 27 GLN GLN B . n B 2 28 ASN 28 28 28 ASN ASN B . n B 2 29 ALA 29 29 29 ALA ALA 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 GLU 32 32 32 GLU GLU B . n B 2 33 GLY 33 33 33 GLY GLY B . n B 2 34 THR 34 34 34 THR THR 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 TYR 38 38 38 TYR TYR B . n B 2 39 LYS 39 39 39 LYS LYS 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 SER 43 43 43 SER SER B . n B 2 44 ALA 44 44 44 ALA ALA B . n B 2 45 ILE 45 45 45 ILE ILE B . n B 2 46 ASP 46 46 46 ASP ASP B . n B 2 47 GLN 47 47 47 GLN GLN 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 GLY 50 50 50 GLY GLY B . n B 2 51 LYS 51 51 51 LYS LYS B . n B 2 52 LEU 52 52 52 LEU LEU B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 ARG 54 54 54 ARG ARG B . n B 2 55 LEU 55 55 55 LEU LEU 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 THR 59 59 59 THR THR B . n B 2 60 ASN 60 60 60 ASN ASN B . n B 2 61 GLN 61 61 61 GLN GLN 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 LEU 65 65 65 LEU LEU B . n B 2 66 ILE 66 66 66 ILE ILE B . n B 2 67 ASP 67 67 67 ASP ASP B . n B 2 68 ASN 68 68 68 ASN ASN B . n B 2 69 GLU 69 69 69 GLU GLU B . n B 2 70 PHE 70 70 70 PHE PHE B . n B 2 71 ASN 71 71 71 ASN ASN B . n B 2 72 GLU 72 72 72 GLU GLU B . n B 2 73 VAL 73 73 73 VAL VAL B . n B 2 74 GLU 74 74 74 GLU GLU B . n B 2 75 LYS 75 75 75 LYS LYS B . n B 2 76 GLN 76 76 76 GLN GLN B . n B 2 77 ILE 77 77 77 ILE ILE B . n B 2 78 GLY 78 78 78 GLY GLY B . n B 2 79 ASN 79 79 79 ASN ASN B . n B 2 80 VAL 80 80 80 VAL VAL B . n B 2 81 ILE 81 81 81 ILE ILE B . n B 2 82 ASN 82 82 82 ASN ASN B . n B 2 83 TRP 83 83 83 TRP TRP B . n B 2 84 THR 84 84 84 THR THR B . n B 2 85 ARG 85 85 85 ARG ARG B . n B 2 86 ASP 86 86 86 ASP ASP B . n B 2 87 SER 87 87 87 SER SER B . n B 2 88 ILE 88 88 88 ILE ILE B . n B 2 89 THR 89 89 89 THR THR B . n B 2 90 GLU 90 90 90 GLU GLU 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 SER 93 93 93 SER SER 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 ALA 101 101 101 ALA ALA 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 GLN 105 105 105 GLN GLN B . n B 2 106 HIS 106 106 106 HIS HIS B . n B 2 107 THR 107 107 107 THR THR B . n B 2 108 ILE 108 108 108 ILE ILE B . n B 2 109 ASP 109 109 109 ASP ASP B . n B 2 110 LEU 110 110 110 LEU LEU B . n B 2 111 ALA 111 111 111 ALA ALA 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 GLU 114 114 114 GLU GLU B . n B 2 115 MET 115 115 115 MET MET B . n B 2 116 ASP 116 116 116 ASP ASP B . n B 2 117 LYS 117 117 117 LYS LYS 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 GLU 120 120 120 GLU GLU B . n B 2 121 ARG 121 121 121 ARG ARG B . n B 2 122 VAL 122 122 122 VAL VAL B . n B 2 123 LYS 123 123 123 LYS LYS B . n B 2 124 ARG 124 124 124 ARG ARG 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 GLU 128 128 128 GLU GLU B . n B 2 129 ASN 129 129 129 ASN ASN B . n B 2 130 ALA 130 130 130 ALA ALA B . n B 2 131 GLU 131 131 131 GLU GLU B . n B 2 132 GLU 132 132 132 GLU GLU B . n B 2 133 ASP 133 133 133 ASP ASP B . n B 2 134 GLY 134 134 134 GLY GLY B . n B 2 135 THR 135 135 135 THR THR 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 ILE 140 140 140 ILE ILE B . n B 2 141 PHE 141 141 141 PHE PHE 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 ASP 147 147 147 ASP ASP 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 ALA 150 150 150 ALA ALA B . n B 2 151 SER 151 151 151 SER SER B . n B 2 152 ILE 152 152 152 ILE ILE B . n B 2 153 ARG 153 153 153 ARG ARG B . n B 2 154 ASN 154 154 154 ASN ASN B . n B 2 155 ASN 155 155 155 ASN ASN 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 HIS 159 159 159 HIS HIS B . n B 2 160 SER 160 160 160 SER SER 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 ARG 163 163 163 ARG ARG 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 ALA 166 166 166 ALA ALA B . n B 2 167 MET 167 167 167 MET MET B . n B 2 168 GLN 168 168 168 GLN GLN 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 ILE 171 171 ? ? ? B . n B 2 172 GLN 172 172 ? ? ? B . n B 2 173 ILE 173 173 ? ? ? B . n B 2 174 ASP 174 174 ? ? ? B . n B 2 175 PRO 175 175 ? ? ? B . n B 2 176 VAL 176 176 ? ? ? B . n B 2 177 LYS 177 177 ? ? ? 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 1317 1317 NAG NAG A . D 3 NAG 1 1318 1318 NAG NAG A . E 3 NAG 1 1319 1319 NAG NAG A . F 3 NAG 1 1320 1320 NAG NAG A . G 4 SIA 1 1321 1321 SIA SIA A . H 5 GAL 2 1322 1322 GAL GAL A . I 3 NAG 3 1323 1323 NAG NAG A . J 6 SO4 1 1324 1324 SO4 SO4 A . K 6 SO4 1 1325 1325 SO4 SO4 A . L 6 SO4 1 1326 1326 SO4 SO4 A . M 6 SO4 1 1327 1327 SO4 SO4 A . N 6 SO4 1 1328 1328 SO4 SO4 A . O 6 SO4 1 1329 1329 SO4 SO4 A . P 6 SO4 1 1330 1330 SO4 SO4 A . Q 6 SO4 1 1331 1331 SO4 SO4 A . R 6 SO4 1 1332 1332 SO4 SO4 A . S 6 SO4 1 1333 1333 SO4 SO4 A . T 3 NAG 1 1171 1171 NAG NAG B . U 3 NAG 2 1172 1172 NAG NAG B . V 6 SO4 1 1173 1173 SO4 SO4 B . W 6 SO4 1 1174 1174 SO4 SO4 B . X 6 SO4 1 1175 1175 SO4 SO4 B . Y 6 SO4 1 1176 1176 SO4 SO4 B . Z 7 HOH 1 2001 2001 HOH HOH A . Z 7 HOH 2 2002 2002 HOH HOH A . Z 7 HOH 3 2003 2003 HOH HOH A . Z 7 HOH 4 2004 2004 HOH HOH A . Z 7 HOH 5 2005 2005 HOH HOH A . Z 7 HOH 6 2006 2006 HOH HOH A . Z 7 HOH 7 2007 2007 HOH HOH A . Z 7 HOH 8 2008 2008 HOH HOH A . Z 7 HOH 9 2009 2009 HOH HOH A . Z 7 HOH 10 2010 2010 HOH HOH A . Z 7 HOH 11 2011 2011 HOH HOH A . Z 7 HOH 12 2012 2012 HOH HOH A . Z 7 HOH 13 2013 2013 HOH HOH A . Z 7 HOH 14 2014 2014 HOH HOH A . Z 7 HOH 15 2015 2015 HOH HOH A . Z 7 HOH 16 2016 2016 HOH HOH A . Z 7 HOH 17 2017 2017 HOH HOH A . Z 7 HOH 18 2018 2018 HOH HOH A . Z 7 HOH 19 2019 2019 HOH HOH A . Z 7 HOH 20 2020 2020 HOH HOH A . Z 7 HOH 21 2021 2021 HOH HOH A . Z 7 HOH 22 2022 2022 HOH HOH A . Z 7 HOH 23 2023 2023 HOH HOH A . Z 7 HOH 24 2024 2024 HOH HOH A . Z 7 HOH 25 2025 2025 HOH HOH A . Z 7 HOH 26 2026 2026 HOH HOH A . Z 7 HOH 27 2027 2027 HOH HOH A . Z 7 HOH 28 2028 2028 HOH HOH A . Z 7 HOH 29 2029 2029 HOH HOH A . Z 7 HOH 30 2030 2030 HOH HOH A . Z 7 HOH 31 2031 2031 HOH HOH A . Z 7 HOH 32 2032 2032 HOH HOH A . Z 7 HOH 33 2033 2033 HOH HOH A . Z 7 HOH 34 2034 2034 HOH HOH A . Z 7 HOH 35 2035 2035 HOH HOH A . Z 7 HOH 36 2036 2036 HOH HOH A . Z 7 HOH 37 2037 2037 HOH HOH A . Z 7 HOH 38 2038 2038 HOH HOH A . Z 7 HOH 39 2039 2039 HOH HOH A . Z 7 HOH 40 2040 2040 HOH HOH A . Z 7 HOH 41 2041 2041 HOH HOH A . Z 7 HOH 42 2042 2042 HOH HOH A . Z 7 HOH 43 2043 2043 HOH HOH A . Z 7 HOH 44 2044 2044 HOH HOH A . Z 7 HOH 45 2045 2045 HOH HOH A . Z 7 HOH 46 2046 2046 HOH HOH A . Z 7 HOH 47 2047 2047 HOH HOH A . Z 7 HOH 48 2048 2048 HOH HOH A . Z 7 HOH 49 2049 2049 HOH HOH A . Z 7 HOH 50 2050 2050 HOH HOH A . Z 7 HOH 51 2051 2051 HOH HOH A . Z 7 HOH 52 2052 2052 HOH HOH A . Z 7 HOH 53 2053 2053 HOH HOH A . Z 7 HOH 54 2054 2054 HOH HOH A . Z 7 HOH 55 2055 2055 HOH HOH A . Z 7 HOH 56 2056 2056 HOH HOH A . Z 7 HOH 57 2057 2057 HOH HOH A . Z 7 HOH 58 2058 2058 HOH HOH A . Z 7 HOH 59 2059 2059 HOH HOH A . Z 7 HOH 60 2060 2060 HOH HOH A . Z 7 HOH 61 2061 2061 HOH HOH A . Z 7 HOH 62 2062 2062 HOH HOH A . Z 7 HOH 63 2063 2063 HOH HOH A . Z 7 HOH 64 2064 2064 HOH HOH A . Z 7 HOH 65 2065 2065 HOH HOH A . Z 7 HOH 66 2066 2066 HOH HOH A . Z 7 HOH 67 2067 2067 HOH HOH A . Z 7 HOH 68 2068 2068 HOH HOH A . Z 7 HOH 69 2069 2069 HOH HOH A . Z 7 HOH 70 2070 2070 HOH HOH A . Z 7 HOH 71 2071 2071 HOH HOH A . Z 7 HOH 72 2072 2072 HOH HOH A . Z 7 HOH 73 2073 2073 HOH HOH A . Z 7 HOH 74 2074 2074 HOH HOH A . Z 7 HOH 75 2075 2075 HOH HOH A . Z 7 HOH 76 2076 2076 HOH HOH A . Z 7 HOH 77 2077 2077 HOH HOH A . Z 7 HOH 78 2078 2078 HOH HOH A . Z 7 HOH 79 2079 2079 HOH HOH A . Z 7 HOH 80 2080 2080 HOH HOH A . Z 7 HOH 81 2081 2081 HOH HOH A . AA 7 HOH 1 2001 2001 HOH HOH B . AA 7 HOH 2 2002 2002 HOH HOH B . AA 7 HOH 3 2003 2003 HOH HOH B . AA 7 HOH 4 2004 2004 HOH HOH B . AA 7 HOH 5 2005 2005 HOH HOH B . AA 7 HOH 6 2006 2006 HOH HOH B . AA 7 HOH 7 2007 2007 HOH HOH B . AA 7 HOH 8 2008 2008 HOH HOH B . AA 7 HOH 9 2009 2009 HOH HOH B . AA 7 HOH 10 2010 2010 HOH HOH B . AA 7 HOH 11 2011 2011 HOH HOH B . AA 7 HOH 12 2012 2012 HOH HOH B . AA 7 HOH 13 2013 2013 HOH HOH B . AA 7 HOH 14 2014 2014 HOH HOH B . AA 7 HOH 15 2015 2015 HOH HOH B . AA 7 HOH 16 2016 2016 HOH HOH B . AA 7 HOH 17 2017 2017 HOH HOH B . AA 7 HOH 18 2018 2018 HOH HOH B . AA 7 HOH 19 2019 2019 HOH HOH B . AA 7 HOH 20 2020 2020 HOH HOH B . AA 7 HOH 21 2021 2021 HOH HOH B . AA 7 HOH 22 2022 2022 HOH HOH B . AA 7 HOH 23 2023 2023 HOH HOH B . AA 7 HOH 24 2024 2024 HOH HOH B . AA 7 HOH 25 2025 2025 HOH HOH B . AA 7 HOH 26 2026 2026 HOH HOH B . AA 7 HOH 27 2027 2027 HOH HOH B . AA 7 HOH 28 2028 2028 HOH HOH B . AA 7 HOH 29 2029 2029 HOH HOH B . AA 7 HOH 30 2030 2030 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 12 A ASN 12 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 28 A ASN 28 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 123 A ASN 123 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 231 A ASN 231 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 82 B ASN 82 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details hexameric _pdbx_struct_assembly.oligomeric_count 6 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2,3 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z,AA # 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)' 46190 ? 1 MORE -599.5 ? 1 'SSA (A^2)' 59260 ? # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 2_545 -y,x-y-1,z -0.5000000000 -0.8660254038 0.0000000000 58.1740000000 0.8660254038 -0.5000000000 0.0000000000 -100.7603236795 0.0000000000 0.0000000000 1.0000000000 0.0000000000 3 'crystal symmetry operation' 3_655 -x+y+1,-x,z -0.5000000000 0.8660254038 0.0000000000 116.3480000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # _pdbx_struct_special_symmetry.id 1 _pdbx_struct_special_symmetry.PDB_model_num 1 _pdbx_struct_special_symmetry.auth_asym_id B _pdbx_struct_special_symmetry.auth_comp_id HOH _pdbx_struct_special_symmetry.auth_seq_id 2016 _pdbx_struct_special_symmetry.PDB_ins_code ? _pdbx_struct_special_symmetry.label_asym_id AA _pdbx_struct_special_symmetry.label_comp_id HOH _pdbx_struct_special_symmetry.label_seq_id . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-07-03 2 'Structure model' 1 1 2013-08-07 # _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 ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 37.6378 -36.4480 -3.6301 0.0564 0.0936 0.2566 -0.0299 0.0401 -0.0312 0.9571 1.2341 2.9472 0.2073 -0.8120 -0.5057 0.1784 0.0559 0.1068 0.1080 0.0127 0.2902 -0.1620 -0.0063 -0.1911 'X-RAY DIFFRACTION' 2 ? refined 40.4447 -45.1075 32.8794 0.6963 0.3842 0.2950 -0.2019 -0.0277 -0.0139 2.7772 2.7774 3.9186 0.6663 0.2126 0.4914 0.4182 -0.6486 -0.1169 1.0432 -0.0302 -0.1901 0.0700 0.1578 -0.3880 'X-RAY DIFFRACTION' 3 ? refined 47.8782 -36.9008 33.0279 1.0942 0.7509 0.4974 -0.4563 -0.0079 -0.1985 2.3031 0.1278 8.8224 -0.4133 -2.7329 0.8215 -0.3855 0.1792 -0.1796 0.2020 0.1451 0.0018 0.6182 0.3816 0.2404 'X-RAY DIFFRACTION' 4 ? refined 42.0371 -45.1690 17.8707 0.3833 0.2690 0.3210 -0.1265 -0.0337 -0.0591 1.7624 2.4314 1.5978 1.2504 -0.0259 1.0955 0.2687 -0.0853 -0.2396 0.7964 0.0409 -0.3916 0.1491 0.5267 -0.3097 'X-RAY DIFFRACTION' 5 ? refined 41.1235 -31.2096 -17.3218 0.0630 0.1495 0.3138 -0.0618 -0.0590 0.0789 1.5961 1.8706 5.2867 -0.2153 -2.4407 -1.2568 0.0176 0.3163 -0.0126 -0.2231 0.0655 0.3721 0.1510 -0.5082 -0.0832 'X-RAY DIFFRACTION' 6 ? refined 40.7740 -29.0084 -51.9569 0.7205 0.8705 0.3296 -0.0937 -0.2377 0.1877 1.7301 3.0579 6.2128 -1.9937 2.2647 -1.3899 0.1958 0.4670 -0.0407 -0.5336 -0.4674 0.4326 0.1650 -0.1839 0.2716 'X-RAY DIFFRACTION' 7 ? refined 41.7016 -39.2838 -36.8505 0.3193 0.4294 0.3746 -0.0828 -0.0594 -0.0501 4.2755 3.6833 20.7893 -0.7376 6.4629 -4.4711 0.1591 -0.1106 -0.3140 -0.1640 0.0884 0.2203 0.4340 -1.0753 -0.2475 'X-RAY DIFFRACTION' 8 ? refined 50.7852 -31.0166 -5.5857 0.0134 0.0585 0.1987 0.0057 0.0117 -0.0188 1.4634 1.7974 6.1549 0.6372 -0.0881 -0.4439 0.0794 -0.0659 0.0780 0.1257 -0.0829 0.0943 -0.1227 -0.4755 0.0035 'X-RAY DIFFRACTION' 9 ? refined 49.7706 -34.4285 -53.3184 0.6910 0.8226 0.1821 -0.0608 -0.1052 0.0529 1.2757 2.6236 2.9079 -0.2384 0.7527 1.2652 0.0827 0.8912 0.1260 -0.9678 0.1117 -0.1908 -0.0748 0.2069 -0.1944 'X-RAY DIFFRACTION' 10 ? refined 43.5936 -38.0044 -68.9469 1.2656 1.3439 0.3314 0.0032 -0.3494 -0.0955 4.6332 4.4343 2.2862 2.5097 -2.4296 -3.0443 -0.1876 0.9467 -0.2804 -0.6293 0.2691 0.3492 0.2403 -0.5044 -0.0816 # 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 114 ? ? ? ? 'X-RAY DIFFRACTION' 2 2 A 115 ? ? A 183 ? ? ? ? 'X-RAY DIFFRACTION' 3 3 A 184 ? ? A 217 ? ? ? ? 'X-RAY DIFFRACTION' 4 4 A 218 ? ? A 268 ? ? ? ? 'X-RAY DIFFRACTION' 5 5 A 269 ? ? A 317 ? ? ? ? 'X-RAY DIFFRACTION' 6 6 B 1 ? ? B 31 ? ? ? ? 'X-RAY DIFFRACTION' 7 7 B 32 ? ? B 59 ? ? ? ? 'X-RAY DIFFRACTION' 8 8 B 60 ? ? B 104 ? ? ? ? 'X-RAY DIFFRACTION' 9 9 B 105 ? ? B 136 ? ? ? ? 'X-RAY DIFFRACTION' 10 10 B 137 ? ? B 170 ? ? ? ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.7.0032 ? 1 xia2 'data reduction' . ? 2 xia2 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 4BSB _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;GLOBAL INITIATIVE ON SHARING ALL INFLUENZA DATA (GISAID) V10L, A125T SUBSTITUTIONS ON GISAID-EPI439507 AMINO ACID SEQUENCE WERE OBSERVED ; # 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 PRO A 39 ? ? -81.70 43.65 2 1 SER A 135 ? ? -149.40 -156.52 3 1 SER A 207 ? ? -158.85 84.79 4 1 ASP A 289 ? ? -162.90 116.57 5 1 ALA B 5 ? ? -102.36 -64.31 # _pdbx_distant_solvent_atoms.id 1 _pdbx_distant_solvent_atoms.PDB_model_num 1 _pdbx_distant_solvent_atoms.auth_atom_id O _pdbx_distant_solvent_atoms.label_alt_id ? _pdbx_distant_solvent_atoms.auth_asym_id B _pdbx_distant_solvent_atoms.auth_comp_id HOH _pdbx_distant_solvent_atoms.auth_seq_id 2030 _pdbx_distant_solvent_atoms.PDB_ins_code ? _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 7.68 _pdbx_distant_solvent_atoms.neighbor_ligand_distance . # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A ILE 317 ? CA ? A ILE 317 CA 2 1 Y 1 A ILE 317 ? C ? A ILE 317 C 3 1 Y 1 A ILE 317 ? O ? A ILE 317 O 4 1 Y 1 A ILE 317 ? CB ? A ILE 317 CB 5 1 Y 1 A ILE 317 ? CG1 ? A ILE 317 CG1 6 1 Y 1 A ILE 317 ? CG2 ? A ILE 317 CG2 7 1 Y 1 A ILE 317 ? CD1 ? A ILE 317 CD1 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A PRO 318 ? A PRO 318 2 1 Y 1 A LYS 319 ? A LYS 319 3 1 Y 1 A GLY 320 ? A GLY 320 4 1 Y 1 A ARG 321 ? A ARG 321 5 1 Y 1 B ILE 171 ? B ILE 171 6 1 Y 1 B GLN 172 ? B GLN 172 7 1 Y 1 B ILE 173 ? B ILE 173 8 1 Y 1 B ASP 174 ? B ASP 174 9 1 Y 1 B PRO 175 ? B PRO 175 10 1 Y 1 B VAL 176 ? B VAL 176 11 1 Y 1 B LYS 177 ? B LYS 177 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 'O-SIALIC ACID' SIA 5 BETA-D-GALACTOSE GAL 6 'SULFATE ION' SO4 7 water HOH #