data_4BSA # _entry.id 4BSA # _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 4BSA PDBE EBI-57227 WWPDB D_1290057227 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4BSB unspecified 'HUMAN H7N9 INFLUENZA VIRUS HAEMAGGLUTININ (WITH ASN-133 GLYCOSYLATION) IN COMPLEX WITH HUMAN RECEPTOR ANALOGUE LSTC' 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 4BSA _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 4BSA _cell.length_a 116.130 _cell.length_b 116.130 _cell.length_c 295.510 _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 4BSA _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 6 ? ? ? ? 4 non-polymer syn 'SULFATE ION' 96.063 14 ? ? ? ? 5 water nat water 18.015 267 ? ? ? ? # 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' ? ? ? ? ? ? ? ? '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' ? ? ? ? ? ? ? ? '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 4BSA A 1 ? 321 ? M4YV75 19 ? 339 ? 1 321 2 2 4BSA 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 4BSA LEU A 10 ? UNP M4YV75 VAL 28 'SEE REMARK 999' 10 1 1 4BSA THR A 125 ? UNP M4YV75 ALA 143 'SEE REMARK 999' 125 2 1 4BSA 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 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 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 4BSA _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 6M' _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 0.97949 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'DIAMOND BEAMLINE I04' _diffrn_source.pdbx_synchrotron_site Diamond _diffrn_source.pdbx_synchrotron_beamline I04 _diffrn_source.pdbx_wavelength 0.97949 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4BSA _reflns.observed_criterion_sigma_I 2.28 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 58.13 _reflns.d_resolution_high 2.30 _reflns.number_obs 34364 _reflns.number_all ? _reflns.percent_possible_obs 99.6 _reflns.pdbx_Rmerge_I_obs 0.08 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 10.92 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 5.7 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.30 _reflns_shell.d_res_low 2.38 _reflns_shell.percent_possible_all 99.5 _reflns_shell.Rmerge_I_obs 0.69 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.28 _reflns_shell.pdbx_redundancy 5.9 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4BSA _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 32404 _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 58.13 _refine.ls_d_res_high 2.30 _refine.ls_percent_reflns_obs 98.90 _refine.ls_R_factor_obs 0.25183 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.24953 _refine.ls_R_factor_R_free 0.29557 _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 1725 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.919 _refine.correlation_coeff_Fo_to_Fc_free 0.886 _refine.B_iso_mean 56.815 _refine.aniso_B[1][1] 0.27 _refine.aniso_B[2][2] 0.27 _refine.aniso_B[3][3] -0.86 _refine.aniso_B[1][2] 0.27 _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 0.305 _refine.pdbx_overall_ESU_R_Free 0.250 _refine.overall_SU_ML 0.209 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 16.190 _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 154 _refine_hist.number_atoms_solvent 267 _refine_hist.number_atoms_total 4216 _refine_hist.d_res_high 2.30 _refine_hist.d_res_low 58.13 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.006 0.019 ? 4017 'X-RAY DIFFRACTION' ? r_bond_other_d 0.001 0.020 ? 3660 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.037 1.979 ? 5441 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.699 3.003 ? 8374 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.885 5.000 ? 484 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 37.060 24.513 ? 195 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 16.051 15.000 ? 665 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 17.546 15.000 ? 28 'X-RAY DIFFRACTION' ? r_chiral_restr 0.058 0.200 ? 600 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.003 0.020 ? 4549 '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 0.365 1.099 ? 1942 'X-RAY DIFFRACTION' ? r_mcbond_other 0.365 1.099 ? 1941 'X-RAY DIFFRACTION' ? r_mcangle_it 0.659 1.648 ? 2424 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 1.240 1.573 ? 2073 '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 2.300 _refine_ls_shell.d_res_low 2.360 _refine_ls_shell.number_reflns_R_work 2347 _refine_ls_shell.R_factor_R_work 0.333 _refine_ls_shell.percent_reflns_obs 98.21 _refine_ls_shell.R_factor_R_free 0.390 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 122 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4BSA _struct.title 'Crystal Structure of the Haemagglutinin (with Asn-133 Glycosylation) from an H7N9 Influenza Virus Isolated from Humans' _struct.pdbx_descriptor HEMAGGLUTININ _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4BSA _struct_keywords.pdbx_keywords 'VIRAL PROTEIN' _struct_keywords.text ;VIRAL PROTEIN, H7N3, H5N1, FOWL PLAGUE VIRUS, SIALIC ACID, GLYCOPROTEIN, GLYCOSYLATION, VIRUS RECEPTOR, BIRD FLU, SIALYLLACTOSAMINE, 3SLN, 6SLN, LSTC, PANDEMIC ; # 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 4 ? I N N 4 ? J N N 4 ? K N N 4 ? L N N 4 ? M N N 4 ? N N N 4 ? O N N 4 ? P N N 4 ? Q N N 3 ? R N N 3 ? S N N 4 ? T N N 4 ? U N N 4 ? V N N 4 ? W N N 5 ? X N N 5 ? # _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 THR A 179 ? GLY A 187 ? THR A 179 GLY A 187 1 ? 9 HELX_P HELX_P5 5 ASP B 37 ? ILE B 56 ? ASP B 37 ILE B 56 1 ? 20 HELX_P HELX_P6 6 GLU B 74 ? ARG B 127 ? GLU B 74 ARG B 127 1 ? 54 HELX_P HELX_P7 7 ASP B 145 ? ASN B 154 ? ASP B 145 ASN B 154 1 ? 10 HELX_P HELX_P8 8 ASP B 158 ? LYS B 161 ? ASP B 158 LYS B 161 5 ? 4 HELX_P HELX_P9 9 TYR B 162 ? ASN B 169 ? TYR B 162 ASN B 169 1 ? 8 # _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 ? ? ? ? ? ? ? 2.040 ? disulf2 disulf ? ? A CYS 42 SG ? ? ? 1_555 A CYS 268 SG ? ? A CYS 42 A CYS 268 1_555 ? ? ? ? ? ? ? 2.057 ? disulf3 disulf ? ? A CYS 54 SG ? ? ? 1_555 A CYS 66 SG ? ? A CYS 54 A CYS 66 1_555 ? ? ? ? ? ? ? 2.059 ? disulf4 disulf ? ? A CYS 87 SG ? ? ? 1_555 A CYS 129 SG ? ? A CYS 87 A CYS 129 1_555 ? ? ? ? ? ? ? 2.052 ? disulf5 disulf ? ? A CYS 272 SG ? ? ? 1_555 A CYS 296 SG ? ? A CYS 272 A CYS 296 1_555 ? ? ? ? ? ? ? 2.055 ? disulf6 disulf ? ? B CYS 144 SG ? ? ? 1_555 B CYS 148 SG ? ? B CYS 144 B CYS 148 1_555 ? ? ? ? ? ? ? 2.050 ? covale1 covale ? ? A ASN 12 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 12 A NAG 405 1_555 ? ? ? ? ? ? ? 1.455 ? covale2 covale ? ? A ASN 28 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 28 A NAG 403 1_555 ? ? ? ? ? ? ? 1.462 ? covale3 covale ? ? A ASN 123 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 123 A NAG 1123 1_555 ? ? ? ? ? ? ? 1.449 ? covale4 covale ? ? A ASN 231 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 231 A NAG 404 1_555 ? ? ? ? ? ? ? 1.439 ? covale5 covale ? ? B ASN 82 ND2 ? ? ? 1_555 Q NAG . C1 ? ? B ASN 82 B NAG 201 1_555 ? ? ? ? ? ? ? 1.458 ? covale6 covale ? ? Q NAG . O4 ? ? ? 1_555 R NAG . C1 ? ? B NAG 201 B NAG 202 1_555 ? ? ? ? ? ? ? 1.441 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details BA ? 5 ? AA ? 2 ? AB ? 2 ? AC ? 3 ? AD ? 2 ? AE ? 3 ? AF ? 5 ? AG ? 5 ? AH ? 2 ? AI ? 4 ? AJ ? 3 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel AA 1 2 ? anti-parallel AB 1 2 ? anti-parallel AC 1 2 ? parallel AC 2 3 ? parallel AD 1 2 ? parallel AE 1 2 ? parallel AE 2 3 ? parallel AF 1 2 ? parallel AF 2 3 ? anti-parallel AF 3 4 ? anti-parallel AF 4 5 ? parallel AG 1 2 ? parallel AG 2 3 ? anti-parallel AG 3 4 ? anti-parallel AG 4 5 ? anti-parallel AH 1 2 ? anti-parallel AI 1 2 ? anti-parallel AI 2 3 ? anti-parallel AI 3 4 ? anti-parallel AJ 1 2 ? anti-parallel AJ 2 3 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id BA 1 GLY B 31 ? ALA B 36 ? GLY B 31 ALA B 36 BA 2 TYR B 22 ? ASN B 28 ? TYR B 22 ASN B 28 BA 3 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 MET A 155 ? LYS A 160 ? MET A 155 LYS A 160 AI 2 THR A 233 ? PHE A 238 ? THR A 233 PHE A 238 AI 3 VAL A 193 ? SER A 197 ? VAL A 193 SER A 197 AI 4 TYR A 200 ? PHE A 204 ? TYR A 200 PHE A 204 AJ 1 GLY A 277 ? THR A 278 ? GLY A 277 THR A 278 AJ 2 CYS A 272 ? HIS A 274 ? CYS A 272 HIS A 274 AJ 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 TYR A 159 ? N TYR A 159 O VAL A 234 ? O VAL A 234 AI 2 3 N SER A 237 ? N SER A 237 O THR A 194 ? O THR A 194 AI 3 4 N SER A 197 ? N SER A 197 O TYR A 200 ? O TYR A 200 AJ 1 2 N GLY A 277 ? N GLY A 277 O HIS A 274 ? O HIS A 274 AJ 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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 1317' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 1318' AC3 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 A 1319' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 1171' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 1172' AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 A 1320' AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1321' AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1322' AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1323' BC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 1324' BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 A 1325' BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 B 1173' BC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 B 1174' BC5 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 A 1326' BC6 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A 405 bound to ASN A 12' BC7 Software ? ? ? ? 5 'Binding site for Mono-Saccharide NAG A 403 bound to ASN A 28' BC8 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A1123 bound to ASN A 123' BC9 Software ? ? ? ? 2 'Binding site for Mono-Saccharide NAG A 404 bound to ASN A 231' CC1 Software ? ? ? ? 6 'Binding site for Poly-Saccharide residues NAG B 201 through NAG B 202 bound to ASN B 82' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 5 TYR A 117 ? TYR A 117 . ? 1_555 ? 2 AC1 5 SER A 118 ? SER A 118 . ? 1_555 ? 3 AC1 5 GLY A 119 ? GLY A 119 . ? 1_555 ? 4 AC1 5 ILE A 120 ? ILE A 120 . ? 1_555 ? 5 AC1 5 ASN A 146 ? ASN A 146 . ? 1_555 ? 6 AC2 6 ASN A 37 ? ASN A 37 . ? 1_555 ? 7 AC2 6 PRO A 39 ? PRO A 39 . ? 1_555 ? 8 AC2 6 HOH W . ? HOH A 2022 . ? 1_555 ? 9 AC2 6 HOH W . ? HOH A 2157 . ? 1_555 ? 10 AC2 6 HOH W . ? HOH A 2197 . ? 1_555 ? 11 AC2 6 HOH W . ? HOH A 2198 . ? 1_555 ? 12 AC3 2 ARG A 35 ? ARG A 35 . ? 1_555 ? 13 AC3 2 ARG A 303 ? ARG A 303 . ? 1_555 ? 14 AC4 4 TRP B 14 ? TRP B 14 . ? 1_555 ? 15 AC4 4 GLU B 15 ? GLU B 15 . ? 1_555 ? 16 AC4 4 GLY B 16 ? GLY B 16 . ? 1_555 ? 17 AC4 4 ARG B 25 ? ARG B 25 . ? 1_555 ? 18 AC5 4 ASN A 199 ? ASN A 199 . ? 3_655 ? 19 AC5 4 ASN A 229 ? ASN A 229 . ? 3_655 ? 20 AC5 4 ASN B 71 ? ASN B 71 . ? 1_555 ? 21 AC5 4 GLU B 72 ? GLU B 72 . ? 1_555 ? 22 AC6 2 ARG A 40 ? ARG A 40 . ? 1_555 ? 23 AC6 2 HOH W . ? HOH A 2025 . ? 1_555 ? 24 AC7 4 SER A 84 ? SER A 84 . ? 1_555 ? 25 AC7 4 ASP A 85 ? ASP A 85 . ? 1_555 ? 26 AC7 4 VAL A 86 ? VAL A 86 . ? 1_555 ? 27 AC7 4 HOH W . ? HOH A 2199 . ? 1_555 ? 28 AC8 4 ARG A 163 ? ARG A 163 . ? 1_555 ? 29 AC8 4 LYS A 164 ? LYS A 164 . ? 1_555 ? 30 AC8 4 SER A 165 ? SER A 165 . ? 1_555 ? 31 AC8 4 HOH W . ? HOH A 2200 . ? 1_555 ? 32 AC9 4 LYS A 110 ? LYS A 110 . ? 1_555 ? 33 AC9 4 GLU A 111 ? GLU A 111 . ? 1_555 ? 34 AC9 4 ALA A 112 ? ALA A 112 . ? 1_555 ? 35 AC9 4 ARG A 247 ? ARG A 247 . ? 1_555 ? 36 BC1 6 LYS A 91 ? LYS A 91 . ? 1_555 ? 37 BC1 6 PHE A 92 ? PHE A 92 . ? 1_555 ? 38 BC1 6 ASN A 94 ? ASN A 94 . ? 1_555 ? 39 BC1 6 GLU A 95 ? GLU A 95 . ? 1_555 ? 40 BC1 6 HOH W . ? HOH A 2070 . ? 1_555 ? 41 BC1 6 HOH W . ? HOH A 2072 . ? 1_555 ? 42 BC2 4 THR A 20 ? THR A 20 . ? 1_555 ? 43 BC2 4 GLU A 21 ? GLU A 21 . ? 1_555 ? 44 BC2 4 ARG A 22 ? ARG A 22 . ? 1_555 ? 45 BC2 4 GLY B 50 ? GLY B 50 . ? 3_655 ? 46 BC3 5 GLN A 302 ? GLN A 302 . ? 1_555 ? 47 BC3 5 HOH W . ? HOH A 2177 . ? 3_655 ? 48 BC3 5 THR B 59 ? THR B 59 . ? 3_655 ? 49 BC3 5 SER B 93 ? SER B 93 . ? 1_555 ? 50 BC3 5 TYR B 94 ? TYR B 94 . ? 1_555 ? 51 BC4 3 LYS B 123 ? LYS B 123 . ? 2_545 ? 52 BC4 3 LYS B 123 ? LYS B 123 . ? 3_655 ? 53 BC4 3 GLU B 132 ? GLU B 132 . ? 3_655 ? 54 BC5 3 ALA A 150 ? ALA A 150 . ? 11_445 ? 55 BC5 3 SER A 178 ? SER A 178 . ? 1_555 ? 56 BC5 3 ALA A 180 ? ALA A 180 . ? 1_555 ? 57 BC6 3 ASN A 12 ? ASN A 12 . ? 1_555 ? 58 BC6 3 GLY A 13 ? GLY A 13 . ? 1_555 ? 59 BC6 3 HOH W . ? HOH A 2193 . ? 1_555 ? 60 BC7 5 ASN A 28 ? ASN A 28 . ? 1_555 ? 61 BC7 5 THR A 30 ? THR A 30 . ? 1_555 ? 62 BC7 5 HOH W . ? HOH A 2017 . ? 1_555 ? 63 BC7 5 HOH W . ? HOH A 2191 . ? 1_555 ? 64 BC7 5 HOH W . ? HOH A 2192 . ? 1_555 ? 65 BC8 3 ASN A 123 ? ASN A 123 . ? 1_555 ? 66 BC8 3 HOH W . ? HOH A 2100 . ? 1_555 ? 67 BC8 3 HOH W . ? HOH A 2195 . ? 1_555 ? 68 BC9 2 ASN A 231 ? ASN A 231 . ? 1_555 ? 69 BC9 2 HOH W . ? HOH A 2133 . ? 1_555 ? 70 CC1 6 GLU B 72 ? GLU B 72 . ? 1_555 ? 71 CC1 6 LYS B 75 ? LYS B 75 . ? 1_555 ? 72 CC1 6 ASN B 79 ? ASN B 79 . ? 1_555 ? 73 CC1 6 ASN B 82 ? ASN B 82 . ? 1_555 ? 74 CC1 6 HOH X . ? HOH B 2027 . ? 1_555 ? 75 CC1 6 HOH X . ? HOH B 2034 . ? 1_555 ? # _database_PDB_matrix.entry_id 4BSA _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 4BSA _atom_sites.fract_transf_matrix[1][1] 0.008611 _atom_sites.fract_transf_matrix[1][2] 0.004972 _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] 0.009943 _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] 0.003384 _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 ? 38.661 -29.678 -68.614 1.00 92.19 ? 1 ASP A N 1 ATOM 2 C CA . ASP A 1 1 ? 40.058 -29.187 -68.788 1.00 91.15 ? 1 ASP A CA 1 ATOM 3 C C . ASP A 1 1 ? 40.926 -29.440 -67.541 1.00 87.69 ? 1 ASP A C 1 ATOM 4 O O . ASP A 1 1 ? 42.050 -29.923 -67.668 1.00 86.82 ? 1 ASP A O 1 ATOM 5 C CB . ASP A 1 1 ? 40.055 -27.694 -69.147 1.00 92.29 ? 1 ASP A CB 1 ATOM 6 C CG . ASP A 1 1 ? 41.208 -27.302 -70.060 1.00 93.19 ? 1 ASP A CG 1 ATOM 7 O OD1 . ASP A 1 1 ? 42.319 -27.836 -69.888 1.00 91.55 ? 1 ASP A OD1 1 ATOM 8 O OD2 . ASP A 1 1 ? 41.000 -26.463 -70.963 1.00 95.70 ? 1 ASP A OD2 1 ATOM 9 N N . LYS A 1 2 ? 40.415 -29.132 -66.347 1.00 85.86 ? 2 LYS A N 1 ATOM 10 C CA . LYS A 1 2 ? 41.237 -29.203 -65.128 1.00 82.70 ? 2 LYS A CA 1 ATOM 11 C C . LYS A 1 2 ? 40.594 -29.954 -63.952 1.00 80.63 ? 2 LYS A C 1 ATOM 12 O O . LYS A 1 2 ? 39.371 -29.987 -63.812 1.00 81.54 ? 2 LYS A O 1 ATOM 13 C CB . LYS A 1 2 ? 41.636 -27.790 -64.681 1.00 82.08 ? 2 LYS A CB 1 ATOM 14 C CG . LYS A 1 2 ? 40.496 -26.961 -64.107 1.00 82.51 ? 2 LYS A CG 1 ATOM 15 C CD . LYS A 1 2 ? 40.915 -25.526 -63.809 1.00 82.34 ? 2 LYS A CD 1 ATOM 16 C CE . LYS A 1 2 ? 40.025 -24.906 -62.734 1.00 81.58 ? 2 LYS A CE 1 ATOM 17 N NZ . LYS A 1 2 ? 40.137 -23.421 -62.663 1.00 82.27 ? 2 LYS A NZ 1 ATOM 18 N N . ILE A 1 3 ? 41.442 -30.549 -63.112 1.00 77.99 ? 3 ILE A N 1 ATOM 19 C CA . ILE A 1 3 ? 41.012 -31.171 -61.849 1.00 75.73 ? 3 ILE A CA 1 ATOM 20 C C . ILE A 1 3 ? 41.819 -30.601 -60.681 1.00 72.92 ? 3 ILE A C 1 ATOM 21 O O . ILE A 1 3 ? 43.050 -30.539 -60.738 1.00 72.06 ? 3 ILE A O 1 ATOM 22 C CB . ILE A 1 3 ? 41.128 -32.714 -61.877 1.00 75.43 ? 3 ILE A CB 1 ATOM 23 C CG1 . ILE A 1 3 ? 40.517 -33.316 -60.607 1.00 73.47 ? 3 ILE A CG1 1 ATOM 24 C CG2 . ILE A 1 3 ? 42.575 -33.167 -62.043 1.00 74.52 ? 3 ILE A CG2 1 ATOM 25 C CD1 . ILE A 1 3 ? 40.425 -34.826 -60.627 1.00 73.59 ? 3 ILE A CD1 1 ATOM 26 N N . CYS A 1 4 ? 41.117 -30.192 -59.623 1.00 71.66 ? 4 CYS A N 1 ATOM 27 C CA . CYS A 1 4 ? 41.743 -29.498 -58.494 1.00 69.31 ? 4 CYS A CA 1 ATOM 28 C C . CYS A 1 4 ? 41.569 -30.251 -57.179 1.00 66.78 ? 4 CYS A C 1 ATOM 29 O O . CYS A 1 4 ? 40.501 -30.796 -56.900 1.00 66.92 ? 4 CYS A O 1 ATOM 30 C CB . CYS A 1 4 ? 41.171 -28.082 -58.363 1.00 70.15 ? 4 CYS A CB 1 ATOM 31 S SG . CYS A 1 4 ? 41.510 -27.017 -59.790 1.00 73.06 ? 4 CYS A SG 1 ATOM 32 N N . LEU A 1 5 ? 42.637 -30.273 -56.384 1.00 64.53 ? 5 LEU A N 1 ATOM 33 C CA . LEU A 1 5 ? 42.617 -30.867 -55.046 1.00 62.12 ? 5 LEU A CA 1 ATOM 34 C C . LEU A 1 5 ? 42.403 -29.783 -53.995 1.00 60.83 ? 5 LEU A C 1 ATOM 35 O O . LEU A 1 5 ? 42.877 -28.659 -54.144 1.00 61.18 ? 5 LEU A O 1 ATOM 36 C CB . LEU A 1 5 ? 43.928 -31.601 -54.761 1.00 60.62 ? 5 LEU A CB 1 ATOM 37 C CG . LEU A 1 5 ? 44.074 -33.002 -55.354 1.00 61.28 ? 5 LEU A CG 1 ATOM 38 C CD1 . LEU A 1 5 ? 43.066 -33.956 -54.730 1.00 60.79 ? 5 LEU A CD1 1 ATOM 39 C CD2 . LEU A 1 5 ? 43.930 -32.979 -56.868 1.00 63.89 ? 5 LEU A CD2 1 ATOM 40 N N . GLY A 1 6 ? 41.687 -30.127 -52.933 1.00 59.54 ? 6 GLY A N 1 ATOM 41 C CA . GLY A 1 6 ? 41.421 -29.179 -51.859 1.00 58.41 ? 6 GLY A CA 1 ATOM 42 C C . GLY A 1 6 ? 41.146 -29.848 -50.532 1.00 56.26 ? 6 GLY A C 1 ATOM 43 O O . GLY A 1 6 ? 41.297 -31.060 -50.392 1.00 55.50 ? 6 GLY A O 1 ATOM 44 N N . HIS A 1 7 ? 40.741 -29.039 -49.558 1.00 55.45 ? 7 HIS A N 1 ATOM 45 C CA . HIS A 1 7 ? 40.431 -29.515 -48.212 1.00 53.53 ? 7 HIS A CA 1 ATOM 46 C C . HIS A 1 7 ? 39.292 -28.697 -47.629 1.00 54.10 ? 7 HIS A C 1 ATOM 47 O O . HIS A 1 7 ? 39.038 -27.579 -48.067 1.00 55.42 ? 7 HIS A O 1 ATOM 48 C CB . HIS A 1 7 ? 41.655 -29.387 -47.307 1.00 51.42 ? 7 HIS A CB 1 ATOM 49 C CG . HIS A 1 7 ? 42.176 -27.986 -47.202 1.00 51.46 ? 7 HIS A CG 1 ATOM 50 N ND1 . HIS A 1 7 ? 41.675 -27.071 -46.301 1.00 50.97 ? 7 HIS A ND1 1 ATOM 51 C CD2 . HIS A 1 7 ? 43.136 -27.339 -47.902 1.00 52.10 ? 7 HIS A CD2 1 ATOM 52 C CE1 . HIS A 1 7 ? 42.313 -25.923 -46.444 1.00 51.45 ? 7 HIS A CE1 1 ATOM 53 N NE2 . HIS A 1 7 ? 43.204 -26.059 -47.408 1.00 52.10 ? 7 HIS A NE2 1 ATOM 54 N N . HIS A 1 8 ? 38.624 -29.248 -46.623 1.00 53.32 ? 8 HIS A N 1 ATOM 55 C CA . HIS A 1 8 ? 37.485 -28.568 -46.019 1.00 54.12 ? 8 HIS A CA 1 ATOM 56 C C . HIS A 1 8 ? 37.915 -27.397 -45.131 1.00 53.68 ? 8 HIS A C 1 ATOM 57 O O . HIS A 1 8 ? 39.090 -27.267 -44.759 1.00 52.38 ? 8 HIS A O 1 ATOM 58 C CB . HIS A 1 8 ? 36.576 -29.563 -45.276 1.00 53.37 ? 8 HIS A CB 1 ATOM 59 C CG . HIS A 1 8 ? 37.110 -30.038 -43.957 1.00 50.81 ? 8 HIS A CG 1 ATOM 60 N ND1 . HIS A 1 8 ? 36.303 -30.619 -43.005 1.00 50.03 ? 8 HIS A ND1 1 ATOM 61 C CD2 . HIS A 1 8 ? 38.357 -30.021 -43.430 1.00 49.06 ? 8 HIS A CD2 1 ATOM 62 C CE1 . HIS A 1 8 ? 37.027 -30.937 -41.947 1.00 47.89 ? 8 HIS A CE1 1 ATOM 63 N NE2 . HIS A 1 8 ? 38.277 -30.583 -42.179 1.00 47.29 ? 8 HIS A NE2 1 ATOM 64 N N . ALA A 1 9 ? 36.952 -26.538 -44.820 1.00 55.24 ? 9 ALA A N 1 ATOM 65 C CA . ALA A 1 9 ? 37.200 -25.344 -44.024 1.00 55.38 ? 9 ALA A CA 1 ATOM 66 C C . ALA A 1 9 ? 35.885 -24.812 -43.479 1.00 56.92 ? 9 ALA A C 1 ATOM 67 O O . ALA A 1 9 ? 34.816 -25.218 -43.926 1.00 58.41 ? 9 ALA A O 1 ATOM 68 C CB . ALA A 1 9 ? 37.888 -24.282 -44.869 1.00 56.62 ? 9 ALA A CB 1 ATOM 69 N N . LEU A 1 10 ? 35.974 -23.910 -42.508 1.00 57.16 ? 10 LEU A N 1 ATOM 70 C CA . LEU A 1 10 ? 34.804 -23.243 -41.951 1.00 58.91 ? 10 LEU A CA 1 ATOM 71 C C . LEU A 1 10 ? 35.027 -21.747 -42.027 1.00 61.17 ? 10 LEU A C 1 ATOM 72 O O . LEU A 1 10 ? 36.152 -21.294 -42.198 1.00 60.51 ? 10 LEU A O 1 ATOM 73 C CB . LEU A 1 10 ? 34.588 -23.655 -40.494 1.00 57.03 ? 10 LEU A CB 1 ATOM 74 C CG . LEU A 1 10 ? 34.682 -25.152 -40.185 1.00 55.39 ? 10 LEU A CG 1 ATOM 75 C CD1 . LEU A 1 10 ? 34.849 -25.390 -38.689 1.00 53.36 ? 10 LEU A CD1 1 ATOM 76 C CD2 . LEU A 1 10 ? 33.470 -25.893 -40.723 1.00 56.71 ? 10 LEU A CD2 1 ATOM 77 N N . SER A 1 11 ? 33.951 -20.982 -41.892 1.00 64.67 ? 11 SER A N 1 ATOM 78 C CA . SER A 1 11 ? 34.045 -19.524 -41.853 1.00 67.58 ? 11 SER A CA 1 ATOM 79 C C . SER A 1 11 ? 34.813 -19.038 -40.625 1.00 67.79 ? 11 SER A C 1 ATOM 80 O O . SER A 1 11 ? 35.383 -17.945 -40.640 1.00 68.45 ? 11 SER A O 1 ATOM 81 C CB . SER A 1 11 ? 32.649 -18.906 -41.834 1.00 69.86 ? 11 SER A CB 1 ATOM 82 O OG . SER A 1 11 ? 32.718 -17.499 -41.673 1.00 71.43 ? 11 SER A OG 1 ATOM 83 N N . ASN A 1 12 ? 34.819 -19.858 -39.572 1.00 67.89 ? 12 ASN A N 1 ATOM 84 C CA . ASN A 1 12 ? 35.291 -19.456 -38.261 1.00 68.68 ? 12 ASN A CA 1 ATOM 85 C C . ASN A 1 12 ? 35.801 -20.703 -37.523 1.00 63.68 ? 12 ASN A C 1 ATOM 86 O O . ASN A 1 12 ? 35.031 -21.631 -37.260 1.00 63.13 ? 12 ASN A O 1 ATOM 87 C CB . ASN A 1 12 ? 34.117 -18.810 -37.503 1.00 74.59 ? 12 ASN A CB 1 ATOM 88 C CG . ASN A 1 12 ? 34.561 -17.851 -36.404 1.00 80.59 ? 12 ASN A CG 1 ATOM 89 O OD1 . ASN A 1 12 ? 35.734 -17.481 -36.336 1.00 80.06 ? 12 ASN A OD1 1 ATOM 90 N ND2 . ASN A 1 12 ? 33.621 -17.433 -35.531 1.00 88.71 ? 12 ASN A ND2 1 ATOM 91 N N . GLY A 1 13 ? 37.094 -20.730 -37.208 1.00 59.59 ? 13 GLY A N 1 ATOM 92 C CA . GLY A 1 13 ? 37.710 -21.896 -36.568 1.00 55.77 ? 13 GLY A CA 1 ATOM 93 C C . GLY A 1 13 ? 37.733 -21.823 -35.048 1.00 52.63 ? 13 GLY A C 1 ATOM 94 O O . GLY A 1 13 ? 37.092 -20.961 -34.452 1.00 53.13 ? 13 GLY A O 1 ATOM 95 N N . THR A 1 14 ? 38.473 -22.738 -34.424 1.00 48.87 ? 14 THR A N 1 ATOM 96 C CA . THR A 1 14 ? 38.691 -22.704 -32.979 1.00 46.15 ? 14 THR A CA 1 ATOM 97 C C . THR A 1 14 ? 40.166 -22.430 -32.718 1.00 44.29 ? 14 THR A C 1 ATOM 98 O O . THR A 1 14 ? 41.034 -23.135 -33.236 1.00 43.38 ? 14 THR A O 1 ATOM 99 C CB . THR A 1 14 ? 38.285 -24.026 -32.306 1.00 44.62 ? 14 THR A CB 1 ATOM 100 O OG1 . THR A 1 14 ? 36.946 -24.375 -32.683 1.00 45.46 ? 14 THR A OG1 1 ATOM 101 C CG2 . THR A 1 14 ? 38.359 -23.899 -30.791 1.00 43.51 ? 14 THR A CG2 1 ATOM 102 N N . LYS A 1 15 ? 40.446 -21.407 -31.918 1.00 43.49 ? 15 LYS A N 1 ATOM 103 C CA . LYS A 1 15 ? 41.823 -21.005 -31.657 1.00 42.64 ? 15 LYS A CA 1 ATOM 104 C C . LYS A 1 15 ? 42.520 -21.991 -30.707 1.00 40.04 ? 15 LYS A C 1 ATOM 105 O O . LYS A 1 15 ? 41.961 -22.393 -29.685 1.00 38.79 ? 15 LYS A O 1 ATOM 106 C CB . LYS A 1 15 ? 41.878 -19.582 -31.095 1.00 43.96 ? 15 LYS A CB 1 ATOM 107 C CG . LYS A 1 15 ? 41.479 -18.523 -32.108 1.00 46.37 ? 15 LYS A CG 1 ATOM 108 C CD . LYS A 1 15 ? 41.698 -17.104 -31.600 1.00 48.01 ? 15 LYS A CD 1 ATOM 109 C CE . LYS A 1 15 ? 40.832 -16.800 -30.380 1.00 48.26 ? 15 LYS A CE 1 ATOM 110 N NZ . LYS A 1 15 ? 40.361 -15.382 -30.377 1.00 50.56 ? 15 LYS A NZ 1 ATOM 111 N N . VAL A 1 16 ? 43.735 -22.386 -31.084 1.00 38.82 ? 16 VAL A N 1 ATOM 112 C CA . VAL A 1 16 ? 44.595 -23.225 -30.255 1.00 36.83 ? 16 VAL A CA 1 ATOM 113 C C . VAL A 1 16 ? 46.032 -22.704 -30.303 1.00 36.95 ? 16 VAL A C 1 ATOM 114 O O . VAL A 1 16 ? 46.390 -21.902 -31.174 1.00 37.93 ? 16 VAL A O 1 ATOM 115 C CB . VAL A 1 16 ? 44.569 -24.711 -30.693 1.00 35.69 ? 16 VAL A CB 1 ATOM 116 C CG1 . VAL A 1 16 ? 43.157 -25.266 -30.622 1.00 35.52 ? 16 VAL A CG1 1 ATOM 117 C CG2 . VAL A 1 16 ? 45.142 -24.894 -32.092 1.00 36.37 ? 16 VAL A CG2 1 ATOM 118 N N . ASN A 1 17 ? 46.847 -23.177 -29.362 1.00 35.76 ? 17 ASN A N 1 ATOM 119 C CA . ASN A 1 17 ? 48.250 -22.790 -29.276 1.00 36.06 ? 17 ASN A CA 1 ATOM 120 C C . ASN A 1 17 ? 49.147 -23.922 -29.768 1.00 35.14 ? 17 ASN A C 1 ATOM 121 O O . ASN A 1 17 ? 48.844 -25.084 -29.543 1.00 33.95 ? 17 ASN A O 1 ATOM 122 C CB . ASN A 1 17 ? 48.593 -22.421 -27.831 1.00 35.79 ? 17 ASN A CB 1 ATOM 123 C CG . ASN A 1 17 ? 47.829 -21.199 -27.340 1.00 36.92 ? 17 ASN A CG 1 ATOM 124 O OD1 . ASN A 1 17 ? 47.591 -20.254 -28.091 1.00 38.28 ? 17 ASN A OD1 1 ATOM 125 N ND2 . ASN A 1 17 ? 47.446 -21.212 -26.069 1.00 36.40 ? 17 ASN A ND2 1 ATOM 126 N N . THR A 1 18 ? 50.241 -23.576 -30.440 1.00 35.85 ? 18 THR A N 1 ATOM 127 C CA . THR A 1 18 ? 51.202 -24.557 -30.945 1.00 35.54 ? 18 THR A CA 1 ATOM 128 C C . THR A 1 18 ? 52.592 -24.209 -30.416 1.00 36.12 ? 18 THR A C 1 ATOM 129 O O . THR A 1 18 ? 52.708 -23.396 -29.500 1.00 36.33 ? 18 THR A O 1 ATOM 130 C CB . THR A 1 18 ? 51.204 -24.610 -32.487 1.00 36.38 ? 18 THR A CB 1 ATOM 131 O OG1 . THR A 1 18 ? 51.737 -23.393 -33.021 1.00 37.71 ? 18 THR A OG1 1 ATOM 132 C CG2 . THR A 1 18 ? 49.790 -24.829 -33.020 1.00 36.38 ? 18 THR A CG2 1 ATOM 133 N N . LEU A 1 19 ? 53.639 -24.834 -30.960 1.00 36.58 ? 19 LEU A N 1 ATOM 134 C CA . LEU A 1 19 ? 55.002 -24.527 -30.537 1.00 37.58 ? 19 LEU A CA 1 ATOM 135 C C . LEU A 1 19 ? 55.416 -23.161 -31.048 1.00 39.67 ? 19 LEU A C 1 ATOM 136 O O . LEU A 1 19 ? 56.165 -22.451 -30.384 1.00 40.34 ? 19 LEU A O 1 ATOM 137 C CB . LEU A 1 19 ? 56.003 -25.561 -31.056 1.00 37.57 ? 19 LEU A CB 1 ATOM 138 C CG . LEU A 1 19 ? 55.900 -27.009 -30.574 1.00 36.36 ? 19 LEU A CG 1 ATOM 139 C CD1 . LEU A 1 19 ? 56.956 -27.836 -31.297 1.00 36.80 ? 19 LEU A CD1 1 ATOM 140 C CD2 . LEU A 1 19 ? 56.066 -27.114 -29.061 1.00 35.62 ? 19 LEU A CD2 1 ATOM 141 N N . THR A 1 20 ? 54.932 -22.807 -32.235 1.00 41.09 ? 20 THR A N 1 ATOM 142 C CA . THR A 1 20 ? 55.357 -21.593 -32.916 1.00 43.42 ? 20 THR A CA 1 ATOM 143 C C . THR A 1 20 ? 54.346 -20.456 -32.821 1.00 44.87 ? 20 THR A C 1 ATOM 144 O O . THR A 1 20 ? 54.695 -19.317 -33.108 1.00 46.61 ? 20 THR A O 1 ATOM 145 C CB . THR A 1 20 ? 55.624 -21.860 -34.410 1.00 44.16 ? 20 THR A CB 1 ATOM 146 O OG1 . THR A 1 20 ? 54.494 -22.514 -35.003 1.00 43.37 ? 20 THR A OG1 1 ATOM 147 C CG2 . THR A 1 20 ? 56.860 -22.736 -34.586 1.00 44.09 ? 20 THR A CG2 1 ATOM 148 N N . GLU A 1 21 ? 53.110 -20.745 -32.413 1.00 44.69 ? 21 GLU A N 1 ATOM 149 C CA . GLU A 1 21 ? 52.025 -19.785 -32.598 1.00 46.12 ? 21 GLU A CA 1 ATOM 150 C C . GLU A 1 21 ? 51.004 -19.792 -31.463 1.00 45.26 ? 21 GLU A C 1 ATOM 151 O O . GLU A 1 21 ? 50.597 -20.851 -30.990 1.00 44.11 ? 21 GLU A O 1 ATOM 152 C CB . GLU A 1 21 ? 51.325 -20.086 -33.926 1.00 47.09 ? 21 GLU A CB 1 ATOM 153 C CG . GLU A 1 21 ? 50.789 -18.863 -34.656 1.00 49.26 ? 21 GLU A CG 1 ATOM 154 C CD . GLU A 1 21 ? 50.454 -19.129 -36.121 1.00 50.42 ? 21 GLU A CD 1 ATOM 155 O OE1 . GLU A 1 21 ? 50.966 -20.113 -36.708 1.00 50.04 ? 21 GLU A OE1 1 ATOM 156 O OE2 . GLU A 1 21 ? 49.681 -18.331 -36.696 1.00 52.12 ? 21 GLU A OE2 1 ATOM 157 N N . ARG A 1 22 ? 50.606 -18.603 -31.022 1.00 46.12 ? 22 ARG A N 1 ATOM 158 C CA . ARG A 1 22 ? 49.459 -18.463 -30.130 1.00 45.50 ? 22 ARG A CA 1 ATOM 159 C C . ARG A 1 22 ? 48.227 -18.169 -30.971 1.00 45.63 ? 22 ARG A C 1 ATOM 160 O O . ARG A 1 22 ? 48.274 -17.346 -31.875 1.00 46.79 ? 22 ARG A O 1 ATOM 161 C CB . ARG A 1 22 ? 49.669 -17.335 -29.109 1.00 46.89 ? 22 ARG A CB 1 ATOM 162 C CG . ARG A 1 22 ? 50.163 -17.798 -27.746 1.00 46.29 ? 22 ARG A CG 1 ATOM 163 C CD . ARG A 1 22 ? 50.120 -16.674 -26.716 1.00 47.89 ? 22 ARG A CD 1 ATOM 164 N NE . ARG A 1 22 ? 48.813 -16.527 -26.063 1.00 48.08 ? 22 ARG A NE 1 ATOM 165 C CZ . ARG A 1 22 ? 48.355 -17.303 -25.076 1.00 47.17 ? 22 ARG A CZ 1 ATOM 166 N NH1 . ARG A 1 22 ? 49.080 -18.322 -24.610 1.00 46.23 ? 22 ARG A NH1 1 ATOM 167 N NH2 . ARG A 1 22 ? 47.151 -17.068 -24.549 1.00 47.21 ? 22 ARG A NH2 1 ATOM 168 N N . GLY A 1 23 ? 47.129 -18.855 -30.679 1.00 44.28 ? 23 GLY A N 1 ATOM 169 C CA . GLY A 1 23 ? 45.838 -18.539 -31.287 1.00 44.82 ? 23 GLY A CA 1 ATOM 170 C C . GLY A 1 23 ? 45.689 -18.846 -32.767 1.00 45.05 ? 23 GLY A C 1 ATOM 171 O O . GLY A 1 23 ? 45.049 -18.088 -33.486 1.00 46.61 ? 23 GLY A O 1 ATOM 172 N N . VAL A 1 24 ? 46.265 -19.953 -33.226 1.00 43.67 ? 24 VAL A N 1 ATOM 173 C CA . VAL A 1 24 ? 46.025 -20.424 -34.599 1.00 44.09 ? 24 VAL A CA 1 ATOM 174 C C . VAL A 1 24 ? 44.669 -21.129 -34.668 1.00 43.67 ? 24 VAL A C 1 ATOM 175 O O . VAL A 1 24 ? 44.343 -21.957 -33.817 1.00 42.22 ? 24 VAL A O 1 ATOM 176 C CB . VAL A 1 24 ? 47.160 -21.335 -35.152 1.00 43.28 ? 24 VAL A CB 1 ATOM 177 C CG1 . VAL A 1 24 ? 47.444 -22.525 -34.256 1.00 41.47 ? 24 VAL A CG1 1 ATOM 178 C CG2 . VAL A 1 24 ? 46.825 -21.820 -36.553 1.00 44.03 ? 24 VAL A CG2 1 ATOM 179 N N . GLU A 1 25 ? 43.875 -20.790 -35.677 1.00 45.07 ? 25 GLU A N 1 ATOM 180 C CA . GLU A 1 25 ? 42.539 -21.359 -35.806 1.00 45.22 ? 25 GLU A CA 1 ATOM 181 C C . GLU A 1 25 ? 42.575 -22.699 -36.530 1.00 44.69 ? 25 GLU A C 1 ATOM 182 O O . GLU A 1 25 ? 43.217 -22.839 -37.575 1.00 45.06 ? 25 GLU A O 1 ATOM 183 C CB . GLU A 1 25 ? 41.595 -20.386 -36.515 1.00 47.30 ? 25 GLU A CB 1 ATOM 184 C CG . GLU A 1 25 ? 41.257 -19.181 -35.653 1.00 48.04 ? 25 GLU A CG 1 ATOM 185 C CD . GLU A 1 25 ? 40.173 -18.291 -36.232 1.00 50.13 ? 25 GLU A CD 1 ATOM 186 O OE1 . GLU A 1 25 ? 39.652 -18.583 -37.334 1.00 51.14 ? 25 GLU A OE1 1 ATOM 187 O OE2 . GLU A 1 25 ? 39.846 -17.284 -35.568 1.00 50.88 ? 25 GLU A OE2 1 ATOM 188 N N . VAL A 1 26 ? 41.883 -23.675 -35.950 1.00 43.92 ? 26 VAL A N 1 ATOM 189 C CA . VAL A 1 26 ? 41.759 -25.010 -36.522 1.00 43.88 ? 26 VAL A CA 1 ATOM 190 C C . VAL A 1 26 ? 40.289 -25.355 -36.733 1.00 45.31 ? 26 VAL A C 1 ATOM 191 O O . VAL A 1 26 ? 39.397 -24.662 -36.241 1.00 45.79 ? 26 VAL A O 1 ATOM 192 C CB . VAL A 1 26 ? 42.430 -26.081 -35.634 1.00 41.85 ? 26 VAL A CB 1 ATOM 193 C CG1 . VAL A 1 26 ? 43.941 -25.904 -35.642 1.00 41.44 ? 26 VAL A CG1 1 ATOM 194 C CG2 . VAL A 1 26 ? 41.901 -26.038 -34.207 1.00 40.75 ? 26 VAL A CG2 1 ATOM 195 N N . VAL A 1 27 ? 40.048 -26.433 -37.465 1.00 46.49 ? 27 VAL A N 1 ATOM 196 C CA . VAL A 1 27 ? 38.698 -26.820 -37.837 1.00 48.51 ? 27 VAL A CA 1 ATOM 197 C C . VAL A 1 27 ? 37.922 -27.269 -36.611 1.00 48.75 ? 27 VAL A C 1 ATOM 198 O O . VAL A 1 27 ? 36.805 -26.823 -36.385 1.00 49.21 ? 27 VAL A O 1 ATOM 199 C CB . VAL A 1 27 ? 38.703 -27.928 -38.913 1.00 48.92 ? 27 VAL A CB 1 ATOM 200 C CG1 . VAL A 1 27 ? 37.303 -28.489 -39.134 1.00 49.98 ? 27 VAL A CG1 1 ATOM 201 C CG2 . VAL A 1 27 ? 39.263 -27.388 -40.219 1.00 50.18 ? 27 VAL A CG2 1 ATOM 202 N N . ASN A 1 28 ? 38.518 -28.154 -35.823 1.00 49.40 ? 28 ASN A N 1 ATOM 203 C CA . ASN A 1 28 ? 37.903 -28.591 -34.577 1.00 50.63 ? 28 ASN A CA 1 ATOM 204 C C . ASN A 1 28 ? 38.952 -28.761 -33.483 1.00 46.97 ? 28 ASN A C 1 ATOM 205 O O . ASN A 1 28 ? 40.131 -28.965 -33.772 1.00 45.94 ? 28 ASN A O 1 ATOM 206 C CB . ASN A 1 28 ? 37.124 -29.894 -34.798 1.00 54.78 ? 28 ASN A CB 1 ATOM 207 C CG . ASN A 1 28 ? 36.125 -30.179 -33.688 1.00 60.39 ? 28 ASN A CG 1 ATOM 208 O OD1 . ASN A 1 28 ? 35.825 -29.311 -32.862 1.00 59.94 ? 28 ASN A OD1 1 ATOM 209 N ND2 . ASN A 1 28 ? 35.600 -31.414 -33.664 1.00 68.51 ? 28 ASN A ND2 1 ATOM 210 N N . ALA A 1 29 ? 38.510 -28.650 -32.232 1.00 44.49 ? 29 ALA A N 1 ATOM 211 C CA . ALA A 1 29 ? 39.376 -28.816 -31.067 1.00 41.86 ? 29 ALA A CA 1 ATOM 212 C C . ALA A 1 29 ? 38.580 -29.311 -29.863 1.00 40.21 ? 29 ALA A C 1 ATOM 213 O O . ALA A 1 29 ? 37.345 -29.261 -29.852 1.00 40.92 ? 29 ALA A O 1 ATOM 214 C CB . ALA A 1 29 ? 40.070 -27.509 -30.727 1.00 41.93 ? 29 ALA A CB 1 ATOM 215 N N . THR A 1 30 ? 39.295 -29.788 -28.851 1.00 37.73 ? 30 THR A N 1 ATOM 216 C CA . THR A 1 30 ? 38.654 -30.287 -27.648 1.00 36.35 ? 30 THR A CA 1 ATOM 217 C C . THR A 1 30 ? 39.449 -29.982 -26.385 1.00 34.31 ? 30 THR A C 1 ATOM 218 O O . THR A 1 30 ? 40.667 -29.817 -26.427 1.00 33.88 ? 30 THR A O 1 ATOM 219 C CB . THR A 1 30 ? 38.372 -31.799 -27.744 1.00 36.06 ? 30 THR A CB 1 ATOM 220 O OG1 . THR A 1 30 ? 37.450 -32.165 -26.711 1.00 36.32 ? 30 THR A OG1 1 ATOM 221 C CG2 . THR A 1 30 ? 39.645 -32.614 -27.605 1.00 35.15 ? 30 THR A CG2 1 ATOM 222 N N . GLU A 1 31 ? 38.733 -29.918 -25.267 1.00 32.97 ? 31 GLU A N 1 ATOM 223 C CA . GLU A 1 31 ? 39.298 -29.486 -24.000 1.00 31.53 ? 31 GLU A CA 1 ATOM 224 C C . GLU A 1 31 ? 40.045 -30.621 -23.307 1.00 29.79 ? 31 GLU A C 1 ATOM 225 O O . GLU A 1 31 ? 39.603 -31.769 -23.336 1.00 29.58 ? 31 GLU A O 1 ATOM 226 C CB . GLU A 1 31 ? 38.184 -28.956 -23.100 1.00 31.71 ? 31 GLU A CB 1 ATOM 227 C CG . GLU A 1 31 ? 38.641 -28.445 -21.751 1.00 31.09 ? 31 GLU A CG 1 ATOM 228 C CD . GLU A 1 31 ? 39.677 -27.339 -21.850 1.00 31.46 ? 31 GLU A CD 1 ATOM 229 O OE1 . GLU A 1 31 ? 39.299 -26.194 -22.204 1.00 32.64 ? 31 GLU A OE1 1 ATOM 230 O OE2 . GLU A 1 31 ? 40.865 -27.617 -21.551 1.00 30.49 ? 31 GLU A OE2 1 ATOM 231 N N . THR A 1 32 ? 41.181 -30.297 -22.696 1.00 28.66 ? 32 THR A N 1 ATOM 232 C CA . THR A 1 32 ? 41.954 -31.270 -21.925 1.00 27.26 ? 32 THR A CA 1 ATOM 233 C C . THR A 1 32 ? 41.933 -31.011 -20.422 1.00 26.63 ? 32 THR A C 1 ATOM 234 O O . THR A 1 32 ? 42.322 -31.878 -19.656 1.00 25.96 ? 32 THR A O 1 ATOM 235 C CB . THR A 1 32 ? 43.423 -31.338 -22.385 1.00 27.15 ? 32 THR A CB 1 ATOM 236 O OG1 . THR A 1 32 ? 44.087 -30.097 -22.112 1.00 27.50 ? 32 THR A OG1 1 ATOM 237 C CG2 . THR A 1 32 ? 43.499 -31.655 -23.861 1.00 27.69 ? 32 THR A CG2 1 ATOM 238 N N . VAL A 1 33 ? 41.491 -29.826 -20.007 1.00 27.09 ? 33 VAL A N 1 ATOM 239 C CA . VAL A 1 33 ? 41.382 -29.474 -18.600 1.00 26.72 ? 33 VAL A CA 1 ATOM 240 C C . VAL A 1 33 ? 39.925 -29.501 -18.137 1.00 27.08 ? 33 VAL A C 1 ATOM 241 O O . VAL A 1 33 ? 39.089 -28.757 -18.647 1.00 27.84 ? 33 VAL A O 1 ATOM 242 C CB . VAL A 1 33 ? 41.954 -28.073 -18.335 1.00 27.38 ? 33 VAL A CB 1 ATOM 243 C CG1 . VAL A 1 33 ? 41.853 -27.723 -16.856 1.00 27.20 ? 33 VAL A CG1 1 ATOM 244 C CG2 . VAL A 1 33 ? 43.396 -28.007 -18.816 1.00 27.41 ? 33 VAL A CG2 1 ATOM 245 N N . GLU A 1 34 ? 39.645 -30.346 -17.147 1.00 26.55 ? 34 GLU A N 1 ATOM 246 C CA . GLU A 1 34 ? 38.308 -30.478 -16.597 1.00 27.04 ? 34 GLU A CA 1 ATOM 247 C C . GLU A 1 34 ? 37.978 -29.313 -15.669 1.00 27.75 ? 34 GLU A C 1 ATOM 248 O O . GLU A 1 34 ? 38.764 -28.991 -14.771 1.00 27.36 ? 34 GLU A O 1 ATOM 249 C CB . GLU A 1 34 ? 38.187 -31.806 -15.834 1.00 26.27 ? 34 GLU A CB 1 ATOM 250 C CG . GLU A 1 34 ? 36.800 -32.087 -15.303 1.00 26.61 ? 34 GLU A CG 1 ATOM 251 C CD . GLU A 1 34 ? 35.767 -32.117 -16.411 1.00 27.72 ? 34 GLU A CD 1 ATOM 252 O OE1 . GLU A 1 34 ? 35.801 -33.061 -17.230 1.00 27.75 ? 34 GLU A OE1 1 ATOM 253 O OE2 . GLU A 1 34 ? 34.931 -31.187 -16.475 1.00 28.93 ? 34 GLU A OE2 1 ATOM 254 N N . ARG A 1 35 ? 36.830 -28.677 -15.907 1.00 29.00 ? 35 ARG A N 1 ATOM 255 C CA . ARG A 1 35 ? 36.312 -27.611 -15.039 1.00 30.11 ? 35 ARG A CA 1 ATOM 256 C C . ARG A 1 35 ? 34.934 -27.917 -14.441 1.00 30.49 ? 35 ARG A C 1 ATOM 257 O O . ARG A 1 35 ? 34.440 -27.160 -13.608 1.00 31.09 ? 35 ARG A O 1 ATOM 258 C CB . ARG A 1 35 ? 36.208 -26.295 -15.812 1.00 31.75 ? 35 ARG A CB 1 ATOM 259 C CG . ARG A 1 35 ? 37.529 -25.740 -16.293 1.00 32.08 ? 35 ARG A CG 1 ATOM 260 C CD . ARG A 1 35 ? 37.352 -24.354 -16.911 1.00 33.94 ? 35 ARG A CD 1 ATOM 261 N NE . ARG A 1 35 ? 36.552 -24.377 -18.138 1.00 34.98 ? 35 ARG A NE 1 ATOM 262 C CZ . ARG A 1 35 ? 36.953 -24.869 -19.311 1.00 35.15 ? 35 ARG A CZ 1 ATOM 263 N NH1 . ARG A 1 35 ? 38.164 -25.400 -19.459 1.00 34.16 ? 35 ARG A NH1 1 ATOM 264 N NH2 . ARG A 1 35 ? 36.126 -24.832 -20.357 1.00 36.40 ? 35 ARG A NH2 1 ATOM 265 N N . THR A 1 36 ? 34.299 -29.000 -14.875 1.00 30.46 ? 36 THR A N 1 ATOM 266 C CA . THR A 1 36 ? 32.956 -29.329 -14.399 1.00 31.32 ? 36 THR A CA 1 ATOM 267 C C . THR A 1 36 ? 33.028 -30.119 -13.108 1.00 30.54 ? 36 THR A C 1 ATOM 268 O O . THR A 1 36 ? 33.589 -31.214 -13.079 1.00 29.82 ? 36 THR A O 1 ATOM 269 C CB . THR A 1 36 ? 32.181 -30.147 -15.441 1.00 31.71 ? 36 THR A CB 1 ATOM 270 O OG1 . THR A 1 36 ? 32.274 -29.486 -16.706 1.00 32.69 ? 36 THR A OG1 1 ATOM 271 C CG2 . THR A 1 36 ? 30.711 -30.280 -15.041 1.00 32.73 ? 36 THR A CG2 1 ATOM 272 N N . ASN A 1 37 ? 32.485 -29.539 -12.044 1.00 31.30 ? 37 ASN A N 1 ATOM 273 C CA . ASN A 1 37 ? 32.350 -30.206 -10.758 1.00 30.97 ? 37 ASN A CA 1 ATOM 274 C C . ASN A 1 37 ? 30.958 -30.813 -10.624 1.00 31.64 ? 37 ASN A C 1 ATOM 275 O O . ASN A 1 37 ? 30.001 -30.318 -11.209 1.00 32.94 ? 37 ASN A O 1 ATOM 276 C CB . ASN A 1 37 ? 32.567 -29.202 -9.627 1.00 31.59 ? 37 ASN A CB 1 ATOM 277 C CG . ASN A 1 37 ? 32.496 -29.846 -8.255 1.00 31.19 ? 37 ASN A CG 1 ATOM 278 O OD1 . ASN A 1 37 ? 33.132 -30.868 -8.004 1.00 30.27 ? 37 ASN A OD1 1 ATOM 279 N ND2 . ASN A 1 37 ? 31.718 -29.259 -7.366 1.00 32.15 ? 37 ASN A ND2 1 ATOM 280 N N . ILE A 1 38 ? 30.849 -31.898 -9.868 1.00 31.07 ? 38 ILE A N 1 ATOM 281 C CA . ILE A 1 38 ? 29.553 -32.389 -9.436 1.00 31.92 ? 38 ILE A CA 1 ATOM 282 C C . ILE A 1 38 ? 29.460 -32.138 -7.941 1.00 31.68 ? 38 ILE A C 1 ATOM 283 O O . ILE A 1 38 ? 30.249 -32.695 -7.191 1.00 30.33 ? 38 ILE A O 1 ATOM 284 C CB . ILE A 1 38 ? 29.375 -33.874 -9.771 1.00 31.77 ? 38 ILE A CB 1 ATOM 285 C CG1 . ILE A 1 38 ? 29.275 -34.019 -11.292 1.00 32.54 ? 38 ILE A CG1 1 ATOM 286 C CG2 . ILE A 1 38 ? 28.128 -34.442 -9.092 1.00 32.33 ? 38 ILE A CG2 1 ATOM 287 C CD1 . ILE A 1 38 ? 29.057 -35.441 -11.757 1.00 32.63 ? 38 ILE A CD1 1 ATOM 288 N N . PRO A 1 39 ? 28.497 -31.301 -7.504 1.00 32.91 ? 39 PRO A N 1 ATOM 289 C CA . PRO A 1 39 ? 28.433 -30.843 -6.112 1.00 33.44 ? 39 PRO A CA 1 ATOM 290 C C . PRO A 1 39 ? 27.802 -31.856 -5.157 1.00 33.78 ? 39 PRO A C 1 ATOM 291 O O . PRO A 1 39 ? 26.964 -31.496 -4.325 1.00 35.03 ? 39 PRO A O 1 ATOM 292 C CB . PRO A 1 39 ? 27.580 -29.572 -6.208 1.00 34.92 ? 39 PRO A CB 1 ATOM 293 C CG . PRO A 1 39 ? 26.654 -29.850 -7.337 1.00 35.69 ? 39 PRO A CG 1 ATOM 294 C CD . PRO A 1 39 ? 27.402 -30.731 -8.310 1.00 34.44 ? 39 PRO A CD 1 ATOM 295 N N . ARG A 1 40 ? 28.215 -33.113 -5.291 1.00 33.26 ? 40 ARG A N 1 ATOM 296 C CA . ARG A 1 40 ? 27.789 -34.207 -4.428 1.00 33.55 ? 40 ARG A CA 1 ATOM 297 C C . ARG A 1 40 ? 28.975 -35.143 -4.233 1.00 31.53 ? 40 ARG A C 1 ATOM 298 O O . ARG A 1 40 ? 29.933 -35.092 -5.000 1.00 30.31 ? 40 ARG A O 1 ATOM 299 C CB . ARG A 1 40 ? 26.628 -34.983 -5.061 1.00 35.05 ? 40 ARG A CB 1 ATOM 300 C CG . ARG A 1 40 ? 25.240 -34.519 -4.640 1.00 37.72 ? 40 ARG A CG 1 ATOM 301 C CD . ARG A 1 40 ? 24.490 -33.825 -5.767 1.00 40.22 ? 40 ARG A CD 1 ATOM 302 N NE . ARG A 1 40 ? 24.385 -34.649 -6.982 1.00 41.30 ? 40 ARG A NE 1 ATOM 303 C CZ . ARG A 1 40 ? 24.323 -34.172 -8.232 1.00 42.75 ? 40 ARG A CZ 1 ATOM 304 N NH1 . ARG A 1 40 ? 24.363 -32.856 -8.478 1.00 43.39 ? 40 ARG A NH1 1 ATOM 305 N NH2 . ARG A 1 40 ? 24.234 -35.021 -9.256 1.00 43.11 ? 40 ARG A NH2 1 ATOM 306 N N . ILE A 1 41 ? 28.915 -35.985 -3.207 1.00 30.97 ? 41 ILE A N 1 ATOM 307 C CA . ILE A 1 41 ? 29.881 -37.067 -3.067 1.00 29.90 ? 41 ILE A CA 1 ATOM 308 C C . ILE A 1 41 ? 29.270 -38.267 -3.766 1.00 29.67 ? 41 ILE A C 1 ATOM 309 O O . ILE A 1 41 ? 28.322 -38.865 -3.268 1.00 30.19 ? 41 ILE A O 1 ATOM 310 C CB . ILE A 1 41 ? 30.195 -37.404 -1.597 1.00 29.98 ? 41 ILE A CB 1 ATOM 311 C CG1 . ILE A 1 41 ? 30.727 -36.173 -0.857 1.00 30.31 ? 41 ILE A CG1 1 ATOM 312 C CG2 . ILE A 1 41 ? 31.188 -38.562 -1.517 1.00 29.07 ? 41 ILE A CG2 1 ATOM 313 C CD1 . ILE A 1 41 ? 32.002 -35.594 -1.435 1.00 30.19 ? 41 ILE A CD1 1 ATOM 314 N N . CYS A 1 42 ? 29.806 -38.590 -4.937 1.00 29.06 ? 42 CYS A N 1 ATOM 315 C CA . CYS A 1 42 ? 29.268 -39.650 -5.781 1.00 29.30 ? 42 CYS A CA 1 ATOM 316 C C . CYS A 1 42 ? 29.789 -40.989 -5.300 1.00 28.44 ? 42 CYS A C 1 ATOM 317 O O . CYS A 1 42 ? 30.943 -41.331 -5.556 1.00 27.51 ? 42 CYS A O 1 ATOM 318 C CB . CYS A 1 42 ? 29.693 -39.433 -7.227 1.00 29.37 ? 42 CYS A CB 1 ATOM 319 S SG . CYS A 1 42 ? 28.809 -38.096 -8.039 1.00 31.04 ? 42 CYS A SG 1 ATOM 320 N N . SER A 1 43 ? 28.934 -41.747 -4.620 1.00 28.64 ? 43 SER A N 1 ATOM 321 C CA . SER A 1 43 ? 29.371 -42.952 -3.928 1.00 28.12 ? 43 SER A CA 1 ATOM 322 C C . SER A 1 43 ? 28.632 -44.223 -4.355 1.00 28.58 ? 43 SER A C 1 ATOM 323 O O . SER A 1 43 ? 28.575 -45.184 -3.590 1.00 28.63 ? 43 SER A O 1 ATOM 324 C CB . SER A 1 43 ? 29.217 -42.735 -2.424 1.00 28.18 ? 43 SER A CB 1 ATOM 325 O OG . SER A 1 43 ? 27.872 -42.466 -2.101 1.00 29.38 ? 43 SER A OG 1 ATOM 326 N N . LYS A 1 44 ? 28.073 -44.234 -5.566 1.00 28.98 ? 44 LYS A N 1 ATOM 327 C CA . LYS A 1 44 ? 27.442 -45.430 -6.102 1.00 29.64 ? 44 LYS A CA 1 ATOM 328 C C . LYS A 1 44 ? 28.379 -46.623 -5.999 1.00 28.84 ? 44 LYS A C 1 ATOM 329 O O . LYS A 1 44 ? 29.513 -46.540 -6.436 1.00 27.73 ? 44 LYS A O 1 ATOM 330 C CB . LYS A 1 44 ? 27.068 -45.252 -7.567 1.00 30.49 ? 44 LYS A CB 1 ATOM 331 C CG . LYS A 1 44 ? 26.564 -46.549 -8.189 1.00 31.81 ? 44 LYS A CG 1 ATOM 332 C CD . LYS A 1 44 ? 25.841 -46.324 -9.497 1.00 33.42 ? 44 LYS A CD 1 ATOM 333 C CE . LYS A 1 44 ? 26.803 -45.943 -10.608 1.00 33.14 ? 44 LYS A CE 1 ATOM 334 N NZ . LYS A 1 44 ? 26.043 -45.586 -11.841 1.00 34.71 ? 44 LYS A NZ 1 ATOM 335 N N . GLY A 1 45 ? 27.893 -47.726 -5.435 1.00 29.45 ? 45 GLY A N 1 ATOM 336 C CA . GLY A 1 45 ? 28.649 -48.980 -5.372 1.00 29.34 ? 45 GLY A CA 1 ATOM 337 C C . GLY A 1 45 ? 29.683 -49.093 -4.254 1.00 28.53 ? 45 GLY A C 1 ATOM 338 O O . GLY A 1 45 ? 30.396 -50.089 -4.175 1.00 28.61 ? 45 GLY A O 1 ATOM 339 N N . LYS A 1 46 ? 29.760 -48.099 -3.375 1.00 27.91 ? 46 LYS A N 1 ATOM 340 C CA . LYS A 1 46 ? 30.780 -48.086 -2.325 1.00 27.29 ? 46 LYS A CA 1 ATOM 341 C C . LYS A 1 46 ? 30.174 -48.139 -0.940 1.00 27.45 ? 46 LYS A C 1 ATOM 342 O O . LYS A 1 46 ? 29.204 -47.449 -0.668 1.00 27.99 ? 46 LYS A O 1 ATOM 343 C CB . LYS A 1 46 ? 31.630 -46.814 -2.433 1.00 26.61 ? 46 LYS A CB 1 ATOM 344 C CG . LYS A 1 46 ? 32.530 -46.776 -3.646 1.00 26.25 ? 46 LYS A CG 1 ATOM 345 C CD . LYS A 1 46 ? 33.220 -45.429 -3.777 1.00 25.91 ? 46 LYS A CD 1 ATOM 346 C CE . LYS A 1 46 ? 34.127 -45.435 -4.995 1.00 25.66 ? 46 LYS A CE 1 ATOM 347 N NZ . LYS A 1 46 ? 34.782 -44.121 -5.151 1.00 25.28 ? 46 LYS A NZ 1 ATOM 348 N N . ARG A 1 47 ? 30.758 -48.940 -0.059 1.00 27.40 ? 47 ARG A N 1 ATOM 349 C CA . ARG A 1 47 ? 30.368 -48.908 1.345 1.00 27.89 ? 47 ARG A CA 1 ATOM 350 C C . ARG A 1 47 ? 30.808 -47.572 1.933 1.00 26.51 ? 47 ARG A C 1 ATOM 351 O O . ARG A 1 47 ? 32.007 -47.337 2.136 1.00 25.58 ? 47 ARG A O 1 ATOM 352 C CB . ARG A 1 47 ? 30.991 -50.061 2.126 1.00 28.99 ? 47 ARG A CB 1 ATOM 353 C CG . ARG A 1 47 ? 30.439 -51.413 1.733 1.00 31.03 ? 47 ARG A CG 1 ATOM 354 C CD . ARG A 1 47 ? 30.843 -52.502 2.716 1.00 32.48 ? 47 ARG A CD 1 ATOM 355 N NE . ARG A 1 47 ? 32.003 -53.245 2.240 1.00 33.44 ? 47 ARG A NE 1 ATOM 356 C CZ . ARG A 1 47 ? 33.262 -53.102 2.666 1.00 34.18 ? 47 ARG A CZ 1 ATOM 357 N NH1 . ARG A 1 47 ? 33.588 -52.228 3.619 1.00 34.09 ? 47 ARG A NH1 1 ATOM 358 N NH2 . ARG A 1 47 ? 34.218 -53.862 2.127 1.00 34.90 ? 47 ARG A NH2 1 ATOM 359 N N . THR A 1 48 ? 29.833 -46.709 2.206 1.00 26.18 ? 48 THR A N 1 ATOM 360 C CA . THR A 1 48 ? 30.096 -45.345 2.656 1.00 25.49 ? 48 THR A CA 1 ATOM 361 C C . THR A 1 48 ? 29.631 -45.102 4.087 1.00 25.73 ? 48 THR A C 1 ATOM 362 O O . THR A 1 48 ? 28.523 -45.483 4.481 1.00 26.66 ? 48 THR A O 1 ATOM 363 C CB . THR A 1 48 ? 29.416 -44.313 1.729 1.00 25.68 ? 48 THR A CB 1 ATOM 364 O OG1 . THR A 1 48 ? 29.770 -44.592 0.369 1.00 25.35 ? 48 THR A OG1 1 ATOM 365 C CG2 . THR A 1 48 ? 29.832 -42.879 2.087 1.00 25.32 ? 48 THR A CG2 1 ATOM 366 N N . VAL A 1 49 ? 30.486 -44.446 4.852 1.00 25.05 ? 49 VAL A N 1 ATOM 367 C CA . VAL A 1 49 ? 30.183 -44.049 6.204 1.00 25.41 ? 49 VAL A CA 1 ATOM 368 C C . VAL A 1 49 ? 30.367 -42.549 6.284 1.00 25.25 ? 49 VAL A C 1 ATOM 369 O O . VAL A 1 49 ? 31.482 -42.045 6.161 1.00 24.84 ? 49 VAL A O 1 ATOM 370 C CB . VAL A 1 49 ? 31.117 -44.750 7.201 1.00 25.28 ? 49 VAL A CB 1 ATOM 371 C CG1 . VAL A 1 49 ? 30.997 -44.135 8.592 1.00 25.87 ? 49 VAL A CG1 1 ATOM 372 C CG2 . VAL A 1 49 ? 30.813 -46.237 7.228 1.00 25.55 ? 49 VAL A CG2 1 ATOM 373 N N . ASP A 1 50 ? 29.259 -41.846 6.470 1.00 26.01 ? 50 ASP A N 1 ATOM 374 C CA . ASP A 1 50 ? 29.244 -40.407 6.665 1.00 26.26 ? 50 ASP A CA 1 ATOM 375 C C . ASP A 1 50 ? 29.215 -40.148 8.170 1.00 26.88 ? 50 ASP A C 1 ATOM 376 O O . ASP A 1 50 ? 28.220 -40.421 8.840 1.00 27.56 ? 50 ASP A O 1 ATOM 377 C CB . ASP A 1 50 ? 28.013 -39.801 5.972 1.00 26.98 ? 50 ASP A CB 1 ATOM 378 C CG . ASP A 1 50 ? 27.932 -38.289 6.131 1.00 27.48 ? 50 ASP A CG 1 ATOM 379 O OD1 . ASP A 1 50 ? 28.820 -37.725 6.793 1.00 27.27 ? 50 ASP A OD1 1 ATOM 380 O OD2 . ASP A 1 50 ? 26.985 -37.666 5.606 1.00 28.17 ? 50 ASP A OD2 1 ATOM 381 N N . LEU A 1 51 ? 30.317 -39.628 8.695 1.00 26.70 ? 51 LEU A N 1 ATOM 382 C CA . LEU A 1 51 ? 30.487 -39.480 10.142 1.00 27.44 ? 51 LEU A CA 1 ATOM 383 C C . LEU A 1 51 ? 29.589 -38.423 10.784 1.00 28.67 ? 51 LEU A C 1 ATOM 384 O O . LEU A 1 51 ? 29.297 -38.506 11.976 1.00 29.38 ? 51 LEU A O 1 ATOM 385 C CB . LEU A 1 51 ? 31.947 -39.190 10.475 1.00 27.03 ? 51 LEU A CB 1 ATOM 386 C CG . LEU A 1 51 ? 32.893 -40.361 10.222 1.00 26.25 ? 51 LEU A CG 1 ATOM 387 C CD1 . LEU A 1 51 ? 34.335 -39.890 10.308 1.00 26.03 ? 51 LEU A CD1 1 ATOM 388 C CD2 . LEU A 1 51 ? 32.645 -41.484 11.209 1.00 26.63 ? 51 LEU A CD2 1 ATOM 389 N N . GLY A 1 52 ? 29.144 -37.443 10.003 1.00 29.11 ? 52 GLY A N 1 ATOM 390 C CA . GLY A 1 52 ? 28.206 -36.441 10.507 1.00 30.54 ? 52 GLY A CA 1 ATOM 391 C C . GLY A 1 52 ? 28.788 -35.745 11.722 1.00 31.41 ? 52 GLY A C 1 ATOM 392 O O . GLY A 1 52 ? 29.889 -35.177 11.652 1.00 31.13 ? 52 GLY A O 1 ATOM 393 N N . GLN A 1 53 ? 28.075 -35.814 12.845 1.00 32.67 ? 53 GLN A N 1 ATOM 394 C CA . GLN A 1 53 ? 28.534 -35.188 14.093 1.00 33.64 ? 53 GLN A CA 1 ATOM 395 C C . GLN A 1 53 ? 29.621 -35.981 14.827 1.00 32.72 ? 53 GLN A C 1 ATOM 396 O O . GLN A 1 53 ? 30.225 -35.474 15.770 1.00 33.02 ? 53 GLN A O 1 ATOM 397 C CB . GLN A 1 53 ? 27.356 -34.959 15.026 1.00 35.66 ? 53 GLN A CB 1 ATOM 398 C CG . GLN A 1 53 ? 26.390 -33.915 14.511 1.00 37.20 ? 53 GLN A CG 1 ATOM 399 C CD . GLN A 1 53 ? 25.184 -33.775 15.401 1.00 39.31 ? 53 GLN A CD 1 ATOM 400 O OE1 . GLN A 1 53 ? 24.145 -34.375 15.144 1.00 39.98 ? 53 GLN A OE1 1 ATOM 401 N NE2 . GLN A 1 53 ? 25.317 -32.995 16.469 1.00 40.79 ? 53 GLN A NE2 1 ATOM 402 N N . CYS A 1 54 ? 29.847 -37.227 14.419 1.00 31.46 ? 54 CYS A N 1 ATOM 403 C CA . CYS A 1 54 ? 30.936 -38.024 14.986 1.00 30.95 ? 54 CYS A CA 1 ATOM 404 C C . CYS A 1 54 ? 32.286 -37.601 14.400 1.00 30.14 ? 54 CYS A C 1 ATOM 405 O O . CYS A 1 54 ? 32.461 -37.556 13.185 1.00 29.36 ? 54 CYS A O 1 ATOM 406 C CB . CYS A 1 54 ? 30.724 -39.509 14.714 1.00 30.28 ? 54 CYS A CB 1 ATOM 407 S SG . CYS A 1 54 ? 32.054 -40.575 15.322 1.00 29.90 ? 54 CYS A SG 1 ATOM 408 N N . GLY A 1 55 ? 33.238 -37.289 15.269 1.00 30.48 ? 55 GLY A N 1 ATOM 409 C CA . GLY A 1 55 ? 34.612 -37.048 14.839 1.00 29.82 ? 55 GLY A CA 1 ATOM 410 C C . GLY A 1 55 ? 35.269 -38.387 14.588 1.00 28.84 ? 55 GLY A C 1 ATOM 411 O O . GLY A 1 55 ? 34.965 -39.368 15.272 1.00 29.12 ? 55 GLY A O 1 ATOM 412 N N . LEU A 1 56 ? 36.161 -38.439 13.605 1.00 27.73 ? 56 LEU A N 1 ATOM 413 C CA . LEU A 1 56 ? 36.807 -39.696 13.226 1.00 26.84 ? 56 LEU A CA 1 ATOM 414 C C . LEU A 1 56 ? 37.603 -40.336 14.368 1.00 27.33 ? 56 LEU A C 1 ATOM 415 O O . LEU A 1 56 ? 37.584 -41.559 14.532 1.00 27.09 ? 56 LEU A O 1 ATOM 416 C CB . LEU A 1 56 ? 37.723 -39.467 12.022 1.00 26.09 ? 56 LEU A CB 1 ATOM 417 C CG . LEU A 1 56 ? 38.554 -40.636 11.499 1.00 25.46 ? 56 LEU A CG 1 ATOM 418 C CD1 . LEU A 1 56 ? 37.669 -41.802 11.089 1.00 25.01 ? 56 LEU A CD1 1 ATOM 419 C CD2 . LEU A 1 56 ? 39.392 -40.169 10.320 1.00 24.91 ? 56 LEU A CD2 1 ATOM 420 N N . LEU A 1 57 ? 38.320 -39.522 15.140 1.00 28.08 ? 57 LEU A N 1 ATOM 421 C CA . LEU A 1 57 ? 39.048 -40.035 16.312 1.00 28.91 ? 57 LEU A CA 1 ATOM 422 C C . LEU A 1 57 ? 38.096 -40.446 17.444 1.00 29.50 ? 57 LEU A C 1 ATOM 423 O O . LEU A 1 57 ? 38.445 -41.277 18.287 1.00 30.04 ? 57 LEU A O 1 ATOM 424 C CB . LEU A 1 57 ? 40.061 -39.028 16.833 1.00 29.84 ? 57 LEU A CB 1 ATOM 425 C CG . LEU A 1 57 ? 41.122 -38.536 15.855 1.00 29.54 ? 57 LEU A CG 1 ATOM 426 C CD1 . LEU A 1 57 ? 42.092 -37.621 16.581 1.00 30.81 ? 57 LEU A CD1 1 ATOM 427 C CD2 . LEU A 1 57 ? 41.868 -39.700 15.209 1.00 28.87 ? 57 LEU A CD2 1 ATOM 428 N N . GLY A 1 58 ? 36.899 -39.873 17.454 1.00 29.49 ? 58 GLY A N 1 ATOM 429 C CA . GLY A 1 58 ? 35.857 -40.288 18.389 1.00 30.20 ? 58 GLY A CA 1 ATOM 430 C C . GLY A 1 58 ? 35.329 -41.706 18.174 1.00 29.66 ? 58 GLY A C 1 ATOM 431 O O . GLY A 1 58 ? 34.758 -42.289 19.079 1.00 30.36 ? 58 GLY A O 1 ATOM 432 N N . THR A 1 59 ? 35.530 -42.273 16.985 1.00 28.63 ? 59 THR A N 1 ATOM 433 C CA . THR A 1 59 ? 35.167 -43.672 16.743 1.00 28.32 ? 59 THR A CA 1 ATOM 434 C C . THR A 1 59 ? 36.016 -44.631 17.577 1.00 29.13 ? 59 THR A C 1 ATOM 435 O O . THR A 1 59 ? 35.597 -45.758 17.840 1.00 29.41 ? 59 THR A O 1 ATOM 436 C CB . THR A 1 59 ? 35.277 -44.089 15.256 1.00 27.11 ? 59 THR A CB 1 ATOM 437 O OG1 . THR A 1 59 ? 36.650 -44.165 14.857 1.00 26.70 ? 59 THR A OG1 1 ATOM 438 C CG2 . THR A 1 59 ? 34.525 -43.131 14.352 1.00 26.57 ? 59 THR A CG2 1 ATOM 439 N N . ILE A 1 60 ? 37.198 -44.189 18.002 1.00 29.77 ? 60 ILE A N 1 ATOM 440 C CA . ILE A 1 60 ? 38.065 -45.013 18.842 1.00 30.81 ? 60 ILE A CA 1 ATOM 441 C C . ILE A 1 60 ? 37.744 -44.914 20.341 1.00 32.25 ? 60 ILE A C 1 ATOM 442 O O . ILE A 1 60 ? 37.962 -45.874 21.082 1.00 33.17 ? 60 ILE A O 1 ATOM 443 C CB . ILE A 1 60 ? 39.547 -44.660 18.629 1.00 30.97 ? 60 ILE A CB 1 ATOM 444 C CG1 . ILE A 1 60 ? 39.913 -44.744 17.148 1.00 29.87 ? 60 ILE A CG1 1 ATOM 445 C CG2 . ILE A 1 60 ? 40.433 -45.598 19.431 1.00 32.04 ? 60 ILE A CG2 1 ATOM 446 C CD1 . ILE A 1 60 ? 39.609 -46.086 16.513 1.00 29.36 ? 60 ILE A CD1 1 ATOM 447 N N . THR A 1 61 ? 37.228 -43.769 20.782 1.00 32.68 ? 61 THR A N 1 ATOM 448 C CA . THR A 1 61 ? 36.993 -43.519 22.203 1.00 34.11 ? 61 THR A CA 1 ATOM 449 C C . THR A 1 61 ? 35.517 -43.591 22.558 1.00 34.46 ? 61 THR A C 1 ATOM 450 O O . THR A 1 61 ? 35.157 -44.053 23.643 1.00 35.53 ? 61 THR A O 1 ATOM 451 C CB . THR A 1 61 ? 37.561 -42.152 22.623 1.00 34.82 ? 61 THR A CB 1 ATOM 452 O OG1 . THR A 1 61 ? 37.031 -41.125 21.776 1.00 34.16 ? 61 THR A OG1 1 ATOM 453 C CG2 . THR A 1 61 ? 39.078 -42.164 22.509 1.00 34.97 ? 61 THR A CG2 1 ATOM 454 N N . GLY A 1 62 ? 34.665 -43.128 21.648 1.00 33.71 ? 62 GLY A N 1 ATOM 455 C CA . GLY A 1 62 ? 33.222 -43.310 21.770 1.00 33.90 ? 62 GLY A CA 1 ATOM 456 C C . GLY A 1 62 ? 32.474 -42.308 22.625 1.00 34.98 ? 62 GLY A C 1 ATOM 457 O O . GLY A 1 62 ? 31.837 -42.688 23.610 1.00 36.10 ? 62 GLY A O 1 ATOM 458 N N . PRO A 1 63 ? 32.534 -41.015 22.260 1.00 34.91 ? 63 PRO A N 1 ATOM 459 C CA . PRO A 1 63 ? 31.588 -40.069 22.843 1.00 35.89 ? 63 PRO A CA 1 ATOM 460 C C . PRO A 1 63 ? 30.188 -40.328 22.276 1.00 35.66 ? 63 PRO A C 1 ATOM 461 O O . PRO A 1 63 ? 30.066 -40.978 21.245 1.00 34.54 ? 63 PRO A O 1 ATOM 462 C CB . PRO A 1 63 ? 32.130 -38.712 22.395 1.00 35.88 ? 63 PRO A CB 1 ATOM 463 C CG . PRO A 1 63 ? 32.877 -38.998 21.138 1.00 34.41 ? 63 PRO A CG 1 ATOM 464 C CD . PRO A 1 63 ? 33.457 -40.367 21.313 1.00 34.00 ? 63 PRO A CD 1 ATOM 465 N N . PRO A 1 64 ? 29.131 -39.821 22.935 1.00 36.88 ? 64 PRO A N 1 ATOM 466 C CA . PRO A 1 64 ? 27.763 -40.211 22.536 1.00 36.96 ? 64 PRO A CA 1 ATOM 467 C C . PRO A 1 64 ? 27.439 -40.011 21.040 1.00 35.84 ? 64 PRO A C 1 ATOM 468 O O . PRO A 1 64 ? 26.764 -40.848 20.437 1.00 35.23 ? 64 PRO A O 1 ATOM 469 C CB . PRO A 1 64 ? 26.868 -39.337 23.416 1.00 38.60 ? 64 PRO A CB 1 ATOM 470 C CG . PRO A 1 64 ? 27.735 -38.890 24.551 1.00 39.48 ? 64 PRO A CG 1 ATOM 471 C CD . PRO A 1 64 ? 29.136 -38.824 24.018 1.00 38.36 ? 64 PRO A CD 1 ATOM 472 N N . GLN A 1 65 ? 27.936 -38.924 20.450 1.00 35.51 ? 65 GLN A N 1 ATOM 473 C CA . GLN A 1 65 ? 27.743 -38.663 19.019 1.00 34.58 ? 65 GLN A CA 1 ATOM 474 C C . GLN A 1 65 ? 28.342 -39.764 18.116 1.00 33.23 ? 65 GLN A C 1 ATOM 475 O O . GLN A 1 65 ? 27.956 -39.886 16.958 1.00 32.60 ? 65 GLN A O 1 ATOM 476 C CB . GLN A 1 65 ? 28.310 -37.284 18.628 1.00 34.55 ? 65 GLN A CB 1 ATOM 477 C CG . GLN A 1 65 ? 29.825 -37.160 18.730 1.00 34.00 ? 65 GLN A CG 1 ATOM 478 C CD . GLN A 1 65 ? 30.308 -36.514 20.021 1.00 35.29 ? 65 GLN A CD 1 ATOM 479 O OE1 . GLN A 1 65 ? 29.619 -36.527 21.038 1.00 36.49 ? 65 GLN A OE1 1 ATOM 480 N NE2 . GLN A 1 65 ? 31.516 -35.951 19.982 1.00 35.20 ? 65 GLN A NE2 1 ATOM 481 N N . CYS A 1 66 ? 29.283 -40.542 18.648 1.00 33.05 ? 66 CYS A N 1 ATOM 482 C CA . CYS A 1 66 ? 29.928 -41.629 17.910 1.00 32.16 ? 66 CYS A CA 1 ATOM 483 C C . CYS A 1 66 ? 29.430 -43.045 18.289 1.00 32.61 ? 66 CYS A C 1 ATOM 484 O O . CYS A 1 66 ? 30.046 -44.035 17.914 1.00 31.74 ? 66 CYS A O 1 ATOM 485 C CB . CYS A 1 66 ? 31.441 -41.541 18.128 1.00 31.83 ? 66 CYS A CB 1 ATOM 486 S SG . CYS A 1 66 ? 32.201 -40.114 17.323 1.00 31.41 ? 66 CYS A SG 1 ATOM 487 N N . ASP A 1 67 ? 28.313 -43.142 19.006 1.00 34.02 ? 67 ASP A N 1 ATOM 488 C CA . ASP A 1 67 ? 27.836 -44.445 19.495 1.00 34.89 ? 67 ASP A CA 1 ATOM 489 C C . ASP A 1 67 ? 27.535 -45.425 18.367 1.00 34.27 ? 67 ASP A C 1 ATOM 490 O O . ASP A 1 67 ? 27.774 -46.616 18.511 1.00 34.49 ? 67 ASP A O 1 ATOM 491 C CB . ASP A 1 67 ? 26.612 -44.290 20.414 1.00 36.36 ? 67 ASP A CB 1 ATOM 492 C CG . ASP A 1 67 ? 26.997 -44.035 21.864 1.00 37.55 ? 67 ASP A CG 1 ATOM 493 O OD1 . ASP A 1 67 ? 28.107 -44.462 22.266 1.00 37.42 ? 67 ASP A OD1 1 ATOM 494 O OD2 . ASP A 1 67 ? 26.192 -43.412 22.606 1.00 38.77 ? 67 ASP A OD2 1 ATOM 495 N N . GLN A 1 68 ? 27.058 -44.917 17.237 1.00 33.95 ? 68 GLN A N 1 ATOM 496 C CA . GLN A 1 68 ? 26.730 -45.767 16.096 1.00 33.65 ? 68 GLN A CA 1 ATOM 497 C C . GLN A 1 68 ? 27.916 -45.998 15.141 1.00 32.21 ? 68 GLN A C 1 ATOM 498 O O . GLN A 1 68 ? 27.731 -46.556 14.065 1.00 31.46 ? 68 GLN A O 1 ATOM 499 C CB . GLN A 1 68 ? 25.532 -45.178 15.331 1.00 34.23 ? 68 GLN A CB 1 ATOM 500 C CG . GLN A 1 68 ? 24.302 -44.917 16.193 1.00 35.99 ? 68 GLN A CG 1 ATOM 501 C CD . GLN A 1 68 ? 23.763 -46.173 16.859 1.00 37.19 ? 68 GLN A CD 1 ATOM 502 O OE1 . GLN A 1 68 ? 23.537 -46.201 18.072 1.00 38.48 ? 68 GLN A OE1 1 ATOM 503 N NE2 . GLN A 1 68 ? 23.564 -47.228 16.069 1.00 37.34 ? 68 GLN A NE2 1 ATOM 504 N N . PHE A 1 69 ? 29.121 -45.591 15.542 1.00 31.86 ? 69 PHE A N 1 ATOM 505 C CA . PHE A 1 69 ? 30.323 -45.705 14.690 1.00 30.98 ? 69 PHE A CA 1 ATOM 506 C C . PHE A 1 69 ? 31.479 -46.461 15.354 1.00 31.18 ? 69 PHE A C 1 ATOM 507 O O . PHE A 1 69 ? 32.610 -46.419 14.881 1.00 30.69 ? 69 PHE A O 1 ATOM 508 C CB . PHE A 1 69 ? 30.797 -44.303 14.282 1.00 30.39 ? 69 PHE A CB 1 ATOM 509 C CG . PHE A 1 69 ? 29.759 -43.512 13.539 1.00 30.40 ? 69 PHE A CG 1 ATOM 510 C CD1 . PHE A 1 69 ? 28.823 -42.771 14.220 1.00 31.42 ? 69 PHE A CD1 1 ATOM 511 C CD2 . PHE A 1 69 ? 29.704 -43.542 12.157 1.00 29.74 ? 69 PHE A CD2 1 ATOM 512 C CE1 . PHE A 1 69 ? 27.848 -42.056 13.541 1.00 31.78 ? 69 PHE A CE1 1 ATOM 513 C CE2 . PHE A 1 69 ? 28.737 -42.832 11.467 1.00 29.99 ? 69 PHE A CE2 1 ATOM 514 C CZ . PHE A 1 69 ? 27.807 -42.086 12.159 1.00 30.99 ? 69 PHE A CZ 1 ATOM 515 N N . LEU A 1 70 ? 31.196 -47.155 16.444 1.00 32.31 ? 70 LEU A N 1 ATOM 516 C CA . LEU A 1 70 ? 32.238 -47.801 17.231 1.00 32.87 ? 70 LEU A CA 1 ATOM 517 C C . LEU A 1 70 ? 32.899 -48.968 16.495 1.00 33.00 ? 70 LEU A C 1 ATOM 518 O O . LEU A 1 70 ? 34.041 -49.317 16.803 1.00 33.06 ? 70 LEU A O 1 ATOM 519 C CB . LEU A 1 70 ? 31.673 -48.271 18.576 1.00 33.96 ? 70 LEU A CB 1 ATOM 520 C CG . LEU A 1 70 ? 31.721 -47.336 19.793 1.00 34.67 ? 70 LEU A CG 1 ATOM 521 C CD1 . LEU A 1 70 ? 31.810 -45.862 19.440 1.00 34.25 ? 70 LEU A CD1 1 ATOM 522 C CD2 . LEU A 1 70 ? 30.506 -47.585 20.676 1.00 35.77 ? 70 LEU A CD2 1 ATOM 523 N N . GLU A 1 71 ? 32.199 -49.562 15.527 1.00 33.27 ? 71 GLU A N 1 ATOM 524 C CA . GLU A 1 71 ? 32.757 -50.680 14.766 1.00 33.66 ? 71 GLU A CA 1 ATOM 525 C C . GLU A 1 71 ? 32.388 -50.637 13.285 1.00 33.24 ? 71 GLU A C 1 ATOM 526 O O . GLU A 1 71 ? 32.111 -51.660 12.661 1.00 34.04 ? 71 GLU A O 1 ATOM 527 C CB . GLU A 1 71 ? 32.331 -52.007 15.394 1.00 34.87 ? 71 GLU A CB 1 ATOM 528 C CG . GLU A 1 71 ? 33.131 -52.356 16.633 1.00 35.98 ? 71 GLU A CG 1 ATOM 529 C CD . GLU A 1 71 ? 32.836 -53.752 17.128 1.00 37.50 ? 71 GLU A CD 1 ATOM 530 O OE1 . GLU A 1 71 ? 31.768 -53.945 17.742 1.00 38.91 ? 71 GLU A OE1 1 ATOM 531 O OE2 . GLU A 1 71 ? 33.658 -54.660 16.879 1.00 37.92 ? 71 GLU A OE2 1 ATOM 532 N N . PHE A 1 72 ? 32.435 -49.450 12.712 1.00 32.72 ? 72 PHE A N 1 ATOM 533 C CA . PHE A 1 72 ? 32.027 -49.267 11.334 1.00 32.15 ? 72 PHE A CA 1 ATOM 534 C C . PHE A 1 72 ? 32.947 -49.981 10.334 1.00 31.89 ? 72 PHE A C 1 ATOM 535 O O . PHE A 1 72 ? 34.113 -50.289 10.619 1.00 32.16 ? 72 PHE A O 1 ATOM 536 C CB . PHE A 1 72 ? 31.920 -47.778 11.012 1.00 31.52 ? 72 PHE A CB 1 ATOM 537 C CG . PHE A 1 72 ? 33.239 -47.097 10.820 1.00 30.99 ? 72 PHE A CG 1 ATOM 538 C CD1 . PHE A 1 72 ? 33.826 -47.050 9.569 1.00 30.05 ? 72 PHE A CD1 1 ATOM 539 C CD2 . PHE A 1 72 ? 33.877 -46.477 11.882 1.00 31.28 ? 72 PHE A CD2 1 ATOM 540 C CE1 . PHE A 1 72 ? 35.033 -46.414 9.382 1.00 29.71 ? 72 PHE A CE1 1 ATOM 541 C CE2 . PHE A 1 72 ? 35.087 -45.839 11.707 1.00 30.88 ? 72 PHE A CE2 1 ATOM 542 C CZ . PHE A 1 72 ? 35.669 -45.805 10.451 1.00 30.24 ? 72 PHE A CZ 1 ATOM 543 N N . SER A 1 73 ? 32.383 -50.242 9.162 1.00 31.54 ? 73 SER A N 1 ATOM 544 C CA . SER A 1 73 ? 33.069 -50.844 8.038 1.00 30.68 ? 73 SER A CA 1 ATOM 545 C C . SER A 1 73 ? 32.823 -49.957 6.818 1.00 29.29 ? 73 SER A C 1 ATOM 546 O O . SER A 1 73 ? 31.719 -49.468 6.636 1.00 29.41 ? 73 SER A O 1 ATOM 547 C CB . SER A 1 73 ? 32.495 -52.233 7.813 1.00 31.67 ? 73 SER A CB 1 ATOM 548 O OG . SER A 1 73 ? 33.322 -52.987 6.958 1.00 32.03 ? 73 SER A OG 1 ATOM 549 N N . ALA A 1 74 ? 33.841 -49.743 5.989 1.00 28.09 ? 74 ALA A N 1 ATOM 550 C CA . ALA A 1 74 ? 33.753 -48.752 4.918 1.00 27.05 ? 74 ALA A CA 1 ATOM 551 C C . ALA A 1 74 ? 34.810 -48.888 3.813 1.00 26.17 ? 74 ALA A C 1 ATOM 552 O O . ALA A 1 74 ? 35.924 -49.349 4.057 1.00 26.14 ? 74 ALA A O 1 ATOM 553 C CB . ALA A 1 74 ? 33.846 -47.360 5.522 1.00 26.82 ? 74 ALA A CB 1 ATOM 554 N N . ASP A 1 75 ? 34.428 -48.487 2.601 1.00 25.35 ? 75 ASP A N 1 ATOM 555 C CA . ASP A 1 75 ? 35.356 -48.213 1.508 1.00 24.54 ? 75 ASP A CA 1 ATOM 556 C C . ASP A 1 75 ? 35.652 -46.706 1.454 1.00 23.63 ? 75 ASP A C 1 ATOM 557 O O . ASP A 1 75 ? 36.719 -46.280 1.010 1.00 23.12 ? 75 ASP A O 1 ATOM 558 C CB . ASP A 1 75 ? 34.747 -48.614 0.158 1.00 24.79 ? 75 ASP A CB 1 ATOM 559 C CG . ASP A 1 75 ? 34.395 -50.082 0.080 1.00 25.83 ? 75 ASP A CG 1 ATOM 560 O OD1 . ASP A 1 75 ? 35.212 -50.917 0.510 1.00 26.44 ? 75 ASP A OD1 1 ATOM 561 O OD2 . ASP A 1 75 ? 33.304 -50.413 -0.443 1.00 26.57 ? 75 ASP A OD2 1 ATOM 562 N N . LEU A 1 76 ? 34.683 -45.906 1.879 1.00 23.44 ? 76 LEU A N 1 ATOM 563 C CA . LEU A 1 76 ? 34.779 -44.470 1.802 1.00 23.08 ? 76 LEU A CA 1 ATOM 564 C C . LEU A 1 76 ? 34.294 -43.883 3.125 1.00 23.47 ? 76 LEU A C 1 ATOM 565 O O . LEU A 1 76 ? 33.214 -44.229 3.619 1.00 24.12 ? 76 LEU A O 1 ATOM 566 C CB . LEU A 1 76 ? 33.957 -43.963 0.623 1.00 23.02 ? 76 LEU A CB 1 ATOM 567 C CG . LEU A 1 76 ? 33.900 -42.462 0.380 1.00 23.05 ? 76 LEU A CG 1 ATOM 568 C CD1 . LEU A 1 76 ? 35.252 -41.938 -0.089 1.00 22.53 ? 76 LEU A CD1 1 ATOM 569 C CD2 . LEU A 1 76 ? 32.810 -42.142 -0.637 1.00 23.37 ? 76 LEU A CD2 1 ATOM 570 N N . ILE A 1 77 ? 35.106 -43.009 3.702 1.00 23.16 ? 77 ILE A N 1 ATOM 571 C CA . ILE A 1 77 ? 34.802 -42.392 4.981 1.00 23.58 ? 77 ILE A CA 1 ATOM 572 C C . ILE A 1 77 ? 34.735 -40.891 4.768 1.00 23.73 ? 77 ILE A C 1 ATOM 573 O O . ILE A 1 77 ? 35.667 -40.315 4.202 1.00 23.70 ? 77 ILE A O 1 ATOM 574 C CB . ILE A 1 77 ? 35.883 -42.758 6.024 1.00 23.61 ? 77 ILE A CB 1 ATOM 575 C CG1 . ILE A 1 77 ? 36.028 -44.291 6.095 1.00 23.58 ? 77 ILE A CG1 1 ATOM 576 C CG2 . ILE A 1 77 ? 35.525 -42.205 7.394 1.00 24.23 ? 77 ILE A CG2 1 ATOM 577 C CD1 . ILE A 1 77 ? 37.053 -44.795 7.084 1.00 23.85 ? 77 ILE A CD1 1 ATOM 578 N N . ILE A 1 78 ? 33.645 -40.266 5.217 1.00 24.39 ? 78 ILE A N 1 ATOM 579 C CA . ILE A 1 78 ? 33.433 -38.835 5.050 1.00 24.78 ? 78 ILE A CA 1 ATOM 580 C C . ILE A 1 78 ? 33.437 -38.078 6.390 1.00 25.71 ? 78 ILE A C 1 ATOM 581 O O . ILE A 1 78 ? 32.575 -38.293 7.242 1.00 26.22 ? 78 ILE A O 1 ATOM 582 C CB . ILE A 1 78 ? 32.097 -38.539 4.332 1.00 25.11 ? 78 ILE A CB 1 ATOM 583 C CG1 . ILE A 1 78 ? 31.980 -39.337 3.027 1.00 24.58 ? 78 ILE A CG1 1 ATOM 584 C CG2 . ILE A 1 78 ? 31.975 -37.051 4.041 1.00 25.56 ? 78 ILE A CG2 1 ATOM 585 C CD1 . ILE A 1 78 ? 30.592 -39.314 2.426 1.00 25.28 ? 78 ILE A CD1 1 ATOM 586 N N . GLU A 1 79 ? 34.392 -37.166 6.546 1.00 25.98 ? 79 GLU A N 1 ATOM 587 C CA . GLU A 1 79 ? 34.460 -36.291 7.711 1.00 27.14 ? 79 GLU A CA 1 ATOM 588 C C . GLU A 1 79 ? 33.702 -35.011 7.406 1.00 27.79 ? 79 GLU A C 1 ATOM 589 O O . GLU A 1 79 ? 33.779 -34.485 6.296 1.00 27.29 ? 79 GLU A O 1 ATOM 590 C CB . GLU A 1 79 ? 35.907 -35.921 8.042 1.00 27.51 ? 79 GLU A CB 1 ATOM 591 C CG . GLU A 1 79 ? 36.788 -37.063 8.527 1.00 27.49 ? 79 GLU A CG 1 ATOM 592 C CD . GLU A 1 79 ? 38.206 -36.584 8.863 1.00 28.09 ? 79 GLU A CD 1 ATOM 593 O OE1 . GLU A 1 79 ? 39.038 -36.383 7.939 1.00 27.63 ? 79 GLU A OE1 1 ATOM 594 O OE2 . GLU A 1 79 ? 38.481 -36.387 10.066 1.00 29.13 ? 79 GLU A OE2 1 ATOM 595 N N . ARG A 1 80 ? 32.991 -34.508 8.404 1.00 28.92 ? 80 ARG A N 1 ATOM 596 C CA . ARG A 1 80 ? 32.181 -33.307 8.253 1.00 30.22 ? 80 ARG A CA 1 ATOM 597 C C . ARG A 1 80 ? 32.681 -32.230 9.200 1.00 31.84 ? 80 ARG A C 1 ATOM 598 O O . ARG A 1 80 ? 33.244 -32.541 10.243 1.00 32.14 ? 80 ARG A O 1 ATOM 599 C CB . ARG A 1 80 ? 30.714 -33.618 8.571 1.00 30.63 ? 80 ARG A CB 1 ATOM 600 C CG . ARG A 1 80 ? 30.109 -34.741 7.736 1.00 29.73 ? 80 ARG A CG 1 ATOM 601 C CD . ARG A 1 80 ? 30.065 -34.351 6.272 1.00 29.20 ? 80 ARG A CD 1 ATOM 602 N NE . ARG A 1 80 ? 29.145 -35.161 5.486 1.00 28.83 ? 80 ARG A NE 1 ATOM 603 C CZ . ARG A 1 80 ? 28.912 -34.978 4.190 1.00 28.61 ? 80 ARG A CZ 1 ATOM 604 N NH1 . ARG A 1 80 ? 29.507 -33.998 3.517 1.00 28.62 ? 80 ARG A NH1 1 ATOM 605 N NH2 . ARG A 1 80 ? 28.055 -35.758 3.564 1.00 28.76 ? 80 ARG A NH2 1 ATOM 606 N N . ARG A 1 81 ? 32.455 -30.967 8.846 1.00 33.33 ? 81 ARG A N 1 ATOM 607 C CA . ARG A 1 81 ? 32.870 -29.853 9.692 1.00 35.35 ? 81 ARG A CA 1 ATOM 608 C C . ARG A 1 81 ? 32.245 -29.912 11.096 1.00 36.22 ? 81 ARG A C 1 ATOM 609 O O . ARG A 1 81 ? 32.892 -29.575 12.087 1.00 36.66 ? 81 ARG A O 1 ATOM 610 C CB . ARG A 1 81 ? 32.521 -28.521 9.029 1.00 37.15 ? 81 ARG A CB 1 ATOM 611 C CG . ARG A 1 81 ? 33.555 -27.449 9.282 1.00 39.05 ? 81 ARG A CG 1 ATOM 612 C CD . ARG A 1 81 ? 33.241 -26.155 8.539 1.00 41.05 ? 81 ARG A CD 1 ATOM 613 N NE . ARG A 1 81 ? 34.467 -25.549 8.013 1.00 42.14 ? 81 ARG A NE 1 ATOM 614 C CZ . ARG A 1 81 ? 34.914 -25.666 6.761 1.00 42.03 ? 81 ARG A CZ 1 ATOM 615 N NH1 . ARG A 1 81 ? 34.235 -26.354 5.846 1.00 41.60 ? 81 ARG A NH1 1 ATOM 616 N NH2 . ARG A 1 81 ? 36.051 -25.069 6.408 1.00 42.64 ? 81 ARG A NH2 1 ATOM 617 N N . GLU A 1 82 ? 30.993 -30.350 11.175 1.00 36.52 ? 82 GLU A N 1 ATOM 618 C CA . GLU A 1 82 ? 30.295 -30.464 12.460 1.00 37.72 ? 82 GLU A CA 1 ATOM 619 C C . GLU A 1 82 ? 30.786 -31.633 13.328 1.00 36.99 ? 82 GLU A C 1 ATOM 620 O O . GLU A 1 82 ? 30.298 -31.820 14.439 1.00 38.04 ? 82 GLU A O 1 ATOM 621 C CB . GLU A 1 82 ? 28.764 -30.550 12.258 1.00 38.56 ? 82 GLU A CB 1 ATOM 622 C CG . GLU A 1 82 ? 28.212 -31.857 11.670 1.00 37.80 ? 82 GLU A CG 1 ATOM 623 C CD . GLU A 1 82 ? 28.122 -31.872 10.147 1.00 37.35 ? 82 GLU A CD 1 ATOM 624 O OE1 . GLU A 1 82 ? 28.725 -30.977 9.500 1.00 37.85 ? 82 GLU A OE1 1 ATOM 625 O OE2 . GLU A 1 82 ? 27.458 -32.791 9.591 1.00 37.08 ? 82 GLU A OE2 1 ATOM 626 N N . GLY A 1 83 ? 31.734 -32.427 12.832 1.00 35.63 ? 83 GLY A N 1 ATOM 627 C CA . GLY A 1 83 ? 32.254 -33.557 13.602 1.00 35.06 ? 83 GLY A CA 1 ATOM 628 C C . GLY A 1 83 ? 32.978 -33.113 14.858 1.00 35.97 ? 83 GLY A C 1 ATOM 629 O O . GLY A 1 83 ? 33.627 -32.079 14.857 1.00 37.05 ? 83 GLY A O 1 ATOM 630 N N . SER A 1 84 ? 32.852 -33.883 15.935 1.00 36.07 ? 84 SER A N 1 ATOM 631 C CA . SER A 1 84 ? 33.624 -33.656 17.158 1.00 36.70 ? 84 SER A CA 1 ATOM 632 C C . SER A 1 84 ? 34.136 -34.982 17.701 1.00 36.09 ? 84 SER A C 1 ATOM 633 O O . SER A 1 84 ? 33.379 -35.944 17.804 1.00 35.53 ? 84 SER A O 1 ATOM 634 C CB . SER A 1 84 ? 32.785 -32.958 18.225 1.00 38.32 ? 84 SER A CB 1 ATOM 635 O OG . SER A 1 84 ? 33.511 -32.861 19.442 1.00 39.29 ? 84 SER A OG 1 ATOM 636 N N . ASP A 1 85 ? 35.425 -35.010 18.042 1.00 36.34 ? 85 ASP A N 1 ATOM 637 C CA . ASP A 1 85 ? 36.096 -36.196 18.574 1.00 36.14 ? 85 ASP A CA 1 ATOM 638 C C . ASP A 1 85 ? 35.832 -36.394 20.047 1.00 37.46 ? 85 ASP A C 1 ATOM 639 O O . ASP A 1 85 ? 36.090 -37.475 20.569 1.00 37.66 ? 85 ASP A O 1 ATOM 640 C CB . ASP A 1 85 ? 37.618 -36.079 18.422 1.00 36.23 ? 85 ASP A CB 1 ATOM 641 C CG . ASP A 1 85 ? 38.071 -36.066 16.986 1.00 35.23 ? 85 ASP A CG 1 ATOM 642 O OD1 . ASP A 1 85 ? 37.614 -36.935 16.217 1.00 33.97 ? 85 ASP A OD1 1 ATOM 643 O OD2 . ASP A 1 85 ? 38.913 -35.201 16.638 1.00 35.75 ? 85 ASP A OD2 1 ATOM 644 N N . VAL A 1 86 ? 35.351 -35.358 20.727 1.00 38.74 ? 86 VAL A N 1 ATOM 645 C CA . VAL A 1 86 ? 35.303 -35.370 22.186 1.00 40.35 ? 86 VAL A CA 1 ATOM 646 C C . VAL A 1 86 ? 33.929 -35.028 22.730 1.00 41.29 ? 86 VAL A C 1 ATOM 647 O O . VAL A 1 86 ? 33.128 -34.376 22.067 1.00 41.09 ? 86 VAL A O 1 ATOM 648 C CB . VAL A 1 86 ? 36.340 -34.390 22.788 1.00 41.73 ? 86 VAL A CB 1 ATOM 649 C CG1 . VAL A 1 86 ? 37.750 -34.834 22.435 1.00 41.13 ? 86 VAL A CG1 1 ATOM 650 C CG2 . VAL A 1 86 ? 36.101 -32.953 22.321 1.00 42.28 ? 86 VAL A CG2 1 ATOM 651 N N . CYS A 1 87 ? 33.658 -35.507 23.937 1.00 42.69 ? 87 CYS A N 1 ATOM 652 C CA . CYS A 1 87 ? 32.517 -35.049 24.709 1.00 44.21 ? 87 CYS A CA 1 ATOM 653 C C . CYS A 1 87 ? 33.090 -34.245 25.861 1.00 46.03 ? 87 CYS A C 1 ATOM 654 O O . CYS A 1 87 ? 32.849 -33.038 25.951 1.00 46.92 ? 87 CYS A O 1 ATOM 655 C CB . CYS A 1 87 ? 31.630 -36.210 25.181 1.00 44.40 ? 87 CYS A CB 1 ATOM 656 S SG . CYS A 1 87 ? 32.420 -37.545 26.124 1.00 44.87 ? 87 CYS A SG 1 ATOM 657 N N . TYR A 1 88 ? 33.882 -34.892 26.717 1.00 46.50 ? 88 TYR A N 1 ATOM 658 C CA . TYR A 1 88 ? 34.645 -34.155 27.722 1.00 48.25 ? 88 TYR A CA 1 ATOM 659 C C . TYR A 1 88 ? 35.803 -33.469 27.004 1.00 48.05 ? 88 TYR A C 1 ATOM 660 O O . TYR A 1 88 ? 36.576 -34.144 26.310 1.00 47.06 ? 88 TYR A O 1 ATOM 661 C CB . TYR A 1 88 ? 35.179 -35.077 28.817 1.00 48.95 ? 88 TYR A CB 1 ATOM 662 C CG . TYR A 1 88 ? 35.700 -34.343 30.036 1.00 51.15 ? 88 TYR A CG 1 ATOM 663 C CD1 . TYR A 1 88 ? 34.856 -34.023 31.092 1.00 52.82 ? 88 TYR A CD1 1 ATOM 664 C CD2 . TYR A 1 88 ? 37.038 -33.966 30.136 1.00 51.85 ? 88 TYR A CD2 1 ATOM 665 C CE1 . TYR A 1 88 ? 35.323 -33.351 32.213 1.00 54.88 ? 88 TYR A CE1 1 ATOM 666 C CE2 . TYR A 1 88 ? 37.515 -33.292 31.251 1.00 53.90 ? 88 TYR A CE2 1 ATOM 667 C CZ . TYR A 1 88 ? 36.652 -32.990 32.287 1.00 55.45 ? 88 TYR A CZ 1 ATOM 668 O OH . TYR A 1 88 ? 37.104 -32.327 33.399 1.00 57.59 ? 88 TYR A OH 1 ATOM 669 N N . PRO A 1 89 ? 35.940 -32.136 27.166 1.00 49.34 ? 89 PRO A N 1 ATOM 670 C CA . PRO A 1 89 ? 36.957 -31.404 26.399 1.00 49.26 ? 89 PRO A CA 1 ATOM 671 C C . PRO A 1 89 ? 38.353 -32.010 26.544 1.00 49.32 ? 89 PRO A C 1 ATOM 672 O O . PRO A 1 89 ? 38.721 -32.474 27.619 1.00 50.34 ? 89 PRO A O 1 ATOM 673 C CB . PRO A 1 89 ? 36.895 -29.981 26.966 1.00 51.14 ? 89 PRO A CB 1 ATOM 674 C CG . PRO A 1 89 ? 36.169 -30.087 28.258 1.00 52.65 ? 89 PRO A CG 1 ATOM 675 C CD . PRO A 1 89 ? 35.257 -31.270 28.143 1.00 51.30 ? 89 PRO A CD 1 ATOM 676 N N . GLY A 1 90 ? 39.099 -32.028 25.446 1.00 48.49 ? 90 GLY A N 1 ATOM 677 C CA . GLY A 1 90 ? 40.374 -32.739 25.382 1.00 48.38 ? 90 GLY A CA 1 ATOM 678 C C . GLY A 1 90 ? 40.866 -32.835 23.949 1.00 46.96 ? 90 GLY A C 1 ATOM 679 O O . GLY A 1 90 ? 40.177 -32.407 23.027 1.00 46.05 ? 90 GLY A O 1 ATOM 680 N N . LYS A 1 91 ? 42.061 -33.377 23.749 1.00 47.06 ? 91 LYS A N 1 ATOM 681 C CA . LYS A 1 91 ? 42.528 -33.644 22.394 1.00 46.05 ? 91 LYS A CA 1 ATOM 682 C C . LYS A 1 91 ? 43.554 -34.770 22.372 1.00 45.82 ? 91 LYS A C 1 ATOM 683 O O . LYS A 1 91 ? 44.069 -35.161 23.421 1.00 47.45 ? 91 LYS A O 1 ATOM 684 C CB . LYS A 1 91 ? 43.075 -32.367 21.732 1.00 46.81 ? 91 LYS A CB 1 ATOM 685 C CG . LYS A 1 91 ? 44.496 -31.977 22.108 1.00 48.52 ? 91 LYS A CG 1 ATOM 686 C CD . LYS A 1 91 ? 44.810 -30.548 21.670 1.00 49.68 ? 91 LYS A CD 1 ATOM 687 C CE . LYS A 1 91 ? 44.890 -30.402 20.154 1.00 48.29 ? 91 LYS A CE 1 ATOM 688 N NZ . LYS A 1 91 ? 46.209 -30.841 19.609 1.00 48.34 ? 91 LYS A NZ 1 ATOM 689 N N . PHE A 1 92 ? 43.816 -35.288 21.172 1.00 44.23 ? 92 PHE A N 1 ATOM 690 C CA . PHE A 1 92 ? 44.777 -36.373 20.952 1.00 43.76 ? 92 PHE A CA 1 ATOM 691 C C . PHE A 1 92 ? 46.158 -35.842 20.666 1.00 44.56 ? 92 PHE A C 1 ATOM 692 O O . PHE A 1 92 ? 46.296 -34.857 19.956 1.00 44.48 ? 92 PHE A O 1 ATOM 693 C CB . PHE A 1 92 ? 44.382 -37.220 19.727 1.00 41.78 ? 92 PHE A CB 1 ATOM 694 C CG . PHE A 1 92 ? 43.359 -38.267 20.010 1.00 40.74 ? 92 PHE A CG 1 ATOM 695 C CD1 . PHE A 1 92 ? 42.011 -37.961 19.983 1.00 40.14 ? 92 PHE A CD1 1 ATOM 696 C CD2 . PHE A 1 92 ? 43.747 -39.568 20.287 1.00 40.68 ? 92 PHE A CD2 1 ATOM 697 C CE1 . PHE A 1 92 ? 41.061 -38.934 20.240 1.00 39.59 ? 92 PHE A CE1 1 ATOM 698 C CE2 . PHE A 1 92 ? 42.803 -40.542 20.551 1.00 40.15 ? 92 PHE A CE2 1 ATOM 699 C CZ . PHE A 1 92 ? 41.457 -40.223 20.522 1.00 39.50 ? 92 PHE A CZ 1 ATOM 700 N N . VAL A 1 93 ? 47.171 -36.539 21.177 1.00 45.82 ? 93 VAL A N 1 ATOM 701 C CA . VAL A 1 93 ? 48.564 -36.337 20.785 1.00 46.67 ? 93 VAL A CA 1 ATOM 702 C C . VAL A 1 93 ? 48.822 -37.139 19.510 1.00 45.22 ? 93 VAL A C 1 ATOM 703 O O . VAL A 1 93 ? 48.421 -38.297 19.421 1.00 44.27 ? 93 VAL A O 1 ATOM 704 C CB . VAL A 1 93 ? 49.519 -36.825 21.896 1.00 48.90 ? 93 VAL A CB 1 ATOM 705 C CG1 . VAL A 1 93 ? 50.977 -36.726 21.468 1.00 49.71 ? 93 VAL A CG1 1 ATOM 706 C CG2 . VAL A 1 93 ? 49.291 -36.037 23.183 1.00 50.87 ? 93 VAL A CG2 1 ATOM 707 N N . ASN A 1 94 ? 49.494 -36.530 18.532 1.00 45.34 ? 94 ASN A N 1 ATOM 708 C CA . ASN A 1 94 ? 49.738 -37.160 17.227 1.00 43.87 ? 94 ASN A CA 1 ATOM 709 C C . ASN A 1 94 ? 48.418 -37.420 16.508 1.00 41.54 ? 94 ASN A C 1 ATOM 710 O O . ASN A 1 94 ? 48.146 -38.535 16.050 1.00 40.33 ? 94 ASN A O 1 ATOM 711 C CB . ASN A 1 94 ? 50.529 -38.472 17.386 1.00 44.59 ? 94 ASN A CB 1 ATOM 712 C CG . ASN A 1 94 ? 51.949 -38.362 16.898 1.00 45.91 ? 94 ASN A CG 1 ATOM 713 O OD1 . ASN A 1 94 ? 52.802 -37.779 17.568 1.00 48.13 ? 94 ASN A OD1 1 ATOM 714 N ND2 . ASN A 1 94 ? 52.223 -38.945 15.734 1.00 45.05 ? 94 ASN A ND2 1 ATOM 715 N N . GLU A 1 95 ? 47.599 -36.383 16.405 1.00 40.99 ? 95 GLU A N 1 ATOM 716 C CA . GLU A 1 95 ? 46.219 -36.573 15.972 1.00 39.59 ? 95 GLU A CA 1 ATOM 717 C C . GLU A 1 95 ? 46.079 -36.816 14.476 1.00 37.30 ? 95 GLU A C 1 ATOM 718 O O . GLU A 1 95 ? 45.316 -37.683 14.064 1.00 36.06 ? 95 GLU A O 1 ATOM 719 C CB . GLU A 1 95 ? 45.318 -35.421 16.434 1.00 40.62 ? 95 GLU A CB 1 ATOM 720 C CG . GLU A 1 95 ? 45.642 -34.045 15.886 1.00 41.64 ? 95 GLU A CG 1 ATOM 721 C CD . GLU A 1 95 ? 44.793 -32.971 16.547 1.00 43.26 ? 95 GLU A CD 1 ATOM 722 O OE1 . GLU A 1 95 ? 45.206 -32.446 17.614 1.00 45.04 ? 95 GLU A OE1 1 ATOM 723 O OE2 . GLU A 1 95 ? 43.694 -32.676 16.019 1.00 42.82 ? 95 GLU A OE2 1 ATOM 724 N N . GLU A 1 96 ? 46.812 -36.061 13.670 1.00 36.55 ? 96 GLU A N 1 ATOM 725 C CA . GLU A 1 96 ? 46.680 -36.160 12.227 1.00 34.67 ? 96 GLU A CA 1 ATOM 726 C C . GLU A 1 96 ? 47.208 -37.481 11.681 1.00 33.51 ? 96 GLU A C 1 ATOM 727 O O . GLU A 1 96 ? 46.638 -38.030 10.745 1.00 31.91 ? 96 GLU A O 1 ATOM 728 C CB . GLU A 1 96 ? 47.366 -34.993 11.517 1.00 35.09 ? 96 GLU A CB 1 ATOM 729 C CG . GLU A 1 96 ? 46.894 -34.822 10.082 1.00 33.94 ? 96 GLU A CG 1 ATOM 730 C CD . GLU A 1 96 ? 45.393 -34.639 9.975 1.00 33.28 ? 96 GLU A CD 1 ATOM 731 O OE1 . GLU A 1 96 ? 44.776 -34.177 10.957 1.00 33.99 ? 96 GLU A OE1 1 ATOM 732 O OE2 . GLU A 1 96 ? 44.824 -34.958 8.909 1.00 32.63 ? 96 GLU A OE2 1 ATOM 733 N N . ALA A 1 97 ? 48.301 -37.968 12.262 1.00 34.10 ? 97 ALA A N 1 ATOM 734 C CA . ALA A 1 97 ? 48.820 -39.290 11.953 1.00 33.50 ? 97 ALA A CA 1 ATOM 735 C C . ALA A 1 97 ? 47.740 -40.365 12.182 1.00 32.44 ? 97 ALA A C 1 ATOM 736 O O . ALA A 1 97 ? 47.545 -41.241 11.350 1.00 31.49 ? 97 ALA A O 1 ATOM 737 C CB . ALA A 1 97 ? 50.044 -39.579 12.808 1.00 35.05 ? 97 ALA A CB 1 ATOM 738 N N . LEU A 1 98 ? 47.038 -40.272 13.309 1.00 32.58 ? 98 LEU A N 1 ATOM 739 C CA . LEU A 1 98 ? 45.976 -41.211 13.648 1.00 31.75 ? 98 LEU A CA 1 ATOM 740 C C . LEU A 1 98 ? 44.774 -41.105 12.697 1.00 30.18 ? 98 LEU A C 1 ATOM 741 O O . LEU A 1 98 ? 44.158 -42.117 12.368 1.00 29.25 ? 98 LEU A O 1 ATOM 742 C CB . LEU A 1 98 ? 45.524 -40.996 15.095 1.00 32.74 ? 98 LEU A CB 1 ATOM 743 C CG . LEU A 1 98 ? 44.470 -41.944 15.673 1.00 32.53 ? 98 LEU A CG 1 ATOM 744 C CD1 . LEU A 1 98 ? 44.897 -43.393 15.530 1.00 32.53 ? 98 LEU A CD1 1 ATOM 745 C CD2 . LEU A 1 98 ? 44.209 -41.615 17.136 1.00 33.79 ? 98 LEU A CD2 1 ATOM 746 N N . ARG A 1 99 ? 44.442 -39.888 12.263 1.00 29.62 ? 99 ARG A N 1 ATOM 747 C CA . ARG A 1 99 ? 43.363 -39.710 11.301 1.00 28.39 ? 99 ARG A CA 1 ATOM 748 C C . ARG A 1 99 ? 43.744 -40.359 9.982 1.00 27.47 ? 99 ARG A C 1 ATOM 749 O O . ARG A 1 99 ? 42.900 -40.946 9.305 1.00 26.74 ? 99 ARG A O 1 ATOM 750 C CB . ARG A 1 99 ? 43.047 -38.234 11.060 1.00 28.52 ? 99 ARG A CB 1 ATOM 751 C CG . ARG A 1 99 ? 42.476 -37.500 12.258 1.00 29.50 ? 99 ARG A CG 1 ATOM 752 C CD . ARG A 1 99 ? 41.658 -36.290 11.839 1.00 29.48 ? 99 ARG A CD 1 ATOM 753 N NE . ARG A 1 99 ? 41.095 -35.605 13.001 1.00 30.49 ? 99 ARG A NE 1 ATOM 754 C CZ . ARG A 1 99 ? 41.743 -34.724 13.757 1.00 31.71 ? 99 ARG A CZ 1 ATOM 755 N NH1 . ARG A 1 99 ? 43.002 -34.374 13.486 1.00 32.11 ? 99 ARG A NH1 1 ATOM 756 N NH2 . ARG A 1 99 ? 41.121 -34.183 14.794 1.00 32.64 ? 99 ARG A NH2 1 ATOM 757 N N . GLN A 1 100 ? 45.018 -40.256 9.621 1.00 27.56 ? 100 GLN A N 1 ATOM 758 C CA . GLN A 1 100 ? 45.483 -40.816 8.368 1.00 26.90 ? 100 GLN A CA 1 ATOM 759 C C . GLN A 1 100 ? 45.411 -42.338 8.392 1.00 26.69 ? 100 GLN A C 1 ATOM 760 O O . GLN A 1 100 ? 45.032 -42.958 7.404 1.00 25.89 ? 100 GLN A O 1 ATOM 761 C CB . GLN A 1 100 ? 46.885 -40.301 8.029 1.00 27.46 ? 100 GLN A CB 1 ATOM 762 C CG . GLN A 1 100 ? 46.823 -38.896 7.440 1.00 27.32 ? 100 GLN A CG 1 ATOM 763 C CD . GLN A 1 100 ? 48.147 -38.162 7.433 1.00 28.23 ? 100 GLN A CD 1 ATOM 764 O OE1 . GLN A 1 100 ? 49.200 -38.729 7.751 1.00 28.99 ? 100 GLN A OE1 1 ATOM 765 N NE2 . GLN A 1 100 ? 48.101 -36.880 7.070 1.00 28.37 ? 100 GLN A NE2 1 ATOM 766 N N . ILE A 1 101 ? 45.746 -42.926 9.531 1.00 27.62 ? 101 ILE A N 1 ATOM 767 C CA . ILE A 1 101 ? 45.613 -44.355 9.723 1.00 27.85 ? 101 ILE A CA 1 ATOM 768 C C . ILE A 1 101 ? 44.145 -44.767 9.585 1.00 27.15 ? 101 ILE A C 1 ATOM 769 O O . ILE A 1 101 ? 43.820 -45.681 8.829 1.00 26.66 ? 101 ILE A O 1 ATOM 770 C CB . ILE A 1 101 ? 46.175 -44.778 11.093 1.00 29.28 ? 101 ILE A CB 1 ATOM 771 C CG1 . ILE A 1 101 ? 47.704 -44.680 11.085 1.00 30.28 ? 101 ILE A CG1 1 ATOM 772 C CG2 . ILE A 1 101 ? 45.774 -46.204 11.437 1.00 29.61 ? 101 ILE A CG2 1 ATOM 773 C CD1 . ILE A 1 101 ? 48.307 -44.541 12.464 1.00 31.79 ? 101 ILE A CD1 1 ATOM 774 N N . LEU A 1 102 ? 43.263 -44.077 10.295 1.00 27.31 ? 102 LEU A N 1 ATOM 775 C CA . LEU A 1 102 ? 41.843 -44.432 10.298 1.00 26.92 ? 102 LEU A CA 1 ATOM 776 C C . LEU A 1 102 ? 41.135 -44.180 8.968 1.00 26.17 ? 102 LEU A C 1 ATOM 777 O O . LEU A 1 102 ? 40.224 -44.910 8.619 1.00 25.82 ? 102 LEU A O 1 ATOM 778 C CB . LEU A 1 102 ? 41.110 -43.714 11.426 1.00 27.33 ? 102 LEU A CB 1 ATOM 779 C CG . LEU A 1 102 ? 41.575 -44.138 12.811 1.00 28.32 ? 102 LEU A CG 1 ATOM 780 C CD1 . LEU A 1 102 ? 40.836 -43.343 13.876 1.00 28.91 ? 102 LEU A CD1 1 ATOM 781 C CD2 . LEU A 1 102 ? 41.388 -45.642 13.005 1.00 28.57 ? 102 LEU A CD2 1 ATOM 782 N N . ARG A 1 103 ? 41.558 -43.164 8.226 1.00 26.14 ? 103 ARG A N 1 ATOM 783 C CA . ARG A 1 103 ? 40.984 -42.904 6.910 1.00 25.67 ? 103 ARG A CA 1 ATOM 784 C C . ARG A 1 103 ? 41.141 -44.078 5.934 1.00 25.39 ? 103 ARG A C 1 ATOM 785 O O . ARG A 1 103 ? 40.254 -44.302 5.116 1.00 25.03 ? 103 ARG A O 1 ATOM 786 C CB . ARG A 1 103 ? 41.584 -41.643 6.279 1.00 25.71 ? 103 ARG A CB 1 ATOM 787 C CG . ARG A 1 103 ? 41.010 -40.351 6.837 1.00 26.27 ? 103 ARG A CG 1 ATOM 788 C CD . ARG A 1 103 ? 41.390 -39.153 5.991 1.00 26.22 ? 103 ARG A CD 1 ATOM 789 N NE . ARG A 1 103 ? 41.207 -37.910 6.728 1.00 26.96 ? 103 ARG A NE 1 ATOM 790 C CZ . ARG A 1 103 ? 42.180 -37.134 7.193 1.00 27.67 ? 103 ARG A CZ 1 ATOM 791 N NH1 . ARG A 1 103 ? 43.464 -37.437 7.003 1.00 27.73 ? 103 ARG A NH1 1 ATOM 792 N NH2 . ARG A 1 103 ? 41.857 -36.027 7.851 1.00 28.55 ? 103 ARG A NH2 1 ATOM 793 N N . GLU A 1 104 ? 42.250 -44.808 6.015 1.00 25.59 ? 104 GLU A N 1 ATOM 794 C CA . GLU A 1 104 ? 42.503 -45.910 5.091 1.00 25.70 ? 104 GLU A CA 1 ATOM 795 C C . GLU A 1 104 ? 42.369 -47.283 5.758 1.00 25.78 ? 104 GLU A C 1 ATOM 796 O O . GLU A 1 104 ? 42.761 -48.288 5.190 1.00 25.66 ? 104 GLU A O 1 ATOM 797 C CB . GLU A 1 104 ? 43.890 -45.754 4.435 1.00 26.46 ? 104 GLU A CB 1 ATOM 798 C CG . GLU A 1 104 ? 45.068 -46.029 5.357 1.00 28.07 ? 104 GLU A CG 1 ATOM 799 C CD . GLU A 1 104 ? 46.421 -45.984 4.649 1.00 29.25 ? 104 GLU A CD 1 ATOM 800 O OE1 . GLU A 1 104 ? 46.466 -45.871 3.389 1.00 29.12 ? 104 GLU A OE1 1 ATOM 801 O OE2 . GLU A 1 104 ? 47.447 -46.061 5.374 1.00 30.33 ? 104 GLU A OE2 1 ATOM 802 N N . SER A 1 105 ? 41.779 -47.306 6.949 1.00 26.06 ? 105 SER A N 1 ATOM 803 C CA . SER A 1 105 ? 41.642 -48.511 7.756 1.00 26.64 ? 105 SER A CA 1 ATOM 804 C C . SER A 1 105 ? 40.683 -49.546 7.183 1.00 26.64 ? 105 SER A C 1 ATOM 805 O O . SER A 1 105 ? 40.788 -50.722 7.510 1.00 27.33 ? 105 SER A O 1 ATOM 806 C CB . SER A 1 105 ? 41.122 -48.141 9.150 1.00 27.04 ? 105 SER A CB 1 ATOM 807 O OG . SER A 1 105 ? 39.806 -47.586 9.079 1.00 26.45 ? 105 SER A OG 1 ATOM 808 N N . GLY A 1 106 ? 39.731 -49.107 6.368 1.00 26.10 ? 106 GLY A N 1 ATOM 809 C CA . GLY A 1 106 ? 38.581 -49.938 6.027 1.00 26.45 ? 106 GLY A CA 1 ATOM 810 C C . GLY A 1 106 ? 37.536 -49.993 7.142 1.00 27.11 ? 106 GLY A C 1 ATOM 811 O O . GLY A 1 106 ? 36.561 -50.755 7.059 1.00 27.29 ? 106 GLY A O 1 ATOM 812 N N . GLY A 1 107 ? 37.727 -49.167 8.172 1.00 27.49 ? 107 GLY A N 1 ATOM 813 C CA . GLY A 1 107 ? 36.922 -49.223 9.395 1.00 28.21 ? 107 GLY A CA 1 ATOM 814 C C . GLY A 1 107 ? 37.579 -50.041 10.496 1.00 29.09 ? 107 GLY A C 1 ATOM 815 O O . GLY A 1 107 ? 38.702 -50.518 10.345 1.00 28.96 ? 107 GLY A O 1 ATOM 816 N N . ILE A 1 108 ? 36.854 -50.229 11.595 1.00 30.09 ? 108 ILE A N 1 ATOM 817 C CA . ILE A 1 108 ? 37.424 -50.811 12.810 1.00 31.41 ? 108 ILE A CA 1 ATOM 818 C C . ILE A 1 108 ? 36.574 -51.898 13.462 1.00 32.72 ? 108 ILE A C 1 ATOM 819 O O . ILE A 1 108 ? 35.341 -51.861 13.429 1.00 32.47 ? 108 ILE A O 1 ATOM 820 C CB . ILE A 1 108 ? 37.692 -49.727 13.875 1.00 31.62 ? 108 ILE A CB 1 ATOM 821 C CG1 . ILE A 1 108 ? 36.410 -48.941 14.169 1.00 31.56 ? 108 ILE A CG1 1 ATOM 822 C CG2 . ILE A 1 108 ? 38.792 -48.792 13.392 1.00 31.28 ? 108 ILE A CG2 1 ATOM 823 C CD1 . ILE A 1 108 ? 36.601 -47.750 15.078 1.00 32.09 ? 108 ILE A CD1 1 ATOM 824 N N . ASP A 1 109 ? 37.279 -52.845 14.073 1.00 34.33 ? 109 ASP A N 1 ATOM 825 C CA . ASP A 1 109 ? 36.706 -53.913 14.880 1.00 36.50 ? 109 ASP A CA 1 ATOM 826 C C . ASP A 1 109 ? 37.268 -53.696 16.288 1.00 37.60 ? 109 ASP A C 1 ATOM 827 O O . ASP A 1 109 ? 38.439 -53.305 16.441 1.00 37.61 ? 109 ASP A O 1 ATOM 828 C CB . ASP A 1 109 ? 37.141 -55.261 14.281 1.00 37.85 ? 109 ASP A CB 1 ATOM 829 C CG . ASP A 1 109 ? 36.830 -56.449 15.167 1.00 40.22 ? 109 ASP A CG 1 ATOM 830 O OD1 . ASP A 1 109 ? 35.877 -56.390 15.985 1.00 41.76 ? 109 ASP A OD1 1 ATOM 831 O OD2 . ASP A 1 109 ? 37.538 -57.475 15.016 1.00 41.65 ? 109 ASP A OD2 1 ATOM 832 N N . LYS A 1 110 ? 36.442 -53.935 17.306 1.00 38.42 ? 110 LYS A N 1 ATOM 833 C CA . LYS A 1 110 ? 36.811 -53.657 18.695 1.00 39.56 ? 110 LYS A CA 1 ATOM 834 C C . LYS A 1 110 ? 36.928 -54.939 19.505 1.00 41.69 ? 110 LYS A C 1 ATOM 835 O O . LYS A 1 110 ? 36.143 -55.878 19.322 1.00 41.88 ? 110 LYS A O 1 ATOM 836 C CB . LYS A 1 110 ? 35.766 -52.754 19.349 1.00 39.29 ? 110 LYS A CB 1 ATOM 837 C CG . LYS A 1 110 ? 35.776 -51.321 18.843 1.00 38.06 ? 110 LYS A CG 1 ATOM 838 C CD . LYS A 1 110 ? 36.787 -50.462 19.590 1.00 38.28 ? 110 LYS A CD 1 ATOM 839 C CE . LYS A 1 110 ? 36.937 -49.090 18.949 1.00 37.16 ? 110 LYS A CE 1 ATOM 840 N NZ . LYS A 1 110 ? 35.641 -48.374 18.855 1.00 36.83 ? 110 LYS A NZ 1 ATOM 841 N N . GLU A 1 111 ? 37.889 -54.969 20.424 1.00 43.41 ? 111 GLU A N 1 ATOM 842 C CA . GLU A 1 111 ? 38.061 -56.134 21.285 1.00 45.51 ? 111 GLU A CA 1 ATOM 843 C C . GLU A 1 111 ? 38.423 -55.757 22.717 1.00 46.72 ? 111 GLU A C 1 ATOM 844 O O . GLU A 1 111 ? 39.227 -54.860 22.944 1.00 46.57 ? 111 GLU A O 1 ATOM 845 C CB . GLU A 1 111 ? 39.126 -57.051 20.698 1.00 46.34 ? 111 GLU A CB 1 ATOM 846 C CG . GLU A 1 111 ? 38.977 -58.504 21.112 1.00 48.14 ? 111 GLU A CG 1 ATOM 847 C CD . GLU A 1 111 ? 39.874 -59.420 20.307 1.00 48.87 ? 111 GLU A CD 1 ATOM 848 O OE1 . GLU A 1 111 ? 39.793 -59.386 19.059 1.00 48.01 ? 111 GLU A OE1 1 ATOM 849 O OE2 . GLU A 1 111 ? 40.667 -60.164 20.920 1.00 50.92 ? 111 GLU A OE2 1 ATOM 850 N N . ALA A 1 112 ? 37.825 -56.461 23.673 1.00 48.34 ? 112 ALA A N 1 ATOM 851 C CA . ALA A 1 112 ? 38.084 -56.242 25.102 1.00 49.78 ? 112 ALA A CA 1 ATOM 852 C C . ALA A 1 112 ? 39.577 -56.353 25.415 1.00 50.87 ? 112 ALA A C 1 ATOM 853 O O . ALA A 1 112 ? 40.244 -57.280 24.945 1.00 51.13 ? 112 ALA A O 1 ATOM 854 C CB . ALA A 1 112 ? 37.291 -57.237 25.935 1.00 51.01 ? 112 ALA A CB 1 ATOM 855 N N . MET A 1 113 ? 40.095 -55.389 26.182 1.00 51.48 ? 113 MET A N 1 ATOM 856 C CA . MET A 1 113 ? 41.510 -55.370 26.579 1.00 52.64 ? 113 MET A CA 1 ATOM 857 C C . MET A 1 113 ? 41.768 -56.413 27.670 1.00 54.48 ? 113 MET A C 1 ATOM 858 O O . MET A 1 113 ? 42.864 -56.972 27.756 1.00 55.37 ? 113 MET A O 1 ATOM 859 C CB . MET A 1 113 ? 41.922 -53.986 27.106 1.00 53.05 ? 113 MET A CB 1 ATOM 860 C CG . MET A 1 113 ? 41.876 -52.843 26.094 1.00 51.26 ? 113 MET A CG 1 ATOM 861 S SD . MET A 1 113 ? 43.411 -52.515 25.202 1.00 51.74 ? 113 MET A SD 1 ATOM 862 C CE . MET A 1 113 ? 44.609 -52.433 26.524 1.00 53.88 ? 113 MET A CE 1 ATOM 863 N N . GLY A 1 114 ? 40.760 -56.662 28.504 1.00 54.60 ? 114 GLY A N 1 ATOM 864 C CA . GLY A 1 114 ? 40.857 -57.657 29.558 1.00 56.55 ? 114 GLY A CA 1 ATOM 865 C C . GLY A 1 114 ? 41.411 -57.145 30.880 1.00 58.20 ? 114 GLY A C 1 ATOM 866 O O . GLY A 1 114 ? 41.916 -57.936 31.680 1.00 60.08 ? 114 GLY A O 1 ATOM 867 N N . PHE A 1 115 ? 41.307 -55.839 31.131 1.00 69.06 ? 115 PHE A N 1 ATOM 868 C CA . PHE A 1 115 ? 41.776 -55.272 32.393 1.00 69.49 ? 115 PHE A CA 1 ATOM 869 C C . PHE A 1 115 ? 40.779 -55.492 33.521 1.00 70.50 ? 115 PHE A C 1 ATOM 870 O O . PHE A 1 115 ? 39.584 -55.226 33.365 1.00 69.45 ? 115 PHE A O 1 ATOM 871 C CB . PHE A 1 115 ? 42.032 -53.770 32.277 1.00 67.08 ? 115 PHE A CB 1 ATOM 872 C CG . PHE A 1 115 ? 43.202 -53.402 31.409 1.00 66.62 ? 115 PHE A CG 1 ATOM 873 C CD1 . PHE A 1 115 ? 44.255 -54.278 31.188 1.00 68.77 ? 115 PHE A CD1 1 ATOM 874 C CD2 . PHE A 1 115 ? 43.246 -52.154 30.812 1.00 64.49 ? 115 PHE A CD2 1 ATOM 875 C CE1 . PHE A 1 115 ? 45.321 -53.911 30.390 1.00 68.73 ? 115 PHE A CE1 1 ATOM 876 C CE2 . PHE A 1 115 ? 44.313 -51.780 30.014 1.00 64.42 ? 115 PHE A CE2 1 ATOM 877 C CZ . PHE A 1 115 ? 45.353 -52.661 29.802 1.00 66.48 ? 115 PHE A CZ 1 ATOM 878 N N . THR A 1 116 ? 41.293 -55.979 34.652 1.00 72.67 ? 116 THR A N 1 ATOM 879 C CA . THR A 1 116 ? 40.568 -55.991 35.917 1.00 73.63 ? 116 THR A CA 1 ATOM 880 C C . THR A 1 116 ? 41.278 -55.062 36.909 1.00 73.47 ? 116 THR A C 1 ATOM 881 O O . THR A 1 116 ? 42.480 -54.808 36.784 1.00 73.53 ? 116 THR A O 1 ATOM 882 C CB . THR A 1 116 ? 40.493 -57.406 36.501 1.00 77.17 ? 116 THR A CB 1 ATOM 883 O OG1 . THR A 1 116 ? 41.801 -57.990 36.500 1.00 79.23 ? 116 THR A OG1 1 ATOM 884 C CG2 . THR A 1 116 ? 39.548 -58.271 35.679 1.00 77.68 ? 116 THR A CG2 1 ATOM 885 N N . TYR A 1 117 ? 40.531 -54.560 37.890 1.00 73.37 ? 117 TYR A N 1 ATOM 886 C CA . TYR A 1 117 ? 41.042 -53.559 38.832 1.00 73.14 ? 117 TYR A CA 1 ATOM 887 C C . TYR A 1 117 ? 40.672 -53.906 40.272 1.00 75.48 ? 117 TYR A C 1 ATOM 888 O O . TYR A 1 117 ? 39.540 -54.311 40.544 1.00 76.07 ? 117 TYR A O 1 ATOM 889 C CB . TYR A 1 117 ? 40.477 -52.181 38.474 1.00 70.49 ? 117 TYR A CB 1 ATOM 890 C CG . TYR A 1 117 ? 40.884 -51.706 37.101 1.00 68.27 ? 117 TYR A CG 1 ATOM 891 C CD1 . TYR A 1 117 ? 42.167 -51.214 36.865 1.00 68.06 ? 117 TYR A CD1 1 ATOM 892 C CD2 . TYR A 1 117 ? 39.996 -51.771 36.031 1.00 66.59 ? 117 TYR A CD2 1 ATOM 893 C CE1 . TYR A 1 117 ? 42.547 -50.789 35.603 1.00 66.42 ? 117 TYR A CE1 1 ATOM 894 C CE2 . TYR A 1 117 ? 40.364 -51.348 34.767 1.00 64.70 ? 117 TYR A CE2 1 ATOM 895 C CZ . TYR A 1 117 ? 41.640 -50.860 34.557 1.00 64.80 ? 117 TYR A CZ 1 ATOM 896 O OH . TYR A 1 117 ? 42.004 -50.440 33.299 1.00 63.39 ? 117 TYR A OH 1 ATOM 897 N N . SER A 1 118 ? 41.626 -53.743 41.186 1.00 77.06 ? 118 SER A N 1 ATOM 898 C CA . SER A 1 118 ? 41.382 -53.970 42.612 1.00 79.70 ? 118 SER A CA 1 ATOM 899 C C . SER A 1 118 ? 42.011 -52.856 43.453 1.00 79.74 ? 118 SER A C 1 ATOM 900 O O . SER A 1 118 ? 43.191 -52.543 43.289 1.00 80.05 ? 118 SER A O 1 ATOM 901 C CB . SER A 1 118 ? 41.917 -55.344 43.048 1.00 82.92 ? 118 SER A CB 1 ATOM 902 O OG . SER A 1 118 ? 43.333 -55.388 43.039 1.00 83.82 ? 118 SER A OG 1 ATOM 903 N N . GLY A 1 119 ? 41.215 -52.261 44.343 1.00 79.99 ? 119 GLY A N 1 ATOM 904 C CA . GLY A 1 119 ? 41.676 -51.180 45.222 1.00 80.26 ? 119 GLY A CA 1 ATOM 905 C C . GLY A 1 119 ? 41.415 -49.769 44.709 1.00 77.95 ? 119 GLY A C 1 ATOM 906 O O . GLY A 1 119 ? 41.874 -48.795 45.315 1.00 78.24 ? 119 GLY A O 1 ATOM 907 N N . ILE A 1 120 ? 40.691 -49.658 43.591 1.00 75.89 ? 120 ILE A N 1 ATOM 908 C CA . ILE A 1 120 ? 40.312 -48.361 43.015 1.00 73.99 ? 120 ILE A CA 1 ATOM 909 C C . ILE A 1 120 ? 38.897 -48.385 42.418 1.00 73.08 ? 120 ILE A C 1 ATOM 910 O O . ILE A 1 120 ? 38.355 -49.451 42.126 1.00 73.08 ? 120 ILE A O 1 ATOM 911 C CB . ILE A 1 120 ? 41.302 -47.907 41.909 1.00 72.27 ? 120 ILE A CB 1 ATOM 912 C CG1 . ILE A 1 120 ? 41.293 -48.870 40.694 1.00 70.95 ? 120 ILE A CG1 1 ATOM 913 C CG2 . ILE A 1 120 ? 42.697 -47.698 42.492 1.00 73.62 ? 120 ILE A CG2 1 ATOM 914 C CD1 . ILE A 1 120 ? 42.476 -49.807 40.589 1.00 71.98 ? 120 ILE A CD1 1 ATOM 915 N N . ARG A 1 121 ? 38.310 -47.205 42.241 1.00 72.76 ? 121 ARG A N 1 ATOM 916 C CA . ARG A 1 121 ? 37.080 -47.064 41.456 1.00 72.28 ? 121 ARG A CA 1 ATOM 917 C C . ARG A 1 121 ? 37.396 -47.174 39.965 1.00 70.90 ? 121 ARG A C 1 ATOM 918 O O . ARG A 1 121 ? 38.564 -47.133 39.569 1.00 70.28 ? 121 ARG A O 1 ATOM 919 C CB . ARG A 1 121 ? 36.393 -45.722 41.732 1.00 72.54 ? 121 ARG A CB 1 ATOM 920 C CG . ARG A 1 121 ? 35.468 -45.716 42.938 1.00 74.74 ? 121 ARG A CG 1 ATOM 921 C CD . ARG A 1 121 ? 34.547 -44.506 42.899 1.00 75.12 ? 121 ARG A CD 1 ATOM 922 N NE . ARG A 1 121 ? 35.292 -43.253 43.031 1.00 75.25 ? 121 ARG A NE 1 ATOM 923 C CZ . ARG A 1 121 ? 35.450 -42.567 44.164 1.00 77.32 ? 121 ARG A CZ 1 ATOM 924 N NH1 . ARG A 1 121 ? 34.906 -42.988 45.302 1.00 79.47 ? 121 ARG A NH1 1 ATOM 925 N NH2 . ARG A 1 121 ? 36.156 -41.441 44.159 1.00 77.65 ? 121 ARG A NH2 1 ATOM 926 N N . THR A 1 122 ? 36.355 -47.317 39.143 1.00 70.97 ? 122 THR A N 1 ATOM 927 C CA . THR A 1 122 ? 36.528 -47.466 37.691 1.00 69.68 ? 122 THR A CA 1 ATOM 928 C C . THR A 1 122 ? 35.436 -46.791 36.843 1.00 69.66 ? 122 THR A C 1 ATOM 929 O O . THR A 1 122 ? 35.459 -46.898 35.617 1.00 68.19 ? 122 THR A O 1 ATOM 930 C CB . THR A 1 122 ? 36.615 -48.966 37.309 1.00 69.96 ? 122 THR A CB 1 ATOM 931 O OG1 . THR A 1 122 ? 37.241 -49.109 36.030 1.00 68.72 ? 122 THR A OG1 1 ATOM 932 C CG2 . THR A 1 122 ? 35.226 -49.630 37.281 1.00 70.40 ? 122 THR A CG2 1 ATOM 933 N N . ASN A 1 123 ? 34.518 -46.068 37.486 1.00 72.23 ? 123 ASN A N 1 ATOM 934 C CA . ASN A 1 123 ? 33.276 -45.608 36.850 1.00 72.94 ? 123 ASN A CA 1 ATOM 935 C C . ASN A 1 123 ? 33.101 -44.084 36.879 1.00 71.34 ? 123 ASN A C 1 ATOM 936 O O . ASN A 1 123 ? 31.998 -43.584 37.120 1.00 72.05 ? 123 ASN A O 1 ATOM 937 C CB . ASN A 1 123 ? 32.069 -46.284 37.518 1.00 77.75 ? 123 ASN A CB 1 ATOM 938 C CG . ASN A 1 123 ? 32.148 -46.259 39.039 1.00 84.11 ? 123 ASN A CG 1 ATOM 939 O OD1 . ASN A 1 123 ? 33.230 -46.431 39.611 1.00 83.87 ? 123 ASN A OD1 1 ATOM 940 N ND2 . ASN A 1 123 ? 31.006 -46.052 39.703 1.00 91.83 ? 123 ASN A ND2 1 ATOM 941 N N . GLY A 1 124 ? 34.182 -43.349 36.620 1.00 68.79 ? 124 GLY A N 1 ATOM 942 C CA . GLY A 1 124 ? 34.120 -41.885 36.590 1.00 68.16 ? 124 GLY A CA 1 ATOM 943 C C . GLY A 1 124 ? 33.343 -41.377 35.387 1.00 66.25 ? 124 GLY A C 1 ATOM 944 O O . GLY A 1 124 ? 33.575 -41.828 34.264 1.00 64.49 ? 124 GLY A O 1 ATOM 945 N N . THR A 1 125 ? 32.419 -40.443 35.625 1.00 66.69 ? 125 THR A N 1 ATOM 946 C CA . THR A 1 125 ? 31.542 -39.896 34.577 1.00 65.67 ? 125 THR A CA 1 ATOM 947 C C . THR A 1 125 ? 31.534 -38.358 34.592 1.00 66.74 ? 125 THR A C 1 ATOM 948 O O . THR A 1 125 ? 32.307 -37.748 35.327 1.00 67.84 ? 125 THR A O 1 ATOM 949 C CB . THR A 1 125 ? 30.098 -40.417 34.741 1.00 66.43 ? 125 THR A CB 1 ATOM 950 O OG1 . THR A 1 125 ? 29.535 -39.898 35.951 1.00 68.94 ? 125 THR A OG1 1 ATOM 951 C CG2 . THR A 1 125 ? 30.078 -41.938 34.765 1.00 65.25 ? 125 THR A CG2 1 ATOM 952 N N . THR A 1 126 ? 30.667 -37.745 33.781 1.00 66.59 ? 126 THR A N 1 ATOM 953 C CA . THR A 1 126 ? 30.574 -36.285 33.700 1.00 68.26 ? 126 THR A CA 1 ATOM 954 C C . THR A 1 126 ? 29.317 -35.786 32.983 1.00 69.17 ? 126 THR A C 1 ATOM 955 O O . THR A 1 126 ? 28.650 -36.533 32.273 1.00 67.55 ? 126 THR A O 1 ATOM 956 C CB . THR A 1 126 ? 31.804 -35.690 32.983 1.00 67.32 ? 126 THR A CB 1 ATOM 957 O OG1 . THR A 1 126 ? 31.563 -34.314 32.663 1.00 69.67 ? 126 THR A OG1 1 ATOM 958 C CG2 . THR A 1 126 ? 32.107 -36.449 31.702 1.00 64.33 ? 126 THR A CG2 1 ATOM 959 N N . SER A 1 127 ? 29.029 -34.501 33.167 1.00 71.90 ? 127 SER A N 1 ATOM 960 C CA . SER A 1 127 ? 27.859 -33.842 32.576 1.00 73.86 ? 127 SER A CA 1 ATOM 961 C C . SER A 1 127 ? 27.964 -33.653 31.061 1.00 72.19 ? 127 SER A C 1 ATOM 962 O O . SER A 1 127 ? 26.945 -33.553 30.382 1.00 73.03 ? 127 SER A O 1 ATOM 963 C CB . SER A 1 127 ? 27.655 -32.464 33.218 1.00 77.96 ? 127 SER A CB 1 ATOM 964 O OG . SER A 1 127 ? 28.158 -32.436 34.541 1.00 79.28 ? 127 SER A OG 1 ATOM 965 N N . ALA A 1 128 ? 29.188 -33.593 30.540 1.00 70.10 ? 128 ALA A N 1 ATOM 966 C CA . ALA A 1 128 ? 29.419 -33.256 29.131 1.00 68.97 ? 128 ALA A CA 1 ATOM 967 C C . ALA A 1 128 ? 29.255 -34.440 28.175 1.00 65.89 ? 128 ALA A C 1 ATOM 968 O O . ALA A 1 128 ? 29.155 -34.247 26.962 1.00 65.28 ? 128 ALA A O 1 ATOM 969 C CB . ALA A 1 128 ? 30.797 -32.639 28.963 1.00 68.73 ? 128 ALA A CB 1 ATOM 970 N N . CYS A 1 129 ? 29.255 -35.660 28.709 1.00 64.13 ? 129 CYS A N 1 ATOM 971 C CA . CYS A 1 129 ? 28.962 -36.842 27.902 1.00 61.66 ? 129 CYS A CA 1 ATOM 972 C C . CYS A 1 129 ? 27.564 -37.323 28.283 1.00 62.71 ? 129 CYS A C 1 ATOM 973 O O . CYS A 1 129 ? 27.389 -38.089 29.227 1.00 62.73 ? 129 CYS A O 1 ATOM 974 C CB . CYS A 1 129 ? 30.036 -37.920 28.089 1.00 59.18 ? 129 CYS A CB 1 ATOM 975 S SG . CYS A 1 129 ? 31.727 -37.260 28.034 0.80 58.81 ? 129 CYS A SG 1 ATOM 976 N N . ARG A 1 130 ? 26.573 -36.836 27.539 1.00 63.89 ? 130 ARG A N 1 ATOM 977 C CA . ARG A 1 130 ? 25.166 -37.033 27.864 1.00 65.90 ? 130 ARG A CA 1 ATOM 978 C C . ARG A 1 130 ? 24.574 -38.273 27.191 1.00 64.11 ? 130 ARG A C 1 ATOM 979 O O . ARG A 1 130 ? 24.459 -38.337 25.963 1.00 63.03 ? 130 ARG A O 1 ATOM 980 C CB . ARG A 1 130 ? 24.363 -35.786 27.466 1.00 69.10 ? 130 ARG A CB 1 ATOM 981 C CG . ARG A 1 130 ? 22.862 -35.888 27.706 1.00 72.01 ? 130 ARG A CG 1 ATOM 982 C CD . ARG A 1 130 ? 22.181 -34.531 27.592 1.00 75.96 ? 130 ARG A CD 1 ATOM 983 N NE . ARG A 1 130 ? 20.810 -34.646 27.088 1.00 78.17 ? 130 ARG A NE 1 ATOM 984 C CZ . ARG A 1 130 ? 19.762 -35.079 27.792 1.00 80.39 ? 130 ARG A CZ 1 ATOM 985 N NH1 . ARG A 1 130 ? 19.892 -35.460 29.063 1.00 80.81 ? 130 ARG A NH1 1 ATOM 986 N NH2 . ARG A 1 130 ? 18.564 -35.137 27.216 1.00 82.39 ? 130 ARG A NH2 1 ATOM 987 N N . ARG A 1 131 ? 24.217 -39.255 28.014 1.00 63.96 ? 131 ARG A N 1 ATOM 988 C CA . ARG A 1 131 ? 23.364 -40.364 27.602 1.00 63.53 ? 131 ARG A CA 1 ATOM 989 C C . ARG A 1 131 ? 22.238 -40.477 28.622 1.00 66.49 ? 131 ARG A C 1 ATOM 990 O O . ARG A 1 131 ? 22.274 -41.338 29.504 1.00 66.64 ? 131 ARG A O 1 ATOM 991 C CB . ARG A 1 131 ? 24.161 -41.665 27.543 1.00 60.84 ? 131 ARG A CB 1 ATOM 992 C CG . ARG A 1 131 ? 25.005 -41.826 26.292 1.00 58.11 ? 131 ARG A CG 1 ATOM 993 C CD . ARG A 1 131 ? 26.131 -42.818 26.520 1.00 55.97 ? 131 ARG A CD 1 ATOM 994 N NE . ARG A 1 131 ? 27.039 -42.874 25.375 1.00 53.72 ? 131 ARG A NE 1 ATOM 995 C CZ . ARG A 1 131 ? 28.363 -43.013 25.451 1.00 52.11 ? 131 ARG A CZ 1 ATOM 996 N NH1 . ARG A 1 131 ? 28.974 -43.103 26.628 1.00 52.33 ? 131 ARG A NH1 1 ATOM 997 N NH2 . ARG A 1 131 ? 29.091 -43.048 24.336 1.00 50.46 ? 131 ARG A NH2 1 ATOM 998 N N . SER A 1 132 ? 21.251 -39.590 28.504 1.00 69.14 ? 132 SER A N 1 ATOM 999 C CA . SER A 1 132 ? 20.174 -39.479 29.492 1.00 72.53 ? 132 SER A CA 1 ATOM 1000 C C . SER A 1 132 ? 20.759 -39.484 30.905 1.00 72.79 ? 132 SER A C 1 ATOM 1001 O O . SER A 1 132 ? 20.720 -40.500 31.603 1.00 72.58 ? 132 SER A O 1 ATOM 1002 C CB . SER A 1 132 ? 19.147 -40.608 29.316 1.00 73.41 ? 132 SER A CB 1 ATOM 1003 O OG . SER A 1 132 ? 19.704 -41.882 29.597 1.00 71.44 ? 132 SER A OG 1 ATOM 1004 N N . GLY A 1 133 ? 21.311 -38.342 31.310 1.00 73.42 ? 133 GLY A N 1 ATOM 1005 C CA . GLY A 1 133 ? 22.119 -38.255 32.525 1.00 73.25 ? 133 GLY A CA 1 ATOM 1006 C C . GLY A 1 133 ? 23.597 -38.364 32.191 1.00 69.64 ? 133 GLY A C 1 ATOM 1007 O O . GLY A 1 133 ? 23.965 -38.622 31.039 1.00 67.20 ? 133 GLY A O 1 ATOM 1008 N N . SER A 1 134 ? 24.442 -38.176 33.202 1.00 69.40 ? 134 SER A N 1 ATOM 1009 C CA . SER A 1 134 ? 25.892 -38.186 33.018 1.00 66.65 ? 134 SER A CA 1 ATOM 1010 C C . SER A 1 134 ? 26.385 -39.527 32.505 1.00 63.37 ? 134 SER A C 1 ATOM 1011 O O . SER A 1 134 ? 25.722 -40.547 32.686 1.00 63.49 ? 134 SER A O 1 ATOM 1012 C CB . SER A 1 134 ? 26.613 -37.853 34.328 1.00 67.81 ? 134 SER A CB 1 ATOM 1013 O OG . SER A 1 134 ? 26.406 -36.500 34.698 1.00 70.80 ? 134 SER A OG 1 ATOM 1014 N N . SER A 1 135 ? 27.549 -39.504 31.860 1.00 60.78 ? 135 SER A N 1 ATOM 1015 C CA . SER A 1 135 ? 28.182 -40.710 31.326 1.00 57.95 ? 135 SER A CA 1 ATOM 1016 C C . SER A 1 135 ? 29.673 -40.475 31.044 1.00 56.04 ? 135 SER A C 1 ATOM 1017 O O . SER A 1 135 ? 30.290 -39.597 31.646 1.00 57.00 ? 135 SER A O 1 ATOM 1018 C CB . SER A 1 135 ? 27.460 -41.177 30.059 1.00 57.02 ? 135 SER A CB 1 ATOM 1019 O OG . SER A 1 135 ? 27.957 -42.434 29.641 1.00 55.10 ? 135 SER A OG 1 ATOM 1020 N N . PHE A 1 136 ? 30.247 -41.274 30.147 1.00 53.66 ? 136 PHE A N 1 ATOM 1021 C CA . PHE A 1 136 ? 31.653 -41.142 29.768 1.00 52.02 ? 136 PHE A CA 1 ATOM 1022 C C . PHE A 1 136 ? 31.896 -41.799 28.404 1.00 50.13 ? 136 PHE A C 1 ATOM 1023 O O . PHE A 1 136 ? 30.989 -42.407 27.838 1.00 49.90 ? 136 PHE A O 1 ATOM 1024 C CB . PHE A 1 136 ? 32.537 -41.780 30.843 1.00 51.88 ? 136 PHE A CB 1 ATOM 1025 C CG . PHE A 1 136 ? 33.980 -41.364 30.772 1.00 51.24 ? 136 PHE A CG 1 ATOM 1026 C CD1 . PHE A 1 136 ? 34.338 -40.028 30.887 1.00 52.26 ? 136 PHE A CD1 1 ATOM 1027 C CD2 . PHE A 1 136 ? 34.980 -42.304 30.592 1.00 50.06 ? 136 PHE A CD2 1 ATOM 1028 C CE1 . PHE A 1 136 ? 35.663 -39.639 30.824 1.00 52.08 ? 136 PHE A CE1 1 ATOM 1029 C CE2 . PHE A 1 136 ? 36.311 -41.920 30.528 1.00 49.91 ? 136 PHE A CE2 1 ATOM 1030 C CZ . PHE A 1 136 ? 36.652 -40.586 30.645 1.00 50.87 ? 136 PHE A CZ 1 ATOM 1031 N N . TYR A 1 137 ? 33.115 -41.663 27.882 1.00 49.00 ? 137 TYR A N 1 ATOM 1032 C CA . TYR A 1 137 ? 33.508 -42.286 26.622 1.00 47.42 ? 137 TYR A CA 1 ATOM 1033 C C . TYR A 1 137 ? 33.271 -43.795 26.659 1.00 47.02 ? 137 TYR A C 1 ATOM 1034 O O . TYR A 1 137 ? 33.812 -44.491 27.513 1.00 47.47 ? 137 TYR A O 1 ATOM 1035 C CB . TYR A 1 137 ? 34.980 -42.011 26.328 1.00 46.82 ? 137 TYR A CB 1 ATOM 1036 C CG . TYR A 1 137 ? 35.296 -40.572 25.978 1.00 47.50 ? 137 TYR A CG 1 ATOM 1037 C CD1 . TYR A 1 137 ? 35.631 -39.651 26.969 1.00 48.97 ? 137 TYR A CD1 1 ATOM 1038 C CD2 . TYR A 1 137 ? 35.275 -40.134 24.658 1.00 46.97 ? 137 TYR A CD2 1 ATOM 1039 C CE1 . TYR A 1 137 ? 35.927 -38.335 26.655 1.00 50.10 ? 137 TYR A CE1 1 ATOM 1040 C CE2 . TYR A 1 137 ? 35.574 -38.822 24.336 1.00 48.09 ? 137 TYR A CE2 1 ATOM 1041 C CZ . TYR A 1 137 ? 35.904 -37.928 25.336 1.00 49.66 ? 137 TYR A CZ 1 ATOM 1042 O OH . TYR A 1 137 ? 36.195 -36.625 25.018 1.00 51.14 ? 137 TYR A OH 1 ATOM 1043 N N . ALA A 1 138 ? 32.481 -44.293 25.711 1.00 46.52 ? 138 ALA A N 1 ATOM 1044 C CA . ALA A 1 138 ? 32.008 -45.674 25.731 1.00 46.69 ? 138 ALA A CA 1 ATOM 1045 C C . ALA A 1 138 ? 33.113 -46.737 25.761 1.00 46.35 ? 138 ALA A C 1 ATOM 1046 O O . ALA A 1 138 ? 32.904 -47.808 26.312 1.00 47.06 ? 138 ALA A O 1 ATOM 1047 C CB . ALA A 1 138 ? 31.080 -45.921 24.549 1.00 46.45 ? 138 ALA A CB 1 ATOM 1048 N N . GLU A 1 139 ? 34.274 -46.440 25.176 1.00 45.65 ? 139 GLU A N 1 ATOM 1049 C CA . GLU A 1 139 ? 35.381 -47.400 25.104 1.00 45.79 ? 139 GLU A CA 1 ATOM 1050 C C . GLU A 1 139 ? 36.430 -47.211 26.197 1.00 46.68 ? 139 GLU A C 1 ATOM 1051 O O . GLU A 1 139 ? 37.418 -47.948 26.233 1.00 47.03 ? 139 GLU A O 1 ATOM 1052 C CB . GLU A 1 139 ? 36.086 -47.304 23.741 1.00 44.94 ? 139 GLU A CB 1 ATOM 1053 C CG . GLU A 1 139 ? 35.178 -47.352 22.518 1.00 44.35 ? 139 GLU A CG 1 ATOM 1054 C CD . GLU A 1 139 ? 34.489 -48.693 22.350 1.00 44.98 ? 139 GLU A CD 1 ATOM 1055 O OE1 . GLU A 1 139 ? 34.175 -49.332 23.370 1.00 46.09 ? 139 GLU A OE1 1 ATOM 1056 O OE2 . GLU A 1 139 ? 34.253 -49.114 21.196 1.00 44.75 ? 139 GLU A OE2 1 ATOM 1057 N N . MET A 1 140 ? 36.226 -46.232 27.078 1.00 47.32 ? 140 MET A N 1 ATOM 1058 C CA . MET A 1 140 ? 37.232 -45.856 28.059 1.00 48.32 ? 140 MET A CA 1 ATOM 1059 C C . MET A 1 140 ? 36.700 -45.995 29.480 1.00 49.69 ? 140 MET A C 1 ATOM 1060 O O . MET A 1 140 ? 35.487 -45.992 29.704 1.00 50.17 ? 140 MET A O 1 ATOM 1061 C CB . MET A 1 140 ? 37.662 -44.402 27.843 1.00 48.33 ? 140 MET A CB 1 ATOM 1062 C CG . MET A 1 140 ? 37.968 -44.027 26.403 1.00 47.49 ? 140 MET A CG 1 ATOM 1063 S SD . MET A 1 140 ? 39.396 -44.923 25.768 1.00 47.67 ? 140 MET A SD 1 ATOM 1064 C CE . MET A 1 140 ? 40.711 -44.066 26.633 1.00 48.70 ? 140 MET A CE 1 ATOM 1065 N N . LYS A 1 141 ? 37.621 -46.083 30.436 1.00 50.62 ? 141 LYS A N 1 ATOM 1066 C CA . LYS A 1 141 ? 37.275 -46.068 31.853 1.00 52.09 ? 141 LYS A CA 1 ATOM 1067 C C . LYS A 1 141 ? 38.059 -45.000 32.612 1.00 52.84 ? 141 LYS A C 1 ATOM 1068 O O . LYS A 1 141 ? 39.292 -44.955 32.553 1.00 52.96 ? 141 LYS A O 1 ATOM 1069 C CB . LYS A 1 141 ? 37.518 -47.447 32.460 1.00 53.12 ? 141 LYS A CB 1 ATOM 1070 C CG . LYS A 1 141 ? 36.395 -48.421 32.156 1.00 53.29 ? 141 LYS A CG 1 ATOM 1071 C CD . LYS A 1 141 ? 36.858 -49.865 32.233 1.00 54.42 ? 141 LYS A CD 1 ATOM 1072 C CE . LYS A 1 141 ? 35.675 -50.823 32.321 1.00 55.45 ? 141 LYS A CE 1 ATOM 1073 N NZ . LYS A 1 141 ? 34.589 -50.501 31.348 1.00 54.40 ? 141 LYS A NZ 1 ATOM 1074 N N . TRP A 1 142 ? 37.328 -44.136 33.309 1.00 53.69 ? 142 TRP A N 1 ATOM 1075 C CA . TRP A 1 142 ? 37.930 -43.094 34.135 1.00 55.03 ? 142 TRP A CA 1 ATOM 1076 C C . TRP A 1 142 ? 38.265 -43.675 35.508 1.00 56.53 ? 142 TRP A C 1 ATOM 1077 O O . TRP A 1 142 ? 37.372 -43.883 36.342 1.00 57.26 ? 142 TRP A O 1 ATOM 1078 C CB . TRP A 1 142 ? 36.968 -41.912 34.285 1.00 55.87 ? 142 TRP A CB 1 ATOM 1079 C CG . TRP A 1 142 ? 37.598 -40.648 34.807 1.00 57.32 ? 142 TRP A CG 1 ATOM 1080 C CD1 . TRP A 1 142 ? 38.806 -40.517 35.445 1.00 58.20 ? 142 TRP A CD1 1 ATOM 1081 C CD2 . TRP A 1 142 ? 37.032 -39.334 34.754 1.00 58.61 ? 142 TRP A CD2 1 ATOM 1082 N NE1 . TRP A 1 142 ? 39.028 -39.204 35.772 1.00 59.82 ? 142 TRP A NE1 1 ATOM 1083 C CE2 . TRP A 1 142 ? 37.956 -38.456 35.360 1.00 60.17 ? 142 TRP A CE2 1 ATOM 1084 C CE3 . TRP A 1 142 ? 35.837 -38.811 34.242 1.00 58.90 ? 142 TRP A CE3 1 ATOM 1085 C CZ2 . TRP A 1 142 ? 37.721 -37.085 35.472 1.00 62.12 ? 142 TRP A CZ2 1 ATOM 1086 C CZ3 . TRP A 1 142 ? 35.604 -37.446 34.355 1.00 60.80 ? 142 TRP A CZ3 1 ATOM 1087 C CH2 . TRP A 1 142 ? 36.544 -36.600 34.966 1.00 62.43 ? 142 TRP A CH2 1 ATOM 1088 N N . LEU A 1 143 ? 39.554 -43.928 35.734 1.00 57.03 ? 143 LEU A N 1 ATOM 1089 C CA . LEU A 1 143 ? 40.015 -44.535 36.984 1.00 58.70 ? 143 LEU A CA 1 ATOM 1090 C C . LEU A 1 143 ? 40.260 -43.487 38.071 1.00 60.30 ? 143 LEU A C 1 ATOM 1091 O O . LEU A 1 143 ? 41.006 -42.533 37.868 1.00 60.41 ? 143 LEU A O 1 ATOM 1092 C CB . LEU A 1 143 ? 41.290 -45.353 36.757 1.00 58.98 ? 143 LEU A CB 1 ATOM 1093 C CG . LEU A 1 143 ? 41.210 -46.602 35.868 1.00 58.26 ? 143 LEU A CG 1 ATOM 1094 C CD1 . LEU A 1 143 ? 42.442 -47.474 36.099 1.00 59.60 ? 143 LEU A CD1 1 ATOM 1095 C CD2 . LEU A 1 143 ? 39.937 -47.402 36.107 1.00 58.29 ? 143 LEU A CD2 1 ATOM 1096 N N . LEU A 1 144 ? 39.624 -43.690 39.223 1.00 61.60 ? 144 LEU A N 1 ATOM 1097 C CA . LEU A 1 144 ? 39.746 -42.807 40.373 1.00 63.51 ? 144 LEU A CA 1 ATOM 1098 C C . LEU A 1 144 ? 40.280 -43.589 41.569 1.00 65.05 ? 144 LEU A C 1 ATOM 1099 O O . LEU A 1 144 ? 40.431 -44.803 41.506 1.00 64.90 ? 144 LEU A O 1 ATOM 1100 C CB . LEU A 1 144 ? 38.374 -42.232 40.723 1.00 64.27 ? 144 LEU A CB 1 ATOM 1101 C CG . LEU A 1 144 ? 37.687 -41.422 39.626 1.00 63.17 ? 144 LEU A CG 1 ATOM 1102 C CD1 . LEU A 1 144 ? 36.259 -41.079 40.036 1.00 64.31 ? 144 LEU A CD1 1 ATOM 1103 C CD2 . LEU A 1 144 ? 38.494 -40.169 39.316 1.00 63.59 ? 144 LEU A CD2 1 ATOM 1104 N N . SER A 1 145 ? 40.568 -42.884 42.655 1.00 66.92 ? 145 SER A N 1 ATOM 1105 C CA . SER A 1 145 ? 40.908 -43.529 43.916 1.00 68.83 ? 145 SER A CA 1 ATOM 1106 C C . SER A 1 145 ? 39.607 -43.840 44.654 1.00 69.73 ? 145 SER A C 1 ATOM 1107 O O . SER A 1 145 ? 38.642 -43.074 44.570 1.00 69.60 ? 145 SER A O 1 ATOM 1108 C CB . SER A 1 145 ? 41.813 -42.631 44.762 1.00 70.79 ? 145 SER A CB 1 ATOM 1109 O OG . SER A 1 145 ? 42.466 -43.382 45.771 1.00 72.63 ? 145 SER A OG 1 ATOM 1110 N N . ASN A 1 146 ? 39.591 -44.964 45.369 1.00 70.92 ? 146 ASN A N 1 ATOM 1111 C CA . ASN A 1 146 ? 38.388 -45.464 46.055 1.00 72.22 ? 146 ASN A CA 1 ATOM 1112 C C . ASN A 1 146 ? 37.489 -44.374 46.626 1.00 73.54 ? 146 ASN A C 1 ATOM 1113 O O . ASN A 1 146 ? 36.268 -44.444 46.492 1.00 73.54 ? 146 ASN A O 1 ATOM 1114 C CB . ASN A 1 146 ? 38.773 -46.422 47.192 1.00 74.49 ? 146 ASN A CB 1 ATOM 1115 C CG . ASN A 1 146 ? 38.839 -47.877 46.753 1.00 74.22 ? 146 ASN A CG 1 ATOM 1116 O OD1 . ASN A 1 146 ? 39.661 -48.640 47.258 1.00 75.69 ? 146 ASN A OD1 1 ATOM 1117 N ND2 . ASN A 1 146 ? 37.961 -48.274 45.836 1.00 72.80 ? 146 ASN A ND2 1 ATOM 1118 N N . THR A 1 147 ? 38.100 -43.385 47.276 1.00 74.99 ? 147 THR A N 1 ATOM 1119 C CA . THR A 1 147 ? 37.366 -42.263 47.860 1.00 76.86 ? 147 THR A CA 1 ATOM 1120 C C . THR A 1 147 ? 38.176 -40.957 47.809 1.00 77.52 ? 147 THR A C 1 ATOM 1121 O O . THR A 1 147 ? 39.362 -40.957 47.454 1.00 76.60 ? 147 THR A O 1 ATOM 1122 C CB . THR A 1 147 ? 36.935 -42.582 49.308 1.00 79.71 ? 147 THR A CB 1 ATOM 1123 O OG1 . THR A 1 147 ? 36.133 -41.512 49.822 1.00 81.79 ? 147 THR A OG1 1 ATOM 1124 C CG2 . THR A 1 147 ? 38.148 -42.815 50.214 1.00 81.10 ? 147 THR A CG2 1 ATOM 1125 N N . ASP A 1 148 ? 37.519 -39.852 48.164 1.00 79.44 ? 148 ASP A N 1 ATOM 1126 C CA . ASP A 1 148 ? 38.114 -38.514 48.077 1.00 80.65 ? 148 ASP A CA 1 ATOM 1127 C C . ASP A 1 148 ? 39.425 -38.423 48.860 1.00 82.12 ? 148 ASP A C 1 ATOM 1128 O O . ASP A 1 148 ? 39.474 -38.761 50.040 1.00 83.87 ? 148 ASP A O 1 ATOM 1129 C CB . ASP A 1 148 ? 37.126 -37.448 48.567 1.00 83.34 ? 148 ASP A CB 1 ATOM 1130 C CG . ASP A 1 148 ? 35.856 -37.393 47.729 1.00 82.44 ? 148 ASP A CG 1 ATOM 1131 O OD1 . ASP A 1 148 ? 35.942 -37.555 46.498 1.00 79.84 ? 148 ASP A OD1 1 ATOM 1132 O OD2 . ASP A 1 148 ? 34.764 -37.201 48.302 1.00 84.67 ? 148 ASP A OD2 1 ATOM 1133 N N . ASN A 1 149 ? 40.488 -38.003 48.168 1.00 81.45 ? 149 ASN A N 1 ATOM 1134 C CA . ASN A 1 149 ? 41.836 -37.841 48.744 1.00 83.09 ? 149 ASN A CA 1 ATOM 1135 C C . ASN A 1 149 ? 42.562 -39.145 49.102 1.00 82.68 ? 149 ASN A C 1 ATOM 1136 O O . ASN A 1 149 ? 43.650 -39.108 49.680 1.00 84.19 ? 149 ASN A O 1 ATOM 1137 C CB . ASN A 1 149 ? 41.813 -36.896 49.963 1.00 86.65 ? 149 ASN A CB 1 ATOM 1138 C CG . ASN A 1 149 ? 41.532 -35.455 49.586 1.00 88.04 ? 149 ASN A CG 1 ATOM 1139 O OD1 . ASN A 1 149 ? 41.871 -35.004 48.486 1.00 86.66 ? 149 ASN A OD1 1 ATOM 1140 N ND2 . ASN A 1 149 ? 40.923 -34.715 50.508 1.00 91.03 ? 149 ASN A ND2 1 ATOM 1141 N N . ALA A 1 150 ? 41.983 -40.288 48.741 1.00 81.06 ? 150 ALA A N 1 ATOM 1142 C CA . ALA A 1 150 ? 42.592 -41.576 49.053 1.00 81.17 ? 150 ALA A CA 1 ATOM 1143 C C . ALA A 1 150 ? 43.784 -41.849 48.137 1.00 80.09 ? 150 ALA A C 1 ATOM 1144 O O . ALA A 1 150 ? 43.833 -41.372 46.996 1.00 78.19 ? 150 ALA A O 1 ATOM 1145 C CB . ALA A 1 150 ? 41.568 -42.693 48.941 1.00 80.12 ? 150 ALA A CB 1 ATOM 1146 N N . ALA A 1 151 ? 44.740 -42.617 48.654 1.00 81.57 ? 151 ALA A N 1 ATOM 1147 C CA . ALA A 1 151 ? 45.920 -43.012 47.895 1.00 81.12 ? 151 ALA A CA 1 ATOM 1148 C C . ALA A 1 151 ? 45.542 -43.942 46.740 1.00 78.95 ? 151 ALA A C 1 ATOM 1149 O O . ALA A 1 151 ? 45.026 -45.039 46.958 1.00 79.03 ? 151 ALA A O 1 ATOM 1150 C CB . ALA A 1 151 ? 46.933 -43.691 48.809 1.00 83.39 ? 151 ALA A CB 1 ATOM 1151 N N . PHE A 1 152 ? 45.780 -43.479 45.517 1.00 77.52 ? 152 PHE A N 1 ATOM 1152 C CA . PHE A 1 152 ? 45.666 -44.312 44.330 1.00 75.73 ? 152 PHE A CA 1 ATOM 1153 C C . PHE A 1 152 ? 46.954 -45.128 44.224 1.00 76.97 ? 152 PHE A C 1 ATOM 1154 O O . PHE A 1 152 ? 48.003 -44.569 43.911 1.00 77.73 ? 152 PHE A O 1 ATOM 1155 C CB . PHE A 1 152 ? 45.493 -43.431 43.086 1.00 73.85 ? 152 PHE A CB 1 ATOM 1156 C CG . PHE A 1 152 ? 45.170 -44.196 41.833 1.00 71.78 ? 152 PHE A CG 1 ATOM 1157 C CD1 . PHE A 1 152 ? 46.146 -44.934 41.174 1.00 71.71 ? 152 PHE A CD1 1 ATOM 1158 C CD2 . PHE A 1 152 ? 43.884 -44.182 41.312 1.00 70.32 ? 152 PHE A CD2 1 ATOM 1159 C CE1 . PHE A 1 152 ? 45.850 -45.639 40.024 1.00 69.98 ? 152 PHE A CE1 1 ATOM 1160 C CE2 . PHE A 1 152 ? 43.578 -44.886 40.159 1.00 68.51 ? 152 PHE A CE2 1 ATOM 1161 C CZ . PHE A 1 152 ? 44.562 -45.617 39.515 1.00 68.35 ? 152 PHE A CZ 1 ATOM 1162 N N . PRO A 1 153 ? 46.883 -46.452 44.467 1.00 77.83 ? 153 PRO A N 1 ATOM 1163 C CA . PRO A 1 153 ? 48.103 -47.278 44.499 1.00 79.62 ? 153 PRO A CA 1 ATOM 1164 C C . PRO A 1 153 ? 48.832 -47.357 43.151 1.00 78.66 ? 153 PRO A C 1 ATOM 1165 O O . PRO A 1 153 ? 48.208 -47.174 42.103 1.00 76.59 ? 153 PRO A O 1 ATOM 1166 C CB . PRO A 1 153 ? 47.585 -48.658 44.912 1.00 80.56 ? 153 PRO A CB 1 ATOM 1167 C CG . PRO A 1 153 ? 46.141 -48.669 44.539 1.00 78.45 ? 153 PRO A CG 1 ATOM 1168 C CD . PRO A 1 153 ? 45.655 -47.258 44.603 1.00 77.21 ? 153 PRO A CD 1 ATOM 1169 N N . GLN A 1 154 ? 50.140 -47.619 43.184 1.00 80.55 ? 154 GLN A N 1 ATOM 1170 C CA . GLN A 1 154 ? 50.923 -47.791 41.957 1.00 80.08 ? 154 GLN A CA 1 ATOM 1171 C C . GLN A 1 154 ? 50.510 -49.097 41.291 1.00 79.46 ? 154 GLN A C 1 ATOM 1172 O O . GLN A 1 154 ? 50.487 -50.150 41.933 1.00 81.27 ? 154 GLN A O 1 ATOM 1173 C CB . GLN A 1 154 ? 52.432 -47.786 42.249 1.00 83.02 ? 154 GLN A CB 1 ATOM 1174 C CG . GLN A 1 154 ? 53.330 -47.917 41.015 1.00 83.09 ? 154 GLN A CG 1 ATOM 1175 C CD . GLN A 1 154 ? 53.346 -46.671 40.135 1.00 81.39 ? 154 GLN A CD 1 ATOM 1176 O OE1 . GLN A 1 154 ? 53.619 -45.569 40.608 1.00 82.44 ? 154 GLN A OE1 1 ATOM 1177 N NE2 . GLN A 1 154 ? 53.082 -46.846 38.846 1.00 79.33 ? 154 GLN A NE2 1 ATOM 1178 N N . MET A 1 155 ? 50.196 -49.021 40.001 1.00 77.16 ? 155 MET A N 1 ATOM 1179 C CA . MET A 1 155 ? 49.541 -50.122 39.307 1.00 76.36 ? 155 MET A CA 1 ATOM 1180 C C . MET A 1 155 ? 50.275 -50.554 38.046 1.00 76.08 ? 155 MET A C 1 ATOM 1181 O O . MET A 1 155 ? 50.874 -49.731 37.351 1.00 75.04 ? 155 MET A O 1 ATOM 1182 C CB . MET A 1 155 ? 48.122 -49.708 38.946 1.00 73.88 ? 155 MET A CB 1 ATOM 1183 C CG . MET A 1 155 ? 47.137 -50.852 38.981 1.00 74.14 ? 155 MET A CG 1 ATOM 1184 S SD . MET A 1 155 ? 45.673 -50.353 39.885 1.00 73.78 ? 155 MET A SD 1 ATOM 1185 C CE . MET A 1 155 ? 45.070 -51.944 40.437 1.00 75.90 ? 155 MET A CE 1 ATOM 1186 N N . THR A 1 156 ? 50.192 -51.850 37.752 1.00 76.99 ? 156 THR A N 1 ATOM 1187 C CA . THR A 1 156 ? 50.913 -52.449 36.632 1.00 77.59 ? 156 THR A CA 1 ATOM 1188 C C . THR A 1 156 ? 49.980 -53.345 35.800 1.00 76.34 ? 156 THR A C 1 ATOM 1189 O O . THR A 1 156 ? 49.660 -54.458 36.213 1.00 78.08 ? 156 THR A O 1 ATOM 1190 C CB . THR A 1 156 ? 52.116 -53.281 37.141 1.00 81.52 ? 156 THR A CB 1 ATOM 1191 O OG1 . THR A 1 156 ? 52.680 -52.675 38.317 1.00 82.99 ? 156 THR A OG1 1 ATOM 1192 C CG2 . THR A 1 156 ? 53.180 -53.385 36.069 1.00 82.61 ? 156 THR A CG2 1 ATOM 1193 N N . LYS A 1 157 ? 49.556 -52.855 34.630 1.00 73.60 ? 157 LYS A N 1 ATOM 1194 C CA . LYS A 1 157 ? 48.594 -53.569 33.766 1.00 72.25 ? 157 LYS A CA 1 ATOM 1195 C C . LYS A 1 157 ? 49.157 -53.915 32.391 1.00 72.25 ? 157 LYS A C 1 ATOM 1196 O O . LYS A 1 157 ? 49.743 -53.062 31.720 1.00 71.20 ? 157 LYS A O 1 ATOM 1197 C CB . LYS A 1 157 ? 47.316 -52.740 33.587 1.00 69.08 ? 157 LYS A CB 1 ATOM 1198 C CG . LYS A 1 157 ? 46.143 -53.157 34.466 1.00 69.12 ? 157 LYS A CG 1 ATOM 1199 C CD . LYS A 1 157 ? 46.525 -53.290 35.928 1.00 71.20 ? 157 LYS A CD 1 ATOM 1200 C CE . LYS A 1 157 ? 45.371 -53.824 36.743 1.00 71.65 ? 157 LYS A CE 1 ATOM 1201 N NZ . LYS A 1 157 ? 45.851 -54.251 38.081 1.00 74.51 ? 157 LYS A NZ 1 ATOM 1202 N N . SER A 1 158 ? 48.948 -55.166 31.975 1.00 73.53 ? 158 SER A N 1 ATOM 1203 C CA . SER A 1 158 ? 49.401 -55.661 30.669 1.00 73.99 ? 158 SER A CA 1 ATOM 1204 C C . SER A 1 158 ? 48.273 -56.010 29.693 1.00 71.69 ? 158 SER A C 1 ATOM 1205 O O . SER A 1 158 ? 47.176 -56.400 30.095 1.00 71.10 ? 158 SER A O 1 ATOM 1206 C CB . SER A 1 158 ? 50.261 -56.915 30.854 1.00 78.28 ? 158 SER A CB 1 ATOM 1207 O OG . SER A 1 158 ? 50.834 -57.309 29.618 1.00 79.41 ? 158 SER A OG 1 ATOM 1208 N N . TYR A 1 159 ? 48.568 -55.876 28.404 1.00 70.56 ? 159 TYR A N 1 ATOM 1209 C CA . TYR A 1 159 ? 47.730 -56.438 27.346 1.00 69.42 ? 159 TYR A CA 1 ATOM 1210 C C . TYR A 1 159 ? 48.615 -56.988 26.243 1.00 71.17 ? 159 TYR A C 1 ATOM 1211 O O . TYR A 1 159 ? 49.418 -56.260 25.661 1.00 70.55 ? 159 TYR A O 1 ATOM 1212 C CB . TYR A 1 159 ? 46.780 -55.390 26.765 1.00 65.60 ? 159 TYR A CB 1 ATOM 1213 C CG . TYR A 1 159 ? 46.025 -55.857 25.528 1.00 64.66 ? 159 TYR A CG 1 ATOM 1214 C CD1 . TYR A 1 159 ? 44.894 -56.652 25.641 1.00 64.88 ? 159 TYR A CD1 1 ATOM 1215 C CD2 . TYR A 1 159 ? 46.449 -55.504 24.250 1.00 63.84 ? 159 TYR A CD2 1 ATOM 1216 C CE1 . TYR A 1 159 ? 44.202 -57.085 24.523 1.00 64.42 ? 159 TYR A CE1 1 ATOM 1217 C CE2 . TYR A 1 159 ? 45.765 -55.930 23.125 1.00 63.32 ? 159 TYR A CE2 1 ATOM 1218 C CZ . TYR A 1 159 ? 44.643 -56.722 23.267 1.00 63.55 ? 159 TYR A CZ 1 ATOM 1219 O OH . TYR A 1 159 ? 43.959 -57.142 22.153 1.00 63.21 ? 159 TYR A OH 1 ATOM 1220 N N . LYS A 1 160 ? 48.470 -58.279 25.966 1.00 73.66 ? 160 LYS A N 1 ATOM 1221 C CA . LYS A 1 160 ? 49.163 -58.905 24.853 1.00 75.77 ? 160 LYS A CA 1 ATOM 1222 C C . LYS A 1 160 ? 48.266 -58.862 23.621 1.00 73.41 ? 160 LYS A C 1 ATOM 1223 O O . LYS A 1 160 ? 47.040 -58.922 23.731 1.00 71.61 ? 160 LYS A O 1 ATOM 1224 C CB . LYS A 1 160 ? 49.511 -60.350 25.195 1.00 80.55 ? 160 LYS A CB 1 ATOM 1225 C CG . LYS A 1 160 ? 50.578 -60.956 24.301 1.00 84.12 ? 160 LYS A CG 1 ATOM 1226 C CD . LYS A 1 160 ? 50.802 -62.416 24.649 1.00 89.34 ? 160 LYS A CD 1 ATOM 1227 C CE . LYS A 1 160 ? 52.189 -62.878 24.243 1.00 93.76 ? 160 LYS A CE 1 ATOM 1228 N NZ . LYS A 1 160 ? 52.420 -62.732 22.781 1.00 93.47 ? 160 LYS A NZ 1 ATOM 1229 N N . ASN A 1 161 ? 48.886 -58.740 22.453 1.00 73.51 ? 161 ASN A N 1 ATOM 1230 C CA . ASN A 1 161 ? 48.162 -58.769 21.194 1.00 71.84 ? 161 ASN A CA 1 ATOM 1231 C C . ASN A 1 161 ? 48.277 -60.153 20.565 1.00 75.40 ? 161 ASN A C 1 ATOM 1232 O O . ASN A 1 161 ? 49.273 -60.471 19.912 1.00 77.90 ? 161 ASN A O 1 ATOM 1233 C CB . ASN A 1 161 ? 48.694 -57.700 20.243 1.00 69.91 ? 161 ASN A CB 1 ATOM 1234 C CG . ASN A 1 161 ? 47.867 -57.584 18.977 1.00 68.02 ? 161 ASN A CG 1 ATOM 1235 O OD1 . ASN A 1 161 ? 46.822 -58.219 18.843 1.00 67.78 ? 161 ASN A OD1 1 ATOM 1236 N ND2 . ASN A 1 161 ? 48.332 -56.768 18.041 1.00 66.90 ? 161 ASN A ND2 1 ATOM 1237 N N . THR A 1 162 ? 47.245 -60.967 20.766 1.00 75.92 ? 162 THR A N 1 ATOM 1238 C CA . THR A 1 162 ? 47.233 -62.341 20.277 1.00 79.84 ? 162 THR A CA 1 ATOM 1239 C C . THR A 1 162 ? 46.738 -62.477 18.832 1.00 79.20 ? 162 THR A C 1 ATOM 1240 O O . THR A 1 162 ? 46.704 -63.582 18.303 1.00 82.60 ? 162 THR A O 1 ATOM 1241 C CB . THR A 1 162 ? 46.377 -63.240 21.190 1.00 81.60 ? 162 THR A CB 1 ATOM 1242 O OG1 . THR A 1 162 ? 45.059 -62.694 21.307 1.00 78.02 ? 162 THR A OG1 1 ATOM 1243 C CG2 . THR A 1 162 ? 47.004 -63.340 22.575 1.00 83.34 ? 162 THR A CG2 1 ATOM 1244 N N . ARG A 1 163 ? 46.367 -61.369 18.196 1.00 75.11 ? 163 ARG A N 1 ATOM 1245 C CA . ARG A 1 163 ? 45.908 -61.401 16.807 1.00 74.52 ? 163 ARG A CA 1 ATOM 1246 C C . ARG A 1 163 ? 47.056 -61.143 15.836 1.00 75.57 ? 163 ARG A C 1 ATOM 1247 O O . ARG A 1 163 ? 48.158 -60.800 16.260 1.00 76.45 ? 163 ARG A O 1 ATOM 1248 C CB . ARG A 1 163 ? 44.766 -60.404 16.605 1.00 70.14 ? 163 ARG A CB 1 ATOM 1249 C CG . ARG A 1 163 ? 43.461 -60.928 17.176 1.00 70.03 ? 163 ARG A CG 1 ATOM 1250 C CD . ARG A 1 163 ? 42.367 -59.881 17.251 1.00 66.00 ? 163 ARG A CD 1 ATOM 1251 N NE . ARG A 1 163 ? 41.945 -59.415 15.930 1.00 64.30 ? 163 ARG A NE 1 ATOM 1252 C CZ . ARG A 1 163 ? 40.781 -58.822 15.666 1.00 61.74 ? 163 ARG A CZ 1 ATOM 1253 N NH1 . ARG A 1 163 ? 39.877 -58.624 16.621 1.00 60.61 ? 163 ARG A NH1 1 ATOM 1254 N NH2 . ARG A 1 163 ? 40.509 -58.431 14.425 1.00 60.60 ? 163 ARG A NH2 1 ATOM 1255 N N . LYS A 1 164 ? 46.788 -61.312 14.541 1.00 75.76 ? 164 LYS A N 1 ATOM 1256 C CA . LYS A 1 164 ? 47.819 -61.237 13.497 1.00 77.53 ? 164 LYS A CA 1 ATOM 1257 C C . LYS A 1 164 ? 48.009 -59.843 12.889 1.00 73.90 ? 164 LYS A C 1 ATOM 1258 O O . LYS A 1 164 ? 48.851 -59.667 12.009 1.00 75.04 ? 164 LYS A O 1 ATOM 1259 C CB . LYS A 1 164 ? 47.517 -62.237 12.368 1.00 80.49 ? 164 LYS A CB 1 ATOM 1260 C CG . LYS A 1 164 ? 47.685 -63.702 12.748 1.00 85.46 ? 164 LYS A CG 1 ATOM 1261 C CD . LYS A 1 164 ? 48.068 -64.537 11.534 1.00 89.49 ? 164 LYS A CD 1 ATOM 1262 C CE . LYS A 1 164 ? 48.085 -66.030 11.836 1.00 94.88 ? 164 LYS A CE 1 ATOM 1263 N NZ . LYS A 1 164 ? 46.730 -66.634 11.690 1.00 94.84 ? 164 LYS A NZ 1 ATOM 1264 N N . SER A 1 165 ? 47.231 -58.862 13.339 1.00 69.68 ? 165 SER A N 1 ATOM 1265 C CA . SER A 1 165 ? 47.381 -57.482 12.866 1.00 66.50 ? 165 SER A CA 1 ATOM 1266 C C . SER A 1 165 ? 47.590 -56.533 14.048 1.00 64.24 ? 165 SER A C 1 ATOM 1267 O O . SER A 1 165 ? 47.166 -56.837 15.165 1.00 63.95 ? 165 SER A O 1 ATOM 1268 C CB . SER A 1 165 ? 46.165 -57.050 12.041 1.00 63.88 ? 165 SER A CB 1 ATOM 1269 O OG . SER A 1 165 ? 45.012 -56.895 12.852 1.00 61.73 ? 165 SER A OG 1 ATOM 1270 N N . PRO A 1 166 ? 48.239 -55.378 13.807 1.00 62.79 ? 166 PRO A N 1 ATOM 1271 C CA . PRO A 1 166 ? 48.550 -54.469 14.908 1.00 61.37 ? 166 PRO A CA 1 ATOM 1272 C C . PRO A 1 166 ? 47.306 -53.943 15.612 1.00 58.26 ? 166 PRO A C 1 ATOM 1273 O O . PRO A 1 166 ? 46.314 -53.620 14.955 1.00 56.35 ? 166 PRO A O 1 ATOM 1274 C CB . PRO A 1 166 ? 49.292 -53.314 14.225 1.00 60.91 ? 166 PRO A CB 1 ATOM 1275 C CG . PRO A 1 166 ? 49.719 -53.828 12.898 1.00 62.85 ? 166 PRO A CG 1 ATOM 1276 C CD . PRO A 1 166 ? 48.700 -54.851 12.511 1.00 62.93 ? 166 PRO A CD 1 ATOM 1277 N N . ALA A 1 167 ? 47.361 -53.865 16.936 1.00 58.02 ? 167 ALA A N 1 ATOM 1278 C CA . ALA A 1 167 ? 46.259 -53.326 17.720 1.00 55.50 ? 167 ALA A CA 1 ATOM 1279 C C . ALA A 1 167 ? 46.501 -51.856 18.039 1.00 53.82 ? 167 ALA A C 1 ATOM 1280 O O . ALA A 1 167 ? 47.553 -51.489 18.565 1.00 55.05 ? 167 ALA A O 1 ATOM 1281 C CB . ALA A 1 167 ? 46.087 -54.118 19.001 1.00 56.61 ? 167 ALA A CB 1 ATOM 1282 N N . LEU A 1 168 ? 45.526 -51.013 17.717 1.00 51.49 ? 168 LEU A N 1 ATOM 1283 C CA . LEU A 1 168 ? 45.567 -49.616 18.123 1.00 50.16 ? 168 LEU A CA 1 ATOM 1284 C C . LEU A 1 168 ? 45.103 -49.492 19.573 1.00 49.63 ? 168 LEU A C 1 ATOM 1285 O O . LEU A 1 168 ? 43.964 -49.815 19.896 1.00 48.65 ? 168 LEU A O 1 ATOM 1286 C CB . LEU A 1 168 ? 44.693 -48.764 17.204 1.00 48.40 ? 168 LEU A CB 1 ATOM 1287 C CG . LEU A 1 168 ? 44.356 -47.352 17.684 1.00 47.25 ? 168 LEU A CG 1 ATOM 1288 C CD1 . LEU A 1 168 ? 45.614 -46.567 18.021 1.00 48.42 ? 168 LEU A CD1 1 ATOM 1289 C CD2 . LEU A 1 168 ? 43.538 -46.641 16.619 1.00 46.10 ? 168 LEU A CD2 1 ATOM 1290 N N . ILE A 1 169 ? 45.997 -49.023 20.435 1.00 50.53 ? 169 ILE A N 1 ATOM 1291 C CA . ILE A 1 169 ? 45.695 -48.822 21.844 1.00 50.45 ? 169 ILE A CA 1 ATOM 1292 C C . ILE A 1 169 ? 45.616 -47.323 22.136 1.00 49.68 ? 169 ILE A C 1 ATOM 1293 O O . ILE A 1 169 ? 46.495 -46.560 21.740 1.00 50.31 ? 169 ILE A O 1 ATOM 1294 C CB . ILE A 1 169 ? 46.778 -49.450 22.750 1.00 52.59 ? 169 ILE A CB 1 ATOM 1295 C CG1 . ILE A 1 169 ? 47.057 -50.906 22.349 1.00 54.24 ? 169 ILE A CG1 1 ATOM 1296 C CG2 . ILE A 1 169 ? 46.365 -49.375 24.219 1.00 52.52 ? 169 ILE A CG2 1 ATOM 1297 C CD1 . ILE A 1 169 ? 45.949 -51.872 22.703 1.00 54.01 ? 169 ILE A CD1 1 ATOM 1298 N N . VAL A 1 170 ? 44.556 -46.911 22.820 1.00 48.69 ? 170 VAL A N 1 ATOM 1299 C CA . VAL A 1 170 ? 44.357 -45.517 23.174 1.00 48.45 ? 170 VAL A CA 1 ATOM 1300 C C . VAL A 1 170 ? 44.178 -45.420 24.677 1.00 49.07 ? 170 VAL A C 1 ATOM 1301 O O . VAL A 1 170 ? 43.487 -46.232 25.272 1.00 48.83 ? 170 VAL A O 1 ATOM 1302 C CB . VAL A 1 170 ? 43.111 -44.923 22.482 1.00 47.02 ? 170 VAL A CB 1 ATOM 1303 C CG1 . VAL A 1 170 ? 42.735 -43.576 23.088 1.00 47.18 ? 170 VAL A CG1 1 ATOM 1304 C CG2 . VAL A 1 170 ? 43.351 -44.774 20.991 1.00 46.77 ? 170 VAL A CG2 1 ATOM 1305 N N . TRP A 1 171 ? 44.810 -44.425 25.282 1.00 50.22 ? 171 TRP A N 1 ATOM 1306 C CA . TRP A 1 171 ? 44.567 -44.099 26.682 1.00 51.15 ? 171 TRP A CA 1 ATOM 1307 C C . TRP A 1 171 ? 44.613 -42.584 26.860 1.00 51.86 ? 171 TRP A C 1 ATOM 1308 O O . TRP A 1 171 ? 45.101 -41.860 25.990 1.00 52.02 ? 171 TRP A O 1 ATOM 1309 C CB . TRP A 1 171 ? 45.578 -44.784 27.601 1.00 52.75 ? 171 TRP A CB 1 ATOM 1310 C CG . TRP A 1 171 ? 46.960 -44.305 27.421 1.00 54.27 ? 171 TRP A CG 1 ATOM 1311 C CD1 . TRP A 1 171 ? 47.629 -43.403 28.199 1.00 55.79 ? 171 TRP A CD1 1 ATOM 1312 C CD2 . TRP A 1 171 ? 47.861 -44.690 26.389 1.00 54.96 ? 171 TRP A CD2 1 ATOM 1313 N NE1 . TRP A 1 171 ? 48.895 -43.209 27.712 1.00 57.28 ? 171 TRP A NE1 1 ATOM 1314 C CE2 . TRP A 1 171 ? 49.065 -43.990 26.601 1.00 56.82 ? 171 TRP A CE2 1 ATOM 1315 C CE3 . TRP A 1 171 ? 47.769 -45.564 25.303 1.00 54.42 ? 171 TRP A CE3 1 ATOM 1316 C CZ2 . TRP A 1 171 ? 50.166 -44.129 25.762 1.00 58.28 ? 171 TRP A CZ2 1 ATOM 1317 C CZ3 . TRP A 1 171 ? 48.857 -45.704 24.472 1.00 55.72 ? 171 TRP A CZ3 1 ATOM 1318 C CH2 . TRP A 1 171 ? 50.047 -44.991 24.703 1.00 57.67 ? 171 TRP A CH2 1 ATOM 1319 N N . GLY A 1 172 ? 44.082 -42.116 27.982 1.00 52.64 ? 172 GLY A N 1 ATOM 1320 C CA . GLY A 1 172 ? 43.982 -40.690 28.233 1.00 53.95 ? 172 GLY A CA 1 ATOM 1321 C C . GLY A 1 172 ? 44.758 -40.249 29.453 1.00 56.14 ? 172 GLY A C 1 ATOM 1322 O O . GLY A 1 172 ? 45.319 -41.071 30.178 1.00 56.68 ? 172 GLY A O 1 ATOM 1323 N N . ILE A 1 173 ? 44.814 -38.937 29.651 1.00 57.91 ? 173 ILE A N 1 ATOM 1324 C CA . ILE A 1 173 ? 45.352 -38.356 30.875 1.00 60.36 ? 173 ILE A CA 1 ATOM 1325 C C . ILE A 1 173 ? 44.487 -37.165 31.256 1.00 61.60 ? 173 ILE A C 1 ATOM 1326 O O . ILE A 1 173 ? 44.198 -36.311 30.416 1.00 61.85 ? 173 ILE A O 1 ATOM 1327 C CB . ILE A 1 173 ? 46.829 -37.932 30.721 1.00 62.23 ? 173 ILE A CB 1 ATOM 1328 C CG1 . ILE A 1 173 ? 47.739 -39.160 30.615 1.00 62.05 ? 173 ILE A CG1 1 ATOM 1329 C CG2 . ILE A 1 173 ? 47.272 -37.065 31.890 1.00 64.87 ? 173 ILE A CG2 1 ATOM 1330 C CD1 . ILE A 1 173 ? 47.720 -40.059 31.836 1.00 62.41 ? 173 ILE A CD1 1 ATOM 1331 N N . HIS A 1 174 ? 44.067 -37.119 32.517 1.00 62.69 ? 174 HIS A N 1 ATOM 1332 C CA . HIS A 1 174 ? 43.155 -36.080 32.969 1.00 64.43 ? 174 HIS A CA 1 ATOM 1333 C C . HIS A 1 174 ? 43.891 -34.860 33.521 1.00 67.86 ? 174 HIS A C 1 ATOM 1334 O O . HIS A 1 174 ? 44.926 -34.982 34.187 1.00 69.26 ? 174 HIS A O 1 ATOM 1335 C CB . HIS A 1 174 ? 42.202 -36.622 34.023 1.00 64.18 ? 174 HIS A CB 1 ATOM 1336 C CG . HIS A 1 174 ? 41.132 -35.654 34.407 1.00 65.73 ? 174 HIS A CG 1 ATOM 1337 N ND1 . HIS A 1 174 ? 40.819 -35.367 35.717 1.00 67.51 ? 174 HIS A ND1 1 ATOM 1338 C CD2 . HIS A 1 174 ? 40.314 -34.887 33.648 1.00 66.07 ? 174 HIS A CD2 1 ATOM 1339 C CE1 . HIS A 1 174 ? 39.843 -34.478 35.749 1.00 68.97 ? 174 HIS A CE1 1 ATOM 1340 N NE2 . HIS A 1 174 ? 39.521 -34.166 34.507 1.00 68.06 ? 174 HIS A NE2 1 ATOM 1341 N N . HIS A 1 175 ? 43.338 -33.686 33.231 1.00 69.80 ? 175 HIS A N 1 ATOM 1342 C CA . HIS A 1 175 ? 43.870 -32.424 33.717 1.00 73.28 ? 175 HIS A CA 1 ATOM 1343 C C . HIS A 1 175 ? 42.785 -31.638 34.434 1.00 75.72 ? 175 HIS A C 1 ATOM 1344 O O . HIS A 1 175 ? 42.086 -30.822 33.826 1.00 76.72 ? 175 HIS A O 1 ATOM 1345 C CB . HIS A 1 175 ? 44.437 -31.614 32.564 1.00 74.23 ? 175 HIS A CB 1 ATOM 1346 C CG . HIS A 1 175 ? 45.602 -32.265 31.893 1.00 73.14 ? 175 HIS A CG 1 ATOM 1347 N ND1 . HIS A 1 175 ? 46.595 -32.913 32.595 1.00 73.34 ? 175 HIS A ND1 1 ATOM 1348 C CD2 . HIS A 1 175 ? 45.933 -32.376 30.584 1.00 71.98 ? 175 HIS A CD2 1 ATOM 1349 C CE1 . HIS A 1 175 ? 47.485 -33.397 31.748 1.00 72.52 ? 175 HIS A CE1 1 ATOM 1350 N NE2 . HIS A 1 175 ? 47.108 -33.084 30.522 1.00 71.55 ? 175 HIS A NE2 1 ATOM 1351 N N . SER A 1 176 ? 42.662 -31.883 35.736 1.00 77.14 ? 176 SER A N 1 ATOM 1352 C CA . SER A 1 176 ? 41.654 -31.219 36.555 1.00 79.71 ? 176 SER A CA 1 ATOM 1353 C C . SER A 1 176 ? 41.825 -29.705 36.606 1.00 83.89 ? 176 SER A C 1 ATOM 1354 O O . SER A 1 176 ? 42.909 -29.179 36.357 1.00 85.32 ? 176 SER A O 1 ATOM 1355 C CB . SER A 1 176 ? 41.661 -31.768 37.982 1.00 80.38 ? 176 SER A CB 1 ATOM 1356 O OG . SER A 1 176 ? 40.803 -32.886 38.105 1.00 78.01 ? 176 SER A OG 1 ATOM 1357 N N . VAL A 1 177 ? 40.736 -29.022 36.951 1.00 86.29 ? 177 VAL A N 1 ATOM 1358 C CA . VAL A 1 177 ? 40.717 -27.564 37.034 1.00 90.92 ? 177 VAL A CA 1 ATOM 1359 C C . VAL A 1 177 ? 41.759 -27.082 38.035 1.00 93.90 ? 177 VAL A C 1 ATOM 1360 O O . VAL A 1 177 ? 42.545 -26.185 37.736 1.00 96.47 ? 177 VAL A O 1 ATOM 1361 C CB . VAL A 1 177 ? 39.326 -27.032 37.463 1.00 93.28 ? 177 VAL A CB 1 ATOM 1362 C CG1 . VAL A 1 177 ? 39.330 -25.509 37.540 1.00 98.34 ? 177 VAL A CG1 1 ATOM 1363 C CG2 . VAL A 1 177 ? 38.240 -27.528 36.510 1.00 90.84 ? 177 VAL A CG2 1 ATOM 1364 N N . SER A 1 178 ? 41.762 -27.689 39.219 1.00 93.71 ? 178 SER A N 1 ATOM 1365 C CA . SER A 1 178 ? 42.664 -27.287 40.294 1.00 96.68 ? 178 SER A CA 1 ATOM 1366 C C . SER A 1 178 ? 43.831 -28.259 40.460 1.00 94.32 ? 178 SER A C 1 ATOM 1367 O O . SER A 1 178 ? 43.885 -29.305 39.810 1.00 90.47 ? 178 SER A O 1 ATOM 1368 C CB . SER A 1 178 ? 41.891 -27.191 41.610 1.00 98.87 ? 178 SER A CB 1 ATOM 1369 O OG . SER A 1 178 ? 40.770 -26.334 41.487 1.00 101.24 ? 178 SER A OG 1 ATOM 1370 N N . THR A 1 179 ? 44.773 -27.877 41.319 1.00 96.93 ? 179 THR A N 1 ATOM 1371 C CA . THR A 1 179 ? 45.789 -28.791 41.836 1.00 95.60 ? 179 THR A CA 1 ATOM 1372 C C . THR A 1 179 ? 45.182 -29.584 42.996 1.00 94.78 ? 179 THR A C 1 ATOM 1373 O O . THR A 1 179 ? 45.661 -30.667 43.342 1.00 92.77 ? 179 THR A O 1 ATOM 1374 C CB . THR A 1 179 ? 47.028 -28.032 42.355 1.00 99.37 ? 179 THR A CB 1 ATOM 1375 O OG1 . THR A 1 179 ? 46.656 -27.211 43.469 1.00 103.24 ? 179 THR A OG1 1 ATOM 1376 C CG2 . THR A 1 179 ? 47.635 -27.157 41.261 1.00 100.84 ? 179 THR A CG2 1 ATOM 1377 N N . ALA A 1 180 ? 44.137 -29.015 43.596 1.00 96.62 ? 180 ALA A N 1 ATOM 1378 C CA . ALA A 1 180 ? 43.378 -29.658 44.667 1.00 96.39 ? 180 ALA A CA 1 ATOM 1379 C C . ALA A 1 180 ? 42.423 -30.725 44.141 1.00 92.04 ? 180 ALA A C 1 ATOM 1380 O O . ALA A 1 180 ? 42.090 -31.664 44.858 1.00 90.83 ? 180 ALA A O 1 ATOM 1381 C CB . ALA A 1 180 ? 42.599 -28.616 45.450 1.00 100.72 ? 180 ALA A CB 1 ATOM 1382 N N . GLU A 1 181 ? 41.978 -30.581 42.895 1.00 89.93 ? 181 GLU A N 1 ATOM 1383 C CA . GLU A 1 181 ? 41.081 -31.569 42.287 1.00 85.92 ? 181 GLU A CA 1 ATOM 1384 C C . GLU A 1 181 ? 41.832 -32.837 41.909 1.00 82.13 ? 181 GLU A C 1 ATOM 1385 O O . GLU A 1 181 ? 41.258 -33.923 41.933 1.00 79.82 ? 181 GLU A O 1 ATOM 1386 C CB . GLU A 1 181 ? 40.350 -30.985 41.075 1.00 85.44 ? 181 GLU A CB 1 ATOM 1387 C CG . GLU A 1 181 ? 39.222 -30.028 41.432 1.00 88.57 ? 181 GLU A CG 1 ATOM 1388 C CD . GLU A 1 181 ? 38.255 -30.614 42.446 1.00 88.90 ? 181 GLU A CD 1 ATOM 1389 O OE1 . GLU A 1 181 ? 37.530 -31.569 42.097 1.00 86.12 ? 181 GLU A OE1 1 ATOM 1390 O OE2 . GLU A 1 181 ? 38.243 -30.131 43.600 1.00 92.01 ? 181 GLU A OE2 1 ATOM 1391 N N . GLN A 1 182 ? 43.113 -32.697 41.577 1.00 81.80 ? 182 GLN A N 1 ATOM 1392 C CA . GLN A 1 182 ? 43.975 -33.853 41.331 1.00 79.19 ? 182 GLN A CA 1 ATOM 1393 C C . GLN A 1 182 ? 44.161 -34.698 42.586 1.00 79.32 ? 182 GLN A C 1 ATOM 1394 O O . GLN A 1 182 ? 44.281 -35.918 42.490 1.00 77.32 ? 182 GLN A O 1 ATOM 1395 C CB . GLN A 1 182 ? 45.348 -33.425 40.794 1.00 80.10 ? 182 GLN A CB 1 ATOM 1396 C CG . GLN A 1 182 ? 46.391 -34.539 40.797 1.00 78.78 ? 182 GLN A CG 1 ATOM 1397 C CD . GLN A 1 182 ? 47.637 -34.198 39.997 1.00 79.51 ? 182 GLN A CD 1 ATOM 1398 O OE1 . GLN A 1 182 ? 47.553 -33.722 38.867 1.00 78.99 ? 182 GLN A OE1 1 ATOM 1399 N NE2 . GLN A 1 182 ? 48.805 -34.461 40.576 1.00 80.99 ? 182 GLN A NE2 1 ATOM 1400 N N . THR A 1 183 ? 44.199 -34.058 43.755 1.00 81.86 ? 183 THR A N 1 ATOM 1401 C CA . THR A 1 183 ? 44.359 -34.794 45.012 1.00 82.33 ? 183 THR A CA 1 ATOM 1402 C C . THR A 1 183 ? 43.063 -35.518 45.397 1.00 80.81 ? 183 THR A C 1 ATOM 1403 O O . THR A 1 183 ? 43.102 -36.684 45.786 1.00 79.56 ? 183 THR A O 1 ATOM 1404 C CB . THR A 1 183 ? 44.842 -33.897 46.181 1.00 86.23 ? 183 THR A CB 1 ATOM 1405 O OG1 . THR A 1 183 ? 43.770 -33.072 46.659 1.00 88.23 ? 183 THR A OG1 1 ATOM 1406 C CG2 . THR A 1 183 ? 46.026 -33.031 45.752 1.00 87.87 ? 183 THR A CG2 1 ATOM 1407 N N . LYS A 1 184 ? 41.927 -34.831 45.277 1.00 110.33 ? 184 LYS A N 1 ATOM 1408 C CA . LYS A 1 184 ? 40.617 -35.448 45.516 1.00 107.96 ? 184 LYS A CA 1 ATOM 1409 C C . LYS A 1 184 ? 40.431 -36.695 44.654 1.00 106.44 ? 184 LYS A C 1 ATOM 1410 O O . LYS A 1 184 ? 40.064 -37.756 45.157 1.00 106.08 ? 184 LYS A O 1 ATOM 1411 C CB . LYS A 1 184 ? 39.486 -34.451 45.245 1.00 107.33 ? 184 LYS A CB 1 ATOM 1412 C CG . LYS A 1 184 ? 38.110 -35.082 45.093 1.00 105.45 ? 184 LYS A CG 1 ATOM 1413 C CD . LYS A 1 184 ? 37.014 -34.033 45.088 1.00 105.88 ? 184 LYS A CD 1 ATOM 1414 C CE . LYS A 1 184 ? 35.685 -34.624 44.647 1.00 104.94 ? 184 LYS A CE 1 ATOM 1415 N NZ . LYS A 1 184 ? 34.528 -33.770 45.030 1.00 105.86 ? 184 LYS A NZ 1 ATOM 1416 N N . LEU A 1 185 ? 40.693 -36.563 43.357 1.00 106.09 ? 185 LEU A N 1 ATOM 1417 C CA . LEU A 1 185 ? 40.498 -37.673 42.430 1.00 105.04 ? 185 LEU A CA 1 ATOM 1418 C C . LEU A 1 185 ? 41.406 -38.869 42.745 1.00 105.83 ? 185 LEU A C 1 ATOM 1419 O O . LEU A 1 185 ? 40.906 -39.962 43.027 1.00 105.84 ? 185 LEU A O 1 ATOM 1420 C CB . LEU A 1 185 ? 40.677 -37.223 40.973 1.00 104.75 ? 185 LEU A CB 1 ATOM 1421 C CG . LEU A 1 185 ? 39.621 -36.266 40.398 1.00 104.62 ? 185 LEU A CG 1 ATOM 1422 C CD1 . LEU A 1 185 ? 39.801 -36.163 38.891 1.00 104.64 ? 185 LEU A CD1 1 ATOM 1423 C CD2 . LEU A 1 185 ? 38.192 -36.674 40.746 1.00 103.99 ? 185 LEU A CD2 1 ATOM 1424 N N . TYR A 1 186 ? 42.722 -38.654 42.738 1.00 107.17 ? 186 TYR A N 1 ATOM 1425 C CA . TYR A 1 186 ? 43.689 -39.759 42.834 1.00 108.61 ? 186 TYR A CA 1 ATOM 1426 C C . TYR A 1 186 ? 44.678 -39.678 44.009 1.00 111.31 ? 186 TYR A C 1 ATOM 1427 O O . TYR A 1 186 ? 45.673 -40.406 44.022 1.00 113.31 ? 186 TYR A O 1 ATOM 1428 C CB . TYR A 1 186 ? 44.504 -39.864 41.542 1.00 108.79 ? 186 TYR A CB 1 ATOM 1429 C CG . TYR A 1 186 ? 43.792 -39.439 40.278 1.00 106.91 ? 186 TYR A CG 1 ATOM 1430 C CD1 . TYR A 1 186 ? 43.738 -38.098 39.911 1.00 106.96 ? 186 TYR A CD1 1 ATOM 1431 C CD2 . TYR A 1 186 ? 43.215 -40.377 39.421 1.00 105.92 ? 186 TYR A CD2 1 ATOM 1432 C CE1 . TYR A 1 186 ? 43.113 -37.699 38.740 1.00 106.00 ? 186 TYR A CE1 1 ATOM 1433 C CE2 . TYR A 1 186 ? 42.592 -39.981 38.246 1.00 104.79 ? 186 TYR A CE2 1 ATOM 1434 C CZ . TYR A 1 186 ? 42.541 -38.643 37.915 1.00 104.77 ? 186 TYR A CZ 1 ATOM 1435 O OH . TYR A 1 186 ? 41.924 -38.238 36.759 1.00 104.26 ? 186 TYR A OH 1 ATOM 1436 N N . GLY A 1 187 ? 44.413 -38.814 44.987 1.00 111.88 ? 187 GLY A N 1 ATOM 1437 C CA . GLY A 1 187 ? 45.334 -38.618 46.113 1.00 115.20 ? 187 GLY A CA 1 ATOM 1438 C C . GLY A 1 187 ? 46.436 -37.629 45.773 1.00 117.53 ? 187 GLY A C 1 ATOM 1439 O O . GLY A 1 187 ? 46.773 -37.439 44.603 1.00 116.79 ? 187 GLY A O 1 ATOM 1440 N N . SER A 1 188 ? 47.000 -36.994 46.797 1.00 120.79 ? 188 SER A N 1 ATOM 1441 C CA . SER A 1 188 ? 48.013 -35.959 46.589 1.00 124.08 ? 188 SER A CA 1 ATOM 1442 C C . SER A 1 188 ? 49.359 -36.556 46.186 1.00 127.15 ? 188 SER A C 1 ATOM 1443 O O . SER A 1 188 ? 49.608 -37.747 46.381 1.00 127.51 ? 188 SER A O 1 ATOM 1444 C CB . SER A 1 188 ? 48.179 -35.105 47.849 1.00 127.42 ? 188 SER A CB 1 ATOM 1445 O OG . SER A 1 188 ? 48.767 -35.851 48.897 1.00 130.43 ? 188 SER A OG 1 ATOM 1446 N N . GLY A 1 189 ? 50.219 -35.711 45.623 1.00 129.94 ? 189 GLY A N 1 ATOM 1447 C CA . GLY A 1 189 ? 51.559 -36.115 45.208 1.00 133.58 ? 189 GLY A CA 1 ATOM 1448 C C . GLY A 1 189 ? 51.689 -36.161 43.702 1.00 131.28 ? 189 GLY A C 1 ATOM 1449 O O . GLY A 1 189 ? 50.688 -36.181 42.990 1.00 126.84 ? 189 GLY A O 1 ATOM 1450 N N . ASN A 1 190 ? 52.928 -36.169 43.214 1.00 134.79 ? 190 ASN A N 1 ATOM 1451 C CA . ASN A 1 190 ? 53.194 -36.239 41.768 1.00 133.08 ? 190 ASN A CA 1 ATOM 1452 C C . ASN A 1 190 ? 52.929 -37.636 41.200 1.00 129.66 ? 190 ASN A C 1 ATOM 1453 O O . ASN A 1 190 ? 53.498 -38.624 41.665 1.00 131.79 ? 190 ASN A O 1 ATOM 1454 C CB . ASN A 1 190 ? 54.622 -35.767 41.421 1.00 138.51 ? 190 ASN A CB 1 ATOM 1455 C CG . ASN A 1 190 ? 55.670 -36.223 42.430 1.00 144.14 ? 190 ASN A CG 1 ATOM 1456 O OD1 . ASN A 1 190 ? 55.435 -37.121 43.239 1.00 143.95 ? 190 ASN A OD1 1 ATOM 1457 N ND2 . ASN A 1 190 ? 56.835 -35.596 42.385 1.00 149.97 ? 190 ASN A ND2 1 ATOM 1458 N N . LYS A 1 191 ? 52.063 -37.707 40.191 1.00 125.01 ? 191 LYS A N 1 ATOM 1459 C CA . LYS A 1 191 ? 51.624 -38.983 39.629 1.00 122.02 ? 191 LYS A CA 1 ATOM 1460 C C . LYS A 1 191 ? 52.403 -39.243 38.346 1.00 122.41 ? 191 LYS A C 1 ATOM 1461 O O . LYS A 1 191 ? 52.647 -38.322 37.569 1.00 122.58 ? 191 LYS A O 1 ATOM 1462 C CB . LYS A 1 191 ? 50.114 -38.972 39.346 1.00 117.39 ? 191 LYS A CB 1 ATOM 1463 C CG . LYS A 1 191 ? 49.269 -38.214 40.363 1.00 116.79 ? 191 LYS A CG 1 ATOM 1464 C CD . LYS A 1 191 ? 49.377 -38.793 41.767 1.00 118.63 ? 191 LYS A CD 1 ATOM 1465 C CE . LYS A 1 191 ? 48.170 -39.634 42.138 1.00 115.91 ? 191 LYS A CE 1 ATOM 1466 N NZ . LYS A 1 191 ? 48.506 -40.627 43.195 1.00 118.32 ? 191 LYS A NZ 1 ATOM 1467 N N . LEU A 1 192 ? 52.797 -40.494 38.128 1.00 122.99 ? 192 LEU A N 1 ATOM 1468 C CA . LEU A 1 192 ? 53.574 -40.858 36.946 1.00 123.55 ? 192 LEU A CA 1 ATOM 1469 C C . LEU A 1 192 ? 52.923 -42.000 36.174 1.00 120.79 ? 192 LEU A C 1 ATOM 1470 O O . LEU A 1 192 ? 52.488 -42.984 36.769 1.00 120.90 ? 192 LEU A O 1 ATOM 1471 C CB . LEU A 1 192 ? 54.992 -41.263 37.355 1.00 128.69 ? 192 LEU A CB 1 ATOM 1472 C CG . LEU A 1 192 ? 55.860 -41.949 36.291 1.00 129.92 ? 192 LEU A CG 1 ATOM 1473 C CD1 . LEU A 1 192 ? 56.129 -41.032 35.103 1.00 128.88 ? 192 LEU A CD1 1 ATOM 1474 C CD2 . LEU A 1 192 ? 57.162 -42.424 36.911 1.00 135.82 ? 192 LEU A CD2 1 ATOM 1475 N N . VAL A 1 193 ? 52.874 -41.864 34.849 1.00 118.90 ? 193 VAL A N 1 ATOM 1476 C CA . VAL A 1 193 ? 52.446 -42.946 33.968 1.00 117.10 ? 193 VAL A CA 1 ATOM 1477 C C . VAL A 1 193 ? 53.486 -43.177 32.873 1.00 118.22 ? 193 VAL A C 1 ATOM 1478 O O . VAL A 1 193 ? 54.030 -42.227 32.308 1.00 118.60 ? 193 VAL A O 1 ATOM 1479 C CB . VAL A 1 193 ? 51.089 -42.647 33.314 1.00 113.56 ? 193 VAL A CB 1 ATOM 1480 C CG1 . VAL A 1 193 ? 50.689 -43.770 32.359 1.00 112.69 ? 193 VAL A CG1 1 ATOM 1481 C CG2 . VAL A 1 193 ? 50.016 -42.433 34.369 1.00 112.45 ? 193 VAL A CG2 1 ATOM 1482 N N . THR A 1 194 ? 53.750 -44.450 32.585 1.00 119.03 ? 194 THR A N 1 ATOM 1483 C CA . THR A 1 194 ? 54.738 -44.849 31.586 1.00 120.45 ? 194 THR A CA 1 ATOM 1484 C C . THR A 1 194 ? 54.188 -45.959 30.686 1.00 118.96 ? 194 THR A C 1 ATOM 1485 O O . THR A 1 194 ? 53.291 -46.710 31.080 1.00 118.28 ? 194 THR A O 1 ATOM 1486 C CB . THR A 1 194 ? 56.041 -45.335 32.251 1.00 125.35 ? 194 THR A CB 1 ATOM 1487 O OG1 . THR A 1 194 ? 55.875 -46.670 32.748 1.00 127.11 ? 194 THR A OG1 1 ATOM 1488 C CG2 . THR A 1 194 ? 56.437 -44.414 33.391 1.00 127.48 ? 194 THR A CG2 1 ATOM 1489 N N . VAL A 1 195 ? 54.736 -46.049 29.478 1.00 118.76 ? 195 VAL A N 1 ATOM 1490 C CA . VAL A 1 195 ? 54.294 -47.025 28.484 1.00 117.83 ? 195 VAL A CA 1 ATOM 1491 C C . VAL A 1 195 ? 55.489 -47.595 27.724 1.00 120.30 ? 195 VAL A C 1 ATOM 1492 O O . VAL A 1 195 ? 56.369 -46.853 27.283 1.00 120.80 ? 195 VAL A O 1 ATOM 1493 C CB . VAL A 1 195 ? 53.310 -46.389 27.487 1.00 114.30 ? 195 VAL A CB 1 ATOM 1494 C CG1 . VAL A 1 195 ? 52.905 -47.385 26.404 1.00 114.12 ? 195 VAL A CG1 1 ATOM 1495 C CG2 . VAL A 1 195 ? 52.089 -45.850 28.223 1.00 112.16 ? 195 VAL A CG2 1 ATOM 1496 N N . GLY A 1 196 ? 55.501 -48.916 27.569 1.00 122.16 ? 196 GLY A N 1 ATOM 1497 C CA . GLY A 1 196 ? 56.638 -49.620 27.000 1.00 125.36 ? 196 GLY A CA 1 ATOM 1498 C C . GLY A 1 196 ? 56.247 -50.806 26.144 1.00 125.91 ? 196 GLY A C 1 ATOM 1499 O O . GLY A 1 196 ? 55.684 -51.784 26.637 1.00 127.53 ? 196 GLY A O 1 ATOM 1500 N N . SER A 1 197 ? 56.545 -50.703 24.851 1.00 124.90 ? 197 SER A N 1 ATOM 1501 C CA . SER A 1 197 ? 56.457 -51.831 23.933 1.00 126.41 ? 197 SER A CA 1 ATOM 1502 C C . SER A 1 197 ? 57.766 -51.937 23.160 1.00 128.60 ? 197 SER A C 1 ATOM 1503 O O . SER A 1 197 ? 58.593 -51.021 23.200 1.00 128.41 ? 197 SER A O 1 ATOM 1504 C CB . SER A 1 197 ? 55.273 -51.664 22.977 1.00 123.05 ? 197 SER A CB 1 ATOM 1505 O OG . SER A 1 197 ? 55.566 -50.746 21.939 1.00 120.64 ? 197 SER A OG 1 ATOM 1506 N N . SER A 1 198 ? 57.940 -53.055 22.457 1.00 131.10 ? 198 SER A N 1 ATOM 1507 C CA . SER A 1 198 ? 59.190 -53.386 21.755 1.00 133.97 ? 198 SER A CA 1 ATOM 1508 C C . SER A 1 198 ? 59.892 -52.202 21.096 1.00 131.76 ? 198 SER A C 1 ATOM 1509 O O . SER A 1 198 ? 61.121 -52.135 21.101 1.00 134.79 ? 198 SER A O 1 ATOM 1510 C CB . SER A 1 198 ? 58.939 -54.460 20.692 1.00 135.41 ? 198 SER A CB 1 ATOM 1511 O OG . SER A 1 198 ? 58.541 -55.681 21.287 1.00 139.23 ? 198 SER A OG 1 ATOM 1512 N N . ASN A 1 199 ? 59.120 -51.283 20.526 1.00 127.24 ? 199 ASN A N 1 ATOM 1513 C CA . ASN A 1 199 ? 59.686 -50.120 19.841 1.00 125.61 ? 199 ASN A CA 1 ATOM 1514 C C . ASN A 1 199 ? 59.069 -48.799 20.304 1.00 122.50 ? 199 ASN A C 1 ATOM 1515 O O . ASN A 1 199 ? 58.967 -47.849 19.526 1.00 120.41 ? 199 ASN A O 1 ATOM 1516 C CB . ASN A 1 199 ? 59.545 -50.287 18.319 1.00 124.37 ? 199 ASN A CB 1 ATOM 1517 C CG . ASN A 1 199 ? 58.121 -50.610 17.888 1.00 121.93 ? 199 ASN A CG 1 ATOM 1518 O OD1 . ASN A 1 199 ? 57.154 -50.240 18.555 1.00 119.96 ? 199 ASN A OD1 1 ATOM 1519 N ND2 . ASN A 1 199 ? 57.989 -51.307 16.766 1.00 122.47 ? 199 ASN A ND2 1 ATOM 1520 N N . TYR A 1 200 ? 58.679 -48.736 21.577 1.00 122.60 ? 200 TYR A N 1 ATOM 1521 C CA . TYR A 1 200 ? 58.038 -47.544 22.120 1.00 120.09 ? 200 TYR A CA 1 ATOM 1522 C C . TYR A 1 200 ? 58.421 -47.307 23.580 1.00 122.20 ? 200 TYR A C 1 ATOM 1523 O O . TYR A 1 200 ? 58.414 -48.236 24.387 1.00 124.19 ? 200 TYR A O 1 ATOM 1524 C CB . TYR A 1 200 ? 56.522 -47.675 21.991 1.00 116.93 ? 200 TYR A CB 1 ATOM 1525 C CG . TYR A 1 200 ? 55.755 -46.455 22.438 1.00 114.39 ? 200 TYR A CG 1 ATOM 1526 C CD1 . TYR A 1 200 ? 55.359 -46.309 23.765 1.00 114.26 ? 200 TYR A CD1 1 ATOM 1527 C CD2 . TYR A 1 200 ? 55.423 -45.447 21.535 1.00 112.54 ? 200 TYR A CD2 1 ATOM 1528 C CE1 . TYR A 1 200 ? 54.659 -45.197 24.179 1.00 112.32 ? 200 TYR A CE1 1 ATOM 1529 C CE2 . TYR A 1 200 ? 54.718 -44.328 21.943 1.00 110.99 ? 200 TYR A CE2 1 ATOM 1530 C CZ . TYR A 1 200 ? 54.339 -44.209 23.269 1.00 110.82 ? 200 TYR A CZ 1 ATOM 1531 O OH . TYR A 1 200 ? 53.642 -43.097 23.672 1.00 109.50 ? 200 TYR A OH 1 ATOM 1532 N N . GLN A 1 201 ? 58.750 -46.054 23.896 1.00 122.40 ? 201 GLN A N 1 ATOM 1533 C CA . GLN A 1 201 ? 59.075 -45.616 25.259 1.00 124.60 ? 201 GLN A CA 1 ATOM 1534 C C . GLN A 1 201 ? 58.573 -44.187 25.469 1.00 122.76 ? 201 GLN A C 1 ATOM 1535 O O . GLN A 1 201 ? 59.049 -43.263 24.809 1.00 123.29 ? 201 GLN A O 1 ATOM 1536 C CB . GLN A 1 201 ? 60.592 -45.608 25.497 1.00 129.62 ? 201 GLN A CB 1 ATOM 1537 C CG . GLN A 1 201 ? 61.340 -46.890 25.153 1.00 132.66 ? 201 GLN A CG 1 ATOM 1538 C CD . GLN A 1 201 ? 62.765 -46.912 25.697 1.00 138.47 ? 201 GLN A CD 1 ATOM 1539 O OE1 . GLN A 1 201 ? 63.427 -47.944 25.661 1.00 141.98 ? 201 GLN A OE1 1 ATOM 1540 N NE2 . GLN A 1 201 ? 63.242 -45.773 26.197 1.00 140.13 ? 201 GLN A NE2 1 ATOM 1541 N N . GLN A 1 202 ? 57.626 -43.991 26.381 1.00 121.15 ? 202 GLN A N 1 ATOM 1542 C CA . GLN A 1 202 ? 57.173 -42.636 26.693 1.00 120.17 ? 202 GLN A CA 1 ATOM 1543 C C . GLN A 1 202 ? 56.552 -42.551 28.085 1.00 119.89 ? 202 GLN A C 1 ATOM 1544 O O . GLN A 1 202 ? 56.073 -43.550 28.626 1.00 119.28 ? 202 GLN A O 1 ATOM 1545 C CB . GLN A 1 202 ? 56.203 -42.131 25.615 1.00 116.91 ? 202 GLN A CB 1 ATOM 1546 C CG . GLN A 1 202 ? 56.489 -40.712 25.142 1.00 117.93 ? 202 GLN A CG 1 ATOM 1547 C CD . GLN A 1 202 ? 55.896 -40.399 23.777 1.00 116.08 ? 202 GLN A CD 1 ATOM 1548 O OE1 . GLN A 1 202 ? 56.170 -41.086 22.786 1.00 115.77 ? 202 GLN A OE1 1 ATOM 1549 N NE2 . GLN A 1 202 ? 55.091 -39.343 23.715 1.00 115.35 ? 202 GLN A NE2 1 ATOM 1550 N N . SER A 1 203 ? 56.583 -41.352 28.662 1.00 120.82 ? 203 SER A N 1 ATOM 1551 C CA . SER A 1 203 ? 56.073 -41.128 30.015 1.00 120.98 ? 203 SER A CA 1 ATOM 1552 C C . SER A 1 203 ? 55.347 -39.797 30.115 1.00 119.78 ? 203 SER A C 1 ATOM 1553 O O . SER A 1 203 ? 55.701 -38.846 29.416 1.00 120.82 ? 203 SER A O 1 ATOM 1554 C CB . SER A 1 203 ? 57.220 -41.167 31.017 1.00 125.60 ? 203 SER A CB 1 ATOM 1555 O OG . SER A 1 203 ? 57.920 -42.391 30.915 1.00 127.57 ? 203 SER A OG 1 ATOM 1556 N N . PHE A 1 204 ? 54.331 -39.736 30.980 1.00 118.05 ? 204 PHE A N 1 ATOM 1557 C CA . PHE A 1 204 ? 53.499 -38.535 31.113 1.00 117.11 ? 204 PHE A CA 1 ATOM 1558 C C . PHE A 1 204 ? 53.110 -38.253 32.560 1.00 117.60 ? 204 PHE A C 1 ATOM 1559 O O . PHE A 1 204 ? 52.364 -39.016 33.178 1.00 115.60 ? 204 PHE A O 1 ATOM 1560 C CB . PHE A 1 204 ? 52.243 -38.651 30.245 1.00 113.67 ? 204 PHE A CB 1 ATOM 1561 C CG . PHE A 1 204 ? 52.506 -39.243 28.895 1.00 113.15 ? 204 PHE A CG 1 ATOM 1562 C CD1 . PHE A 1 204 ? 53.198 -38.521 27.931 1.00 114.81 ? 204 PHE A CD1 1 ATOM 1563 C CD2 . PHE A 1 204 ? 52.113 -40.532 28.605 1.00 111.62 ? 204 PHE A CD2 1 ATOM 1564 C CE1 . PHE A 1 204 ? 53.473 -39.074 26.696 1.00 114.35 ? 204 PHE A CE1 1 ATOM 1565 C CE2 . PHE A 1 204 ? 52.375 -41.086 27.371 1.00 111.38 ? 204 PHE A CE2 1 ATOM 1566 C CZ . PHE A 1 204 ? 53.053 -40.361 26.413 1.00 112.50 ? 204 PHE A CZ 1 ATOM 1567 N N . VAL A 1 205 ? 53.645 -37.151 33.084 1.00 120.73 ? 205 VAL A N 1 ATOM 1568 C CA . VAL A 1 205 ? 53.251 -36.596 34.372 1.00 121.64 ? 205 VAL A CA 1 ATOM 1569 C C . VAL A 1 205 ? 52.152 -35.574 34.080 1.00 119.96 ? 205 VAL A C 1 ATOM 1570 O O . VAL A 1 205 ? 52.293 -34.781 33.148 1.00 121.06 ? 205 VAL A O 1 ATOM 1571 C CB . VAL A 1 205 ? 54.437 -35.882 35.067 1.00 126.98 ? 205 VAL A CB 1 ATOM 1572 C CG1 . VAL A 1 205 ? 54.068 -35.450 36.486 1.00 128.23 ? 205 VAL A CG1 1 ATOM 1573 C CG2 . VAL A 1 205 ? 55.672 -36.776 35.090 1.00 129.76 ? 205 VAL A CG2 1 ATOM 1574 N N . PRO A 1 206 ? 51.055 -35.582 34.865 1.00 117.88 ? 206 PRO A N 1 ATOM 1575 C CA . PRO A 1 206 ? 49.960 -34.641 34.597 1.00 116.78 ? 206 PRO A CA 1 ATOM 1576 C C . PRO A 1 206 ? 50.331 -33.169 34.814 1.00 120.62 ? 206 PRO A C 1 ATOM 1577 O O . PRO A 1 206 ? 51.434 -32.860 35.268 1.00 124.31 ? 206 PRO A O 1 ATOM 1578 C CB . PRO A 1 206 ? 48.870 -35.067 35.587 1.00 114.40 ? 206 PRO A CB 1 ATOM 1579 C CG . PRO A 1 206 ? 49.579 -35.802 36.661 1.00 115.57 ? 206 PRO A CG 1 ATOM 1580 C CD . PRO A 1 206 ? 50.764 -36.454 36.015 1.00 116.91 ? 206 PRO A CD 1 ATOM 1581 N N . SER A 1 207 ? 49.394 -32.280 34.495 1.00 120.37 ? 207 SER A N 1 ATOM 1582 C CA . SER A 1 207 ? 49.596 -30.844 34.640 1.00 124.53 ? 207 SER A CA 1 ATOM 1583 C C . SER A 1 207 ? 48.280 -30.105 34.913 1.00 123.92 ? 207 SER A C 1 ATOM 1584 O O . SER A 1 207 ? 47.668 -29.576 33.985 1.00 124.24 ? 207 SER A O 1 ATOM 1585 C CB . SER A 1 207 ? 50.227 -30.299 33.370 1.00 127.07 ? 207 SER A CB 1 ATOM 1586 O OG . SER A 1 207 ? 49.388 -30.541 32.257 1.00 124.32 ? 207 SER A OG 1 ATOM 1587 N N . PRO A 1 208 ? 47.842 -30.066 36.183 1.00 123.37 ? 208 PRO A N 1 ATOM 1588 C CA . PRO A 1 208 ? 46.619 -29.333 36.542 1.00 123.34 ? 208 PRO A CA 1 ATOM 1589 C C . PRO A 1 208 ? 46.753 -27.809 36.439 1.00 128.55 ? 208 PRO A C 1 ATOM 1590 O O . PRO A 1 208 ? 47.862 -27.287 36.344 1.00 132.55 ? 208 PRO A O 1 ATOM 1591 C CB . PRO A 1 208 ? 46.359 -29.748 37.998 1.00 122.03 ? 208 PRO A CB 1 ATOM 1592 C CG . PRO A 1 208 ? 47.652 -30.272 38.506 1.00 123.40 ? 208 PRO A CG 1 ATOM 1593 C CD . PRO A 1 208 ? 48.400 -30.816 37.321 1.00 122.97 ? 208 PRO A CD 1 ATOM 1594 N N . GLY A 1 209 ? 45.616 -27.118 36.486 1.00 129.05 ? 209 GLY A N 1 ATOM 1595 C CA . GLY A 1 209 ? 45.547 -25.671 36.250 1.00 134.54 ? 209 GLY A CA 1 ATOM 1596 C C . GLY A 1 209 ? 44.254 -25.321 35.535 1.00 134.22 ? 209 GLY A C 1 ATOM 1597 O O . GLY A 1 209 ? 43.625 -26.189 34.933 1.00 130.15 ? 209 GLY A O 1 ATOM 1598 N N . ALA A 1 210 ? 43.842 -24.060 35.599 1.00 139.16 ? 210 ALA A N 1 ATOM 1599 C CA . ALA A 1 210 ? 42.555 -23.658 35.024 1.00 139.92 ? 210 ALA A CA 1 ATOM 1600 C C . ALA A 1 210 ? 42.654 -23.464 33.511 1.00 141.90 ? 210 ALA A C 1 ATOM 1601 O O . ALA A 1 210 ? 43.683 -23.021 33.005 1.00 145.23 ? 210 ALA A O 1 ATOM 1602 C CB . ALA A 1 210 ? 42.035 -22.394 35.694 1.00 145.14 ? 210 ALA A CB 1 ATOM 1603 N N . ARG A 1 211 ? 41.590 -23.833 32.798 1.00 140.12 ? 211 ARG A N 1 ATOM 1604 C CA . ARG A 1 211 ? 41.493 -23.643 31.348 1.00 142.36 ? 211 ARG A CA 1 ATOM 1605 C C . ARG A 1 211 ? 40.133 -23.041 31.002 1.00 145.40 ? 211 ARG A C 1 ATOM 1606 O O . ARG A 1 211 ? 39.233 -23.038 31.841 1.00 144.52 ? 211 ARG A O 1 ATOM 1607 C CB . ARG A 1 211 ? 41.666 -24.976 30.615 1.00 137.16 ? 211 ARG A CB 1 ATOM 1608 C CG . ARG A 1 211 ? 43.099 -25.464 30.505 1.00 135.76 ? 211 ARG A CG 1 ATOM 1609 C CD . ARG A 1 211 ? 43.614 -26.058 31.807 1.00 132.73 ? 211 ARG A CD 1 ATOM 1610 N NE . ARG A 1 211 ? 44.661 -27.047 31.569 1.00 129.88 ? 211 ARG A NE 1 ATOM 1611 C CZ . ARG A 1 211 ? 45.068 -27.979 32.429 1.00 126.51 ? 211 ARG A CZ 1 ATOM 1612 N NH1 . ARG A 1 211 ? 44.508 -28.110 33.626 1.00 125.06 ? 211 ARG A NH1 1 ATOM 1613 N NH2 . ARG A 1 211 ? 46.047 -28.804 32.070 1.00 124.83 ? 211 ARG A NH2 1 ATOM 1614 N N . PRO A 1 212 ? 39.973 -22.526 29.768 1.00 149.47 ? 212 PRO A N 1 ATOM 1615 C CA . PRO A 1 212 ? 38.684 -21.936 29.392 1.00 153.44 ? 212 PRO A CA 1 ATOM 1616 C C . PRO A 1 212 ? 37.541 -22.944 29.447 1.00 148.93 ? 212 PRO A C 1 ATOM 1617 O O . PRO A 1 212 ? 37.740 -24.118 29.133 1.00 143.63 ? 212 PRO A O 1 ATOM 1618 C CB . PRO A 1 212 ? 38.912 -21.467 27.947 1.00 158.18 ? 212 PRO A CB 1 ATOM 1619 C CG . PRO A 1 212 ? 40.388 -21.357 27.792 1.00 158.38 ? 212 PRO A CG 1 ATOM 1620 C CD . PRO A 1 212 ? 40.964 -22.417 28.680 1.00 151.34 ? 212 PRO A CD 1 ATOM 1621 N N . GLN A 1 213 ? 36.358 -22.487 29.844 1.00 151.53 ? 213 GLN A N 1 ATOM 1622 C CA . GLN A 1 213 ? 35.203 -23.371 29.957 1.00 148.37 ? 213 GLN A CA 1 ATOM 1623 C C . GLN A 1 213 ? 34.708 -23.809 28.580 1.00 149.64 ? 213 GLN A C 1 ATOM 1624 O O . GLN A 1 213 ? 33.936 -23.107 27.929 1.00 155.58 ? 213 GLN A O 1 ATOM 1625 C CB . GLN A 1 213 ? 34.075 -22.717 30.761 1.00 151.50 ? 213 GLN A CB 1 ATOM 1626 C CG . GLN A 1 213 ? 34.329 -22.729 32.263 1.00 148.39 ? 213 GLN A CG 1 ATOM 1627 C CD . GLN A 1 213 ? 33.158 -22.215 33.080 1.00 150.94 ? 213 GLN A CD 1 ATOM 1628 O OE1 . GLN A 1 213 ? 32.087 -21.932 32.545 1.00 154.98 ? 213 GLN A OE1 1 ATOM 1629 N NE2 . GLN A 1 213 ? 33.359 -22.096 34.388 1.00 148.97 ? 213 GLN A NE2 1 ATOM 1630 N N . VAL A 1 214 ? 35.190 -24.967 28.140 1.00 144.61 ? 214 VAL A N 1 ATOM 1631 C CA . VAL A 1 214 ? 34.688 -25.620 26.938 1.00 145.09 ? 214 VAL A CA 1 ATOM 1632 C C . VAL A 1 214 ? 33.638 -26.633 27.374 1.00 142.22 ? 214 VAL A C 1 ATOM 1633 O O . VAL A 1 214 ? 33.840 -27.354 28.354 1.00 137.18 ? 214 VAL A O 1 ATOM 1634 C CB . VAL A 1 214 ? 35.814 -26.335 26.173 1.00 141.79 ? 214 VAL A CB 1 ATOM 1635 C CG1 . VAL A 1 214 ? 35.258 -27.079 24.965 1.00 142.38 ? 214 VAL A CG1 1 ATOM 1636 C CG2 . VAL A 1 214 ? 36.876 -25.331 25.745 1.00 145.18 ? 214 VAL A CG2 1 ATOM 1637 N N . ASN A 1 215 ? 32.515 -26.674 26.659 1.00 146.10 ? 215 ASN A N 1 ATOM 1638 C CA . ASN A 1 215 ? 31.341 -27.446 27.084 1.00 145.23 ? 215 ASN A CA 1 ATOM 1639 C C . ASN A 1 215 ? 30.918 -27.123 28.522 1.00 144.17 ? 215 ASN A C 1 ATOM 1640 O O . ASN A 1 215 ? 30.345 -27.969 29.208 1.00 141.22 ? 215 ASN A O 1 ATOM 1641 C CB . ASN A 1 215 ? 31.593 -28.955 26.940 1.00 139.91 ? 215 ASN A CB 1 ATOM 1642 C CG . ASN A 1 215 ? 31.785 -29.384 25.502 1.00 141.39 ? 215 ASN A CG 1 ATOM 1643 O OD1 . ASN A 1 215 ? 31.152 -28.848 24.594 1.00 147.11 ? 215 ASN A OD1 1 ATOM 1644 N ND2 . ASN A 1 215 ? 32.650 -30.370 25.287 1.00 136.68 ? 215 ASN A ND2 1 ATOM 1645 N N . GLY A 1 216 ? 31.198 -25.898 28.966 1.00 147.07 ? 216 GLY A N 1 ATOM 1646 C CA . GLY A 1 216 ? 30.958 -25.492 30.354 1.00 146.24 ? 216 GLY A CA 1 ATOM 1647 C C . GLY A 1 216 ? 31.962 -26.029 31.366 1.00 140.05 ? 216 GLY A C 1 ATOM 1648 O O . GLY A 1 216 ? 31.803 -25.815 32.567 1.00 138.85 ? 216 GLY A O 1 ATOM 1649 N N . LEU A 1 217 ? 33.004 -26.705 30.882 1.00 136.62 ? 217 LEU A N 1 ATOM 1650 C CA . LEU A 1 217 ? 33.980 -27.372 31.740 1.00 131.25 ? 217 LEU A CA 1 ATOM 1651 C C . LEU A 1 217 ? 35.398 -26.891 31.448 1.00 131.63 ? 217 LEU A C 1 ATOM 1652 O O . LEU A 1 217 ? 35.761 -26.649 30.296 1.00 133.88 ? 217 LEU A O 1 ATOM 1653 C CB . LEU A 1 217 ? 33.901 -28.882 31.541 1.00 126.80 ? 217 LEU A CB 1 ATOM 1654 C CG . LEU A 1 217 ? 32.518 -29.494 31.761 1.00 127.08 ? 217 LEU A CG 1 ATOM 1655 C CD1 . LEU A 1 217 ? 32.539 -30.966 31.388 1.00 123.87 ? 217 LEU A CD1 1 ATOM 1656 C CD2 . LEU A 1 217 ? 32.057 -29.306 33.201 1.00 126.08 ? 217 LEU A CD2 1 ATOM 1657 N N . SER A 1 218 ? 36.192 -26.777 32.508 1.00 58.01 ? 218 SER A N 1 ATOM 1658 C CA . SER A 1 218 ? 37.538 -26.210 32.448 1.00 58.43 ? 218 SER A CA 1 ATOM 1659 C C . SER A 1 218 ? 38.617 -27.261 32.645 1.00 58.13 ? 218 SER A C 1 ATOM 1660 O O . SER A 1 218 ? 39.797 -26.936 32.647 1.00 58.47 ? 218 SER A O 1 ATOM 1661 C CB . SER A 1 218 ? 37.692 -25.118 33.506 1.00 61.30 ? 218 SER A CB 1 ATOM 1662 O OG . SER A 1 218 ? 37.070 -23.918 33.088 1.00 61.81 ? 218 SER A OG 1 ATOM 1663 N N . GLY A 1 219 ? 38.210 -28.511 32.834 1.00 57.73 ? 219 GLY A N 1 ATOM 1664 C CA . GLY A 1 219 ? 39.141 -29.634 32.824 1.00 57.58 ? 219 GLY A CA 1 ATOM 1665 C C . GLY A 1 219 ? 39.433 -30.076 31.399 1.00 55.02 ? 219 GLY A C 1 ATOM 1666 O O . GLY A 1 219 ? 38.710 -29.710 30.473 1.00 53.46 ? 219 GLY A O 1 ATOM 1667 N N . ARG A 1 220 ? 40.502 -30.848 31.217 1.00 54.99 ? 220 ARG A N 1 ATOM 1668 C CA . ARG A 1 220 ? 40.843 -31.417 29.915 1.00 52.85 ? 220 ARG A CA 1 ATOM 1669 C C . ARG A 1 220 ? 41.274 -32.869 30.068 1.00 53.01 ? 220 ARG A C 1 ATOM 1670 O O . ARG A 1 220 ? 41.847 -33.243 31.094 1.00 54.96 ? 220 ARG A O 1 ATOM 1671 C CB . ARG A 1 220 ? 41.993 -30.642 29.257 1.00 52.91 ? 220 ARG A CB 1 ATOM 1672 C CG . ARG A 1 220 ? 41.718 -29.171 28.993 1.00 53.05 ? 220 ARG A CG 1 ATOM 1673 C CD . ARG A 1 220 ? 40.808 -28.977 27.798 1.00 50.92 ? 220 ARG A CD 1 ATOM 1674 N NE . ARG A 1 220 ? 40.603 -27.562 27.530 1.00 51.40 ? 220 ARG A NE 1 ATOM 1675 C CZ . ARG A 1 220 ? 39.706 -26.785 28.136 1.00 52.77 ? 220 ARG A CZ 1 ATOM 1676 N NH1 . ARG A 1 220 ? 38.883 -27.268 29.070 1.00 53.73 ? 220 ARG A NH1 1 ATOM 1677 N NH2 . ARG A 1 220 ? 39.631 -25.499 27.806 1.00 53.29 ? 220 ARG A NH2 1 ATOM 1678 N N . ILE A 1 221 ? 41.015 -33.675 29.038 1.00 50.99 ? 221 ILE A N 1 ATOM 1679 C CA . ILE A 1 221 ? 41.548 -35.032 28.966 1.00 51.11 ? 221 ILE A CA 1 ATOM 1680 C C . ILE A 1 221 ? 42.511 -35.137 27.773 1.00 50.03 ? 221 ILE A C 1 ATOM 1681 O O . ILE A 1 221 ? 42.121 -34.900 26.626 1.00 48.04 ? 221 ILE A O 1 ATOM 1682 C CB . ILE A 1 221 ? 40.410 -36.081 28.886 1.00 50.19 ? 221 ILE A CB 1 ATOM 1683 C CG1 . ILE A 1 221 ? 39.684 -36.152 30.233 1.00 52.15 ? 221 ILE A CG1 1 ATOM 1684 C CG2 . ILE A 1 221 ? 40.950 -37.461 28.542 1.00 49.93 ? 221 ILE A CG2 1 ATOM 1685 C CD1 . ILE A 1 221 ? 38.412 -36.973 30.227 1.00 51.54 ? 221 ILE A CD1 1 ATOM 1686 N N . ASP A 1 222 ? 43.774 -35.449 28.058 1.00 51.57 ? 222 ASP A N 1 ATOM 1687 C CA . ASP A 1 222 ? 44.739 -35.834 27.024 1.00 51.00 ? 222 ASP A CA 1 ATOM 1688 C C . ASP A 1 222 ? 44.341 -37.208 26.480 1.00 49.80 ? 222 ASP A C 1 ATOM 1689 O O . ASP A 1 222 ? 43.834 -38.037 27.231 1.00 50.51 ? 222 ASP A O 1 ATOM 1690 C CB . ASP A 1 222 ? 46.155 -35.941 27.609 1.00 53.61 ? 222 ASP A CB 1 ATOM 1691 C CG . ASP A 1 222 ? 46.916 -34.614 27.604 1.00 54.70 ? 222 ASP A CG 1 ATOM 1692 O OD1 . ASP A 1 222 ? 46.389 -33.637 28.170 1.00 55.21 ? 222 ASP A OD1 1 ATOM 1693 O OD2 . ASP A 1 222 ? 48.052 -34.548 27.066 1.00 55.30 ? 222 ASP A OD2 1 ATOM 1694 N N . PHE A 1 223 ? 44.556 -37.441 25.187 1.00 48.13 ? 223 PHE A N 1 ATOM 1695 C CA . PHE A 1 223 ? 44.425 -38.780 24.598 1.00 47.30 ? 223 PHE A CA 1 ATOM 1696 C C . PHE A 1 223 ? 45.721 -39.162 23.880 1.00 47.97 ? 223 PHE A C 1 ATOM 1697 O O . PHE A 1 223 ? 46.304 -38.347 23.172 1.00 47.80 ? 223 PHE A O 1 ATOM 1698 C CB . PHE A 1 223 ? 43.231 -38.855 23.640 1.00 44.69 ? 223 PHE A CB 1 ATOM 1699 C CG . PHE A 1 223 ? 41.890 -38.912 24.330 1.00 44.35 ? 223 PHE A CG 1 ATOM 1700 C CD1 . PHE A 1 223 ? 41.525 -40.017 25.070 1.00 45.13 ? 223 PHE A CD1 1 ATOM 1701 C CD2 . PHE A 1 223 ? 40.989 -37.857 24.231 1.00 43.61 ? 223 PHE A CD2 1 ATOM 1702 C CE1 . PHE A 1 223 ? 40.294 -40.078 25.697 1.00 45.17 ? 223 PHE A CE1 1 ATOM 1703 C CE2 . PHE A 1 223 ? 39.752 -37.912 24.861 1.00 43.60 ? 223 PHE A CE2 1 ATOM 1704 C CZ . PHE A 1 223 ? 39.406 -39.025 25.596 1.00 44.40 ? 223 PHE A CZ 1 ATOM 1705 N N . HIS A 1 224 ? 46.145 -40.410 24.083 1.00 49.31 ? 224 HIS A N 1 ATOM 1706 C CA . HIS A 1 224 ? 47.430 -40.955 23.624 1.00 50.65 ? 224 HIS A CA 1 ATOM 1707 C C . HIS A 1 224 ? 47.230 -42.298 22.916 1.00 49.93 ? 224 HIS A C 1 ATOM 1708 O O . HIS A 1 224 ? 46.293 -43.023 23.244 1.00 49.17 ? 224 HIS A O 1 ATOM 1709 C CB . HIS A 1 224 ? 48.306 -41.247 24.832 1.00 53.88 ? 224 HIS A CB 1 ATOM 1710 C CG . HIS A 1 224 ? 49.298 -40.181 25.140 1.00 55.67 ? 224 HIS A CG 1 ATOM 1711 N ND1 . HIS A 1 224 ? 49.246 -39.425 26.290 1.00 57.08 ? 224 HIS A ND1 1 ATOM 1712 C CD2 . HIS A 1 224 ? 50.389 -39.764 24.458 1.00 56.48 ? 224 HIS A CD2 1 ATOM 1713 C CE1 . HIS A 1 224 ? 50.261 -38.579 26.298 1.00 58.65 ? 224 HIS A CE1 1 ATOM 1714 N NE2 . HIS A 1 224 ? 50.965 -38.760 25.194 1.00 58.25 ? 224 HIS A NE2 1 ATOM 1715 N N . TRP A 1 225 ? 48.141 -42.659 22.007 1.00 50.21 ? 225 TRP A N 1 ATOM 1716 C CA . TRP A 1 225 ? 48.021 -43.925 21.275 1.00 49.77 ? 225 TRP A CA 1 ATOM 1717 C C . TRP A 1 225 ? 49.332 -44.511 20.737 1.00 51.80 ? 225 TRP A C 1 ATOM 1718 O O . TRP A 1 225 ? 50.279 -43.786 20.445 1.00 52.64 ? 225 TRP A O 1 ATOM 1719 C CB . TRP A 1 225 ? 47.048 -43.746 20.106 1.00 46.61 ? 225 TRP A CB 1 ATOM 1720 C CG . TRP A 1 225 ? 47.543 -42.783 19.092 1.00 45.59 ? 225 TRP A CG 1 ATOM 1721 C CD1 . TRP A 1 225 ? 47.436 -41.430 19.130 1.00 44.91 ? 225 TRP A CD1 1 ATOM 1722 C CD2 . TRP A 1 225 ? 48.255 -43.097 17.894 1.00 45.45 ? 225 TRP A CD2 1 ATOM 1723 N NE1 . TRP A 1 225 ? 48.028 -40.877 18.022 1.00 44.38 ? 225 TRP A NE1 1 ATOM 1724 C CE2 . TRP A 1 225 ? 48.542 -41.881 17.248 1.00 44.73 ? 225 TRP A CE2 1 ATOM 1725 C CE3 . TRP A 1 225 ? 48.667 -44.293 17.298 1.00 46.09 ? 225 TRP A CE3 1 ATOM 1726 C CZ2 . TRP A 1 225 ? 49.223 -41.821 16.033 1.00 44.88 ? 225 TRP A CZ2 1 ATOM 1727 C CZ3 . TRP A 1 225 ? 49.347 -44.234 16.091 1.00 46.16 ? 225 TRP A CZ3 1 ATOM 1728 C CH2 . TRP A 1 225 ? 49.622 -43.003 15.474 1.00 45.56 ? 225 TRP A CH2 1 ATOM 1729 N N . LEU A 1 226 ? 49.354 -45.839 20.603 1.00 53.06 ? 226 LEU A N 1 ATOM 1730 C CA . LEU A 1 226 ? 50.401 -46.560 19.864 1.00 54.77 ? 226 LEU A CA 1 ATOM 1731 C C . LEU A 1 226 ? 49.839 -47.797 19.157 1.00 54.09 ? 226 LEU A C 1 ATOM 1732 O O . LEU A 1 226 ? 48.769 -48.293 19.517 1.00 52.71 ? 226 LEU A O 1 ATOM 1733 C CB . LEU A 1 226 ? 51.560 -46.971 20.776 1.00 58.33 ? 226 LEU A CB 1 ATOM 1734 C CG . LEU A 1 226 ? 51.503 -48.182 21.732 1.00 60.60 ? 226 LEU A CG 1 ATOM 1735 C CD1 . LEU A 1 226 ? 50.407 -48.033 22.769 1.00 59.92 ? 226 LEU A CD1 1 ATOM 1736 C CD2 . LEU A 1 226 ? 51.380 -49.529 21.032 1.00 60.76 ? 226 LEU A CD2 1 ATOM 1737 N N . MET A 1 227 ? 50.585 -48.293 18.168 1.00 55.06 ? 227 MET A N 1 ATOM 1738 C CA . MET A 1 227 ? 50.237 -49.526 17.459 1.00 55.07 ? 227 MET A CA 1 ATOM 1739 C C . MET A 1 227 ? 51.000 -50.690 18.066 1.00 58.34 ? 227 MET A C 1 ATOM 1740 O O . MET A 1 227 ? 52.213 -50.793 17.898 1.00 60.48 ? 227 MET A O 1 ATOM 1741 C CB . MET A 1 227 ? 50.578 -49.425 15.968 1.00 54.34 ? 227 MET A CB 1 ATOM 1742 C CG . MET A 1 227 ? 49.765 -48.398 15.204 1.00 51.57 ? 227 MET A CG 1 ATOM 1743 S SD . MET A 1 227 ? 48.040 -48.877 14.969 1.00 49.39 ? 227 MET A SD 1 ATOM 1744 C CE . MET A 1 227 ? 47.365 -47.280 14.546 1.00 46.92 ? 227 MET A CE 1 ATOM 1745 N N . LEU A 1 228 ? 50.284 -51.558 18.775 1.00 59.03 ? 228 LEU A N 1 ATOM 1746 C CA . LEU A 1 228 ? 50.884 -52.731 19.392 1.00 62.59 ? 228 LEU A CA 1 ATOM 1747 C C . LEU A 1 228 ? 50.935 -53.885 18.393 1.00 63.37 ? 228 LEU A C 1 ATOM 1748 O O . LEU A 1 228 ? 49.896 -54.345 17.921 1.00 61.42 ? 228 LEU A O 1 ATOM 1749 C CB . LEU A 1 228 ? 50.088 -53.146 20.630 1.00 63.03 ? 228 LEU A CB 1 ATOM 1750 C CG . LEU A 1 228 ? 50.716 -54.249 21.481 1.00 66.71 ? 228 LEU A CG 1 ATOM 1751 C CD1 . LEU A 1 228 ? 52.101 -53.825 21.967 1.00 69.64 ? 228 LEU A CD1 1 ATOM 1752 C CD2 . LEU A 1 228 ? 49.800 -54.599 22.645 1.00 67.07 ? 228 LEU A CD2 1 ATOM 1753 N N . ASN A 1 229 ? 52.143 -54.351 18.089 1.00 66.62 ? 229 ASN A N 1 ATOM 1754 C CA . ASN A 1 229 ? 52.349 -55.404 17.099 1.00 67.87 ? 229 ASN A CA 1 ATOM 1755 C C . ASN A 1 229 ? 51.834 -56.773 17.552 1.00 69.95 ? 229 ASN A C 1 ATOM 1756 O O . ASN A 1 229 ? 51.680 -57.010 18.751 1.00 70.95 ? 229 ASN A O 1 ATOM 1757 C CB . ASN A 1 229 ? 53.839 -55.527 16.749 1.00 70.87 ? 229 ASN A CB 1 ATOM 1758 C CG . ASN A 1 229 ? 54.310 -54.455 15.783 1.00 69.48 ? 229 ASN A CG 1 ATOM 1759 O OD1 . ASN A 1 229 ? 53.559 -53.999 14.924 1.00 66.59 ? 229 ASN A OD1 1 ATOM 1760 N ND2 . ASN A 1 229 ? 55.569 -54.061 15.909 1.00 72.16 ? 229 ASN A ND2 1 ATOM 1761 N N . PRO A 1 230 ? 51.561 -57.675 16.584 1.00 70.94 ? 230 PRO A N 1 ATOM 1762 C CA . PRO A 1 230 ? 51.211 -59.068 16.872 1.00 73.70 ? 230 PRO A CA 1 ATOM 1763 C C . PRO A 1 230 ? 52.259 -59.761 17.748 1.00 79.61 ? 230 PRO A C 1 ATOM 1764 O O . PRO A 1 230 ? 53.453 -59.670 17.469 1.00 81.40 ? 230 PRO A O 1 ATOM 1765 C CB . PRO A 1 230 ? 51.164 -59.709 15.479 1.00 72.68 ? 230 PRO A CB 1 ATOM 1766 C CG . PRO A 1 230 ? 50.782 -58.593 14.575 1.00 68.97 ? 230 PRO A CG 1 ATOM 1767 C CD . PRO A 1 230 ? 51.455 -57.376 15.142 1.00 69.00 ? 230 PRO A CD 1 ATOM 1768 N N . ASN A 1 231 ? 51.795 -60.432 18.800 1.00 83.43 ? 231 ASN A N 1 ATOM 1769 C CA . ASN A 1 231 ? 52.654 -61.067 19.809 1.00 90.19 ? 231 ASN A CA 1 ATOM 1770 C C . ASN A 1 231 ? 53.473 -60.107 20.671 1.00 89.81 ? 231 ASN A C 1 ATOM 1771 O O . ASN A 1 231 ? 54.279 -60.555 21.483 1.00 93.36 ? 231 ASN A O 1 ATOM 1772 C CB . ASN A 1 231 ? 53.589 -62.122 19.191 1.00 97.33 ? 231 ASN A CB 1 ATOM 1773 C CG . ASN A 1 231 ? 52.852 -63.356 18.713 1.00 102.80 ? 231 ASN A CG 1 ATOM 1774 O OD1 . ASN A 1 231 ? 51.757 -63.667 19.187 1.00 101.39 ? 231 ASN A OD1 1 ATOM 1775 N ND2 . ASN A 1 231 ? 53.458 -64.073 17.772 1.00 112.00 ? 231 ASN A ND2 1 ATOM 1776 N N . ASP A 1 232 ? 53.264 -58.801 20.517 1.00 85.28 ? 232 ASP A N 1 ATOM 1777 C CA . ASP A 1 232 ? 53.921 -57.827 21.381 1.00 85.41 ? 232 ASP A CA 1 ATOM 1778 C C . ASP A 1 232 ? 53.032 -57.558 22.595 1.00 83.93 ? 232 ASP A C 1 ATOM 1779 O O . ASP A 1 232 ? 51.816 -57.769 22.549 1.00 81.31 ? 232 ASP A O 1 ATOM 1780 C CB . ASP A 1 232 ? 54.226 -56.528 20.625 1.00 82.68 ? 232 ASP A CB 1 ATOM 1781 C CG . ASP A 1 232 ? 55.303 -55.680 21.308 1.00 84.79 ? 232 ASP A CG 1 ATOM 1782 O OD1 . ASP A 1 232 ? 55.736 -56.018 22.429 1.00 87.54 ? 232 ASP A OD1 1 ATOM 1783 O OD2 . ASP A 1 232 ? 55.723 -54.664 20.718 1.00 83.43 ? 232 ASP A OD2 1 ATOM 1784 N N . THR A 1 233 ? 53.656 -57.114 23.682 1.00 85.32 ? 233 THR A N 1 ATOM 1785 C CA . THR A 1 233 ? 52.956 -56.805 24.920 1.00 84.59 ? 233 THR A CA 1 ATOM 1786 C C . THR A 1 233 ? 53.201 -55.336 25.260 1.00 83.05 ? 233 THR A C 1 ATOM 1787 O O . THR A 1 233 ? 54.258 -54.792 24.938 1.00 84.11 ? 233 THR A O 1 ATOM 1788 C CB . THR A 1 233 ? 53.439 -57.713 26.072 1.00 88.98 ? 233 THR A CB 1 ATOM 1789 O OG1 . THR A 1 233 ? 53.442 -59.083 25.643 1.00 90.46 ? 233 THR A OG1 1 ATOM 1790 C CG2 . THR A 1 233 ? 52.537 -57.577 27.285 1.00 88.88 ? 233 THR A CG2 1 ATOM 1791 N N . VAL A 1 234 ? 52.211 -54.700 25.889 1.00 80.49 ? 234 VAL A N 1 ATOM 1792 C CA . VAL A 1 234 ? 52.297 -53.291 26.283 1.00 78.78 ? 234 VAL A CA 1 ATOM 1793 C C . VAL A 1 234 ? 51.920 -53.139 27.754 1.00 80.06 ? 234 VAL A C 1 ATOM 1794 O O . VAL A 1 234 ? 50.920 -53.711 28.204 1.00 79.29 ? 234 VAL A O 1 ATOM 1795 C CB . VAL A 1 234 ? 51.397 -52.382 25.409 1.00 74.39 ? 234 VAL A CB 1 ATOM 1796 C CG1 . VAL A 1 234 ? 49.914 -52.686 25.611 1.00 72.26 ? 234 VAL A CG1 1 ATOM 1797 C CG2 . VAL A 1 234 ? 51.682 -50.913 25.690 1.00 73.63 ? 234 VAL A CG2 1 ATOM 1798 N N . THR A 1 235 ? 52.724 -52.362 28.486 1.00 81.49 ? 235 THR A N 1 ATOM 1799 C CA . THR A 1 235 ? 52.558 -52.202 29.926 1.00 83.38 ? 235 THR A CA 1 ATOM 1800 C C . THR A 1 235 ? 52.236 -50.764 30.313 1.00 81.35 ? 235 THR A C 1 ATOM 1801 O O . THR A 1 235 ? 52.806 -49.821 29.762 1.00 79.89 ? 235 THR A O 1 ATOM 1802 C CB . THR A 1 235 ? 53.833 -52.623 30.675 1.00 88.30 ? 235 THR A CB 1 ATOM 1803 O OG1 . THR A 1 235 ? 54.159 -53.977 30.342 1.00 90.29 ? 235 THR A OG1 1 ATOM 1804 C CG2 . THR A 1 235 ? 53.648 -52.493 32.194 1.00 90.91 ? 235 THR A CG2 1 ATOM 1805 N N . PHE A 1 236 ? 51.335 -50.618 31.282 1.00 81.15 ? 236 PHE A N 1 ATOM 1806 C CA . PHE A 1 236 ? 50.952 -49.317 31.815 1.00 80.08 ? 236 PHE A CA 1 ATOM 1807 C C . PHE A 1 236 ? 51.223 -49.229 33.323 1.00 83.59 ? 236 PHE A C 1 ATOM 1808 O O . PHE A 1 236 ? 50.489 -49.805 34.129 1.00 84.94 ? 236 PHE A O 1 ATOM 1809 C CB . PHE A 1 236 ? 49.471 -49.068 31.551 1.00 76.73 ? 236 PHE A CB 1 ATOM 1810 C CG . PHE A 1 236 ? 49.122 -48.946 30.095 1.00 73.05 ? 236 PHE A CG 1 ATOM 1811 C CD1 . PHE A 1 236 ? 49.292 -47.742 29.427 1.00 70.89 ? 236 PHE A CD1 1 ATOM 1812 C CD2 . PHE A 1 236 ? 48.619 -50.036 29.392 1.00 72.02 ? 236 PHE A CD2 1 ATOM 1813 C CE1 . PHE A 1 236 ? 48.970 -47.626 28.085 1.00 67.72 ? 236 PHE A CE1 1 ATOM 1814 C CE2 . PHE A 1 236 ? 48.298 -49.928 28.050 1.00 68.87 ? 236 PHE A CE2 1 ATOM 1815 C CZ . PHE A 1 236 ? 48.470 -48.720 27.396 1.00 66.78 ? 236 PHE A CZ 1 ATOM 1816 N N . SER A 1 237 ? 52.283 -48.519 33.699 1.00 85.37 ? 237 SER A N 1 ATOM 1817 C CA . SER A 1 237 ? 52.532 -48.197 35.104 1.00 88.54 ? 237 SER A CA 1 ATOM 1818 C C . SER A 1 237 ? 51.827 -46.881 35.407 1.00 86.40 ? 237 SER A C 1 ATOM 1819 O O . SER A 1 237 ? 51.999 -45.915 34.664 1.00 83.80 ? 237 SER A O 1 ATOM 1820 C CB . SER A 1 237 ? 54.027 -48.055 35.377 1.00 91.91 ? 237 SER A CB 1 ATOM 1821 O OG . SER A 1 237 ? 54.533 -46.869 34.793 1.00 90.33 ? 237 SER A OG 1 ATOM 1822 N N . PHE A 1 238 ? 51.028 -46.837 36.473 1.00 87.44 ? 238 PHE A N 1 ATOM 1823 C CA . PHE A 1 238 ? 50.297 -45.608 36.806 1.00 85.84 ? 238 PHE A CA 1 ATOM 1824 C C . PHE A 1 238 ? 49.969 -45.418 38.289 1.00 88.58 ? 238 PHE A C 1 ATOM 1825 O O . PHE A 1 238 ? 49.614 -46.363 38.992 1.00 90.86 ? 238 PHE A O 1 ATOM 1826 C CB . PHE A 1 238 ? 49.021 -45.476 35.959 1.00 81.88 ? 238 PHE A CB 1 ATOM 1827 C CG . PHE A 1 238 ? 48.089 -46.657 36.041 1.00 81.95 ? 238 PHE A CG 1 ATOM 1828 C CD1 . PHE A 1 238 ? 48.348 -47.814 35.315 1.00 81.91 ? 238 PHE A CD1 1 ATOM 1829 C CD2 . PHE A 1 238 ? 46.929 -46.596 36.804 1.00 82.06 ? 238 PHE A CD2 1 ATOM 1830 C CE1 . PHE A 1 238 ? 47.484 -48.896 35.366 1.00 82.00 ? 238 PHE A CE1 1 ATOM 1831 C CE2 . PHE A 1 238 ? 46.059 -47.675 36.858 1.00 82.19 ? 238 PHE A CE2 1 ATOM 1832 C CZ . PHE A 1 238 ? 46.336 -48.825 36.137 1.00 82.06 ? 238 PHE A CZ 1 ATOM 1833 N N . ASN A 1 239 ? 50.106 -44.171 38.734 1.00 88.59 ? 239 ASN A N 1 ATOM 1834 C CA . ASN A 1 239 ? 49.740 -43.737 40.077 1.00 90.97 ? 239 ASN A CA 1 ATOM 1835 C C . ASN A 1 239 ? 48.464 -42.898 40.082 1.00 88.22 ? 239 ASN A C 1 ATOM 1836 O O . ASN A 1 239 ? 47.990 -42.511 41.146 1.00 89.92 ? 239 ASN A O 1 ATOM 1837 C CB . ASN A 1 239 ? 50.886 -42.915 40.703 1.00 93.77 ? 239 ASN A CB 1 ATOM 1838 C CG . ASN A 1 239 ? 51.568 -43.630 41.860 1.00 98.62 ? 239 ASN A CG 1 ATOM 1839 O OD1 . ASN A 1 239 ? 51.223 -44.761 42.197 1.00 100.19 ? 239 ASN A OD1 1 ATOM 1840 N ND2 . ASN A 1 239 ? 52.543 -42.966 42.478 1.00 101.31 ? 239 ASN A ND2 1 ATOM 1841 N N . GLY A 1 240 ? 47.915 -42.618 38.901 1.00 84.03 ? 240 GLY A N 1 ATOM 1842 C CA . GLY A 1 240 ? 46.692 -41.824 38.785 1.00 81.45 ? 240 GLY A CA 1 ATOM 1843 C C . GLY A 1 240 ? 46.626 -41.006 37.510 1.00 77.61 ? 240 GLY A C 1 ATOM 1844 O O . GLY A 1 240 ? 47.324 -41.297 36.540 1.00 76.66 ? 240 GLY A O 1 ATOM 1845 N N . ALA A 1 241 ? 45.770 -39.985 37.520 1.00 75.87 ? 241 ALA A N 1 ATOM 1846 C CA . ALA A 1 241 ? 45.563 -39.083 36.382 1.00 72.60 ? 241 ALA A CA 1 ATOM 1847 C C . ALA A 1 241 ? 45.187 -39.772 35.058 1.00 69.37 ? 241 ALA A C 1 ATOM 1848 O O . ALA A 1 241 ? 45.148 -39.119 34.015 1.00 66.93 ? 241 ALA A O 1 ATOM 1849 C CB . ALA A 1 241 ? 46.806 -38.228 36.183 1.00 73.34 ? 241 ALA A CB 1 ATOM 1850 N N . PHE A 1 242 ? 44.863 -41.062 35.116 1.00 69.59 ? 242 PHE A N 1 ATOM 1851 C CA . PHE A 1 242 ? 44.932 -41.951 33.954 1.00 67.54 ? 242 PHE A CA 1 ATOM 1852 C C . PHE A 1 242 ? 43.537 -42.445 33.519 1.00 65.26 ? 242 PHE A C 1 ATOM 1853 O O . PHE A 1 242 ? 42.702 -42.800 34.357 1.00 66.23 ? 242 PHE A O 1 ATOM 1854 C CB . PHE A 1 242 ? 45.886 -43.107 34.311 1.00 70.22 ? 242 PHE A CB 1 ATOM 1855 C CG . PHE A 1 242 ? 45.982 -44.193 33.273 1.00 69.09 ? 242 PHE A CG 1 ATOM 1856 C CD1 . PHE A 1 242 ? 46.391 -43.918 31.983 1.00 66.86 ? 242 PHE A CD1 1 ATOM 1857 C CD2 . PHE A 1 242 ? 45.718 -45.511 33.613 1.00 70.67 ? 242 PHE A CD2 1 ATOM 1858 C CE1 . PHE A 1 242 ? 46.496 -44.932 31.043 1.00 65.93 ? 242 PHE A CE1 1 ATOM 1859 C CE2 . PHE A 1 242 ? 45.815 -46.526 32.679 1.00 69.79 ? 242 PHE A CE2 1 ATOM 1860 C CZ . PHE A 1 242 ? 46.206 -46.238 31.387 1.00 67.32 ? 242 PHE A CZ 1 ATOM 1861 N N . ILE A 1 243 ? 43.289 -42.425 32.206 1.00 61.97 ? 243 ILE A N 1 ATOM 1862 C CA . ILE A 1 243 ? 42.021 -42.874 31.621 1.00 59.67 ? 243 ILE A CA 1 ATOM 1863 C C . ILE A 1 243 ? 42.267 -44.172 30.856 1.00 58.89 ? 243 ILE A C 1 ATOM 1864 O O . ILE A 1 243 ? 42.898 -44.167 29.804 1.00 57.29 ? 243 ILE A O 1 ATOM 1865 C CB . ILE A 1 243 ? 41.437 -41.816 30.662 1.00 56.83 ? 243 ILE A CB 1 ATOM 1866 C CG1 . ILE A 1 243 ? 41.260 -40.467 31.375 1.00 57.59 ? 243 ILE A CG1 1 ATOM 1867 C CG2 . ILE A 1 243 ? 40.120 -42.292 30.055 1.00 54.90 ? 243 ILE A CG2 1 ATOM 1868 C CD1 . ILE A 1 243 ? 40.180 -40.445 32.438 1.00 58.90 ? 243 ILE A CD1 1 ATOM 1869 N N . ALA A 1 244 ? 41.758 -45.278 31.388 1.00 60.19 ? 244 ALA A N 1 ATOM 1870 C CA . ALA A 1 244 ? 42.153 -46.612 30.931 1.00 60.62 ? 244 ALA A CA 1 ATOM 1871 C C . ALA A 1 244 ? 41.369 -47.099 29.711 1.00 57.66 ? 244 ALA A C 1 ATOM 1872 O O . ALA A 1 244 ? 40.141 -46.984 29.669 1.00 56.62 ? 244 ALA A O 1 ATOM 1873 C CB . ALA A 1 244 ? 42.003 -47.615 32.061 1.00 63.82 ? 244 ALA A CB 1 ATOM 1874 N N . PRO A 1 245 ? 42.072 -47.680 28.728 1.00 56.68 ? 245 PRO A N 1 ATOM 1875 C CA . PRO A 1 245 ? 41.350 -48.271 27.598 1.00 54.44 ? 245 PRO A CA 1 ATOM 1876 C C . PRO A 1 245 ? 40.615 -49.532 28.001 1.00 55.49 ? 245 PRO A C 1 ATOM 1877 O O . PRO A 1 245 ? 41.204 -50.417 28.624 1.00 57.96 ? 245 PRO A O 1 ATOM 1878 C CB . PRO A 1 245 ? 42.455 -48.625 26.600 1.00 54.04 ? 245 PRO A CB 1 ATOM 1879 C CG . PRO A 1 245 ? 43.714 -48.701 27.400 1.00 56.88 ? 245 PRO A CG 1 ATOM 1880 C CD . PRO A 1 245 ? 43.528 -47.893 28.649 1.00 58.12 ? 245 PRO A CD 1 ATOM 1881 N N . ASP A 1 246 ? 39.338 -49.607 27.644 1.00 54.00 ? 246 ASP A N 1 ATOM 1882 C CA . ASP A 1 246 ? 38.558 -50.817 27.857 1.00 54.89 ? 246 ASP A CA 1 ATOM 1883 C C . ASP A 1 246 ? 38.726 -51.778 26.680 1.00 53.60 ? 246 ASP A C 1 ATOM 1884 O O . ASP A 1 246 ? 38.944 -52.969 26.878 1.00 55.45 ? 246 ASP A O 1 ATOM 1885 C CB . ASP A 1 246 ? 37.081 -50.484 28.044 1.00 54.12 ? 246 ASP A CB 1 ATOM 1886 C CG . ASP A 1 246 ? 36.273 -51.686 28.430 1.00 55.67 ? 246 ASP A CG 1 ATOM 1887 O OD1 . ASP A 1 246 ? 36.624 -52.315 29.446 1.00 58.78 ? 246 ASP A OD1 1 ATOM 1888 O OD2 . ASP A 1 246 ? 35.309 -52.027 27.712 1.00 54.50 ? 246 ASP A OD2 1 ATOM 1889 N N . ARG A 1 247 ? 38.619 -51.257 25.460 1.00 50.69 ? 247 ARG A N 1 ATOM 1890 C CA . ARG A 1 247 ? 38.766 -52.069 24.251 1.00 49.38 ? 247 ARG A CA 1 ATOM 1891 C C . ARG A 1 247 ? 39.894 -51.585 23.344 1.00 47.96 ? 247 ARG A C 1 ATOM 1892 O O . ARG A 1 247 ? 40.252 -50.407 23.342 1.00 47.09 ? 247 ARG A O 1 ATOM 1893 C CB . ARG A 1 247 ? 37.472 -52.063 23.444 1.00 47.43 ? 247 ARG A CB 1 ATOM 1894 C CG . ARG A 1 247 ? 36.261 -52.645 24.154 1.00 48.62 ? 247 ARG A CG 1 ATOM 1895 C CD . ARG A 1 247 ? 34.978 -52.166 23.489 1.00 46.75 ? 247 ARG A CD 1 ATOM 1896 N NE . ARG A 1 247 ? 34.355 -53.161 22.634 1.00 46.35 ? 247 ARG A NE 1 ATOM 1897 C CZ . ARG A 1 247 ? 33.358 -52.917 21.781 1.00 44.77 ? 247 ARG A CZ 1 ATOM 1898 N NH1 . ARG A 1 247 ? 32.862 -51.690 21.637 1.00 43.42 ? 247 ARG A NH1 1 ATOM 1899 N NH2 . ARG A 1 247 ? 32.852 -53.915 21.064 1.00 44.46 ? 247 ARG A NH2 1 ATOM 1900 N N . ALA A 1 248 ? 40.436 -52.516 22.564 1.00 47.75 ? 248 ALA A N 1 ATOM 1901 C CA . ALA A 1 248 ? 41.441 -52.214 21.550 1.00 46.65 ? 248 ALA A CA 1 ATOM 1902 C C . ALA A 1 248 ? 40.783 -52.216 20.175 1.00 43.74 ? 248 ALA A C 1 ATOM 1903 O O . ALA A 1 248 ? 39.778 -52.897 19.963 1.00 43.12 ? 248 ALA A O 1 ATOM 1904 C CB . ALA A 1 248 ? 42.557 -53.249 21.591 1.00 48.96 ? 248 ALA A CB 1 ATOM 1905 N N . SER A 1 249 ? 41.361 -51.458 19.246 1.00 42.06 ? 249 SER A N 1 ATOM 1906 C CA . SER A 1 249 ? 40.870 -51.401 17.872 1.00 39.59 ? 249 SER A CA 1 ATOM 1907 C C . SER A 1 249 ? 41.777 -52.160 16.917 1.00 39.77 ? 249 SER A C 1 ATOM 1908 O O . SER A 1 249 ? 43.000 -52.088 17.031 1.00 41.21 ? 249 SER A O 1 ATOM 1909 C CB . SER A 1 249 ? 40.764 -49.952 17.421 1.00 37.82 ? 249 SER A CB 1 ATOM 1910 O OG . SER A 1 249 ? 39.845 -49.267 18.233 1.00 37.51 ? 249 SER A OG 1 ATOM 1911 N N . PHE A 1 250 ? 41.167 -52.889 15.987 1.00 38.47 ? 250 PHE A N 1 ATOM 1912 C CA . PHE A 1 250 ? 41.890 -53.544 14.904 1.00 38.54 ? 250 PHE A CA 1 ATOM 1913 C C . PHE A 1 250 ? 41.345 -53.029 13.585 1.00 36.28 ? 250 PHE A C 1 ATOM 1914 O O . PHE A 1 250 ? 40.137 -52.827 13.450 1.00 34.66 ? 250 PHE A O 1 ATOM 1915 C CB . PHE A 1 250 ? 41.734 -55.055 15.001 1.00 39.87 ? 250 PHE A CB 1 ATOM 1916 C CG . PHE A 1 250 ? 42.416 -55.648 16.192 1.00 42.44 ? 250 PHE A CG 1 ATOM 1917 C CD1 . PHE A 1 250 ? 41.763 -55.731 17.412 1.00 43.14 ? 250 PHE A CD1 1 ATOM 1918 C CD2 . PHE A 1 250 ? 43.727 -56.089 16.104 1.00 44.48 ? 250 PHE A CD2 1 ATOM 1919 C CE1 . PHE A 1 250 ? 42.400 -56.257 18.525 1.00 45.81 ? 250 PHE A CE1 1 ATOM 1920 C CE2 . PHE A 1 250 ? 44.369 -56.620 17.210 1.00 47.23 ? 250 PHE A CE2 1 ATOM 1921 C CZ . PHE A 1 250 ? 43.705 -56.700 18.423 1.00 47.87 ? 250 PHE A CZ 1 ATOM 1922 N N . LEU A 1 251 ? 42.232 -52.809 12.616 1.00 36.32 ? 251 LEU A N 1 ATOM 1923 C CA . LEU A 1 251 ? 41.833 -52.234 11.323 1.00 34.51 ? 251 LEU A CA 1 ATOM 1924 C C . LEU A 1 251 ? 41.336 -53.338 10.396 1.00 34.42 ? 251 LEU A C 1 ATOM 1925 O O . LEU A 1 251 ? 41.933 -54.409 10.331 1.00 35.87 ? 251 LEU A O 1 ATOM 1926 C CB . LEU A 1 251 ? 42.990 -51.479 10.664 1.00 34.81 ? 251 LEU A CB 1 ATOM 1927 C CG . LEU A 1 251 ? 43.829 -50.542 11.553 1.00 35.70 ? 251 LEU A CG 1 ATOM 1928 C CD1 . LEU A 1 251 ? 44.851 -49.798 10.710 1.00 35.99 ? 251 LEU A CD1 1 ATOM 1929 C CD2 . LEU A 1 251 ? 42.945 -49.573 12.319 1.00 34.48 ? 251 LEU A CD2 1 ATOM 1930 N N . ARG A 1 252 ? 40.266 -53.046 9.658 1.00 32.84 ? 252 ARG A N 1 ATOM 1931 C CA . ARG A 1 252 ? 39.544 -54.049 8.877 1.00 32.77 ? 252 ARG A CA 1 ATOM 1932 C C . ARG A 1 252 ? 40.152 -54.377 7.526 1.00 33.32 ? 252 ARG A C 1 ATOM 1933 O O . ARG A 1 252 ? 40.129 -55.534 7.100 1.00 34.23 ? 252 ARG A O 1 ATOM 1934 C CB . ARG A 1 252 ? 38.101 -53.595 8.654 1.00 31.02 ? 252 ARG A CB 1 ATOM 1935 C CG . ARG A 1 252 ? 37.257 -53.656 9.907 1.00 31.19 ? 252 ARG A CG 1 ATOM 1936 C CD . ARG A 1 252 ? 35.819 -53.277 9.620 1.00 29.96 ? 252 ARG A CD 1 ATOM 1937 N NE . ARG A 1 252 ? 35.027 -53.277 10.847 1.00 30.40 ? 252 ARG A NE 1 ATOM 1938 C CZ . ARG A 1 252 ? 34.427 -54.347 11.364 1.00 31.25 ? 252 ARG A CZ 1 ATOM 1939 N NH1 . ARG A 1 252 ? 34.498 -55.534 10.762 1.00 31.73 ? 252 ARG A NH1 1 ATOM 1940 N NH2 . ARG A 1 252 ? 33.745 -54.220 12.496 1.00 31.85 ? 252 ARG A NH2 1 ATOM 1941 N N . GLY A 1 253 ? 40.651 -53.363 6.830 1.00 33.13 ? 253 GLY A N 1 ATOM 1942 C CA . GLY A 1 253 ? 41.153 -53.555 5.478 1.00 33.83 ? 253 GLY A CA 1 ATOM 1943 C C . GLY A 1 253 ? 41.651 -52.278 4.831 1.00 33.78 ? 253 GLY A C 1 ATOM 1944 O O . GLY A 1 253 ? 42.703 -51.761 5.205 1.00 35.02 ? 253 GLY A O 1 ATOM 1945 N N . LYS A 1 254 ? 40.898 -51.778 3.856 1.00 32.93 ? 254 LYS A N 1 ATOM 1946 C CA . LYS A 1 254 ? 41.312 -50.631 3.058 1.00 33.11 ? 254 LYS A CA 1 ATOM 1947 C C . LYS A 1 254 ? 40.150 -49.684 2.863 1.00 31.04 ? 254 LYS A C 1 ATOM 1948 O O . LYS A 1 254 ? 39.015 -50.114 2.698 1.00 30.21 ? 254 LYS A O 1 ATOM 1949 C CB . LYS A 1 254 ? 41.813 -51.093 1.690 1.00 34.76 ? 254 LYS A CB 1 ATOM 1950 C CG . LYS A 1 254 ? 43.197 -51.723 1.723 1.00 37.82 ? 254 LYS A CG 1 ATOM 1951 C CD . LYS A 1 254 ? 43.542 -52.432 0.411 1.00 39.47 ? 254 LYS A CD 1 ATOM 1952 C CE . LYS A 1 254 ? 44.734 -53.369 0.559 1.00 42.25 ? 254 LYS A CE 1 ATOM 1953 N NZ . LYS A 1 254 ? 46.031 -52.639 0.675 1.00 44.21 ? 254 LYS A NZ 1 ATOM 1954 N N . SER A 1 255 ? 40.441 -48.393 2.894 1.00 30.26 ? 255 SER A N 1 ATOM 1955 C CA . SER A 1 255 ? 39.451 -47.387 2.577 1.00 28.95 ? 255 SER A CA 1 ATOM 1956 C C . SER A 1 255 ? 40.149 -46.131 2.115 1.00 29.49 ? 255 SER A C 1 ATOM 1957 O O . SER A 1 255 ? 41.370 -46.064 2.077 1.00 30.88 ? 255 SER A O 1 ATOM 1958 C CB . SER A 1 255 ? 38.554 -47.084 3.786 1.00 27.96 ? 255 SER A CB 1 ATOM 1959 O OG . SER A 1 255 ? 39.293 -46.639 4.912 1.00 28.23 ? 255 SER A OG 1 ATOM 1960 N N . MET A 1 256 ? 39.336 -45.148 1.771 1.00 29.00 ? 256 MET A N 1 ATOM 1961 C CA . MET A 1 256 ? 39.748 -43.848 1.306 1.00 29.59 ? 256 MET A CA 1 ATOM 1962 C C . MET A 1 256 ? 38.977 -42.879 2.199 1.00 28.12 ? 256 MET A C 1 ATOM 1963 O O . MET A 1 256 ? 37.777 -43.068 2.422 1.00 27.33 ? 256 MET A O 1 ATOM 1964 C CB . MET A 1 256 ? 39.306 -43.742 -0.159 1.00 30.84 ? 256 MET A CB 1 ATOM 1965 C CG . MET A 1 256 ? 39.302 -42.363 -0.787 1.00 32.40 ? 256 MET A CG 1 ATOM 1966 S SD . MET A 1 256 ? 40.858 -42.007 -1.608 1.00 36.44 ? 256 MET A SD 1 ATOM 1967 C CE . MET A 1 256 ? 40.915 -40.238 -1.367 1.00 36.71 ? 256 MET A CE 1 ATOM 1968 N N . GLY A 1 257 ? 39.649 -41.868 2.731 1.00 27.82 ? 257 GLY A N 1 ATOM 1969 C CA . GLY A 1 257 ? 39.011 -40.870 3.593 1.00 26.96 ? 257 GLY A CA 1 ATOM 1970 C C . GLY A 1 257 ? 38.950 -39.493 2.954 1.00 26.93 ? 257 GLY A C 1 ATOM 1971 O O . GLY A 1 257 ? 39.922 -39.050 2.374 1.00 27.65 ? 257 GLY A O 1 ATOM 1972 N N . ILE A 1 258 ? 37.800 -38.819 3.057 1.00 26.22 ? 258 ILE A N 1 ATOM 1973 C CA . ILE A 1 258 ? 37.647 -37.458 2.535 1.00 26.61 ? 258 ILE A CA 1 ATOM 1974 C C . ILE A 1 258 ? 36.979 -36.529 3.547 1.00 26.55 ? 258 ILE A C 1 ATOM 1975 O O . ILE A 1 258 ? 36.285 -36.975 4.460 1.00 25.79 ? 258 ILE A O 1 ATOM 1976 C CB . ILE A 1 258 ? 36.851 -37.430 1.210 1.00 26.62 ? 258 ILE A CB 1 ATOM 1977 C CG1 . ILE A 1 258 ? 35.362 -37.692 1.445 1.00 25.93 ? 258 ILE A CG1 1 ATOM 1978 C CG2 . ILE A 1 258 ? 37.410 -38.453 0.226 1.00 26.68 ? 258 ILE A CG2 1 ATOM 1979 C CD1 . ILE A 1 258 ? 34.547 -37.600 0.178 1.00 26.28 ? 258 ILE A CD1 1 ATOM 1980 N N . GLN A 1 259 ? 37.226 -35.235 3.381 1.00 27.34 ? 259 GLN A N 1 ATOM 1981 C CA . GLN A 1 259 ? 36.532 -34.203 4.128 1.00 27.75 ? 259 GLN A CA 1 ATOM 1982 C C . GLN A 1 259 ? 35.660 -33.471 3.131 1.00 28.37 ? 259 GLN A C 1 ATOM 1983 O O . GLN A 1 259 ? 36.109 -33.168 2.024 1.00 29.03 ? 259 GLN A O 1 ATOM 1984 C CB . GLN A 1 259 ? 37.524 -33.228 4.751 1.00 28.70 ? 259 GLN A CB 1 ATOM 1985 C CG . GLN A 1 259 ? 38.581 -33.885 5.627 1.00 28.58 ? 259 GLN A CG 1 ATOM 1986 C CD . GLN A 1 259 ? 39.514 -32.878 6.250 1.00 29.70 ? 259 GLN A CD 1 ATOM 1987 O OE1 . GLN A 1 259 ? 40.198 -32.136 5.546 1.00 30.80 ? 259 GLN A OE1 1 ATOM 1988 N NE2 . GLN A 1 259 ? 39.555 -32.847 7.573 1.00 29.74 ? 259 GLN A NE2 1 ATOM 1989 N N . SER A 1 260 ? 34.422 -33.180 3.511 1.00 28.40 ? 260 SER A N 1 ATOM 1990 C CA . SER A 1 260 ? 33.483 -32.581 2.573 1.00 29.29 ? 260 SER A CA 1 ATOM 1991 C C . SER A 1 260 ? 32.290 -31.958 3.245 1.00 29.76 ? 260 SER A C 1 ATOM 1992 O O . SER A 1 260 ? 31.920 -32.351 4.347 1.00 29.33 ? 260 SER A O 1 ATOM 1993 C CB . SER A 1 260 ? 32.978 -33.640 1.593 1.00 28.82 ? 260 SER A CB 1 ATOM 1994 O OG . SER A 1 260 ? 31.832 -33.169 0.898 1.00 29.76 ? 260 SER A OG 1 ATOM 1995 N N . GLY A 1 261 ? 31.676 -31.007 2.547 1.00 31.05 ? 261 GLY A N 1 ATOM 1996 C CA . GLY A 1 261 ? 30.469 -30.343 3.023 1.00 32.09 ? 261 GLY A CA 1 ATOM 1997 C C . GLY A 1 261 ? 29.245 -30.518 2.133 1.00 32.74 ? 261 GLY A C 1 ATOM 1998 O O . GLY A 1 261 ? 28.269 -29.788 2.295 1.00 34.21 ? 261 GLY A O 1 ATOM 1999 N N . VAL A 1 262 ? 29.273 -31.479 1.210 1.00 32.00 ? 262 VAL A N 1 ATOM 2000 C CA . VAL A 1 262 ? 28.125 -31.718 0.325 1.00 32.79 ? 262 VAL A CA 1 ATOM 2001 C C . VAL A 1 262 ? 27.503 -33.106 0.507 1.00 31.79 ? 262 VAL A C 1 ATOM 2002 O O . VAL A 1 262 ? 28.071 -33.984 1.155 1.00 30.17 ? 262 VAL A O 1 ATOM 2003 C CB . VAL A 1 262 ? 28.482 -31.487 -1.161 1.00 33.51 ? 262 VAL A CB 1 ATOM 2004 C CG1 . VAL A 1 262 ? 28.973 -30.065 -1.355 1.00 35.06 ? 262 VAL A CG1 1 ATOM 2005 C CG2 . VAL A 1 262 ? 29.516 -32.494 -1.649 1.00 32.18 ? 262 VAL A CG2 1 ATOM 2006 N N . GLN A 1 263 ? 26.331 -33.285 -0.087 1.00 32.94 ? 263 GLN A N 1 ATOM 2007 C CA . GLN A 1 263 ? 25.533 -34.479 0.127 1.00 32.59 ? 263 GLN A CA 1 ATOM 2008 C C . GLN A 1 263 ? 26.067 -35.695 -0.587 1.00 31.22 ? 263 GLN A C 1 ATOM 2009 O O . GLN A 1 263 ? 26.669 -35.599 -1.647 1.00 31.47 ? 263 GLN A O 1 ATOM 2010 C CB . GLN A 1 263 ? 24.112 -34.276 -0.379 1.00 34.52 ? 263 GLN A CB 1 ATOM 2011 C CG . GLN A 1 263 ? 23.307 -33.256 0.376 1.00 36.73 ? 263 GLN A CG 1 ATOM 2012 C CD . GLN A 1 263 ? 22.108 -32.801 -0.437 1.00 39.35 ? 263 GLN A CD 1 ATOM 2013 O OE1 . GLN A 1 263 ? 21.487 -33.603 -1.151 1.00 39.82 ? 263 GLN A OE1 1 ATOM 2014 N NE2 . GLN A 1 263 ? 21.787 -31.513 -0.353 1.00 41.51 ? 263 GLN A NE2 1 ATOM 2015 N N . VAL A 1 264 ? 25.769 -36.848 -0.013 1.00 30.12 ? 264 VAL A N 1 ATOM 2016 C CA . VAL A 1 264 ? 26.053 -38.132 -0.634 1.00 29.28 ? 264 VAL A CA 1 ATOM 2017 C C . VAL A 1 264 ? 25.018 -38.408 -1.724 1.00 30.13 ? 264 VAL A C 1 ATOM 2018 O O . VAL A 1 264 ? 23.856 -38.018 -1.607 1.00 31.44 ? 264 VAL A O 1 ATOM 2019 C CB . VAL A 1 264 ? 26.049 -39.250 0.430 1.00 28.19 ? 264 VAL A CB 1 ATOM 2020 C CG1 . VAL A 1 264 ? 26.177 -40.623 -0.207 1.00 27.67 ? 264 VAL A CG1 1 ATOM 2021 C CG2 . VAL A 1 264 ? 27.183 -39.017 1.421 1.00 27.47 ? 264 VAL A CG2 1 ATOM 2022 N N . ASP A 1 265 ? 25.455 -39.066 -2.789 1.00 29.86 ? 265 ASP A N 1 ATOM 2023 C CA . ASP A 1 265 ? 24.589 -39.397 -3.918 1.00 30.65 ? 265 ASP A CA 1 ATOM 2024 C C . ASP A 1 265 ? 24.980 -40.767 -4.460 1.00 29.31 ? 265 ASP A C 1 ATOM 2025 O O . ASP A 1 265 ? 26.088 -40.941 -4.960 1.00 28.81 ? 265 ASP A O 1 ATOM 2026 C CB . ASP A 1 265 ? 24.736 -38.317 -4.995 1.00 32.40 ? 265 ASP A CB 1 ATOM 2027 C CG . ASP A 1 265 ? 23.786 -38.515 -6.171 1.00 34.22 ? 265 ASP A CG 1 ATOM 2028 O OD1 . ASP A 1 265 ? 23.263 -39.632 -6.331 1.00 34.06 ? 265 ASP A OD1 1 ATOM 2029 O OD2 . ASP A 1 265 ? 23.568 -37.551 -6.944 1.00 36.18 ? 265 ASP A OD2 1 ATOM 2030 N N . ALA A 1 266 ? 24.075 -41.740 -4.350 1.00 28.77 ? 266 ALA A N 1 ATOM 2031 C CA . ALA A 1 266 ? 24.350 -43.112 -4.799 1.00 27.84 ? 266 ALA A CA 1 ATOM 2032 C C . ALA A 1 266 ? 23.931 -43.348 -6.249 1.00 28.77 ? 266 ALA A C 1 ATOM 2033 O O . ALA A 1 266 ? 23.928 -44.483 -6.734 1.00 28.26 ? 266 ALA A O 1 ATOM 2034 C CB . ALA A 1 266 ? 23.665 -44.115 -3.876 1.00 27.33 ? 266 ALA A CB 1 ATOM 2035 N N . ASN A 1 267 ? 23.570 -42.268 -6.932 1.00 30.22 ? 267 ASN A N 1 ATOM 2036 C CA . ASN A 1 267 ? 23.156 -42.314 -8.322 1.00 31.82 ? 267 ASN A CA 1 ATOM 2037 C C . ASN A 1 267 ? 24.315 -42.092 -9.304 1.00 32.59 ? 267 ASN A C 1 ATOM 2038 O O . ASN A 1 267 ? 24.217 -42.470 -10.467 1.00 33.33 ? 267 ASN A O 1 ATOM 2039 C CB . ASN A 1 267 ? 22.040 -41.280 -8.548 1.00 33.41 ? 267 ASN A CB 1 ATOM 2040 C CG . ASN A 1 267 ? 21.618 -41.178 -9.992 1.00 34.95 ? 267 ASN A CG 1 ATOM 2041 O OD1 . ASN A 1 267 ? 21.901 -40.181 -10.647 1.00 35.96 ? 267 ASN A OD1 1 ATOM 2042 N ND2 . ASN A 1 267 ? 20.958 -42.211 -10.500 1.00 35.11 ? 267 ASN A ND2 1 ATOM 2043 N N . CYS A 1 268 ? 25.401 -41.481 -8.834 1.00 32.97 ? 268 CYS A N 1 ATOM 2044 C CA . CYS A 1 268 ? 26.595 -41.268 -9.654 1.00 34.27 ? 268 CYS A CA 1 ATOM 2045 C C . CYS A 1 268 ? 27.805 -41.960 -9.046 1.00 33.20 ? 268 CYS A C 1 ATOM 2046 O O . CYS A 1 268 ? 27.911 -42.094 -7.825 1.00 32.18 ? 268 CYS A O 1 ATOM 2047 C CB . CYS A 1 268 ? 26.895 -39.772 -9.825 1.00 35.79 ? 268 CYS A CB 1 ATOM 2048 S SG . CYS A 1 268 ? 26.903 -38.832 -8.279 0.80 35.89 ? 268 CYS A SG 1 ATOM 2049 N N . GLU A 1 269 ? 28.717 -42.390 -9.910 1.00 42.52 ? 269 GLU A N 1 ATOM 2050 C CA . GLU A 1 269 ? 29.954 -43.018 -9.483 1.00 41.23 ? 269 GLU A CA 1 ATOM 2051 C C . GLU A 1 269 ? 31.130 -42.100 -9.777 1.00 38.06 ? 269 GLU A C 1 ATOM 2052 O O . GLU A 1 269 ? 31.196 -41.476 -10.830 1.00 38.16 ? 269 GLU A O 1 ATOM 2053 C CB . GLU A 1 269 ? 30.156 -44.348 -10.204 1.00 44.26 ? 269 GLU A CB 1 ATOM 2054 C CG . GLU A 1 269 ? 31.518 -44.972 -9.946 1.00 43.77 ? 269 GLU A CG 1 ATOM 2055 C CD . GLU A 1 269 ? 31.523 -46.466 -10.156 1.00 47.26 ? 269 GLU A CD 1 ATOM 2056 O OE1 . GLU A 1 269 ? 30.813 -46.939 -11.072 1.00 50.80 ? 269 GLU A OE1 1 ATOM 2057 O OE2 . GLU A 1 269 ? 32.237 -47.169 -9.402 1.00 47.84 ? 269 GLU A OE2 1 ATOM 2058 N N . GLY A 1 270 ? 32.059 -42.016 -8.838 1.00 35.33 ? 270 GLY A N 1 ATOM 2059 C CA . GLY A 1 270 ? 33.271 -41.241 -9.049 1.00 32.74 ? 270 GLY A CA 1 ATOM 2060 C C . GLY A 1 270 ? 34.390 -41.770 -8.189 1.00 31.00 ? 270 GLY A C 1 ATOM 2061 O O . GLY A 1 270 ? 34.148 -42.503 -7.242 1.00 31.46 ? 270 GLY A O 1 ATOM 2062 N N . ASP A 1 271 ? 35.617 -41.404 -8.537 1.00 29.29 ? 271 ASP A N 1 ATOM 2063 C CA . ASP A 1 271 ? 36.798 -41.814 -7.785 1.00 28.02 ? 271 ASP A CA 1 ATOM 2064 C C . ASP A 1 271 ? 37.717 -40.652 -7.421 1.00 25.70 ? 271 ASP A C 1 ATOM 2065 O O . ASP A 1 271 ? 38.742 -40.860 -6.779 1.00 25.08 ? 271 ASP A O 1 ATOM 2066 C CB . ASP A 1 271 ? 37.567 -42.870 -8.578 1.00 29.19 ? 271 ASP A CB 1 ATOM 2067 C CG . ASP A 1 271 ? 36.858 -44.208 -8.604 1.00 31.69 ? 271 ASP A CG 1 ATOM 2068 O OD1 . ASP A 1 271 ? 36.264 -44.592 -7.575 1.00 32.33 ? 271 ASP A OD1 1 ATOM 2069 O OD2 . ASP A 1 271 ? 36.898 -44.895 -9.651 1.00 33.73 ? 271 ASP A OD2 1 ATOM 2070 N N . CYS A 1 272 ? 37.341 -39.437 -7.803 1.00 24.67 ? 272 CYS A N 1 ATOM 2071 C CA . CYS A 1 272 ? 38.094 -38.255 -7.462 1.00 23.21 ? 272 CYS A CA 1 ATOM 2072 C C . CYS A 1 272 ? 37.223 -37.281 -6.681 1.00 22.70 ? 272 CYS A C 1 ATOM 2073 O O . CYS A 1 272 ? 36.221 -36.781 -7.202 1.00 23.37 ? 272 CYS A O 1 ATOM 2074 C CB . CYS A 1 272 ? 38.626 -37.570 -8.716 1.00 23.06 ? 272 CYS A CB 1 ATOM 2075 S SG . CYS A 1 272 ? 39.659 -36.147 -8.315 1.00 22.25 ? 272 CYS A SG 1 ATOM 2076 N N . TYR A 1 273 ? 37.625 -36.999 -5.445 1.00 21.69 ? 273 TYR A N 1 ATOM 2077 C CA . TYR A 1 273 ? 36.817 -36.213 -4.536 1.00 21.72 ? 273 TYR A CA 1 ATOM 2078 C C . TYR A 1 273 ? 37.577 -35.016 -3.996 1.00 21.10 ? 273 TYR A C 1 ATOM 2079 O O . TYR A 1 273 ? 38.790 -35.050 -3.871 1.00 20.61 ? 273 TYR A O 1 ATOM 2080 C CB . TYR A 1 273 ? 36.386 -37.059 -3.345 1.00 21.85 ? 273 TYR A CB 1 ATOM 2081 C CG . TYR A 1 273 ? 35.632 -38.312 -3.677 1.00 22.72 ? 273 TYR A CG 1 ATOM 2082 C CD1 . TYR A 1 273 ? 34.303 -38.254 -4.072 1.00 23.73 ? 273 TYR A CD1 1 ATOM 2083 C CD2 . TYR A 1 273 ? 36.230 -39.558 -3.564 1.00 22.81 ? 273 TYR A CD2 1 ATOM 2084 C CE1 . TYR A 1 273 ? 33.593 -39.400 -4.351 1.00 25.05 ? 273 TYR A CE1 1 ATOM 2085 C CE2 . TYR A 1 273 ? 35.521 -40.719 -3.840 1.00 24.20 ? 273 TYR A CE2 1 ATOM 2086 C CZ . TYR A 1 273 ? 34.198 -40.628 -4.232 1.00 25.24 ? 273 TYR A CZ 1 ATOM 2087 O OH . TYR A 1 273 ? 33.477 -41.748 -4.520 1.00 26.81 ? 273 TYR A OH 1 ATOM 2088 N N . HIS A 1 274 ? 36.829 -33.970 -3.665 1.00 21.87 ? 274 HIS A N 1 ATOM 2089 C CA . HIS A 1 274 ? 37.343 -32.796 -2.956 1.00 21.88 ? 274 HIS A CA 1 ATOM 2090 C C . HIS A 1 274 ? 36.206 -32.285 -2.061 1.00 22.82 ? 274 HIS A C 1 ATOM 2091 O O . HIS A 1 274 ? 35.108 -32.857 -2.082 1.00 23.46 ? 274 HIS A O 1 ATOM 2092 C CB . HIS A 1 274 ? 37.829 -31.736 -3.940 1.00 21.86 ? 274 HIS A CB 1 ATOM 2093 C CG . HIS A 1 274 ? 36.756 -31.189 -4.823 1.00 22.85 ? 274 HIS A CG 1 ATOM 2094 N ND1 . HIS A 1 274 ? 36.288 -29.899 -4.714 1.00 23.82 ? 274 HIS A ND1 1 ATOM 2095 C CD2 . HIS A 1 274 ? 36.052 -31.759 -5.828 1.00 23.56 ? 274 HIS A CD2 1 ATOM 2096 C CE1 . HIS A 1 274 ? 35.345 -29.695 -5.615 1.00 24.72 ? 274 HIS A CE1 1 ATOM 2097 N NE2 . HIS A 1 274 ? 35.177 -30.812 -6.299 1.00 24.56 ? 274 HIS A NE2 1 ATOM 2098 N N . SER A 1 275 ? 36.438 -31.235 -1.275 1.00 23.07 ? 275 SER A N 1 ATOM 2099 C CA . SER A 1 275 ? 35.431 -30.840 -0.279 1.00 24.15 ? 275 SER A CA 1 ATOM 2100 C C . SER A 1 275 ? 34.121 -30.389 -0.920 1.00 25.09 ? 275 SER A C 1 ATOM 2101 O O . SER A 1 275 ? 33.036 -30.585 -0.355 1.00 26.17 ? 275 SER A O 1 ATOM 2102 C CB . SER A 1 275 ? 35.967 -29.760 0.656 1.00 24.69 ? 275 SER A CB 1 ATOM 2103 O OG . SER A 1 275 ? 36.376 -28.624 -0.072 1.00 25.40 ? 275 SER A OG 1 ATOM 2104 N N . GLY A 1 276 ? 34.230 -29.818 -2.111 1.00 24.96 ? 276 GLY A N 1 ATOM 2105 C CA . GLY A 1 276 ? 33.075 -29.334 -2.845 1.00 26.20 ? 276 GLY A CA 1 ATOM 2106 C C . GLY A 1 276 ? 32.356 -30.375 -3.681 1.00 26.36 ? 276 GLY A C 1 ATOM 2107 O O . GLY A 1 276 ? 31.319 -30.071 -4.271 1.00 28.02 ? 276 GLY A O 1 ATOM 2108 N N . GLY A 1 277 ? 32.877 -31.599 -3.739 1.00 24.97 ? 277 GLY A N 1 ATOM 2109 C CA . GLY A 1 277 ? 32.193 -32.650 -4.482 1.00 25.50 ? 277 GLY A CA 1 ATOM 2110 C C . GLY A 1 277 ? 33.076 -33.654 -5.202 1.00 24.43 ? 277 GLY A C 1 ATOM 2111 O O . GLY A 1 277 ? 34.123 -34.072 -4.699 1.00 23.11 ? 277 GLY A O 1 ATOM 2112 N N . THR A 1 278 ? 32.647 -34.030 -6.398 1.00 25.25 ? 278 THR A N 1 ATOM 2113 C CA . THR A 1 278 ? 33.278 -35.109 -7.138 1.00 25.06 ? 278 THR A CA 1 ATOM 2114 C C . THR A 1 278 ? 33.662 -34.654 -8.530 1.00 25.24 ? 278 THR A C 1 ATOM 2115 O O . THR A 1 278 ? 32.883 -33.997 -9.209 1.00 26.24 ? 278 THR A O 1 ATOM 2116 C CB . THR A 1 278 ? 32.334 -36.329 -7.251 1.00 26.54 ? 278 THR A CB 1 ATOM 2117 O OG1 . THR A 1 278 ? 31.892 -36.711 -5.942 1.00 26.54 ? 278 THR A OG1 1 ATOM 2118 C CG2 . THR A 1 278 ? 33.041 -37.506 -7.925 1.00 26.42 ? 278 THR A CG2 1 ATOM 2119 N N . ILE A 1 279 ? 34.869 -35.016 -8.954 1.00 24.58 ? 279 ILE A N 1 ATOM 2120 C CA . ILE A 1 279 ? 35.327 -34.715 -10.308 1.00 25.06 ? 279 ILE A CA 1 ATOM 2121 C C . ILE A 1 279 ? 35.174 -35.981 -11.129 1.00 26.50 ? 279 ILE A C 1 ATOM 2122 O O . ILE A 1 279 ? 35.948 -36.910 -10.963 1.00 26.16 ? 279 ILE A O 1 ATOM 2123 C CB . ILE A 1 279 ? 36.795 -34.269 -10.325 1.00 23.63 ? 279 ILE A CB 1 ATOM 2124 C CG1 . ILE A 1 279 ? 36.978 -33.047 -9.424 1.00 23.05 ? 279 ILE A CG1 1 ATOM 2125 C CG2 . ILE A 1 279 ? 37.247 -33.978 -11.753 1.00 23.81 ? 279 ILE A CG2 1 ATOM 2126 C CD1 . ILE A 1 279 ? 38.417 -32.619 -9.260 1.00 21.94 ? 279 ILE A CD1 1 ATOM 2127 N N . ILE A 1 280 ? 34.158 -36.022 -11.986 1.00 28.79 ? 280 ILE A N 1 ATOM 2128 C CA . ILE A 1 280 ? 33.950 -37.138 -12.904 1.00 30.81 ? 280 ILE A CA 1 ATOM 2129 C C . ILE A 1 280 ? 34.400 -36.682 -14.279 1.00 31.44 ? 280 ILE A C 1 ATOM 2130 O O . ILE A 1 280 ? 33.836 -35.742 -14.838 1.00 32.64 ? 280 ILE A O 1 ATOM 2131 C CB . ILE A 1 280 ? 32.466 -37.547 -12.985 1.00 33.32 ? 280 ILE A CB 1 ATOM 2132 C CG1 . ILE A 1 280 ? 31.960 -37.962 -11.604 1.00 33.45 ? 280 ILE A CG1 1 ATOM 2133 C CG2 . ILE A 1 280 ? 32.261 -38.691 -13.981 1.00 35.26 ? 280 ILE A CG2 1 ATOM 2134 C CD1 . ILE A 1 280 ? 30.526 -38.430 -11.599 1.00 36.10 ? 280 ILE A CD1 1 ATOM 2135 N N . SER A 1 281 ? 35.401 -37.353 -14.829 1.00 31.28 ? 281 SER A N 1 ATOM 2136 C CA . SER A 1 281 ? 36.024 -36.912 -16.072 1.00 31.36 ? 281 SER A CA 1 ATOM 2137 C C . SER A 1 281 ? 36.991 -37.961 -16.599 1.00 31.64 ? 281 SER A C 1 ATOM 2138 O O . SER A 1 281 ? 37.603 -38.689 -15.822 1.00 30.56 ? 281 SER A O 1 ATOM 2139 C CB . SER A 1 281 ? 36.798 -35.613 -15.830 1.00 29.45 ? 281 SER A CB 1 ATOM 2140 O OG . SER A 1 281 ? 37.304 -35.088 -17.041 1.00 29.28 ? 281 SER A OG 1 ATOM 2141 N N . ASN A 1 282 ? 37.124 -38.024 -17.920 1.00 33.33 ? 282 ASN A N 1 ATOM 2142 C CA . ASN A 1 282 ? 38.178 -38.813 -18.549 1.00 34.05 ? 282 ASN A CA 1 ATOM 2143 C C . ASN A 1 282 ? 39.377 -37.942 -18.968 1.00 31.98 ? 282 ASN A C 1 ATOM 2144 O O . ASN A 1 282 ? 40.379 -38.455 -19.465 1.00 31.47 ? 282 ASN A O 1 ATOM 2145 C CB . ASN A 1 282 ? 37.622 -39.559 -19.755 1.00 37.37 ? 282 ASN A CB 1 ATOM 2146 C CG . ASN A 1 282 ? 36.381 -40.370 -19.415 1.00 40.49 ? 282 ASN A CG 1 ATOM 2147 O OD1 . ASN A 1 282 ? 36.430 -41.280 -18.577 1.00 41.46 ? 282 ASN A OD1 1 ATOM 2148 N ND2 . ASN A 1 282 ? 35.256 -40.043 -20.061 1.00 42.78 ? 282 ASN A ND2 1 ATOM 2149 N N . LEU A 1 283 ? 39.290 -36.634 -18.737 1.00 30.33 ? 283 LEU A N 1 ATOM 2150 C CA . LEU A 1 283 ? 40.328 -35.718 -19.197 1.00 28.71 ? 283 LEU A CA 1 ATOM 2151 C C . LEU A 1 283 ? 41.574 -35.870 -18.339 1.00 27.10 ? 283 LEU A C 1 ATOM 2152 O O . LEU A 1 283 ? 41.476 -36.202 -17.164 1.00 27.25 ? 283 LEU A O 1 ATOM 2153 C CB . LEU A 1 283 ? 39.827 -34.279 -19.183 1.00 28.41 ? 283 LEU A CB 1 ATOM 2154 C CG . LEU A 1 283 ? 38.587 -33.988 -20.033 1.00 30.35 ? 283 LEU A CG 1 ATOM 2155 C CD1 . LEU A 1 283 ? 38.356 -32.484 -20.127 1.00 30.33 ? 283 LEU A CD1 1 ATOM 2156 C CD2 . LEU A 1 283 ? 38.681 -34.588 -21.431 1.00 31.56 ? 283 LEU A CD2 1 ATOM 2157 N N . PRO A 1 284 ? 42.762 -35.662 -18.930 1.00 25.93 ? 284 PRO A N 1 ATOM 2158 C CA . PRO A 1 284 ? 43.998 -35.909 -18.185 1.00 24.73 ? 284 PRO A CA 1 ATOM 2159 C C . PRO A 1 284 ? 44.305 -34.870 -17.093 1.00 22.98 ? 284 PRO A C 1 ATOM 2160 O O . PRO A 1 284 ? 45.056 -35.169 -16.155 1.00 22.69 ? 284 PRO A O 1 ATOM 2161 C CB . PRO A 1 284 ? 45.078 -35.879 -19.274 1.00 24.94 ? 284 PRO A CB 1 ATOM 2162 C CG . PRO A 1 284 ? 44.495 -35.041 -20.361 1.00 25.34 ? 284 PRO A CG 1 ATOM 2163 C CD . PRO A 1 284 ? 43.017 -35.284 -20.328 1.00 26.25 ? 284 PRO A CD 1 ATOM 2164 N N . PHE A 1 285 ? 43.735 -33.675 -17.214 1.00 21.97 ? 285 PHE A N 1 ATOM 2165 C CA . PHE A 1 285 ? 43.994 -32.592 -16.270 1.00 20.82 ? 285 PHE A CA 1 ATOM 2166 C C . PHE A 1 285 ? 42.706 -32.006 -15.691 1.00 20.81 ? 285 PHE A C 1 ATOM 2167 O O . PHE A 1 285 ? 41.635 -32.155 -16.271 1.00 21.59 ? 285 PHE A O 1 ATOM 2168 C CB . PHE A 1 285 ? 44.807 -31.491 -16.956 1.00 20.58 ? 285 PHE A CB 1 ATOM 2169 C CG . PHE A 1 285 ? 45.968 -32.008 -17.757 1.00 20.47 ? 285 PHE A CG 1 ATOM 2170 C CD1 . PHE A 1 285 ? 47.015 -32.664 -17.137 1.00 20.23 ? 285 PHE A CD1 1 ATOM 2171 C CD2 . PHE A 1 285 ? 45.994 -31.873 -19.144 1.00 20.97 ? 285 PHE A CD2 1 ATOM 2172 C CE1 . PHE A 1 285 ? 48.080 -33.159 -17.873 1.00 20.52 ? 285 PHE A CE1 1 ATOM 2173 C CE2 . PHE A 1 285 ? 47.057 -32.369 -19.887 1.00 20.99 ? 285 PHE A CE2 1 ATOM 2174 C CZ . PHE A 1 285 ? 48.098 -33.014 -19.247 1.00 20.84 ? 285 PHE A CZ 1 ATOM 2175 N N . GLN A 1 286 ? 42.827 -31.333 -14.549 1.00 20.19 ? 286 GLN A N 1 ATOM 2176 C CA . GLN A 1 286 ? 41.718 -30.600 -13.938 1.00 20.39 ? 286 GLN A CA 1 ATOM 2177 C C . GLN A 1 286 ? 42.198 -29.330 -13.268 1.00 20.23 ? 286 GLN A C 1 ATOM 2178 O O . GLN A 1 286 ? 43.326 -29.275 -12.765 1.00 19.75 ? 286 GLN A O 1 ATOM 2179 C CB . GLN A 1 286 ? 40.987 -31.470 -12.914 1.00 20.47 ? 286 GLN A CB 1 ATOM 2180 C CG . GLN A 1 286 ? 41.874 -32.025 -11.793 1.00 19.94 ? 286 GLN A CG 1 ATOM 2181 C CD . GLN A 1 286 ? 41.775 -31.274 -10.473 1.00 19.88 ? 286 GLN A CD 1 ATOM 2182 O OE1 . GLN A 1 286 ? 41.096 -30.257 -10.363 1.00 20.52 ? 286 GLN A OE1 1 ATOM 2183 N NE2 . GLN A 1 286 ? 42.456 -31.787 -9.455 1.00 19.61 ? 286 GLN A NE2 1 ATOM 2184 N N . ASN A 1 287 ? 41.334 -28.314 -13.260 1.00 20.94 ? 287 ASN A N 1 ATOM 2185 C CA . ASN A 1 287 ? 41.625 -27.031 -12.646 1.00 21.65 ? 287 ASN A CA 1 ATOM 2186 C C . ASN A 1 287 ? 40.564 -26.688 -11.580 1.00 22.59 ? 287 ASN A C 1 ATOM 2187 O O . ASN A 1 287 ? 40.211 -25.534 -11.392 1.00 23.39 ? 287 ASN A O 1 ATOM 2188 C CB . ASN A 1 287 ? 41.694 -25.962 -13.747 1.00 22.47 ? 287 ASN A CB 1 ATOM 2189 C CG . ASN A 1 287 ? 42.026 -24.574 -13.222 1.00 23.45 ? 287 ASN A CG 1 ATOM 2190 O OD1 . ASN A 1 287 ? 41.247 -23.643 -13.413 1.00 24.80 ? 287 ASN A OD1 1 ATOM 2191 N ND2 . ASN A 1 287 ? 43.188 -24.421 -12.570 1.00 23.20 ? 287 ASN A ND2 1 ATOM 2192 N N . ILE A 1 288 ? 40.074 -27.701 -10.871 1.00 22.65 ? 288 ILE A N 1 ATOM 2193 C CA . ILE A 1 288 ? 39.044 -27.497 -9.840 1.00 23.64 ? 288 ILE A CA 1 ATOM 2194 C C . ILE A 1 288 ? 39.629 -27.357 -8.421 1.00 23.59 ? 288 ILE A C 1 ATOM 2195 O O . ILE A 1 288 ? 39.228 -26.471 -7.673 1.00 24.62 ? 288 ILE A O 1 ATOM 2196 C CB . ILE A 1 288 ? 37.986 -28.622 -9.887 1.00 23.86 ? 288 ILE A CB 1 ATOM 2197 C CG1 . ILE A 1 288 ? 37.183 -28.535 -11.193 1.00 24.91 ? 288 ILE A CG1 1 ATOM 2198 C CG2 . ILE A 1 288 ? 37.010 -28.512 -8.723 1.00 24.51 ? 288 ILE A CG2 1 ATOM 2199 C CD1 . ILE A 1 288 ? 36.633 -29.863 -11.663 1.00 25.10 ? 288 ILE A CD1 1 ATOM 2200 N N . ASP A 1 289 ? 40.559 -28.231 -8.048 1.00 22.87 ? 289 ASP A N 1 ATOM 2201 C CA . ASP A 1 289 ? 41.078 -28.263 -6.674 1.00 22.89 ? 289 ASP A CA 1 ATOM 2202 C C . ASP A 1 289 ? 42.370 -29.072 -6.636 1.00 22.04 ? 289 ASP A C 1 ATOM 2203 O O . ASP A 1 289 ? 42.392 -30.270 -6.949 1.00 21.30 ? 289 ASP A O 1 ATOM 2204 C CB . ASP A 1 289 ? 40.034 -28.889 -5.725 1.00 23.21 ? 289 ASP A CB 1 ATOM 2205 C CG . ASP A 1 289 ? 40.367 -28.693 -4.229 1.00 23.66 ? 289 ASP A CG 1 ATOM 2206 O OD1 . ASP A 1 289 ? 41.537 -28.487 -3.854 1.00 23.75 ? 289 ASP A OD1 1 ATOM 2207 O OD2 . ASP A 1 289 ? 39.424 -28.760 -3.416 1.00 24.34 ? 289 ASP A OD2 1 ATOM 2208 N N . SER A 1 290 ? 43.438 -28.407 -6.228 1.00 22.55 ? 290 SER A N 1 ATOM 2209 C CA . SER A 1 290 ? 44.762 -29.009 -6.159 1.00 22.48 ? 290 SER A CA 1 ATOM 2210 C C . SER A 1 290 ? 44.892 -30.033 -5.048 1.00 22.25 ? 290 SER A C 1 ATOM 2211 O O . SER A 1 290 ? 45.859 -30.772 -5.032 1.00 22.71 ? 290 SER A O 1 ATOM 2212 C CB . SER A 1 290 ? 45.799 -27.922 -5.921 1.00 23.72 ? 290 SER A CB 1 ATOM 2213 O OG . SER A 1 290 ? 45.588 -27.338 -4.642 1.00 25.01 ? 290 SER A OG 1 ATOM 2214 N N . ARG A 1 291 ? 43.945 -30.060 -4.112 1.00 22.06 ? 291 ARG A N 1 ATOM 2215 C CA . ARG A 1 291 ? 43.962 -31.022 -3.020 1.00 21.94 ? 291 ARG A CA 1 ATOM 2216 C C . ARG A 1 291 ? 42.935 -32.139 -3.215 1.00 21.46 ? 291 ARG A C 1 ATOM 2217 O O . ARG A 1 291 ? 42.622 -32.863 -2.274 1.00 21.64 ? 291 ARG A O 1 ATOM 2218 C CB . ARG A 1 291 ? 43.721 -30.316 -1.682 1.00 22.50 ? 291 ARG A CB 1 ATOM 2219 C CG . ARG A 1 291 ? 44.825 -29.340 -1.302 1.00 23.41 ? 291 ARG A CG 1 ATOM 2220 C CD . ARG A 1 291 ? 44.569 -28.621 0.026 1.00 24.39 ? 291 ARG A CD 1 ATOM 2221 N NE . ARG A 1 291 ? 44.416 -29.544 1.151 1.00 24.14 ? 291 ARG A NE 1 ATOM 2222 C CZ . ARG A 1 291 ? 43.249 -29.955 1.639 1.00 23.68 ? 291 ARG A CZ 1 ATOM 2223 N NH1 . ARG A 1 291 ? 42.103 -29.522 1.129 1.00 23.53 ? 291 ARG A NH1 1 ATOM 2224 N NH2 . ARG A 1 291 ? 43.224 -30.799 2.655 1.00 23.72 ? 291 ARG A NH2 1 ATOM 2225 N N . ALA A 1 292 ? 42.424 -32.294 -4.434 1.00 21.13 ? 292 ALA A N 1 ATOM 2226 C CA . ALA A 1 292 ? 41.531 -33.408 -4.746 1.00 20.93 ? 292 ALA A CA 1 ATOM 2227 C C . ALA A 1 292 ? 42.249 -34.712 -4.486 1.00 20.93 ? 292 ALA A C 1 ATOM 2228 O O . ALA A 1 292 ? 43.454 -34.797 -4.675 1.00 20.83 ? 292 ALA A O 1 ATOM 2229 C CB . ALA A 1 292 ? 41.084 -33.353 -6.193 1.00 20.99 ? 292 ALA A CB 1 ATOM 2230 N N . VAL A 1 293 ? 41.500 -35.727 -4.063 1.00 21.06 ? 293 VAL A N 1 ATOM 2231 C CA . VAL A 1 293 ? 42.080 -37.017 -3.743 1.00 21.52 ? 293 VAL A CA 1 ATOM 2232 C C . VAL A 1 293 ? 41.295 -38.163 -4.367 1.00 22.00 ? 293 VAL A C 1 ATOM 2233 O O . VAL A 1 293 ? 40.183 -37.975 -4.871 1.00 22.27 ? 293 VAL A O 1 ATOM 2234 C CB . VAL A 1 293 ? 42.195 -37.205 -2.210 1.00 21.99 ? 293 VAL A CB 1 ATOM 2235 C CG1 . VAL A 1 293 ? 43.217 -36.224 -1.639 1.00 22.04 ? 293 VAL A CG1 1 ATOM 2236 C CG2 . VAL A 1 293 ? 40.849 -37.033 -1.531 1.00 21.98 ? 293 VAL A CG2 1 ATOM 2237 N N . GLY A 1 294 ? 41.905 -39.340 -4.333 1.00 22.65 ? 294 GLY A N 1 ATOM 2238 C CA . GLY A 1 294 ? 41.425 -40.524 -5.016 1.00 23.78 ? 294 GLY A CA 1 ATOM 2239 C C . GLY A 1 294 ? 42.265 -40.744 -6.262 1.00 24.18 ? 294 GLY A C 1 ATOM 2240 O O . GLY A 1 294 ? 43.481 -40.557 -6.233 1.00 24.01 ? 294 GLY A O 1 ATOM 2241 N N . LYS A 1 295 ? 41.611 -41.137 -7.351 1.00 24.95 ? 295 LYS A N 1 ATOM 2242 C CA . LYS A 1 295 ? 42.267 -41.332 -8.641 1.00 25.46 ? 295 LYS A CA 1 ATOM 2243 C C . LYS A 1 295 ? 41.800 -40.208 -9.534 1.00 24.81 ? 295 LYS A C 1 ATOM 2244 O O . LYS A 1 295 ? 40.673 -40.232 -10.017 1.00 26.09 ? 295 LYS A O 1 ATOM 2245 C CB . LYS A 1 295 ? 41.891 -42.695 -9.214 1.00 27.25 ? 295 LYS A CB 1 ATOM 2246 C CG . LYS A 1 295 ? 42.333 -43.837 -8.317 1.00 28.37 ? 295 LYS A CG 1 ATOM 2247 C CD . LYS A 1 295 ? 41.704 -45.164 -8.700 1.00 30.71 ? 295 LYS A CD 1 ATOM 2248 C CE . LYS A 1 295 ? 42.158 -46.256 -7.746 1.00 32.09 ? 295 LYS A CE 1 ATOM 2249 N NZ . LYS A 1 295 ? 41.983 -47.610 -8.323 1.00 35.01 ? 295 LYS A NZ 1 ATOM 2250 N N . CYS A 1 296 ? 42.651 -39.204 -9.715 1.00 23.74 ? 296 CYS A N 1 ATOM 2251 C CA . CYS A 1 296 ? 42.240 -37.928 -10.279 1.00 22.98 ? 296 CYS A CA 1 ATOM 2252 C C . CYS A 1 296 ? 43.040 -37.546 -11.523 1.00 22.84 ? 296 CYS A C 1 ATOM 2253 O O . CYS A 1 296 ? 44.169 -37.995 -11.687 1.00 22.60 ? 296 CYS A O 1 ATOM 2254 C CB . CYS A 1 296 ? 42.450 -36.824 -9.240 1.00 22.10 ? 296 CYS A CB 1 ATOM 2255 S SG . CYS A 1 296 ? 41.453 -36.972 -7.746 0.80 22.25 ? 296 CYS A SG 1 ATOM 2256 N N . PRO A 1 297 ? 42.454 -36.689 -12.387 1.00 22.87 ? 297 PRO A N 1 ATOM 2257 C CA . PRO A 1 297 ? 43.249 -35.957 -13.369 1.00 22.79 ? 297 PRO A CA 1 ATOM 2258 C C . PRO A 1 297 ? 44.285 -35.110 -12.637 1.00 22.35 ? 297 PRO A C 1 ATOM 2259 O O . PRO A 1 297 ? 44.065 -34.753 -11.488 1.00 22.25 ? 297 PRO A O 1 ATOM 2260 C CB . PRO A 1 297 ? 42.228 -35.055 -14.069 1.00 22.95 ? 297 PRO A CB 1 ATOM 2261 C CG . PRO A 1 297 ? 40.879 -35.637 -13.755 1.00 23.64 ? 297 PRO A CG 1 ATOM 2262 C CD . PRO A 1 297 ? 41.029 -36.302 -12.422 1.00 23.35 ? 297 PRO A CD 1 ATOM 2263 N N . ARG A 1 298 ? 45.410 -34.810 -13.276 1.00 22.58 ? 298 ARG A N 1 ATOM 2264 C CA . ARG A 1 298 ? 46.435 -33.991 -12.632 1.00 22.57 ? 298 ARG A CA 1 ATOM 2265 C C . ARG A 1 298 ? 45.960 -32.560 -12.548 1.00 21.35 ? 298 ARG A C 1 ATOM 2266 O O . ARG A 1 298 ? 45.393 -32.039 -13.505 1.00 20.97 ? 298 ARG A O 1 ATOM 2267 C CB . ARG A 1 298 ? 47.761 -34.037 -13.397 1.00 23.90 ? 298 ARG A CB 1 ATOM 2268 C CG . ARG A 1 298 ? 48.723 -35.102 -12.911 1.00 25.85 ? 298 ARG A CG 1 ATOM 2269 C CD . ARG A 1 298 ? 48.259 -36.506 -13.194 1.00 27.60 ? 298 ARG A CD 1 ATOM 2270 N NE . ARG A 1 298 ? 47.739 -36.634 -14.557 1.00 29.13 ? 298 ARG A NE 1 ATOM 2271 C CZ . ARG A 1 298 ? 46.781 -37.495 -14.932 1.00 30.94 ? 298 ARG A CZ 1 ATOM 2272 N NH1 . ARG A 1 298 ? 46.211 -38.338 -14.054 1.00 30.81 ? 298 ARG A NH1 1 ATOM 2273 N NH2 . ARG A 1 298 ? 46.383 -37.503 -16.207 1.00 31.59 ? 298 ARG A NH2 1 ATOM 2274 N N . TYR A 1 299 ? 46.197 -31.925 -11.406 1.00 20.71 ? 299 TYR A N 1 ATOM 2275 C CA . TYR A 1 299 ? 45.851 -30.525 -11.248 1.00 20.51 ? 299 TYR A CA 1 ATOM 2276 C C . TYR A 1 299 ? 46.831 -29.661 -12.002 1.00 20.80 ? 299 TYR A C 1 ATOM 2277 O O . TYR A 1 299 ? 48.053 -29.806 -11.857 1.00 21.07 ? 299 TYR A O 1 ATOM 2278 C CB . TYR A 1 299 ? 45.831 -30.081 -9.788 1.00 20.69 ? 299 TYR A CB 1 ATOM 2279 C CG . TYR A 1 299 ? 45.482 -28.613 -9.638 1.00 21.15 ? 299 TYR A CG 1 ATOM 2280 C CD1 . TYR A 1 299 ? 44.167 -28.179 -9.735 1.00 21.36 ? 299 TYR A CD1 1 ATOM 2281 C CD2 . TYR A 1 299 ? 46.460 -27.672 -9.419 1.00 21.94 ? 299 TYR A CD2 1 ATOM 2282 C CE1 . TYR A 1 299 ? 43.839 -26.849 -9.618 1.00 22.21 ? 299 TYR A CE1 1 ATOM 2283 C CE2 . TYR A 1 299 ? 46.151 -26.327 -9.297 1.00 22.93 ? 299 TYR A CE2 1 ATOM 2284 C CZ . TYR A 1 299 ? 44.839 -25.924 -9.396 1.00 23.05 ? 299 TYR A CZ 1 ATOM 2285 O OH . TYR A 1 299 ? 44.534 -24.598 -9.274 1.00 24.29 ? 299 TYR A OH 1 ATOM 2286 N N . VAL A 1 300 ? 46.286 -28.758 -12.804 1.00 20.78 ? 300 VAL A N 1 ATOM 2287 C CA . VAL A 1 300 ? 47.074 -27.724 -13.451 1.00 21.23 ? 300 VAL A CA 1 ATOM 2288 C C . VAL A 1 300 ? 46.480 -26.345 -13.165 1.00 22.00 ? 300 VAL A C 1 ATOM 2289 O O . VAL A 1 300 ? 45.307 -26.226 -12.841 1.00 21.78 ? 300 VAL A O 1 ATOM 2290 C CB . VAL A 1 300 ? 47.145 -27.941 -14.969 1.00 21.04 ? 300 VAL A CB 1 ATOM 2291 C CG1 . VAL A 1 300 ? 47.688 -29.323 -15.277 1.00 20.71 ? 300 VAL A CG1 1 ATOM 2292 C CG2 . VAL A 1 300 ? 45.786 -27.725 -15.627 1.00 21.19 ? 300 VAL A CG2 1 ATOM 2293 N N . LYS A 1 301 ? 47.306 -25.319 -13.321 1.00 23.15 ? 301 LYS A N 1 ATOM 2294 C CA . LYS A 1 301 ? 46.931 -23.937 -13.030 1.00 24.78 ? 301 LYS A CA 1 ATOM 2295 C C . LYS A 1 301 ? 46.108 -23.298 -14.131 1.00 25.06 ? 301 LYS A C 1 ATOM 2296 O O . LYS A 1 301 ? 45.445 -22.307 -13.882 1.00 26.32 ? 301 LYS A O 1 ATOM 2297 C CB . LYS A 1 301 ? 48.181 -23.068 -12.850 1.00 26.46 ? 301 LYS A CB 1 ATOM 2298 C CG . LYS A 1 301 ? 48.957 -23.296 -11.564 1.00 27.49 ? 301 LYS A CG 1 ATOM 2299 C CD . LYS A 1 301 ? 50.229 -22.448 -11.511 1.00 29.65 ? 301 LYS A CD 1 ATOM 2300 C CE . LYS A 1 301 ? 51.010 -22.523 -12.825 1.00 29.94 ? 301 LYS A CE 1 ATOM 2301 N NZ . LYS A 1 301 ? 52.382 -21.925 -12.775 1.00 32.00 ? 301 LYS A NZ 1 ATOM 2302 N N . GLN A 1 302 ? 46.189 -23.830 -15.346 1.00 24.50 ? 302 GLN A N 1 ATOM 2303 C CA . GLN A 1 302 ? 45.469 -23.265 -16.483 1.00 25.30 ? 302 GLN A CA 1 ATOM 2304 C C . GLN A 1 302 ? 44.009 -23.708 -16.419 1.00 25.74 ? 302 GLN A C 1 ATOM 2305 O O . GLN A 1 302 ? 43.716 -24.856 -16.033 1.00 24.59 ? 302 GLN A O 1 ATOM 2306 C CB . GLN A 1 302 ? 46.088 -23.723 -17.817 1.00 24.86 ? 302 GLN A CB 1 ATOM 2307 C CG . GLN A 1 302 ? 47.571 -23.385 -18.035 1.00 25.00 ? 302 GLN A CG 1 ATOM 2308 C CD . GLN A 1 302 ? 48.525 -24.524 -17.630 1.00 24.12 ? 302 GLN A CD 1 ATOM 2309 O OE1 . GLN A 1 302 ? 48.270 -25.251 -16.679 1.00 23.49 ? 302 GLN A OE1 1 ATOM 2310 N NE2 . GLN A 1 302 ? 49.630 -24.665 -18.350 1.00 24.03 ? 302 GLN A NE2 1 ATOM 2311 N N . ARG A 1 303 ? 43.099 -22.811 -16.809 1.00 27.54 ? 303 ARG A N 1 ATOM 2312 C CA . ARG A 1 303 ? 41.675 -23.125 -16.854 1.00 28.63 ? 303 ARG A CA 1 ATOM 2313 C C . ARG A 1 303 ? 41.334 -23.946 -18.091 1.00 28.09 ? 303 ARG A C 1 ATOM 2314 O O . ARG A 1 303 ? 40.361 -24.699 -18.087 1.00 27.97 ? 303 ARG A O 1 ATOM 2315 C CB . ARG A 1 303 ? 40.810 -21.853 -16.814 1.00 31.88 ? 303 ARG A CB 1 ATOM 2316 C CG . ARG A 1 303 ? 40.914 -20.969 -18.045 1.00 34.34 ? 303 ARG A CG 1 ATOM 2317 C CD . ARG A 1 303 ? 39.782 -19.943 -18.145 1.00 37.98 ? 303 ARG A CD 1 ATOM 2318 N NE . ARG A 1 303 ? 38.589 -20.473 -18.828 1.00 39.63 ? 303 ARG A NE 1 ATOM 2319 C CZ . ARG A 1 303 ? 37.424 -20.778 -18.246 1.00 41.66 ? 303 ARG A CZ 1 ATOM 2320 N NH1 . ARG A 1 303 ? 37.219 -20.609 -16.934 1.00 41.84 ? 303 ARG A NH1 1 ATOM 2321 N NH2 . ARG A 1 303 ? 36.432 -21.262 -18.995 1.00 43.52 ? 303 ARG A NH2 1 ATOM 2322 N N . SER A 1 304 ? 42.137 -23.806 -19.144 1.00 27.39 ? 304 SER A N 1 ATOM 2323 C CA . SER A 1 304 ? 41.819 -24.417 -20.427 1.00 27.33 ? 304 SER A CA 1 ATOM 2324 C C . SER A 1 304 ? 43.053 -24.635 -21.298 1.00 26.41 ? 304 SER A C 1 ATOM 2325 O O . SER A 1 304 ? 43.921 -23.760 -21.405 1.00 26.42 ? 304 SER A O 1 ATOM 2326 C CB . SER A 1 304 ? 40.822 -23.527 -21.183 1.00 29.14 ? 304 SER A CB 1 ATOM 2327 O OG . SER A 1 304 ? 40.722 -23.910 -22.543 1.00 29.53 ? 304 SER A OG 1 ATOM 2328 N N . LEU A 1 305 ? 43.104 -25.799 -21.938 1.00 25.59 ? 305 LEU A N 1 ATOM 2329 C CA . LEU A 1 305 ? 44.175 -26.139 -22.877 1.00 25.01 ? 305 LEU A CA 1 ATOM 2330 C C . LEU A 1 305 ? 43.564 -26.948 -24.021 1.00 25.54 ? 305 LEU A C 1 ATOM 2331 O O . LEU A 1 305 ? 43.342 -28.157 -23.899 1.00 25.15 ? 305 LEU A O 1 ATOM 2332 C CB . LEU A 1 305 ? 45.269 -26.953 -22.182 1.00 23.72 ? 305 LEU A CB 1 ATOM 2333 C CG . LEU A 1 305 ? 46.114 -26.269 -21.104 1.00 23.33 ? 305 LEU A CG 1 ATOM 2334 C CD1 . LEU A 1 305 ? 46.945 -27.300 -20.348 1.00 22.35 ? 305 LEU A CD1 1 ATOM 2335 C CD2 . LEU A 1 305 ? 47.007 -25.171 -21.673 1.00 23.70 ? 305 LEU A CD2 1 ATOM 2336 N N . LEU A 1 306 ? 43.273 -26.268 -25.124 1.00 26.57 ? 306 LEU A N 1 ATOM 2337 C CA . LEU A 1 306 ? 42.568 -26.888 -26.240 1.00 27.59 ? 306 LEU A CA 1 ATOM 2338 C C . LEU A 1 306 ? 43.514 -27.692 -27.126 1.00 27.12 ? 306 LEU A C 1 ATOM 2339 O O . LEU A 1 306 ? 44.591 -27.229 -27.491 1.00 26.48 ? 306 LEU A O 1 ATOM 2340 C CB . LEU A 1 306 ? 41.823 -25.837 -27.060 1.00 29.18 ? 306 LEU A CB 1 ATOM 2341 C CG . LEU A 1 306 ? 40.751 -25.066 -26.286 1.00 30.15 ? 306 LEU A CG 1 ATOM 2342 C CD1 . LEU A 1 306 ? 40.075 -24.046 -27.191 1.00 32.17 ? 306 LEU A CD1 1 ATOM 2343 C CD2 . LEU A 1 306 ? 39.712 -26.005 -25.686 1.00 30.57 ? 306 LEU A CD2 1 ATOM 2344 N N . LEU A 1 307 ? 43.078 -28.904 -27.454 1.00 27.64 ? 307 LEU A N 1 ATOM 2345 C CA . LEU A 1 307 ? 43.821 -29.830 -28.293 1.00 27.59 ? 307 LEU A CA 1 ATOM 2346 C C . LEU A 1 307 ? 43.181 -29.885 -29.678 1.00 29.42 ? 307 LEU A C 1 ATOM 2347 O O . LEU A 1 307 ? 42.003 -30.225 -29.805 1.00 30.91 ? 307 LEU A O 1 ATOM 2348 C CB . LEU A 1 307 ? 43.759 -31.204 -27.660 1.00 27.33 ? 307 LEU A CB 1 ATOM 2349 C CG . LEU A 1 307 ? 44.515 -32.323 -28.353 1.00 27.72 ? 307 LEU A CG 1 ATOM 2350 C CD1 . LEU A 1 307 ? 46.009 -32.179 -28.118 1.00 26.46 ? 307 LEU A CD1 1 ATOM 2351 C CD2 . LEU A 1 307 ? 44.005 -33.659 -27.837 1.00 28.30 ? 307 LEU A CD2 1 ATOM 2352 N N . ALA A 1 308 ? 43.949 -29.550 -30.712 1.00 29.54 ? 308 ALA A N 1 ATOM 2353 C CA . ALA A 1 308 ? 43.445 -29.583 -32.083 1.00 31.25 ? 308 ALA A CA 1 ATOM 2354 C C . ALA A 1 308 ? 43.018 -30.995 -32.445 1.00 32.38 ? 308 ALA A C 1 ATOM 2355 O O . ALA A 1 308 ? 43.724 -31.957 -32.132 1.00 31.73 ? 308 ALA A O 1 ATOM 2356 C CB . ALA A 1 308 ? 44.504 -29.100 -33.057 1.00 31.08 ? 308 ALA A CB 1 ATOM 2357 N N . THR A 1 309 ? 41.856 -31.112 -33.082 1.00 34.28 ? 309 THR A N 1 ATOM 2358 C CA . THR A 1 309 ? 41.374 -32.391 -33.600 1.00 36.10 ? 309 THR A CA 1 ATOM 2359 C C . THR A 1 309 ? 40.999 -32.263 -35.082 1.00 38.50 ? 309 THR A C 1 ATOM 2360 O O . THR A 1 309 ? 40.261 -33.082 -35.636 1.00 40.84 ? 309 THR A O 1 ATOM 2361 C CB . THR A 1 309 ? 40.175 -32.898 -32.786 1.00 36.94 ? 309 THR A CB 1 ATOM 2362 O OG1 . THR A 1 309 ? 39.167 -31.888 -32.737 1.00 37.89 ? 309 THR A OG1 1 ATOM 2363 C CG2 . THR A 1 309 ? 40.607 -33.232 -31.370 1.00 34.82 ? 309 THR A CG2 1 ATOM 2364 N N . GLY A 1 310 ? 41.536 -31.232 -35.723 1.00 38.03 ? 310 GLY A N 1 ATOM 2365 C CA . GLY A 1 310 ? 41.306 -31.002 -37.134 1.00 40.19 ? 310 GLY A CA 1 ATOM 2366 C C . GLY A 1 310 ? 42.449 -30.191 -37.685 1.00 38.98 ? 310 GLY A C 1 ATOM 2367 O O . GLY A 1 310 ? 43.261 -29.642 -36.926 1.00 36.61 ? 310 GLY A O 1 ATOM 2368 N N . MET A 1 311 ? 42.504 -30.119 -39.010 1.00 40.76 ? 311 MET A N 1 ATOM 2369 C CA . MET A 1 311 ? 43.508 -29.332 -39.706 1.00 40.08 ? 311 MET A CA 1 ATOM 2370 C C . MET A 1 311 ? 43.339 -27.854 -39.405 1.00 39.79 ? 311 MET A C 1 ATOM 2371 O O . MET A 1 311 ? 42.345 -27.444 -38.812 1.00 40.34 ? 311 MET A O 1 ATOM 2372 C CB . MET A 1 311 ? 43.401 -29.558 -41.212 1.00 42.33 ? 311 MET A CB 1 ATOM 2373 C CG . MET A 1 311 ? 42.119 -29.031 -41.834 1.00 44.96 ? 311 MET A CG 1 ATOM 2374 S SD . MET A 1 311 ? 42.064 -29.334 -43.600 1.00 47.79 ? 311 MET A SD 1 ATOM 2375 C CE . MET A 1 311 ? 41.764 -31.098 -43.638 1.00 49.23 ? 311 MET A CE 1 ATOM 2376 N N . LYS A 1 312 ? 44.320 -27.063 -39.821 1.00 39.43 ? 312 LYS A N 1 ATOM 2377 C CA . LYS A 1 312 ? 44.246 -25.615 -39.714 1.00 39.96 ? 312 LYS A CA 1 ATOM 2378 C C . LYS A 1 312 ? 43.115 -25.070 -40.590 1.00 42.88 ? 312 LYS A C 1 ATOM 2379 O O . LYS A 1 312 ? 42.904 -25.537 -41.710 1.00 44.73 ? 312 LYS A O 1 ATOM 2380 C CB . LYS A 1 312 ? 45.564 -24.985 -40.153 1.00 39.33 ? 312 LYS A CB 1 ATOM 2381 C CG . LYS A 1 312 ? 45.608 -23.476 -39.989 1.00 39.89 ? 312 LYS A CG 1 ATOM 2382 C CD . LYS A 1 312 ? 46.766 -22.892 -40.761 1.00 40.15 ? 312 LYS A CD 1 ATOM 2383 C CE . LYS A 1 312 ? 46.838 -21.386 -40.587 1.00 41.02 ? 312 LYS A CE 1 ATOM 2384 N NZ . LYS A 1 312 ? 48.188 -20.913 -41.007 1.00 40.84 ? 312 LYS A NZ 1 ATOM 2385 N N . ASN A 1 313 ? 42.400 -24.077 -40.074 1.00 43.62 ? 313 ASN A N 1 ATOM 2386 C CA . ASN A 1 313 ? 41.284 -23.495 -40.796 1.00 46.73 ? 313 ASN A CA 1 ATOM 2387 C C . ASN A 1 313 ? 41.764 -22.340 -41.668 1.00 47.77 ? 313 ASN A C 1 ATOM 2388 O O . ASN A 1 313 ? 42.290 -21.340 -41.162 1.00 46.65 ? 313 ASN A O 1 ATOM 2389 C CB . ASN A 1 313 ? 40.197 -23.024 -39.833 1.00 47.43 ? 313 ASN A CB 1 ATOM 2390 C CG . ASN A 1 313 ? 38.896 -22.701 -40.547 1.00 51.05 ? 313 ASN A CG 1 ATOM 2391 O OD1 . ASN A 1 313 ? 38.386 -23.517 -41.311 1.00 52.96 ? 313 ASN A OD1 1 ATOM 2392 N ND2 . ASN A 1 313 ? 38.358 -21.508 -40.308 1.00 52.26 ? 313 ASN A ND2 1 ATOM 2393 N N . VAL A 1 314 ? 41.585 -22.502 -42.980 1.00 50.11 ? 314 VAL A N 1 ATOM 2394 C CA . VAL A 1 314 ? 42.030 -21.525 -43.968 1.00 51.35 ? 314 VAL A CA 1 ATOM 2395 C C . VAL A 1 314 ? 40.837 -21.159 -44.844 1.00 55.20 ? 314 VAL A C 1 ATOM 2396 O O . VAL A 1 314 ? 40.694 -21.676 -45.956 1.00 57.04 ? 314 VAL A O 1 ATOM 2397 C CB . VAL A 1 314 ? 43.168 -22.082 -44.847 1.00 50.46 ? 314 VAL A CB 1 ATOM 2398 C CG1 . VAL A 1 314 ? 43.825 -20.958 -45.634 1.00 51.11 ? 314 VAL A CG1 1 ATOM 2399 C CG2 . VAL A 1 314 ? 44.202 -22.804 -44.000 1.00 47.44 ? 314 VAL A CG2 1 ATOM 2400 N N . PRO A 1 315 ? 39.977 -20.253 -44.351 1.00 56.81 ? 315 PRO A N 1 ATOM 2401 C CA . PRO A 1 315 ? 38.736 -19.959 -45.054 1.00 60.94 ? 315 PRO A CA 1 ATOM 2402 C C . PRO A 1 315 ? 38.934 -19.118 -46.319 1.00 63.33 ? 315 PRO A C 1 ATOM 2403 O O . PRO A 1 315 ? 40.040 -18.643 -46.581 1.00 61.77 ? 315 PRO A O 1 ATOM 2404 C CB . PRO A 1 315 ? 37.911 -19.178 -44.017 1.00 61.59 ? 315 PRO A CB 1 ATOM 2405 C CG . PRO A 1 315 ? 38.826 -18.872 -42.878 1.00 58.07 ? 315 PRO A CG 1 ATOM 2406 C CD . PRO A 1 315 ? 40.206 -19.321 -43.236 1.00 55.37 ? 315 PRO A CD 1 ATOM 2407 N N . GLU A 1 316 ? 37.857 -18.948 -47.084 1.00 67.54 ? 316 GLU A N 1 ATOM 2408 C CA . GLU A 1 316 ? 37.864 -18.110 -48.295 1.00 70.57 ? 316 GLU A CA 1 ATOM 2409 C C . GLU A 1 316 ? 38.115 -16.627 -47.993 1.00 70.83 ? 316 GLU A C 1 ATOM 2410 O O . GLU A 1 316 ? 38.573 -15.868 -48.851 1.00 72.01 ? 316 GLU A O 1 ATOM 2411 C CB . GLU A 1 316 ? 36.533 -18.251 -49.052 1.00 75.34 ? 316 GLU A CB 1 ATOM 2412 C CG . GLU A 1 316 ? 36.525 -19.336 -50.122 1.00 76.81 ? 316 GLU A CG 1 ATOM 2413 C CD . GLU A 1 316 ? 37.109 -18.869 -51.449 1.00 78.17 ? 316 GLU A CD 1 ATOM 2414 O OE1 . GLU A 1 316 ? 36.410 -18.161 -52.209 1.00 81.92 ? 316 GLU A OE1 1 ATOM 2415 O OE2 . GLU A 1 316 ? 38.271 -19.222 -51.741 1.00 75.66 ? 316 GLU A OE2 1 ATOM 2416 N N . ILE A 1 317 ? 37.852 -16.141 -46.893 1.00 70.26 ? 317 ILE A N 1 ATOM 2417 N N . GLY B 2 1 ? 51.781 -25.326 -42.413 1.00 61.56 ? 1 GLY B N 1 ATOM 2418 C CA . GLY B 2 1 ? 52.622 -26.423 -41.853 1.00 61.20 ? 1 GLY B CA 1 ATOM 2419 C C . GLY B 2 1 ? 53.888 -26.681 -42.652 1.00 63.39 ? 1 GLY B C 1 ATOM 2420 O O . GLY B 2 1 ? 54.222 -25.934 -43.572 1.00 65.37 ? 1 GLY B O 1 ATOM 2421 N N . LEU B 2 2 ? 54.569 -27.766 -42.303 1.00 63.32 ? 2 LEU B N 1 ATOM 2422 C CA . LEU B 2 2 ? 55.871 -28.095 -42.866 1.00 66.03 ? 2 LEU B CA 1 ATOM 2423 C C . LEU B 2 2 ? 55.824 -28.494 -44.335 1.00 67.08 ? 2 LEU B C 1 ATOM 2424 O O . LEU B 2 2 ? 56.784 -28.256 -45.070 1.00 70.11 ? 2 LEU B O 1 ATOM 2425 C CB . LEU B 2 2 ? 56.517 -29.226 -42.066 1.00 65.95 ? 2 LEU B CB 1 ATOM 2426 C CG . LEU B 2 2 ? 56.844 -28.926 -40.605 1.00 65.65 ? 2 LEU B CG 1 ATOM 2427 C CD1 . LEU B 2 2 ? 57.260 -30.198 -39.885 1.00 65.32 ? 2 LEU B CD1 1 ATOM 2428 C CD2 . LEU B 2 2 ? 57.934 -27.872 -40.509 1.00 68.85 ? 2 LEU B CD2 1 ATOM 2429 N N . PHE B 2 3 ? 54.716 -29.093 -44.761 1.00 64.99 ? 3 PHE B N 1 ATOM 2430 C CA . PHE B 2 3 ? 54.612 -29.637 -46.118 1.00 66.08 ? 3 PHE B CA 1 ATOM 2431 C C . PHE B 2 3 ? 54.065 -28.643 -47.142 1.00 66.71 ? 3 PHE B C 1 ATOM 2432 O O . PHE B 2 3 ? 53.967 -28.965 -48.324 1.00 67.93 ? 3 PHE B O 1 ATOM 2433 C CB . PHE B 2 3 ? 53.816 -30.942 -46.095 1.00 64.26 ? 3 PHE B CB 1 ATOM 2434 C CG . PHE B 2 3 ? 54.471 -32.005 -45.262 1.00 64.44 ? 3 PHE B CG 1 ATOM 2435 C CD1 . PHE B 2 3 ? 54.293 -32.035 -43.889 1.00 62.69 ? 3 PHE B CD1 1 ATOM 2436 C CD2 . PHE B 2 3 ? 55.315 -32.936 -45.845 1.00 66.76 ? 3 PHE B CD2 1 ATOM 2437 C CE1 . PHE B 2 3 ? 54.922 -32.992 -43.117 1.00 63.16 ? 3 PHE B CE1 1 ATOM 2438 C CE2 . PHE B 2 3 ? 55.943 -33.900 -45.081 1.00 67.33 ? 3 PHE B CE2 1 ATOM 2439 C CZ . PHE B 2 3 ? 55.750 -33.927 -43.715 1.00 65.47 ? 3 PHE B CZ 1 ATOM 2440 N N . GLY B 2 4 ? 53.733 -27.434 -46.693 1.00 66.44 ? 4 GLY B N 1 ATOM 2441 C CA . GLY B 2 4 ? 53.476 -26.307 -47.600 1.00 67.85 ? 4 GLY B CA 1 ATOM 2442 C C . GLY B 2 4 ? 52.278 -26.439 -48.524 1.00 66.72 ? 4 GLY B C 1 ATOM 2443 O O . GLY B 2 4 ? 52.246 -25.820 -49.587 1.00 68.40 ? 4 GLY B O 1 ATOM 2444 N N . ALA B 2 5 ? 51.290 -27.231 -48.121 1.00 64.24 ? 5 ALA B N 1 ATOM 2445 C CA . ALA B 2 5 ? 50.095 -27.439 -48.929 1.00 63.50 ? 5 ALA B CA 1 ATOM 2446 C C . ALA B 2 5 ? 48.927 -26.641 -48.354 1.00 62.20 ? 5 ALA B C 1 ATOM 2447 O O . ALA B 2 5 ? 48.413 -25.730 -49.008 1.00 62.94 ? 5 ALA B O 1 ATOM 2448 C CB . ALA B 2 5 ? 49.764 -28.923 -49.013 1.00 62.61 ? 5 ALA B CB 1 ATOM 2449 N N . ILE B 2 6 ? 48.525 -26.980 -47.130 1.00 60.60 ? 6 ILE B N 1 ATOM 2450 C CA . ILE B 2 6 ? 47.457 -26.265 -46.429 1.00 59.82 ? 6 ILE B CA 1 ATOM 2451 C C . ILE B 2 6 ? 48.000 -24.937 -45.921 1.00 61.08 ? 6 ILE B C 1 ATOM 2452 O O . ILE B 2 6 ? 49.009 -24.907 -45.216 1.00 61.50 ? 6 ILE B O 1 ATOM 2453 C CB . ILE B 2 6 ? 46.905 -27.078 -45.244 1.00 58.12 ? 6 ILE B CB 1 ATOM 2454 C CG1 . ILE B 2 6 ? 46.245 -28.361 -45.754 1.00 57.64 ? 6 ILE B CG1 1 ATOM 2455 C CG2 . ILE B 2 6 ? 45.904 -26.254 -44.441 1.00 57.81 ? 6 ILE B CG2 1 ATOM 2456 C CD1 . ILE B 2 6 ? 45.950 -29.368 -44.664 1.00 56.60 ? 6 ILE B CD1 1 ATOM 2457 N N . ALA B 2 7 ? 47.313 -23.851 -46.276 1.00 62.15 ? 7 ALA B N 1 ATOM 2458 C CA . ALA B 2 7 ? 47.819 -22.495 -46.076 1.00 64.09 ? 7 ALA B CA 1 ATOM 2459 C C . ALA B 2 7 ? 49.180 -22.361 -46.754 1.00 66.09 ? 7 ALA B C 1 ATOM 2460 O O . ALA B 2 7 ? 50.097 -21.734 -46.223 1.00 67.63 ? 7 ALA B O 1 ATOM 2461 C CB . ALA B 2 7 ? 47.899 -22.153 -44.594 1.00 63.72 ? 7 ALA B CB 1 ATOM 2462 N N . GLY B 2 8 ? 49.287 -22.970 -47.934 1.00 66.55 ? 8 GLY B N 1 ATOM 2463 C CA . GLY B 2 8 ? 50.504 -22.961 -48.735 1.00 69.00 ? 8 GLY B CA 1 ATOM 2464 C C . GLY B 2 8 ? 50.136 -22.791 -50.194 1.00 70.44 ? 8 GLY B C 1 ATOM 2465 O O . GLY B 2 8 ? 49.404 -21.860 -50.538 1.00 71.12 ? 8 GLY B O 1 ATOM 2466 N N . PHE B 2 9 ? 50.615 -23.690 -51.054 1.00 71.28 ? 9 PHE B N 1 ATOM 2467 C CA . PHE B 2 9 ? 50.357 -23.566 -52.492 1.00 72.99 ? 9 PHE B CA 1 ATOM 2468 C C . PHE B 2 9 ? 48.874 -23.736 -52.830 1.00 71.37 ? 9 PHE B C 1 ATOM 2469 O O . PHE B 2 9 ? 48.418 -23.239 -53.853 1.00 72.70 ? 9 PHE B O 1 ATOM 2470 C CB . PHE B 2 9 ? 51.260 -24.491 -53.327 1.00 74.65 ? 9 PHE B CB 1 ATOM 2471 C CG . PHE B 2 9 ? 50.828 -25.929 -53.350 1.00 72.87 ? 9 PHE B CG 1 ATOM 2472 C CD1 . PHE B 2 9 ? 49.942 -26.387 -54.311 1.00 72.79 ? 9 PHE B CD1 1 ATOM 2473 C CD2 . PHE B 2 9 ? 51.342 -26.833 -52.441 1.00 71.88 ? 9 PHE B CD2 1 ATOM 2474 C CE1 . PHE B 2 9 ? 49.557 -27.717 -54.339 1.00 71.71 ? 9 PHE B CE1 1 ATOM 2475 C CE2 . PHE B 2 9 ? 50.962 -28.163 -52.464 1.00 70.73 ? 9 PHE B CE2 1 ATOM 2476 C CZ . PHE B 2 9 ? 50.067 -28.606 -53.416 1.00 70.69 ? 9 PHE B CZ 1 ATOM 2477 N N . ILE B 2 10 ? 48.127 -24.434 -51.976 1.00 69.00 ? 10 ILE B N 1 ATOM 2478 C CA . ILE B 2 10 ? 46.670 -24.370 -52.038 1.00 68.05 ? 10 ILE B CA 1 ATOM 2479 C C . ILE B 2 10 ? 46.244 -23.099 -51.309 1.00 68.36 ? 10 ILE B C 1 ATOM 2480 O O . ILE B 2 10 ? 46.464 -22.962 -50.101 1.00 67.53 ? 10 ILE B O 1 ATOM 2481 C CB . ILE B 2 10 ? 45.966 -25.589 -51.403 1.00 66.02 ? 10 ILE B CB 1 ATOM 2482 C CG1 . ILE B 2 10 ? 46.318 -26.878 -52.155 1.00 66.37 ? 10 ILE B CG1 1 ATOM 2483 C CG2 . ILE B 2 10 ? 44.456 -25.386 -51.413 1.00 65.63 ? 10 ILE B CG2 1 ATOM 2484 C CD1 . ILE B 2 10 ? 47.477 -27.639 -51.560 1.00 66.22 ? 10 ILE B CD1 1 ATOM 2485 N N . GLU B 2 11 ? 45.641 -22.182 -52.063 1.00 69.94 ? 11 GLU B N 1 ATOM 2486 C CA . GLU B 2 11 ? 45.224 -20.866 -51.570 1.00 71.01 ? 11 GLU B CA 1 ATOM 2487 C C . GLU B 2 11 ? 44.380 -20.950 -50.294 1.00 69.24 ? 11 GLU B C 1 ATOM 2488 O O . GLU B 2 11 ? 44.666 -20.269 -49.307 1.00 69.51 ? 11 GLU B O 1 ATOM 2489 C CB . GLU B 2 11 ? 44.420 -20.151 -52.665 1.00 72.98 ? 11 GLU B CB 1 ATOM 2490 C CG . GLU B 2 11 ? 44.304 -18.640 -52.503 1.00 75.42 ? 11 GLU B CG 1 ATOM 2491 C CD . GLU B 2 11 ? 45.466 -17.891 -53.130 1.00 78.07 ? 11 GLU B CD 1 ATOM 2492 O OE1 . GLU B 2 11 ? 46.588 -17.954 -52.576 1.00 78.43 ? 11 GLU B OE1 1 ATOM 2493 O OE2 . GLU B 2 11 ? 45.249 -17.236 -54.170 1.00 80.30 ? 11 GLU B OE2 1 ATOM 2494 N N . ASN B 2 12 ? 43.341 -21.782 -50.328 1.00 67.82 ? 12 ASN B N 1 ATOM 2495 C CA . ASN B 2 12 ? 42.388 -21.878 -49.221 1.00 66.84 ? 12 ASN B CA 1 ATOM 2496 C C . ASN B 2 12 ? 41.541 -23.146 -49.261 1.00 65.54 ? 12 ASN B C 1 ATOM 2497 O O . ASN B 2 12 ? 41.564 -23.895 -50.236 1.00 65.54 ? 12 ASN B O 1 ATOM 2498 C CB . ASN B 2 12 ? 41.471 -20.653 -49.211 1.00 68.69 ? 12 ASN B CB 1 ATOM 2499 C CG . ASN B 2 12 ? 40.622 -20.552 -50.456 1.00 69.95 ? 12 ASN B CG 1 ATOM 2500 O OD1 . ASN B 2 12 ? 41.007 -19.900 -51.420 1.00 71.46 ? 12 ASN B OD1 1 ATOM 2501 N ND2 . ASN B 2 12 ? 39.468 -21.210 -50.450 1.00 69.78 ? 12 ASN B ND2 1 ATOM 2502 N N . GLY B 2 13 ? 40.792 -23.370 -48.188 1.00 64.96 ? 13 GLY B N 1 ATOM 2503 C CA . GLY B 2 13 ? 39.914 -24.526 -48.077 1.00 64.48 ? 13 GLY B CA 1 ATOM 2504 C C . GLY B 2 13 ? 38.543 -24.273 -48.663 1.00 66.24 ? 13 GLY B C 1 ATOM 2505 O O . GLY B 2 13 ? 38.172 -23.134 -48.941 1.00 67.64 ? 13 GLY B O 1 ATOM 2506 N N . TRP B 2 14 ? 37.789 -25.351 -48.843 1.00 66.58 ? 14 TRP B N 1 ATOM 2507 C CA . TRP B 2 14 ? 36.440 -25.282 -49.371 1.00 68.76 ? 14 TRP B CA 1 ATOM 2508 C C . TRP B 2 14 ? 35.428 -25.428 -48.246 1.00 69.88 ? 14 TRP B C 1 ATOM 2509 O O . TRP B 2 14 ? 35.457 -26.407 -47.506 1.00 69.19 ? 14 TRP B O 1 ATOM 2510 C CB . TRP B 2 14 ? 36.230 -26.383 -50.406 1.00 69.26 ? 14 TRP B CB 1 ATOM 2511 C CG . TRP B 2 14 ? 37.168 -26.294 -51.576 1.00 68.85 ? 14 TRP B CG 1 ATOM 2512 C CD1 . TRP B 2 14 ? 37.715 -25.159 -52.107 1.00 69.06 ? 14 TRP B CD1 1 ATOM 2513 C CD2 . TRP B 2 14 ? 37.647 -27.380 -52.376 1.00 68.69 ? 14 TRP B CD2 1 ATOM 2514 N NE1 . TRP B 2 14 ? 38.514 -25.473 -53.178 1.00 69.03 ? 14 TRP B NE1 1 ATOM 2515 C CE2 . TRP B 2 14 ? 38.489 -26.830 -53.368 1.00 68.81 ? 14 TRP B CE2 1 ATOM 2516 C CE3 . TRP B 2 14 ? 37.452 -28.767 -52.349 1.00 68.85 ? 14 TRP B CE3 1 ATOM 2517 C CZ2 . TRP B 2 14 ? 39.137 -27.618 -54.326 1.00 69.07 ? 14 TRP B CZ2 1 ATOM 2518 C CZ3 . TRP B 2 14 ? 38.097 -29.551 -53.305 1.00 69.15 ? 14 TRP B CZ3 1 ATOM 2519 C CH2 . TRP B 2 14 ? 38.926 -28.971 -54.280 1.00 69.23 ? 14 TRP B CH2 1 ATOM 2520 N N . GLU B 2 15 ? 34.539 -24.447 -48.120 1.00 72.12 ? 15 GLU B N 1 ATOM 2521 C CA . GLU B 2 15 ? 33.487 -24.469 -47.103 1.00 74.08 ? 15 GLU B CA 1 ATOM 2522 C C . GLU B 2 15 ? 32.302 -25.330 -47.533 1.00 76.51 ? 15 GLU B C 1 ATOM 2523 O O . GLU B 2 15 ? 31.489 -25.732 -46.702 1.00 78.22 ? 15 GLU B O 1 ATOM 2524 C CB . GLU B 2 15 ? 33.026 -23.042 -46.780 1.00 76.07 ? 15 GLU B CB 1 ATOM 2525 C CG . GLU B 2 15 ? 34.133 -22.178 -46.184 1.00 74.59 ? 15 GLU B CG 1 ATOM 2526 C CD . GLU B 2 15 ? 33.704 -20.753 -45.869 1.00 77.07 ? 15 GLU B CD 1 ATOM 2527 O OE1 . GLU B 2 15 ? 32.499 -20.516 -45.631 1.00 79.94 ? 15 GLU B OE1 1 ATOM 2528 O OE2 . GLU B 2 15 ? 34.587 -19.868 -45.843 1.00 76.59 ? 15 GLU B OE2 1 ATOM 2529 N N . GLY B 2 16 ? 32.210 -25.608 -48.832 1.00 77.26 ? 16 GLY B N 1 ATOM 2530 C CA . GLY B 2 16 ? 31.156 -26.458 -49.383 1.00 79.79 ? 16 GLY B CA 1 ATOM 2531 C C . GLY B 2 16 ? 31.448 -27.943 -49.246 1.00 79.02 ? 16 GLY B C 1 ATOM 2532 O O . GLY B 2 16 ? 30.552 -28.773 -49.421 1.00 81.51 ? 16 GLY B O 1 ATOM 2533 N N . LEU B 2 17 ? 32.699 -28.281 -48.937 1.00 75.96 ? 17 LEU B N 1 ATOM 2534 C CA . LEU B 2 17 ? 33.098 -29.675 -48.775 1.00 75.29 ? 17 LEU B CA 1 ATOM 2535 C C . LEU B 2 17 ? 32.720 -30.178 -47.379 1.00 75.82 ? 17 LEU B C 1 ATOM 2536 O O . LEU B 2 17 ? 33.531 -30.148 -46.458 1.00 73.76 ? 17 LEU B O 1 ATOM 2537 C CB . LEU B 2 17 ? 34.603 -29.830 -49.020 1.00 72.25 ? 17 LEU B CB 1 ATOM 2538 C CG . LEU B 2 17 ? 35.141 -31.265 -49.035 1.00 71.73 ? 17 LEU B CG 1 ATOM 2539 C CD1 . LEU B 2 17 ? 34.584 -32.037 -50.226 1.00 73.99 ? 17 LEU B CD1 1 ATOM 2540 C CD2 . LEU B 2 17 ? 36.661 -31.256 -49.053 1.00 69.04 ? 17 LEU B CD2 1 ATOM 2541 N N . ILE B 2 18 ? 31.481 -30.646 -47.240 1.00 79.14 ? 18 ILE B N 1 ATOM 2542 C CA . ILE B 2 18 ? 30.976 -31.168 -45.961 1.00 80.47 ? 18 ILE B CA 1 ATOM 2543 C C . ILE B 2 18 ? 31.041 -32.698 -45.883 1.00 81.03 ? 18 ILE B C 1 ATOM 2544 O O . ILE B 2 18 ? 30.616 -33.293 -44.893 1.00 82.61 ? 18 ILE B O 1 ATOM 2545 C CB . ILE B 2 18 ? 29.533 -30.677 -45.655 1.00 84.61 ? 18 ILE B CB 1 ATOM 2546 C CG1 . ILE B 2 18 ? 28.576 -30.873 -46.842 1.00 88.03 ? 18 ILE B CG1 1 ATOM 2547 C CG2 . ILE B 2 18 ? 29.547 -29.207 -45.266 1.00 84.06 ? 18 ILE B CG2 1 ATOM 2548 C CD1 . ILE B 2 18 ? 28.292 -32.314 -47.204 1.00 90.15 ? 18 ILE B CD1 1 ATOM 2549 N N . ASP B 2 19 ? 31.594 -33.320 -46.922 1.00 79.94 ? 19 ASP B N 1 ATOM 2550 C CA . ASP B 2 19 ? 31.555 -34.770 -47.094 1.00 81.32 ? 19 ASP B CA 1 ATOM 2551 C C . ASP B 2 19 ? 32.791 -35.445 -46.491 1.00 78.15 ? 19 ASP B C 1 ATOM 2552 O O . ASP B 2 19 ? 32.704 -36.547 -45.951 1.00 79.55 ? 19 ASP B O 1 ATOM 2553 C CB . ASP B 2 19 ? 31.434 -35.089 -48.592 1.00 82.84 ? 19 ASP B CB 1 ATOM 2554 C CG . ASP B 2 19 ? 30.924 -36.494 -48.871 1.00 86.34 ? 19 ASP B CG 1 ATOM 2555 O OD1 . ASP B 2 19 ? 30.786 -37.303 -47.926 1.00 87.57 ? 19 ASP B OD1 1 ATOM 2556 O OD2 . ASP B 2 19 ? 30.655 -36.783 -50.059 1.00 88.22 ? 19 ASP B OD2 1 ATOM 2557 N N . GLY B 2 20 ? 33.938 -34.781 -46.585 1.00 74.16 ? 20 GLY B N 1 ATOM 2558 C CA . GLY B 2 20 ? 35.177 -35.289 -46.005 1.00 71.35 ? 20 GLY B CA 1 ATOM 2559 C C . GLY B 2 20 ? 36.150 -34.170 -45.696 1.00 67.84 ? 20 GLY B C 1 ATOM 2560 O O . GLY B 2 20 ? 35.802 -32.991 -45.791 1.00 67.60 ? 20 GLY B O 1 ATOM 2561 N N . TRP B 2 21 ? 37.371 -34.544 -45.322 1.00 65.45 ? 21 TRP B N 1 ATOM 2562 C CA . TRP B 2 21 ? 38.422 -33.577 -45.007 1.00 62.61 ? 21 TRP B CA 1 ATOM 2563 C C . TRP B 2 21 ? 39.097 -33.088 -46.276 1.00 61.87 ? 21 TRP B C 1 ATOM 2564 O O . TRP B 2 21 ? 39.416 -31.911 -46.395 1.00 60.88 ? 21 TRP B O 1 ATOM 2565 C CB . TRP B 2 21 ? 39.474 -34.200 -44.088 1.00 61.15 ? 21 TRP B CB 1 ATOM 2566 C CG . TRP B 2 21 ? 39.044 -34.325 -42.662 1.00 61.20 ? 21 TRP B CG 1 ATOM 2567 C CD1 . TRP B 2 21 ? 37.776 -34.513 -42.202 1.00 63.19 ? 21 TRP B CD1 1 ATOM 2568 C CD2 . TRP B 2 21 ? 39.889 -34.292 -41.509 1.00 59.58 ? 21 TRP B CD2 1 ATOM 2569 N NE1 . TRP B 2 21 ? 37.776 -34.590 -40.835 1.00 62.99 ? 21 TRP B NE1 1 ATOM 2570 C CE2 . TRP B 2 21 ? 39.061 -34.459 -40.381 1.00 60.68 ? 21 TRP B CE2 1 ATOM 2571 C CE3 . TRP B 2 21 ? 41.266 -34.133 -41.320 1.00 57.77 ? 21 TRP B CE3 1 ATOM 2572 C CZ2 . TRP B 2 21 ? 39.561 -34.474 -39.077 1.00 59.76 ? 21 TRP B CZ2 1 ATOM 2573 C CZ3 . TRP B 2 21 ? 41.765 -34.148 -40.022 1.00 56.97 ? 21 TRP B CZ3 1 ATOM 2574 C CH2 . TRP B 2 21 ? 40.911 -34.319 -38.918 1.00 57.86 ? 21 TRP B CH2 1 ATOM 2575 N N . TYR B 2 22 ? 39.321 -34.008 -47.211 1.00 62.73 ? 22 TYR B N 1 ATOM 2576 C CA . TYR B 2 22 ? 39.958 -33.703 -48.490 1.00 62.65 ? 22 TYR B CA 1 ATOM 2577 C C . TYR B 2 22 ? 39.048 -34.109 -49.651 1.00 65.02 ? 22 TYR B C 1 ATOM 2578 O O . TYR B 2 22 ? 38.108 -34.885 -49.471 1.00 66.73 ? 22 TYR B O 1 ATOM 2579 C CB . TYR B 2 22 ? 41.293 -34.440 -48.590 1.00 62.01 ? 22 TYR B CB 1 ATOM 2580 C CG . TYR B 2 22 ? 42.119 -34.361 -47.330 1.00 60.19 ? 22 TYR B CG 1 ATOM 2581 C CD1 . TYR B 2 22 ? 41.984 -35.317 -46.324 1.00 60.30 ? 22 TYR B CD1 1 ATOM 2582 C CD2 . TYR B 2 22 ? 43.026 -33.329 -47.135 1.00 58.73 ? 22 TYR B CD2 1 ATOM 2583 C CE1 . TYR B 2 22 ? 42.735 -35.246 -45.163 1.00 58.82 ? 22 TYR B CE1 1 ATOM 2584 C CE2 . TYR B 2 22 ? 43.781 -33.251 -45.980 1.00 57.48 ? 22 TYR B CE2 1 ATOM 2585 C CZ . TYR B 2 22 ? 43.634 -34.212 -44.998 1.00 57.39 ? 22 TYR B CZ 1 ATOM 2586 O OH . TYR B 2 22 ? 44.382 -34.135 -43.850 1.00 56.22 ? 22 TYR B OH 1 ATOM 2587 N N . GLY B 2 23 ? 39.325 -33.581 -50.840 1.00 65.49 ? 23 GLY B N 1 ATOM 2588 C CA . GLY B 2 23 ? 38.507 -33.895 -52.007 1.00 67.99 ? 23 GLY B CA 1 ATOM 2589 C C . GLY B 2 23 ? 38.961 -33.294 -53.324 1.00 68.54 ? 23 GLY B C 1 ATOM 2590 O O . GLY B 2 23 ? 39.914 -32.516 -53.378 1.00 67.14 ? 23 GLY B O 1 ATOM 2591 N N . PHE B 2 24 ? 38.253 -33.671 -54.385 1.00 71.10 ? 24 PHE B N 1 ATOM 2592 C CA . PHE B 2 24 ? 38.533 -33.219 -55.743 1.00 72.30 ? 24 PHE B CA 1 ATOM 2593 C C . PHE B 2 24 ? 37.412 -32.303 -56.209 1.00 73.60 ? 24 PHE B C 1 ATOM 2594 O O . PHE B 2 24 ? 36.239 -32.574 -55.952 1.00 74.96 ? 24 PHE B O 1 ATOM 2595 C CB . PHE B 2 24 ? 38.602 -34.405 -56.711 1.00 74.67 ? 24 PHE B CB 1 ATOM 2596 C CG . PHE B 2 24 ? 39.431 -35.560 -56.221 1.00 74.56 ? 24 PHE B CG 1 ATOM 2597 C CD1 . PHE B 2 24 ? 38.904 -36.481 -55.323 1.00 75.03 ? 24 PHE B CD1 1 ATOM 2598 C CD2 . PHE B 2 24 ? 40.726 -35.749 -56.686 1.00 74.54 ? 24 PHE B CD2 1 ATOM 2599 C CE1 . PHE B 2 24 ? 39.659 -37.552 -54.881 1.00 75.32 ? 24 PHE B CE1 1 ATOM 2600 C CE2 . PHE B 2 24 ? 41.486 -36.821 -56.249 1.00 74.95 ? 24 PHE B CE2 1 ATOM 2601 C CZ . PHE B 2 24 ? 40.954 -37.722 -55.342 1.00 75.23 ? 24 PHE B CZ 1 ATOM 2602 N N . ARG B 2 25 ? 37.781 -31.224 -56.895 1.00 73.72 ? 25 ARG B N 1 ATOM 2603 C CA . ARG B 2 25 ? 36.820 -30.360 -57.585 1.00 75.53 ? 25 ARG B CA 1 ATOM 2604 C C . ARG B 2 25 ? 37.221 -30.261 -59.054 1.00 77.25 ? 25 ARG B C 1 ATOM 2605 O O . ARG B 2 25 ? 38.282 -29.720 -59.372 1.00 76.60 ? 25 ARG B O 1 ATOM 2606 C CB . ARG B 2 25 ? 36.789 -28.969 -56.944 1.00 74.31 ? 25 ARG B CB 1 ATOM 2607 C CG . ARG B 2 25 ? 35.736 -28.029 -57.516 1.00 76.23 ? 25 ARG B CG 1 ATOM 2608 C CD . ARG B 2 25 ? 35.534 -26.809 -56.626 1.00 75.50 ? 25 ARG B CD 1 ATOM 2609 N NE . ARG B 2 25 ? 34.753 -27.113 -55.425 1.00 75.45 ? 25 ARG B NE 1 ATOM 2610 C CZ . ARG B 2 25 ? 34.573 -26.269 -54.407 1.00 75.02 ? 25 ARG B CZ 1 ATOM 2611 N NH1 . ARG B 2 25 ? 35.130 -25.057 -54.416 1.00 74.53 ? 25 ARG B NH1 1 ATOM 2612 N NH2 . ARG B 2 25 ? 33.846 -26.644 -53.357 1.00 75.35 ? 25 ARG B NH2 1 ATOM 2613 N N . HIS B 2 26 ? 36.380 -30.789 -59.941 1.00 80.05 ? 26 HIS B N 1 ATOM 2614 C CA . HIS B 2 26 ? 36.690 -30.839 -61.377 1.00 82.12 ? 26 HIS B CA 1 ATOM 2615 C C . HIS B 2 26 ? 35.933 -29.782 -62.176 1.00 83.97 ? 26 HIS B C 1 ATOM 2616 O O . HIS B 2 26 ? 34.968 -29.195 -61.694 1.00 84.18 ? 26 HIS B O 1 ATOM 2617 C CB . HIS B 2 26 ? 36.386 -32.226 -61.951 1.00 84.41 ? 26 HIS B CB 1 ATOM 2618 C CG . HIS B 2 26 ? 34.929 -32.568 -61.975 1.00 86.59 ? 26 HIS B CG 1 ATOM 2619 N ND1 . HIS B 2 26 ? 34.126 -32.334 -63.072 1.00 89.33 ? 26 HIS B ND1 1 ATOM 2620 C CD2 . HIS B 2 26 ? 34.128 -33.121 -61.035 1.00 86.87 ? 26 HIS B CD2 1 ATOM 2621 C CE1 . HIS B 2 26 ? 32.894 -32.731 -62.805 1.00 91.39 ? 26 HIS B CE1 1 ATOM 2622 N NE2 . HIS B 2 26 ? 32.869 -33.212 -61.575 1.00 90.06 ? 26 HIS B NE2 1 ATOM 2623 N N . GLN B 2 27 ? 36.386 -29.557 -63.404 1.00 85.80 ? 27 GLN B N 1 ATOM 2624 C CA . GLN B 2 27 ? 35.769 -28.593 -64.309 1.00 88.01 ? 27 GLN B CA 1 ATOM 2625 C C . GLN B 2 27 ? 36.010 -29.053 -65.743 1.00 90.71 ? 27 GLN B C 1 ATOM 2626 O O . GLN B 2 27 ? 37.150 -29.061 -66.209 1.00 90.66 ? 27 GLN B O 1 ATOM 2627 C CB . GLN B 2 27 ? 36.359 -27.197 -64.072 1.00 86.82 ? 27 GLN B CB 1 ATOM 2628 C CG . GLN B 2 27 ? 36.033 -26.151 -65.136 1.00 89.10 ? 27 GLN B CG 1 ATOM 2629 C CD . GLN B 2 27 ? 34.547 -25.858 -65.255 1.00 91.08 ? 27 GLN B CD 1 ATOM 2630 O OE1 . GLN B 2 27 ? 33.801 -26.611 -65.883 1.00 93.35 ? 27 GLN B OE1 1 ATOM 2631 N NE2 . GLN B 2 27 ? 34.114 -24.746 -64.669 1.00 90.87 ? 27 GLN B NE2 1 ATOM 2632 N N . ASN B 2 28 ? 34.937 -29.448 -66.427 1.00 93.57 ? 28 ASN B N 1 ATOM 2633 C CA . ASN B 2 28 ? 35.021 -29.967 -67.797 1.00 96.69 ? 28 ASN B CA 1 ATOM 2634 C C . ASN B 2 28 ? 33.869 -29.452 -68.669 1.00 99.48 ? 28 ASN B C 1 ATOM 2635 O O . ASN B 2 28 ? 33.167 -28.517 -68.278 1.00 99.08 ? 28 ASN B O 1 ATOM 2636 C CB . ASN B 2 28 ? 35.073 -31.506 -67.769 1.00 98.04 ? 28 ASN B CB 1 ATOM 2637 C CG . ASN B 2 28 ? 33.864 -32.132 -67.084 1.00 99.03 ? 28 ASN B CG 1 ATOM 2638 O OD1 . ASN B 2 28 ? 32.820 -31.501 -66.924 1.00 99.78 ? 28 ASN B OD1 1 ATOM 2639 N ND2 . ASN B 2 28 ? 34.003 -33.392 -66.687 1.00 99.51 ? 28 ASN B ND2 1 ATOM 2640 N N . ALA B 2 29 ? 33.682 -30.047 -69.846 1.00 102.63 ? 29 ALA B N 1 ATOM 2641 C CA . ALA B 2 29 ? 32.581 -29.670 -70.733 1.00 105.74 ? 29 ALA B CA 1 ATOM 2642 C C . ALA B 2 29 ? 31.207 -29.906 -70.095 1.00 106.78 ? 29 ALA B C 1 ATOM 2643 O O . ALA B 2 29 ? 30.249 -29.202 -70.414 1.00 108.66 ? 29 ALA B O 1 ATOM 2644 C CB . ALA B 2 29 ? 32.686 -30.412 -72.059 1.00 109.21 ? 29 ALA B CB 1 ATOM 2645 N N . GLN B 2 30 ? 31.117 -30.883 -69.192 1.00 105.96 ? 30 GLN B N 1 ATOM 2646 C CA . GLN B 2 30 ? 29.867 -31.183 -68.484 1.00 107.34 ? 30 GLN B CA 1 ATOM 2647 C C . GLN B 2 30 ? 29.628 -30.321 -67.235 1.00 104.58 ? 30 GLN B C 1 ATOM 2648 O O . GLN B 2 30 ? 28.583 -30.444 -66.597 1.00 106.06 ? 30 GLN B O 1 ATOM 2649 C CB . GLN B 2 30 ? 29.824 -32.660 -68.087 1.00 108.49 ? 30 GLN B CB 1 ATOM 2650 C CG . GLN B 2 30 ? 29.922 -33.620 -69.260 1.00 111.95 ? 30 GLN B CG 1 ATOM 2651 C CD . GLN B 2 30 ? 29.704 -35.059 -68.845 1.00 113.94 ? 30 GLN B CD 1 ATOM 2652 O OE1 . GLN B 2 30 ? 30.617 -35.883 -68.916 1.00 113.49 ? 30 GLN B OE1 1 ATOM 2653 N NE2 . GLN B 2 30 ? 28.493 -35.369 -68.397 1.00 116.56 ? 30 GLN B NE2 1 ATOM 2654 N N . GLY B 2 31 ? 30.587 -29.465 -66.885 1.00 101.01 ? 31 GLY B N 1 ATOM 2655 C CA . GLY B 2 31 ? 30.433 -28.540 -65.758 1.00 98.70 ? 31 GLY B CA 1 ATOM 2656 C C . GLY B 2 31 ? 31.302 -28.905 -64.568 1.00 95.13 ? 31 GLY B C 1 ATOM 2657 O O . GLY B 2 31 ? 32.112 -29.834 -64.642 1.00 94.20 ? 31 GLY B O 1 ATOM 2658 N N . GLU B 2 32 ? 31.130 -28.168 -63.471 1.00 97.16 ? 32 GLU B N 1 ATOM 2659 C CA . GLU B 2 32 ? 31.917 -28.378 -62.252 1.00 92.40 ? 32 GLU B CA 1 ATOM 2660 C C . GLU B 2 32 ? 31.228 -29.343 -61.281 1.00 90.96 ? 32 GLU B C 1 ATOM 2661 O O . GLU B 2 32 ? 30.000 -29.392 -61.200 1.00 94.70 ? 32 GLU B O 1 ATOM 2662 C CB . GLU B 2 32 ? 32.215 -27.036 -61.555 1.00 93.57 ? 32 GLU B CB 1 ATOM 2663 C CG . GLU B 2 32 ? 32.789 -27.167 -60.145 1.00 89.73 ? 32 GLU B CG 1 ATOM 2664 C CD . GLU B 2 32 ? 33.542 -25.934 -59.672 1.00 90.60 ? 32 GLU B CD 1 ATOM 2665 O OE1 . GLU B 2 32 ? 34.556 -25.575 -60.310 1.00 90.33 ? 32 GLU B OE1 1 ATOM 2666 O OE2 . GLU B 2 32 ? 33.128 -25.333 -58.653 1.00 92.22 ? 32 GLU B OE2 1 ATOM 2667 N N . GLY B 2 33 ? 32.041 -30.112 -60.559 1.00 86.10 ? 33 GLY B N 1 ATOM 2668 C CA . GLY B 2 33 ? 31.571 -30.974 -59.470 1.00 84.63 ? 33 GLY B CA 1 ATOM 2669 C C . GLY B 2 33 ? 32.652 -31.159 -58.415 1.00 79.65 ? 33 GLY B C 1 ATOM 2670 O O . GLY B 2 33 ? 33.826 -30.885 -58.673 1.00 77.29 ? 33 GLY B O 1 ATOM 2671 N N . THR B 2 34 ? 32.257 -31.616 -57.227 1.00 78.59 ? 34 THR B N 1 ATOM 2672 C CA . THR B 2 34 ? 33.188 -31.787 -56.105 1.00 74.28 ? 34 THR B CA 1 ATOM 2673 C C . THR B 2 34 ? 32.895 -33.086 -55.348 1.00 72.89 ? 34 THR B C 1 ATOM 2674 O O . THR B 2 34 ? 31.735 -33.394 -55.077 1.00 75.87 ? 34 THR B O 1 ATOM 2675 C CB . THR B 2 34 ? 33.121 -30.606 -55.104 1.00 74.95 ? 34 THR B CB 1 ATOM 2676 O OG1 . THR B 2 34 ? 32.411 -31.001 -53.922 1.00 75.41 ? 34 THR B OG1 1 ATOM 2677 C CG2 . THR B 2 34 ? 32.445 -29.374 -55.721 1.00 79.72 ? 34 THR B CG2 1 ATOM 2678 N N . ALA B 2 35 ? 33.940 -33.832 -54.990 1.00 69.03 ? 35 ALA B N 1 ATOM 2679 C CA . ALA B 2 35 ? 33.763 -35.111 -54.294 1.00 68.21 ? 35 ALA B CA 1 ATOM 2680 C C . ALA B 2 35 ? 34.866 -35.361 -53.278 1.00 64.12 ? 35 ALA B C 1 ATOM 2681 O O . ALA B 2 35 ? 36.021 -35.008 -53.506 1.00 61.91 ? 35 ALA B O 1 ATOM 2682 C CB . ALA B 2 35 ? 33.705 -36.253 -55.295 1.00 69.80 ? 35 ALA B CB 1 ATOM 2683 N N . ALA B 2 36 ? 34.498 -35.995 -52.168 1.00 63.76 ? 36 ALA B N 1 ATOM 2684 C CA . ALA B 2 36 ? 35.416 -36.223 -51.056 1.00 60.28 ? 36 ALA B CA 1 ATOM 2685 C C . ALA B 2 36 ? 36.240 -37.491 -51.247 1.00 59.24 ? 36 ALA B C 1 ATOM 2686 O O . ALA B 2 36 ? 35.704 -38.524 -51.644 1.00 61.59 ? 36 ALA B O 1 ATOM 2687 C CB . ALA B 2 36 ? 34.646 -36.298 -49.746 1.00 60.90 ? 36 ALA B CB 1 ATOM 2688 N N . ASP B 2 37 ? 37.540 -37.401 -50.955 1.00 56.55 ? 37 ASP B N 1 ATOM 2689 C CA . ASP B 2 37 ? 38.421 -38.567 -50.926 1.00 56.06 ? 37 ASP B CA 1 ATOM 2690 C C . ASP B 2 37 ? 38.350 -39.236 -49.557 1.00 55.23 ? 37 ASP B C 1 ATOM 2691 O O . ASP B 2 37 ? 38.735 -38.640 -48.544 1.00 52.95 ? 37 ASP B O 1 ATOM 2692 C CB . ASP B 2 37 ? 39.871 -38.177 -51.215 1.00 54.49 ? 37 ASP B CB 1 ATOM 2693 C CG . ASP B 2 37 ? 40.793 -39.387 -51.288 1.00 55.13 ? 37 ASP B CG 1 ATOM 2694 O OD1 . ASP B 2 37 ? 40.758 -40.095 -52.317 1.00 57.64 ? 37 ASP B OD1 1 ATOM 2695 O OD2 . ASP B 2 37 ? 41.549 -39.634 -50.319 1.00 53.52 ? 37 ASP B OD2 1 ATOM 2696 N N . TYR B 2 38 ? 37.870 -40.477 -49.540 1.00 57.62 ? 38 TYR B N 1 ATOM 2697 C CA . TYR B 2 38 ? 37.728 -41.255 -48.310 1.00 57.70 ? 38 TYR B CA 1 ATOM 2698 C C . TYR B 2 38 ? 39.089 -41.602 -47.689 1.00 55.22 ? 38 TYR B C 1 ATOM 2699 O O . TYR B 2 38 ? 39.322 -41.333 -46.513 1.00 53.01 ? 38 TYR B O 1 ATOM 2700 C CB . TYR B 2 38 ? 36.924 -42.531 -48.611 1.00 62.25 ? 38 TYR B CB 1 ATOM 2701 C CG . TYR B 2 38 ? 36.742 -43.484 -47.447 1.00 63.79 ? 38 TYR B CG 1 ATOM 2702 C CD1 . TYR B 2 38 ? 35.738 -43.283 -46.502 1.00 64.90 ? 38 TYR B CD1 1 ATOM 2703 C CD2 . TYR B 2 38 ? 37.560 -44.603 -47.308 1.00 65.04 ? 38 TYR B CD2 1 ATOM 2704 C CE1 . TYR B 2 38 ? 35.566 -44.161 -45.440 1.00 66.69 ? 38 TYR B CE1 1 ATOM 2705 C CE2 . TYR B 2 38 ? 37.398 -45.485 -46.251 1.00 66.85 ? 38 TYR B CE2 1 ATOM 2706 C CZ . TYR B 2 38 ? 36.402 -45.262 -45.320 1.00 67.54 ? 38 TYR B CZ 1 ATOM 2707 O OH . TYR B 2 38 ? 36.241 -46.144 -44.272 1.00 69.79 ? 38 TYR B OH 1 ATOM 2708 N N . LYS B 2 39 ? 39.984 -42.174 -48.492 1.00 56.10 ? 39 LYS B N 1 ATOM 2709 C CA . LYS B 2 39 ? 41.240 -42.751 -47.990 1.00 55.43 ? 39 LYS B CA 1 ATOM 2710 C C . LYS B 2 39 ? 42.068 -41.738 -47.190 1.00 51.78 ? 39 LYS B C 1 ATOM 2711 O O . LYS B 2 39 ? 42.411 -41.985 -46.035 1.00 50.61 ? 39 LYS B O 1 ATOM 2712 C CB . LYS B 2 39 ? 42.084 -43.320 -49.142 1.00 58.04 ? 39 LYS B CB 1 ATOM 2713 C CG . LYS B 2 39 ? 42.539 -44.758 -48.930 1.00 61.40 ? 39 LYS B CG 1 ATOM 2714 C CD . LYS B 2 39 ? 41.380 -45.731 -49.114 1.00 65.06 ? 39 LYS B CD 1 ATOM 2715 C CE . LYS B 2 39 ? 41.840 -47.178 -49.203 1.00 69.98 ? 39 LYS B CE 1 ATOM 2716 N NZ . LYS B 2 39 ? 42.400 -47.520 -50.540 1.00 73.59 ? 39 LYS B NZ 1 ATOM 2717 N N . SER B 2 40 ? 42.378 -40.603 -47.812 1.00 50.45 ? 40 SER B N 1 ATOM 2718 C CA . SER B 2 40 ? 43.134 -39.533 -47.160 1.00 47.79 ? 40 SER B CA 1 ATOM 2719 C C . SER B 2 40 ? 42.425 -39.034 -45.906 1.00 45.89 ? 40 SER B C 1 ATOM 2720 O O . SER B 2 40 ? 43.047 -38.907 -44.847 1.00 44.42 ? 40 SER B O 1 ATOM 2721 C CB . SER B 2 40 ? 43.326 -38.364 -48.121 1.00 47.93 ? 40 SER B CB 1 ATOM 2722 O OG . SER B 2 40 ? 42.072 -37.902 -48.588 1.00 48.33 ? 40 SER B OG 1 ATOM 2723 N N . THR B 2 41 ? 41.132 -38.739 -46.042 1.00 46.45 ? 41 THR B N 1 ATOM 2724 C CA . THR B 2 41 ? 40.308 -38.278 -44.926 1.00 45.89 ? 41 THR B CA 1 ATOM 2725 C C . THR B 2 41 ? 40.414 -39.247 -43.751 1.00 45.52 ? 41 THR B C 1 ATOM 2726 O O . THR B 2 41 ? 40.680 -38.842 -42.619 1.00 44.05 ? 41 THR B O 1 ATOM 2727 C CB . THR B 2 41 ? 38.831 -38.125 -45.352 1.00 48.18 ? 41 THR B CB 1 ATOM 2728 O OG1 . THR B 2 41 ? 38.693 -36.973 -46.191 1.00 48.77 ? 41 THR B OG1 1 ATOM 2729 C CG2 . THR B 2 41 ? 37.902 -37.971 -44.152 1.00 48.92 ? 41 THR B CG2 1 ATOM 2730 N N . GLN B 2 42 ? 40.230 -40.529 -44.041 1.00 47.41 ? 42 GLN B N 1 ATOM 2731 C CA . GLN B 2 42 ? 40.190 -41.559 -43.014 1.00 48.16 ? 42 GLN B CA 1 ATOM 2732 C C . GLN B 2 42 ? 41.541 -41.736 -42.322 1.00 46.40 ? 42 GLN B C 1 ATOM 2733 O O . GLN B 2 42 ? 41.599 -42.011 -41.125 1.00 45.82 ? 42 GLN B O 1 ATOM 2734 C CB . GLN B 2 42 ? 39.743 -42.889 -43.623 1.00 51.82 ? 42 GLN B CB 1 ATOM 2735 C CG . GLN B 2 42 ? 39.156 -43.862 -42.617 1.00 54.17 ? 42 GLN B CG 1 ATOM 2736 C CD . GLN B 2 42 ? 37.884 -43.337 -41.968 1.00 55.15 ? 42 GLN B CD 1 ATOM 2737 O OE1 . GLN B 2 42 ? 37.087 -42.636 -42.600 1.00 56.06 ? 42 GLN B OE1 1 ATOM 2738 N NE2 . GLN B 2 42 ? 37.688 -43.676 -40.697 1.00 55.70 ? 42 GLN B NE2 1 ATOM 2739 N N . SER B 2 43 ? 42.621 -41.575 -43.080 1.00 46.06 ? 43 SER B N 1 ATOM 2740 C CA . SER B 2 43 ? 43.971 -41.730 -42.547 1.00 45.37 ? 43 SER B CA 1 ATOM 2741 C C . SER B 2 43 ? 44.296 -40.637 -41.530 1.00 42.71 ? 43 SER B C 1 ATOM 2742 O O . SER B 2 43 ? 44.952 -40.892 -40.525 1.00 42.04 ? 43 SER B O 1 ATOM 2743 C CB . SER B 2 43 ? 44.996 -41.714 -43.679 1.00 46.78 ? 43 SER B CB 1 ATOM 2744 O OG . SER B 2 43 ? 46.138 -42.470 -43.320 1.00 48.45 ? 43 SER B OG 1 ATOM 2745 N N . ALA B 2 44 ? 43.815 -39.426 -41.792 1.00 41.69 ? 44 ALA B N 1 ATOM 2746 C CA . ALA B 2 44 ? 44.011 -38.311 -40.875 1.00 40.21 ? 44 ALA B CA 1 ATOM 2747 C C . ALA B 2 44 ? 43.122 -38.460 -39.643 1.00 39.82 ? 44 ALA B C 1 ATOM 2748 O O . ALA B 2 44 ? 43.580 -38.250 -38.518 1.00 39.14 ? 44 ALA B O 1 ATOM 2749 C CB . ALA B 2 44 ? 43.728 -36.993 -41.577 1.00 40.49 ? 44 ALA B CB 1 ATOM 2750 N N . ILE B 2 45 ? 41.854 -38.813 -39.855 1.00 40.96 ? 45 ILE B N 1 ATOM 2751 C CA . ILE B 2 45 ? 40.919 -39.024 -38.750 1.00 41.59 ? 45 ILE B CA 1 ATOM 2752 C C . ILE B 2 45 ? 41.458 -40.094 -37.795 1.00 41.42 ? 45 ILE B C 1 ATOM 2753 O O . ILE B 2 45 ? 41.460 -39.901 -36.579 1.00 40.97 ? 45 ILE B O 1 ATOM 2754 C CB . ILE B 2 45 ? 39.505 -39.401 -39.258 1.00 44.09 ? 45 ILE B CB 1 ATOM 2755 C CG1 . ILE B 2 45 ? 38.822 -38.164 -39.852 1.00 44.91 ? 45 ILE B CG1 1 ATOM 2756 C CG2 . ILE B 2 45 ? 38.647 -39.977 -38.133 1.00 45.82 ? 45 ILE B CG2 1 ATOM 2757 C CD1 . ILE B 2 45 ? 37.467 -38.426 -40.480 1.00 48.00 ? 45 ILE B CD1 1 ATOM 2758 N N . ASP B 2 46 ? 41.933 -41.200 -38.359 1.00 42.27 ? 46 ASP B N 1 ATOM 2759 C CA . ASP B 2 46 ? 42.452 -42.320 -37.576 1.00 43.08 ? 46 ASP B CA 1 ATOM 2760 C C . ASP B 2 46 ? 43.683 -41.957 -36.748 1.00 41.26 ? 46 ASP B C 1 ATOM 2761 O O . ASP B 2 46 ? 43.833 -42.439 -35.626 1.00 41.49 ? 46 ASP B O 1 ATOM 2762 C CB . ASP B 2 46 ? 42.771 -43.522 -38.486 1.00 45.48 ? 46 ASP B CB 1 ATOM 2763 C CG . ASP B 2 46 ? 41.522 -44.273 -38.939 1.00 48.58 ? 46 ASP B CG 1 ATOM 2764 O OD1 . ASP B 2 46 ? 40.408 -43.943 -38.473 1.00 49.04 ? 46 ASP B OD1 1 ATOM 2765 O OD2 . ASP B 2 46 ? 41.655 -45.207 -39.764 1.00 51.41 ? 46 ASP B OD2 1 ATOM 2766 N N . GLN B 2 47 ? 44.561 -41.126 -37.297 1.00 40.09 ? 47 GLN B N 1 ATOM 2767 C CA . GLN B 2 47 ? 45.734 -40.677 -36.554 1.00 39.28 ? 47 GLN B CA 1 ATOM 2768 C C . GLN B 2 47 ? 45.335 -39.720 -35.428 1.00 37.99 ? 47 GLN B C 1 ATOM 2769 O O . GLN B 2 47 ? 45.886 -39.783 -34.332 1.00 37.65 ? 47 GLN B O 1 ATOM 2770 C CB . GLN B 2 47 ? 46.753 -40.005 -37.480 1.00 39.58 ? 47 GLN B CB 1 ATOM 2771 C CG . GLN B 2 47 ? 47.457 -40.948 -38.441 1.00 41.74 ? 47 GLN B CG 1 ATOM 2772 C CD . GLN B 2 47 ? 48.380 -40.214 -39.407 1.00 42.82 ? 47 GLN B CD 1 ATOM 2773 O OE1 . GLN B 2 47 ? 49.409 -39.658 -39.005 1.00 43.47 ? 47 GLN B OE1 1 ATOM 2774 N NE2 . GLN B 2 47 ? 48.022 -40.215 -40.687 1.00 43.55 ? 47 GLN B NE2 1 ATOM 2775 N N . ILE B 2 48 ? 44.383 -38.835 -35.708 1.00 37.81 ? 48 ILE B N 1 ATOM 2776 C CA . ILE B 2 48 ? 43.934 -37.862 -34.720 1.00 37.76 ? 48 ILE B CA 1 ATOM 2777 C C . ILE B 2 48 ? 43.193 -38.564 -33.587 1.00 38.35 ? 48 ILE B C 1 ATOM 2778 O O . ILE B 2 48 ? 43.412 -38.246 -32.422 1.00 38.50 ? 48 ILE B O 1 ATOM 2779 C CB . ILE B 2 48 ? 43.070 -36.739 -35.351 1.00 38.60 ? 48 ILE B CB 1 ATOM 2780 C CG1 . ILE B 2 48 ? 43.938 -35.533 -35.721 1.00 38.76 ? 48 ILE B CG1 1 ATOM 2781 C CG2 . ILE B 2 48 ? 41.998 -36.243 -34.388 1.00 40.04 ? 48 ILE B CG2 1 ATOM 2782 C CD1 . ILE B 2 48 ? 44.926 -35.784 -36.839 1.00 38.53 ? 48 ILE B CD1 1 ATOM 2783 N N . THR B 2 49 ? 42.330 -39.518 -33.921 1.00 39.45 ? 49 THR B N 1 ATOM 2784 C CA . THR B 2 49 ? 41.593 -40.267 -32.904 1.00 40.84 ? 49 THR B CA 1 ATOM 2785 C C . THR B 2 49 ? 42.533 -41.111 -32.045 1.00 40.26 ? 49 THR B C 1 ATOM 2786 O O . THR B 2 49 ? 42.293 -41.303 -30.854 1.00 41.01 ? 49 THR B O 1 ATOM 2787 C CB . THR B 2 49 ? 40.561 -41.219 -33.535 1.00 43.38 ? 49 THR B CB 1 ATOM 2788 O OG1 . THR B 2 49 ? 41.232 -42.102 -34.443 1.00 43.58 ? 49 THR B OG1 1 ATOM 2789 C CG2 . THR B 2 49 ? 39.469 -40.445 -34.263 1.00 44.56 ? 49 THR B CG2 1 ATOM 2790 N N . GLY B 2 50 ? 43.589 -41.634 -32.660 1.00 39.48 ? 50 GLY B N 1 ATOM 2791 C CA . GLY B 2 50 ? 44.607 -42.378 -31.932 1.00 39.61 ? 50 GLY B CA 1 ATOM 2792 C C . GLY B 2 50 ? 45.326 -41.529 -30.897 1.00 38.21 ? 50 GLY B C 1 ATOM 2793 O O . GLY B 2 50 ? 45.688 -42.022 -29.837 1.00 38.59 ? 50 GLY B O 1 ATOM 2794 N N . LYS B 2 51 ? 45.536 -40.251 -31.210 1.00 37.01 ? 51 LYS B N 1 ATOM 2795 C CA . LYS B 2 51 ? 46.078 -39.299 -30.241 1.00 36.58 ? 51 LYS B CA 1 ATOM 2796 C C . LYS B 2 51 ? 45.158 -39.126 -29.050 1.00 37.19 ? 51 LYS B C 1 ATOM 2797 O O . LYS B 2 51 ? 45.611 -39.102 -27.903 1.00 37.28 ? 51 LYS B O 1 ATOM 2798 C CB . LYS B 2 51 ? 46.261 -37.922 -30.859 1.00 36.35 ? 51 LYS B CB 1 ATOM 2799 C CG . LYS B 2 51 ? 47.504 -37.755 -31.689 1.00 36.62 ? 51 LYS B CG 1 ATOM 2800 C CD . LYS B 2 51 ? 47.652 -36.291 -32.040 1.00 37.30 ? 51 LYS B CD 1 ATOM 2801 C CE . LYS B 2 51 ? 48.857 -36.050 -32.912 1.00 38.37 ? 51 LYS B CE 1 ATOM 2802 N NZ . LYS B 2 51 ? 49.308 -34.640 -32.789 1.00 40.25 ? 51 LYS B NZ 1 ATOM 2803 N N . LEU B 2 52 ? 43.869 -38.960 -29.337 1.00 38.13 ? 52 LEU B N 1 ATOM 2804 C CA . LEU B 2 52 ? 42.871 -38.781 -28.297 1.00 39.90 ? 52 LEU B CA 1 ATOM 2805 C C . LEU B 2 52 ? 42.795 -40.001 -27.396 1.00 40.91 ? 52 LEU B C 1 ATOM 2806 O O . LEU B 2 52 ? 42.762 -39.859 -26.179 1.00 41.74 ? 52 LEU B O 1 ATOM 2807 C CB . LEU B 2 52 ? 41.502 -38.492 -28.906 1.00 41.66 ? 52 LEU B CB 1 ATOM 2808 C CG . LEU B 2 52 ? 41.365 -37.114 -29.545 1.00 41.91 ? 52 LEU B CG 1 ATOM 2809 C CD1 . LEU B 2 52 ? 40.127 -37.066 -30.427 1.00 43.81 ? 52 LEU B CD1 1 ATOM 2810 C CD2 . LEU B 2 52 ? 41.301 -36.033 -28.478 1.00 43.52 ? 52 LEU B CD2 1 ATOM 2811 N N . ASN B 2 53 ? 42.782 -41.193 -27.989 1.00 41.55 ? 53 ASN B N 1 ATOM 2812 C CA . ASN B 2 53 ? 42.714 -42.434 -27.212 1.00 43.61 ? 53 ASN B CA 1 ATOM 2813 C C . ASN B 2 53 ? 43.855 -42.507 -26.206 1.00 43.08 ? 53 ASN B C 1 ATOM 2814 O O . ASN B 2 53 ? 43.642 -42.851 -25.049 1.00 44.33 ? 53 ASN B O 1 ATOM 2815 C CB . ASN B 2 53 ? 42.742 -43.661 -28.132 1.00 44.95 ? 53 ASN B CB 1 ATOM 2816 C CG . ASN B 2 53 ? 41.463 -43.822 -28.942 1.00 46.97 ? 53 ASN B CG 1 ATOM 2817 O OD1 . ASN B 2 53 ? 40.394 -43.344 -28.550 1.00 48.49 ? 53 ASN B OD1 1 ATOM 2818 N ND2 . ASN B 2 53 ? 41.567 -44.506 -30.080 1.00 47.74 ? 53 ASN B ND2 1 ATOM 2819 N N . ARG B 2 54 ? 45.060 -42.165 -26.663 1.00 41.82 ? 54 ARG B N 1 ATOM 2820 C CA . ARG B 2 54 ? 46.237 -42.047 -25.800 1.00 41.95 ? 54 ARG B CA 1 ATOM 2821 C C . ARG B 2 54 ? 46.081 -41.029 -24.676 1.00 41.96 ? 54 ARG B C 1 ATOM 2822 O O . ARG B 2 54 ? 46.468 -41.285 -23.546 1.00 42.66 ? 54 ARG B O 1 ATOM 2823 C CB . ARG B 2 54 ? 47.463 -41.618 -26.617 1.00 41.43 ? 54 ARG B CB 1 ATOM 2824 C CG . ARG B 2 54 ? 48.503 -42.704 -26.872 1.00 43.13 ? 54 ARG B CG 1 ATOM 2825 C CD . ARG B 2 54 ? 49.879 -42.073 -27.046 1.00 43.61 ? 54 ARG B CD 1 ATOM 2826 N NE . ARG B 2 54 ? 49.765 -40.805 -27.770 1.00 42.62 ? 54 ARG B NE 1 ATOM 2827 C CZ . ARG B 2 54 ? 50.081 -39.595 -27.308 1.00 42.34 ? 54 ARG B CZ 1 ATOM 2828 N NH1 . ARG B 2 54 ? 50.588 -39.417 -26.089 1.00 43.25 ? 54 ARG B NH1 1 ATOM 2829 N NH2 . ARG B 2 54 ? 49.886 -38.545 -28.096 1.00 41.76 ? 54 ARG B NH2 1 ATOM 2830 N N . LEU B 2 55 ? 45.551 -39.859 -25.002 1.00 41.93 ? 55 LEU B N 1 ATOM 2831 C CA . LEU B 2 55 ? 45.570 -38.732 -24.073 1.00 43.20 ? 55 LEU B CA 1 ATOM 2832 C C . LEU B 2 55 ? 44.394 -38.681 -23.116 1.00 45.52 ? 55 LEU B C 1 ATOM 2833 O O . LEU B 2 55 ? 44.549 -38.233 -21.986 1.00 46.30 ? 55 LEU B O 1 ATOM 2834 C CB . LEU B 2 55 ? 45.658 -37.408 -24.842 1.00 43.15 ? 55 LEU B CB 1 ATOM 2835 C CG . LEU B 2 55 ? 47.025 -37.181 -25.475 1.00 42.47 ? 55 LEU B CG 1 ATOM 2836 C CD1 . LEU B 2 55 ? 47.023 -35.935 -26.342 1.00 43.11 ? 55 LEU B CD1 1 ATOM 2837 C CD2 . LEU B 2 55 ? 48.092 -37.092 -24.398 1.00 43.42 ? 55 LEU B CD2 1 ATOM 2838 N N . ILE B 2 56 ? 43.224 -39.128 -23.563 1.00 47.43 ? 56 ILE B N 1 ATOM 2839 C CA . ILE B 2 56 ? 42.020 -39.033 -22.745 1.00 51.24 ? 56 ILE B CA 1 ATOM 2840 C C . ILE B 2 56 ? 41.991 -40.187 -21.752 1.00 53.59 ? 56 ILE B C 1 ATOM 2841 O O . ILE B 2 56 ? 41.320 -41.201 -21.964 1.00 55.15 ? 56 ILE B O 1 ATOM 2842 C CB . ILE B 2 56 ? 40.729 -38.969 -23.602 1.00 53.03 ? 56 ILE B CB 1 ATOM 2843 C CG1 . ILE B 2 56 ? 40.811 -37.812 -24.609 1.00 52.08 ? 56 ILE B CG1 1 ATOM 2844 C CG2 . ILE B 2 56 ? 39.489 -38.795 -22.727 1.00 57.32 ? 56 ILE B CG2 1 ATOM 2845 C CD1 . ILE B 2 56 ? 41.182 -36.470 -24.005 1.00 53.02 ? 56 ILE B CD1 1 ATOM 2846 N N . GLU B 2 57 ? 42.759 -40.020 -20.674 1.00 54.77 ? 57 GLU B N 1 ATOM 2847 C CA . GLU B 2 57 ? 42.677 -40.897 -19.511 1.00 57.63 ? 57 GLU B CA 1 ATOM 2848 C C . GLU B 2 57 ? 43.442 -40.337 -18.306 1.00 58.32 ? 57 GLU B C 1 ATOM 2849 O O . GLU B 2 57 ? 44.460 -39.649 -18.457 1.00 56.43 ? 57 GLU B O 1 ATOM 2850 C CB . GLU B 2 57 ? 43.191 -42.310 -19.831 1.00 57.47 ? 57 GLU B CB 1 ATOM 2851 C CG . GLU B 2 57 ? 44.643 -42.378 -20.287 1.00 55.16 ? 57 GLU B CG 1 ATOM 2852 C CD . GLU B 2 57 ? 45.368 -43.596 -19.741 1.00 56.47 ? 57 GLU B CD 1 ATOM 2853 O OE1 . GLU B 2 57 ? 44.755 -44.692 -19.699 1.00 58.80 ? 57 GLU B OE1 1 ATOM 2854 O OE2 . GLU B 2 57 ? 46.549 -43.451 -19.347 1.00 55.48 ? 57 GLU B OE2 1 ATOM 2855 N N . LYS B 2 58 ? 42.926 -40.633 -17.115 1.00 61.67 ? 58 LYS B N 1 ATOM 2856 C CA . LYS B 2 58 ? 43.684 -40.486 -15.876 1.00 62.75 ? 58 LYS B CA 1 ATOM 2857 C C . LYS B 2 58 ? 44.222 -41.859 -15.465 1.00 63.45 ? 58 LYS B C 1 ATOM 2858 O O . LYS B 2 58 ? 43.815 -42.891 -16.016 1.00 63.74 ? 58 LYS B O 1 ATOM 2859 C CB . LYS B 2 58 ? 42.834 -39.865 -14.753 1.00 66.48 ? 58 LYS B CB 1 ATOM 2860 C CG . LYS B 2 58 ? 41.647 -40.696 -14.271 1.00 69.98 ? 58 LYS B CG 1 ATOM 2861 C CD . LYS B 2 58 ? 40.748 -39.886 -13.344 1.00 74.44 ? 58 LYS B CD 1 ATOM 2862 C CE . LYS B 2 58 ? 39.412 -40.570 -13.078 1.00 78.97 ? 58 LYS B CE 1 ATOM 2863 N NZ . LYS B 2 58 ? 38.372 -39.603 -12.620 1.00 83.87 ? 58 LYS B NZ 1 ATOM 2864 N N . THR B 2 59 ? 45.141 -41.856 -14.500 1.00 64.40 ? 59 THR B N 1 ATOM 2865 C CA . THR B 2 59 ? 45.820 -43.075 -14.053 1.00 65.40 ? 59 THR B CA 1 ATOM 2866 C C . THR B 2 59 ? 45.054 -43.756 -12.934 1.00 69.15 ? 59 THR B C 1 ATOM 2867 O O . THR B 2 59 ? 44.198 -43.142 -12.297 1.00 71.11 ? 59 THR B O 1 ATOM 2868 C CB . THR B 2 59 ? 47.235 -42.759 -13.527 1.00 64.74 ? 59 THR B CB 1 ATOM 2869 O OG1 . THR B 2 59 ? 47.145 -41.895 -12.384 1.00 65.73 ? 59 THR B OG1 1 ATOM 2870 C CG2 . THR B 2 59 ? 48.080 -42.096 -14.616 1.00 62.14 ? 59 THR B CG2 1 ATOM 2871 N N . ASN B 2 60 ? 45.397 -45.017 -12.675 1.00 47.12 ? 60 ASN B N 1 ATOM 2872 C CA . ASN B 2 60 ? 44.791 -45.772 -11.578 1.00 48.92 ? 60 ASN B CA 1 ATOM 2873 C C . ASN B 2 60 ? 45.486 -45.480 -10.239 1.00 46.34 ? 60 ASN B C 1 ATOM 2874 O O . ASN B 2 60 ? 45.205 -46.152 -9.237 1.00 49.03 ? 60 ASN B O 1 ATOM 2875 C CB . ASN B 2 60 ? 44.811 -47.289 -11.888 1.00 53.28 ? 60 ASN B CB 1 ATOM 2876 C CG . ASN B 2 60 ? 43.618 -48.039 -11.296 1.00 57.36 ? 60 ASN B CG 1 ATOM 2877 O OD1 . ASN B 2 60 ? 42.563 -47.457 -11.037 1.00 58.53 ? 60 ASN B OD1 1 ATOM 2878 N ND2 . ASN B 2 60 ? 43.778 -49.346 -11.096 1.00 60.55 ? 60 ASN B ND2 1 ATOM 2879 N N . GLN B 2 61 ? 46.376 -44.485 -10.206 1.00 41.78 ? 61 GLN B N 1 ATOM 2880 C CA . GLN B 2 61 ? 47.156 -44.204 -8.997 1.00 39.32 ? 61 GLN B CA 1 ATOM 2881 C C . GLN B 2 61 ? 46.366 -43.364 -8.011 1.00 36.55 ? 61 GLN B C 1 ATOM 2882 O O . GLN B 2 61 ? 45.971 -42.239 -8.309 1.00 33.95 ? 61 GLN B O 1 ATOM 2883 C CB . GLN B 2 61 ? 48.477 -43.496 -9.315 1.00 37.95 ? 61 GLN B CB 1 ATOM 2884 C CG . GLN B 2 61 ? 49.368 -43.297 -8.092 1.00 37.66 ? 61 GLN B CG 1 ATOM 2885 C CD . GLN B 2 61 ? 49.725 -44.600 -7.395 1.00 40.76 ? 61 GLN B CD 1 ATOM 2886 O OE1 . GLN B 2 61 ? 49.971 -45.625 -8.039 1.00 43.30 ? 61 GLN B OE1 1 ATOM 2887 N NE2 . GLN B 2 61 ? 49.752 -44.570 -6.066 1.00 41.45 ? 61 GLN B NE2 1 ATOM 2888 N N . GLN B 2 62 ? 46.143 -43.924 -6.832 1.00 36.45 ? 62 GLN B N 1 ATOM 2889 C CA . GLN B 2 62 ? 45.413 -43.225 -5.804 1.00 35.62 ? 62 GLN B CA 1 ATOM 2890 C C . GLN B 2 62 ? 46.332 -42.362 -4.933 1.00 32.40 ? 62 GLN B C 1 ATOM 2891 O O . GLN B 2 62 ? 47.423 -42.776 -4.562 1.00 31.55 ? 62 GLN B O 1 ATOM 2892 C CB . GLN B 2 62 ? 44.656 -44.212 -4.938 1.00 38.52 ? 62 GLN B CB 1 ATOM 2893 C CG . GLN B 2 62 ? 43.672 -43.520 -4.019 1.00 39.43 ? 62 GLN B CG 1 ATOM 2894 C CD . GLN B 2 62 ? 42.841 -44.497 -3.258 1.00 43.01 ? 62 GLN B CD 1 ATOM 2895 O OE1 . GLN B 2 62 ? 43.033 -44.693 -2.054 1.00 44.17 ? 62 GLN B OE1 1 ATOM 2896 N NE2 . GLN B 2 62 ? 41.917 -45.149 -3.959 1.00 46.12 ? 62 GLN B NE2 1 ATOM 2897 N N . PHE B 2 63 ? 45.870 -41.162 -4.617 1.00 30.67 ? 63 PHE B N 1 ATOM 2898 C CA . PHE B 2 63 ? 46.522 -40.310 -3.626 1.00 28.99 ? 63 PHE B CA 1 ATOM 2899 C C . PHE B 2 63 ? 45.546 -40.035 -2.476 1.00 30.22 ? 63 PHE B C 1 ATOM 2900 O O . PHE B 2 63 ? 44.340 -39.886 -2.703 1.00 31.27 ? 63 PHE B O 1 ATOM 2901 C CB . PHE B 2 63 ? 47.006 -39.015 -4.272 1.00 26.88 ? 63 PHE B CB 1 ATOM 2902 C CG . PHE B 2 63 ? 48.163 -39.207 -5.218 1.00 25.82 ? 63 PHE B CG 1 ATOM 2903 C CD1 . PHE B 2 63 ? 47.945 -39.477 -6.559 1.00 26.13 ? 63 PHE B CD1 1 ATOM 2904 C CD2 . PHE B 2 63 ? 49.476 -39.123 -4.761 1.00 25.28 ? 63 PHE B CD2 1 ATOM 2905 C CE1 . PHE B 2 63 ? 49.010 -39.667 -7.433 1.00 25.51 ? 63 PHE B CE1 1 ATOM 2906 C CE2 . PHE B 2 63 ? 50.551 -39.304 -5.626 1.00 24.73 ? 63 PHE B CE2 1 ATOM 2907 C CZ . PHE B 2 63 ? 50.316 -39.582 -6.966 1.00 24.90 ? 63 PHE B CZ 1 ATOM 2908 N N . GLU B 2 64 ? 46.069 -39.992 -1.252 1.00 30.23 ? 64 GLU B N 1 ATOM 2909 C CA . GLU B 2 64 ? 45.267 -39.714 -0.066 1.00 32.10 ? 64 GLU B CA 1 ATOM 2910 C C . GLU B 2 64 ? 45.584 -38.328 0.474 1.00 30.15 ? 64 GLU B C 1 ATOM 2911 O O . GLU B 2 64 ? 46.575 -37.708 0.090 1.00 28.01 ? 64 GLU B O 1 ATOM 2912 C CB . GLU B 2 64 ? 45.519 -40.721 1.068 1.00 34.55 ? 64 GLU B CB 1 ATOM 2913 C CG . GLU B 2 64 ? 46.098 -42.073 0.687 1.00 36.42 ? 64 GLU B CG 1 ATOM 2914 C CD . GLU B 2 64 ? 45.095 -42.990 0.043 1.00 39.53 ? 64 GLU B CD 1 ATOM 2915 O OE1 . GLU B 2 64 ? 44.156 -43.440 0.742 1.00 43.70 ? 64 GLU B OE1 1 ATOM 2916 O OE2 . GLU B 2 64 ? 45.273 -43.298 -1.154 1.00 40.25 ? 64 GLU B OE2 1 ATOM 2917 N N . LEU B 2 65 ? 44.738 -37.869 1.391 1.00 30.88 ? 65 LEU B N 1 ATOM 2918 C CA . LEU B 2 65 ? 44.998 -36.654 2.168 1.00 30.23 ? 65 LEU B CA 1 ATOM 2919 C C . LEU B 2 65 ? 46.302 -36.754 2.970 1.00 29.22 ? 65 LEU B C 1 ATOM 2920 O O . LEU B 2 65 ? 46.554 -37.766 3.617 1.00 29.68 ? 65 LEU B O 1 ATOM 2921 C CB . LEU B 2 65 ? 43.835 -36.392 3.135 1.00 32.17 ? 65 LEU B CB 1 ATOM 2922 C CG . LEU B 2 65 ? 42.531 -35.959 2.474 1.00 33.61 ? 65 LEU B CG 1 ATOM 2923 C CD1 . LEU B 2 65 ? 41.386 -35.936 3.472 1.00 36.21 ? 65 LEU B CD1 1 ATOM 2924 C CD2 . LEU B 2 65 ? 42.706 -34.597 1.822 1.00 32.71 ? 65 LEU B CD2 1 ATOM 2925 N N . ILE B 2 66 ? 47.135 -35.716 2.899 1.00 28.39 ? 66 ILE B N 1 ATOM 2926 C CA . ILE B 2 66 ? 48.252 -35.547 3.856 1.00 28.43 ? 66 ILE B CA 1 ATOM 2927 C C . ILE B 2 66 ? 48.134 -34.285 4.722 1.00 28.65 ? 66 ILE B C 1 ATOM 2928 O O . ILE B 2 66 ? 48.948 -34.078 5.616 1.00 28.47 ? 66 ILE B O 1 ATOM 2929 C CB . ILE B 2 66 ? 49.674 -35.636 3.220 1.00 27.59 ? 66 ILE B CB 1 ATOM 2930 C CG1 . ILE B 2 66 ? 49.702 -35.163 1.777 1.00 26.89 ? 66 ILE B CG1 1 ATOM 2931 C CG2 . ILE B 2 66 ? 50.188 -37.065 3.279 1.00 28.19 ? 66 ILE B CG2 1 ATOM 2932 C CD1 . ILE B 2 66 ? 49.497 -33.680 1.626 1.00 27.19 ? 66 ILE B CD1 1 ATOM 2933 N N . ASP B 2 67 ? 47.115 -33.459 4.480 1.00 29.34 ? 67 ASP B N 1 ATOM 2934 C CA . ASP B 2 67 ? 46.826 -32.327 5.354 1.00 30.34 ? 67 ASP B CA 1 ATOM 2935 C C . ASP B 2 67 ? 45.334 -32.247 5.609 1.00 32.29 ? 67 ASP B C 1 ATOM 2936 O O . ASP B 2 67 ? 44.593 -33.156 5.231 1.00 33.58 ? 67 ASP B O 1 ATOM 2937 C CB . ASP B 2 67 ? 47.423 -31.007 4.816 1.00 29.91 ? 67 ASP B CB 1 ATOM 2938 C CG . ASP B 2 67 ? 46.993 -30.673 3.390 1.00 29.49 ? 67 ASP B CG 1 ATOM 2939 O OD1 . ASP B 2 67 ? 46.054 -31.295 2.850 1.00 30.14 ? 67 ASP B OD1 1 ATOM 2940 O OD2 . ASP B 2 67 ? 47.612 -29.753 2.803 1.00 29.01 ? 67 ASP B OD2 1 ATOM 2941 N N . ASN B 2 68 ? 44.898 -31.184 6.274 1.00 33.34 ? 68 ASN B N 1 ATOM 2942 C CA . ASN B 2 68 ? 43.575 -31.146 6.861 1.00 35.59 ? 68 ASN B CA 1 ATOM 2943 C C . ASN B 2 68 ? 42.941 -29.760 6.768 1.00 37.35 ? 68 ASN B C 1 ATOM 2944 O O . ASN B 2 68 ? 43.483 -28.764 7.239 1.00 37.91 ? 68 ASN B O 1 ATOM 2945 C CB . ASN B 2 68 ? 43.668 -31.618 8.310 1.00 36.45 ? 68 ASN B CB 1 ATOM 2946 C CG . ASN B 2 68 ? 42.318 -31.755 8.975 1.00 39.01 ? 68 ASN B CG 1 ATOM 2947 O OD1 . ASN B 2 68 ? 41.364 -31.073 8.620 1.00 40.69 ? 68 ASN B OD1 1 ATOM 2948 N ND2 . ASN B 2 68 ? 42.240 -32.624 9.967 1.00 39.80 ? 68 ASN B ND2 1 ATOM 2949 N N . GLU B 2 69 ? 41.764 -29.741 6.175 1.00 39.01 ? 69 GLU B N 1 ATOM 2950 C CA . GLU B 2 69 ? 41.042 -28.534 5.822 1.00 41.32 ? 69 GLU B CA 1 ATOM 2951 C C . GLU B 2 69 ? 40.179 -28.036 6.976 1.00 44.52 ? 69 GLU B C 1 ATOM 2952 O O . GLU B 2 69 ? 39.802 -26.871 7.006 1.00 46.61 ? 69 GLU B O 1 ATOM 2953 C CB . GLU B 2 69 ? 40.161 -28.882 4.630 1.00 42.23 ? 69 GLU B CB 1 ATOM 2954 C CG . GLU B 2 69 ? 39.565 -27.732 3.855 1.00 44.32 ? 69 GLU B CG 1 ATOM 2955 C CD . GLU B 2 69 ? 38.960 -28.215 2.546 1.00 44.50 ? 69 GLU B CD 1 ATOM 2956 O OE1 . GLU B 2 69 ? 39.639 -28.982 1.810 1.00 41.76 ? 69 GLU B OE1 1 ATOM 2957 O OE2 . GLU B 2 69 ? 37.806 -27.842 2.265 1.00 47.19 ? 69 GLU B OE2 1 ATOM 2958 N N . PHE B 2 70 ? 39.852 -28.933 7.905 1.00 45.32 ? 70 PHE B N 1 ATOM 2959 C CA . PHE B 2 70 ? 39.038 -28.606 9.074 1.00 48.44 ? 70 PHE B CA 1 ATOM 2960 C C . PHE B 2 70 ? 39.878 -28.398 10.330 1.00 48.62 ? 70 PHE B C 1 ATOM 2961 O O . PHE B 2 70 ? 39.398 -27.843 11.306 1.00 51.38 ? 70 PHE B O 1 ATOM 2962 C CB . PHE B 2 70 ? 38.031 -29.727 9.354 1.00 49.88 ? 70 PHE B CB 1 ATOM 2963 C CG . PHE B 2 70 ? 37.012 -29.954 8.263 1.00 50.75 ? 70 PHE B CG 1 ATOM 2964 C CD1 . PHE B 2 70 ? 36.784 -29.016 7.259 1.00 50.95 ? 70 PHE B CD1 1 ATOM 2965 C CD2 . PHE B 2 70 ? 36.268 -31.125 8.251 1.00 51.87 ? 70 PHE B CD2 1 ATOM 2966 C CE1 . PHE B 2 70 ? 35.842 -29.248 6.274 1.00 52.23 ? 70 PHE B CE1 1 ATOM 2967 C CE2 . PHE B 2 70 ? 35.315 -31.357 7.274 1.00 53.29 ? 70 PHE B CE2 1 ATOM 2968 C CZ . PHE B 2 70 ? 35.100 -30.416 6.285 1.00 53.52 ? 70 PHE B CZ 1 ATOM 2969 N N . ASN B 2 71 ? 41.127 -28.848 10.313 1.00 46.46 ? 71 ASN B N 1 ATOM 2970 C CA . ASN B 2 71 ? 41.960 -28.833 11.507 1.00 46.68 ? 71 ASN B CA 1 ATOM 2971 C C . ASN B 2 71 ? 43.421 -28.780 11.105 1.00 43.57 ? 71 ASN B C 1 ATOM 2972 O O . ASN B 2 71 ? 44.076 -29.814 10.957 1.00 41.43 ? 71 ASN B O 1 ATOM 2973 C CB . ASN B 2 71 ? 41.668 -30.078 12.351 1.00 48.04 ? 71 ASN B CB 1 ATOM 2974 C CG . ASN B 2 71 ? 41.519 -29.762 13.819 1.00 51.01 ? 71 ASN B CG 1 ATOM 2975 O OD1 . ASN B 2 71 ? 42.346 -29.047 14.401 1.00 51.49 ? 71 ASN B OD1 1 ATOM 2976 N ND2 . ASN B 2 71 ? 40.453 -30.287 14.435 1.00 53.62 ? 71 ASN B ND2 1 ATOM 2977 N N . GLU B 2 72 ? 43.923 -27.561 10.933 1.00 43.58 ? 72 GLU B N 1 ATOM 2978 C CA . GLU B 2 72 ? 45.209 -27.329 10.291 1.00 41.29 ? 72 GLU B CA 1 ATOM 2979 C C . GLU B 2 72 ? 46.331 -28.159 10.905 1.00 39.22 ? 72 GLU B C 1 ATOM 2980 O O . GLU B 2 72 ? 46.471 -28.235 12.116 1.00 40.39 ? 72 GLU B O 1 ATOM 2981 C CB . GLU B 2 72 ? 45.580 -25.843 10.316 1.00 43.30 ? 72 GLU B CB 1 ATOM 2982 C CG . GLU B 2 72 ? 46.616 -25.471 9.257 1.00 42.08 ? 72 GLU B CG 1 ATOM 2983 C CD . GLU B 2 72 ? 47.240 -24.091 9.451 1.00 44.33 ? 72 GLU B CD 1 ATOM 2984 O OE1 . GLU B 2 72 ? 47.321 -23.598 10.600 1.00 46.63 ? 72 GLU B OE1 1 ATOM 2985 O OE2 . GLU B 2 72 ? 47.665 -23.492 8.438 1.00 44.46 ? 72 GLU B OE2 1 ATOM 2986 N N . VAL B 2 73 ? 47.122 -28.799 10.055 1.00 36.32 ? 73 VAL B N 1 ATOM 2987 C CA . VAL B 2 73 ? 48.292 -29.525 10.535 1.00 35.02 ? 73 VAL B CA 1 ATOM 2988 C C . VAL B 2 73 ? 49.326 -28.528 11.031 1.00 35.37 ? 73 VAL B C 1 ATOM 2989 O O . VAL B 2 73 ? 49.277 -27.345 10.687 1.00 35.54 ? 73 VAL B O 1 ATOM 2990 C CB . VAL B 2 73 ? 48.932 -30.415 9.450 1.00 32.69 ? 73 VAL B CB 1 ATOM 2991 C CG1 . VAL B 2 73 ? 47.932 -31.452 8.959 1.00 32.41 ? 73 VAL B CG1 1 ATOM 2992 C CG2 . VAL B 2 73 ? 49.485 -29.574 8.297 1.00 31.42 ? 73 VAL B CG2 1 ATOM 2993 N N . GLU B 2 74 ? 50.252 -29.026 11.841 1.00 35.56 ? 74 GLU B N 1 ATOM 2994 C CA . GLU B 2 74 ? 51.359 -28.231 12.358 1.00 36.67 ? 74 GLU B CA 1 ATOM 2995 C C . GLU B 2 74 ? 52.024 -27.418 11.231 1.00 35.66 ? 74 GLU B C 1 ATOM 2996 O O . GLU B 2 74 ? 52.188 -27.903 10.108 1.00 33.58 ? 74 GLU B O 1 ATOM 2997 C CB . GLU B 2 74 ? 52.361 -29.153 13.062 1.00 37.01 ? 74 GLU B CB 1 ATOM 2998 C CG . GLU B 2 74 ? 53.507 -28.444 13.767 1.00 38.94 ? 74 GLU B CG 1 ATOM 2999 C CD . GLU B 2 74 ? 54.722 -28.217 12.873 1.00 38.30 ? 74 GLU B CD 1 ATOM 3000 O OE1 . GLU B 2 74 ? 54.990 -29.064 11.974 1.00 36.86 ? 74 GLU B OE1 1 ATOM 3001 O OE2 . GLU B 2 74 ? 55.413 -27.187 13.082 1.00 39.69 ? 74 GLU B OE2 1 ATOM 3002 N N . LYS B 2 75 ? 52.396 -26.179 11.538 1.00 37.08 ? 75 LYS B N 1 ATOM 3003 C CA . LYS B 2 75 ? 52.809 -25.218 10.515 1.00 36.80 ? 75 LYS B CA 1 ATOM 3004 C C . LYS B 2 75 ? 54.023 -25.678 9.687 1.00 34.32 ? 75 LYS B C 1 ATOM 3005 O O . LYS B 2 75 ? 53.997 -25.610 8.467 1.00 32.65 ? 75 LYS B O 1 ATOM 3006 C CB . LYS B 2 75 ? 53.077 -23.851 11.153 1.00 40.33 ? 75 LYS B CB 1 ATOM 3007 C CG . LYS B 2 75 ? 52.820 -22.675 10.220 1.00 41.87 ? 75 LYS B CG 1 ATOM 3008 C CD . LYS B 2 75 ? 51.337 -22.310 10.145 1.00 43.28 ? 75 LYS B CD 1 ATOM 3009 C CE . LYS B 2 75 ? 51.082 -21.231 9.094 1.00 44.55 ? 75 LYS B CE 1 ATOM 3010 N NZ . LYS B 2 75 ? 50.046 -20.239 9.533 1.00 47.86 ? 75 LYS B NZ 1 ATOM 3011 N N . GLN B 2 76 ? 55.073 -26.158 10.343 1.00 34.10 ? 76 GLN B N 1 ATOM 3012 C CA . GLN B 2 76 ? 56.288 -26.567 9.635 1.00 32.67 ? 76 GLN B CA 1 ATOM 3013 C C . GLN B 2 76 ? 56.030 -27.660 8.598 1.00 29.90 ? 76 GLN B C 1 ATOM 3014 O O . GLN B 2 76 ? 56.428 -27.534 7.442 1.00 28.63 ? 76 GLN B O 1 ATOM 3015 C CB . GLN B 2 76 ? 57.382 -27.036 10.597 1.00 33.95 ? 76 GLN B CB 1 ATOM 3016 C CG . GLN B 2 76 ? 58.652 -27.433 9.855 1.00 33.70 ? 76 GLN B CG 1 ATOM 3017 C CD . GLN B 2 76 ? 59.881 -27.571 10.735 1.00 35.63 ? 76 GLN B CD 1 ATOM 3018 O OE1 . GLN B 2 76 ? 59.830 -28.173 11.800 1.00 36.43 ? 76 GLN B OE1 1 ATOM 3019 N NE2 . GLN B 2 76 ? 61.005 -27.041 10.264 1.00 36.65 ? 76 GLN B NE2 1 ATOM 3020 N N . ILE B 2 77 ? 55.377 -28.735 9.019 1.00 29.06 ? 77 ILE B N 1 ATOM 3021 C CA . ILE B 2 77 ? 55.087 -29.837 8.105 1.00 27.11 ? 77 ILE B CA 1 ATOM 3022 C C . ILE B 2 77 ? 54.122 -29.338 7.032 1.00 25.77 ? 77 ILE B C 1 ATOM 3023 O O . ILE B 2 77 ? 54.250 -29.701 5.869 1.00 24.33 ? 77 ILE B O 1 ATOM 3024 C CB . ILE B 2 77 ? 54.567 -31.101 8.848 1.00 27.25 ? 77 ILE B CB 1 ATOM 3025 C CG1 . ILE B 2 77 ? 54.549 -32.317 7.929 1.00 26.01 ? 77 ILE B CG1 1 ATOM 3026 C CG2 . ILE B 2 77 ? 53.185 -30.885 9.439 1.00 27.95 ? 77 ILE B CG2 1 ATOM 3027 C CD1 . ILE B 2 77 ? 55.922 -32.885 7.626 1.00 26.16 ? 77 ILE B CD1 1 ATOM 3028 N N . GLY B 2 78 ? 53.190 -28.479 7.425 1.00 26.62 ? 78 GLY B N 1 ATOM 3029 C CA . GLY B 2 78 ? 52.222 -27.898 6.499 1.00 26.19 ? 78 GLY B CA 1 ATOM 3030 C C . GLY B 2 78 ? 52.846 -27.094 5.377 1.00 25.61 ? 78 GLY B C 1 ATOM 3031 O O . GLY B 2 78 ? 52.442 -27.209 4.224 1.00 24.28 ? 78 GLY B O 1 ATOM 3032 N N . ASN B 2 79 ? 53.842 -26.286 5.718 1.00 26.80 ? 79 ASN B N 1 ATOM 3033 C CA . ASN B 2 79 ? 54.585 -25.520 4.727 1.00 26.79 ? 79 ASN B CA 1 ATOM 3034 C C . ASN B 2 79 ? 55.420 -26.397 3.796 1.00 25.14 ? 79 ASN B C 1 ATOM 3035 O O . ASN B 2 79 ? 55.541 -26.090 2.614 1.00 24.31 ? 79 ASN B O 1 ATOM 3036 C CB . ASN B 2 79 ? 55.471 -24.479 5.411 1.00 28.98 ? 79 ASN B CB 1 ATOM 3037 C CG . ASN B 2 79 ? 54.685 -23.274 5.891 1.00 31.16 ? 79 ASN B CG 1 ATOM 3038 O OD1 . ASN B 2 79 ? 53.682 -22.895 5.283 1.00 31.61 ? 79 ASN B OD1 1 ATOM 3039 N ND2 . ASN B 2 79 ? 55.135 -22.661 6.978 1.00 33.29 ? 79 ASN B ND2 1 ATOM 3040 N N . VAL B 2 80 ? 55.998 -27.473 4.321 1.00 24.85 ? 80 VAL B N 1 ATOM 3041 C CA . VAL B 2 80 ? 56.717 -28.423 3.472 1.00 23.90 ? 80 VAL B CA 1 ATOM 3042 C C . VAL B 2 80 ? 55.748 -29.054 2.472 1.00 22.60 ? 80 VAL B C 1 ATOM 3043 O O . VAL B 2 80 ? 56.035 -29.131 1.290 1.00 21.94 ? 80 VAL B O 1 ATOM 3044 C CB . VAL B 2 80 ? 57.403 -29.540 4.285 1.00 24.30 ? 80 VAL B CB 1 ATOM 3045 C CG1 . VAL B 2 80 ? 57.907 -30.643 3.362 1.00 23.32 ? 80 VAL B CG1 1 ATOM 3046 C CG2 . VAL B 2 80 ? 58.554 -28.979 5.107 1.00 26.09 ? 80 VAL B CG2 1 ATOM 3047 N N . ILE B 2 81 ? 54.597 -29.498 2.953 1.00 22.78 ? 81 ILE B N 1 ATOM 3048 C CA . ILE B 2 81 ? 53.548 -30.048 2.087 1.00 22.14 ? 81 ILE B CA 1 ATOM 3049 C C . ILE B 2 81 ? 53.106 -29.078 0.972 1.00 22.69 ? 81 ILE B C 1 ATOM 3050 O O . ILE B 2 81 ? 53.007 -29.464 -0.185 1.00 21.18 ? 81 ILE B O 1 ATOM 3051 C CB . ILE B 2 81 ? 52.332 -30.474 2.939 1.00 22.50 ? 81 ILE B CB 1 ATOM 3052 C CG1 . ILE B 2 81 ? 52.674 -31.755 3.713 1.00 22.57 ? 81 ILE B CG1 1 ATOM 3053 C CG2 . ILE B 2 81 ? 51.084 -30.675 2.081 1.00 22.14 ? 81 ILE B CG2 1 ATOM 3054 C CD1 . ILE B 2 81 ? 51.739 -32.063 4.862 1.00 23.55 ? 81 ILE B CD1 1 ATOM 3055 N N . ASN B 2 82 ? 52.835 -27.828 1.340 1.00 25.17 ? 82 ASN B N 1 ATOM 3056 C CA . ASN B 2 82 ? 52.381 -26.819 0.392 1.00 26.95 ? 82 ASN B CA 1 ATOM 3057 C C . ASN B 2 82 ? 53.443 -26.526 -0.678 1.00 25.43 ? 82 ASN B C 1 ATOM 3058 O O . ASN B 2 82 ? 53.150 -26.410 -1.859 1.00 23.94 ? 82 ASN B O 1 ATOM 3059 C CB . ASN B 2 82 ? 51.984 -25.536 1.148 1.00 31.41 ? 82 ASN B CB 1 ATOM 3060 C CG . ASN B 2 82 ? 50.589 -25.621 1.759 1.00 36.16 ? 82 ASN B CG 1 ATOM 3061 O OD1 . ASN B 2 82 ? 49.997 -26.702 1.876 1.00 34.71 ? 82 ASN B OD1 1 ATOM 3062 N ND2 . ASN B 2 82 ? 50.055 -24.461 2.156 1.00 43.81 ? 82 ASN B ND2 1 ATOM 3063 N N . TRP B 2 83 ? 54.685 -26.432 -0.233 1.00 25.47 ? 83 TRP B N 1 ATOM 3064 C CA . TRP B 2 83 ? 55.827 -26.232 -1.110 1.00 25.19 ? 83 TRP B CA 1 ATOM 3065 C C . TRP B 2 83 ? 55.939 -27.382 -2.104 1.00 22.83 ? 83 TRP B C 1 ATOM 3066 O O . TRP B 2 83 ? 56.114 -27.165 -3.294 1.00 21.86 ? 83 TRP B O 1 ATOM 3067 C CB . TRP B 2 83 ? 57.068 -26.129 -0.236 1.00 26.65 ? 83 TRP B CB 1 ATOM 3068 C CG . TRP B 2 83 ? 58.367 -26.078 -0.928 1.00 27.72 ? 83 TRP B CG 1 ATOM 3069 C CD1 . TRP B 2 83 ? 58.928 -25.002 -1.551 1.00 29.08 ? 83 TRP B CD1 1 ATOM 3070 C CD2 . TRP B 2 83 ? 59.320 -27.134 -1.005 1.00 27.93 ? 83 TRP B CD2 1 ATOM 3071 N NE1 . TRP B 2 83 ? 60.168 -25.330 -2.031 1.00 29.83 ? 83 TRP B NE1 1 ATOM 3072 C CE2 . TRP B 2 83 ? 60.435 -26.636 -1.710 1.00 29.40 ? 83 TRP B CE2 1 ATOM 3073 C CE3 . TRP B 2 83 ? 59.342 -28.457 -0.543 1.00 27.72 ? 83 TRP B CE3 1 ATOM 3074 C CZ2 . TRP B 2 83 ? 61.568 -27.416 -1.969 1.00 30.17 ? 83 TRP B CZ2 1 ATOM 3075 C CZ3 . TRP B 2 83 ? 60.462 -29.242 -0.807 1.00 28.49 ? 83 TRP B CZ3 1 ATOM 3076 C CH2 . TRP B 2 83 ? 61.565 -28.715 -1.510 1.00 29.78 ? 83 TRP B CH2 1 ATOM 3077 N N . THR B 2 84 ? 55.810 -28.602 -1.600 1.00 21.96 ? 84 THR B N 1 ATOM 3078 C CA . THR B 2 84 ? 55.865 -29.806 -2.433 1.00 20.75 ? 84 THR B CA 1 ATOM 3079 C C . THR B 2 84 ? 54.700 -29.845 -3.414 1.00 20.11 ? 84 THR B C 1 ATOM 3080 O O . THR B 2 84 ? 54.910 -30.019 -4.598 1.00 19.63 ? 84 THR B O 1 ATOM 3081 C CB . THR B 2 84 ? 55.885 -31.088 -1.579 1.00 20.64 ? 84 THR B CB 1 ATOM 3082 O OG1 . THR B 2 84 ? 57.065 -31.095 -0.765 1.00 21.19 ? 84 THR B OG1 1 ATOM 3083 C CG2 . THR B 2 84 ? 55.883 -32.349 -2.472 1.00 20.05 ? 84 THR B CG2 1 ATOM 3084 N N . ARG B 2 85 ? 53.476 -29.633 -2.938 1.00 20.50 ? 85 ARG B N 1 ATOM 3085 C CA . ARG B 2 85 ? 52.330 -29.585 -3.839 1.00 20.44 ? 85 ARG B CA 1 ATOM 3086 C C . ARG B 2 85 ? 52.478 -28.506 -4.930 1.00 20.23 ? 85 ARG B C 1 ATOM 3087 O O . ARG B 2 85 ? 52.266 -28.771 -6.109 1.00 19.51 ? 85 ARG B O 1 ATOM 3088 C CB . ARG B 2 85 ? 51.042 -29.373 -3.054 1.00 21.91 ? 85 ARG B CB 1 ATOM 3089 C CG . ARG B 2 85 ? 49.780 -29.418 -3.896 1.00 22.73 ? 85 ARG B CG 1 ATOM 3090 C CD . ARG B 2 85 ? 48.571 -29.010 -3.079 1.00 24.71 ? 85 ARG B CD 1 ATOM 3091 N NE . ARG B 2 85 ? 48.325 -29.987 -2.025 1.00 25.70 ? 85 ARG B NE 1 ATOM 3092 C CZ . ARG B 2 85 ? 48.301 -29.743 -0.712 1.00 26.89 ? 85 ARG B CZ 1 ATOM 3093 N NH1 . ARG B 2 85 ? 48.472 -28.510 -0.221 1.00 28.03 ? 85 ARG B NH1 1 ATOM 3094 N NH2 . ARG B 2 85 ? 48.064 -30.752 0.121 1.00 26.88 ? 85 ARG B NH2 1 ATOM 3095 N N . ASP B 2 86 ? 52.836 -27.294 -4.536 1.00 20.83 ? 86 ASP B N 1 ATOM 3096 C CA . ASP B 2 86 ? 53.041 -26.218 -5.499 1.00 21.27 ? 86 ASP B CA 1 ATOM 3097 C C . ASP B 2 86 ? 54.135 -26.574 -6.529 1.00 20.23 ? 86 ASP B C 1 ATOM 3098 O O . ASP B 2 86 ? 53.983 -26.297 -7.712 1.00 19.72 ? 86 ASP B O 1 ATOM 3099 C CB . ASP B 2 86 ? 53.372 -24.910 -4.777 1.00 23.04 ? 86 ASP B CB 1 ATOM 3100 C CG . ASP B 2 86 ? 52.209 -24.377 -3.956 1.00 24.61 ? 86 ASP B CG 1 ATOM 3101 O OD1 . ASP B 2 86 ? 51.101 -24.939 -4.020 1.00 24.80 ? 86 ASP B OD1 1 ATOM 3102 O OD2 . ASP B 2 86 ? 52.397 -23.375 -3.236 1.00 26.77 ? 86 ASP B OD2 1 ATOM 3103 N N . SER B 2 87 ? 55.210 -27.209 -6.076 1.00 19.77 ? 87 SER B N 1 ATOM 3104 C CA . SER B 2 87 ? 56.271 -27.660 -6.976 1.00 19.68 ? 87 SER B CA 1 ATOM 3105 C C . SER B 2 87 ? 55.733 -28.669 -8.006 1.00 18.98 ? 87 SER B C 1 ATOM 3106 O O . SER B 2 87 ? 56.019 -28.567 -9.203 1.00 18.78 ? 87 SER B O 1 ATOM 3107 C CB . SER B 2 87 ? 57.405 -28.314 -6.187 1.00 19.92 ? 87 SER B CB 1 ATOM 3108 O OG . SER B 2 87 ? 58.006 -27.417 -5.277 1.00 21.14 ? 87 SER B OG 1 ATOM 3109 N N . ILE B 2 88 ? 54.948 -29.629 -7.528 1.00 18.37 ? 88 ILE B N 1 ATOM 3110 C CA . ILE B 2 88 ? 54.306 -30.604 -8.400 1.00 18.12 ? 88 ILE B CA 1 ATOM 3111 C C . ILE B 2 88 ? 53.315 -29.944 -9.362 1.00 17.87 ? 88 ILE B C 1 ATOM 3112 O O . ILE B 2 88 ? 53.290 -30.268 -10.539 1.00 17.54 ? 88 ILE B O 1 ATOM 3113 C CB . ILE B 2 88 ? 53.576 -31.694 -7.582 1.00 18.43 ? 88 ILE B CB 1 ATOM 3114 C CG1 . ILE B 2 88 ? 54.584 -32.524 -6.768 1.00 19.06 ? 88 ILE B CG1 1 ATOM 3115 C CG2 . ILE B 2 88 ? 52.747 -32.612 -8.480 1.00 18.47 ? 88 ILE B CG2 1 ATOM 3116 C CD1 . ILE B 2 88 ? 55.670 -33.196 -7.585 1.00 19.34 ? 88 ILE B CD1 1 ATOM 3117 N N . THR B 2 89 ? 52.491 -29.034 -8.862 1.00 18.28 ? 89 THR B N 1 ATOM 3118 C CA . THR B 2 89 ? 51.584 -28.275 -9.724 1.00 18.89 ? 89 THR B CA 1 ATOM 3119 C C . THR B 2 89 ? 52.342 -27.573 -10.859 1.00 19.28 ? 89 THR B C 1 ATOM 3120 O O . THR B 2 89 ? 51.869 -27.509 -11.997 1.00 19.53 ? 89 THR B O 1 ATOM 3121 C CB . THR B 2 89 ? 50.810 -27.236 -8.918 1.00 19.95 ? 89 THR B CB 1 ATOM 3122 O OG1 . THR B 2 89 ? 49.918 -27.910 -8.028 1.00 20.36 ? 89 THR B OG1 1 ATOM 3123 C CG2 . THR B 2 89 ? 50.008 -26.309 -9.821 1.00 21.13 ? 89 THR B CG2 1 ATOM 3124 N N . GLU B 2 90 ? 53.511 -27.044 -10.533 1.00 19.44 ? 90 GLU B N 1 ATOM 3125 C CA . GLU B 2 90 ? 54.319 -26.338 -11.502 1.00 20.41 ? 90 GLU B CA 1 ATOM 3126 C C . GLU B 2 90 ? 54.830 -27.296 -12.600 1.00 19.38 ? 90 GLU B C 1 ATOM 3127 O O . GLU B 2 90 ? 54.801 -26.961 -13.782 1.00 19.42 ? 90 GLU B O 1 ATOM 3128 C CB . GLU B 2 90 ? 55.467 -25.661 -10.772 1.00 21.87 ? 90 GLU B CB 1 ATOM 3129 C CG . GLU B 2 90 ? 55.845 -24.317 -11.314 1.00 24.27 ? 90 GLU B CG 1 ATOM 3130 C CD . GLU B 2 90 ? 54.744 -23.265 -11.251 1.00 26.07 ? 90 GLU B CD 1 ATOM 3131 O OE1 . GLU B 2 90 ? 53.680 -23.476 -10.631 1.00 26.81 ? 90 GLU B OE1 1 ATOM 3132 O OE2 . GLU B 2 90 ? 54.943 -22.194 -11.864 1.00 28.44 ? 90 GLU B OE2 1 ATOM 3133 N N . VAL B 2 91 ? 55.260 -28.494 -12.213 1.00 18.14 ? 91 VAL B N 1 ATOM 3134 C CA . VAL B 2 91 ? 55.642 -29.502 -13.188 1.00 17.90 ? 91 VAL B CA 1 ATOM 3135 C C . VAL B 2 91 ? 54.487 -29.901 -14.123 1.00 17.70 ? 91 VAL B C 1 ATOM 3136 O O . VAL B 2 91 ? 54.655 -29.926 -15.345 1.00 17.98 ? 91 VAL B O 1 ATOM 3137 C CB . VAL B 2 91 ? 56.199 -30.777 -12.513 1.00 17.72 ? 91 VAL B CB 1 ATOM 3138 C CG1 . VAL B 2 91 ? 56.382 -31.896 -13.530 1.00 17.75 ? 91 VAL B CG1 1 ATOM 3139 C CG2 . VAL B 2 91 ? 57.523 -30.474 -11.838 1.00 18.38 ? 91 VAL B CG2 1 ATOM 3140 N N . TRP B 2 92 ? 53.325 -30.217 -13.563 1.00 17.36 ? 92 TRP B N 1 ATOM 3141 C CA . TRP B 2 92 ? 52.187 -30.641 -14.385 1.00 17.53 ? 92 TRP B CA 1 ATOM 3142 C C . TRP B 2 92 ? 51.634 -29.545 -15.278 1.00 18.16 ? 92 TRP B C 1 ATOM 3143 O O . TRP B 2 92 ? 51.231 -29.825 -16.398 1.00 18.38 ? 92 TRP B O 1 ATOM 3144 C CB . TRP B 2 92 ? 51.073 -31.230 -13.532 1.00 17.69 ? 92 TRP B CB 1 ATOM 3145 C CG . TRP B 2 92 ? 51.421 -32.600 -13.082 1.00 17.74 ? 92 TRP B CG 1 ATOM 3146 C CD1 . TRP B 2 92 ? 51.654 -33.005 -11.811 1.00 17.50 ? 92 TRP B CD1 1 ATOM 3147 C CD2 . TRP B 2 92 ? 51.633 -33.739 -13.916 1.00 18.07 ? 92 TRP B CD2 1 ATOM 3148 N NE1 . TRP B 2 92 ? 51.965 -34.332 -11.791 1.00 17.94 ? 92 TRP B NE1 1 ATOM 3149 C CE2 . TRP B 2 92 ? 51.969 -34.810 -13.072 1.00 18.30 ? 92 TRP B CE2 1 ATOM 3150 C CE3 . TRP B 2 92 ? 51.550 -33.962 -15.293 1.00 18.61 ? 92 TRP B CE3 1 ATOM 3151 C CZ2 . TRP B 2 92 ? 52.235 -36.090 -13.555 1.00 19.01 ? 92 TRP B CZ2 1 ATOM 3152 C CZ3 . TRP B 2 92 ? 51.813 -35.244 -15.778 1.00 19.26 ? 92 TRP B CZ3 1 ATOM 3153 C CH2 . TRP B 2 92 ? 52.150 -36.284 -14.909 1.00 19.54 ? 92 TRP B CH2 1 ATOM 3154 N N . SER B 2 93 ? 51.617 -28.308 -14.789 1.00 18.70 ? 93 SER B N 1 ATOM 3155 C CA . SER B 2 93 ? 51.152 -27.171 -15.602 1.00 19.90 ? 93 SER B CA 1 ATOM 3156 C C . SER B 2 93 ? 52.061 -26.984 -16.822 1.00 20.16 ? 93 SER B C 1 ATOM 3157 O O . SER B 2 93 ? 51.592 -26.674 -17.919 1.00 20.59 ? 93 SER B O 1 ATOM 3158 C CB . SER B 2 93 ? 51.125 -25.900 -14.766 1.00 20.78 ? 93 SER B CB 1 ATOM 3159 O OG . SER B 2 93 ? 50.212 -26.010 -13.685 1.00 21.10 ? 93 SER B OG 1 ATOM 3160 N N . TYR B 2 94 ? 53.361 -27.196 -16.613 1.00 19.65 ? 94 TYR B N 1 ATOM 3161 C CA . TYR B 2 94 ? 54.338 -27.153 -17.685 1.00 20.34 ? 94 TYR B CA 1 ATOM 3162 C C . TYR B 2 94 ? 54.107 -28.323 -18.645 1.00 20.23 ? 94 TYR B C 1 ATOM 3163 O O . TYR B 2 94 ? 53.984 -28.122 -19.852 1.00 20.70 ? 94 TYR B O 1 ATOM 3164 C CB . TYR B 2 94 ? 55.763 -27.184 -17.101 1.00 20.56 ? 94 TYR B CB 1 ATOM 3165 C CG . TYR B 2 94 ? 56.868 -27.453 -18.103 1.00 21.51 ? 94 TYR B CG 1 ATOM 3166 C CD1 . TYR B 2 94 ? 57.440 -26.422 -18.837 1.00 23.03 ? 94 TYR B CD1 1 ATOM 3167 C CD2 . TYR B 2 94 ? 57.348 -28.734 -18.299 1.00 21.49 ? 94 TYR B CD2 1 ATOM 3168 C CE1 . TYR B 2 94 ? 58.450 -26.670 -19.751 1.00 24.06 ? 94 TYR B CE1 1 ATOM 3169 C CE2 . TYR B 2 94 ? 58.359 -28.994 -19.203 1.00 22.44 ? 94 TYR B CE2 1 ATOM 3170 C CZ . TYR B 2 94 ? 58.902 -27.964 -19.933 1.00 23.83 ? 94 TYR B CZ 1 ATOM 3171 O OH . TYR B 2 94 ? 59.915 -28.236 -20.838 1.00 25.23 ? 94 TYR B OH 1 ATOM 3172 N N . ASN B 2 95 ? 54.050 -29.538 -18.100 1.00 19.76 ? 95 ASN B N 1 ATOM 3173 C CA . ASN B 2 95 ? 53.813 -30.738 -18.896 1.00 20.09 ? 95 ASN B CA 1 ATOM 3174 C C . ASN B 2 95 ? 52.579 -30.600 -19.773 1.00 20.66 ? 95 ASN B C 1 ATOM 3175 O O . ASN B 2 95 ? 52.628 -30.886 -20.963 1.00 21.27 ? 95 ASN B O 1 ATOM 3176 C CB . ASN B 2 95 ? 53.650 -31.969 -18.002 1.00 19.93 ? 95 ASN B CB 1 ATOM 3177 C CG . ASN B 2 95 ? 54.962 -32.455 -17.415 1.00 20.29 ? 95 ASN B CG 1 ATOM 3178 O OD1 . ASN B 2 95 ? 56.041 -31.964 -17.745 1.00 21.06 ? 95 ASN B OD1 1 ATOM 3179 N ND2 . ASN B 2 95 ? 54.872 -33.446 -16.547 1.00 20.54 ? 95 ASN B ND2 1 ATOM 3180 N N . ALA B 2 96 ? 51.482 -30.154 -19.175 1.00 20.65 ? 96 ALA B N 1 ATOM 3181 C CA . ALA B 2 96 ? 50.210 -30.004 -19.888 1.00 21.79 ? 96 ALA B CA 1 ATOM 3182 C C . ALA B 2 96 ? 50.294 -29.000 -21.035 1.00 22.80 ? 96 ALA B C 1 ATOM 3183 O O . ALA B 2 96 ? 49.804 -29.267 -22.135 1.00 23.19 ? 96 ALA B O 1 ATOM 3184 C CB . ALA B 2 96 ? 49.111 -29.600 -18.922 1.00 22.03 ? 96 ALA B CB 1 ATOM 3185 N N . GLU B 2 97 ? 50.909 -27.846 -20.762 1.00 23.22 ? 97 GLU B N 1 ATOM 3186 C CA . GLU B 2 97 ? 51.091 -26.786 -21.757 1.00 24.71 ? 97 GLU B CA 1 ATOM 3187 C C . GLU B 2 97 ? 51.975 -27.244 -22.917 1.00 24.33 ? 97 GLU B C 1 ATOM 3188 O O . GLU B 2 97 ? 51.670 -26.973 -24.078 1.00 25.29 ? 97 GLU B O 1 ATOM 3189 C CB . GLU B 2 97 ? 51.745 -25.562 -21.104 1.00 25.75 ? 97 GLU B CB 1 ATOM 3190 C CG . GLU B 2 97 ? 51.897 -24.346 -22.016 1.00 28.21 ? 97 GLU B CG 1 ATOM 3191 C CD . GLU B 2 97 ? 50.777 -23.328 -21.871 1.00 30.56 ? 97 GLU B CD 1 ATOM 3192 O OE1 . GLU B 2 97 ? 50.232 -23.198 -20.755 1.00 30.87 ? 97 GLU B OE1 1 ATOM 3193 O OE2 . GLU B 2 97 ? 50.459 -22.632 -22.872 1.00 33.11 ? 97 GLU B OE2 1 ATOM 3194 N N . LEU B 2 98 ? 53.076 -27.916 -22.593 1.00 22.91 ? 98 LEU B N 1 ATOM 3195 C CA . LEU B 2 98 ? 54.013 -28.376 -23.604 1.00 23.24 ? 98 LEU B CA 1 ATOM 3196 C C . LEU B 2 98 ? 53.422 -29.515 -24.425 1.00 23.48 ? 98 LEU B C 1 ATOM 3197 O O . LEU B 2 98 ? 53.630 -29.584 -25.639 1.00 24.37 ? 98 LEU B O 1 ATOM 3198 C CB . LEU B 2 98 ? 55.330 -28.821 -22.964 1.00 22.78 ? 98 LEU B CB 1 ATOM 3199 C CG . LEU B 2 98 ? 56.413 -29.349 -23.923 1.00 23.78 ? 98 LEU B CG 1 ATOM 3200 C CD1 . LEU B 2 98 ? 56.803 -28.293 -24.949 1.00 24.95 ? 98 LEU B CD1 1 ATOM 3201 C CD2 . LEU B 2 98 ? 57.653 -29.824 -23.170 1.00 23.78 ? 98 LEU B CD2 1 ATOM 3202 N N . LEU B 2 99 ? 52.687 -30.405 -23.765 1.00 22.78 ? 99 LEU B N 1 ATOM 3203 C CA . LEU B 2 99 ? 52.070 -31.552 -24.445 1.00 23.41 ? 99 LEU B CA 1 ATOM 3204 C C . LEU B 2 99 ? 51.107 -31.075 -25.518 1.00 24.63 ? 99 LEU B C 1 ATOM 3205 O O . LEU B 2 99 ? 51.159 -31.514 -26.661 1.00 25.45 ? 99 LEU B O 1 ATOM 3206 C CB . LEU B 2 99 ? 51.315 -32.424 -23.440 1.00 23.01 ? 99 LEU B CB 1 ATOM 3207 C CG . LEU B 2 99 ? 50.412 -33.538 -23.985 1.00 24.22 ? 99 LEU B CG 1 ATOM 3208 C CD1 . LEU B 2 99 ? 51.235 -34.688 -24.548 1.00 24.66 ? 99 LEU B CD1 1 ATOM 3209 C CD2 . LEU B 2 99 ? 49.496 -34.030 -22.878 1.00 24.15 ? 99 LEU B CD2 1 ATOM 3210 N N . VAL B 2 100 ? 50.237 -30.153 -25.137 1.00 24.97 ? 100 VAL B N 1 ATOM 3211 C CA . VAL B 2 100 ? 49.194 -29.671 -26.035 1.00 26.67 ? 100 VAL B CA 1 ATOM 3212 C C . VAL B 2 100 ? 49.788 -28.909 -27.233 1.00 27.69 ? 100 VAL B C 1 ATOM 3213 O O . VAL B 2 100 ? 49.373 -29.124 -28.365 1.00 28.98 ? 100 VAL B O 1 ATOM 3214 C CB . VAL B 2 100 ? 48.153 -28.843 -25.265 1.00 27.17 ? 100 VAL B CB 1 ATOM 3215 C CG1 . VAL B 2 100 ? 47.155 -28.194 -26.209 1.00 29.45 ? 100 VAL B CG1 1 ATOM 3216 C CG2 . VAL B 2 100 ? 47.408 -29.753 -24.293 1.00 26.97 ? 100 VAL B CG2 1 ATOM 3217 N N . ALA B 2 101 ? 50.773 -28.056 -26.984 1.00 27.24 ? 101 ALA B N 1 ATOM 3218 C CA . ALA B 2 101 ? 51.414 -27.290 -28.051 1.00 28.63 ? 101 ALA B CA 1 ATOM 3219 C C . ALA B 2 101 ? 52.158 -28.198 -29.046 1.00 29.36 ? 101 ALA B C 1 ATOM 3220 O O . ALA B 2 101 ? 52.039 -28.022 -30.259 1.00 30.57 ? 101 ALA B O 1 ATOM 3221 C CB . ALA B 2 101 ? 52.363 -26.265 -27.454 1.00 28.14 ? 101 ALA B CB 1 ATOM 3222 N N . MET B 2 102 ? 52.914 -29.162 -28.517 1.00 28.79 ? 102 MET B N 1 ATOM 3223 C CA . MET B 2 102 ? 53.601 -30.164 -29.329 1.00 30.22 ? 102 MET B CA 1 ATOM 3224 C C . MET B 2 102 ? 52.624 -30.998 -30.149 1.00 30.38 ? 102 MET B C 1 ATOM 3225 O O . MET B 2 102 ? 52.830 -31.189 -31.350 1.00 31.63 ? 102 MET B O 1 ATOM 3226 C CB . MET B 2 102 ? 54.453 -31.081 -28.438 1.00 31.34 ? 102 MET B CB 1 ATOM 3227 C CG . MET B 2 102 ? 55.220 -32.177 -29.171 1.00 34.27 ? 102 MET B CG 1 ATOM 3228 S SD . MET B 2 102 ? 54.341 -33.754 -29.330 1.00 39.00 ? 102 MET B SD 1 ATOM 3229 C CE . MET B 2 102 ? 54.573 -34.449 -27.688 1.00 36.53 ? 102 MET B CE 1 ATOM 3230 N N . GLU B 2 103 ? 51.567 -31.501 -29.511 1.00 29.09 ? 103 GLU B N 1 ATOM 3231 C CA . GLU B 2 103 ? 50.559 -32.295 -30.225 1.00 29.99 ? 103 GLU B CA 1 ATOM 3232 C C . GLU B 2 103 ? 49.896 -31.501 -31.347 1.00 30.99 ? 103 GLU B C 1 ATOM 3233 O O . GLU B 2 103 ? 49.687 -32.027 -32.445 1.00 32.23 ? 103 GLU B O 1 ATOM 3234 C CB . GLU B 2 103 ? 49.470 -32.800 -29.279 1.00 29.89 ? 103 GLU B CB 1 ATOM 3235 C CG . GLU B 2 103 ? 49.940 -33.835 -28.272 1.00 29.01 ? 103 GLU B CG 1 ATOM 3236 C CD . GLU B 2 103 ? 50.159 -35.213 -28.865 1.00 30.44 ? 103 GLU B CD 1 ATOM 3237 O OE1 . GLU B 2 103 ? 50.067 -35.396 -30.095 1.00 32.27 ? 103 GLU B OE1 1 ATOM 3238 O OE2 . GLU B 2 103 ? 50.454 -36.130 -28.080 1.00 30.44 ? 103 GLU B OE2 1 ATOM 3239 N N . ASN B 2 104 ? 49.570 -30.241 -31.054 1.00 30.21 ? 104 ASN B N 1 ATOM 3240 C CA . ASN B 2 104 ? 48.856 -29.381 -31.995 1.00 31.70 ? 104 ASN B CA 1 ATOM 3241 C C . ASN B 2 104 ? 49.729 -29.057 -33.197 1.00 32.40 ? 104 ASN B C 1 ATOM 3242 O O . ASN B 2 104 ? 49.250 -29.057 -34.324 1.00 34.27 ? 104 ASN B O 1 ATOM 3243 C CB . ASN B 2 104 ? 48.390 -28.095 -31.308 1.00 31.58 ? 104 ASN B CB 1 ATOM 3244 C CG . ASN B 2 104 ? 47.282 -28.337 -30.294 1.00 31.42 ? 104 ASN B CG 1 ATOM 3245 O OD1 . ASN B 2 104 ? 46.736 -29.438 -30.185 1.00 31.42 ? 104 ASN B OD1 1 ATOM 3246 N ND2 . ASN B 2 104 ? 46.934 -27.296 -29.555 1.00 31.53 ? 104 ASN B ND2 1 ATOM 3247 N N . GLN B 2 105 ? 51.013 -28.801 -32.949 1.00 31.44 ? 105 GLN B N 1 ATOM 3248 C CA . GLN B 2 105 ? 51.981 -28.614 -34.023 1.00 32.80 ? 105 GLN B CA 1 ATOM 3249 C C . GLN B 2 105 ? 51.991 -29.836 -34.935 1.00 32.78 ? 105 GLN B C 1 ATOM 3250 O O . GLN B 2 105 ? 51.959 -29.706 -36.158 1.00 33.74 ? 105 GLN B O 1 ATOM 3251 C CB . GLN B 2 105 ? 53.387 -28.376 -33.456 1.00 33.69 ? 105 GLN B CB 1 ATOM 3252 C CG . GLN B 2 105 ? 54.382 -27.788 -34.453 1.00 36.04 ? 105 GLN B CG 1 ATOM 3253 C CD . GLN B 2 105 ? 54.241 -26.283 -34.624 1.00 37.64 ? 105 GLN B CD 1 ATOM 3254 O OE1 . GLN B 2 105 ? 54.049 -25.547 -33.653 1.00 37.62 ? 105 GLN B OE1 1 ATOM 3255 N NE2 . GLN B 2 105 ? 54.366 -25.817 -35.855 1.00 39.48 ? 105 GLN B NE2 1 ATOM 3256 N N . HIS B 2 106 ? 52.025 -31.021 -34.331 1.00 32.03 ? 106 HIS B N 1 ATOM 3257 C CA . HIS B 2 106 ? 52.091 -32.274 -35.086 1.00 32.65 ? 106 HIS B CA 1 ATOM 3258 C C . HIS B 2 106 ? 50.779 -32.561 -35.829 1.00 32.35 ? 106 HIS B C 1 ATOM 3259 O O . HIS B 2 106 ? 50.797 -33.004 -36.978 1.00 33.22 ? 106 HIS B O 1 ATOM 3260 C CB . HIS B 2 106 ? 52.462 -33.429 -34.155 1.00 32.81 ? 106 HIS B CB 1 ATOM 3261 C CG . HIS B 2 106 ? 52.636 -34.739 -34.854 1.00 34.40 ? 106 HIS B CG 1 ATOM 3262 N ND1 . HIS B 2 106 ? 51.710 -35.758 -34.771 1.00 34.64 ? 106 HIS B ND1 1 ATOM 3263 C CD2 . HIS B 2 106 ? 53.629 -35.197 -35.653 1.00 36.42 ? 106 HIS B CD2 1 ATOM 3264 C CE1 . HIS B 2 106 ? 52.127 -36.789 -35.485 1.00 36.62 ? 106 HIS B CE1 1 ATOM 3265 N NE2 . HIS B 2 106 ? 53.287 -36.474 -36.034 1.00 37.65 ? 106 HIS B NE2 1 ATOM 3266 N N . THR B 2 107 ? 49.651 -32.278 -35.181 1.00 31.41 ? 107 THR B N 1 ATOM 3267 C CA . THR B 2 107 ? 48.322 -32.466 -35.785 1.00 31.84 ? 107 THR B CA 1 ATOM 3268 C C . THR B 2 107 ? 48.134 -31.620 -37.047 1.00 32.84 ? 107 THR B C 1 ATOM 3269 O O . THR B 2 107 ? 47.632 -32.107 -38.067 1.00 33.72 ? 107 THR B O 1 ATOM 3270 C CB . THR B 2 107 ? 47.203 -32.148 -34.771 1.00 31.36 ? 107 THR B CB 1 ATOM 3271 O OG1 . THR B 2 107 ? 47.182 -33.162 -33.753 1.00 30.92 ? 107 THR B OG1 1 ATOM 3272 C CG2 . THR B 2 107 ? 45.834 -32.087 -35.445 1.00 32.65 ? 107 THR B CG2 1 ATOM 3273 N N . ILE B 2 108 ? 48.545 -30.362 -36.974 1.00 33.04 ? 108 ILE B N 1 ATOM 3274 C CA . ILE B 2 108 ? 48.452 -29.450 -38.108 1.00 34.62 ? 108 ILE B CA 1 ATOM 3275 C C . ILE B 2 108 ? 49.340 -29.919 -39.261 1.00 35.38 ? 108 ILE B C 1 ATOM 3276 O O . ILE B 2 108 ? 48.906 -29.937 -40.411 1.00 36.34 ? 108 ILE B O 1 ATOM 3277 C CB . ILE B 2 108 ? 48.826 -28.014 -37.678 1.00 35.40 ? 108 ILE B CB 1 ATOM 3278 C CG1 . ILE B 2 108 ? 47.714 -27.458 -36.785 1.00 35.55 ? 108 ILE B CG1 1 ATOM 3279 C CG2 . ILE B 2 108 ? 49.054 -27.104 -38.880 1.00 37.53 ? 108 ILE B CG2 1 ATOM 3280 C CD1 . ILE B 2 108 ? 48.018 -26.117 -36.151 1.00 36.58 ? 108 ILE B CD1 1 ATOM 3281 N N . ASP B 2 109 ? 50.580 -30.288 -38.945 1.00 35.27 ? 109 ASP B N 1 ATOM 3282 C CA . ASP B 2 109 ? 51.530 -30.775 -39.950 1.00 36.63 ? 109 ASP B CA 1 ATOM 3283 C C . ASP B 2 109 ? 51.085 -32.103 -40.546 1.00 36.72 ? 109 ASP B C 1 ATOM 3284 O O . ASP B 2 109 ? 51.226 -32.344 -41.746 1.00 37.89 ? 109 ASP B O 1 ATOM 3285 C CB . ASP B 2 109 ? 52.929 -30.947 -39.342 1.00 37.17 ? 109 ASP B CB 1 ATOM 3286 C CG . ASP B 2 109 ? 53.599 -29.622 -39.017 1.00 38.28 ? 109 ASP B CG 1 ATOM 3287 O OD1 . ASP B 2 109 ? 53.368 -28.628 -39.751 1.00 39.54 ? 109 ASP B OD1 1 ATOM 3288 O OD2 . ASP B 2 109 ? 54.366 -29.580 -38.027 1.00 38.53 ? 109 ASP B OD2 1 ATOM 3289 N N . LEU B 2 110 ? 50.556 -32.963 -39.692 1.00 35.90 ? 110 LEU B N 1 ATOM 3290 C CA . LEU B 2 110 ? 50.046 -34.261 -40.108 1.00 36.62 ? 110 LEU B CA 1 ATOM 3291 C C . LEU B 2 110 ? 48.932 -34.114 -41.135 1.00 37.25 ? 110 LEU B C 1 ATOM 3292 O O . LEU B 2 110 ? 48.902 -34.836 -42.132 1.00 38.42 ? 110 LEU B O 1 ATOM 3293 C CB . LEU B 2 110 ? 49.557 -34.998 -38.872 1.00 36.16 ? 110 LEU B CB 1 ATOM 3294 C CG . LEU B 2 110 ? 48.818 -36.317 -38.947 1.00 37.39 ? 110 LEU B CG 1 ATOM 3295 C CD1 . LEU B 2 110 ? 48.970 -36.942 -37.568 1.00 37.28 ? 110 LEU B CD1 1 ATOM 3296 C CD2 . LEU B 2 110 ? 47.348 -36.135 -39.313 1.00 37.83 ? 110 LEU B CD2 1 ATOM 3297 N N . ALA B 2 111 ? 48.030 -33.167 -40.897 1.00 36.85 ? 111 ALA B N 1 ATOM 3298 C CA . ALA B 2 111 ? 46.966 -32.867 -41.855 1.00 38.05 ? 111 ALA B CA 1 ATOM 3299 C C . ALA B 2 111 ? 47.523 -32.272 -43.144 1.00 39.08 ? 111 ALA B C 1 ATOM 3300 O O . ALA B 2 111 ? 47.018 -32.551 -44.234 1.00 40.22 ? 111 ALA B O 1 ATOM 3301 C CB . ALA B 2 111 ? 45.954 -31.923 -41.238 1.00 38.15 ? 111 ALA B CB 1 ATOM 3302 N N . ASP B 2 112 ? 48.564 -31.450 -43.009 1.00 38.96 ? 112 ASP B N 1 ATOM 3303 C CA . ASP B 2 112 ? 49.226 -30.817 -44.154 1.00 40.38 ? 112 ASP B CA 1 ATOM 3304 C C . ASP B 2 112 ? 49.796 -31.893 -45.073 1.00 41.03 ? 112 ASP B C 1 ATOM 3305 O O . ASP B 2 112 ? 49.589 -31.859 -46.282 1.00 42.16 ? 112 ASP B O 1 ATOM 3306 C CB . ASP B 2 112 ? 50.344 -29.881 -43.664 1.00 40.67 ? 112 ASP B CB 1 ATOM 3307 C CG . ASP B 2 112 ? 50.855 -28.920 -44.743 1.00 42.88 ? 112 ASP B CG 1 ATOM 3308 O OD1 . ASP B 2 112 ? 50.216 -28.769 -45.802 1.00 43.97 ? 112 ASP B OD1 1 ATOM 3309 O OD2 . ASP B 2 112 ? 51.915 -28.295 -44.513 1.00 43.94 ? 112 ASP B OD2 1 ATOM 3310 N N . SER B 2 113 ? 50.489 -32.862 -44.482 1.00 40.58 ? 113 SER B N 1 ATOM 3311 C CA . SER B 2 113 ? 51.132 -33.928 -45.246 1.00 41.87 ? 113 SER B CA 1 ATOM 3312 C C . SER B 2 113 ? 50.123 -34.825 -45.962 1.00 42.56 ? 113 SER B C 1 ATOM 3313 O O . SER B 2 113 ? 50.363 -35.237 -47.098 1.00 43.88 ? 113 SER B O 1 ATOM 3314 C CB . SER B 2 113 ? 52.019 -34.786 -44.341 1.00 41.92 ? 113 SER B CB 1 ATOM 3315 O OG . SER B 2 113 ? 51.246 -35.743 -43.651 1.00 41.55 ? 113 SER B OG 1 ATOM 3316 N N . GLU B 2 114 ? 49.009 -35.137 -45.301 1.00 42.00 ? 114 GLU B N 1 ATOM 3317 C CA . GLU B 2 114 ? 47.979 -35.971 -45.922 1.00 43.34 ? 114 GLU B CA 1 ATOM 3318 C C . GLU B 2 114 ? 47.439 -35.302 -47.170 1.00 44.35 ? 114 GLU B C 1 ATOM 3319 O O . GLU B 2 114 ? 47.181 -35.972 -48.173 1.00 45.87 ? 114 GLU B O 1 ATOM 3320 C CB . GLU B 2 114 ? 46.832 -36.261 -44.957 1.00 43.21 ? 114 GLU B CB 1 ATOM 3321 C CG . GLU B 2 114 ? 47.196 -37.183 -43.801 1.00 42.96 ? 114 GLU B CG 1 ATOM 3322 C CD . GLU B 2 114 ? 47.554 -38.596 -44.226 1.00 44.98 ? 114 GLU B CD 1 ATOM 3323 O OE1 . GLU B 2 114 ? 47.065 -39.058 -45.272 1.00 46.77 ? 114 GLU B OE1 1 ATOM 3324 O OE2 . GLU B 2 114 ? 48.323 -39.255 -43.492 1.00 45.31 ? 114 GLU B OE2 1 ATOM 3325 N N . MET B 2 115 ? 47.275 -33.981 -47.104 1.00 43.94 ? 115 MET B N 1 ATOM 3326 C CA . MET B 2 115 ? 46.878 -33.190 -48.271 1.00 45.39 ? 115 MET B CA 1 ATOM 3327 C C . MET B 2 115 ? 47.913 -33.329 -49.381 1.00 46.18 ? 115 MET B C 1 ATOM 3328 O O . MET B 2 115 ? 47.560 -33.538 -50.544 1.00 47.64 ? 115 MET B O 1 ATOM 3329 C CB . MET B 2 115 ? 46.718 -31.713 -47.888 1.00 45.35 ? 115 MET B CB 1 ATOM 3330 C CG . MET B 2 115 ? 46.392 -30.755 -49.031 1.00 47.31 ? 115 MET B CG 1 ATOM 3331 S SD . MET B 2 115 ? 44.643 -30.726 -49.472 1.00 49.49 ? 115 MET B SD 1 ATOM 3332 C CE . MET B 2 115 ? 44.612 -31.877 -50.842 1.00 50.54 ? 115 MET B CE 1 ATOM 3333 N N . ASP B 2 116 ? 49.186 -33.213 -49.010 1.00 45.62 ? 116 ASP B N 1 ATOM 3334 C CA . ASP B 2 116 ? 50.295 -33.317 -49.963 1.00 46.92 ? 116 ASP B CA 1 ATOM 3335 C C . ASP B 2 116 ? 50.380 -34.715 -50.586 1.00 47.86 ? 116 ASP B C 1 ATOM 3336 O O . ASP B 2 116 ? 50.603 -34.851 -51.788 1.00 49.29 ? 116 ASP B O 1 ATOM 3337 C CB . ASP B 2 116 ? 51.620 -32.959 -49.271 1.00 46.75 ? 116 ASP B CB 1 ATOM 3338 C CG . ASP B 2 116 ? 52.780 -32.840 -50.244 1.00 48.77 ? 116 ASP B CG 1 ATOM 3339 O OD1 . ASP B 2 116 ? 52.676 -32.077 -51.233 1.00 50.02 ? 116 ASP B OD1 1 ATOM 3340 O OD2 . ASP B 2 116 ? 53.805 -33.510 -50.010 1.00 49.61 ? 116 ASP B OD2 1 ATOM 3341 N N . LYS B 2 117 ? 50.199 -35.746 -49.762 1.00 47.41 ? 117 LYS B N 1 ATOM 3342 C CA . LYS B 2 117 ? 50.234 -37.136 -50.229 1.00 48.98 ? 117 LYS B CA 1 ATOM 3343 C C . LYS B 2 117 ? 49.146 -37.441 -51.254 1.00 50.22 ? 117 LYS B C 1 ATOM 3344 O O . LYS B 2 117 ? 49.371 -38.215 -52.189 1.00 51.94 ? 117 LYS B O 1 ATOM 3345 C CB . LYS B 2 117 ? 50.136 -38.107 -49.048 1.00 48.77 ? 117 LYS B CB 1 ATOM 3346 C CG . LYS B 2 117 ? 51.489 -38.470 -48.466 1.00 49.25 ? 117 LYS B CG 1 ATOM 3347 C CD . LYS B 2 117 ? 51.494 -38.506 -46.952 1.00 47.93 ? 117 LYS B CD 1 ATOM 3348 C CE . LYS B 2 117 ? 50.624 -39.609 -46.388 1.00 48.62 ? 117 LYS B CE 1 ATOM 3349 N NZ . LYS B 2 117 ? 51.046 -39.904 -44.986 1.00 48.11 ? 117 LYS B NZ 1 ATOM 3350 N N . LEU B 2 118 ? 47.975 -36.838 -51.071 1.00 49.69 ? 118 LEU B N 1 ATOM 3351 C CA . LEU B 2 118 ? 46.893 -36.953 -52.044 1.00 51.29 ? 118 LEU B CA 1 ATOM 3352 C C . LEU B 2 118 ? 47.272 -36.234 -53.336 1.00 52.14 ? 118 LEU B C 1 ATOM 3353 O O . LEU B 2 118 ? 47.071 -36.758 -54.431 1.00 53.82 ? 118 LEU B O 1 ATOM 3354 C CB . LEU B 2 118 ? 45.597 -36.369 -51.478 1.00 51.08 ? 118 LEU B CB 1 ATOM 3355 C CG . LEU B 2 118 ? 44.372 -36.333 -52.397 1.00 53.26 ? 118 LEU B CG 1 ATOM 3356 C CD1 . LEU B 2 118 ? 44.059 -37.718 -52.938 1.00 55.33 ? 118 LEU B CD1 1 ATOM 3357 C CD2 . LEU B 2 118 ? 43.164 -35.763 -51.667 1.00 53.65 ? 118 LEU B CD2 1 ATOM 3358 N N . TYR B 2 119 ? 47.822 -35.033 -53.196 1.00 51.37 ? 119 TYR B N 1 ATOM 3359 C CA . TYR B 2 119 ? 48.276 -34.260 -54.340 1.00 52.54 ? 119 TYR B CA 1 ATOM 3360 C C . TYR B 2 119 ? 49.298 -35.039 -55.175 1.00 53.67 ? 119 TYR B C 1 ATOM 3361 O O . TYR B 2 119 ? 49.177 -35.089 -56.399 1.00 55.16 ? 119 TYR B O 1 ATOM 3362 C CB . TYR B 2 119 ? 48.851 -32.907 -53.894 1.00 52.06 ? 119 TYR B CB 1 ATOM 3363 C CG . TYR B 2 119 ? 49.227 -32.011 -55.048 1.00 53.94 ? 119 TYR B CG 1 ATOM 3364 C CD1 . TYR B 2 119 ? 48.267 -31.246 -55.706 1.00 55.49 ? 119 TYR B CD1 1 ATOM 3365 C CD2 . TYR B 2 119 ? 50.536 -31.945 -55.499 1.00 54.84 ? 119 TYR B CD2 1 ATOM 3366 C CE1 . TYR B 2 119 ? 48.606 -30.433 -56.782 1.00 57.57 ? 119 TYR B CE1 1 ATOM 3367 C CE2 . TYR B 2 119 ? 50.886 -31.137 -56.566 1.00 56.99 ? 119 TYR B CE2 1 ATOM 3368 C CZ . TYR B 2 119 ? 49.919 -30.381 -57.209 1.00 58.28 ? 119 TYR B CZ 1 ATOM 3369 O OH . TYR B 2 119 ? 50.264 -29.578 -58.278 1.00 60.89 ? 119 TYR B OH 1 ATOM 3370 N N . GLU B 2 120 ? 50.286 -35.651 -54.522 1.00 53.35 ? 120 GLU B N 1 ATOM 3371 C CA . GLU B 2 120 ? 51.341 -36.381 -55.238 1.00 55.22 ? 120 GLU B CA 1 ATOM 3372 C C . GLU B 2 120 ? 50.834 -37.696 -55.835 1.00 56.69 ? 120 GLU B C 1 ATOM 3373 O O . GLU B 2 120 ? 51.343 -38.150 -56.855 1.00 58.36 ? 120 GLU B O 1 ATOM 3374 C CB . GLU B 2 120 ? 52.548 -36.675 -54.336 1.00 55.31 ? 120 GLU B CB 1 ATOM 3375 C CG . GLU B 2 120 ? 53.220 -35.460 -53.700 1.00 54.71 ? 120 GLU B CG 1 ATOM 3376 C CD . GLU B 2 120 ? 53.799 -34.479 -54.705 1.00 56.40 ? 120 GLU B CD 1 ATOM 3377 O OE1 . GLU B 2 120 ? 54.451 -34.915 -55.679 1.00 58.56 ? 120 GLU B OE1 1 ATOM 3378 O OE2 . GLU B 2 120 ? 53.603 -33.258 -54.511 1.00 56.17 ? 120 GLU B OE2 1 ATOM 3379 N N . ARG B 2 121 ? 49.849 -38.313 -55.187 1.00 56.34 ? 121 ARG B N 1 ATOM 3380 C CA . ARG B 2 121 ? 49.238 -39.535 -55.699 1.00 58.37 ? 121 ARG B CA 1 ATOM 3381 C C . ARG B 2 121 ? 48.656 -39.278 -57.084 1.00 59.72 ? 121 ARG B C 1 ATOM 3382 O O . ARG B 2 121 ? 48.919 -40.018 -58.031 1.00 61.92 ? 121 ARG B O 1 ATOM 3383 C CB . ARG B 2 121 ? 48.122 -40.001 -54.764 1.00 58.15 ? 121 ARG B CB 1 ATOM 3384 C CG . ARG B 2 121 ? 47.433 -41.290 -55.187 1.00 60.95 ? 121 ARG B CG 1 ATOM 3385 C CD . ARG B 2 121 ? 45.940 -41.255 -54.903 1.00 61.50 ? 121 ARG B CD 1 ATOM 3386 N NE . ARG B 2 121 ? 45.642 -41.164 -53.476 1.00 60.19 ? 121 ARG B NE 1 ATOM 3387 C CZ . ARG B 2 121 ? 44.414 -41.095 -52.963 1.00 60.78 ? 121 ARG B CZ 1 ATOM 3388 N NH1 . ARG B 2 121 ? 43.342 -41.105 -53.760 1.00 62.87 ? 121 ARG B NH1 1 ATOM 3389 N NH2 . ARG B 2 121 ? 44.254 -41.014 -51.642 1.00 59.46 ? 121 ARG B NH2 1 ATOM 3390 N N . VAL B 2 122 ? 47.868 -38.215 -57.181 1.00 58.85 ? 122 VAL B N 1 ATOM 3391 C CA . VAL B 2 122 ? 47.170 -37.868 -58.405 1.00 60.34 ? 122 VAL B CA 1 ATOM 3392 C C . VAL B 2 122 ? 48.163 -37.475 -59.493 1.00 61.18 ? 122 VAL B C 1 ATOM 3393 O O . VAL B 2 122 ? 48.057 -37.946 -60.622 1.00 62.91 ? 122 VAL B O 1 ATOM 3394 C CB . VAL B 2 122 ? 46.164 -36.726 -58.163 1.00 59.84 ? 122 VAL B CB 1 ATOM 3395 C CG1 . VAL B 2 122 ? 45.539 -36.261 -59.472 1.00 61.83 ? 122 VAL B CG1 1 ATOM 3396 C CG2 . VAL B 2 122 ? 45.081 -37.171 -57.190 1.00 59.80 ? 122 VAL B CG2 1 ATOM 3397 N N . LYS B 2 123 ? 49.128 -36.625 -59.152 1.00 60.29 ? 123 LYS B N 1 ATOM 3398 C CA . LYS B 2 123 ? 50.191 -36.259 -60.093 1.00 61.68 ? 123 LYS B CA 1 ATOM 3399 C C . LYS B 2 123 ? 50.794 -37.509 -60.728 1.00 63.48 ? 123 LYS B C 1 ATOM 3400 O O . LYS B 2 123 ? 51.000 -37.565 -61.940 1.00 65.04 ? 123 LYS B O 1 ATOM 3401 C CB . LYS B 2 123 ? 51.306 -35.477 -59.395 1.00 61.05 ? 123 LYS B CB 1 ATOM 3402 C CG . LYS B 2 123 ? 52.263 -34.780 -60.357 1.00 62.94 ? 123 LYS B CG 1 ATOM 3403 C CD . LYS B 2 123 ? 53.709 -35.197 -60.149 1.00 64.17 ? 123 LYS B CD 1 ATOM 3404 C CE . LYS B 2 123 ? 54.287 -34.699 -58.831 1.00 63.22 ? 123 LYS B CE 1 ATOM 3405 N NZ . LYS B 2 123 ? 54.463 -33.220 -58.779 1.00 63.60 ? 123 LYS B NZ 1 ATOM 3406 N N . ARG B 2 124 ? 51.070 -38.511 -59.899 1.00 63.48 ? 124 ARG B N 1 ATOM 3407 C CA . ARG B 2 124 ? 51.643 -39.767 -60.383 1.00 65.96 ? 124 ARG B CA 1 ATOM 3408 C C . ARG B 2 124 ? 50.687 -40.578 -61.257 1.00 67.54 ? 124 ARG B C 1 ATOM 3409 O O . ARG B 2 124 ? 51.128 -41.221 -62.206 1.00 69.95 ? 124 ARG B O 1 ATOM 3410 C CB . ARG B 2 124 ? 52.145 -40.611 -59.214 1.00 66.17 ? 124 ARG B CB 1 ATOM 3411 C CG . ARG B 2 124 ? 53.383 -40.020 -58.572 1.00 65.82 ? 124 ARG B CG 1 ATOM 3412 C CD . ARG B 2 124 ? 53.950 -40.921 -57.495 1.00 66.71 ? 124 ARG B CD 1 ATOM 3413 N NE . ARG B 2 124 ? 55.169 -40.348 -56.929 1.00 66.90 ? 124 ARG B NE 1 ATOM 3414 C CZ . ARG B 2 124 ? 55.252 -39.691 -55.774 1.00 64.81 ? 124 ARG B CZ 1 ATOM 3415 N NH1 . ARG B 2 124 ? 54.184 -39.511 -54.999 1.00 62.30 ? 124 ARG B NH1 1 ATOM 3416 N NH2 . ARG B 2 124 ? 56.430 -39.218 -55.384 1.00 65.71 ? 124 ARG B NH2 1 ATOM 3417 N N . GLN B 2 125 ? 49.393 -40.551 -60.939 1.00 66.70 ? 125 GLN B N 1 ATOM 3418 C CA . GLN B 2 125 ? 48.380 -41.236 -61.752 1.00 68.71 ? 125 GLN B CA 1 ATOM 3419 C C . GLN B 2 125 ? 48.309 -40.647 -63.162 1.00 69.54 ? 125 GLN B C 1 ATOM 3420 O O . GLN B 2 125 ? 48.238 -41.380 -64.147 1.00 71.92 ? 125 GLN B O 1 ATOM 3421 C CB . GLN B 2 125 ? 46.994 -41.128 -61.108 1.00 68.28 ? 125 GLN B CB 1 ATOM 3422 C CG . GLN B 2 125 ? 46.844 -41.826 -59.768 1.00 67.94 ? 125 GLN B CG 1 ATOM 3423 C CD . GLN B 2 125 ? 45.521 -41.512 -59.092 1.00 67.55 ? 125 GLN B CD 1 ATOM 3424 O OE1 . GLN B 2 125 ? 45.485 -41.038 -57.953 1.00 65.44 ? 125 GLN B OE1 1 ATOM 3425 N NE2 . GLN B 2 125 ? 44.421 -41.777 -59.793 1.00 69.91 ? 125 GLN B NE2 1 ATOM 3426 N N . LEU B 2 126 ? 48.331 -39.319 -63.242 1.00 67.91 ? 126 LEU B N 1 ATOM 3427 C CA . LEU B 2 126 ? 48.170 -38.604 -64.505 1.00 68.92 ? 126 LEU B CA 1 ATOM 3428 C C . LEU B 2 126 ? 49.383 -38.696 -65.430 1.00 70.19 ? 126 LEU B C 1 ATOM 3429 O O . LEU B 2 126 ? 49.248 -38.502 -66.636 1.00 71.70 ? 126 LEU B O 1 ATOM 3430 C CB . LEU B 2 126 ? 47.824 -37.135 -64.242 1.00 67.62 ? 126 LEU B CB 1 ATOM 3431 C CG . LEU B 2 126 ? 46.514 -36.897 -63.482 1.00 67.09 ? 126 LEU B CG 1 ATOM 3432 C CD1 . LEU B 2 126 ? 46.260 -35.409 -63.290 1.00 66.58 ? 126 LEU B CD1 1 ATOM 3433 C CD2 . LEU B 2 126 ? 45.339 -37.554 -64.190 1.00 69.38 ? 126 LEU B CD2 1 ATOM 3434 N N . ARG B 2 127 ? 50.561 -38.982 -64.879 1.00 69.95 ? 127 ARG B N 1 ATOM 3435 C CA . ARG B 2 127 ? 51.755 -39.214 -65.697 1.00 71.96 ? 127 ARG B CA 1 ATOM 3436 C C . ARG B 2 127 ? 52.064 -37.999 -66.600 1.00 72.48 ? 127 ARG B C 1 ATOM 3437 O O . ARG B 2 127 ? 52.169 -36.886 -66.096 1.00 71.22 ? 127 ARG B O 1 ATOM 3438 C CB . ARG B 2 127 ? 51.584 -40.518 -66.491 1.00 74.46 ? 127 ARG B CB 1 ATOM 3439 C CG . ARG B 2 127 ? 52.051 -41.764 -65.764 1.00 75.61 ? 127 ARG B CG 1 ATOM 3440 C CD . ARG B 2 127 ? 53.450 -42.149 -66.213 1.00 78.12 ? 127 ARG B CD 1 ATOM 3441 N NE . ARG B 2 127 ? 53.693 -43.571 -66.016 1.00 80.82 ? 127 ARG B NE 1 ATOM 3442 C CZ . ARG B 2 127 ? 54.620 -44.279 -66.655 1.00 84.35 ? 127 ARG B CZ 1 ATOM 3443 N NH1 . ARG B 2 127 ? 55.421 -43.714 -67.559 1.00 85.46 ? 127 ARG B NH1 1 ATOM 3444 N NH2 . ARG B 2 127 ? 54.741 -45.572 -66.392 1.00 87.28 ? 127 ARG B NH2 1 ATOM 3445 N N . GLU B 2 128 ? 52.192 -38.196 -67.915 1.00 74.78 ? 128 GLU B N 1 ATOM 3446 C CA . GLU B 2 128 ? 52.492 -37.103 -68.840 1.00 75.85 ? 128 GLU B CA 1 ATOM 3447 C C . GLU B 2 128 ? 51.227 -36.573 -69.509 1.00 75.96 ? 128 GLU B C 1 ATOM 3448 O O . GLU B 2 128 ? 51.306 -35.793 -70.465 1.00 77.60 ? 128 GLU B O 1 ATOM 3449 C CB . GLU B 2 128 ? 53.474 -37.576 -69.913 1.00 78.72 ? 128 GLU B CB 1 ATOM 3450 C CG . GLU B 2 128 ? 54.789 -38.118 -69.374 1.00 79.82 ? 128 GLU B CG 1 ATOM 3451 C CD . GLU B 2 128 ? 55.653 -37.046 -68.737 1.00 79.59 ? 128 GLU B CD 1 ATOM 3452 O OE1 . GLU B 2 128 ? 55.807 -35.964 -69.341 1.00 80.58 ? 128 GLU B OE1 1 ATOM 3453 O OE2 . GLU B 2 128 ? 56.185 -37.286 -67.632 1.00 78.91 ? 128 GLU B OE2 1 ATOM 3454 N N . ASN B 2 129 ? 50.063 -36.992 -69.012 1.00 74.89 ? 129 ASN B N 1 ATOM 3455 C CA . ASN B 2 129 ? 48.781 -36.561 -69.570 1.00 75.63 ? 129 ASN B CA 1 ATOM 3456 C C . ASN B 2 129 ? 48.283 -35.239 -68.981 1.00 74.65 ? 129 ASN B C 1 ATOM 3457 O O . ASN B 2 129 ? 47.224 -34.748 -69.372 1.00 75.85 ? 129 ASN B O 1 ATOM 3458 C CB . ASN B 2 129 ? 47.713 -37.647 -69.371 1.00 76.01 ? 129 ASN B CB 1 ATOM 3459 C CG . ASN B 2 129 ? 48.063 -38.956 -70.062 1.00 77.84 ? 129 ASN B CG 1 ATOM 3460 O OD1 . ASN B 2 129 ? 49.205 -39.182 -70.461 1.00 78.55 ? 129 ASN B OD1 1 ATOM 3461 N ND2 . ASN B 2 129 ? 47.072 -39.825 -70.205 1.00 79.24 ? 129 ASN B ND2 1 ATOM 3462 N N . ALA B 2 130 ? 49.042 -34.669 -68.049 1.00 73.14 ? 130 ALA B N 1 ATOM 3463 C CA . ALA B 2 130 ? 48.654 -33.426 -67.377 1.00 72.46 ? 130 ALA B CA 1 ATOM 3464 C C . ALA B 2 130 ? 49.878 -32.635 -66.921 1.00 72.07 ? 130 ALA B C 1 ATOM 3465 O O . ALA B 2 130 ? 51.004 -33.127 -66.977 1.00 72.12 ? 130 ALA B O 1 ATOM 3466 C CB . ALA B 2 130 ? 47.760 -33.736 -66.187 1.00 70.70 ? 130 ALA B CB 1 ATOM 3467 N N . GLU B 2 131 ? 49.644 -31.403 -66.481 1.00 72.30 ? 131 GLU B N 1 ATOM 3468 C CA . GLU B 2 131 ? 50.704 -30.551 -65.947 1.00 72.56 ? 131 GLU B CA 1 ATOM 3469 C C . GLU B 2 131 ? 50.206 -29.793 -64.721 1.00 71.42 ? 131 GLU B C 1 ATOM 3470 O O . GLU B 2 131 ? 49.013 -29.520 -64.591 1.00 71.47 ? 131 GLU B O 1 ATOM 3471 C CB . GLU B 2 131 ? 51.211 -29.588 -67.026 1.00 75.70 ? 131 GLU B CB 1 ATOM 3472 C CG . GLU B 2 131 ? 51.977 -30.301 -68.136 1.00 77.05 ? 131 GLU B CG 1 ATOM 3473 C CD . GLU B 2 131 ? 52.446 -29.391 -69.257 1.00 80.45 ? 131 GLU B CD 1 ATOM 3474 O OE1 . GLU B 2 131 ? 52.286 -28.155 -69.152 1.00 82.10 ? 131 GLU B OE1 1 ATOM 3475 O OE2 . GLU B 2 131 ? 52.981 -29.931 -70.251 1.00 81.77 ? 131 GLU B OE2 1 ATOM 3476 N N . GLU B 2 132 ? 51.129 -29.474 -63.819 1.00 70.84 ? 132 GLU B N 1 ATOM 3477 C CA . GLU B 2 132 ? 50.793 -28.797 -62.569 1.00 69.71 ? 132 GLU B CA 1 ATOM 3478 C C . GLU B 2 132 ? 50.442 -27.337 -62.805 1.00 72.44 ? 132 GLU B C 1 ATOM 3479 O O . GLU B 2 132 ? 51.150 -26.627 -63.516 1.00 75.32 ? 132 GLU B O 1 ATOM 3480 C CB . GLU B 2 132 ? 51.959 -28.869 -61.584 1.00 68.66 ? 132 GLU B CB 1 ATOM 3481 C CG . GLU B 2 132 ? 52.188 -30.242 -60.985 1.00 66.27 ? 132 GLU B CG 1 ATOM 3482 C CD . GLU B 2 132 ? 53.218 -30.207 -59.872 1.00 65.56 ? 132 GLU B CD 1 ATOM 3483 O OE1 . GLU B 2 132 ? 54.429 -30.146 -60.172 1.00 67.52 ? 132 GLU B OE1 1 ATOM 3484 O OE2 . GLU B 2 132 ? 52.816 -30.232 -58.695 1.00 63.34 ? 132 GLU B OE2 1 ATOM 3485 N N . ASP B 2 133 ? 49.349 -26.898 -62.193 1.00 72.18 ? 133 ASP B N 1 ATOM 3486 C CA . ASP B 2 133 ? 48.928 -25.506 -62.257 1.00 75.26 ? 133 ASP B CA 1 ATOM 3487 C C . ASP B 2 133 ? 49.770 -24.657 -61.306 1.00 75.50 ? 133 ASP B C 1 ATOM 3488 O O . ASP B 2 133 ? 50.289 -23.612 -61.691 1.00 78.92 ? 133 ASP B O 1 ATOM 3489 C CB . ASP B 2 133 ? 47.450 -25.401 -61.886 1.00 75.46 ? 133 ASP B CB 1 ATOM 3490 C CG . ASP B 2 133 ? 46.880 -24.026 -62.138 1.00 79.65 ? 133 ASP B CG 1 ATOM 3491 O OD1 . ASP B 2 133 ? 46.997 -23.165 -61.238 1.00 80.48 ? 133 ASP B OD1 1 ATOM 3492 O OD2 . ASP B 2 133 ? 46.297 -23.818 -63.225 1.00 82.38 ? 133 ASP B OD2 1 ATOM 3493 N N . GLY B 2 134 ? 49.900 -25.117 -60.065 1.00 72.17 ? 134 GLY B N 1 ATOM 3494 C CA . GLY B 2 134 ? 50.658 -24.400 -59.042 1.00 72.22 ? 134 GLY B CA 1 ATOM 3495 C C . GLY B 2 134 ? 49.801 -23.947 -57.875 1.00 71.13 ? 134 GLY B C 1 ATOM 3496 O O . GLY B 2 134 ? 50.325 -23.556 -56.828 1.00 70.51 ? 134 GLY B O 1 ATOM 3497 N N . THR B 2 135 ? 48.485 -23.996 -58.060 1.00 71.22 ? 135 THR B N 1 ATOM 3498 C CA . THR B 2 135 ? 47.528 -23.573 -57.046 1.00 70.91 ? 135 THR B CA 1 ATOM 3499 C C . THR B 2 135 ? 46.835 -24.779 -56.412 1.00 67.28 ? 135 THR B C 1 ATOM 3500 O O . THR B 2 135 ? 45.915 -24.619 -55.608 1.00 67.09 ? 135 THR B O 1 ATOM 3501 C CB . THR B 2 135 ? 46.450 -22.669 -57.668 1.00 74.99 ? 135 THR B CB 1 ATOM 3502 O OG1 . THR B 2 135 ? 45.722 -23.410 -58.652 1.00 75.05 ? 135 THR B OG1 1 ATOM 3503 C CG2 . THR B 2 135 ? 47.080 -21.438 -58.320 1.00 79.31 ? 135 THR B CG2 1 ATOM 3504 N N . GLY B 2 136 ? 47.284 -25.979 -56.776 1.00 64.91 ? 136 GLY B N 1 ATOM 3505 C CA . GLY B 2 136 ? 46.635 -27.219 -56.362 1.00 62.30 ? 136 GLY B CA 1 ATOM 3506 C C . GLY B 2 136 ? 45.729 -27.797 -57.432 1.00 63.57 ? 136 GLY B C 1 ATOM 3507 O O . GLY B 2 136 ? 44.739 -28.455 -57.115 1.00 63.07 ? 136 GLY B O 1 ATOM 3508 N N . CYS B 2 137 ? 46.075 -27.565 -58.700 1.00 83.36 ? 137 CYS B N 1 ATOM 3509 C CA . CYS B 2 137 ? 45.258 -28.019 -59.825 1.00 82.93 ? 137 CYS B CA 1 ATOM 3510 C C . CYS B 2 137 ? 46.093 -28.677 -60.917 1.00 81.96 ? 137 CYS B C 1 ATOM 3511 O O . CYS B 2 137 ? 47.261 -28.343 -61.109 1.00 82.16 ? 137 CYS B O 1 ATOM 3512 C CB . CYS B 2 137 ? 44.477 -26.849 -60.423 1.00 85.03 ? 137 CYS B CB 1 ATOM 3513 S SG . CYS B 2 137 ? 43.271 -26.110 -59.301 1.00 86.83 ? 137 CYS B SG 1 ATOM 3514 N N . PHE B 2 138 ? 45.473 -29.616 -61.625 1.00 81.27 ? 138 PHE B N 1 ATOM 3515 C CA . PHE B 2 138 ? 46.103 -30.292 -62.749 1.00 80.95 ? 138 PHE B CA 1 ATOM 3516 C C . PHE B 2 138 ? 45.302 -30.021 -64.013 1.00 82.37 ? 138 PHE B C 1 ATOM 3517 O O . PHE B 2 138 ? 44.187 -30.520 -64.165 1.00 82.71 ? 138 PHE B O 1 ATOM 3518 C CB . PHE B 2 138 ? 46.175 -31.796 -62.494 1.00 79.62 ? 138 PHE B CB 1 ATOM 3519 C CG . PHE B 2 138 ? 47.090 -32.170 -61.370 1.00 78.62 ? 138 PHE B CG 1 ATOM 3520 C CD1 . PHE B 2 138 ? 48.446 -32.349 -61.595 1.00 78.66 ? 138 PHE B CD1 1 ATOM 3521 C CD2 . PHE B 2 138 ? 46.600 -32.331 -60.082 1.00 78.01 ? 138 PHE B CD2 1 ATOM 3522 C CE1 . PHE B 2 138 ? 49.296 -32.689 -60.560 1.00 78.33 ? 138 PHE B CE1 1 ATOM 3523 C CE2 . PHE B 2 138 ? 47.444 -32.672 -59.042 1.00 77.55 ? 138 PHE B CE2 1 ATOM 3524 C CZ . PHE B 2 138 ? 48.794 -32.851 -59.280 1.00 77.80 ? 138 PHE B CZ 1 ATOM 3525 N N . GLU B 2 139 ? 45.868 -29.212 -64.905 1.00 83.46 ? 139 GLU B N 1 ATOM 3526 C CA . GLU B 2 139 ? 45.265 -28.964 -66.211 1.00 85.25 ? 139 GLU B CA 1 ATOM 3527 C C . GLU B 2 139 ? 45.486 -30.188 -67.097 1.00 85.24 ? 139 GLU B C 1 ATOM 3528 O O . GLU B 2 139 ? 46.612 -30.655 -67.254 1.00 84.62 ? 139 GLU B O 1 ATOM 3529 C CB . GLU B 2 139 ? 45.838 -27.691 -66.844 1.00 86.55 ? 139 GLU B CB 1 ATOM 3530 C CG . GLU B 2 139 ? 45.331 -26.421 -66.167 1.00 87.53 ? 139 GLU B CG 1 ATOM 3531 C CD . GLU B 2 139 ? 46.001 -25.149 -66.661 1.00 88.94 ? 139 GLU B CD 1 ATOM 3532 O OE1 . GLU B 2 139 ? 46.923 -25.230 -67.500 1.00 88.99 ? 139 GLU B OE1 1 ATOM 3533 O OE2 . GLU B 2 139 ? 45.609 -24.056 -66.198 1.00 90.22 ? 139 GLU B OE2 1 ATOM 3534 N N . ILE B 2 140 ? 44.393 -30.707 -67.648 1.00 86.53 ? 140 ILE B N 1 ATOM 3535 C CA . ILE B 2 140 ? 44.392 -31.962 -68.393 1.00 87.11 ? 140 ILE B CA 1 ATOM 3536 C C . ILE B 2 140 ? 44.237 -31.664 -69.884 1.00 89.86 ? 140 ILE B C 1 ATOM 3537 O O . ILE B 2 140 ? 43.295 -30.980 -70.291 1.00 91.81 ? 140 ILE B O 1 ATOM 3538 C CB . ILE B 2 140 ? 43.246 -32.880 -67.911 1.00 87.08 ? 140 ILE B CB 1 ATOM 3539 C CG1 . ILE B 2 140 ? 43.239 -32.949 -66.376 1.00 84.79 ? 140 ILE B CG1 1 ATOM 3540 C CG2 . ILE B 2 140 ? 43.377 -34.272 -68.515 1.00 87.64 ? 140 ILE B CG2 1 ATOM 3541 C CD1 . ILE B 2 140 ? 42.121 -33.779 -65.784 1.00 84.77 ? 140 ILE B CD1 1 ATOM 3542 N N . PHE B 2 141 ? 45.167 -32.178 -70.689 1.00 90.47 ? 141 PHE B N 1 ATOM 3543 C CA . PHE B 2 141 ? 45.183 -31.926 -72.133 1.00 93.37 ? 141 PHE B CA 1 ATOM 3544 C C . PHE B 2 141 ? 44.021 -32.600 -72.854 1.00 95.91 ? 141 PHE B C 1 ATOM 3545 O O . PHE B 2 141 ? 43.251 -31.940 -73.556 1.00 98.58 ? 141 PHE B O 1 ATOM 3546 C CB . PHE B 2 141 ? 46.497 -32.407 -72.751 1.00 93.62 ? 141 PHE B CB 1 ATOM 3547 C CG . PHE B 2 141 ? 47.680 -31.559 -72.395 1.00 92.49 ? 141 PHE B CG 1 ATOM 3548 C CD1 . PHE B 2 141 ? 47.815 -30.280 -72.920 1.00 93.73 ? 141 PHE B CD1 1 ATOM 3549 C CD2 . PHE B 2 141 ? 48.659 -32.035 -71.533 1.00 90.62 ? 141 PHE B CD2 1 ATOM 3550 C CE1 . PHE B 2 141 ? 48.904 -29.491 -72.592 1.00 92.91 ? 141 PHE B CE1 1 ATOM 3551 C CE2 . PHE B 2 141 ? 49.752 -31.252 -71.201 1.00 89.95 ? 141 PHE B CE2 1 ATOM 3552 C CZ . PHE B 2 141 ? 49.874 -29.978 -71.730 1.00 91.07 ? 141 PHE B CZ 1 ATOM 3553 N N . HIS B 2 142 ? 43.908 -33.915 -72.687 1.00 95.58 ? 142 HIS B N 1 ATOM 3554 C CA . HIS B 2 142 ? 42.835 -34.680 -73.319 1.00 98.36 ? 142 HIS B CA 1 ATOM 3555 C C . HIS B 2 142 ? 41.498 -34.439 -72.617 1.00 98.53 ? 142 HIS B C 1 ATOM 3556 O O . HIS B 2 142 ? 41.444 -33.796 -71.568 1.00 96.16 ? 142 HIS B O 1 ATOM 3557 C CB . HIS B 2 142 ? 43.173 -36.173 -73.342 1.00 98.37 ? 142 HIS B CB 1 ATOM 3558 C CG . HIS B 2 142 ? 43.124 -36.828 -71.997 1.00 95.45 ? 142 HIS B CG 1 ATOM 3559 N ND1 . HIS B 2 142 ? 41.967 -37.358 -71.470 1.00 95.82 ? 142 HIS B ND1 1 ATOM 3560 C CD2 . HIS B 2 142 ? 44.094 -37.053 -71.079 1.00 92.41 ? 142 HIS B CD2 1 ATOM 3561 C CE1 . HIS B 2 142 ? 42.224 -37.874 -70.282 1.00 92.98 ? 142 HIS B CE1 1 ATOM 3562 N NE2 . HIS B 2 142 ? 43.508 -37.705 -70.023 1.00 90.98 ? 142 HIS B NE2 1 ATOM 3563 N N . LYS B 2 143 ? 40.428 -34.971 -73.201 1.00 101.77 ? 143 LYS B N 1 ATOM 3564 C CA . LYS B 2 143 ? 39.067 -34.681 -72.751 1.00 103.09 ? 143 LYS B CA 1 ATOM 3565 C C . LYS B 2 143 ? 38.606 -35.668 -71.683 1.00 101.45 ? 143 LYS B C 1 ATOM 3566 O O . LYS B 2 143 ? 38.385 -36.842 -71.975 1.00 102.83 ? 143 LYS B O 1 ATOM 3567 C CB . LYS B 2 143 ? 38.090 -34.716 -73.939 1.00 108.17 ? 143 LYS B CB 1 ATOM 3568 C CG . LYS B 2 143 ? 38.491 -33.870 -75.146 1.00 110.59 ? 143 LYS B CG 1 ATOM 3569 C CD . LYS B 2 143 ? 37.986 -32.433 -75.074 1.00 111.49 ? 143 LYS B CD 1 ATOM 3570 C CE . LYS B 2 143 ? 38.669 -31.630 -73.977 1.00 107.24 ? 143 LYS B CE 1 ATOM 3571 N NZ . LYS B 2 143 ? 38.501 -30.162 -74.160 1.00 108.50 ? 143 LYS B NZ 1 ATOM 3572 N N . CYS B 2 144 ? 38.461 -35.185 -70.450 1.00 98.87 ? 144 CYS B N 1 ATOM 3573 C CA . CYS B 2 144 ? 37.936 -36.002 -69.351 1.00 97.47 ? 144 CYS B CA 1 ATOM 3574 C C . CYS B 2 144 ? 36.451 -35.722 -69.139 1.00 100.00 ? 144 CYS B C 1 ATOM 3575 O O . CYS B 2 144 ? 36.082 -34.666 -68.620 1.00 99.77 ? 144 CYS B O 1 ATOM 3576 C CB . CYS B 2 144 ? 38.680 -35.724 -68.034 1.00 93.45 ? 144 CYS B CB 1 ATOM 3577 S SG . CYS B 2 144 ? 39.944 -36.907 -67.485 1.00 90.49 ? 144 CYS B SG 1 ATOM 3578 N N . ASP B 2 145 ? 35.604 -36.668 -69.536 1.00 102.83 ? 145 ASP B N 1 ATOM 3579 C CA . ASP B 2 145 ? 34.179 -36.607 -69.195 1.00 105.41 ? 145 ASP B CA 1 ATOM 3580 C C . ASP B 2 145 ? 34.007 -36.963 -67.716 1.00 102.38 ? 145 ASP B C 1 ATOM 3581 O O . ASP B 2 145 ? 34.967 -37.363 -67.060 1.00 98.78 ? 145 ASP B O 1 ATOM 3582 C CB . ASP B 2 145 ? 33.346 -37.535 -70.095 1.00 109.85 ? 145 ASP B CB 1 ATOM 3583 C CG . ASP B 2 145 ? 33.769 -38.997 -70.008 1.00 108.88 ? 145 ASP B CG 1 ATOM 3584 O OD1 . ASP B 2 145 ? 34.810 -39.298 -69.391 1.00 104.94 ? 145 ASP B OD1 1 ATOM 3585 O OD2 . ASP B 2 145 ? 33.055 -39.851 -70.570 1.00 112.60 ? 145 ASP B OD2 1 ATOM 3586 N N . ASP B 2 146 ? 32.793 -36.820 -67.190 1.00 104.25 ? 146 ASP B N 1 ATOM 3587 C CA . ASP B 2 146 ? 32.538 -37.115 -65.774 1.00 101.84 ? 146 ASP B CA 1 ATOM 3588 C C . ASP B 2 146 ? 32.958 -38.543 -65.403 1.00 99.95 ? 146 ASP B C 1 ATOM 3589 O O . ASP B 2 146 ? 33.365 -38.800 -64.268 1.00 96.71 ? 146 ASP B O 1 ATOM 3590 C CB . ASP B 2 146 ? 31.064 -36.879 -65.420 1.00 105.03 ? 146 ASP B CB 1 ATOM 3591 C CG . ASP B 2 146 ? 30.671 -35.405 -65.474 1.00 106.74 ? 146 ASP B CG 1 ATOM 3592 O OD1 . ASP B 2 146 ? 31.562 -34.530 -65.383 1.00 104.48 ? 146 ASP B OD1 1 ATOM 3593 O OD2 . ASP B 2 146 ? 29.459 -35.123 -65.601 1.00 110.64 ? 146 ASP B OD2 1 ATOM 3594 N N . ASP B 2 147 ? 32.863 -39.459 -66.366 1.00 102.37 ? 147 ASP B N 1 ATOM 3595 C CA . ASP B 2 147 ? 33.406 -40.811 -66.220 1.00 101.12 ? 147 ASP B CA 1 ATOM 3596 C C . ASP B 2 147 ? 34.911 -40.751 -65.975 1.00 97.06 ? 147 ASP B C 1 ATOM 3597 O O . ASP B 2 147 ? 35.415 -41.357 -65.032 1.00 94.28 ? 147 ASP B O 1 ATOM 3598 C CB . ASP B 2 147 ? 33.125 -41.648 -67.478 1.00 105.29 ? 147 ASP B CB 1 ATOM 3599 C CG . ASP B 2 147 ? 33.235 -43.147 -67.227 1.00 105.29 ? 147 ASP B CG 1 ATOM 3600 O OD1 . ASP B 2 147 ? 34.185 -43.578 -66.537 1.00 101.73 ? 147 ASP B OD1 1 ATOM 3601 O OD2 . ASP B 2 147 ? 32.373 -43.898 -67.729 1.00 109.22 ? 147 ASP B OD2 1 ATOM 3602 N N . CYS B 2 148 ? 35.614 -40.019 -66.839 1.00 97.13 ? 148 CYS B N 1 ATOM 3603 C CA . CYS B 2 148 ? 37.066 -39.839 -66.737 1.00 93.97 ? 148 CYS B CA 1 ATOM 3604 C C . CYS B 2 148 ? 37.467 -39.341 -65.353 1.00 90.18 ? 148 CYS B C 1 ATOM 3605 O O . CYS B 2 148 ? 38.380 -39.880 -64.727 1.00 87.70 ? 148 CYS B O 1 ATOM 3606 C CB . CYS B 2 148 ? 37.546 -38.836 -67.791 1.00 95.17 ? 148 CYS B CB 1 ATOM 3607 S SG . CYS B 2 148 ? 39.333 -38.778 -68.058 1.00 92.86 ? 148 CYS B SG 1 ATOM 3608 N N . MET B 2 149 ? 36.769 -38.312 -64.881 1.00 90.17 ? 149 MET B N 1 ATOM 3609 C CA . MET B 2 149 ? 37.063 -37.704 -63.586 1.00 87.33 ? 149 MET B CA 1 ATOM 3610 C C . MET B 2 149 ? 36.887 -38.707 -62.441 1.00 85.58 ? 149 MET B C 1 ATOM 3611 O O . MET B 2 149 ? 37.696 -38.742 -61.512 1.00 83.00 ? 149 MET B O 1 ATOM 3612 C CB . MET B 2 149 ? 36.174 -36.473 -63.359 1.00 88.79 ? 149 MET B CB 1 ATOM 3613 C CG . MET B 2 149 ? 36.390 -35.332 -64.350 1.00 90.34 ? 149 MET B CG 1 ATOM 3614 S SD . MET B 2 149 ? 38.008 -34.537 -64.223 1.00 87.70 ? 149 MET B SD 1 ATOM 3615 C CE . MET B 2 149 ? 37.816 -33.188 -65.387 1.00 90.37 ? 149 MET B CE 1 ATOM 3616 N N . ALA B 2 150 ? 35.841 -39.527 -62.522 1.00 87.25 ? 150 ALA B N 1 ATOM 3617 C CA . ALA B 2 150 ? 35.574 -40.558 -61.518 1.00 86.02 ? 150 ALA B CA 1 ATOM 3618 C C . ALA B 2 150 ? 36.633 -41.665 -61.516 1.00 84.37 ? 150 ALA B C 1 ATOM 3619 O O . ALA B 2 150 ? 36.913 -42.257 -60.468 1.00 82.54 ? 150 ALA B O 1 ATOM 3620 C CB . ALA B 2 150 ? 34.189 -41.155 -61.730 1.00 88.96 ? 150 ALA B CB 1 ATOM 3621 N N . SER B 2 151 ? 37.216 -41.946 -62.680 1.00 85.33 ? 151 SER B N 1 ATOM 3622 C CA . SER B 2 151 ? 38.302 -42.928 -62.777 1.00 84.31 ? 151 SER B CA 1 ATOM 3623 C C . SER B 2 151 ? 39.550 -42.446 -62.032 1.00 81.32 ? 151 SER B C 1 ATOM 3624 O O . SER B 2 151 ? 40.268 -43.242 -61.425 1.00 80.08 ? 151 SER B O 1 ATOM 3625 C CB . SER B 2 151 ? 38.657 -43.209 -64.239 1.00 86.62 ? 151 SER B CB 1 ATOM 3626 O OG . SER B 2 151 ? 39.464 -42.175 -64.771 1.00 86.00 ? 151 SER B OG 1 ATOM 3627 N N . ILE B 2 152 ? 39.805 -41.142 -62.094 1.00 80.59 ? 152 ILE B N 1 ATOM 3628 C CA . ILE B 2 152 ? 40.928 -40.546 -61.379 1.00 78.36 ? 152 ILE B CA 1 ATOM 3629 C C . ILE B 2 152 ? 40.681 -40.641 -59.872 1.00 76.74 ? 152 ILE B C 1 ATOM 3630 O O . ILE B 2 152 ? 41.548 -41.085 -59.127 1.00 75.25 ? 152 ILE B O 1 ATOM 3631 C CB . ILE B 2 152 ? 41.156 -39.074 -61.797 1.00 78.52 ? 152 ILE B CB 1 ATOM 3632 C CG1 . ILE B 2 152 ? 41.628 -39.007 -63.255 1.00 79.97 ? 152 ILE B CG1 1 ATOM 3633 C CG2 . ILE B 2 152 ? 42.178 -38.405 -60.882 1.00 76.71 ? 152 ILE B CG2 1 ATOM 3634 C CD1 . ILE B 2 152 ? 41.538 -37.628 -63.876 1.00 80.83 ? 152 ILE B CD1 1 ATOM 3635 N N . ARG B 2 153 ? 39.486 -40.237 -59.448 1.00 77.32 ? 153 ARG B N 1 ATOM 3636 C CA . ARG B 2 153 ? 39.088 -40.292 -58.041 1.00 76.32 ? 153 ARG B CA 1 ATOM 3637 C C . ARG B 2 153 ? 39.182 -41.696 -57.450 1.00 75.70 ? 153 ARG B C 1 ATOM 3638 O O . ARG B 2 153 ? 39.599 -41.862 -56.305 1.00 74.44 ? 153 ARG B O 1 ATOM 3639 C CB . ARG B 2 153 ? 37.655 -39.776 -57.872 1.00 77.75 ? 153 ARG B CB 1 ATOM 3640 C CG . ARG B 2 153 ? 37.508 -38.274 -58.051 1.00 78.46 ? 153 ARG B CG 1 ATOM 3641 C CD . ARG B 2 153 ? 36.182 -37.780 -57.497 1.00 80.01 ? 153 ARG B CD 1 ATOM 3642 N NE . ARG B 2 153 ? 35.063 -38.105 -58.382 1.00 82.49 ? 153 ARG B NE 1 ATOM 3643 C CZ . ARG B 2 153 ? 34.447 -37.249 -59.201 1.00 84.82 ? 153 ARG B CZ 1 ATOM 3644 N NH1 . ARG B 2 153 ? 34.809 -35.972 -59.272 1.00 84.92 ? 153 ARG B NH1 1 ATOM 3645 N NH2 . ARG B 2 153 ? 33.444 -37.677 -59.958 1.00 87.51 ? 153 ARG B NH2 1 ATOM 3646 N N . ASN B 2 154 ? 38.794 -42.696 -58.237 1.00 77.08 ? 154 ASN B N 1 ATOM 3647 C CA . ASN B 2 154 ? 38.710 -44.079 -57.766 1.00 77.11 ? 154 ASN B CA 1 ATOM 3648 C C . ASN B 2 154 ? 39.955 -44.913 -58.077 1.00 76.60 ? 154 ASN B C 1 ATOM 3649 O O . ASN B 2 154 ? 39.954 -46.128 -57.877 1.00 77.00 ? 154 ASN B O 1 ATOM 3650 C CB . ASN B 2 154 ? 37.452 -44.750 -58.341 1.00 79.57 ? 154 ASN B CB 1 ATOM 3651 C CG . ASN B 2 154 ? 36.165 -44.132 -57.812 1.00 80.42 ? 154 ASN B CG 1 ATOM 3652 O OD1 . ASN B 2 154 ? 35.229 -43.874 -58.569 1.00 82.80 ? 154 ASN B OD1 1 ATOM 3653 N ND2 . ASN B 2 154 ? 36.117 -43.886 -56.504 1.00 78.94 ? 154 ASN B ND2 1 ATOM 3654 N N . ASN B 2 155 ? 41.012 -44.256 -58.558 1.00 75.98 ? 155 ASN B N 1 ATOM 3655 C CA . ASN B 2 155 ? 42.327 -44.882 -58.731 1.00 75.74 ? 155 ASN B CA 1 ATOM 3656 C C . ASN B 2 155 ? 42.408 -45.872 -59.910 1.00 77.69 ? 155 ASN B C 1 ATOM 3657 O O . ASN B 2 155 ? 43.323 -46.693 -59.973 1.00 78.09 ? 155 ASN B O 1 ATOM 3658 C CB . ASN B 2 155 ? 42.752 -45.569 -57.420 1.00 74.67 ? 155 ASN B CB 1 ATOM 3659 C CG . ASN B 2 155 ? 44.212 -45.348 -57.087 1.00 74.09 ? 155 ASN B CG 1 ATOM 3660 O OD1 . ASN B 2 155 ? 45.090 -45.512 -57.935 1.00 74.93 ? 155 ASN B OD1 1 ATOM 3661 N ND2 . ASN B 2 155 ? 44.481 -44.968 -55.842 1.00 73.04 ? 155 ASN B ND2 1 ATOM 3662 N N . THR B 2 156 ? 41.465 -45.779 -60.848 1.00 79.36 ? 156 THR B N 1 ATOM 3663 C CA . THR B 2 156 ? 41.401 -46.704 -61.992 1.00 81.96 ? 156 THR B CA 1 ATOM 3664 C C . THR B 2 156 ? 41.906 -46.085 -63.307 1.00 83.20 ? 156 THR B C 1 ATOM 3665 O O . THR B 2 156 ? 42.087 -46.796 -64.294 1.00 85.63 ? 156 THR B O 1 ATOM 3666 C CB . THR B 2 156 ? 39.959 -47.224 -62.211 1.00 84.00 ? 156 THR B CB 1 ATOM 3667 O OG1 . THR B 2 156 ? 39.154 -46.202 -62.814 1.00 84.97 ? 156 THR B OG1 1 ATOM 3668 C CG2 . THR B 2 156 ? 39.321 -47.657 -60.888 1.00 82.69 ? 156 THR B CG2 1 ATOM 3669 N N . TYR B 2 157 ? 42.129 -44.771 -63.308 1.00 81.83 ? 157 TYR B N 1 ATOM 3670 C CA . TYR B 2 157 ? 42.521 -44.017 -64.505 1.00 82.94 ? 157 TYR B CA 1 ATOM 3671 C C . TYR B 2 157 ? 43.770 -44.586 -65.175 1.00 83.90 ? 157 TYR B C 1 ATOM 3672 O O . TYR B 2 157 ? 44.826 -44.679 -64.552 1.00 82.44 ? 157 TYR B O 1 ATOM 3673 C CB . TYR B 2 157 ? 42.764 -42.549 -64.124 1.00 81.03 ? 157 TYR B CB 1 ATOM 3674 C CG . TYR B 2 157 ? 43.330 -41.674 -65.223 1.00 81.90 ? 157 TYR B CG 1 ATOM 3675 C CD1 . TYR B 2 157 ? 44.705 -41.540 -65.393 1.00 81.32 ? 157 TYR B CD1 1 ATOM 3676 C CD2 . TYR B 2 157 ? 42.492 -40.959 -66.076 1.00 83.60 ? 157 TYR B CD2 1 ATOM 3677 C CE1 . TYR B 2 157 ? 45.231 -40.733 -66.389 1.00 82.25 ? 157 TYR B CE1 1 ATOM 3678 C CE2 . TYR B 2 157 ? 43.008 -40.146 -67.075 1.00 84.54 ? 157 TYR B CE2 1 ATOM 3679 C CZ . TYR B 2 157 ? 44.380 -40.037 -67.228 1.00 83.76 ? 157 TYR B CZ 1 ATOM 3680 O OH . TYR B 2 157 ? 44.902 -39.233 -68.214 1.00 84.77 ? 157 TYR B OH 1 ATOM 3681 N N . ASP B 2 158 ? 43.635 -44.958 -66.446 1.00 86.82 ? 158 ASP B N 1 ATOM 3682 C CA . ASP B 2 158 ? 44.749 -45.479 -67.235 1.00 88.47 ? 158 ASP B CA 1 ATOM 3683 C C . ASP B 2 158 ? 45.307 -44.374 -68.128 1.00 88.88 ? 158 ASP B C 1 ATOM 3684 O O . ASP B 2 158 ? 44.638 -43.916 -69.060 1.00 90.70 ? 158 ASP B O 1 ATOM 3685 C CB . ASP B 2 158 ? 44.285 -46.666 -68.083 1.00 92.07 ? 158 ASP B CB 1 ATOM 3686 C CG . ASP B 2 158 ? 45.411 -47.292 -68.898 1.00 94.36 ? 158 ASP B CG 1 ATOM 3687 O OD1 . ASP B 2 158 ? 46.582 -46.879 -68.752 1.00 93.07 ? 158 ASP B OD1 1 ATOM 3688 O OD2 . ASP B 2 158 ? 45.116 -48.211 -69.689 1.00 97.89 ? 158 ASP B OD2 1 ATOM 3689 N N . HIS B 2 159 ? 46.539 -43.963 -67.838 1.00 87.50 ? 159 HIS B N 1 ATOM 3690 C CA . HIS B 2 159 ? 47.186 -42.854 -68.541 1.00 87.68 ? 159 HIS B CA 1 ATOM 3691 C C . HIS B 2 159 ? 47.516 -43.171 -70.000 1.00 91.03 ? 159 HIS B C 1 ATOM 3692 O O . HIS B 2 159 ? 47.494 -42.278 -70.845 1.00 91.93 ? 159 HIS B O 1 ATOM 3693 C CB . HIS B 2 159 ? 48.473 -42.442 -67.815 1.00 85.86 ? 159 HIS B CB 1 ATOM 3694 C CG . HIS B 2 159 ? 49.632 -43.359 -68.065 1.00 87.46 ? 159 HIS B CG 1 ATOM 3695 N ND1 . HIS B 2 159 ? 49.765 -44.580 -67.440 1.00 87.76 ? 159 HIS B ND1 1 ATOM 3696 C CD2 . HIS B 2 159 ? 50.712 -43.231 -68.872 1.00 89.19 ? 159 HIS B CD2 1 ATOM 3697 C CE1 . HIS B 2 159 ? 50.876 -45.164 -67.852 1.00 89.73 ? 159 HIS B CE1 1 ATOM 3698 N NE2 . HIS B 2 159 ? 51.469 -44.366 -68.720 1.00 90.62 ? 159 HIS B NE2 1 ATOM 3699 N N . SER B 2 160 ? 47.829 -44.433 -70.288 1.00 93.18 ? 160 SER B N 1 ATOM 3700 C CA . SER B 2 160 ? 48.271 -44.833 -71.624 1.00 96.86 ? 160 SER B CA 1 ATOM 3701 C C . SER B 2 160 ? 47.160 -44.738 -72.675 1.00 99.69 ? 160 SER B C 1 ATOM 3702 O O . SER B 2 160 ? 47.444 -44.583 -73.862 1.00 102.57 ? 160 SER B O 1 ATOM 3703 C CB . SER B 2 160 ? 48.850 -46.251 -71.593 1.00 98.90 ? 160 SER B CB 1 ATOM 3704 O OG . SER B 2 160 ? 47.918 -47.169 -71.056 1.00 99.09 ? 160 SER B OG 1 ATOM 3705 N N . LYS B 2 161 ? 45.905 -44.824 -72.236 1.00 99.25 ? 161 LYS B N 1 ATOM 3706 C CA . LYS B 2 161 ? 44.756 -44.780 -73.148 1.00 102.45 ? 161 LYS B CA 1 ATOM 3707 C C . LYS B 2 161 ? 44.398 -43.373 -73.638 1.00 102.18 ? 161 LYS B C 1 ATOM 3708 O O . LYS B 2 161 ? 43.625 -43.232 -74.588 1.00 105.51 ? 161 LYS B O 1 ATOM 3709 C CB . LYS B 2 161 ? 43.535 -45.432 -72.493 1.00 102.62 ? 161 LYS B CB 1 ATOM 3710 C CG . LYS B 2 161 ? 43.624 -46.948 -72.441 1.00 104.79 ? 161 LYS B CG 1 ATOM 3711 C CD . LYS B 2 161 ? 42.567 -47.541 -71.525 1.00 104.12 ? 161 LYS B CD 1 ATOM 3712 C CE . LYS B 2 161 ? 42.626 -49.061 -71.509 1.00 106.66 ? 161 LYS B CE 1 ATOM 3713 N NZ . LYS B 2 161 ? 42.024 -49.612 -70.262 1.00 104.59 ? 161 LYS B NZ 1 ATOM 3714 N N . TYR B 2 162 ? 44.946 -42.345 -72.992 1.00 98.65 ? 162 TYR B N 1 ATOM 3715 C CA . TYR B 2 162 ? 44.759 -40.959 -73.433 1.00 98.46 ? 162 TYR B CA 1 ATOM 3716 C C . TYR B 2 162 ? 46.089 -40.253 -73.714 1.00 97.43 ? 162 TYR B C 1 ATOM 3717 O O . TYR B 2 162 ? 46.114 -39.036 -73.913 1.00 96.76 ? 162 TYR B O 1 ATOM 3718 C CB . TYR B 2 162 ? 44.005 -40.158 -72.370 1.00 95.71 ? 162 TYR B CB 1 ATOM 3719 C CG . TYR B 2 162 ? 42.746 -40.808 -71.849 1.00 96.26 ? 162 TYR B CG 1 ATOM 3720 C CD1 . TYR B 2 162 ? 41.526 -40.609 -72.483 1.00 99.26 ? 162 TYR B CD1 1 ATOM 3721 C CD2 . TYR B 2 162 ? 42.771 -41.601 -70.705 1.00 94.09 ? 162 TYR B CD2 1 ATOM 3722 C CE1 . TYR B 2 162 ? 40.365 -41.194 -72.005 1.00 100.12 ? 162 TYR B CE1 1 ATOM 3723 C CE2 . TYR B 2 162 ? 41.615 -42.191 -70.217 1.00 94.69 ? 162 TYR B CE2 1 ATOM 3724 C CZ . TYR B 2 162 ? 40.416 -41.985 -70.872 1.00 97.73 ? 162 TYR B CZ 1 ATOM 3725 O OH . TYR B 2 162 ? 39.264 -42.568 -70.396 1.00 98.72 ? 162 TYR B OH 1 ATOM 3726 N N . ARG B 2 163 ? 47.184 -41.012 -73.746 1.00 97.54 ? 163 ARG B N 1 ATOM 3727 C CA . ARG B 2 163 ? 48.525 -40.426 -73.737 1.00 96.35 ? 163 ARG B CA 1 ATOM 3728 C C . ARG B 2 163 ? 48.833 -39.603 -74.984 1.00 98.49 ? 163 ARG B C 1 ATOM 3729 O O . ARG B 2 163 ? 49.119 -38.410 -74.881 1.00 96.98 ? 163 ARG B O 1 ATOM 3730 C CB . ARG B 2 163 ? 49.594 -41.509 -73.549 1.00 96.90 ? 163 ARG B CB 1 ATOM 3731 C CG . ARG B 2 163 ? 50.995 -40.948 -73.354 1.00 95.84 ? 163 ARG B CG 1 ATOM 3732 C CD . ARG B 2 163 ? 52.019 -42.027 -73.046 1.00 96.65 ? 163 ARG B CD 1 ATOM 3733 N NE . ARG B 2 163 ? 53.268 -41.450 -72.549 1.00 95.39 ? 163 ARG B NE 1 ATOM 3734 C CZ . ARG B 2 163 ? 54.342 -42.152 -72.192 1.00 96.21 ? 163 ARG B CZ 1 ATOM 3735 N NH1 . ARG B 2 163 ? 54.346 -43.479 -72.270 1.00 98.19 ? 163 ARG B NH1 1 ATOM 3736 N NH2 . ARG B 2 163 ? 55.423 -41.519 -71.752 1.00 95.47 ? 163 ARG B NH2 1 ATOM 3737 N N . GLU B 2 164 ? 48.772 -40.240 -76.151 1.00 102.28 ? 164 GLU B N 1 ATOM 3738 C CA . GLU B 2 164 ? 49.145 -39.588 -77.411 1.00 104.91 ? 164 GLU B CA 1 ATOM 3739 C C . GLU B 2 164 ? 48.386 -38.279 -77.629 1.00 104.41 ? 164 GLU B C 1 ATOM 3740 O O . GLU B 2 164 ? 48.996 -37.249 -77.903 1.00 103.84 ? 164 GLU B O 1 ATOM 3741 C CB . GLU B 2 164 ? 48.926 -40.520 -78.609 1.00 109.78 ? 164 GLU B CB 1 ATOM 3742 C CG . GLU B 2 164 ? 49.956 -41.635 -78.752 1.00 111.42 ? 164 GLU B CG 1 ATOM 3743 C CD . GLU B 2 164 ? 49.598 -42.886 -77.969 1.00 111.01 ? 164 GLU B CD 1 ATOM 3744 O OE1 . GLU B 2 164 ? 49.408 -42.786 -76.737 1.00 107.17 ? 164 GLU B OE1 1 ATOM 3745 O OE2 . GLU B 2 164 ? 49.503 -43.967 -78.590 1.00 114.79 ? 164 GLU B OE2 1 ATOM 3746 N N . GLU B 2 165 ? 47.063 -38.321 -77.493 1.00 104.88 ? 165 GLU B N 1 ATOM 3747 C CA . GLU B 2 165 ? 46.236 -37.120 -77.673 1.00 105.05 ? 165 GLU B CA 1 ATOM 3748 C C . GLU B 2 165 ? 46.584 -35.996 -76.690 1.00 101.14 ? 165 GLU B C 1 ATOM 3749 O O . GLU B 2 165 ? 46.528 -34.818 -77.050 1.00 101.46 ? 165 GLU B O 1 ATOM 3750 C CB . GLU B 2 165 ? 44.738 -37.453 -77.599 1.00 106.70 ? 165 GLU B CB 1 ATOM 3751 C CG . GLU B 2 165 ? 44.274 -38.131 -76.318 1.00 104.04 ? 165 GLU B CG 1 ATOM 3752 C CD . GLU B 2 165 ? 42.768 -38.321 -76.271 1.00 105.98 ? 165 GLU B CD 1 ATOM 3753 O OE1 . GLU B 2 165 ? 42.032 -37.331 -76.475 1.00 106.93 ? 165 GLU B OE1 1 ATOM 3754 O OE2 . GLU B 2 165 ? 42.318 -39.461 -76.022 1.00 106.82 ? 165 GLU B OE2 1 ATOM 3755 N N . ALA B 2 166 ? 46.943 -36.365 -75.460 1.00 97.86 ? 166 ALA B N 1 ATOM 3756 C CA . ALA B 2 166 ? 47.396 -35.399 -74.455 1.00 94.54 ? 166 ALA B CA 1 ATOM 3757 C C . ALA B 2 166 ? 48.815 -34.918 -74.762 1.00 94.26 ? 166 ALA B C 1 ATOM 3758 O O . ALA B 2 166 ? 49.106 -33.722 -74.692 1.00 93.49 ? 166 ALA B O 1 ATOM 3759 C CB . ALA B 2 166 ? 47.336 -36.019 -73.068 1.00 91.74 ? 166 ALA B CB 1 ATOM 3760 N N . MET B 2 167 ? 49.689 -35.864 -75.094 1.00 95.21 ? 167 MET B N 1 ATOM 3761 C CA . MET B 2 167 ? 51.056 -35.566 -75.528 1.00 95.82 ? 167 MET B CA 1 ATOM 3762 C C . MET B 2 167 ? 51.091 -34.662 -76.760 1.00 98.18 ? 167 MET B C 1 ATOM 3763 O O . MET B 2 167 ? 51.880 -33.719 -76.813 1.00 97.72 ? 167 MET B O 1 ATOM 3764 C CB . MET B 2 167 ? 51.800 -36.865 -75.850 1.00 97.50 ? 167 MET B CB 1 ATOM 3765 C CG . MET B 2 167 ? 52.317 -37.615 -74.636 1.00 95.42 ? 167 MET B CG 1 ATOM 3766 S SD . MET B 2 167 ? 53.840 -36.889 -74.001 1.00 94.04 ? 167 MET B SD 1 ATOM 3767 C CE . MET B 2 167 ? 54.624 -38.309 -73.244 1.00 94.17 ? 167 MET B CE 1 ATOM 3768 N N . GLN B 2 168 ? 50.244 -34.961 -77.745 1.00 101.06 ? 168 GLN B N 1 ATOM 3769 C CA . GLN B 2 168 ? 50.151 -34.166 -78.975 1.00 103.88 ? 168 GLN B CA 1 ATOM 3770 C C . GLN B 2 168 ? 49.763 -32.710 -78.702 1.00 102.57 ? 168 GLN B C 1 ATOM 3771 O O . GLN B 2 168 ? 50.133 -31.815 -79.463 1.00 104.05 ? 168 GLN B O 1 ATOM 3772 C CB . GLN B 2 168 ? 49.142 -34.791 -79.946 1.00 107.61 ? 168 GLN B CB 1 ATOM 3773 C CG . GLN B 2 168 ? 49.614 -36.081 -80.608 1.00 110.39 ? 168 GLN B CG 1 ATOM 3774 C CD . GLN B 2 168 ? 50.444 -35.848 -81.856 1.00 113.63 ? 168 GLN B CD 1 ATOM 3775 O OE1 . GLN B 2 168 ? 51.537 -36.396 -81.994 1.00 114.22 ? 168 GLN B OE1 1 ATOM 3776 N NE2 . GLN B 2 168 ? 49.928 -35.041 -82.776 1.00 116.11 ? 168 GLN B NE2 1 ATOM 3777 N N . ASN B 2 169 ? 49.012 -32.483 -77.626 1.00 100.15 ? 169 ASN B N 1 ATOM 3778 C CA . ASN B 2 169 ? 48.646 -31.130 -77.195 1.00 99.03 ? 169 ASN B CA 1 ATOM 3779 C C . ASN B 2 169 ? 49.728 -30.429 -76.362 1.00 96.44 ? 169 ASN B C 1 ATOM 3780 O O . ASN B 2 169 ? 49.533 -29.284 -75.949 1.00 95.68 ? 169 ASN B O 1 ATOM 3781 C CB . ASN B 2 169 ? 47.333 -31.165 -76.403 1.00 98.18 ? 169 ASN B CB 1 ATOM 3782 C CG . ASN B 2 169 ? 46.157 -31.639 -77.239 1.00 101.43 ? 169 ASN B CG 1 ATOM 3783 O OD1 . ASN B 2 169 ? 46.035 -31.291 -78.415 1.00 104.61 ? 169 ASN B OD1 1 ATOM 3784 N ND2 . ASN B 2 169 ? 45.280 -32.433 -76.635 1.00 101.06 ? 169 ASN B ND2 1 ATOM 3785 N N . ARG B 2 170 ? 50.851 -31.114 -76.120 1.00 95.56 ? 170 ARG B N 1 ATOM 3786 C CA . ARG B 2 170 ? 51.996 -30.566 -75.374 1.00 93.82 ? 170 ARG B CA 1 ATOM 3787 C C . ARG B 2 170 ? 51.914 -29.052 -75.180 1.00 93.54 ? 170 ARG B C 1 ATOM 3788 O O . ARG B 2 170 ? 52.885 -28.411 -74.787 1.00 93.01 ? 170 ARG B O 1 ATOM 3789 C CB . ARG B 2 170 ? 53.335 -30.943 -76.048 1.00 95.23 ? 170 ARG B CB 1 ATOM 3790 C CG . ARG B 2 170 ? 53.701 -30.155 -77.306 1.00 97.73 ? 170 ARG B CG 1 ATOM 3791 C CD . ARG B 2 170 ? 52.870 -30.550 -78.516 1.00 100.42 ? 170 ARG B CD 1 ATOM 3792 N NE . ARG B 2 170 ? 52.205 -29.396 -79.122 1.00 101.70 ? 170 ARG B NE 1 ATOM 3793 C CZ . ARG B 2 170 ? 52.790 -28.499 -79.917 1.00 103.38 ? 170 ARG B CZ 1 ATOM 3794 N NH1 . ARG B 2 170 ? 54.078 -28.595 -80.231 1.00 104.02 ? 170 ARG B NH1 1 ATOM 3795 N NH2 . ARG B 2 170 ? 52.076 -27.491 -80.405 1.00 104.72 ? 170 ARG B NH2 1 HETATM 3796 C C1 . NAG C 3 . ? 34.630 -31.841 -32.657 1.00 56.87 ? 403 NAG A C1 1 HETATM 3797 C C2 . NAG C 3 . ? 33.715 -32.942 -33.217 1.00 64.26 ? 403 NAG A C2 1 HETATM 3798 C C3 . NAG C 3 . ? 32.862 -33.656 -32.170 1.00 67.38 ? 403 NAG A C3 1 HETATM 3799 C C4 . NAG C 3 . ? 33.632 -33.928 -30.884 1.00 68.42 ? 403 NAG A C4 1 HETATM 3800 C C5 . NAG C 3 . ? 34.288 -32.629 -30.404 1.00 67.93 ? 403 NAG A C5 1 HETATM 3801 C C6 . NAG C 3 . ? 35.009 -32.790 -29.061 1.00 67.88 ? 403 NAG A C6 1 HETATM 3802 C C7 . NAG C 3 . ? 33.013 -32.615 -35.549 1.00 68.77 ? 403 NAG A C7 1 HETATM 3803 C C8 . NAG C 3 . ? 32.027 -31.976 -36.489 1.00 68.59 ? 403 NAG A C8 1 HETATM 3804 N N2 . NAG C 3 . ? 32.841 -32.390 -34.243 1.00 66.68 ? 403 NAG A N2 1 HETATM 3805 O O3 . NAG C 3 . ? 32.402 -34.878 -32.708 1.00 69.19 ? 403 NAG A O3 1 HETATM 3806 O O4 . NAG C 3 . ? 32.738 -34.457 -29.923 1.00 71.86 ? 403 NAG A O4 1 HETATM 3807 O O5 . NAG C 3 . ? 35.205 -32.176 -31.392 1.00 63.04 ? 403 NAG A O5 1 HETATM 3808 O O6 . NAG C 3 . ? 34.889 -31.615 -28.281 1.00 67.30 ? 403 NAG A O6 1 HETATM 3809 O O7 . NAG C 3 . ? 33.925 -33.306 -36.005 1.00 70.10 ? 403 NAG A O7 1 HETATM 3810 C C1 . NAG D 3 . ? 52.886 -65.267 17.209 1.00 59.14 ? 404 NAG A C1 1 HETATM 3811 C C2 . NAG D 3 . ? 53.492 -65.653 15.863 1.00 68.49 ? 404 NAG A C2 1 HETATM 3812 C C3 . NAG D 3 . ? 52.675 -66.811 15.288 1.00 70.01 ? 404 NAG A C3 1 HETATM 3813 C C4 . NAG D 3 . ? 52.557 -67.961 16.292 1.00 71.55 ? 404 NAG A C4 1 HETATM 3814 C C5 . NAG D 3 . ? 52.148 -67.470 17.687 1.00 71.21 ? 404 NAG A C5 1 HETATM 3815 C C6 . NAG D 3 . ? 52.270 -68.590 18.722 1.00 72.15 ? 404 NAG A C6 1 HETATM 3816 C C7 . NAG D 3 . ? 54.642 -63.869 14.562 1.00 75.53 ? 404 NAG A C7 1 HETATM 3817 C C8 . NAG D 3 . ? 54.480 -62.699 13.630 1.00 74.79 ? 404 NAG A C8 1 HETATM 3818 N N2 . NAG D 3 . ? 53.520 -64.504 14.958 1.00 71.88 ? 404 NAG A N2 1 HETATM 3819 O O3 . NAG D 3 . ? 53.266 -67.273 14.094 1.00 70.74 ? 404 NAG A O3 1 HETATM 3820 O O4 . NAG D 3 . ? 51.614 -68.904 15.821 1.00 73.33 ? 404 NAG A O4 1 HETATM 3821 O O5 . NAG D 3 . ? 52.952 -66.372 18.090 1.00 64.69 ? 404 NAG A O5 1 HETATM 3822 O O6 . NAG D 3 . ? 51.519 -68.281 19.877 1.00 73.00 ? 404 NAG A O6 1 HETATM 3823 O O7 . NAG D 3 . ? 55.784 -64.180 14.907 1.00 76.22 ? 404 NAG A O7 1 HETATM 3824 C C1 . NAG E 3 . ? 32.209 -17.781 -35.497 1.00 59.17 ? 405 NAG A C1 1 HETATM 3825 C C2 . NAG E 3 . ? 31.850 -18.516 -34.203 1.00 66.58 ? 405 NAG A C2 1 HETATM 3826 C C3 . NAG E 3 . ? 30.373 -18.346 -33.872 1.00 70.02 ? 405 NAG A C3 1 HETATM 3827 C C4 . NAG E 3 . ? 30.083 -16.875 -33.616 1.00 71.63 ? 405 NAG A C4 1 HETATM 3828 C C5 . NAG E 3 . ? 30.720 -15.968 -34.683 1.00 70.71 ? 405 NAG A C5 1 HETATM 3829 C C6 . NAG E 3 . ? 31.662 -14.949 -34.047 1.00 72.16 ? 405 NAG A C6 1 HETATM 3830 C C7 . NAG E 3 . ? 33.306 -20.481 -33.894 1.00 70.91 ? 405 NAG A C7 1 HETATM 3831 C C8 . NAG E 3 . ? 33.459 -21.964 -34.076 1.00 68.94 ? 405 NAG A C8 1 HETATM 3832 N N2 . NAG E 3 . ? 32.155 -19.936 -34.310 1.00 70.08 ? 405 NAG A N2 1 HETATM 3833 O O3 . NAG E 3 . ? 30.024 -19.101 -32.729 1.00 72.66 ? 405 NAG A O3 1 HETATM 3834 O O4 . NAG E 3 . ? 28.681 -16.686 -33.577 1.00 72.78 ? 405 NAG A O4 1 HETATM 3835 O O5 . NAG E 3 . ? 31.370 -16.657 -35.755 1.00 63.30 ? 405 NAG A O5 1 HETATM 3836 O O6 . NAG E 3 . ? 31.983 -13.961 -35.004 1.00 76.54 ? 405 NAG A O6 1 HETATM 3837 O O7 . NAG E 3 . ? 34.224 -19.836 -33.384 1.00 73.80 ? 405 NAG A O7 1 HETATM 3838 C C1 . NAG F 3 . ? 30.978 -46.030 41.152 1.00 49.75 ? 1123 NAG A C1 1 HETATM 3839 C C2 . NAG F 3 . ? 29.586 -45.873 41.782 1.00 56.82 ? 1123 NAG A C2 1 HETATM 3840 C C3 . NAG F 3 . ? 29.607 -46.028 43.294 1.00 59.05 ? 1123 NAG A C3 1 HETATM 3841 C C4 . NAG F 3 . ? 30.279 -47.338 43.679 1.00 58.99 ? 1123 NAG A C4 1 HETATM 3842 C C5 . NAG F 3 . ? 31.649 -47.468 43.007 1.00 56.87 ? 1123 NAG A C5 1 HETATM 3843 C C6 . NAG F 3 . ? 32.216 -48.878 43.191 1.00 56.77 ? 1123 NAG A C6 1 HETATM 3844 C C7 . NAG F 3 . ? 28.070 -44.498 40.491 1.00 58.67 ? 1123 NAG A C7 1 HETATM 3845 C C8 . NAG F 3 . ? 27.463 -43.142 40.266 1.00 58.32 ? 1123 NAG A C8 1 HETATM 3846 N N2 . NAG F 3 . ? 28.948 -44.604 41.479 1.00 57.15 ? 1123 NAG A N2 1 HETATM 3847 O O3 . NAG F 3 . ? 28.278 -45.993 43.775 1.00 60.44 ? 1123 NAG A O3 1 HETATM 3848 O O4 . NAG F 3 . ? 30.411 -47.376 45.086 1.00 62.12 ? 1123 NAG A O4 1 HETATM 3849 O O5 . NAG F 3 . ? 31.574 -47.234 41.610 1.00 53.44 ? 1123 NAG A O5 1 HETATM 3850 O O6 . NAG F 3 . ? 33.208 -48.891 44.190 1.00 54.83 ? 1123 NAG A O6 1 HETATM 3851 O O7 . NAG F 3 . ? 27.769 -45.457 39.779 1.00 62.20 ? 1123 NAG A O7 1 HETATM 3852 S S . SO4 G 4 . ? 37.609 -53.099 44.354 1.00 96.58 ? 1317 SO4 A S 1 HETATM 3853 O O1 . SO4 G 4 . ? 37.808 -51.680 44.741 1.00 92.01 ? 1317 SO4 A O1 1 HETATM 3854 O O2 . SO4 G 4 . ? 38.708 -53.920 44.909 1.00 94.01 ? 1317 SO4 A O2 1 HETATM 3855 O O3 . SO4 G 4 . ? 37.611 -53.219 42.879 1.00 95.93 ? 1317 SO4 A O3 1 HETATM 3856 O O4 . SO4 G 4 . ? 36.313 -53.585 44.884 1.00 95.64 ? 1317 SO4 A O4 1 HETATM 3857 S S . SO4 H 4 . ? 29.717 -26.403 -8.299 1.00 119.27 ? 1318 SO4 A S 1 HETATM 3858 O O1 . SO4 H 4 . ? 30.566 -26.325 -7.087 1.00 115.47 ? 1318 SO4 A O1 1 HETATM 3859 O O2 . SO4 H 4 . ? 30.390 -25.715 -9.424 1.00 118.32 ? 1318 SO4 A O2 1 HETATM 3860 O O3 . SO4 H 4 . ? 28.414 -25.752 -8.027 1.00 118.69 ? 1318 SO4 A O3 1 HETATM 3861 O O4 . SO4 H 4 . ? 29.496 -27.822 -8.658 1.00 116.73 ? 1318 SO4 A O4 1 HETATM 3862 S S . SO4 I 4 . ? 33.366 -23.246 -17.298 1.00 111.12 ? 1319 SO4 A S 1 HETATM 3863 O O1 . SO4 I 4 . ? 34.599 -22.430 -17.375 1.00 110.04 ? 1319 SO4 A O1 1 HETATM 3864 O O2 . SO4 I 4 . ? 33.545 -24.314 -16.288 1.00 108.30 ? 1319 SO4 A O2 1 HETATM 3865 O O3 . SO4 I 4 . ? 33.079 -23.855 -18.619 1.00 108.56 ? 1319 SO4 A O3 1 HETATM 3866 O O4 . SO4 I 4 . ? 32.239 -22.369 -16.907 1.00 112.06 ? 1319 SO4 A O4 1 HETATM 3867 S S . SO4 J 4 . ? 24.285 -32.550 -11.962 1.00 118.51 ? 1320 SO4 A S 1 HETATM 3868 O O1 . SO4 J 4 . ? 25.343 -31.601 -11.551 1.00 112.80 ? 1320 SO4 A O1 1 HETATM 3869 O O2 . SO4 J 4 . ? 24.744 -33.939 -11.731 1.00 116.95 ? 1320 SO4 A O2 1 HETATM 3870 O O3 . SO4 J 4 . ? 23.985 -32.372 -13.402 1.00 119.71 ? 1320 SO4 A O3 1 HETATM 3871 O O4 . SO4 J 4 . ? 23.062 -32.288 -11.169 1.00 119.41 ? 1320 SO4 A O4 1 HETATM 3872 S S . SO4 K 4 . ? 37.039 -31.535 18.421 1.00 90.55 ? 1321 SO4 A S 1 HETATM 3873 O O1 . SO4 K 4 . ? 37.851 -31.612 19.660 1.00 86.96 ? 1321 SO4 A O1 1 HETATM 3874 O O2 . SO4 K 4 . ? 37.155 -32.813 17.679 1.00 83.79 ? 1321 SO4 A O2 1 HETATM 3875 O O3 . SO4 K 4 . ? 37.553 -30.436 17.572 1.00 92.72 ? 1321 SO4 A O3 1 HETATM 3876 O O4 . SO4 K 4 . ? 35.625 -31.246 18.769 1.00 84.23 ? 1321 SO4 A O4 1 HETATM 3877 S S . SO4 L 4 . ? 43.734 -60.545 12.516 1.00 71.04 ? 1322 SO4 A S 1 HETATM 3878 O O1 . SO4 L 4 . ? 43.769 -61.609 13.550 1.00 66.48 ? 1322 SO4 A O1 1 HETATM 3879 O O2 . SO4 L 4 . ? 43.140 -61.088 11.275 1.00 71.93 ? 1322 SO4 A O2 1 HETATM 3880 O O3 . SO4 L 4 . ? 45.104 -60.110 12.197 1.00 67.61 ? 1322 SO4 A O3 1 HETATM 3881 O O4 . SO4 L 4 . ? 42.948 -59.382 12.996 1.00 65.53 ? 1322 SO4 A O4 1 HETATM 3882 S S . SO4 M 4 . ? 34.467 -57.584 22.726 1.00 105.46 ? 1323 SO4 A S 1 HETATM 3883 O O1 . SO4 M 4 . ? 35.836 -58.153 22.759 1.00 97.21 ? 1323 SO4 A O1 1 HETATM 3884 O O2 . SO4 M 4 . ? 34.129 -57.171 21.344 1.00 105.52 ? 1323 SO4 A O2 1 HETATM 3885 O O3 . SO4 M 4 . ? 34.382 -56.409 23.622 1.00 105.61 ? 1323 SO4 A O3 1 HETATM 3886 O O4 . SO4 M 4 . ? 33.509 -58.614 23.184 1.00 107.18 ? 1323 SO4 A O4 1 HETATM 3887 S S . SO4 N 4 . ? 49.768 -32.864 17.958 1.00 95.36 ? 1324 SO4 A S 1 HETATM 3888 O O1 . SO4 N 4 . ? 50.718 -33.637 18.794 1.00 90.94 ? 1324 SO4 A O1 1 HETATM 3889 O O2 . SO4 N 4 . ? 50.277 -32.742 16.572 1.00 94.95 ? 1324 SO4 A O2 1 HETATM 3890 O O3 . SO4 N 4 . ? 49.617 -31.509 18.533 1.00 95.86 ? 1324 SO4 A O3 1 HETATM 3891 O O4 . SO4 N 4 . ? 48.452 -33.543 17.931 1.00 92.14 ? 1324 SO4 A O4 1 HETATM 3892 S S . SO4 O 4 . ? 52.761 -15.989 -31.624 1.00 92.52 ? 1325 SO4 A S 1 HETATM 3893 O O1 . SO4 O 4 . ? 52.926 -17.146 -30.715 1.00 93.73 ? 1325 SO4 A O1 1 HETATM 3894 O O2 . SO4 O 4 . ? 52.055 -16.417 -32.852 1.00 89.41 ? 1325 SO4 A O2 1 HETATM 3895 O O3 . SO4 O 4 . ? 54.093 -15.441 -31.978 1.00 91.13 ? 1325 SO4 A O3 1 HETATM 3896 O O4 . SO4 O 4 . ? 51.950 -14.953 -30.941 1.00 93.28 ? 1325 SO4 A O4 1 HETATM 3897 S S . SO4 P 4 . ? 41.919 -25.086 45.103 1.00 103.23 ? 1326 SO4 A S 1 HETATM 3898 O O1 . SO4 P 4 . ? 43.269 -25.668 44.920 1.00 99.92 ? 1326 SO4 A O1 1 HETATM 3899 O O2 . SO4 P 4 . ? 40.965 -25.718 44.164 1.00 101.68 ? 1326 SO4 A O2 1 HETATM 3900 O O3 . SO4 P 4 . ? 41.984 -23.628 44.850 1.00 103.77 ? 1326 SO4 A O3 1 HETATM 3901 O O4 . SO4 P 4 . ? 41.444 -25.326 46.482 1.00 105.46 ? 1326 SO4 A O4 1 HETATM 3902 C C1 . NAG Q 3 . ? 48.721 -24.340 2.732 1.00 38.15 ? 201 NAG B C1 1 HETATM 3903 C C2 . NAG Q 3 . ? 48.574 -23.417 3.943 1.00 44.11 ? 201 NAG B C2 1 HETATM 3904 C C3 . NAG Q 3 . ? 47.128 -23.197 4.360 1.00 47.25 ? 201 NAG B C3 1 HETATM 3905 C C4 . NAG Q 3 . ? 46.242 -22.873 3.160 1.00 49.80 ? 201 NAG B C4 1 HETATM 3906 C C5 . NAG Q 3 . ? 46.481 -23.904 2.057 1.00 48.69 ? 201 NAG B C5 1 HETATM 3907 C C6 . NAG Q 3 . ? 45.657 -23.624 0.802 1.00 49.05 ? 201 NAG B C6 1 HETATM 3908 C C7 . NAG Q 3 . ? 50.225 -23.164 5.719 1.00 45.14 ? 201 NAG B C7 1 HETATM 3909 C C8 . NAG Q 3 . ? 50.951 -23.824 6.849 1.00 44.59 ? 201 NAG B C8 1 HETATM 3910 N N2 . NAG Q 3 . ? 49.341 -23.920 5.070 1.00 44.58 ? 201 NAG B N2 1 HETATM 3911 O O3 . NAG Q 3 . ? 47.111 -22.143 5.297 1.00 47.93 ? 201 NAG B O3 1 HETATM 3912 O O4 . NAG Q 3 . ? 44.900 -22.945 3.585 1.00 56.97 ? 201 NAG B O4 1 HETATM 3913 O O5 . NAG Q 3 . ? 47.848 -23.884 1.713 1.00 41.96 ? 201 NAG B O5 1 HETATM 3914 O O6 . NAG Q 3 . ? 46.003 -24.552 -0.203 1.00 53.35 ? 201 NAG B O6 1 HETATM 3915 O O7 . NAG Q 3 . ? 50.468 -21.987 5.436 1.00 46.80 ? 201 NAG B O7 1 HETATM 3916 C C1 . NAG R 3 . ? 44.092 -21.847 3.117 1.00 61.89 ? 202 NAG B C1 1 HETATM 3917 C C2 . NAG R 3 . ? 42.621 -22.240 3.286 1.00 62.35 ? 202 NAG B C2 1 HETATM 3918 C C3 . NAG R 3 . ? 41.660 -21.069 3.035 1.00 64.63 ? 202 NAG B C3 1 HETATM 3919 C C4 . NAG R 3 . ? 42.170 -19.721 3.551 1.00 66.32 ? 202 NAG B C4 1 HETATM 3920 C C5 . NAG R 3 . ? 43.671 -19.541 3.311 1.00 67.23 ? 202 NAG B C5 1 HETATM 3921 C C6 . NAG R 3 . ? 44.209 -18.280 3.981 1.00 68.40 ? 202 NAG B C6 1 HETATM 3922 C C7 . NAG R 3 . ? 42.370 -24.642 2.780 1.00 59.69 ? 202 NAG B C7 1 HETATM 3923 C C8 . NAG R 3 . ? 41.963 -25.664 1.755 1.00 58.35 ? 202 NAG B C8 1 HETATM 3924 N N2 . NAG R 3 . ? 42.274 -23.358 2.413 1.00 59.98 ? 202 NAG B N2 1 HETATM 3925 O O3 . NAG R 3 . ? 40.420 -21.355 3.648 1.00 64.66 ? 202 NAG B O3 1 HETATM 3926 O O4 . NAG R 3 . ? 41.451 -18.681 2.914 1.00 66.96 ? 202 NAG B O4 1 HETATM 3927 O O5 . NAG R 3 . ? 44.376 -20.656 3.822 1.00 65.19 ? 202 NAG B O5 1 HETATM 3928 O O6 . NAG R 3 . ? 44.216 -18.456 5.380 1.00 69.25 ? 202 NAG B O6 1 HETATM 3929 O O7 . NAG R 3 . ? 42.769 -25.019 3.884 1.00 58.46 ? 202 NAG B O7 1 HETATM 3930 S S . SO4 S 4 . ? 33.729 -23.065 -51.378 1.00 92.28 ? 1171 SO4 B S 1 HETATM 3931 O O1 . SO4 S 4 . ? 34.911 -23.164 -52.268 1.00 91.16 ? 1171 SO4 B O1 1 HETATM 3932 O O2 . SO4 S 4 . ? 33.245 -24.432 -51.066 1.00 86.88 ? 1171 SO4 B O2 1 HETATM 3933 O O3 . SO4 S 4 . ? 32.648 -22.317 -52.061 1.00 92.07 ? 1171 SO4 B O3 1 HETATM 3934 O O4 . SO4 S 4 . ? 34.111 -22.341 -50.141 1.00 87.10 ? 1171 SO4 B O4 1 HETATM 3935 S S . SO4 T 4 . ? 42.586 -25.168 13.769 1.00 81.89 ? 1172 SO4 B S 1 HETATM 3936 O O1 . SO4 T 4 . ? 43.940 -25.537 14.248 1.00 81.24 ? 1172 SO4 B O1 1 HETATM 3937 O O2 . SO4 T 4 . ? 42.472 -25.434 12.314 1.00 78.96 ? 1172 SO4 B O2 1 HETATM 3938 O O3 . SO4 T 4 . ? 42.355 -23.726 14.005 1.00 82.28 ? 1172 SO4 B O3 1 HETATM 3939 O O4 . SO4 T 4 . ? 41.578 -25.958 14.516 1.00 80.65 ? 1172 SO4 B O4 1 HETATM 3940 S S . SO4 U 4 . ? 53.814 -23.130 -17.330 1.00 75.92 ? 1173 SO4 B S 1 HETATM 3941 O O1 . SO4 U 4 . ? 52.851 -24.019 -16.649 1.00 72.84 ? 1173 SO4 B O1 1 HETATM 3942 O O2 . SO4 U 4 . ? 53.796 -23.402 -18.789 1.00 74.09 ? 1173 SO4 B O2 1 HETATM 3943 O O3 . SO4 U 4 . ? 55.170 -23.376 -16.776 1.00 72.49 ? 1173 SO4 B O3 1 HETATM 3944 O O4 . SO4 U 4 . ? 53.410 -21.722 -17.092 1.00 76.89 ? 1173 SO4 B O4 1 HETATM 3945 S S . SO4 V 4 . ? 59.598 -33.005 -61.508 0.33 99.27 ? 1174 SO4 B S 1 HETATM 3946 O O1 . SO4 V 4 . ? 60.787 -33.846 -61.770 1.00 115.06 ? 1174 SO4 B O1 1 HETATM 3947 O O2 . SO4 V 4 . ? 58.522 -33.352 -62.463 0.33 95.93 ? 1174 SO4 B O2 1 HETATM 3948 O O3 . SO4 V 4 . ? 59.976 -31.584 -61.676 1.00 115.14 ? 1174 SO4 B O3 1 HETATM 3949 O O4 . SO4 V 4 . ? 59.118 -33.231 -60.126 0.33 103.73 ? 1174 SO4 B O4 1 HETATM 3950 O O . HOH W 5 . ? 40.304 -26.530 -50.751 1.00 42.73 ? 2001 HOH A O 1 HETATM 3951 O O . HOH W 5 . ? 41.012 -25.111 -43.681 1.00 32.60 ? 2002 HOH A O 1 HETATM 3952 O O . HOH W 5 . ? 44.870 -23.552 -47.671 1.00 35.51 ? 2003 HOH A O 1 HETATM 3953 O O . HOH W 5 . ? 33.610 -31.359 -43.779 1.00 46.36 ? 2004 HOH A O 1 HETATM 3954 O O . HOH W 5 . ? 40.007 -31.259 -40.033 1.00 29.39 ? 2005 HOH A O 1 HETATM 3955 O O . HOH W 5 . ? 35.245 -30.092 -21.146 1.00 49.35 ? 2006 HOH A O 1 HETATM 3956 O O . HOH W 5 . ? 27.531 -27.318 -14.174 1.00 48.00 ? 2007 HOH A O 1 HETATM 3957 O O . HOH W 5 . ? 38.882 -13.404 -31.617 1.00 48.09 ? 2008 HOH A O 1 HETATM 3958 O O . HOH W 5 . ? 45.836 -24.797 -27.094 1.00 19.05 ? 2009 HOH A O 1 HETATM 3959 O O . HOH W 5 . ? 44.933 -20.085 -28.320 1.00 35.41 ? 2010 HOH A O 1 HETATM 3960 O O . HOH W 5 . ? 47.696 -23.658 -24.764 1.00 42.38 ? 2011 HOH A O 1 HETATM 3961 O O . HOH W 5 . ? 51.654 -22.594 -26.434 1.00 41.11 ? 2012 HOH A O 1 HETATM 3962 O O . HOH W 5 . ? 51.925 -23.965 -36.183 1.00 36.09 ? 2013 HOH A O 1 HETATM 3963 O O . HOH W 5 . ? 23.108 -36.378 7.321 1.00 54.61 ? 2014 HOH A O 1 HETATM 3964 O O . HOH W 5 . ? 44.055 -18.282 -37.469 1.00 57.78 ? 2015 HOH A O 1 HETATM 3965 O O . HOH W 5 . ? 36.266 -26.392 -28.562 1.00 47.00 ? 2016 HOH A O 1 HETATM 3966 O O . HOH W 5 . ? 35.491 -29.800 -25.933 1.00 43.14 ? 2017 HOH A O 1 HETATM 3967 O O . HOH W 5 . ? 36.482 -25.502 -22.948 1.00 36.79 ? 2018 HOH A O 1 HETATM 3968 O O . HOH W 5 . ? 36.079 -28.783 -18.867 1.00 31.56 ? 2019 HOH A O 1 HETATM 3969 O O . HOH W 5 . ? 48.020 -31.891 13.652 1.00 39.72 ? 2020 HOH A O 1 HETATM 3970 O O . HOH W 5 . ? 33.652 -30.687 -18.918 1.00 40.67 ? 2021 HOH A O 1 HETATM 3971 O O . HOH W 5 . ? 31.167 -26.932 -12.064 1.00 34.40 ? 2022 HOH A O 1 HETATM 3972 O O . HOH W 5 . ? 33.892 -27.958 -18.153 1.00 34.57 ? 2023 HOH A O 1 HETATM 3973 O O . HOH W 5 . ? 32.781 -33.661 -12.782 1.00 30.89 ? 2024 HOH A O 1 HETATM 3974 O O . HOH W 5 . ? 27.536 -30.423 -13.040 1.00 42.44 ? 2025 HOH A O 1 HETATM 3975 O O . HOH W 5 . ? 25.402 -29.056 -3.169 1.00 45.51 ? 2026 HOH A O 1 HETATM 3976 O O . HOH W 5 . ? 23.109 -29.533 -7.669 1.00 52.34 ? 2027 HOH A O 1 HETATM 3977 O O . HOH W 5 . ? 31.127 -44.112 -6.482 1.00 25.33 ? 2028 HOH A O 1 HETATM 3978 O O . HOH W 5 . ? 27.293 -47.545 -2.917 1.00 58.06 ? 2029 HOH A O 1 HETATM 3979 O O . HOH W 5 . ? 28.870 -45.787 -12.894 1.00 37.13 ? 2030 HOH A O 1 HETATM 3980 O O . HOH W 5 . ? 27.004 -46.421 1.450 1.00 26.46 ? 2031 HOH A O 1 HETATM 3981 O O . HOH W 5 . ? 36.771 -44.279 -3.311 1.00 29.36 ? 2032 HOH A O 1 HETATM 3982 O O . HOH W 5 . ? 32.259 -45.971 32.524 1.00 43.00 ? 2033 HOH A O 1 HETATM 3983 O O . HOH W 5 . ? 31.963 -55.357 0.000 0.50 65.96 ? 2034 HOH A O 1 HETATM 3984 O O . HOH W 5 . ? 36.231 -53.182 5.676 1.00 34.52 ? 2035 HOH A O 1 HETATM 3985 O O . HOH W 5 . ? 33.817 -56.459 2.961 1.00 53.55 ? 2036 HOH A O 1 HETATM 3986 O O . HOH W 5 . ? 25.821 -35.228 6.623 1.00 38.10 ? 2037 HOH A O 1 HETATM 3987 O O . HOH W 5 . ? 32.552 -35.930 10.962 1.00 27.44 ? 2038 HOH A O 1 HETATM 3988 O O . HOH W 5 . ? 25.885 -37.504 12.918 1.00 28.87 ? 2039 HOH A O 1 HETATM 3989 O O . HOH W 5 . ? 25.644 -30.705 14.518 1.00 62.15 ? 2040 HOH A O 1 HETATM 3990 O O . HOH W 5 . ? 27.601 -33.724 18.673 1.00 56.28 ? 2041 HOH A O 1 HETATM 3991 O O . HOH W 5 . ? 28.292 -31.592 16.527 1.00 58.70 ? 2042 HOH A O 1 HETATM 3992 O O . HOH W 5 . ? 38.514 -36.346 13.894 1.00 33.37 ? 2043 HOH A O 1 HETATM 3993 O O . HOH W 5 . ? 36.610 -36.135 11.950 1.00 29.80 ? 2044 HOH A O 1 HETATM 3994 O O . HOH W 5 . ? 37.753 -38.783 22.035 1.00 34.03 ? 2045 HOH A O 1 HETATM 3995 O O . HOH W 5 . ? 26.353 -42.263 16.459 1.00 29.37 ? 2046 HOH A O 1 HETATM 3996 O O . HOH W 5 . ? 26.284 -38.499 15.184 1.00 33.96 ? 2047 HOH A O 1 HETATM 3997 O O . HOH W 5 . ? 28.533 -34.459 22.669 1.00 40.70 ? 2048 HOH A O 1 HETATM 3998 O O . HOH W 5 . ? 28.273 -48.760 16.772 1.00 43.08 ? 2049 HOH A O 1 HETATM 3999 O O . HOH W 5 . ? 25.018 -48.004 20.249 1.00 51.92 ? 2050 HOH A O 1 HETATM 4000 O O . HOH W 5 . ? 29.698 -49.390 14.211 1.00 62.16 ? 2051 HOH A O 1 HETATM 4001 O O . HOH W 5 . ? 30.354 -53.654 10.328 1.00 51.16 ? 2052 HOH A O 1 HETATM 4002 O O . HOH W 5 . ? 30.847 -52.096 19.789 1.00 48.99 ? 2053 HOH A O 1 HETATM 4003 O O . HOH W 5 . ? 35.405 -55.680 6.490 1.00 32.83 ? 2054 HOH A O 1 HETATM 4004 O O . HOH W 5 . ? 44.908 -28.350 27.709 1.00 38.52 ? 2055 HOH A O 1 HETATM 4005 O O . HOH W 5 . ? 38.435 -50.388 -0.110 1.00 42.42 ? 2056 HOH A O 1 HETATM 4006 O O . HOH W 5 . ? 38.364 -38.419 6.166 1.00 36.39 ? 2057 HOH A O 1 HETATM 4007 O O . HOH W 5 . ? 35.128 -34.098 11.377 1.00 38.45 ? 2058 HOH A O 1 HETATM 4008 O O . HOH W 5 . ? 26.989 -32.575 6.687 1.00 43.16 ? 2059 HOH A O 1 HETATM 4009 O O . HOH W 5 . ? 24.736 -34.233 3.614 1.00 45.49 ? 2060 HOH A O 1 HETATM 4010 O O . HOH W 5 . ? 31.564 -30.523 6.323 1.00 18.93 ? 2061 HOH A O 1 HETATM 4011 O O . HOH W 5 . ? 35.506 -28.871 12.120 1.00 39.16 ? 2062 HOH A O 1 HETATM 4012 O O . HOH W 5 . ? 33.309 -29.165 15.540 1.00 44.02 ? 2063 HOH A O 1 HETATM 4013 O O . HOH W 5 . ? 32.336 -27.971 5.349 1.00 37.58 ? 2064 HOH A O 1 HETATM 4014 O O . HOH W 5 . ? 28.942 -30.184 6.895 1.00 45.13 ? 2065 HOH A O 1 HETATM 4015 O O . HOH W 5 . ? 36.115 -31.969 12.931 1.00 48.76 ? 2066 HOH A O 1 HETATM 4016 O O . HOH W 5 . ? 40.786 -33.735 18.245 1.00 34.90 ? 2067 HOH A O 1 HETATM 4017 O O . HOH W 5 . ? 35.625 -31.044 35.187 1.00 48.41 ? 2068 HOH A O 1 HETATM 4018 O O . HOH W 5 . ? 43.221 -34.352 18.985 1.00 44.42 ? 2069 HOH A O 1 HETATM 4019 O O . HOH W 5 . ? 52.334 -34.591 16.582 1.00 51.94 ? 2070 HOH A O 1 HETATM 4020 O O . HOH W 5 . ? 50.524 -36.573 13.987 1.00 46.52 ? 2071 HOH A O 1 HETATM 4021 O O . HOH W 5 . ? 49.112 -34.221 14.328 1.00 39.01 ? 2072 HOH A O 1 HETATM 4022 O O . HOH W 5 . ? 31.050 -26.921 -1.588 1.00 57.18 ? 2073 HOH A O 1 HETATM 4023 O O . HOH W 5 . ? 45.665 -31.900 12.265 1.00 36.00 ? 2074 HOH A O 1 HETATM 4024 O O . HOH W 5 . ? 45.784 -35.626 6.520 1.00 32.06 ? 2075 HOH A O 1 HETATM 4025 O O . HOH W 5 . ? 44.729 -41.977 4.846 1.00 22.98 ? 2076 HOH A O 1 HETATM 4026 O O . HOH W 5 . ? 45.783 -47.561 8.171 1.00 36.25 ? 2077 HOH A O 1 HETATM 4027 O O . HOH W 5 . ? 44.457 -39.369 4.792 1.00 27.68 ? 2078 HOH A O 1 HETATM 4028 O O . HOH W 5 . ? 47.255 -42.473 4.034 1.00 46.36 ? 2079 HOH A O 1 HETATM 4029 O O . HOH W 5 . ? 38.403 -55.581 28.358 1.00 51.35 ? 2080 HOH A O 1 HETATM 4030 O O . HOH W 5 . ? 39.665 -53.500 29.915 1.00 56.83 ? 2081 HOH A O 1 HETATM 4031 O O . HOH W 5 . ? 38.370 -57.073 31.604 1.00 43.15 ? 2082 HOH A O 1 HETATM 4032 O O . HOH W 5 . ? 44.711 -57.124 34.640 1.00 37.65 ? 2083 HOH A O 1 HETATM 4033 O O . HOH W 5 . ? 37.886 -54.656 37.471 1.00 40.20 ? 2084 HOH A O 1 HETATM 4034 O O . HOH W 5 . ? 40.253 -50.187 31.233 1.00 38.07 ? 2085 HOH A O 1 HETATM 4035 O O . HOH W 5 . ? 44.727 -54.831 40.759 1.00 52.52 ? 2086 HOH A O 1 HETATM 4036 O O . HOH W 5 . ? 45.869 -53.504 43.853 1.00 51.37 ? 2087 HOH A O 1 HETATM 4037 O O . HOH W 5 . ? 43.599 -57.604 41.026 1.00 58.83 ? 2088 HOH A O 1 HETATM 4038 O O . HOH W 5 . ? 38.352 -39.478 43.355 1.00 36.67 ? 2089 HOH A O 1 HETATM 4039 O O . HOH W 5 . ? 32.779 -38.938 39.296 1.00 41.95 ? 2090 HOH A O 1 HETATM 4040 O O . HOH W 5 . ? 31.350 -34.941 37.733 1.00 38.14 ? 2091 HOH A O 1 HETATM 4041 O O . HOH W 5 . ? 34.105 -36.019 38.027 1.00 49.52 ? 2092 HOH A O 1 HETATM 4042 O O . HOH W 5 . ? 27.253 -34.413 36.170 1.00 49.02 ? 2093 HOH A O 1 HETATM 4043 O O . HOH W 5 . ? 29.971 -31.563 36.126 1.00 52.86 ? 2094 HOH A O 1 HETATM 4044 O O . HOH W 5 . ? 27.407 -35.333 25.111 1.00 43.65 ? 2095 HOH A O 1 HETATM 4045 O O . HOH W 5 . ? 22.146 -35.195 31.647 1.00 48.19 ? 2096 HOH A O 1 HETATM 4046 O O . HOH W 5 . ? 24.105 -42.877 31.046 1.00 54.72 ? 2097 HOH A O 1 HETATM 4047 O O . HOH W 5 . ? 32.607 -45.329 29.834 1.00 37.50 ? 2098 HOH A O 1 HETATM 4048 O O . HOH W 5 . ? 31.563 -50.083 24.047 1.00 44.21 ? 2099 HOH A O 1 HETATM 4049 O O . HOH W 5 . ? 34.362 -47.430 46.272 1.00 49.30 ? 2100 HOH A O 1 HETATM 4050 O O . HOH W 5 . ? 34.090 -40.089 47.761 1.00 47.47 ? 2101 HOH A O 1 HETATM 4051 O O . HOH W 5 . ? 38.174 -34.577 50.174 1.00 46.86 ? 2102 HOH A O 1 HETATM 4052 O O . HOH W 5 . ? 47.321 -49.774 42.018 1.00 45.50 ? 2103 HOH A O 1 HETATM 4053 O O . HOH W 5 . ? 54.368 -49.792 38.291 1.00 46.34 ? 2104 HOH A O 1 HETATM 4054 O O . HOH W 5 . ? 52.003 -54.797 31.676 1.00 36.67 ? 2105 HOH A O 1 HETATM 4055 O O . HOH W 5 . ? 46.565 -55.563 32.669 1.00 39.72 ? 2106 HOH A O 1 HETATM 4056 O O . HOH W 5 . ? 45.748 -61.193 24.878 1.00 50.86 ? 2107 HOH A O 1 HETATM 4057 O O . HOH W 5 . ? 52.478 -65.449 22.629 1.00 45.96 ? 2108 HOH A O 1 HETATM 4058 O O . HOH W 5 . ? 44.780 -53.820 12.636 1.00 27.36 ? 2109 HOH A O 1 HETATM 4059 O O . HOH W 5 . ? 50.191 -41.202 31.028 1.00 34.18 ? 2110 HOH A O 1 HETATM 4060 O O . HOH W 5 . ? 45.005 -33.053 36.380 1.00 30.20 ? 2111 HOH A O 1 HETATM 4061 O O . HOH W 5 . ? 46.410 -35.410 37.091 1.00 33.16 ? 2112 HOH A O 1 HETATM 4062 O O . HOH W 5 . ? 41.938 -28.123 32.712 1.00 30.75 ? 2113 HOH A O 1 HETATM 4063 O O . HOH W 5 . ? 50.105 -34.716 31.369 1.00 45.63 ? 2114 HOH A O 1 HETATM 4064 O O . HOH W 5 . ? 38.642 -30.760 36.430 1.00 41.87 ? 2115 HOH A O 1 HETATM 4065 O O . HOH W 5 . ? 43.792 -34.406 38.166 1.00 43.14 ? 2116 HOH A O 1 HETATM 4066 O O . HOH W 5 . ? 35.083 -30.194 42.868 1.00 45.49 ? 2117 HOH A O 1 HETATM 4067 O O . HOH W 5 . ? 54.233 -37.197 45.800 1.00 60.64 ? 2118 HOH A O 1 HETATM 4068 O O . HOH W 5 . ? 49.889 -42.201 37.346 1.00 45.26 ? 2119 HOH A O 1 HETATM 4069 O O . HOH W 5 . ? 59.418 -53.039 24.957 1.00 30.20 ? 2120 HOH A O 1 HETATM 4070 O O . HOH W 5 . ? 61.828 -50.666 24.228 1.00 37.09 ? 2121 HOH A O 1 HETATM 4071 O O . HOH W 5 . ? 53.211 -43.550 26.182 1.00 36.79 ? 2122 HOH A O 1 HETATM 4072 O O . HOH W 5 . ? 52.564 -40.602 22.210 1.00 52.80 ? 2123 HOH A O 1 HETATM 4073 O O . HOH W 5 . ? 58.259 -43.476 21.853 1.00 52.44 ? 2124 HOH A O 1 HETATM 4074 O O . HOH W 5 . ? 60.037 -41.166 27.764 1.00 32.19 ? 2125 HOH A O 1 HETATM 4075 O O . HOH W 5 . ? 45.756 -26.861 29.548 1.00 25.25 ? 2126 HOH A O 1 HETATM 4076 O O . HOH W 5 . ? 35.130 -27.764 35.487 1.00 34.96 ? 2127 HOH A O 1 HETATM 4077 O O . HOH W 5 . ? 48.081 -37.097 25.787 1.00 45.10 ? 2128 HOH A O 1 HETATM 4078 O O . HOH W 5 . ? 49.852 -35.761 28.898 1.00 47.26 ? 2129 HOH A O 1 HETATM 4079 O O . HOH W 5 . ? 52.891 -43.602 18.307 1.00 40.98 ? 2130 HOH A O 1 HETATM 4080 O O . HOH W 5 . ? 52.797 -46.427 17.162 1.00 44.53 ? 2131 HOH A O 1 HETATM 4081 O O . HOH W 5 . ? 57.236 -60.467 20.622 1.00 62.24 ? 2132 HOH A O 1 HETATM 4082 O O . HOH W 5 . ? 56.904 -64.563 17.422 1.00 48.64 ? 2133 HOH A O 1 HETATM 4083 O O . HOH W 5 . ? 46.667 -49.636 32.466 1.00 53.97 ? 2134 HOH A O 1 HETATM 4084 O O . HOH W 5 . ? 52.848 -41.222 45.551 1.00 47.07 ? 2135 HOH A O 1 HETATM 4085 O O . HOH W 5 . ? 43.246 -45.578 34.163 1.00 43.67 ? 2136 HOH A O 1 HETATM 4086 O O . HOH W 5 . ? 35.973 -56.647 8.663 1.00 37.21 ? 2137 HOH A O 1 HETATM 4087 O O . HOH W 5 . ? 33.014 -57.626 12.862 1.00 50.01 ? 2138 HOH A O 1 HETATM 4088 O O . HOH W 5 . ? 45.636 -52.076 3.382 1.00 54.78 ? 2139 HOH A O 1 HETATM 4089 O O . HOH W 5 . ? 38.954 -53.586 2.595 1.00 40.81 ? 2140 HOH A O 1 HETATM 4090 O O . HOH W 5 . ? 42.958 -48.044 0.651 1.00 48.48 ? 2141 HOH A O 1 HETATM 4091 O O . HOH W 5 . ? 42.374 -39.689 2.010 1.00 25.05 ? 2142 HOH A O 1 HETATM 4092 O O . HOH W 5 . ? 42.525 -42.116 3.046 1.00 25.91 ? 2143 HOH A O 1 HETATM 4093 O O . HOH W 5 . ? 38.834 -33.640 1.520 1.00 20.89 ? 2144 HOH A O 1 HETATM 4094 O O . HOH W 5 . ? 40.557 -31.942 2.942 1.00 24.42 ? 2145 HOH A O 1 HETATM 4095 O O . HOH W 5 . ? 24.966 -31.017 -1.127 1.00 34.60 ? 2146 HOH A O 1 HETATM 4096 O O . HOH W 5 . ? 24.447 -36.862 2.507 1.00 28.84 ? 2147 HOH A O 1 HETATM 4097 O O . HOH W 5 . ? 21.983 -36.394 -3.565 1.00 42.27 ? 2148 HOH A O 1 HETATM 4098 O O . HOH W 5 . ? 21.719 -37.615 0.000 0.50 51.55 ? 2149 HOH A O 1 HETATM 4099 O O . HOH W 5 . ? 21.355 -41.013 -4.264 1.00 22.13 ? 2150 HOH A O 1 HETATM 4100 O O . HOH W 5 . ? 28.121 -41.165 -12.594 1.00 47.90 ? 2151 HOH A O 1 HETATM 4101 O O . HOH W 5 . ? 38.986 -43.414 -5.025 1.00 39.09 ? 2152 HOH A O 1 HETATM 4102 O O . HOH W 5 . ? 38.881 -47.478 -8.765 1.00 58.60 ? 2153 HOH A O 1 HETATM 4103 O O . HOH W 5 . ? 39.218 -30.203 -1.126 1.00 19.86 ? 2154 HOH A O 1 HETATM 4104 O O . HOH W 5 . ? 34.461 -26.618 -1.295 1.00 53.25 ? 2155 HOH A O 1 HETATM 4105 O O . HOH W 5 . ? 39.010 -26.630 -0.278 1.00 50.39 ? 2156 HOH A O 1 HETATM 4106 O O . HOH W 5 . ? 30.260 -27.491 -4.246 1.00 28.25 ? 2157 HOH A O 1 HETATM 4107 O O . HOH W 5 . ? 35.932 -40.053 -13.402 1.00 41.59 ? 2158 HOH A O 1 HETATM 4108 O O . HOH W 5 . ? 40.271 -38.770 -16.199 1.00 44.97 ? 2159 HOH A O 1 HETATM 4109 O O . HOH W 5 . ? 35.423 -36.884 -19.893 1.00 39.62 ? 2160 HOH A O 1 HETATM 4110 O O . HOH W 5 . ? 44.502 -33.728 -9.112 1.00 36.70 ? 2161 HOH A O 1 HETATM 4111 O O . HOH W 5 . ? 38.374 -23.464 -13.170 1.00 31.23 ? 2162 HOH A O 1 HETATM 4112 O O . HOH W 5 . ? 41.960 -23.838 -9.533 1.00 33.56 ? 2163 HOH A O 1 HETATM 4113 O O . HOH W 5 . ? 44.701 -21.670 -11.188 1.00 38.66 ? 2164 HOH A O 1 HETATM 4114 O O . HOH W 5 . ? 41.540 -27.574 -1.162 1.00 34.48 ? 2165 HOH A O 1 HETATM 4115 O O . HOH W 5 . ? 43.069 -25.536 -5.384 1.00 36.28 ? 2166 HOH A O 1 HETATM 4116 O O . HOH W 5 . ? 47.727 -31.817 -6.680 1.00 22.03 ? 2167 HOH A O 1 HETATM 4117 O O . HOH W 5 . ? 43.809 -25.453 -2.427 1.00 46.48 ? 2168 HOH A O 1 HETATM 4118 O O . HOH W 5 . ? 46.918 -25.190 -3.483 1.00 43.53 ? 2169 HOH A O 1 HETATM 4119 O O . HOH W 5 . ? 40.226 -32.843 -0.931 1.00 22.66 ? 2170 HOH A O 1 HETATM 4120 O O . HOH W 5 . ? 45.054 -33.619 -1.125 1.00 30.92 ? 2171 HOH A O 1 HETATM 4121 O O . HOH W 5 . ? 44.695 -36.968 -6.693 1.00 57.71 ? 2172 HOH A O 1 HETATM 4122 O O . HOH W 5 . ? 45.066 -39.304 -8.436 1.00 32.42 ? 2173 HOH A O 1 HETATM 4123 O O . HOH W 5 . ? 41.725 -49.129 -5.456 1.00 47.77 ? 2174 HOH A O 1 HETATM 4124 O O . HOH W 5 . ? 43.564 -49.946 -7.629 1.00 48.32 ? 2175 HOH A O 1 HETATM 4125 O O . HOH W 5 . ? 46.932 -37.346 -10.037 1.00 27.99 ? 2176 HOH A O 1 HETATM 4126 O O . HOH W 5 . ? 49.569 -38.866 -15.371 1.00 59.11 ? 2177 HOH A O 1 HETATM 4127 O O . HOH W 5 . ? 48.889 -39.445 -12.506 1.00 44.91 ? 2178 HOH A O 1 HETATM 4128 O O . HOH W 5 . ? 47.841 -33.262 -9.203 1.00 34.05 ? 2179 HOH A O 1 HETATM 4129 O O . HOH W 5 . ? 49.420 -31.157 -10.071 1.00 19.62 ? 2180 HOH A O 1 HETATM 4130 O O . HOH W 5 . ? 45.946 -23.960 -6.062 1.00 53.55 ? 2181 HOH A O 1 HETATM 4131 O O . HOH W 5 . ? 44.551 -19.603 -17.644 1.00 35.63 ? 2182 HOH A O 1 HETATM 4132 O O . HOH W 5 . ? 43.770 -20.955 -19.606 1.00 43.69 ? 2183 HOH A O 1 HETATM 4133 O O . HOH W 5 . ? 37.130 -21.931 -14.656 1.00 46.48 ? 2184 HOH A O 1 HETATM 4134 O O . HOH W 5 . ? 39.224 -19.904 -14.797 1.00 68.01 ? 2185 HOH A O 1 HETATM 4135 O O . HOH W 5 . ? 44.326 -23.473 -25.316 1.00 32.77 ? 2186 HOH A O 1 HETATM 4136 O O . HOH W 5 . ? 46.525 -32.045 -31.533 1.00 25.80 ? 2187 HOH A O 1 HETATM 4137 O O . HOH W 5 . ? 46.832 -28.178 -41.402 1.00 28.63 ? 2188 HOH A O 1 HETATM 4138 O O . HOH W 5 . ? 42.296 -18.535 -40.105 1.00 54.57 ? 2189 HOH A O 1 HETATM 4139 O O . HOH W 5 . ? 38.439 -21.969 -54.399 1.00 55.15 ? 2190 HOH A O 1 HETATM 4140 O O . HOH W 5 . ? 33.129 -37.331 -30.185 1.00 53.19 ? 2191 HOH A O 1 HETATM 4141 O O . HOH W 5 . ? 37.066 -34.526 -31.188 1.00 60.44 ? 2192 HOH A O 1 HETATM 4142 O O . HOH W 5 . ? 32.261 -12.273 -32.601 1.00 53.87 ? 2193 HOH A O 1 HETATM 4143 O O . HOH W 5 . ? 26.098 -15.009 -31.256 1.00 58.74 ? 2194 HOH A O 1 HETATM 4144 O O . HOH W 5 . ? 25.042 -44.875 39.990 1.00 53.16 ? 2195 HOH A O 1 HETATM 4145 O O . HOH W 5 . ? 32.448 -46.101 47.656 1.00 48.73 ? 2196 HOH A O 1 HETATM 4146 O O . HOH W 5 . ? 26.804 -27.226 -9.856 1.00 55.61 ? 2197 HOH A O 1 HETATM 4147 O O . HOH W 5 . ? 26.481 -26.313 -5.753 1.00 54.35 ? 2198 HOH A O 1 HETATM 4148 O O . HOH W 5 . ? 38.844 -27.697 17.533 1.00 53.32 ? 2199 HOH A O 1 HETATM 4149 O O . HOH W 5 . ? 41.606 -63.034 14.636 1.00 57.78 ? 2200 HOH A O 1 HETATM 4150 O O . HOH X 5 . ? 51.524 -25.414 -45.139 1.00 42.78 ? 2001 HOH B O 1 HETATM 4151 O O . HOH X 5 . ? 48.897 -26.188 -42.291 1.00 36.47 ? 2002 HOH B O 1 HETATM 4152 O O . HOH X 5 . ? 53.896 -22.986 -42.288 1.00 44.21 ? 2003 HOH B O 1 HETATM 4153 O O . HOH X 5 . ? 53.469 -23.410 -45.529 1.00 42.92 ? 2004 HOH B O 1 HETATM 4154 O O . HOH X 5 . ? 47.446 -20.011 -48.432 1.00 45.59 ? 2005 HOH B O 1 HETATM 4155 O O . HOH X 5 . ? 49.437 -18.968 -52.162 1.00 59.09 ? 2006 HOH B O 1 HETATM 4156 O O . HOH X 5 . ? 49.201 -20.850 -55.249 1.00 45.80 ? 2007 HOH B O 1 HETATM 4157 O O . HOH X 5 . ? 40.771 -23.138 -55.675 1.00 50.47 ? 2008 HOH B O 1 HETATM 4158 O O . HOH X 5 . ? 30.871 -32.116 -49.553 1.00 57.78 ? 2009 HOH B O 1 HETATM 4159 O O . HOH X 5 . ? 33.912 -34.148 -43.218 1.00 57.82 ? 2010 HOH B O 1 HETATM 4160 O O . HOH X 5 . ? 33.036 -32.864 -69.886 1.00 54.73 ? 2011 HOH B O 1 HETATM 4161 O O . HOH X 5 . ? 35.104 -23.223 -57.919 1.00 44.67 ? 2012 HOH B O 1 HETATM 4162 O O . HOH X 5 . ? 31.459 -33.459 -51.792 1.00 62.33 ? 2013 HOH B O 1 HETATM 4163 O O . HOH X 5 . ? 42.197 -44.978 -34.896 1.00 51.84 ? 2014 HOH B O 1 HETATM 4164 O O . HOH X 5 . ? 45.249 -26.718 -74.859 1.00 50.68 ? 2015 HOH B O 1 HETATM 4165 O O . HOH X 5 . ? 50.903 -38.915 -22.556 1.00 42.48 ? 2016 HOH B O 1 HETATM 4166 O O . HOH X 5 . ? 44.818 -46.634 -15.162 1.00 59.82 ? 2017 HOH B O 1 HETATM 4167 O O . HOH X 5 . ? 46.557 -46.843 -6.860 1.00 40.80 ? 2018 HOH B O 1 HETATM 4168 O O . HOH X 5 . ? 48.038 -44.506 -1.567 1.00 49.11 ? 2019 HOH B O 1 HETATM 4169 O O . HOH X 5 . ? 49.701 -42.097 -3.094 1.00 40.67 ? 2020 HOH B O 1 HETATM 4170 O O . HOH X 5 . ? 44.107 -47.865 -4.265 1.00 53.55 ? 2021 HOH B O 1 HETATM 4171 O O . HOH X 5 . ? 49.043 -40.278 -0.842 1.00 33.72 ? 2022 HOH B O 1 HETATM 4172 O O . HOH X 5 . ? 48.280 -39.914 3.853 1.00 38.83 ? 2023 HOH B O 1 HETATM 4173 O O . HOH X 5 . ? 46.191 -33.262 1.129 1.00 30.50 ? 2024 HOH B O 1 HETATM 4174 O O . HOH X 5 . ? 49.597 -28.394 4.360 1.00 21.77 ? 2025 HOH B O 1 HETATM 4175 O O . HOH X 5 . ? 46.143 -28.830 7.371 1.00 20.78 ? 2026 HOH B O 1 HETATM 4176 O O . HOH X 5 . ? 49.562 -25.920 8.283 1.00 37.64 ? 2027 HOH B O 1 HETATM 4177 O O . HOH X 5 . ? 57.634 -30.218 11.976 1.00 44.09 ? 2028 HOH B O 1 HETATM 4178 O O . HOH X 5 . ? 51.438 -25.214 14.171 1.00 40.99 ? 2029 HOH B O 1 HETATM 4179 O O . HOH X 5 . ? 50.771 -18.834 7.330 1.00 55.05 ? 2030 HOH B O 1 HETATM 4180 O O . HOH X 5 . ? 49.914 -17.545 9.653 1.00 50.80 ? 2031 HOH B O 1 HETATM 4181 O O . HOH X 5 . ? 60.676 -26.520 7.500 1.00 34.62 ? 2032 HOH B O 1 HETATM 4182 O O . HOH X 5 . ? 55.769 -23.304 1.806 1.00 35.69 ? 2033 HOH B O 1 HETATM 4183 O O . HOH X 5 . ? 52.307 -22.614 3.028 1.00 43.55 ? 2034 HOH B O 1 HETATM 4184 O O . HOH X 5 . ? 54.114 -20.076 6.732 1.00 54.28 ? 2035 HOH B O 1 HETATM 4185 O O . HOH X 5 . ? 51.031 -23.014 -1.021 1.00 48.43 ? 2036 HOH B O 1 HETATM 4186 O O . HOH X 5 . ? 61.870 -22.852 -1.901 1.00 39.81 ? 2037 HOH B O 1 HETATM 4187 O O . HOH X 5 . ? 58.067 -33.524 0.128 0.33 14.43 ? 2038 HOH B O 1 HETATM 4188 O O . HOH X 5 . ? 49.854 -30.337 -7.417 1.00 27.83 ? 2039 HOH B O 1 HETATM 4189 O O . HOH X 5 . ? 47.584 -32.640 -2.065 1.00 38.70 ? 2040 HOH B O 1 HETATM 4190 O O . HOH X 5 . ? 49.283 -25.799 -1.724 1.00 56.05 ? 2041 HOH B O 1 HETATM 4191 O O . HOH X 5 . ? 52.483 -23.885 -8.455 1.00 38.08 ? 2042 HOH B O 1 HETATM 4192 O O . HOH X 5 . ? 49.354 -26.196 -6.166 1.00 22.97 ? 2043 HOH B O 1 HETATM 4193 O O . HOH X 5 . ? 58.606 -29.345 -9.221 1.00 74.27 ? 2044 HOH B O 1 HETATM 4194 O O . HOH X 5 . ? 60.820 -28.512 -4.540 1.00 50.95 ? 2045 HOH B O 1 HETATM 4195 O O . HOH X 5 . ? 52.338 -36.156 -9.568 1.00 17.87 ? 2046 HOH B O 1 HETATM 4196 O O . HOH X 5 . ? 54.563 -33.005 -21.610 1.00 20.77 ? 2047 HOH B O 1 HETATM 4197 O O . HOH X 5 . ? 58.067 -33.524 -16.362 0.33 36.85 ? 2048 HOH B O 1 HETATM 4198 O O . HOH X 5 . ? 50.241 -24.787 -24.981 1.00 26.00 ? 2049 HOH B O 1 HETATM 4199 O O . HOH X 5 . ? 55.644 -31.797 -33.260 1.00 58.77 ? 2050 HOH B O 1 HETATM 4200 O O . HOH X 5 . ? 55.919 -27.338 -37.733 1.00 31.65 ? 2051 HOH B O 1 HETATM 4201 O O . HOH X 5 . ? 55.589 -31.435 -36.114 1.00 36.01 ? 2052 HOH B O 1 HETATM 4202 O O . HOH X 5 . ? 49.033 -27.422 -58.733 1.00 42.68 ? 2053 HOH B O 1 HETATM 4203 O O . HOH X 5 . ? 49.044 -42.856 -57.543 1.00 43.69 ? 2054 HOH B O 1 HETATM 4204 O O . HOH X 5 . ? 46.231 -40.942 -49.764 1.00 40.75 ? 2055 HOH B O 1 HETATM 4205 O O . HOH X 5 . ? 51.595 -40.242 -69.980 1.00 54.24 ? 2056 HOH B O 1 HETATM 4206 O O . HOH X 5 . ? 53.579 -33.944 -70.470 1.00 39.30 ? 2057 HOH B O 1 HETATM 4207 O O . HOH X 5 . ? 47.051 -29.810 -70.064 1.00 52.56 ? 2058 HOH B O 1 HETATM 4208 O O . HOH X 5 . ? 43.708 -29.231 -74.633 1.00 52.90 ? 2059 HOH B O 1 HETATM 4209 O O . HOH X 5 . ? 30.442 -41.930 -66.163 1.00 39.25 ? 2060 HOH B O 1 HETATM 4210 O O . HOH X 5 . ? 35.430 -46.261 -60.166 1.00 47.21 ? 2061 HOH B O 1 HETATM 4211 O O . HOH X 5 . ? 48.749 -50.411 -71.927 1.00 55.24 ? 2062 HOH B O 1 HETATM 4212 O O . HOH X 5 . ? 46.156 -41.209 -76.758 1.00 39.62 ? 2063 HOH B O 1 HETATM 4213 O O . HOH X 5 . ? 49.702 -36.970 -85.391 1.00 59.09 ? 2064 HOH B O 1 HETATM 4214 O O . HOH X 5 . ? 42.867 -32.856 -77.325 1.00 49.82 ? 2065 HOH B O 1 HETATM 4215 O O . HOH X 5 . ? 42.751 -22.345 -0.768 1.00 48.04 ? 2066 HOH B O 1 HETATM 4216 O O . HOH X 5 . ? 44.358 -24.040 -75.687 1.00 61.56 ? 2067 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 ? 1.4948 1.5362 0.4718 0.1430 -0.2544 0.2475 1 ASP A N 2 C CA . ASP A 1 ? 1.5020 1.4991 0.4622 0.1510 -0.2210 0.2476 1 ASP A CA 3 C C . ASP A 1 ? 1.4501 1.4279 0.4538 0.1465 -0.1986 0.2310 1 ASP A C 4 O O . ASP A 1 ? 1.4559 1.4023 0.4404 0.1403 -0.1786 0.2152 1 ASP A O 5 C CB . ASP A 1 ? 1.5185 1.5123 0.4757 0.1739 -0.2104 0.2785 1 ASP A CB 6 C CG . ASP A 1 ? 1.5589 1.5133 0.4686 0.1793 -0.1860 0.2821 1 ASP A CG 7 O OD1 . ASP A 1 ? 1.5497 1.4752 0.4537 0.1703 -0.1654 0.2629 1 ASP A OD1 8 O OD2 . ASP A 1 ? 1.6017 1.5550 0.4794 0.1931 -0.1872 0.3049 1 ASP A OD2 9 N N . LYS A 2 ? 1.4010 1.3988 0.4623 0.1498 -0.2016 0.2349 2 LYS A N 10 C CA . LYS A 2 ? 1.3526 1.3336 0.4561 0.1472 -0.1798 0.2224 2 LYS A CA 11 C C . LYS A 2 ? 1.3032 1.3069 0.4536 0.1363 -0.1934 0.2081 2 LYS A C 12 O O . LYS A 2 ? 1.2976 1.3356 0.4648 0.1358 -0.2174 0.2152 2 LYS A O 13 C CB . LYS A 2 ? 1.3403 1.3097 0.4686 0.1643 -0.1583 0.2429 2 LYS A CB 14 C CG . LYS A 2 ? 1.3237 1.3215 0.4896 0.1766 -0.1709 0.2629 2 LYS A CG 15 C CD . LYS A 2 ? 1.3234 1.3019 0.5034 0.1936 -0.1476 0.2837 2 LYS A CD 16 C CE . LYS A 2 ? 1.2895 1.2892 0.5208 0.2031 -0.1531 0.2954 2 LYS A CE 17 N NZ . LYS A 2 ? 1.3030 1.2845 0.5386 0.2222 -0.1345 0.3202 2 LYS A NZ 18 N N . ILE A 3 ? 1.2687 1.2545 0.4401 0.1279 -0.1773 0.1886 3 ILE A N 19 C CA . ILE A 3 ? 1.2189 1.2207 0.4377 0.1188 -0.1848 0.1755 3 ILE A CA 20 C C . ILE A 3 ? 1.1736 1.1619 0.4353 0.1246 -0.1606 0.1755 3 ILE A C 21 O O . ILE A 3 ? 1.1752 1.1366 0.4260 0.1253 -0.1372 0.1697 3 ILE A O 22 C CB . ILE A 3 ? 1.2233 1.2181 0.4247 0.1000 -0.1927 0.1486 3 ILE A CB 23 C CG1 . ILE A 3 ? 1.1762 1.1900 0.4255 0.0908 -0.2028 0.1375 3 ILE A CG1 24 C CG2 . ILE A 3 ? 1.2315 1.1896 0.4102 0.0979 -0.1675 0.1338 3 ILE A CG2 25 C CD1 . ILE A 3 ? 1.1858 1.1931 0.4171 0.0717 -0.2129 0.1126 3 ILE A CD1 26 N N . CYS A 4 ? 1.1346 1.1435 0.4446 0.1281 -0.1663 0.1821 4 CYS A N 27 C CA . CYS A 4 ? 1.0951 1.0930 0.4454 0.1336 -0.1449 0.1845 4 CYS A CA 28 C C . CYS A 4 ? 1.0452 1.0536 0.4384 0.1235 -0.1484 0.1681 4 CYS A C 29 O O . CYS A 4 ? 1.0335 1.0672 0.4418 0.1177 -0.1699 0.1649 4 CYS A O 30 C CB . CYS A 4 ? 1.0974 1.1030 0.4648 0.1501 -0.1426 0.2101 4 CYS A CB 31 S SG . CYS A 4 ? 1.1567 1.1440 0.4753 0.1643 -0.1332 0.2321 4 CYS A SG 32 N N . LEU A 5 ? 1.0165 1.0067 0.4287 0.1209 -0.1271 0.1583 5 LEU A N 33 C CA . LEU A 5 ? 0.9698 0.9671 0.4235 0.1129 -0.1268 0.1443 5 LEU A CA 34 C C . LEU A 5 ? 0.9375 0.9401 0.4335 0.1209 -0.1183 0.1567 5 LEU A C 35 O O . LEU A 5 ? 0.9476 0.9364 0.4404 0.1301 -0.1021 0.1707 5 LEU A O 36 C CB . LEU A 5 ? 0.9591 0.9359 0.4084 0.1056 -0.1091 0.1261 5 LEU A CB 37 C CG . LEU A 5 ? 0.9805 0.9502 0.3977 0.0954 -0.1170 0.1076 5 LEU A CG 38 C CD1 . LEU A 5 ? 0.9622 0.9493 0.3982 0.0852 -0.1376 0.0964 5 LEU A CD1 39 C CD2 . LEU A 5 ? 1.0329 0.9963 0.3984 0.0975 -0.1240 0.1135 5 LEU A CD2 40 N N . GLY A 6 ? 0.9027 0.9232 0.4363 0.1166 -0.1282 0.1514 6 GLY A N 41 C CA . GLY A 6 ? 0.8738 0.8984 0.4472 0.1236 -0.1202 0.1615 6 GLY A CA 42 C C . GLY A 6 ? 0.8296 0.8656 0.4423 0.1150 -0.1243 0.1481 6 GLY A C 43 O O . GLY A 6 ? 0.8204 0.8582 0.4301 0.1035 -0.1309 0.1302 6 GLY A O 44 N N . HIS A 7 ? 0.8061 0.8472 0.4535 0.1211 -0.1190 0.1571 7 HIS A N 45 C CA . HIS A 7 ? 0.7652 0.8169 0.4517 0.1143 -0.1214 0.1466 7 HIS A CA 46 C C . HIS A 7 ? 0.7572 0.8258 0.4728 0.1243 -0.1269 0.1619 7 HIS A C 47 O O . HIS A 7 ? 0.7776 0.8420 0.4859 0.1378 -0.1219 0.1807 7 HIS A O 48 C CB . HIS A 7 ? 0.7403 0.7721 0.4412 0.1093 -0.0997 0.1370 7 HIS A CB 49 C CG . HIS A 7 ? 0.7464 0.7601 0.4486 0.1177 -0.0800 0.1508 7 HIS A CG 50 N ND1 . HIS A 7 ? 0.7310 0.7446 0.4609 0.1238 -0.0741 0.1606 7 HIS A ND1 51 C CD2 . HIS A 7 ? 0.7700 0.7629 0.4468 0.1203 -0.0639 0.1566 7 HIS A CD2 52 C CE1 . HIS A 7 ? 0.7478 0.7389 0.4680 0.1290 -0.0551 0.1712 7 HIS A CE1 53 N NE2 . HIS A 7 ? 0.7704 0.7497 0.4594 0.1265 -0.0488 0.1692 7 HIS A NE2 54 N N . HIS A 8 ? 0.7307 0.8168 0.4785 0.1185 -0.1356 0.1543 8 HIS A N 55 C CA . HIS A 8 ? 0.7245 0.8295 0.5021 0.1284 -0.1407 0.1682 8 HIS A CA 56 C C . HIS A 8 ? 0.7198 0.8040 0.5159 0.1365 -0.1186 0.1759 8 HIS A C 57 O O . HIS A 8 ? 0.7127 0.7722 0.5052 0.1305 -0.1009 0.1672 8 HIS A O 58 C CB . HIS A 8 ? 0.6970 0.8289 0.5020 0.1188 -0.1573 0.1580 8 HIS A CB 59 C CG . HIS A 8 ? 0.6596 0.7813 0.4898 0.1089 -0.1471 0.1421 8 HIS A CG 60 N ND1 . HIS A 8 ? 0.6327 0.7743 0.4938 0.1029 -0.1563 0.1360 8 HIS A ND1 61 C CD2 . HIS A 8 ? 0.6463 0.7423 0.4754 0.1039 -0.1289 0.1318 8 HIS A CD2 62 C CE1 . HIS A 8 ? 0.6056 0.7321 0.4820 0.0953 -0.1443 0.1228 8 HIS A CE1 63 N NE2 . HIS A 8 ? 0.6128 0.7132 0.4709 0.0958 -0.1280 0.1201 8 HIS A NE2 64 N N . ALA A 9 ? 0.7297 0.8246 0.5444 0.1501 -0.1194 0.1926 9 ALA A N 65 C CA . ALA A 9 ? 0.7344 0.8068 0.5631 0.1589 -0.0982 0.2014 9 ALA A CA 66 C C . ALA A 9 ? 0.7380 0.8304 0.5942 0.1725 -0.1035 0.2158 9 ALA A C 67 O O . ALA A 9 ? 0.7439 0.8698 0.6055 0.1769 -0.1235 0.2225 9 ALA A O 68 C CB . ALA A 9 ? 0.7697 0.8138 0.5677 0.1680 -0.0827 0.2145 9 ALA A CB 69 N N . LEU A 10 ? 0.7420 0.8145 0.6152 0.1785 -0.0850 0.2205 10 LEU A N 70 C CA . LEU A 10 ? 0.7516 0.8374 0.6494 0.1944 -0.0850 0.2358 10 LEU A CA 71 C C . LEU A 10 ? 0.7960 0.8476 0.6805 0.2106 -0.0629 0.2532 10 LEU A C 72 O O . LEU A 10 ? 0.8065 0.8235 0.6691 0.2047 -0.0463 0.2495 10 LEU A O 73 C CB . LEU A 10 ? 0.7143 0.8058 0.6468 0.1857 -0.0823 0.2230 10 LEU A CB 74 C CG . LEU A 10 ? 0.6827 0.7956 0.6263 0.1660 -0.0981 0.2019 10 LEU A CG 75 C CD1 . LEU A 10 ? 0.6501 0.7562 0.6213 0.1566 -0.0889 0.1886 10 LEU A CD1 76 C CD2 . LEU A 10 ? 0.6821 0.8384 0.6344 0.1677 -0.1232 0.2064 10 LEU A CD2 77 N N . SER A 11 ? 0.8328 0.8940 0.7303 0.2310 -0.0619 0.2727 11 SER A N 78 C CA . SER A 11 ? 0.8861 0.9106 0.7710 0.2483 -0.0389 0.2903 11 SER A CA 79 C C . SER A 11 ? 0.8991 0.8850 0.7915 0.2384 -0.0150 0.2788 11 SER A C 80 O O . SER A 11 ? 0.9282 0.8719 0.8006 0.2435 0.0074 0.2863 11 SER A O 81 C CB . SER A 11 ? 0.9022 0.9483 0.8036 0.2740 -0.0427 0.3133 11 SER A CB 82 O OG . SER A 11 ? 0.9399 0.9452 0.8288 0.2917 -0.0178 0.3298 11 SER A OG 83 N N . ASN A 12 ? 0.8868 0.8867 0.8062 0.2234 -0.0200 0.2605 12 ASN A N 84 C CA . ASN A 12 ? 0.9023 0.8736 0.8338 0.2150 -0.0004 0.2504 12 ASN A CA 85 C C . ASN A 12 ? 0.8278 0.8151 0.7766 0.1918 -0.0098 0.2258 12 ASN A C 86 O O . ASN A 12 ? 0.8012 0.8244 0.7730 0.1898 -0.0277 0.2208 12 ASN A O 87 C CB . ASN A 12 ? 0.9683 0.9435 0.9223 0.2336 0.0056 0.2638 12 ASN A CB 88 C CG . ASN A 12 ? 1.0595 0.9898 1.0125 0.2318 0.0327 0.2611 12 ASN A CG 89 O OD1 . ASN A 12 ? 1.0715 0.9664 1.0040 0.2180 0.0480 0.2524 12 ASN A OD1 90 N ND2 . ASN A 12 ? 1.1546 1.0866 1.1292 0.2451 0.0395 0.2685 12 ASN A ND2 91 N N . GLY A 13 ? 0.7884 0.7502 0.7258 0.1744 0.0025 0.2113 13 GLY A N 92 C CA . GLY A 13 ? 0.7311 0.7063 0.6816 0.1540 -0.0049 0.1891 13 GLY A CA 93 C C . GLY A 13 ? 0.6867 0.6530 0.6601 0.1462 0.0053 0.1791 13 GLY A C 94 O O . GLY A 13 ? 0.6945 0.6477 0.6763 0.1573 0.0165 0.1889 13 GLY A O 95 N N . THR A 14 ? 0.6341 0.6069 0.6159 0.1279 0.0021 0.1601 14 THR A N 96 C CA . THR A 14 ? 0.5969 0.5602 0.5966 0.1180 0.0122 0.1491 14 THR A CA 97 C C . THR A 14 ? 0.5862 0.5255 0.5713 0.1017 0.0271 0.1386 14 THR A C 98 O O . THR A 14 ? 0.5747 0.5228 0.5506 0.0919 0.0214 0.1298 14 THR A O 99 C CB . THR A 14 ? 0.5594 0.5527 0.5834 0.1101 -0.0040 0.1361 14 THR A CB 100 O OG1 . THR A 14 ? 0.5565 0.5774 0.5936 0.1226 -0.0198 0.1456 14 THR A OG1 101 C CG2 . THR A 14 ? 0.5428 0.5261 0.5845 0.1022 0.0067 0.1272 14 THR A CG2 102 N N . LYS A 15 ? 0.5867 0.4964 0.5693 0.0985 0.0467 0.1395 15 LYS A N 103 C CA . LYS A 15 ? 0.5879 0.4757 0.5564 0.0814 0.0619 0.1307 15 LYS A CA 104 C C . LYS A 15 ? 0.5439 0.4490 0.5285 0.0637 0.0568 0.1120 15 LYS A C 105 O O . LYS A 15 ? 0.5181 0.4326 0.5231 0.0627 0.0526 0.1062 15 LYS A O 106 C CB . LYS A 15 ? 0.6216 0.4695 0.5791 0.0815 0.0849 0.1370 15 LYS A CB 107 C CG . LYS A 15 ? 0.6673 0.4918 0.6028 0.0980 0.0938 0.1560 15 LYS A CG 108 C CD . LYS A 15 ? 0.7095 0.4868 0.6279 0.0960 0.1195 0.1612 15 LYS A CD 109 C CE . LYS A 15 ? 0.7103 0.4782 0.6450 0.1017 0.1259 0.1608 15 LYS A CE 110 N NZ . LYS A 15 ? 0.7606 0.4843 0.6763 0.1154 0.1474 0.1757 15 LYS A NZ 111 N N . VAL A 16 ? 0.5299 0.4402 0.5047 0.0512 0.0574 0.1039 16 VAL A N 112 C CA . VAL A 16 ? 0.4955 0.4214 0.4825 0.0352 0.0549 0.0878 16 VAL A CA 113 C C . VAL A 16 ? 0.5057 0.4199 0.4785 0.0195 0.0694 0.0834 16 VAL A C 114 O O . VAL A 16 ? 0.5308 0.4273 0.4830 0.0209 0.0792 0.0920 16 VAL A O 115 C CB . VAL A 16 ? 0.4682 0.4250 0.4628 0.0371 0.0358 0.0809 16 VAL A CB 116 C CG1 . VAL A 16 ? 0.4565 0.4275 0.4658 0.0492 0.0209 0.0844 16 VAL A CG1 117 C CG2 . VAL A 16 ? 0.4825 0.4426 0.4567 0.0400 0.0332 0.0846 16 VAL A CG2 118 N N . ASN A 17 ? 0.4828 0.4090 0.4668 0.0043 0.0707 0.0706 17 ASN A N 119 C CA . ASN A 17 ? 0.4905 0.4139 0.4656 -0.0130 0.0831 0.0654 17 ASN A CA 120 C C . ASN A 17 ? 0.4680 0.4212 0.4460 -0.0158 0.0742 0.0586 17 ASN A C 121 O O . ASN A 17 ? 0.4413 0.4159 0.4328 -0.0106 0.0602 0.0527 17 ASN A O 122 C CB . ASN A 17 ? 0.4860 0.4033 0.4705 -0.0289 0.0919 0.0567 17 ASN A CB 123 C CG . ASN A 17 ? 0.5146 0.3964 0.4917 -0.0269 0.1047 0.0629 17 ASN A CG 124 O OD1 . ASN A 17 ? 0.5466 0.4023 0.5054 -0.0203 0.1145 0.0739 17 ASN A OD1 125 N ND2 . ASN A 17 ? 0.5049 0.3838 0.4943 -0.0319 0.1056 0.0564 17 ASN A ND2 126 N N . THR A 18 ? 0.4817 0.4346 0.4458 -0.0238 0.0837 0.0599 18 THR A N 127 C CA . THR A 18 ? 0.4683 0.4484 0.4335 -0.0256 0.0786 0.0545 18 THR A CA 128 C C . THR A 18 ? 0.4716 0.4615 0.4394 -0.0450 0.0910 0.0488 18 THR A C 129 O O . THR A 18 ? 0.4775 0.4548 0.4480 -0.0583 0.1004 0.0466 18 THR A O 130 C CB . THR A 18 ? 0.4868 0.4633 0.4321 -0.0145 0.0771 0.0626 18 THR A CB 131 O OG1 . THR A 18 ? 0.5168 0.4722 0.4437 -0.0214 0.0935 0.0703 18 THR A OG1 132 C CG2 . THR A 18 ? 0.4907 0.4593 0.4325 0.0031 0.0644 0.0694 18 THR A CG2 133 N N . LEU A 19 ? 0.4698 0.4833 0.4366 -0.0472 0.0912 0.0462 19 LEU A N 134 C CA . LEU A 19 ? 0.4756 0.5055 0.4467 -0.0658 0.1025 0.0420 19 LEU A CA 135 C C . LEU A 19 ? 0.5163 0.5223 0.4688 -0.0772 0.1195 0.0489 19 LEU A C 136 O O . LEU A 19 ? 0.5241 0.5303 0.4784 -0.0973 0.1308 0.0458 19 LEU A O 137 C CB . LEU A 19 ? 0.4629 0.5261 0.4383 -0.0625 0.0996 0.0390 19 LEU A CB 138 C CG . LEU A 19 ? 0.4338 0.5221 0.4254 -0.0524 0.0856 0.0318 19 LEU A CG 139 C CD1 . LEU A 19 ? 0.4312 0.5460 0.4211 -0.0474 0.0872 0.0311 19 LEU A CD1 140 C CD2 . LEU A 19 ? 0.4131 0.5153 0.4248 -0.0637 0.0837 0.0244 19 LEU A CD2 141 N N . THR A 20 ? 0.5478 0.5328 0.4807 -0.0651 0.1213 0.0584 20 THR A N 142 C CA . THR A 20 ? 0.5926 0.5531 0.5040 -0.0737 0.1380 0.0665 20 THR A CA 143 C C . THR A 20 ? 0.6298 0.5477 0.5275 -0.0703 0.1447 0.0743 20 THR A C 144 O O . THR A 20 ? 0.6667 0.5581 0.5461 -0.0804 0.1612 0.0801 20 THR A O 145 C CB . THR A 20 ? 0.6067 0.5702 0.5009 -0.0624 0.1383 0.0737 20 THR A CB 146 O OG1 . THR A 20 ? 0.5994 0.5588 0.4897 -0.0405 0.1232 0.0774 20 THR A OG1 147 C CG2 . THR A 20 ? 0.5899 0.5917 0.4936 -0.0676 0.1382 0.0676 20 THR A CG2 148 N N . GLU A 21 ? 0.6271 0.5379 0.5331 -0.0560 0.1333 0.0748 21 GLU A N 149 C CA . GLU A 21 ? 0.6624 0.5357 0.5544 -0.0456 0.1385 0.0854 21 GLU A CA 150 C C . GLU A 21 ? 0.6489 0.5148 0.5561 -0.0412 0.1330 0.0822 21 GLU A C 151 O O . GLU A 21 ? 0.6192 0.5103 0.5463 -0.0351 0.1176 0.0755 21 GLU A O 152 C CB . GLU A 21 ? 0.6791 0.5513 0.5586 -0.0240 0.1292 0.0961 21 GLU A CB 153 C CG . GLU A 21 ? 0.7277 0.5615 0.5824 -0.0153 0.1409 0.1111 21 GLU A CG 154 C CD . GLU A 21 ? 0.7470 0.5837 0.5848 0.0020 0.1334 0.1217 21 GLU A CD 155 O OE1 . GLU A 21 ? 0.7326 0.5966 0.5721 0.0027 0.1240 0.1166 21 GLU A OE1 156 O OE2 . GLU A 21 ? 0.7830 0.5933 0.6038 0.0154 0.1376 0.1356 21 GLU A OE2 157 N N . ARG A 22 ? 0.6757 0.5049 0.5718 -0.0444 0.1472 0.0870 22 ARG A N 158 C CA . ARG A 22 ? 0.6686 0.4850 0.5751 -0.0356 0.1444 0.0873 22 ARG A CA 159 C C . ARG A 22 ? 0.6784 0.4793 0.5762 -0.0108 0.1406 0.1023 22 ARG A C 160 O O . ARG A 22 ? 0.7088 0.4852 0.5838 -0.0056 0.1510 0.1137 22 ARG A O 161 C CB . ARG A 22 ? 0.7004 0.4831 0.5981 -0.0521 0.1632 0.0839 22 ARG A CB 162 C CG . ARG A 22 ? 0.6806 0.4819 0.5962 -0.0704 0.1605 0.0687 22 ARG A CG 163 C CD . ARG A 22 ? 0.7175 0.4808 0.6213 -0.0847 0.1784 0.0654 22 ARG A CD 164 N NE . ARG A 22 ? 0.7239 0.4694 0.6337 -0.0692 0.1773 0.0685 22 ARG A NE 165 C CZ . ARG A 22 ? 0.6981 0.4645 0.6298 -0.0675 0.1660 0.0603 22 ARG A CZ 166 N NH1 . ARG A 22 ? 0.6673 0.4726 0.6166 -0.0792 0.1539 0.0489 22 ARG A NH1 167 N NH2 . ARG A 22 ? 0.7031 0.4518 0.6390 -0.0528 0.1674 0.0645 22 ARG A NH2 168 N N . GLY A 23 ? 0.6499 0.4668 0.5658 0.0043 0.1256 0.1028 23 GLY A N 169 C CA . GLY A 23 ? 0.6616 0.4682 0.5733 0.0278 0.1215 0.1175 23 GLY A CA 170 C C . GLY A 23 ? 0.6647 0.4827 0.5643 0.0415 0.1118 0.1276 23 GLY A C 171 O O . GLY A 23 ? 0.6961 0.4945 0.5803 0.0569 0.1166 0.1429 23 GLY A O 172 N N . VAL A 24 ? 0.6352 0.4840 0.5400 0.0368 0.0986 0.1196 24 VAL A N 173 C CA . VAL A 24 ? 0.6401 0.5022 0.5331 0.0497 0.0868 0.1274 24 VAL A CA 174 C C . VAL A 24 ? 0.6228 0.5056 0.5307 0.0660 0.0675 0.1311 24 VAL A C 175 O O . VAL A 24 ? 0.5903 0.4928 0.5209 0.0627 0.0573 0.1211 24 VAL A O 176 C CB . VAL A 24 ? 0.6238 0.5078 0.5128 0.0395 0.0818 0.1177 24 VAL A CB 177 C CG1 . VAL A 24 ? 0.5838 0.4955 0.4963 0.0306 0.0713 0.1019 24 VAL A CG1 178 C CG2 . VAL A 24 ? 0.6350 0.5295 0.5085 0.0529 0.0698 0.1252 24 VAL A CG2 179 N N . GLU A 25 ? 0.6459 0.5255 0.5409 0.0831 0.0627 0.1461 25 GLU A N 180 C CA . GLU A 25 ? 0.6356 0.5378 0.5446 0.0979 0.0443 0.1514 25 GLU A CA 181 C C . GLU A 25 ? 0.6188 0.5516 0.5278 0.0966 0.0244 0.1441 25 GLU A C 182 O O . GLU A 25 ? 0.6309 0.5627 0.5183 0.0954 0.0239 0.1453 25 GLU A O 183 C CB . GLU A 25 ? 0.6707 0.5594 0.5671 0.1180 0.0472 0.1721 25 GLU A CB 184 C CG . GLU A 25 ? 0.6893 0.5475 0.5885 0.1227 0.0659 0.1794 25 GLU A CG 185 C CD . GLU A 25 ? 0.7221 0.5698 0.6127 0.1464 0.0684 0.2012 25 GLU A CD 186 O OE1 . GLU A 25 ? 0.7310 0.5982 0.6138 0.1591 0.0542 0.2116 25 GLU A OE1 187 O OE2 . GLU A 25 ? 0.7413 0.5604 0.6316 0.1528 0.0853 0.2083 25 GLU A OE2 188 N N . VAL A 26 ? 0.5933 0.5507 0.5248 0.0961 0.0091 0.1364 26 VAL A N 189 C CA . VAL A 26 ? 0.5842 0.5677 0.5154 0.0940 -0.0101 0.1285 26 VAL A CA 190 C C . VAL A 26 ? 0.5911 0.5966 0.5338 0.1054 -0.0276 0.1361 26 VAL A C 191 O O . VAL A 26 ? 0.5932 0.5971 0.5496 0.1150 -0.0247 0.1461 26 VAL A O 192 C CB . VAL A 26 ? 0.5499 0.5441 0.4960 0.0795 -0.0126 0.1099 26 VAL A CB 193 C CG1 . VAL A 26 ? 0.5530 0.5344 0.4870 0.0684 0.0019 0.1029 26 VAL A CG1 194 C CG2 . VAL A 26 ? 0.5263 0.5226 0.4995 0.0768 -0.0106 0.1056 26 VAL A CG2 195 N N . VAL A 27 ? 0.6012 0.6275 0.5376 0.1038 -0.0453 0.1313 27 VAL A N 196 C CA . VAL A 27 ? 0.6158 0.6672 0.5603 0.1119 -0.0639 0.1384 27 VAL A CA 197 C C . VAL A 27 ? 0.6030 0.6696 0.5796 0.1088 -0.0690 0.1326 27 VAL A C 198 O O . VAL A 27 ? 0.5995 0.6783 0.5920 0.1192 -0.0727 0.1440 27 VAL A O 199 C CB . VAL A 27 ? 0.6220 0.6890 0.5478 0.1072 -0.0812 0.1322 27 VAL A CB 200 C CG1 . VAL A 27 ? 0.6214 0.7189 0.5588 0.1106 -0.1021 0.1366 27 VAL A CG1 201 C CG2 . VAL A 27 ? 0.6533 0.7070 0.5461 0.1129 -0.0768 0.1410 27 VAL A CG2 202 N N . ASN A 28 ? 0.6082 0.6748 0.5941 0.0953 -0.0687 0.1156 28 ASN A N 203 C CA . ASN A 28 ? 0.6104 0.6882 0.6252 0.0911 -0.0715 0.1092 28 ASN A CA 204 C C . ASN A 28 ? 0.5667 0.6295 0.5883 0.0798 -0.0588 0.0958 28 ASN A C 205 O O . ASN A 28 ? 0.5627 0.6145 0.5684 0.0731 -0.0528 0.0885 28 ASN A O 206 C CB . ASN A 28 ? 0.6520 0.7561 0.6732 0.0857 -0.0922 0.1025 28 ASN A CB 207 C CG . ASN A 28 ? 0.7074 0.8278 0.7594 0.0845 -0.0966 0.1012 28 ASN A CG 208 O OD1 . ASN A 28 ? 0.6983 0.8124 0.7668 0.0910 -0.0853 0.1079 28 ASN A OD1 209 N ND2 . ASN A 28 ? 0.8017 0.9413 0.8600 0.0754 -0.1122 0.0922 28 ASN A ND2 210 N N . ALA A 29 ? 0.5269 0.5910 0.5723 0.0783 -0.0545 0.0935 29 ALA A N 211 C CA . ALA A 29 ? 0.4945 0.5477 0.5482 0.0674 -0.0439 0.0813 29 ALA A CA 212 C C . ALA A 29 ? 0.4612 0.5259 0.5407 0.0646 -0.0480 0.0763 29 ALA A C 213 O O . ALA A 29 ? 0.4607 0.5399 0.5540 0.0722 -0.0556 0.0842 29 ALA A O 214 C CB . ALA A 29 ? 0.5060 0.5342 0.5529 0.0677 -0.0241 0.0861 29 ALA A CB 215 N N . THR A 30 ? 0.4290 0.4891 0.5154 0.0540 -0.0427 0.0640 30 THR A N 216 C CA . THR A 30 ? 0.4012 0.4699 0.5099 0.0504 -0.0452 0.0585 30 THR A CA 217 C C . THR A 30 ? 0.3782 0.4329 0.4924 0.0421 -0.0314 0.0509 30 THR A C 218 O O . THR A 30 ? 0.3804 0.4250 0.4821 0.0357 -0.0235 0.0460 30 THR A O 219 C CB . THR A 30 ? 0.3905 0.4765 0.5029 0.0444 -0.0610 0.0493 30 THR A CB 220 O OG1 . THR A 30 ? 0.3830 0.4791 0.5180 0.0426 -0.0640 0.0474 30 THR A OG1 221 C CG2 . THR A 30 ? 0.3847 0.4648 0.4862 0.0354 -0.0591 0.0367 30 THR A CG2 222 N N . GLU A 31 ? 0.3546 0.4110 0.4873 0.0419 -0.0288 0.0503 31 GLU A N 223 C CA . GLU A 31 ? 0.3395 0.3820 0.4766 0.0344 -0.0155 0.0443 31 GLU A CA 224 C C . GLU A 31 ? 0.3139 0.3639 0.4540 0.0233 -0.0198 0.0309 31 GLU A C 225 O O . GLU A 31 ? 0.3041 0.3687 0.4510 0.0226 -0.0320 0.0265 31 GLU A O 226 C CB . GLU A 31 ? 0.3370 0.3770 0.4908 0.0399 -0.0101 0.0495 31 GLU A CB 227 C CG . GLU A 31 ? 0.3341 0.3572 0.4900 0.0319 0.0042 0.0433 31 GLU A CG 228 C CD . GLU A 31 ? 0.3529 0.3521 0.4904 0.0271 0.0191 0.0439 31 GLU A CD 229 O OE1 . GLU A 31 ? 0.3761 0.3578 0.5063 0.0356 0.0292 0.0542 31 GLU A OE1 230 O OE2 . GLU A 31 ? 0.3433 0.3416 0.4734 0.0146 0.0212 0.0345 31 GLU A OE2 231 N N . THR A 32 ? 0.3050 0.3451 0.4388 0.0144 -0.0094 0.0249 32 THR A N 232 C CA . THR A 32 ? 0.2836 0.3318 0.4205 0.0054 -0.0119 0.0138 32 THR A CA 233 C C . THR A 32 ? 0.2742 0.3167 0.4209 -0.0016 -0.0038 0.0091 32 THR A C 234 O O . THR A 32 ? 0.2613 0.3121 0.4129 -0.0074 -0.0071 0.0013 32 THR A O 235 C CB . THR A 32 ? 0.2863 0.3358 0.4093 -0.0003 -0.0083 0.0098 32 THR A CB 236 O OG1 . THR A 32 ? 0.2976 0.3335 0.4137 -0.0067 0.0058 0.0117 32 THR A OG1 237 C CG2 . THR A 32 ? 0.2961 0.3497 0.4065 0.0064 -0.0155 0.0136 32 THR A CG2 238 N N . VAL A 33 ? 0.2850 0.3116 0.4325 -0.0005 0.0074 0.0142 33 VAL A N 239 C CA . VAL A 33 ? 0.2814 0.2989 0.4350 -0.0070 0.0163 0.0100 33 VAL A CA 240 C C . VAL A 33 ? 0.2806 0.2988 0.4495 0.0014 0.0150 0.0145 33 VAL A C 241 O O . VAL A 33 ? 0.2919 0.3036 0.4622 0.0118 0.0183 0.0243 33 VAL A O 242 C CB . VAL A 33 ? 0.3018 0.2961 0.4423 -0.0133 0.0329 0.0113 33 VAL A CB 243 C CG1 . VAL A 33 ? 0.3025 0.2852 0.4458 -0.0215 0.0424 0.0057 33 VAL A CG1 244 C CG2 . VAL A 33 ? 0.3057 0.3030 0.4328 -0.0230 0.0347 0.0075 33 VAL A CG2 245 N N . GLU A 34 ? 0.2672 0.2943 0.4474 -0.0027 0.0109 0.0082 34 GLU A N 246 C CA . GLU A 34 ? 0.2667 0.2976 0.4631 0.0037 0.0101 0.0118 34 GLU A CA 247 C C . GLU A 34 ? 0.2829 0.2931 0.4784 0.0040 0.0265 0.0140 34 GLU A C 248 O O . GLU A 34 ? 0.2854 0.2826 0.4717 -0.0067 0.0355 0.0068 34 GLU A O 249 C CB . GLU A 34 ? 0.2490 0.2939 0.4553 -0.0019 0.0014 0.0040 34 GLU A CB 250 C CG . GLU A 34 ? 0.2447 0.2973 0.4692 0.0031 -0.0002 0.0075 34 GLU A CG 251 C CD . GLU A 34 ? 0.2509 0.3177 0.4845 0.0134 -0.0089 0.0169 34 GLU A CD 252 O OE1 . GLU A 34 ? 0.2472 0.3278 0.4795 0.0122 -0.0224 0.0153 34 GLU A OE1 253 O OE2 . GLU A 34 ? 0.2649 0.3287 0.5055 0.0229 -0.0018 0.0263 34 GLU A OE2 254 N N . ARG A 35 ? 0.2969 0.3042 0.5007 0.0165 0.0308 0.0242 35 ARG A N 255 C CA . ARG A 35 ? 0.3184 0.3040 0.5215 0.0201 0.0478 0.0274 35 ARG A CA 256 C C . ARG A 35 ? 0.3121 0.3099 0.5364 0.0288 0.0475 0.0319 35 ARG A C 257 O O . ARG A 35 ? 0.3254 0.3060 0.5500 0.0326 0.0623 0.0341 35 ARG A O 258 C CB . ARG A 35 ? 0.3499 0.3154 0.5412 0.0302 0.0589 0.0379 35 ARG A CB 259 C CG . ARG A 35 ? 0.3672 0.3157 0.5360 0.0206 0.0638 0.0343 35 ARG A CG 260 C CD . ARG A 35 ? 0.4044 0.3263 0.5590 0.0305 0.0780 0.0451 35 ARG A CD 261 N NE . ARG A 35 ? 0.4100 0.3472 0.5721 0.0476 0.0693 0.0583 35 ARG A NE 262 C CZ . ARG A 35 ? 0.4077 0.3614 0.5665 0.0480 0.0561 0.0601 35 ARG A CZ 263 N NH1 . ARG A 35 ? 0.3970 0.3546 0.5464 0.0336 0.0508 0.0500 35 ARG A NH1 264 N NH2 . ARG A 35 ? 0.4169 0.3846 0.5815 0.0634 0.0483 0.0726 35 ARG A NH2 265 N N . THR A 36 ? 0.2966 0.3231 0.5375 0.0315 0.0316 0.0334 36 THR A N 266 C CA . THR A 36 ? 0.2946 0.3376 0.5577 0.0386 0.0304 0.0386 36 THR A CA 267 C C . THR A 36 ? 0.2828 0.3267 0.5510 0.0276 0.0312 0.0283 36 THR A C 268 O O . THR A 36 ? 0.2712 0.3246 0.5374 0.0175 0.0199 0.0198 36 THR A O 269 C CB . THR A 36 ? 0.2840 0.3589 0.5621 0.0437 0.0126 0.0447 36 THR A CB 270 O OG1 . THR A 36 ? 0.2994 0.3737 0.5690 0.0530 0.0103 0.0537 36 THR A OG1 271 C CG2 . THR A 36 ? 0.2816 0.3771 0.5849 0.0519 0.0128 0.0525 36 THR A CG2 272 N N . ASN A 37 ? 0.2952 0.3265 0.5676 0.0305 0.0458 0.0294 37 ASN A N 273 C CA . ASN A 37 ? 0.2889 0.3209 0.5668 0.0220 0.0482 0.0215 37 ASN A CA 274 C C . ASN A 37 ? 0.2804 0.3377 0.5841 0.0285 0.0434 0.0278 37 ASN A C 275 O O . ASN A 37 ? 0.2882 0.3577 0.6056 0.0418 0.0446 0.0395 37 ASN A O 276 C CB . ASN A 37 ? 0.3112 0.3131 0.5760 0.0201 0.0681 0.0184 37 ASN A CB 277 C CG . ASN A 37 ? 0.3057 0.3066 0.5728 0.0109 0.0712 0.0101 37 ASN A CG 278 O OD1 . ASN A 37 ? 0.2920 0.3018 0.5563 -0.0002 0.0607 0.0018 37 ASN A OD1 279 N ND2 . ASN A 37 ? 0.3205 0.3096 0.5914 0.0165 0.0865 0.0128 37 ASN A ND2 280 N N . ILE A 38 ? 0.2677 0.3347 0.5782 0.0190 0.0380 0.0207 38 ILE A N 281 C CA . ILE A 38 ? 0.2638 0.3512 0.5978 0.0224 0.0376 0.0256 38 ILE A CA 282 C C . ILE A 38 ? 0.2677 0.3375 0.5986 0.0193 0.0533 0.0210 38 ILE A C 283 O O . ILE A 38 ? 0.2586 0.3172 0.5765 0.0074 0.0527 0.0107 38 ILE A O 284 C CB . ILE A 38 ? 0.2511 0.3617 0.5942 0.0131 0.0199 0.0215 38 ILE A CB 285 C CG1 . ILE A 38 ? 0.2540 0.3825 0.5998 0.0170 0.0053 0.0270 38 ILE A CG1 286 C CG2 . ILE A 38 ? 0.2442 0.3740 0.6101 0.0125 0.0213 0.0247 38 ILE A CG2 287 C CD1 . ILE A 38 ? 0.2467 0.3950 0.5980 0.0071 -0.0117 0.0229 38 ILE A CD1 288 N N . PRO A 39 ? 0.2804 0.3479 0.6223 0.0310 0.0680 0.0293 39 PRO A N 289 C CA . PRO A 39 ? 0.2972 0.3420 0.6313 0.0294 0.0861 0.0252 39 PRO A CA 290 C C . PRO A 39 ? 0.2922 0.3512 0.6401 0.0227 0.0850 0.0219 39 PRO A C 291 O O . PRO A 39 ? 0.3059 0.3625 0.6627 0.0288 0.0994 0.0258 39 PRO A O 292 C CB . PRO A 39 ? 0.3162 0.3537 0.6569 0.0474 0.1026 0.0370 39 PRO A CB 293 C CG . PRO A 39 ? 0.3055 0.3791 0.6716 0.0581 0.0903 0.0491 39 PRO A CG 294 C CD . PRO A 39 ? 0.2867 0.3736 0.6481 0.0475 0.0688 0.0438 39 PRO A CD 295 N N . ARG A 40 ? 0.2813 0.3530 0.6293 0.0106 0.0691 0.0152 40 ARG A N 296 C CA . ARG A 40 ? 0.2790 0.3603 0.6354 0.0018 0.0670 0.0112 40 ARG A CA 297 C C . ARG A 40 ? 0.2629 0.3349 0.6003 -0.0117 0.0568 0.0002 40 ARG A C 298 O O . ARG A 40 ? 0.2534 0.3207 0.5777 -0.0135 0.0485 -0.0028 40 ARG A O 299 C CB . ARG A 40 ? 0.2772 0.3934 0.6613 0.0034 0.0561 0.0185 40 ARG A CB 300 C CG . ARG A 40 ? 0.2975 0.4298 0.7060 0.0137 0.0681 0.0287 40 ARG A CG 301 C CD . ARG A 40 ? 0.3155 0.4704 0.7422 0.0282 0.0652 0.0416 40 ARG A CD 302 N NE . ARG A 40 ? 0.3172 0.4990 0.7529 0.0227 0.0441 0.0430 40 ARG A NE 303 C CZ . ARG A 40 ? 0.3302 0.5249 0.7693 0.0315 0.0357 0.0506 40 ARG A CZ 304 N NH1 . ARG A 40 ? 0.3439 0.5261 0.7784 0.0473 0.0471 0.0584 40 ARG A NH1 305 N NH2 . ARG A 40 ? 0.3254 0.5430 0.7696 0.0242 0.0164 0.0504 40 ARG A NH2 306 N N . ILE A 41 ? 0.2572 0.3268 0.5928 -0.0202 0.0584 -0.0050 41 ILE A N 307 C CA . ILE A 41 ? 0.2503 0.3152 0.5707 -0.0308 0.0478 -0.0133 41 ILE A CA 308 C C . ILE A 41 ? 0.2355 0.3213 0.5705 -0.0343 0.0340 -0.0114 41 ILE A C 309 O O . ILE A 41 ? 0.2341 0.3300 0.5831 -0.0374 0.0360 -0.0093 41 ILE A O 310 C CB . ILE A 41 ? 0.2608 0.3103 0.5681 -0.0381 0.0564 -0.0194 41 ILE A CB 311 C CG1 . ILE A 41 ? 0.2778 0.3054 0.5684 -0.0370 0.0707 -0.0221 41 ILE A CG1 312 C CG2 . ILE A 41 ? 0.2552 0.3018 0.5474 -0.0463 0.0452 -0.0260 41 ILE A CG2 313 C CD1 . ILE A 41 ? 0.2853 0.3035 0.5581 -0.0387 0.0666 -0.0260 41 ILE A CD1 314 N N . CYS A 42 ? 0.2275 0.3189 0.5578 -0.0346 0.0208 -0.0123 42 CYS A N 315 C CA . CYS A 42 ? 0.2214 0.3302 0.5616 -0.0389 0.0072 -0.0112 42 CYS A CA 316 C C . CYS A 42 ? 0.2184 0.3171 0.5451 -0.0487 0.0022 -0.0186 42 CYS A C 317 O O . CYS A 42 ? 0.2169 0.3039 0.5245 -0.0498 -0.0030 -0.0238 42 CYS A O 318 C CB . CYS A 42 ? 0.2215 0.3367 0.5577 -0.0351 -0.0039 -0.0097 42 CYS A CB 319 S SG . CYS A 42 ? 0.2310 0.3629 0.5855 -0.0225 -0.0008 0.0017 42 CYS A SG 320 N N . SER A 43 ? 0.2162 0.3195 0.5526 -0.0551 0.0046 -0.0182 43 SER A N 321 C CA . SER A 43 ? 0.2194 0.3082 0.5410 -0.0633 0.0035 -0.0241 43 SER A CA 322 C C . SER A 43 ? 0.2207 0.3170 0.5481 -0.0729 -0.0050 -0.0247 43 SER A C 323 O O . SER A 43 ? 0.2277 0.3126 0.5476 -0.0802 -0.0023 -0.0276 43 SER A O 324 C CB . SER A 43 ? 0.2240 0.3028 0.5441 -0.0641 0.0173 -0.0244 43 SER A CB 325 O OG . SER A 43 ? 0.2265 0.3204 0.5695 -0.0643 0.0243 -0.0187 43 SER A OG 326 N N . LYS A 44 ? 0.2160 0.3303 0.5549 -0.0740 -0.0150 -0.0220 44 LYS A N 327 C CA . LYS A 44 ? 0.2216 0.3420 0.5625 -0.0858 -0.0243 -0.0238 44 LYS A CA 328 C C . LYS A 44 ? 0.2296 0.3231 0.5432 -0.0911 -0.0274 -0.0314 44 LYS A C 329 O O . LYS A 44 ? 0.2256 0.3067 0.5212 -0.0847 -0.0307 -0.0346 44 LYS A O 330 C CB . LYS A 44 ? 0.2231 0.3634 0.5720 -0.0859 -0.0368 -0.0212 44 LYS A CB 331 C CG . LYS A 44 ? 0.2406 0.3830 0.5852 -0.1008 -0.0473 -0.0251 44 LYS A CG 332 C CD . LYS A 44 ? 0.2474 0.4174 0.6051 -0.1034 -0.0595 -0.0211 44 LYS A CD 333 C CE . LYS A 44 ? 0.2520 0.4145 0.5926 -0.0951 -0.0672 -0.0229 44 LYS A CE 334 N NZ . LYS A 44 ? 0.2576 0.4496 0.6115 -0.0961 -0.0788 -0.0175 44 LYS A NZ 335 N N . GLY A 45 ? 0.2412 0.3260 0.5515 -0.1021 -0.0255 -0.0337 45 GLY A N 336 C CA . GLY A 45 ? 0.2583 0.3151 0.5414 -0.1066 -0.0275 -0.0399 45 GLY A CA 337 C C . GLY A 45 ? 0.2615 0.2960 0.5264 -0.0995 -0.0188 -0.0414 45 GLY A C 338 O O . GLY A 45 ? 0.2781 0.2893 0.5196 -0.0999 -0.0195 -0.0451 45 GLY A O 339 N N . LYS A 46 ? 0.2486 0.2895 0.5224 -0.0929 -0.0102 -0.0383 46 LYS A N 340 C CA . LYS A 46 ? 0.2522 0.2762 0.5083 -0.0868 -0.0032 -0.0396 46 LYS A CA 341 C C . LYS A 46 ? 0.2541 0.2743 0.5147 -0.0907 0.0081 -0.0376 46 LYS A C 342 O O . LYS A 46 ? 0.2488 0.2843 0.5302 -0.0923 0.0137 -0.0342 46 LYS A O 343 C CB . LYS A 46 ? 0.2415 0.2722 0.4974 -0.0769 -0.0023 -0.0391 46 LYS A CB 344 C CG . LYS A 46 ? 0.2399 0.2711 0.4862 -0.0717 -0.0118 -0.0411 46 LYS A CG 345 C CD . LYS A 46 ? 0.2323 0.2715 0.4806 -0.0643 -0.0098 -0.0401 46 LYS A CD 346 C CE . LYS A 46 ? 0.2321 0.2723 0.4707 -0.0595 -0.0184 -0.0418 46 LYS A CE 347 N NZ . LYS A 46 ? 0.2246 0.2715 0.4645 -0.0541 -0.0158 -0.0407 46 LYS A NZ 348 N N . ARG A 47 ? 0.2669 0.2670 0.5073 -0.0908 0.0123 -0.0389 47 ARG A N 349 C CA . ARG A 47 ? 0.2750 0.2695 0.5153 -0.0932 0.0238 -0.0369 47 ARG A CA 350 C C . ARG A 47 ? 0.2545 0.2559 0.4970 -0.0863 0.0297 -0.0363 47 ARG A C 351 O O . ARG A 47 ? 0.2502 0.2457 0.4760 -0.0803 0.0281 -0.0380 47 ARG A O 352 C CB . ARG A 47 ? 0.3053 0.2758 0.5203 -0.0935 0.0264 -0.0374 47 ARG A CB 353 C CG . ARG A 47 ? 0.3376 0.2944 0.5469 -0.1023 0.0240 -0.0383 47 ARG A CG 354 C CD . ARG A 47 ? 0.3731 0.3034 0.5578 -0.1022 0.0302 -0.0371 47 ARG A CD 355 N NE . ARG A 47 ? 0.3991 0.3119 0.5595 -0.0940 0.0246 -0.0384 47 ARG A NE 356 C CZ . ARG A 47 ? 0.4151 0.3244 0.5591 -0.0817 0.0243 -0.0369 47 ARG A CZ 357 N NH1 . ARG A 47 ? 0.4096 0.3298 0.5560 -0.0779 0.0287 -0.0351 47 ARG A NH1 358 N NH2 . ARG A 47 ? 0.4356 0.3308 0.5597 -0.0734 0.0199 -0.0371 47 ARG A NH2 359 N N . THR A 48 ? 0.2393 0.2536 0.5019 -0.0874 0.0371 -0.0337 48 THR A N 360 C CA . THR A 48 ? 0.2289 0.2465 0.4931 -0.0816 0.0444 -0.0335 48 THR A CA 361 C C . THR A 48 ? 0.2352 0.2455 0.4970 -0.0836 0.0586 -0.0325 48 THR A C 362 O O . THR A 48 ? 0.2414 0.2556 0.5161 -0.0884 0.0650 -0.0296 48 THR A O 363 C CB . THR A 48 ? 0.2175 0.2535 0.5046 -0.0776 0.0436 -0.0306 48 THR A CB 364 O OG1 . THR A 48 ? 0.2107 0.2535 0.4990 -0.0764 0.0303 -0.0314 48 THR A OG1 365 C CG2 . THR A 48 ? 0.2153 0.2482 0.4988 -0.0713 0.0518 -0.0310 48 THR A CG2 366 N N . VAL A 49 ? 0.2356 0.2361 0.4801 -0.0810 0.0636 -0.0350 49 VAL A N 367 C CA . VAL A 49 ? 0.2455 0.2369 0.4830 -0.0827 0.0774 -0.0350 49 VAL A CA 368 C C . VAL A 49 ? 0.2437 0.2346 0.4810 -0.0789 0.0846 -0.0366 49 VAL A C 369 O O . VAL A 49 ? 0.2450 0.2319 0.4670 -0.0780 0.0804 -0.0402 49 VAL A O 370 C CB . VAL A 49 ? 0.2579 0.2346 0.4681 -0.0850 0.0771 -0.0371 49 VAL A CB 371 C CG1 . VAL A 49 ? 0.2729 0.2392 0.4707 -0.0872 0.0909 -0.0382 49 VAL A CG1 372 C CG2 . VAL A 49 ? 0.2639 0.2351 0.4719 -0.0884 0.0733 -0.0347 49 VAL A CG2 373 N N . ASP A 50 ? 0.2464 0.2414 0.5004 -0.0766 0.0963 -0.0336 50 ASP A N 374 C CA . ASP A 50 ? 0.2524 0.2412 0.5043 -0.0721 0.1072 -0.0345 50 ASP A CA 375 C C . ASP A 50 ? 0.2722 0.2434 0.5056 -0.0757 0.1218 -0.0371 50 ASP A C 376 O O . ASP A 50 ? 0.2778 0.2494 0.5199 -0.0761 0.1323 -0.0340 50 ASP A O 377 C CB . ASP A 50 ? 0.2468 0.2505 0.5276 -0.0650 0.1126 -0.0281 50 ASP A CB 378 C CG . ASP A 50 ? 0.2580 0.2510 0.5353 -0.0581 0.1262 -0.0280 50 ASP A CG 379 O OD1 . ASP A 50 ? 0.2705 0.2436 0.5221 -0.0616 0.1312 -0.0341 50 ASP A OD1 380 O OD2 . ASP A 50 ? 0.2556 0.2598 0.5548 -0.0495 0.1322 -0.0216 50 ASP A OD2 381 N N . LEU A 51 ? 0.2834 0.2405 0.4906 -0.0791 0.1225 -0.0430 51 LEU A N 382 C CA . LEU A 51 ? 0.3064 0.2463 0.4899 -0.0845 0.1340 -0.0466 51 LEU A CA 383 C C . LEU A 51 ? 0.3258 0.2531 0.5104 -0.0816 0.1541 -0.0464 51 LEU A C 384 O O . LEU A 51 ? 0.3436 0.2584 0.5143 -0.0850 0.1659 -0.0476 51 LEU A O 385 C CB . LEU A 51 ? 0.3133 0.2454 0.4684 -0.0907 0.1277 -0.0529 51 LEU A CB 386 C CG . LEU A 51 ? 0.3021 0.2447 0.4507 -0.0924 0.1108 -0.0524 51 LEU A CG 387 C CD1 . LEU A 51 ? 0.3065 0.2492 0.4331 -0.0975 0.1038 -0.0575 51 LEU A CD1 388 C CD2 . LEU A 51 ? 0.3114 0.2495 0.4509 -0.0946 0.1127 -0.0501 51 LEU A CD2 389 N N . GLY A 52 ? 0.3256 0.2550 0.5252 -0.0742 0.1591 -0.0441 52 GLY A N 390 C CA . GLY A 52 ? 0.3468 0.2641 0.5494 -0.0681 0.1799 -0.0423 52 GLY A CA 391 C C . GLY A 52 ? 0.3791 0.2680 0.5464 -0.0751 0.1925 -0.0502 52 GLY A C 392 O O . GLY A 52 ? 0.3866 0.2642 0.5318 -0.0814 0.1879 -0.0567 52 GLY A O 393 N N . GLN A 53 ? 0.4007 0.2789 0.5616 -0.0755 0.2081 -0.0498 53 GLN A N 394 C CA . GLN A 53 ? 0.4348 0.2843 0.5591 -0.0831 0.2213 -0.0577 53 GLN A CA 395 C C . GLN A 53 ? 0.4324 0.2805 0.5302 -0.0958 0.2094 -0.0632 53 GLN A C 396 O O . GLN A 53 ? 0.4542 0.2817 0.5186 -0.1048 0.2162 -0.0706 53 GLN A O 397 C CB . GLN A 53 ? 0.4638 0.3017 0.5893 -0.0779 0.2438 -0.0550 53 GLN A CB 398 C CG . GLN A 53 ? 0.4782 0.3126 0.6226 -0.0640 0.2598 -0.0498 53 GLN A CG 399 C CD . GLN A 53 ? 0.5057 0.3330 0.6550 -0.0571 0.2826 -0.0457 53 GLN A CD 400 O OE1 . GLN A 53 ? 0.4949 0.3472 0.6772 -0.0497 0.2837 -0.0366 53 GLN A OE1 401 N NE2 . GLN A 53 ? 0.5470 0.3406 0.6624 -0.0604 0.3013 -0.0526 53 GLN A NE2 402 N N . CYS A 54 ? 0.4050 0.2743 0.5161 -0.0964 0.1924 -0.0592 54 CYS A N 403 C CA . CYS A 54 ? 0.4057 0.2765 0.4935 -0.1053 0.1798 -0.0624 54 CYS A CA 404 C C . CYS A 54 ? 0.3982 0.2734 0.4738 -0.1103 0.1661 -0.0674 54 CYS A C 405 O O . CYS A 54 ? 0.3773 0.2659 0.4722 -0.1056 0.1560 -0.0653 54 CYS A O 406 C CB . CYS A 54 ? 0.3862 0.2742 0.4902 -0.1028 0.1681 -0.0560 54 CYS A CB 407 S SG . CYS A 54 ? 0.3894 0.2804 0.4663 -0.1094 0.1529 -0.0572 54 CYS A SG 408 N N . GLY A 55 ? 0.4165 0.2818 0.4597 -0.1208 0.1659 -0.0739 55 GLY A N 409 C CA . GLY A 55 ? 0.4090 0.2838 0.4402 -0.1276 0.1517 -0.0781 55 GLY A CA 410 C C . GLY A 55 ? 0.3874 0.2843 0.4240 -0.1251 0.1335 -0.0732 55 GLY A C 411 O O . GLY A 55 ? 0.3921 0.2894 0.4251 -0.1233 0.1336 -0.0692 55 GLY A O 412 N N . LEU A 56 ? 0.3653 0.2790 0.4094 -0.1243 0.1191 -0.0729 56 LEU A N 413 C CA . LEU A 56 ? 0.3455 0.2791 0.3953 -0.1195 0.1028 -0.0677 56 LEU A CA 414 C C . LEU A 56 ? 0.3590 0.2966 0.3829 -0.1244 0.0980 -0.0673 56 LEU A C 415 O O . LEU A 56 ? 0.3536 0.2967 0.3790 -0.1180 0.0922 -0.0611 56 LEU A O 416 C CB . LEU A 56 ? 0.3274 0.2776 0.3865 -0.1182 0.0902 -0.0682 56 LEU A CB 417 C CG . LEU A 56 ? 0.3113 0.2816 0.3746 -0.1119 0.0741 -0.0631 56 LEU A CG 418 C CD1 . LEU A 56 ? 0.3004 0.2688 0.3812 -0.1020 0.0727 -0.0569 56 LEU A CD1 419 C CD2 . LEU A 56 ? 0.2965 0.2816 0.3685 -0.1115 0.0649 -0.0645 56 LEU A CD2 420 N N . LEU A 57 ? 0.3778 0.3123 0.3766 -0.1360 0.1003 -0.0735 57 LEU A N 421 C CA . LEU A 57 ? 0.3953 0.3356 0.3674 -0.1415 0.0959 -0.0728 57 LEU A CA 422 C C . LEU A 57 ? 0.4129 0.3341 0.3739 -0.1408 0.1083 -0.0711 57 LEU A C 423 O O . LEU A 57 ? 0.4239 0.3495 0.3681 -0.1402 0.1041 -0.0669 57 LEU A O 424 C CB . LEU A 57 ? 0.4142 0.3584 0.3613 -0.1569 0.0943 -0.0806 57 LEU A CB 425 C CG . LEU A 57 ? 0.4010 0.3657 0.3556 -0.1607 0.0830 -0.0827 57 LEU A CG 426 C CD1 . LEU A 57 ? 0.4253 0.3939 0.3514 -0.1794 0.0820 -0.0906 57 LEU A CD1 427 C CD2 . LEU A 57 ? 0.3785 0.3715 0.3470 -0.1494 0.0664 -0.0742 57 LEU A CD2 428 N N . GLY A 58 ? 0.4164 0.3173 0.3867 -0.1399 0.1240 -0.0733 58 GLY A N 429 C CA . GLY A 58 ? 0.4328 0.3169 0.3978 -0.1380 0.1374 -0.0708 58 GLY A CA 430 C C . GLY A 58 ? 0.4183 0.3085 0.4001 -0.1278 0.1331 -0.0617 58 GLY A C 431 O O . GLY A 58 ? 0.4340 0.3134 0.4060 -0.1275 0.1412 -0.0585 58 GLY A O 432 N N . THR A 59 ? 0.3926 0.2979 0.3973 -0.1204 0.1209 -0.0577 59 THR A N 433 C CA . THR A 59 ? 0.3840 0.2922 0.4000 -0.1126 0.1160 -0.0498 59 THR A CA 434 C C . THR A 59 ? 0.4017 0.3125 0.3927 -0.1115 0.1088 -0.0452 59 THR A C 435 O O . THR A 59 ? 0.4078 0.3117 0.3982 -0.1067 0.1101 -0.0387 59 THR A O 436 C CB . THR A 59 ? 0.3556 0.2771 0.3973 -0.1054 0.1044 -0.0473 59 THR A CB 437 O OG1 . THR A 59 ? 0.3481 0.2852 0.3812 -0.1040 0.0900 -0.0475 59 THR A OG1 438 C CG2 . THR A 59 ? 0.3405 0.2627 0.4065 -0.1052 0.1097 -0.0505 59 THR A CG2 439 N N . ILE A 60 ? 0.4133 0.3345 0.3832 -0.1162 0.1014 -0.0480 60 ILE A N 440 C CA . ILE A 60 ? 0.4324 0.3604 0.3777 -0.1142 0.0940 -0.0425 60 ILE A CA 441 C C . ILE A 60 ? 0.4650 0.3778 0.3826 -0.1210 0.1049 -0.0431 60 ILE A C 442 O O . ILE A 60 ? 0.4829 0.3941 0.3832 -0.1166 0.1029 -0.0360 60 ILE A O 443 C CB . ILE A 60 ? 0.4294 0.3822 0.3653 -0.1164 0.0795 -0.0438 60 ILE A CB 444 C CG1 . ILE A 60 ? 0.4020 0.3694 0.3635 -0.1095 0.0696 -0.0430 60 ILE A CG1 445 C CG2 . ILE A 60 ? 0.4465 0.4110 0.3598 -0.1114 0.0710 -0.0357 60 ILE A CG2 446 C CD1 . ILE A 60 ? 0.3922 0.3564 0.3671 -0.0960 0.0659 -0.0349 60 ILE A CD1 447 N N . THR A 61 ? 0.4767 0.3766 0.3883 -0.1309 0.1172 -0.0514 61 THR A N 448 C CA . THR A 61 ? 0.5101 0.3944 0.3916 -0.1387 0.1284 -0.0536 61 THR A CA 449 C C . THR A 61 ? 0.5194 0.3807 0.4094 -0.1371 0.1470 -0.0529 61 THR A C 450 O O . THR A 61 ? 0.5439 0.3923 0.4138 -0.1383 0.1555 -0.0498 61 THR A O 451 C CB . THR A 61 ? 0.5265 0.4093 0.3872 -0.1527 0.1307 -0.0642 61 THR A CB 452 O OG1 . THR A 61 ? 0.5140 0.3890 0.3950 -0.1544 0.1382 -0.0708 61 THR A OG1 453 C CG2 . THR A 61 ? 0.5232 0.4332 0.3721 -0.1566 0.1121 -0.0640 61 THR A CG2 454 N N . GLY A 62 ? 0.5010 0.3591 0.4207 -0.1342 0.1537 -0.0550 62 GLY A N 455 C CA . GLY A 62 ? 0.5026 0.3467 0.4388 -0.1309 0.1699 -0.0524 62 GLY A CA 456 C C . GLY A 62 ? 0.5272 0.3513 0.4505 -0.1365 0.1901 -0.0582 62 GLY A C 457 O O . GLY A 62 ? 0.5502 0.3607 0.4605 -0.1375 0.2025 -0.0556 62 GLY A O 458 N N . PRO A 63 ? 0.5271 0.3468 0.4523 -0.1399 0.1950 -0.0659 63 PRO A N 459 C CA . PRO A 63 ? 0.5487 0.3468 0.4681 -0.1416 0.2173 -0.0704 63 PRO A CA 460 C C . PRO A 63 ? 0.5325 0.3336 0.4890 -0.1318 0.2279 -0.0640 63 PRO A C 461 O O . PRO A 63 ? 0.5023 0.3217 0.4885 -0.1259 0.2164 -0.0586 63 PRO A O 462 C CB . PRO A 63 ? 0.5527 0.3452 0.4654 -0.1467 0.2177 -0.0793 63 PRO A CB 463 C CG . PRO A 63 ? 0.5189 0.3351 0.4533 -0.1435 0.1974 -0.0771 63 PRO A CG 464 C CD . PRO A 63 ? 0.5095 0.3417 0.4405 -0.1418 0.1819 -0.0705 63 PRO A CD 465 N N . PRO A 64 ? 0.5539 0.3385 0.5088 -0.1304 0.2501 -0.0646 64 PRO A N 466 C CA . PRO A 64 ? 0.5401 0.3331 0.5311 -0.1218 0.2603 -0.0569 64 PRO A CA 467 C C . PRO A 64 ? 0.5059 0.3190 0.5371 -0.1141 0.2521 -0.0538 64 PRO A C 468 O O . PRO A 64 ? 0.4821 0.3128 0.5437 -0.1101 0.2478 -0.0466 64 PRO A O 469 C CB . PRO A 64 ? 0.5714 0.3434 0.5516 -0.1205 0.2866 -0.0594 64 PRO A CB 470 C CG . PRO A 64 ? 0.6065 0.3554 0.5382 -0.1305 0.2898 -0.0678 64 PRO A CG 471 C CD . PRO A 64 ? 0.5930 0.3512 0.5134 -0.1366 0.2675 -0.0723 64 PRO A CD 472 N N . GLN A 65 ? 0.5033 0.3131 0.5326 -0.1133 0.2500 -0.0594 65 GLN A N 473 C CA . GLN A 65 ? 0.4743 0.3020 0.5375 -0.1059 0.2414 -0.0565 65 GLN A CA 474 C C . GLN A 65 ? 0.4449 0.2947 0.5231 -0.1064 0.2179 -0.0529 65 GLN A C 475 O O . GLN A 65 ? 0.4207 0.2881 0.5300 -0.1005 0.2106 -0.0487 65 GLN A O 476 C CB . GLN A 65 ? 0.4817 0.2973 0.5336 -0.1061 0.2439 -0.0633 65 GLN A CB 477 C CG . GLN A 65 ? 0.4859 0.2976 0.5083 -0.1165 0.2291 -0.0707 65 GLN A CG 478 C CD . GLN A 65 ? 0.5252 0.3110 0.5046 -0.1271 0.2403 -0.0792 65 GLN A CD 479 O OE1 . GLN A 65 ? 0.5497 0.3201 0.5165 -0.1273 0.2568 -0.0791 65 GLN A OE1 480 N NE2 . GLN A 65 ? 0.5333 0.3151 0.4890 -0.1370 0.2311 -0.0867 65 GLN A NE2 481 N N . CYS A 66 ? 0.4511 0.2993 0.5055 -0.1128 0.2067 -0.0541 66 CYS A N 482 C CA . CYS A 66 ? 0.4315 0.2961 0.4945 -0.1120 0.1865 -0.0506 66 CYS A CA 483 C C . CYS A 66 ? 0.4354 0.3016 0.5021 -0.1120 0.1858 -0.0438 66 CYS A C 484 O O . CYS A 66 ? 0.4226 0.2957 0.4877 -0.1115 0.1712 -0.0410 66 CYS A O 485 C CB . CYS A 66 ? 0.4368 0.3012 0.4715 -0.1172 0.1734 -0.0553 66 CYS A CB 486 S SG . CYS A 66 ? 0.4310 0.2974 0.4651 -0.1191 0.1692 -0.0626 66 CYS A SG 487 N N . ASP A 67 ? 0.4542 0.3129 0.5254 -0.1125 0.2026 -0.0409 67 ASP A N 488 C CA . ASP A 67 ? 0.4662 0.3227 0.5368 -0.1145 0.2044 -0.0347 67 ASP A CA 489 C C . ASP A 67 ? 0.4442 0.3158 0.5423 -0.1130 0.1925 -0.0298 67 ASP A C 490 O O . ASP A 67 ? 0.4514 0.3185 0.5404 -0.1149 0.1861 -0.0260 67 ASP A O 491 C CB . ASP A 67 ? 0.4867 0.3346 0.5601 -0.1158 0.2264 -0.0323 67 ASP A CB 492 C CG . ASP A 67 ? 0.5220 0.3486 0.5563 -0.1198 0.2370 -0.0355 67 ASP A CG 493 O OD1 . ASP A 67 ? 0.5316 0.3526 0.5375 -0.1226 0.2256 -0.0367 67 ASP A OD1 494 O OD2 . ASP A 67 ? 0.5419 0.3583 0.5730 -0.1198 0.2569 -0.0363 67 ASP A OD2 495 N N . GLN A 68 ? 0.4245 0.3121 0.5532 -0.1096 0.1894 -0.0298 68 GLN A N 496 C CA . GLN A 68 ? 0.4075 0.3099 0.5613 -0.1097 0.1778 -0.0261 68 GLN A CA 497 C C . GLN A 68 ? 0.3895 0.2965 0.5380 -0.1072 0.1581 -0.0285 68 GLN A C 498 O O . GLN A 68 ? 0.3700 0.2880 0.5373 -0.1070 0.1479 -0.0266 68 GLN A O 499 C CB . GLN A 68 ? 0.3961 0.3175 0.5870 -0.1072 0.1839 -0.0235 68 GLN A CB 500 C CG . GLN A 68 ? 0.4151 0.3364 0.6157 -0.1080 0.2045 -0.0200 68 GLN A CG 501 C CD . GLN A 68 ? 0.4334 0.3492 0.6304 -0.1158 0.2096 -0.0157 68 GLN A CD 502 O OE1 . GLN A 68 ? 0.4606 0.3617 0.6398 -0.1179 0.2241 -0.0150 68 GLN A OE1 503 N NE2 . GLN A 68 ? 0.4274 0.3525 0.6387 -0.1210 0.1983 -0.0129 68 GLN A NE2 504 N N . PHE A 69 ? 0.3963 0.2958 0.5185 -0.1060 0.1531 -0.0325 69 PHE A N 505 C CA . PHE A 69 ? 0.3845 0.2910 0.5016 -0.1029 0.1357 -0.0344 69 PHE A CA 506 C C . PHE A 69 ? 0.3998 0.2985 0.4865 -0.1025 0.1282 -0.0335 69 PHE A C 507 O O . PHE A 69 ? 0.3938 0.2998 0.4726 -0.0995 0.1157 -0.0350 69 PHE A O 508 C CB . PHE A 69 ? 0.3746 0.2867 0.4934 -0.1014 0.1348 -0.0398 69 PHE A CB 509 C CG . PHE A 69 ? 0.3623 0.2829 0.5101 -0.0987 0.1415 -0.0393 69 PHE A CG 510 C CD1 . PHE A 69 ? 0.3759 0.2901 0.5278 -0.0987 0.1590 -0.0392 69 PHE A CD1 511 C CD2 . PHE A 69 ? 0.3413 0.2768 0.5117 -0.0951 0.1306 -0.0381 69 PHE A CD2 512 C CE1 . PHE A 69 ? 0.3678 0.2922 0.5475 -0.0938 0.1658 -0.0370 69 PHE A CE1 513 C CE2 . PHE A 69 ? 0.3321 0.2782 0.5293 -0.0914 0.1360 -0.0362 69 PHE A CE2 514 C CZ . PHE A 69 ? 0.3444 0.2859 0.5471 -0.0901 0.1536 -0.0350 69 PHE A CZ 515 N N . LEU A 70 ? 0.4240 0.3095 0.4942 -0.1049 0.1363 -0.0300 70 LEU A N 516 C CA . LEU A 70 ? 0.4438 0.3222 0.4830 -0.1032 0.1308 -0.0276 70 LEU A CA 517 C C . LEU A 70 ? 0.4452 0.3255 0.4831 -0.0971 0.1173 -0.0232 70 LEU A C 518 O O . LEU A 70 ? 0.4525 0.3345 0.4689 -0.0924 0.1090 -0.0210 70 LEU A O 519 C CB . LEU A 70 ? 0.4693 0.3311 0.4901 -0.1067 0.1441 -0.0241 70 LEU A CB 520 C CG . LEU A 70 ? 0.4875 0.3424 0.4872 -0.1114 0.1551 -0.0280 70 LEU A CG 521 C CD1 . LEU A 70 ? 0.4771 0.3392 0.4850 -0.1137 0.1569 -0.0358 70 LEU A CD1 522 C CD2 . LEU A 70 ? 0.5065 0.3471 0.5056 -0.1152 0.1730 -0.0252 70 LEU A CD2 523 N N . GLU A 71 ? 0.4413 0.3217 0.5012 -0.0970 0.1155 -0.0218 71 GLU A N 524 C CA . GLU A 71 ? 0.4484 0.3256 0.5050 -0.0914 0.1046 -0.0183 71 GLU A CA 525 C C . GLU A 71 ? 0.4309 0.3180 0.5140 -0.0917 0.0974 -0.0209 71 GLU A C 526 O O . GLU A 71 ? 0.4428 0.3214 0.5293 -0.0919 0.0943 -0.0187 71 GLU A O 527 C CB . GLU A 71 ? 0.4756 0.3314 0.5177 -0.0923 0.1111 -0.0121 71 GLU A CB 528 C CG . GLU A 71 ? 0.5038 0.3501 0.5132 -0.0876 0.1129 -0.0074 71 GLU A CG 529 C CD . GLU A 71 ? 0.5369 0.3587 0.5291 -0.0865 0.1188 -0.0001 71 GLU A CD 530 O OE1 . GLU A 71 ? 0.5579 0.3681 0.5524 -0.0946 0.1316 0.0011 71 GLU A OE1 531 O OE2 . GLU A 71 ? 0.5504 0.3639 0.5267 -0.0773 0.1117 0.0048 71 GLU A OE2 532 N N . PHE A 72 ? 0.4136 0.3170 0.5128 -0.0919 0.0947 -0.0257 72 PHE A N 533 C CA . PHE A 72 ? 0.3941 0.3088 0.5184 -0.0921 0.0883 -0.0277 72 PHE A CA 534 C C . PHE A 72 ? 0.3925 0.3078 0.5113 -0.0860 0.0749 -0.0273 72 PHE A C 535 O O . PHE A 72 ? 0.4036 0.3167 0.5018 -0.0795 0.0696 -0.0257 72 PHE A O 536 C CB . PHE A 72 ? 0.3764 0.3056 0.5157 -0.0923 0.0899 -0.0318 72 PHE A CB 537 C CG . PHE A 72 ? 0.3712 0.3077 0.4985 -0.0882 0.0818 -0.0349 72 PHE A CG 538 C CD1 . PHE A 72 ? 0.3531 0.3000 0.4888 -0.0840 0.0702 -0.0361 72 PHE A CD1 539 C CD2 . PHE A 72 ? 0.3823 0.3163 0.4897 -0.0897 0.0861 -0.0367 72 PHE A CD2 540 C CE1 . PHE A 72 ? 0.3489 0.3049 0.4750 -0.0813 0.0634 -0.0385 72 PHE A CE1 541 C CE2 . PHE A 72 ? 0.3775 0.3211 0.4747 -0.0885 0.0785 -0.0397 72 PHE A CE2 542 C CZ . PHE A 72 ? 0.3620 0.3174 0.4697 -0.0841 0.0674 -0.0404 72 PHE A CZ 543 N N . SER A 73 ? 0.3805 0.3000 0.5177 -0.0879 0.0701 -0.0283 73 SER A N 544 C CA . SER A 73 ? 0.3709 0.2899 0.5050 -0.0828 0.0587 -0.0288 73 SER A CA 545 C C . SER A 73 ? 0.3396 0.2768 0.4966 -0.0834 0.0525 -0.0322 73 SER A C 546 O O . SER A 73 ? 0.3312 0.2770 0.5093 -0.0893 0.0569 -0.0326 73 SER A O 547 C CB . SER A 73 ? 0.3912 0.2918 0.5203 -0.0869 0.0597 -0.0268 73 SER A CB 548 O OG . SER A 73 ? 0.4025 0.2951 0.5195 -0.0802 0.0509 -0.0269 73 SER A OG 549 N N . ALA A 74 ? 0.3233 0.2676 0.4764 -0.0767 0.0430 -0.0338 74 ALA A N 550 C CA . ALA A 74 ? 0.2984 0.2595 0.4700 -0.0763 0.0378 -0.0365 74 ALA A CA 551 C C . ALA A 74 ? 0.2876 0.2532 0.4534 -0.0694 0.0270 -0.0378 74 ALA A C 552 O O . ALA A 74 ? 0.2947 0.2563 0.4422 -0.0629 0.0240 -0.0366 74 ALA A O 553 C CB . ALA A 74 ? 0.2909 0.2614 0.4667 -0.0767 0.0438 -0.0379 74 ALA A CB 554 N N . ASP A 75 ? 0.2686 0.2441 0.4504 -0.0703 0.0216 -0.0394 75 ASP A N 555 C CA . ASP A 75 ? 0.2564 0.2399 0.4361 -0.0642 0.0128 -0.0409 75 ASP A CA 556 C C . ASP A 75 ? 0.2371 0.2352 0.4255 -0.0634 0.0143 -0.0421 75 ASP A C 557 O O . ASP A 75 ? 0.2304 0.2356 0.4126 -0.0589 0.0097 -0.0430 75 ASP A O 558 C CB . ASP A 75 ? 0.2559 0.2407 0.4455 -0.0663 0.0060 -0.0420 75 ASP A CB 559 C CG . ASP A 75 ? 0.2786 0.2452 0.4575 -0.0696 0.0051 -0.0421 75 ASP A CG 560 O OD1 . ASP A 75 ? 0.2982 0.2501 0.4563 -0.0640 0.0060 -0.0411 75 ASP A OD1 561 O OD2 . ASP A 75 ? 0.2840 0.2510 0.4744 -0.0779 0.0037 -0.0428 75 ASP A OD2 562 N N . LEU A 76 ? 0.2289 0.2303 0.4313 -0.0678 0.0216 -0.0417 76 LEU A N 563 C CA . LEU A 76 ? 0.2193 0.2288 0.4286 -0.0672 0.0253 -0.0426 76 LEU A CA 564 C C . LEU A 76 ? 0.2267 0.2304 0.4346 -0.0710 0.0375 -0.0426 76 LEU A C 565 O O . LEU A 76 ? 0.2331 0.2336 0.4498 -0.0738 0.0437 -0.0407 76 LEU A O 566 C CB . LEU A 76 ? 0.2086 0.2280 0.4381 -0.0661 0.0224 -0.0411 76 LEU A CB 567 C CG . LEU A 76 ? 0.2046 0.2293 0.4418 -0.0639 0.0274 -0.0407 76 LEU A CG 568 C CD1 . LEU A 76 ? 0.2018 0.2279 0.4263 -0.0618 0.0227 -0.0432 76 LEU A CD1 569 C CD2 . LEU A 76 ? 0.1977 0.2336 0.4565 -0.0616 0.0253 -0.0369 76 LEU A CD2 570 N N . ILE A 77 ? 0.2274 0.2297 0.4231 -0.0719 0.0412 -0.0451 77 ILE A N 571 C CA . ILE A 77 ? 0.2379 0.2316 0.4265 -0.0761 0.0533 -0.0464 77 ILE A CA 572 C C . ILE A 77 ? 0.2388 0.2316 0.4313 -0.0765 0.0600 -0.0483 77 ILE A C 573 O O . ILE A 77 ? 0.2390 0.2359 0.4255 -0.0766 0.0552 -0.0504 77 ILE A O 574 C CB . ILE A 77 ? 0.2475 0.2375 0.4121 -0.0788 0.0522 -0.0482 77 ILE A CB 575 C CG1 . ILE A 77 ? 0.2495 0.2377 0.4085 -0.0757 0.0457 -0.0450 77 ILE A CG1 576 C CG2 . ILE A 77 ? 0.2626 0.2417 0.4165 -0.0843 0.0648 -0.0499 77 ILE A CG2 577 C CD1 . ILE A 77 ? 0.2611 0.2480 0.3971 -0.0757 0.0440 -0.0444 77 ILE A CD1 578 N N . ILE A 78 ? 0.2463 0.2328 0.4478 -0.0764 0.0723 -0.0470 78 ILE A N 579 C CA . ILE A 78 ? 0.2523 0.2330 0.4561 -0.0749 0.0817 -0.0479 78 ILE A CA 580 C C . ILE A 78 ? 0.2759 0.2392 0.4618 -0.0801 0.0963 -0.0517 78 ILE A C 581 O O . ILE A 78 ? 0.2837 0.2410 0.4717 -0.0801 0.1062 -0.0503 78 ILE A O 582 C CB . ILE A 78 ? 0.2455 0.2333 0.4754 -0.0677 0.0859 -0.0420 78 ILE A CB 583 C CG1 . ILE A 78 ? 0.2277 0.2325 0.4737 -0.0644 0.0712 -0.0387 78 ILE A CG1 584 C CG2 . ILE A 78 ? 0.2539 0.2333 0.4841 -0.0635 0.0958 -0.0417 78 ILE A CG2 585 C CD1 . ILE A 78 ? 0.2232 0.2413 0.4960 -0.0592 0.0731 -0.0323 78 ILE A CD1 586 N N . GLU A 79 ? 0.2885 0.2432 0.4557 -0.0854 0.0984 -0.0568 79 GLU A N 587 C CA . GLU A 79 ? 0.3167 0.2517 0.4628 -0.0922 0.1126 -0.0618 79 GLU A CA 588 C C . GLU A 79 ? 0.3278 0.2484 0.4798 -0.0871 0.1270 -0.0608 79 GLU A C 589 O O . GLU A 79 ? 0.3167 0.2413 0.4789 -0.0822 0.1236 -0.0585 79 GLU A O 590 C CB . GLU A 79 ? 0.3304 0.2637 0.4512 -0.1031 0.1076 -0.0684 79 GLU A CB 591 C CG . GLU A 79 ? 0.3288 0.2762 0.4394 -0.1071 0.0951 -0.0687 79 GLU A CG 592 C CD . GLU A 79 ? 0.3428 0.2941 0.4304 -0.1185 0.0902 -0.0745 79 GLU A CD 593 O OE1 . GLU A 79 ? 0.3315 0.2955 0.4229 -0.1192 0.0812 -0.0747 79 GLU A OE1 594 O OE2 . GLU A 79 ? 0.3663 0.3091 0.4315 -0.1278 0.0957 -0.0788 79 GLU A OE2 595 N N . ARG A 80 ? 0.3509 0.2534 0.4946 -0.0874 0.1439 -0.0620 80 ARG A N 596 C CA . ARG A 80 ? 0.3716 0.2572 0.5192 -0.0801 0.1609 -0.0601 80 ARG A CA 597 C C . ARG A 80 ? 0.4134 0.2686 0.5277 -0.0897 0.1755 -0.0684 80 ARG A C 598 O O . ARG A 80 ? 0.4266 0.2760 0.5187 -0.1009 0.1751 -0.0745 80 ARG A O 599 C CB . ARG A 80 ? 0.3683 0.2583 0.5370 -0.0701 0.1714 -0.0532 80 ARG A CB 600 C CG . ARG A 80 ? 0.3365 0.2562 0.5367 -0.0637 0.1576 -0.0456 80 ARG A CG 601 C CD . ARG A 80 ? 0.3195 0.2518 0.5380 -0.0556 0.1496 -0.0407 80 ARG A CD 602 N NE . ARG A 80 ? 0.2955 0.2544 0.5453 -0.0487 0.1408 -0.0327 80 ARG A NE 603 C CZ . ARG A 80 ? 0.2815 0.2559 0.5498 -0.0411 0.1327 -0.0271 80 ARG A CZ 604 N NH1 . ARG A 80 ? 0.2879 0.2523 0.5473 -0.0381 0.1331 -0.0279 80 ARG A NH1 605 N NH2 . ARG A 80 ? 0.2662 0.2657 0.5610 -0.0374 0.1244 -0.0206 80 ARG A NH2 606 N N . ARG A 81 ? 0.4409 0.2754 0.5501 -0.0854 0.1889 -0.0684 81 ARG A N 607 C CA . ARG A 81 ? 0.4897 0.2895 0.5641 -0.0955 0.2050 -0.0771 81 ARG A CA 608 C C . ARG A 81 ? 0.5114 0.2940 0.5709 -0.0975 0.2206 -0.0800 81 ARG A C 609 O O . ARG A 81 ? 0.5347 0.2974 0.5609 -0.1121 0.2262 -0.0894 81 ARG A O 610 C CB . ARG A 81 ? 0.5210 0.2972 0.5934 -0.0872 0.2198 -0.0748 81 ARG A CB 611 C CG . ARG A 81 ? 0.5671 0.3133 0.6031 -0.1029 0.2267 -0.0849 81 ARG A CG 612 C CD . ARG A 81 ? 0.6027 0.3220 0.6350 -0.0940 0.2418 -0.0818 81 ARG A CD 613 N NE . ARG A 81 ? 0.6257 0.3365 0.6388 -0.1084 0.2358 -0.0880 81 ARG A NE 614 C CZ . ARG A 81 ? 0.6120 0.3430 0.6421 -0.1051 0.2216 -0.0832 81 ARG A CZ 615 N NH1 . ARG A 81 ? 0.5848 0.3452 0.6506 -0.0878 0.2111 -0.0723 81 ARG A NH1 616 N NH2 . ARG A 81 ? 0.6294 0.3512 0.6396 -0.1202 0.2184 -0.0895 81 ARG A NH2 617 N N . GLU A 82 ? 0.5038 0.2958 0.5878 -0.0838 0.2274 -0.0719 82 GLU A N 618 C CA . GLU A 82 ? 0.5275 0.3053 0.6004 -0.0840 0.2433 -0.0734 82 GLU A CA 619 C C . GLU A 82 ? 0.5174 0.3080 0.5803 -0.0954 0.2317 -0.0769 82 GLU A C 620 O O . GLU A 82 ? 0.5383 0.3176 0.5893 -0.0971 0.2436 -0.0783 82 GLU A O 621 C CB . GLU A 82 ? 0.5242 0.3118 0.6290 -0.0656 0.2552 -0.0625 82 GLU A CB 622 C CG . GLU A 82 ? 0.4891 0.3162 0.6311 -0.0597 0.2390 -0.0538 82 GLU A CG 623 C CD . GLU A 82 ? 0.4660 0.3164 0.6368 -0.0506 0.2256 -0.0466 82 GLU A CD 624 O OE1 . GLU A 82 ? 0.4800 0.3177 0.6405 -0.0503 0.2253 -0.0488 82 GLU A OE1 625 O OE2 . GLU A 82 ? 0.4420 0.3228 0.6442 -0.0450 0.2153 -0.0389 82 GLU A OE2 626 N N . GLY A 83 ? 0.4912 0.3046 0.5580 -0.1020 0.2095 -0.0775 83 GLY A N 627 C CA . GLY A 83 ? 0.4833 0.3089 0.5399 -0.1106 0.1982 -0.0793 83 GLY A CA 628 C C . GLY A 83 ? 0.5155 0.3196 0.5315 -0.1255 0.2050 -0.0889 83 GLY A C 629 O O . GLY A 83 ? 0.5424 0.3289 0.5364 -0.1343 0.2096 -0.0961 83 GLY A O 630 N N . SER A 84 ? 0.5207 0.3251 0.5248 -0.1293 0.2062 -0.0890 84 SER A N 631 C CA . SER A 84 ? 0.5471 0.3364 0.5112 -0.1445 0.2090 -0.0975 84 SER A CA 632 C C . SER A 84 ? 0.5338 0.3438 0.4937 -0.1479 0.1939 -0.0945 84 SER A C 633 O O . SER A 84 ? 0.5179 0.3367 0.4955 -0.1391 0.1939 -0.0873 84 SER A O 634 C CB . SER A 84 ? 0.5851 0.3422 0.5286 -0.1453 0.2335 -0.1014 84 SER A CB 635 O OG . SER A 84 ? 0.6153 0.3593 0.5183 -0.1611 0.2348 -0.1096 84 SER A OG 636 N N . ASP A 85 ? 0.5423 0.3601 0.4781 -0.1606 0.1815 -0.0996 85 ASP A N 637 C CA . ASP A 85 ? 0.5358 0.3738 0.4636 -0.1630 0.1666 -0.0960 85 ASP A CA 638 C C . ASP A 85 ? 0.5672 0.3897 0.4663 -0.1689 0.1768 -0.0980 85 ASP A C 639 O O . ASP A 85 ? 0.5672 0.4027 0.4610 -0.1674 0.1679 -0.0928 85 ASP A O 640 C CB . ASP A 85 ? 0.5357 0.3926 0.4485 -0.1742 0.1498 -0.0998 85 ASP A CB 641 C CG . ASP A 85 ? 0.5077 0.3840 0.4468 -0.1685 0.1374 -0.0971 85 ASP A CG 642 O OD1 . ASP A 85 ? 0.4779 0.3671 0.4456 -0.1549 0.1310 -0.0892 85 ASP A OD1 643 O OD2 . ASP A 85 ? 0.5169 0.3951 0.4463 -0.1790 0.1340 -0.1031 85 ASP A OD2 644 N N . VAL A 86 ? 0.6004 0.3932 0.4782 -0.1753 0.1960 -0.1053 86 VAL A N 645 C CA . VAL A 86 ? 0.6384 0.4140 0.4807 -0.1843 0.2056 -0.1093 86 VAL A CA 646 C C . VAL A 86 ? 0.6596 0.4075 0.5019 -0.1775 0.2302 -0.1091 86 VAL A C 647 O O . VAL A 86 ? 0.6539 0.3909 0.5166 -0.1687 0.2424 -0.1084 86 VAL A O 648 C CB . VAL A 86 ? 0.6731 0.4373 0.4751 -0.2043 0.2053 -0.1210 86 VAL A CB 649 C CG1 . VAL A 86 ? 0.6546 0.4524 0.4555 -0.2118 0.1807 -0.1201 86 VAL A CG1 650 C CG2 . VAL A 86 ? 0.6907 0.4277 0.4883 -0.2084 0.2202 -0.1292 86 VAL A CG2 651 N N . CYS A 87 ? 0.6879 0.4263 0.5078 -0.1805 0.2374 -0.1087 87 CYS A N 652 C CA . CYS A 87 ? 0.7204 0.4295 0.5301 -0.1772 0.2629 -0.1103 87 CYS A CA 653 C C . CYS A 87 ? 0.7691 0.4520 0.5276 -0.1943 0.2716 -0.1219 87 CYS A C 654 O O . CYS A 87 ? 0.7958 0.4490 0.5378 -0.1984 0.2888 -0.1302 87 CYS A O 655 C CB . CYS A 87 ? 0.7157 0.4318 0.5396 -0.1676 0.2673 -0.1006 87 CYS A CB 656 S SG . CYS A 87 ? 0.7244 0.4556 0.5246 -0.1739 0.2511 -0.0962 87 CYS A SG 657 N N . TYR A 88 ? 0.7808 0.4738 0.5121 -0.2045 0.2595 -0.1224 88 TYR A N 658 C CA . TYR A 88 ? 0.8260 0.5004 0.5070 -0.2243 0.2625 -0.1340 88 TYR A CA 659 C C . TYR A 88 ? 0.8207 0.5067 0.4983 -0.2365 0.2477 -0.1409 88 TYR A C 660 O O . TYR A 88 ? 0.7894 0.5108 0.4880 -0.2342 0.2252 -0.1349 88 TYR A O 661 C CB . TYR A 88 ? 0.8397 0.5266 0.4936 -0.2310 0.2521 -0.1311 88 TYR A CB 662 C CG . TYR A 88 ? 0.8936 0.5578 0.4922 -0.2514 0.2590 -0.1429 88 TYR A CG 663 C CD1 . TYR A 88 ? 0.9359 0.5649 0.5061 -0.2529 0.2827 -0.1471 88 TYR A CD1 664 C CD2 . TYR A 88 ? 0.9058 0.5847 0.4795 -0.2703 0.2420 -0.1501 88 TYR A CD2 665 C CE1 . TYR A 88 ? 0.9879 0.5935 0.5037 -0.2728 0.2894 -0.1589 88 TYR A CE1 666 C CE2 . TYR A 88 ? 0.9560 0.6150 0.4770 -0.2916 0.2475 -0.1617 88 TYR A CE2 667 C CZ . TYR A 88 ? 0.9984 0.6191 0.4893 -0.2928 0.2712 -0.1664 88 TYR A CZ 668 O OH . TYR A 88 ? 1.0516 0.6498 0.4869 -0.3149 0.2772 -0.1787 88 TYR A OH 669 N N . PRO A 89 ? 0.8566 0.5116 0.5064 -0.2498 0.2612 -0.1533 89 PRO A N 670 C CA . PRO A 89 ? 0.8534 0.5168 0.5016 -0.2622 0.2496 -0.1598 89 PRO A CA 671 C C . PRO A 89 ? 0.8443 0.5466 0.4830 -0.2753 0.2227 -0.1590 89 PRO A C 672 O O . PRO A 89 ? 0.8646 0.5730 0.4748 -0.2841 0.2177 -0.1596 89 PRO A O 673 C CB . PRO A 89 ? 0.9068 0.5237 0.5126 -0.2785 0.2708 -0.1744 89 PRO A CB 674 C CG . PRO A 89 ? 0.9448 0.5348 0.5210 -0.2786 0.2887 -0.1766 89 PRO A CG 675 C CD . PRO A 89 ? 0.9088 0.5181 0.5222 -0.2558 0.2880 -0.1623 89 PRO A CD 676 N N . GLY A 90 ? 0.8162 0.5463 0.4799 -0.2750 0.2059 -0.1566 90 GLY A N 677 C CA . GLY A 90 ? 0.7995 0.5741 0.4647 -0.2819 0.1798 -0.1525 90 GLY A CA 678 C C . GLY A 90 ? 0.7599 0.5619 0.4626 -0.2744 0.1657 -0.1476 90 GLY A C 679 O O . GLY A 90 ? 0.7452 0.5319 0.4726 -0.2637 0.1754 -0.1467 90 GLY A O 680 N N . LYS A 91 ? 0.7459 0.5894 0.4528 -0.2794 0.1432 -0.1437 91 LYS A N 681 C CA . LYS A 91 ? 0.7114 0.5833 0.4549 -0.2699 0.1295 -0.1375 91 LYS A CA 682 C C . LYS A 91 ? 0.6895 0.6093 0.4421 -0.2656 0.1062 -0.1279 91 LYS A C 683 O O . LYS A 91 ? 0.7142 0.6474 0.4413 -0.2735 0.0993 -0.1271 91 LYS A O 684 C CB . LYS A 91 ? 0.7257 0.5892 0.4638 -0.2859 0.1322 -0.1473 91 LYS A CB 685 C CG . LYS A 91 ? 0.7473 0.6360 0.4604 -0.3105 0.1186 -0.1537 91 LYS A CG 686 C CD . LYS A 91 ? 0.7742 0.6403 0.4731 -0.3300 0.1277 -0.1658 91 LYS A CD 687 C CE . LYS A 91 ? 0.7410 0.6173 0.4764 -0.3190 0.1240 -0.1612 91 LYS A CE 688 N NZ . LYS A 91 ? 0.7197 0.6476 0.4695 -0.3241 0.1015 -0.1566 91 LYS A NZ 689 N N . PHE A 92 ? 0.6494 0.5938 0.4372 -0.2517 0.0949 -0.1201 92 PHE A N 690 C CA . PHE A 92 ? 0.6245 0.6134 0.4248 -0.2435 0.0743 -0.1097 92 PHE A CA 691 C C . PHE A 92 ? 0.6256 0.6469 0.4205 -0.2596 0.0608 -0.1134 92 PHE A C 692 O O . PHE A 92 ? 0.6259 0.6385 0.4255 -0.2696 0.0652 -0.1208 92 PHE A O 693 C CB . PHE A 92 ? 0.5832 0.5810 0.4233 -0.2202 0.0697 -0.0998 92 PHE A CB 694 C CG . PHE A 92 ? 0.5718 0.5555 0.4207 -0.2025 0.0753 -0.0918 92 PHE A CG 695 C CD1 . PHE A 92 ? 0.5735 0.5224 0.4293 -0.1977 0.0927 -0.0944 92 PHE A CD1 696 C CD2 . PHE A 92 ? 0.5630 0.5689 0.4136 -0.1903 0.0638 -0.0808 92 PHE A CD2 697 C CE1 . PHE A 92 ? 0.5671 0.5052 0.4320 -0.1835 0.0981 -0.0870 92 PHE A CE1 698 C CE2 . PHE A 92 ? 0.5596 0.5497 0.4164 -0.1759 0.0700 -0.0736 92 PHE A CE2 699 C CZ . PHE A 92 ? 0.5597 0.5169 0.4244 -0.1736 0.0869 -0.0770 92 PHE A CZ 700 N N . VAL A 93 ? 0.6312 0.6918 0.4179 -0.2610 0.0445 -0.1069 93 VAL A N 701 C CA . VAL A 93 ? 0.6262 0.7307 0.4164 -0.2718 0.0285 -0.1063 93 VAL A CA 702 C C . VAL A 93 ? 0.5869 0.7162 0.4151 -0.2500 0.0190 -0.0955 93 VAL A C 703 O O . VAL A 93 ? 0.5698 0.7007 0.4117 -0.2277 0.0166 -0.0848 93 VAL A O 704 C CB . VAL A 93 ? 0.6500 0.7911 0.4169 -0.2797 0.0147 -0.1017 93 VAL A CB 705 C CG1 . VAL A 93 ? 0.6396 0.8343 0.4148 -0.2888 -0.0029 -0.0988 93 VAL A CG1 706 C CG2 . VAL A 93 ? 0.6972 0.8131 0.4225 -0.3030 0.0237 -0.1132 93 VAL A CG2 707 N N . ASN A 94 ? 0.5778 0.7241 0.4207 -0.2571 0.0145 -0.0984 94 ASN A N 708 C CA . ASN A 94 ? 0.5411 0.7076 0.4182 -0.2377 0.0071 -0.0896 94 ASN A CA 709 C C . ASN A 94 ? 0.5176 0.6466 0.4142 -0.2197 0.0186 -0.0883 94 ASN A C 710 O O . ASN A 94 ? 0.4942 0.6285 0.4096 -0.1978 0.0145 -0.0784 94 ASN A O 711 C CB . ASN A 94 ? 0.5336 0.7425 0.4183 -0.2211 -0.0083 -0.0756 94 ASN A CB 712 C CG . ASN A 94 ? 0.5303 0.7898 0.4243 -0.2270 -0.0224 -0.0722 94 ASN A CG 713 O OD1 . ASN A 94 ? 0.5561 0.8410 0.4319 -0.2483 -0.0286 -0.0765 94 ASN A OD1 714 N ND2 . ASN A 94 ? 0.5046 0.7806 0.4265 -0.2086 -0.0274 -0.0644 94 ASN A ND2 715 N N . GLU A 95 ? 0.5252 0.6161 0.4163 -0.2293 0.0334 -0.0981 95 GLU A N 716 C CA . GLU A 95 ? 0.5139 0.5701 0.4204 -0.2139 0.0455 -0.0968 95 GLU A CA 717 C C . GLU A 95 ? 0.4723 0.5341 0.4109 -0.1989 0.0423 -0.0919 95 GLU A C 718 O O . GLU A 95 ? 0.4530 0.5074 0.4096 -0.1806 0.0430 -0.0852 95 GLU A O 719 C CB . GLU A 95 ? 0.5469 0.5604 0.4362 -0.2259 0.0640 -0.1073 95 GLU A CB 720 C CG . GLU A 95 ? 0.5655 0.5673 0.4492 -0.2421 0.0702 -0.1167 95 GLU A CG 721 C CD . GLU A 95 ? 0.6091 0.5653 0.4693 -0.2532 0.0901 -0.1266 95 GLU A CD 722 O OE1 . GLU A 95 ? 0.6449 0.5944 0.4719 -0.2729 0.0931 -0.1347 95 GLU A OE1 723 O OE2 . GLU A 95 ? 0.6085 0.5361 0.4826 -0.2414 0.1032 -0.1260 95 GLU A OE2 724 N N . GLU A 96 ? 0.4567 0.5309 0.4009 -0.2078 0.0389 -0.0955 96 GLU A N 725 C CA . GLU A 96 ? 0.4228 0.5000 0.3944 -0.1952 0.0368 -0.0917 96 GLU A CA 726 C C . GLU A 96 ? 0.3918 0.5000 0.3814 -0.1773 0.0231 -0.0810 96 GLU A C 727 O O . GLU A 96 ? 0.3668 0.4684 0.3771 -0.1612 0.0230 -0.0763 96 GLU A O 728 C CB . GLU A 96 ? 0.4271 0.5083 0.3978 -0.2099 0.0378 -0.0980 96 GLU A CB 729 C CG . GLU A 96 ? 0.4079 0.4792 0.4026 -0.1979 0.0405 -0.0956 96 GLU A CG 730 C CD . GLU A 96 ? 0.4099 0.4435 0.4109 -0.1882 0.0538 -0.0961 96 GLU A CD 731 O OE1 . GLU A 96 ? 0.4333 0.4417 0.4164 -0.1956 0.0650 -0.1013 96 GLU A OE1 732 O OE2 . GLU A 96 ? 0.3953 0.4258 0.4187 -0.1731 0.0532 -0.0912 96 GLU A OE2 733 N N . ALA A 97 ? 0.3911 0.5329 0.3715 -0.1803 0.0119 -0.0771 97 ALA A N 734 C CA . ALA A 97 ? 0.3704 0.5393 0.3631 -0.1614 0.0006 -0.0659 97 ALA A CA 735 C C . ALA A 97 ? 0.3636 0.5090 0.3600 -0.1440 0.0048 -0.0603 97 ALA A C 736 O O . ALA A 97 ? 0.3459 0.4916 0.3590 -0.1267 0.0018 -0.0539 97 ALA A O 737 C CB . ALA A 97 ? 0.3819 0.5894 0.3605 -0.1674 -0.0103 -0.0618 97 ALA A CB 738 N N . LEU A 98 ? 0.3783 0.5019 0.3575 -0.1501 0.0126 -0.0633 98 LEU A N 739 C CA . LEU A 98 ? 0.3749 0.4754 0.3558 -0.1368 0.0182 -0.0585 98 LEU A CA 740 C C . LEU A 98 ? 0.3572 0.4310 0.3586 -0.1298 0.0266 -0.0603 98 LEU A C 741 O O . LEU A 98 ? 0.3446 0.4098 0.3571 -0.1156 0.0266 -0.0544 98 LEU A O 742 C CB . LEU A 98 ? 0.4013 0.4851 0.3577 -0.1468 0.0259 -0.0618 98 LEU A CB 743 C CG . LEU A 98 ? 0.4071 0.4679 0.3612 -0.1359 0.0328 -0.0567 98 LEU A CG 744 C CD1 . LEU A 98 ? 0.4005 0.4766 0.3589 -0.1182 0.0234 -0.0451 98 LEU A CD1 745 C CD2 . LEU A 98 ? 0.4367 0.4842 0.3631 -0.1475 0.0403 -0.0605 98 LEU A CD2 746 N N . ARG A 99 ? 0.3531 0.4138 0.3585 -0.1399 0.0339 -0.0682 99 ARG A N 747 C CA . ARG A 99 ? 0.3373 0.3780 0.3632 -0.1326 0.0408 -0.0688 99 ARG A CA 748 C C . ARG A 99 ? 0.3136 0.3705 0.3595 -0.1202 0.0310 -0.0634 99 ARG A C 749 O O . ARG A 99 ? 0.3026 0.3489 0.3646 -0.1092 0.0322 -0.0601 99 ARG A O 750 C CB . ARG A 99 ? 0.3452 0.3691 0.3693 -0.1442 0.0509 -0.0769 99 ARG A CB 751 C CG . ARG A 99 ? 0.3725 0.3724 0.3760 -0.1554 0.0642 -0.0832 99 ARG A CG 752 C CD . ARG A 99 ? 0.3797 0.3532 0.3872 -0.1588 0.0782 -0.0885 99 ARG A CD 753 N NE . ARG A 99 ? 0.4086 0.3559 0.3941 -0.1682 0.0930 -0.0945 99 ARG A NE 754 C CZ . ARG A 99 ? 0.4356 0.3757 0.3934 -0.1859 0.0970 -0.1027 99 ARG A CZ 755 N NH1 . ARG A 99 ? 0.4365 0.3969 0.3868 -0.1976 0.0870 -0.1057 99 ARG A NH1 756 N NH2 . ARG A 99 ? 0.4637 0.3762 0.4004 -0.1929 0.1119 -0.1081 99 ARG A NH2 757 N N . GLN A 100 ? 0.3064 0.3900 0.3508 -0.1226 0.0214 -0.0626 100 GLN A N 758 C CA . GLN A 100 ? 0.2873 0.3864 0.3482 -0.1109 0.0131 -0.0578 100 GLN A CA 759 C C . GLN A 100 ? 0.2831 0.3848 0.3464 -0.0945 0.0079 -0.0496 100 GLN A C 760 O O . GLN A 100 ? 0.2703 0.3660 0.3473 -0.0832 0.0061 -0.0467 100 GLN A O 761 C CB . GLN A 100 ? 0.2852 0.4143 0.3440 -0.1179 0.0055 -0.0586 100 GLN A CB 762 C CG . GLN A 100 ? 0.2854 0.4058 0.3470 -0.1308 0.0114 -0.0660 100 GLN A CG 763 C CD . GLN A 100 ? 0.2904 0.4375 0.3448 -0.1447 0.0065 -0.0687 100 GLN A CD 764 O OE1 . GLN A 100 ? 0.2904 0.4696 0.3415 -0.1433 -0.0029 -0.0641 100 GLN A OE1 765 N NE2 . GLN A 100 ? 0.2972 0.4318 0.3490 -0.1584 0.0135 -0.0757 100 GLN A NE2 766 N N . ILE A 101 ? 0.2979 0.4059 0.3455 -0.0939 0.0061 -0.0459 101 ILE A N 767 C CA . ILE A 101 ? 0.3028 0.4071 0.3481 -0.0787 0.0036 -0.0377 101 ILE A CA 768 C C . ILE A 101 ? 0.3021 0.3746 0.3549 -0.0751 0.0118 -0.0385 101 ILE A C 769 O O . ILE A 101 ? 0.2956 0.3600 0.3572 -0.0637 0.0101 -0.0346 101 ILE A O 770 C CB . ILE A 101 ? 0.3243 0.4396 0.3487 -0.0795 0.0013 -0.0332 101 ILE A CB 771 C CG1 . ILE A 101 ? 0.3251 0.4796 0.3457 -0.0794 -0.0092 -0.0295 101 ILE A CG1 772 C CG2 . ILE A 101 ? 0.3351 0.4362 0.3537 -0.0645 0.0023 -0.0248 101 ILE A CG2 773 C CD1 . ILE A 101 ? 0.3457 0.5170 0.3452 -0.0878 -0.0120 -0.0279 101 ILE A CD1 774 N N . LEU A 102 ? 0.3112 0.3662 0.3601 -0.0855 0.0212 -0.0436 102 LEU A N 775 C CA . LEU A 102 ? 0.3121 0.3415 0.3693 -0.0832 0.0297 -0.0437 102 LEU A CA 776 C C . LEU A 102 ? 0.2971 0.3204 0.3768 -0.0805 0.0304 -0.0457 102 LEU A C 777 O O . LEU A 102 ? 0.2937 0.3042 0.3831 -0.0753 0.0326 -0.0433 102 LEU A O 778 C CB . LEU A 102 ? 0.3258 0.3398 0.3729 -0.0939 0.0410 -0.0481 102 LEU A CB 779 C CG . LEU A 102 ? 0.3457 0.3619 0.3686 -0.0962 0.0411 -0.0454 102 LEU A CG 780 C CD1 . LEU A 102 ? 0.3631 0.3616 0.3740 -0.1074 0.0535 -0.0508 102 LEU A CD1 781 C CD2 . LEU A 102 ? 0.3519 0.3619 0.3717 -0.0841 0.0391 -0.0369 102 LEU A CD2 782 N N . ARG A 103 ? 0.2912 0.3240 0.3780 -0.0849 0.0285 -0.0498 103 ARG A N 783 C CA . ARG A 103 ? 0.2798 0.3092 0.3864 -0.0814 0.0280 -0.0507 103 ARG A CA 784 C C . ARG A 103 ? 0.2725 0.3058 0.3865 -0.0700 0.0197 -0.0461 103 ARG A C 785 O O . ARG A 103 ? 0.2661 0.2909 0.3942 -0.0670 0.0203 -0.0458 103 ARG A O 786 C CB . ARG A 103 ? 0.2763 0.3148 0.3857 -0.0876 0.0273 -0.0550 103 ARG A CB 787 C CG . ARG A 103 ? 0.2894 0.3138 0.3949 -0.0979 0.0386 -0.0604 103 ARG A CG 788 C CD . ARG A 103 ? 0.2866 0.3136 0.3962 -0.1027 0.0395 -0.0639 103 ARG A CD 789 N NE . ARG A 103 ? 0.3051 0.3171 0.4023 -0.1142 0.0509 -0.0697 103 ARG A NE 790 C CZ . ARG A 103 ? 0.3182 0.3349 0.3982 -0.1268 0.0513 -0.0746 103 ARG A CZ 791 N NH1 . ARG A 103 ? 0.3122 0.3536 0.3879 -0.1294 0.0403 -0.0737 103 ARG A NH1 792 N NH2 . ARG A 103 ? 0.3408 0.3371 0.4070 -0.1374 0.0637 -0.0805 103 ARG A NH2 793 N N . GLU A 104 ? 0.2740 0.3204 0.3778 -0.0637 0.0125 -0.0423 104 GLU A N 794 C CA . GLU A 104 ? 0.2742 0.3210 0.3811 -0.0519 0.0063 -0.0382 104 GLU A CA 795 C C . GLU A 104 ? 0.2833 0.3181 0.3782 -0.0442 0.0071 -0.0327 104 GLU A C 796 O O . GLU A 104 ? 0.2837 0.3163 0.3749 -0.0334 0.0031 -0.0287 104 GLU A O 797 C CB . GLU A 104 ? 0.2765 0.3467 0.3822 -0.0471 -0.0013 -0.0368 104 GLU A CB 798 C CG . GLU A 104 ? 0.2953 0.3848 0.3865 -0.0445 -0.0048 -0.0325 104 GLU A CG 799 C CD . GLU A 104 ? 0.3006 0.4173 0.3935 -0.0384 -0.0119 -0.0298 104 GLU A CD 800 O OE1 . GLU A 104 ? 0.2952 0.4125 0.3987 -0.0348 -0.0138 -0.0312 104 GLU A OE1 801 O OE2 . GLU A 104 ? 0.3097 0.4494 0.3933 -0.0374 -0.0156 -0.0258 104 GLU A OE2 802 N N . SER A 105 ? 0.2930 0.3171 0.3801 -0.0497 0.0135 -0.0325 105 SER A N 803 C CA . SER A 105 ? 0.3095 0.3203 0.3823 -0.0436 0.0159 -0.0268 105 SER A CA 804 C C . SER A 105 ? 0.3156 0.3036 0.3930 -0.0400 0.0184 -0.0255 105 SER A C 805 O O . SER A 105 ? 0.3333 0.3080 0.3971 -0.0324 0.0194 -0.0201 105 SER A O 806 C CB . SER A 105 ? 0.3201 0.3237 0.3836 -0.0523 0.0236 -0.0277 105 SER A CB 807 O OG . SER A 105 ? 0.3125 0.3028 0.3896 -0.0609 0.0314 -0.0323 105 SER A OG 808 N N . GLY A 106 ? 0.3043 0.2876 0.3998 -0.0461 0.0198 -0.0301 106 GLY A N 809 C CA . GLY A 106 ? 0.3135 0.2771 0.4146 -0.0480 0.0232 -0.0298 106 GLY A CA 810 C C . GLY A 106 ? 0.3261 0.2773 0.4264 -0.0557 0.0328 -0.0293 106 GLY A C 811 O O . GLY A 106 ? 0.3325 0.2680 0.4362 -0.0592 0.0368 -0.0285 106 GLY A O 812 N N . GLY A 107 ? 0.3304 0.2886 0.4254 -0.0597 0.0372 -0.0301 107 GLY A N 813 C CA . GLY A 107 ? 0.3454 0.2917 0.4347 -0.0657 0.0474 -0.0291 107 GLY A CA 814 C C . GLY A 107 ? 0.3675 0.3063 0.4316 -0.0608 0.0485 -0.0236 107 GLY A C 815 O O . GLY A 107 ? 0.3676 0.3131 0.4196 -0.0517 0.0412 -0.0201 107 GLY A O 816 N N . ILE A 108 ? 0.3871 0.3127 0.4434 -0.0659 0.0582 -0.0220 108 ILE A N 817 C CA . ILE A 108 ? 0.4146 0.3340 0.4450 -0.0620 0.0603 -0.0165 108 ILE A CA 818 C C . ILE A 108 ? 0.4425 0.3373 0.4634 -0.0630 0.0694 -0.0116 108 ILE A C 819 O O . ILE A 108 ? 0.4379 0.3232 0.4726 -0.0712 0.0776 -0.0138 108 ILE A O 820 C CB . ILE A 108 ? 0.4173 0.3463 0.4379 -0.0687 0.0639 -0.0195 108 ILE A CB 821 C CG1 . ILE A 108 ? 0.4149 0.3358 0.4485 -0.0790 0.0756 -0.0245 108 ILE A CG1 822 C CG2 . ILE A 108 ? 0.4042 0.3568 0.4273 -0.0685 0.0545 -0.0232 108 ILE A CG2 823 C CD1 . ILE A 108 ? 0.4235 0.3492 0.4465 -0.0864 0.0809 -0.0292 108 ILE A CD1 824 N N . ASP A 109 ? 0.4737 0.3600 0.4707 -0.0541 0.0681 -0.0043 109 ASP A N 825 C CA . ASP A 109 ? 0.5152 0.3760 0.4957 -0.0538 0.0773 0.0019 109 ASP A CA 826 C C . ASP A 109 ? 0.5358 0.4006 0.4924 -0.0522 0.0796 0.0060 109 ASP A C 827 O O . ASP A 109 ? 0.5320 0.4175 0.4796 -0.0462 0.0708 0.0073 109 ASP A O 828 C CB . ASP A 109 ? 0.5416 0.3857 0.5107 -0.0425 0.0739 0.0080 109 ASP A CB 829 C CG . ASP A 109 ? 0.5894 0.4043 0.5346 -0.0396 0.0832 0.0161 109 ASP A CG 830 O OD1 . ASP A 109 ? 0.6130 0.4166 0.5570 -0.0497 0.0936 0.0158 109 ASP A OD1 831 O OD2 . ASP A 109 ? 0.6182 0.4196 0.5448 -0.0263 0.0810 0.0234 109 ASP A OD2 832 N N . LYS A 110 ? 0.5553 0.4026 0.5017 -0.0584 0.0913 0.0081 110 LYS A N 833 C CA . LYS A 110 ? 0.5770 0.4266 0.4995 -0.0591 0.0948 0.0111 110 LYS A CA 834 C C . LYS A 110 ? 0.6204 0.4480 0.5154 -0.0510 0.0995 0.0220 110 LYS A C 835 O O . LYS A 110 ? 0.6311 0.4335 0.5267 -0.0517 0.1072 0.0250 110 LYS A O 836 C CB . LYS A 110 ? 0.5725 0.4186 0.5019 -0.0726 0.1065 0.0048 110 LYS A CB 837 C CG . LYS A 110 ? 0.5438 0.4096 0.4927 -0.0796 0.1037 -0.0050 110 LYS A CG 838 C CD . LYS A 110 ? 0.5476 0.4294 0.4774 -0.0815 0.0987 -0.0074 110 LYS A CD 839 C CE . LYS A 110 ? 0.5222 0.4205 0.4690 -0.0882 0.0955 -0.0169 110 LYS A CE 840 N NZ . LYS A 110 ? 0.5155 0.4034 0.4804 -0.0961 0.1084 -0.0228 110 LYS A NZ 841 N N . GLU A 111 ? 0.6476 0.4847 0.5172 -0.0441 0.0953 0.0281 111 GLU A N 842 C CA . GLU A 111 ? 0.6907 0.5074 0.5311 -0.0346 0.1000 0.0400 111 GLU A CA 843 C C . GLU A 111 ? 0.7124 0.5365 0.5264 -0.0366 0.1017 0.0434 111 GLU A C 844 O O . GLU A 111 ? 0.7019 0.5542 0.5134 -0.0387 0.0927 0.0400 111 GLU A O 845 C CB . GLU A 111 ? 0.7032 0.5225 0.5350 -0.0162 0.0907 0.0489 111 GLU A CB 846 C CG . GLU A 111 ? 0.7455 0.5309 0.5527 -0.0054 0.0989 0.0609 111 GLU A CG 847 C CD . GLU A 111 ? 0.7576 0.5399 0.5593 0.0136 0.0923 0.0687 111 GLU A CD 848 O OE1 . GLU A 111 ? 0.7393 0.5227 0.5622 0.0129 0.0886 0.0623 111 GLU A OE1 849 O OE2 . GLU A 111 ? 0.7935 0.5725 0.5688 0.0302 0.0914 0.0816 111 GLU A OE2 850 N N . ALA A 112 ? 0.7486 0.5464 0.5415 -0.0369 0.1134 0.0501 112 ALA A N 851 C CA . ALA A 112 ? 0.7760 0.5762 0.5392 -0.0386 0.1163 0.0544 112 ALA A CA 852 C C . ALA A 112 ? 0.7876 0.6141 0.5312 -0.0254 0.1019 0.0628 112 ALA A C 853 O O . ALA A 112 ? 0.7926 0.6182 0.5319 -0.0088 0.0960 0.0725 112 ALA A O 854 C CB . ALA A 112 ? 0.8104 0.5754 0.5525 -0.0379 0.1311 0.0628 112 ALA A CB 855 N N . MET A 113 ? 0.7913 0.6418 0.5230 -0.0332 0.0965 0.0588 113 MET A N 856 C CA . MET A 113 ? 0.8011 0.6839 0.5149 -0.0236 0.0818 0.0665 113 MET A CA 857 C C . MET A 113 ? 0.8405 0.7106 0.5189 -0.0109 0.0848 0.0823 113 MET A C 858 O O . MET A 113 ? 0.8494 0.7393 0.5150 0.0056 0.0741 0.0946 113 MET A O 859 C CB . MET A 113 ? 0.7986 0.7093 0.5079 -0.0398 0.0757 0.0562 113 MET A CB 860 C CG . MET A 113 ? 0.7605 0.6867 0.5005 -0.0516 0.0717 0.0416 113 MET A CG 861 S SD . MET A 113 ? 0.7465 0.7191 0.5005 -0.0448 0.0515 0.0427 113 MET A SD 862 C CE . MET A 113 ? 0.7745 0.7794 0.4933 -0.0444 0.0403 0.0511 113 MET A CE 863 N N . GLY A 114 ? 0.8580 0.6960 0.5205 -0.0179 0.0999 0.0829 114 GLY A N 864 C CA . GLY A 114 ? 0.9005 0.7206 0.5277 -0.0068 0.1052 0.0980 114 GLY A CA 865 C C . GLY A 114 ? 0.9254 0.7648 0.5210 -0.0115 0.1006 0.1007 114 GLY A C 866 O O . GLY A 114 ? 0.9601 0.7976 0.5252 0.0020 0.0990 0.1159 114 GLY A O 867 N N . PHE A 115 ? 1.2136 0.6785 0.7317 -0.1024 -0.2594 0.0709 115 PHE A N 868 C CA . PHE A 115 ? 1.1982 0.7227 0.7195 -0.1208 -0.2477 0.0740 115 PHE A CA 869 C C . PHE A 115 ? 1.2182 0.7385 0.7220 -0.1624 -0.2516 0.1000 115 PHE A C 870 O O . PHE A 115 ? 1.2065 0.7189 0.7134 -0.1880 -0.2387 0.1050 115 PHE A O 871 C CB . PHE A 115 ? 1.1362 0.7255 0.6872 -0.1298 -0.2071 0.0491 115 PHE A CB 872 C CG . PHE A 115 ? 1.1158 0.7323 0.6832 -0.0975 -0.2009 0.0246 115 PHE A CG 873 C CD1 . PHE A 115 ? 1.1476 0.7594 0.7058 -0.0601 -0.2285 0.0235 115 PHE A CD1 874 C CD2 . PHE A 115 ? 1.0705 0.7196 0.6601 -0.1042 -0.1675 0.0028 115 PHE A CD2 875 C CE1 . PHE A 115 ? 1.1283 0.7805 0.7026 -0.0318 -0.2217 0.0002 115 PHE A CE1 876 C CE2 . PHE A 115 ? 1.0544 0.7361 0.6572 -0.0809 -0.1615 -0.0181 115 PHE A CE2 877 C CZ . PHE A 115 ? 1.0798 0.7696 0.6765 -0.0453 -0.1881 -0.0199 115 PHE A CZ 878 N N . THR A 116 ? 1.2475 0.7810 0.7328 -0.1685 -0.2698 0.1171 116 THR A N 879 C CA . THR A 116 ? 1.2572 0.8119 0.7286 -0.2112 -0.2693 0.1396 116 THR A CA 880 C C . THR A 116 ? 1.2235 0.8594 0.7085 -0.2225 -0.2471 0.1281 116 THR A C 881 O O . THR A 116 ? 1.2109 0.8771 0.7059 -0.1967 -0.2449 0.1119 116 THR A O 882 C CB . THR A 116 ? 1.3340 0.8326 0.7655 -0.2157 -0.3123 0.1742 116 THR A CB 883 O OG1 . THR A 116 ? 1.3670 0.8544 0.7890 -0.1750 -0.3358 0.1732 116 THR A OG1 884 C CG2 . THR A 116 ? 1.3748 0.7912 0.7856 -0.2199 -0.3327 0.1875 116 THR A CG2 885 N N . TYR A 117 ? 1.2093 0.8854 0.6929 -0.2623 -0.2308 0.1353 117 TYR A N 886 C CA . TYR A 117 ? 1.1774 0.9297 0.6718 -0.2789 -0.2056 0.1205 117 TYR A CA 887 C C . TYR A 117 ? 1.2032 0.9876 0.6773 -0.3145 -0.2158 0.1454 117 TYR A C 888 O O . TYR A 117 ? 1.2202 0.9886 0.6814 -0.3407 -0.2227 0.1658 117 TYR A O 889 C CB . TYR A 117 ? 1.1274 0.9065 0.6443 -0.2899 -0.1639 0.0923 117 TYR A CB 890 C CG . TYR A 117 ? 1.1008 0.8562 0.6370 -0.2594 -0.1516 0.0685 117 TYR A CG 891 C CD1 . TYR A 117 ? 1.0852 0.8694 0.6312 -0.2416 -0.1439 0.0479 117 TYR A CD1 892 C CD2 . TYR A 117 ? 1.0918 0.8029 0.6353 -0.2506 -0.1485 0.0678 117 TYR A CD2 893 C CE1 . TYR A 117 ? 1.0643 0.8331 0.6263 -0.2173 -0.1334 0.0279 117 TYR A CE1 894 C CE2 . TYR A 117 ? 1.0682 0.7616 0.6286 -0.2242 -0.1379 0.0477 117 TYR A CE2 895 C CZ . TYR A 117 ? 1.0571 0.7787 0.6263 -0.2081 -0.1305 0.0281 117 TYR A CZ 896 O OH . TYR A 117 ? 1.0380 0.7480 0.6224 -0.1854 -0.1205 0.0097 117 TYR A OH 897 N N . SER A 118 ? 1.2066 1.0438 0.6775 -0.3179 -0.2168 0.1443 118 SER A N 898 C CA . SER A 118 ? 1.2317 1.1122 0.6845 -0.3531 -0.2243 0.1663 118 SER A CA 899 C C . SER A 118 ? 1.2007 1.1647 0.6645 -0.3694 -0.1956 0.1425 118 SER A C 900 O O . SER A 118 ? 1.1932 1.1826 0.6657 -0.3494 -0.1921 0.1258 118 SER A O 901 C CB . SER A 118 ? 1.2922 1.1416 0.7168 -0.3422 -0.2689 0.2021 118 SER A CB 902 O OG . SER A 118 ? 1.2941 1.1678 0.7230 -0.3100 -0.2770 0.1933 118 SER A OG 903 N N . GLY A 119 ? 1.1893 1.1993 0.6508 -0.4068 -0.1754 0.1397 119 GLY A N 904 C CA . GLY A 119 ? 1.1661 1.2513 0.6323 -0.4276 -0.1473 0.1149 119 GLY A CA 905 C C . GLY A 119 ? 1.1293 1.2198 0.6125 -0.4278 -0.1059 0.0740 119 GLY A C 906 O O . GLY A 119 ? 1.1164 1.2569 0.5994 -0.4442 -0.0817 0.0486 119 GLY A O 907 N N . ILE A 120 ? 1.1176 1.1536 0.6121 -0.4102 -0.0989 0.0680 120 ILE A N 908 C CA . ILE A 120 ? 1.0917 1.1206 0.5990 -0.4066 -0.0620 0.0333 120 ILE A CA 909 C C . ILE A 120 ? 1.0893 1.0853 0.6022 -0.4030 -0.0557 0.0385 120 ILE A C 910 O O . ILE A 120 ? 1.1003 1.0671 0.6093 -0.4003 -0.0815 0.0672 120 ILE A O 911 C CB . ILE A 120 ? 1.0751 1.0759 0.5948 -0.3797 -0.0549 0.0123 120 ILE A CB 912 C CG1 . ILE A 120 ? 1.0754 1.0175 0.6030 -0.3479 -0.0798 0.0294 120 ILE A CG1 913 C CG2 . ILE A 120 ? 1.0780 1.1267 0.5924 -0.3864 -0.0562 0.0028 120 ILE A CG2 914 C CD1 . ILE A 120 ? 1.0896 1.0316 0.6136 -0.3274 -0.1102 0.0434 120 ILE A CD1 915 N N . ARG A 121 ? 1.0816 1.0821 0.6008 -0.4031 -0.0222 0.0108 121 ARG A N 916 C CA . ARG A 121 ? 1.0818 1.0544 0.6099 -0.3913 -0.0129 0.0113 121 ARG A CA 917 C C . ARG A 121 ? 1.0798 0.9924 0.6216 -0.3605 -0.0179 0.0087 121 ARG A C 918 O O . ARG A 121 ? 1.0758 0.9740 0.6205 -0.3482 -0.0225 0.0004 121 ARG A O 919 C CB . ARG A 121 ? 1.0781 1.0723 0.6058 -0.3938 0.0242 -0.0190 121 ARG A CB 920 C CG . ARG A 121 ? 1.0889 1.1447 0.6063 -0.4189 0.0298 -0.0142 121 ARG A CG 921 C CD . ARG A 121 ? 1.0900 1.1562 0.6081 -0.4081 0.0641 -0.0432 121 ARG A CD 922 N NE . ARG A 121 ? 1.0994 1.1508 0.6090 -0.4036 0.0906 -0.0804 121 ARG A NE 923 C CZ . ARG A 121 ? 1.1172 1.2101 0.6104 -0.4225 0.1076 -0.1027 121 ARG A CZ 924 N NH1 . ARG A 121 ? 1.1241 1.2851 0.6104 -0.4459 0.1022 -0.0917 121 ARG A NH1 925 N NH2 . ARG A 121 ? 1.1345 1.2007 0.6150 -0.4209 0.1300 -0.1365 121 ARG A NH2 926 N N . THR A 122 ? 1.0868 0.9730 0.6367 -0.3490 -0.0169 0.0157 122 THR A N 927 C CA . THR A 122 ? 1.0839 0.9171 0.6466 -0.3210 -0.0220 0.0143 122 THR A CA 928 C C . THR A 122 ? 1.0847 0.9035 0.6584 -0.3069 -0.0009 0.0049 122 THR A C 929 O O . THR A 122 ? 1.0755 0.8553 0.6600 -0.2854 -0.0043 0.0048 122 THR A O 930 C CB . THR A 122 ? 1.0997 0.9012 0.6574 -0.3170 -0.0602 0.0441 122 THR A CB 931 O OG1 . THR A 122 ? 1.0952 0.8525 0.6633 -0.2882 -0.0667 0.0372 122 THR A OG1 932 C CG2 . THR A 122 ? 1.1076 0.9076 0.6598 -0.3312 -0.0710 0.0672 122 THR A CG2 933 N N . ASN A 123 ? 1.1065 0.9609 0.6772 -0.3163 0.0212 -0.0043 123 ASN A N 934 C CA . ASN A 123 ? 1.1125 0.9673 0.6918 -0.3020 0.0372 -0.0073 123 ASN A CA 935 C C . ASN A 123 ? 1.0924 0.9477 0.6706 -0.2871 0.0732 -0.0390 123 ASN A C 936 O O . ASN A 123 ? 1.0916 0.9767 0.6691 -0.2816 0.0899 -0.0446 123 ASN A O 937 C CB . ASN A 123 ? 1.1588 1.0623 0.7330 -0.3231 0.0273 0.0146 123 ASN A CB 938 C CG . ASN A 123 ? 1.2260 1.1840 0.7860 -0.3509 0.0289 0.0141 123 ASN A CG 939 O OD1 . ASN A 123 ? 1.2269 1.1808 0.7791 -0.3617 0.0201 0.0127 123 ASN A OD1 940 N ND2 . ASN A 123 ? 1.3049 1.3225 0.8615 -0.3624 0.0400 0.0153 123 ASN A ND2 941 N N . GLY A 124 ? 1.0724 0.8941 0.6470 -0.2803 0.0844 -0.0596 124 GLY A N 942 C CA . GLY A 124 ? 1.0737 0.8769 0.6390 -0.2681 0.1164 -0.0898 124 GLY A CA 943 C C . GLY A 124 ? 1.0576 0.8273 0.6323 -0.2376 0.1283 -0.0915 124 GLY A C 944 O O . GLY A 124 ? 1.0407 0.7810 0.6285 -0.2259 0.1158 -0.0793 124 GLY A O 945 N N . THR A 125 ? 1.0633 0.8404 0.6301 -0.2224 0.1522 -0.1071 125 THR A N 946 C CA . THR A 125 ? 1.0560 0.8092 0.6300 -0.1892 0.1646 -0.1077 125 THR A CA 947 C C . THR A 125 ? 1.0909 0.8013 0.6435 -0.1693 0.1943 -0.1378 125 THR A C 948 O O . THR A 125 ? 1.1175 0.8112 0.6489 -0.1855 0.2043 -0.1590 125 THR A O 949 C CB . THR A 125 ? 1.0419 0.8549 0.6273 -0.1823 0.1612 -0.0916 125 THR A CB 950 O OG1 . THR A 125 ? 1.0628 0.9221 0.6344 -0.1854 0.1771 -0.1077 125 THR A OG1 951 C CG2 . THR A 125 ? 1.0126 0.8560 0.6104 -0.2073 0.1301 -0.0610 125 THR A CG2 952 N N . THR A 126 ? 1.0950 0.7853 0.6499 -0.1349 0.2072 -0.1391 126 THR A N 953 C CA . THR A 126 ? 1.1430 0.7785 0.6721 -0.1103 0.2334 -0.1656 126 THR A CA 954 C C . THR A 126 ? 1.1532 0.7881 0.6870 -0.0662 0.2452 -0.1623 126 THR A C 955 O O . THR A 126 ? 1.1121 0.7828 0.6717 -0.0566 0.2329 -0.1383 126 THR A O 956 C CB . THR A 126 ? 1.1619 0.7193 0.6765 -0.1188 0.2357 -0.1736 126 THR A CB 957 O OG1 . THR A 126 ? 1.2234 0.7139 0.7098 -0.0924 0.2582 -0.1933 126 THR A OG1 958 C CG2 . THR A 126 ? 1.1181 0.6680 0.6583 -0.1173 0.2173 -0.1487 126 THR A CG2 959 N N . SER A 127 ? 1.2117 0.8029 0.7172 -0.0389 0.2685 -0.1874 127 SER A N 960 C CA . SER A 127 ? 1.2386 0.8252 0.7425 0.0109 0.2819 -0.1879 127 SER A CA 961 C C . SER A 127 ? 1.2329 0.7652 0.7446 0.0301 0.2782 -0.1710 127 SER A C 962 O O . SER A 127 ? 1.2327 0.7858 0.7562 0.0669 0.2814 -0.1594 127 SER A O 963 C CB . SER A 127 ? 1.3204 0.8582 0.7837 0.0376 0.3068 -0.2225 127 SER A CB 964 O OG . SER A 127 ? 1.3369 0.8924 0.7829 0.0070 0.3107 -0.2442 127 SER A OG 965 N N . ALA A 128 ? 1.2292 0.7002 0.7340 0.0047 0.2717 -0.1695 128 ALA A N 966 C CA . ALA A 128 ? 1.2334 0.6478 0.7395 0.0195 0.2700 -0.1563 128 ALA A CA 967 C C . ALA A 128 ? 1.1651 0.6276 0.7108 0.0146 0.2494 -0.1264 128 ALA A C 968 O O . ALA A 128 ? 1.1645 0.5994 0.7164 0.0326 0.2480 -0.1131 128 ALA A O 969 C CB . ALA A 128 ? 1.2655 0.6017 0.7444 -0.0082 0.2723 -0.1682 128 ALA A CB 970 N N . CYS A 129 ? 1.1128 0.6422 0.6815 -0.0111 0.2325 -0.1160 129 CYS A N 971 C CA . CYS A 129 ? 1.0566 0.6289 0.6572 -0.0158 0.2119 -0.0896 129 CYS A CA 972 C C . CYS A 129 ? 1.0396 0.6888 0.6544 -0.0029 0.2109 -0.0793 129 CYS A C 973 O O . CYS A 129 ? 1.0204 0.7230 0.6401 -0.0265 0.2015 -0.0762 129 CYS A O 974 C CB . CYS A 129 ? 1.0190 0.5999 0.6297 -0.0541 0.1899 -0.0830 129 CYS A CB 975 S SG . CYS A 129 ? 1.0436 0.5578 0.6333 -0.0748 0.1939 -0.1003 129 CYS A SG 976 N N . ARG A 130 ? 1.0499 0.7083 0.6694 0.0342 0.2206 -0.0730 130 ARG A N 977 C CA . ARG A 130 ? 1.0450 0.7841 0.6748 0.0527 0.2243 -0.0659 130 ARG A CA 978 C C . ARG A 130 ? 0.9932 0.7926 0.6501 0.0382 0.2036 -0.0381 130 ARG A C 979 O O . ARG A 130 ? 0.9804 0.7654 0.6488 0.0516 0.1991 -0.0246 130 ARG A O 980 C CB . ARG A 130 ? 1.0950 0.8179 0.7125 0.1058 0.2463 -0.0748 130 ARG A CB 981 C CG . ARG A 130 ? 1.0962 0.9148 0.7250 0.1326 0.2519 -0.0684 130 ARG A CG 982 C CD . ARG A 130 ? 1.1600 0.9566 0.7694 0.1917 0.2752 -0.0837 130 ARG A CD 983 N NE . ARG A 130 ? 1.1531 1.0363 0.7807 0.2262 0.2771 -0.0680 130 ARG A NE 984 C CZ . ARG A 130 ? 1.1401 1.1355 0.7789 0.2282 0.2778 -0.0660 130 ARG A CZ 985 N NH1 . ARG A 130 ? 1.1341 1.1684 0.7678 0.1973 0.2766 -0.0780 130 ARG A NH1 986 N NH2 . ARG A 130 ? 1.1327 1.2101 0.7875 0.2595 0.2794 -0.0506 130 ARG A NH2 987 N N . ARG A 131 ? 0.9673 0.8321 0.6308 0.0076 0.1905 -0.0294 131 ARG A N 988 C CA . ARG A 131 ? 0.9335 0.8659 0.6147 -0.0084 0.1726 -0.0042 131 ARG A CA 989 C C . ARG A 131 ? 0.9397 0.9668 0.6196 -0.0116 0.1780 -0.0032 131 ARG A C 990 O O . ARG A 131 ? 0.9305 0.9943 0.6073 -0.0510 0.1638 0.0042 131 ARG A O 991 C CB . ARG A 131 ? 0.9052 0.8165 0.5899 -0.0525 0.1447 0.0097 131 ARG A CB 992 C CG . ARG A 131 ? 0.8903 0.7358 0.5818 -0.0487 0.1352 0.0134 131 ARG A CG 993 C CD . ARG A 131 ? 0.8766 0.6856 0.5644 -0.0830 0.1121 0.0166 131 ARG A CD 994 N NE . ARG A 131 ? 0.8652 0.6172 0.5586 -0.0758 0.1051 0.0155 131 ARG A NE 995 C CZ . ARG A 131 ? 0.8626 0.5669 0.5505 -0.0865 0.0973 0.0064 131 ARG A CZ 996 N NH1 . ARG A 131 ? 0.8698 0.5721 0.5464 -0.1053 0.0953 -0.0016 131 ARG A NH1 997 N NH2 . ARG A 131 ? 0.8522 0.5188 0.5463 -0.0781 0.0917 0.0053 131 ARG A NH2 998 N N . SER A 132 ? 0.9594 1.0279 0.6399 0.0312 0.1982 -0.0102 132 SER A N 999 C CA . SER A 132 ? 0.9700 1.1377 0.6482 0.0372 0.2078 -0.0147 132 SER A CA 1000 C C . SER A 132 ? 0.9797 1.1440 0.6421 0.0112 0.2097 -0.0313 132 SER A C 1001 O O . SER A 132 ? 0.9604 1.1731 0.6240 -0.0345 0.1926 -0.0176 132 SER A O 1002 C CB . SER A 132 ? 0.9427 1.2112 0.6355 0.0087 0.1905 0.0131 132 SER A CB 1003 O OG . SER A 132 ? 0.9222 1.1789 0.6134 -0.0495 0.1641 0.0299 132 SER A OG 1004 N N . GLY A 133 ? 1.0138 1.1174 0.6583 0.0386 0.2298 -0.0599 133 GLY A N 1005 C CA . GLY A 133 ? 1.0244 1.1068 0.6519 0.0126 0.2319 -0.0782 133 GLY A CA 1006 C C . GLY A 133 ? 1.0142 0.9956 0.6361 -0.0100 0.2223 -0.0800 133 GLY A C 1007 O O . GLY A 133 ? 0.9954 0.9300 0.6280 -0.0082 0.2123 -0.0659 133 GLY A O 1008 N N . SER A 134 ? 1.0250 0.9818 0.6301 -0.0318 0.2253 -0.0977 134 SER A N 1009 C CA . SER A 134 ? 1.0205 0.8939 0.6182 -0.0531 0.2181 -0.1024 134 SER A CA 1010 C C . SER A 134 ? 0.9730 0.8465 0.5884 -0.0863 0.1893 -0.0746 134 SER A C 1011 O O . SER A 134 ? 0.9498 0.8861 0.5765 -0.1061 0.1729 -0.0530 134 SER A O 1012 C CB . SER A 134 ? 1.0441 0.9119 0.6207 -0.0753 0.2252 -0.1249 134 SER A CB 1013 O OG . SER A 134 ? 1.0992 0.9391 0.6518 -0.0438 0.2519 -0.1562 134 SER A OG 1014 N N . SER A 135 ? 0.9643 0.7666 0.5786 -0.0923 0.1828 -0.0760 135 SER A N 1015 C CA . SER A 135 ? 0.9278 0.7189 0.5552 -0.1171 0.1556 -0.0547 135 SER A CA 1016 C C . SER A 135 ? 0.9277 0.6534 0.5482 -0.1252 0.1530 -0.0653 135 SER A C 1017 O O . SER A 135 ? 0.9543 0.6544 0.5570 -0.1272 0.1686 -0.0873 135 SER A O 1018 C CB . SER A 135 ? 0.9075 0.7061 0.5528 -0.1022 0.1465 -0.0348 135 SER A CB 1019 O OG . SER A 135 ? 0.8836 0.6727 0.5371 -0.1261 0.1187 -0.0160 135 SER A OG 1020 N N . PHE A 136 ? 0.9009 0.6044 0.5334 -0.1313 0.1331 -0.0509 136 PHE A N 1021 C CA . PHE A 136 ? 0.8971 0.5535 0.5257 -0.1377 0.1289 -0.0595 136 PHE A CA 1022 C C . PHE A 136 ? 0.8746 0.5112 0.5189 -0.1293 0.1124 -0.0456 136 PHE A C 1023 O O . PHE A 136 ? 0.8611 0.5173 0.5175 -0.1223 0.1031 -0.0293 136 PHE A O 1024 C CB . PHE A 136 ? 0.8927 0.5647 0.5139 -0.1668 0.1148 -0.0604 136 PHE A CB 1025 C CG . PHE A 136 ? 0.8981 0.5382 0.5107 -0.1749 0.1167 -0.0749 136 PHE A CG 1026 C CD1 . PHE A 136 ? 0.9268 0.5368 0.5220 -0.1722 0.1412 -0.0974 136 PHE A CD1 1027 C CD2 . PHE A 136 ? 0.8808 0.5218 0.4995 -0.1854 0.0935 -0.0666 136 PHE A CD2 1028 C CE1 . PHE A 136 ? 0.9355 0.5235 0.5199 -0.1863 0.1427 -0.1099 136 PHE A CE1 1029 C CE2 . PHE A 136 ? 0.8860 0.5131 0.4975 -0.1933 0.0954 -0.0799 136 PHE A CE2 1030 C CZ . PHE A 136 ? 0.9115 0.5154 0.5061 -0.1971 0.1202 -0.1010 136 PHE A CZ 1031 N N . TYR A 137 ? 0.8718 0.4755 0.5145 -0.1315 0.1090 -0.0532 137 TYR A N 1032 C CA . TYR A 137 ? 0.8520 0.4414 0.5083 -0.1233 0.0931 -0.0440 137 TYR A CA 1033 C C . TYR A 137 ? 0.8377 0.4465 0.5022 -0.1324 0.0644 -0.0262 137 TYR A C 1034 O O . TYR A 137 ? 0.8426 0.4606 0.5005 -0.1493 0.0492 -0.0238 137 TYR A O 1035 C CB . TYR A 137 ? 0.8531 0.4214 0.5046 -0.1292 0.0919 -0.0563 137 TYR A CB 1036 C CG . TYR A 137 ? 0.8766 0.4129 0.5151 -0.1245 0.1167 -0.0710 137 TYR A CG 1037 C CD1 . TYR A 137 ? 0.9063 0.4313 0.5232 -0.1381 0.1339 -0.0875 137 TYR A CD1 1038 C CD2 . TYR A 137 ? 0.8758 0.3895 0.5194 -0.1090 0.1218 -0.0680 137 TYR A CD2 1039 C CE1 . TYR A 137 ? 0.9413 0.4239 0.5383 -0.1373 0.1548 -0.1007 137 TYR A CE1 1040 C CE2 . TYR A 137 ? 0.9087 0.3843 0.5342 -0.1079 0.1423 -0.0785 137 TYR A CE2 1041 C CZ . TYR A 137 ? 0.9436 0.3991 0.5441 -0.1226 0.1582 -0.0949 137 TYR A CZ 1042 O OH . TYR A 137 ? 0.9876 0.3928 0.5626 -0.1245 0.1770 -0.1050 137 TYR A OH 1043 N N . ALA A 138 ? 0.8268 0.4384 0.5022 -0.1220 0.0562 -0.0132 138 ALA A N 1044 C CA . ALA A 138 ? 0.8251 0.4476 0.5013 -0.1341 0.0296 0.0046 138 ALA A CA 1045 C C . ALA A 138 ? 0.8298 0.4308 0.5006 -0.1410 0.0026 0.0059 138 ALA A C 1046 O O . ALA A 138 ? 0.8417 0.4435 0.5028 -0.1570 -0.0198 0.0195 138 ALA A O 1047 C CB . ALA A 138 ? 0.8169 0.4442 0.5036 -0.1228 0.0267 0.0153 138 ALA A CB 1048 N N . GLU A 139 ? 0.8255 0.4089 0.5001 -0.1287 0.0040 -0.0076 139 GLU A N 1049 C CA . GLU A 139 ? 0.8333 0.4029 0.5036 -0.1267 -0.0210 -0.0090 139 GLU A CA 1050 C C . GLU A 139 ? 0.8436 0.4247 0.5052 -0.1364 -0.0204 -0.0174 139 GLU A C 1051 O O . GLU A 139 ? 0.8508 0.4280 0.5083 -0.1309 -0.0406 -0.0190 139 GLU A O 1052 C CB . GLU A 139 ? 0.8227 0.3816 0.5031 -0.1063 -0.0222 -0.0193 139 GLU A CB 1053 C CG . GLU A 139 ? 0.8140 0.3668 0.5042 -0.0957 -0.0204 -0.0133 139 GLU A CG 1054 C CD . GLU A 139 ? 0.8289 0.3677 0.5124 -0.1006 -0.0469 0.0009 139 GLU A CD 1055 O OE1 . GLU A 139 ? 0.8483 0.3844 0.5185 -0.1179 -0.0598 0.0120 139 GLU A OE1 1056 O OE2 . GLU A 139 ? 0.8275 0.3570 0.5158 -0.0901 -0.0555 0.0014 139 GLU A OE2 1057 N N . MET A 140 ? 0.8478 0.4452 0.5051 -0.1489 0.0022 -0.0237 140 MET A N 1058 C CA . MET A 140 ? 0.8582 0.4713 0.5064 -0.1611 0.0070 -0.0346 140 MET A CA 1059 C C . MET A 140 ? 0.8722 0.5062 0.5095 -0.1818 0.0071 -0.0273 140 MET A C 1060 O O . MET A 140 ? 0.8760 0.5171 0.5132 -0.1867 0.0124 -0.0180 140 MET A O 1061 C CB . MET A 140 ? 0.8599 0.4703 0.5063 -0.1616 0.0358 -0.0537 140 MET A CB 1062 C CG . MET A 140 ? 0.8519 0.4452 0.5075 -0.1450 0.0407 -0.0591 140 MET A CG 1063 S SD . MET A 140 ? 0.8477 0.4545 0.5092 -0.1350 0.0163 -0.0625 140 MET A SD 1064 C CE . MET A 140 ? 0.8561 0.4897 0.5046 -0.1559 0.0292 -0.0794 140 MET A CE 1065 N N . LYS A 141 ? 0.8809 0.5335 0.5090 -0.1945 0.0020 -0.0317 141 LYS A N 1066 C CA . LYS A 141 ? 0.8943 0.5743 0.5108 -0.2168 0.0047 -0.0275 141 LYS A CA 1067 C C . LYS A 141 ? 0.9002 0.5997 0.5077 -0.2300 0.0258 -0.0484 141 LYS A C 1068 O O . LYS A 141 ? 0.8998 0.6068 0.5056 -0.2305 0.0215 -0.0570 141 LYS A O 1069 C CB . LYS A 141 ? 0.9082 0.5936 0.5167 -0.2246 -0.0278 -0.0068 141 LYS A CB 1070 C CG . LYS A 141 ? 0.9166 0.5845 0.5235 -0.2261 -0.0463 0.0156 141 LYS A CG 1071 C CD . LYS A 141 ? 0.9428 0.5874 0.5374 -0.2248 -0.0836 0.0348 141 LYS A CD 1072 C CE . LYS A 141 ? 0.9649 0.5943 0.5476 -0.2411 -0.1028 0.0600 141 LYS A CE 1073 N NZ . LYS A 141 ? 0.9496 0.5734 0.5439 -0.2361 -0.0898 0.0585 141 LYS A NZ 1074 N N . TRP A 142 ? 0.9098 0.6204 0.5096 -0.2407 0.0487 -0.0578 142 TRP A N 1075 C CA . TRP A 142 ? 0.9273 0.6512 0.5123 -0.2572 0.0695 -0.0797 142 TRP A CA 1076 C C . TRP A 142 ? 0.9350 0.7020 0.5108 -0.2801 0.0571 -0.0729 142 TRP A C 1077 O O . TRP A 142 ? 0.9375 0.7291 0.5089 -0.2907 0.0575 -0.0649 142 TRP A O 1078 C CB . TRP A 142 ? 0.9449 0.6564 0.5214 -0.2537 0.0989 -0.0955 142 TRP A CB 1079 C CG . TRP A 142 ? 0.9736 0.6754 0.5289 -0.2676 0.1228 -0.1230 142 TRP A CG 1080 C CD1 . TRP A 142 ? 0.9825 0.7031 0.5257 -0.2909 0.1212 -0.1335 142 TRP A CD1 1081 C CD2 . TRP A 142 ? 1.0065 0.6748 0.5455 -0.2597 0.1512 -0.1439 142 TRP A CD2 1082 N NE1 . TRP A 142 ? 1.0186 0.7169 0.5375 -0.3031 0.1469 -0.1602 142 TRP A NE1 1083 C CE2 . TRP A 142 ? 1.0375 0.6972 0.5517 -0.2826 0.1652 -0.1674 142 TRP A CE2 1084 C CE3 . TRP A 142 ? 1.0176 0.6619 0.5583 -0.2340 0.1654 -0.1450 142 TRP A CE3 1085 C CZ2 . TRP A 142 ? 1.0861 0.7013 0.5729 -0.2815 0.1920 -0.1927 142 TRP A CZ2 1086 C CZ3 . TRP A 142 ? 1.0633 0.6676 0.5793 -0.2270 0.1921 -0.1695 142 TRP A CZ3 1087 C CH2 . TRP A 142 ? 1.1003 0.6841 0.5876 -0.2511 0.2047 -0.1935 142 TRP A CH2 1088 N N . LEU A 143 ? 0.9370 0.7205 0.5094 -0.2878 0.0460 -0.0753 143 LEU A N 1089 C CA . LEU A 143 ? 0.9465 0.7739 0.5100 -0.3076 0.0314 -0.0662 143 LEU A CA 1090 C C . LEU A 143 ? 0.9625 0.8195 0.5090 -0.3333 0.0550 -0.0886 143 LEU A C 1091 O O . LEU A 143 ? 0.9692 0.8189 0.5074 -0.3400 0.0725 -0.1112 143 LEU A O 1092 C CB . LEU A 143 ? 0.9446 0.7846 0.5117 -0.2994 0.0065 -0.0575 143 LEU A CB 1093 C CG . LEU A 143 ? 0.9418 0.7525 0.5193 -0.2733 -0.0229 -0.0359 143 LEU A CG 1094 C CD1 . LEU A 143 ? 0.9518 0.7864 0.5265 -0.2646 -0.0494 -0.0270 143 LEU A CD1 1095 C CD2 . LEU A 143 ? 0.9484 0.7426 0.5237 -0.2766 -0.0364 -0.0127 143 LEU A CD2 1096 N N . LEU A 144 ? 0.9704 0.8613 0.5089 -0.3506 0.0547 -0.0821 144 LEU A N 1097 C CA . LEU A 144 ? 0.9896 0.9136 0.5099 -0.3758 0.0755 -0.1037 144 LEU A CA 1098 C C . LEU A 144 ? 0.9921 0.9735 0.5059 -0.3981 0.0563 -0.0885 144 LEU A C 1099 O O . LEU A 144 ? 0.9857 0.9731 0.5070 -0.3915 0.0268 -0.0598 144 LEU A O 1100 C CB . LEU A 144 ? 1.0011 0.9246 0.5164 -0.3745 0.0956 -0.1126 144 LEU A CB 1101 C CG . LEU A 144 ? 1.0037 0.8733 0.5233 -0.3488 0.1150 -0.1259 144 LEU A CG 1102 C CD1 . LEU A 144 ? 1.0139 0.8989 0.5307 -0.3419 0.1300 -0.1301 144 LEU A CD1 1103 C CD2 . LEU A 144 ? 1.0267 0.8595 0.5300 -0.3522 0.1372 -0.1560 144 LEU A CD2 1104 N N . SER A 145 ? 1.0086 1.0287 0.5052 -0.4242 0.0726 -0.1080 145 SER A N 1105 C CA . SER A 145 ? 1.0144 1.0974 0.5033 -0.4480 0.0571 -0.0935 145 SER A CA 1106 C C . SER A 145 ? 1.0183 1.1265 0.5047 -0.4569 0.0570 -0.0811 145 SER A C 1107 O O . SER A 145 ? 1.0218 1.1171 0.5057 -0.4516 0.0801 -0.0992 145 SER A O 1108 C CB . SER A 145 ? 1.0327 1.1540 0.5029 -0.4759 0.0748 -0.1210 145 SER A CB 1109 O OG . SER A 145 ? 1.0363 1.2213 0.5020 -0.4950 0.0546 -0.1029 145 SER A OG 1110 N N . ASN A 146 ? 1.0211 1.1675 0.5061 -0.4698 0.0300 -0.0495 146 ASN A N 1111 C CA . ASN A 146 ? 1.0281 1.2067 0.5094 -0.4838 0.0240 -0.0303 146 ASN A CA 1112 C C . ASN A 146 ? 1.0377 1.2454 0.5112 -0.4929 0.0567 -0.0598 146 ASN A C 1113 O O . ASN A 146 ? 1.0347 1.2470 0.5125 -0.4873 0.0611 -0.0538 146 ASN A O 1114 C CB . ASN A 146 ? 1.0425 1.2750 0.5125 -0.5096 -0.0021 -0.0012 146 ASN A CB 1115 C CG . ASN A 146 ? 1.0495 1.2491 0.5213 -0.4997 -0.0414 0.0414 146 ASN A CG 1116 O OD1 . ASN A 146 ? 1.0653 1.2818 0.5286 -0.5058 -0.0665 0.0631 146 ASN A OD1 1117 N ND2 . ASN A 146 ? 1.0449 1.1965 0.5246 -0.4842 -0.0478 0.0534 146 ASN A ND2 1118 N N . THR A 147 ? 1.0530 1.2833 0.5128 -0.5069 0.0788 -0.0922 147 THR A N 1119 C CA . THR A 147 ? 1.0741 1.3255 0.5207 -0.5121 0.1107 -0.1266 147 THR A CA 1120 C C . THR A 147 ? 1.0980 1.3193 0.5280 -0.5143 0.1373 -0.1691 147 THR A C 1121 O O . THR A 147 ? 1.0931 1.2948 0.5226 -0.5188 0.1304 -0.1699 147 THR A O 1122 C CB . THR A 147 ? 1.0850 1.4233 0.5204 -0.5429 0.1074 -0.1190 147 THR A CB 1123 O OG1 . THR A 147 ? 1.1082 1.4688 0.5305 -0.5417 0.1386 -0.1552 147 THR A OG1 1124 C CG2 . THR A 147 ? 1.0915 1.4743 0.5157 -0.5722 0.0964 -0.1153 147 THR A CG2 1125 N N . ASP A 148 ? 1.1290 1.3473 0.5422 -0.5114 0.1669 -0.2046 148 ASP A N 1126 C CA . ASP A 148 ? 1.1678 1.3401 0.5565 -0.5141 0.1934 -0.2473 148 ASP A CA 1127 C C . ASP A 148 ? 1.1797 1.3885 0.5522 -0.5513 0.1902 -0.2562 148 ASP A C 1128 O O . ASP A 148 ? 1.1790 1.4627 0.5450 -0.5775 0.1851 -0.2521 148 ASP A O 1129 C CB . ASP A 148 ? 1.2101 1.3792 0.5774 -0.5041 0.2230 -0.2841 148 ASP A CB 1130 C CG . ASP A 148 ? 1.2045 1.3415 0.5865 -0.4634 0.2287 -0.2784 148 ASP A CG 1131 O OD1 . ASP A 148 ? 1.1861 1.2637 0.5839 -0.4412 0.2214 -0.2637 148 ASP A OD1 1132 O OD2 . ASP A 148 ? 1.2199 1.3992 0.5979 -0.4534 0.2402 -0.2886 148 ASP A OD2 1133 N N . ASN A 149 ? 1.1886 1.3512 0.5550 -0.5549 0.1921 -0.2659 149 ASN A N 1134 C CA . ASN A 149 ? 1.2024 1.4015 0.5529 -0.5907 0.1897 -0.2754 149 ASN A CA 1135 C C . ASN A 149 ? 1.1674 1.4360 0.5380 -0.6010 0.1578 -0.2369 149 ASN A C 1136 O O . ASN A 149 ? 1.1742 1.4908 0.5337 -0.6295 0.1539 -0.2415 149 ASN A O 1137 C CB . ASN A 149 ? 1.2494 1.4782 0.5649 -0.6217 0.2131 -0.3136 149 ASN A CB 1138 C CG . ASN A 149 ? 1.3055 1.4506 0.5890 -0.6155 0.2437 -0.3573 149 ASN A CG 1139 O OD1 . ASN A 149 ? 1.3139 1.3844 0.5945 -0.6033 0.2477 -0.3616 149 ASN A OD1 1140 N ND2 . ASN A 149 ? 1.3491 1.5047 0.6050 -0.6236 0.2648 -0.3903 149 ASN A ND2 1141 N N . ALA A 150 ? 1.1371 1.4087 0.5341 -0.5777 0.1342 -0.1991 150 ALA A N 1142 C CA . ALA A 150 ? 1.1168 1.4395 0.5276 -0.5819 0.1012 -0.1606 150 ALA A CA 1143 C C . ALA A 150 ? 1.1065 1.4090 0.5275 -0.5692 0.0872 -0.1525 150 ALA A C 1144 O O . ALA A 150 ? 1.1015 1.3416 0.5279 -0.5501 0.0967 -0.1646 150 ALA A O 1145 C CB . ALA A 150 ? 1.0985 1.4191 0.5265 -0.5644 0.0795 -0.1235 150 ALA A CB 1146 N N . ALA A 151 ? 1.1048 1.4664 0.5280 -0.5789 0.0642 -0.1316 151 ALA A N 1147 C CA . ALA A 151 ? 1.0955 1.4577 0.5290 -0.5635 0.0477 -0.1221 151 ALA A CA 1148 C C . ALA A 151 ? 1.0797 1.3849 0.5354 -0.5221 0.0259 -0.0953 151 ALA A C 1149 O O . ALA A 151 ? 1.0784 1.3838 0.5407 -0.5101 0.0012 -0.0625 151 ALA A O 1150 C CB . ALA A 151 ? 1.0974 1.5437 0.5272 -0.5779 0.0262 -0.1036 151 ALA A CB 1151 N N . PHE A 152 ? 1.0759 1.3302 0.5393 -0.5037 0.0351 -0.1096 152 PHE A N 1152 C CA . PHE A 152 ? 1.0625 1.2692 0.5458 -0.4649 0.0147 -0.0887 152 PHE A CA 1153 C C . PHE A 152 ? 1.0618 1.3117 0.5511 -0.4507 -0.0118 -0.0728 152 PHE A C 1154 O O . PHE A 152 ? 1.0627 1.3407 0.5501 -0.4568 -0.0035 -0.0910 152 PHE A O 1155 C CB . PHE A 152 ? 1.0575 1.2029 0.5454 -0.4527 0.0358 -0.1113 152 PHE A CB 1156 C CG . PHE A 152 ? 1.0419 1.1358 0.5496 -0.4144 0.0184 -0.0931 152 PHE A CG 1157 C CD1 . PHE A 152 ? 1.0333 1.1394 0.5519 -0.3910 -0.0042 -0.0815 152 PHE A CD1 1158 C CD2 . PHE A 152 ? 1.0396 1.0782 0.5540 -0.4007 0.0247 -0.0889 152 PHE A CD2 1159 C CE1 . PHE A 152 ? 1.0225 1.0801 0.5564 -0.3559 -0.0201 -0.0679 152 PHE A CE1 1160 C CE2 . PHE A 152 ? 1.0263 1.0197 0.5569 -0.3688 0.0088 -0.0732 152 PHE A CE2 1161 C CZ . PHE A 152 ? 1.0193 1.0188 0.5587 -0.3470 -0.0137 -0.0636 152 PHE A CZ 1162 N N . PRO A 153 ? 1.0694 1.3245 0.5631 -0.4313 -0.0448 -0.0384 153 PRO A N 1163 C CA . PRO A 153 ? 1.0764 1.3764 0.5724 -0.4117 -0.0723 -0.0223 153 PRO A CA 1164 C C . PRO A 153 ? 1.0662 1.3463 0.5761 -0.3776 -0.0775 -0.0306 153 PRO A C 1165 O O . PRO A 153 ? 1.0584 1.2737 0.5778 -0.3622 -0.0695 -0.0374 153 PRO A O 1166 C CB . PRO A 153 ? 1.0964 1.3763 0.5883 -0.3952 -0.1065 0.0171 153 PRO A CB 1167 C CG . PRO A 153 ? 1.0919 1.3029 0.5860 -0.3970 -0.0994 0.0216 153 PRO A CG 1168 C CD . PRO A 153 ? 1.0754 1.2889 0.5694 -0.4242 -0.0595 -0.0123 153 PRO A CD 1169 N N . GLN A 154 ? 1.0685 1.4123 0.5797 -0.3659 -0.0908 -0.0301 154 GLN A N 1170 C CA . GLN A 154 ? 1.0588 1.4010 0.5831 -0.3312 -0.0984 -0.0373 154 GLN A CA 1171 C C . GLN A 154 ? 1.0696 1.3493 0.6003 -0.2834 -0.1300 -0.0121 154 GLN A C 1172 O O . GLN A 154 ? 1.0953 1.3753 0.6172 -0.2683 -0.1587 0.0156 154 GLN A O 1173 C CB . GLN A 154 ? 1.0628 1.5055 0.5860 -0.3296 -0.1058 -0.0427 154 GLN A CB 1174 C CG . GLN A 154 ? 1.0530 1.5143 0.5896 -0.2947 -0.1127 -0.0527 154 GLN A CG 1175 C CD . GLN A 154 ? 1.0353 1.4824 0.5749 -0.3195 -0.0809 -0.0825 154 GLN A CD 1176 O OE1 . GLN A 154 ? 1.0407 1.5235 0.5680 -0.3666 -0.0555 -0.1023 154 GLN A OE1 1177 N NE2 . GLN A 154 ? 1.0229 1.4159 0.5754 -0.2890 -0.0834 -0.0853 154 GLN A NE2 1178 N N . MET A 155 ? 1.0553 1.2787 0.5978 -0.2612 -0.1255 -0.0216 155 MET A N 1179 C CA . MET A 155 ? 1.0697 1.2173 0.6145 -0.2237 -0.1508 -0.0019 155 MET A CA 1180 C C . MET A 155 ? 1.0638 1.2070 0.6199 -0.1784 -0.1643 -0.0095 155 MET A C 1181 O O . MET A 155 ? 1.0355 1.2131 0.6024 -0.1821 -0.1448 -0.0335 155 MET A O 1182 C CB . MET A 155 ? 1.0613 1.1371 0.6086 -0.2408 -0.1330 -0.0040 155 MET A CB 1183 C CG . MET A 155 ? 1.0897 1.0987 0.6286 -0.2271 -0.1588 0.0246 155 MET A CG 1184 S SD . MET A 155 ? 1.0931 1.0861 0.6243 -0.2722 -0.1394 0.0310 155 MET A SD 1185 C CE . MET A 155 ? 1.1406 1.0914 0.6517 -0.2654 -0.1807 0.0734 155 MET A CE 1186 N N . THR A 156 ? 1.0927 1.1900 0.6427 -0.1372 -0.1983 0.0109 156 THR A N 1187 C CA . THR A 156 ? 1.0991 1.1929 0.6562 -0.0865 -0.2162 0.0037 156 THR A CA 1188 C C . THR A 156 ? 1.1193 1.1101 0.6711 -0.0597 -0.2352 0.0153 156 THR A C 1189 O O . THR A 156 ? 1.1648 1.1048 0.6969 -0.0433 -0.2657 0.0404 156 THR A O 1190 C CB . THR A 156 ? 1.1321 1.2850 0.6805 -0.0507 -0.2454 0.0142 156 THR A CB 1191 O OG1 . THR A 156 ? 1.1227 1.3619 0.6685 -0.0854 -0.2332 0.0141 156 THR A OG1 1192 C CG2 . THR A 156 ? 1.1268 1.3244 0.6877 -0.0067 -0.2510 -0.0056 156 THR A CG2 1193 N N . LYS A 157 ? 1.0902 1.0499 0.6565 -0.0579 -0.2180 -0.0021 157 LYS A N 1194 C CA . LYS A 157 ? 1.1055 0.9725 0.6674 -0.0394 -0.2318 0.0059 157 LYS A CA 1195 C C . LYS A 157 ? 1.1048 0.9647 0.6757 0.0059 -0.2411 -0.0110 157 LYS A C 1196 O O . LYS A 157 ? 1.0674 0.9811 0.6567 0.0048 -0.2195 -0.0340 157 LYS A O 1197 C CB . LYS A 157 ? 1.0748 0.9054 0.6444 -0.0783 -0.2036 0.0031 157 LYS A CB 1198 C CG . LYS A 157 ? 1.0961 0.8806 0.6494 -0.1058 -0.2111 0.0281 157 LYS A CG 1199 C CD . LYS A 157 ? 1.1123 0.9409 0.6522 -0.1248 -0.2187 0.0430 157 LYS A CD 1200 C CE . LYS A 157 ? 1.1382 0.9246 0.6597 -0.1521 -0.2297 0.0703 157 LYS A CE 1201 N NZ . LYS A 157 ? 1.1675 0.9915 0.6719 -0.1629 -0.2462 0.0899 157 LYS A NZ 1202 N N . SER A 158 ? 1.1495 0.9403 0.7038 0.0431 -0.2738 0.0004 158 SER A N 1203 C CA . SER A 158 ? 1.1591 0.9348 0.7176 0.0909 -0.2866 -0.0165 158 SER A CA 1204 C C . SER A 158 ? 1.1608 0.8475 0.7156 0.0913 -0.2895 -0.0157 158 SER A C 1205 O O . SER A 158 ? 1.1815 0.7997 0.7203 0.0672 -0.2969 0.0050 158 SER A O 1206 C CB . SER A 158 ? 1.2235 0.9903 0.7606 0.1451 -0.3259 -0.0094 158 SER A CB 1207 O OG . SER A 158 ? 1.2358 1.0040 0.7776 0.1951 -0.3361 -0.0312 158 SER A OG 1208 N N . TYR A 159 ? 1.1387 0.8348 0.7076 0.1172 -0.2841 -0.0382 159 TYR A N 1209 C CA . TYR A 159 ? 1.1528 0.7697 0.7151 0.1296 -0.2938 -0.0402 159 TYR A CA 1210 C C . TYR A 159 ? 1.1702 0.8002 0.7336 0.1851 -0.3096 -0.0627 159 TYR A C 1211 O O . TYR A 159 ? 1.1276 0.8388 0.7143 0.1938 -0.2914 -0.0843 159 TYR A O 1212 C CB . TYR A 159 ? 1.0977 0.7139 0.6808 0.0910 -0.2604 -0.0456 159 TYR A CB 1213 C CG . TYR A 159 ? 1.1076 0.6613 0.6880 0.1040 -0.2675 -0.0509 159 TYR A CG 1214 C CD1 . TYR A 159 ? 1.1465 0.6146 0.7042 0.0912 -0.2849 -0.0319 159 TYR A CD1 1215 C CD2 . TYR A 159 ? 1.0804 0.6663 0.6790 0.1254 -0.2570 -0.0746 159 TYR A CD2 1216 C CE1 . TYR A 159 ? 1.1600 0.5747 0.7129 0.0992 -0.2916 -0.0374 159 TYR A CE1 1217 C CE2 . TYR A 159 ? 1.0920 0.6261 0.6876 0.1359 -0.2634 -0.0802 159 TYR A CE2 1218 C CZ . TYR A 159 ? 1.1313 0.5792 0.7039 0.1228 -0.2806 -0.0622 159 TYR A CZ 1219 O OH . TYR A 159 ? 1.1447 0.5448 0.7123 0.1295 -0.2869 -0.0683 159 TYR A OH 1220 N N . LYS A 160 ? 1.2381 0.7879 0.7729 0.2214 -0.3443 -0.0581 160 LYS A N 1221 C CA . LYS A 160 ? 1.2661 0.8155 0.7974 0.2782 -0.3614 -0.0821 160 LYS A CA 1222 C C . LYS A 160 ? 1.2509 0.7514 0.7870 0.2695 -0.3533 -0.0927 160 LYS A C 1223 O O . LYS A 160 ? 1.2541 0.6862 0.7807 0.2321 -0.3508 -0.0755 160 LYS A O 1224 C CB . LYS A 160 ? 1.3639 0.8419 0.8549 0.3267 -0.4054 -0.0738 160 LYS A CB 1225 C CG . LYS A 160 ? 1.4020 0.9051 0.8888 0.3975 -0.4240 -0.1022 160 LYS A CG 1226 C CD . LYS A 160 ? 1.5150 0.9256 0.9541 0.4479 -0.4697 -0.0929 160 LYS A CD 1227 C CE . LYS A 160 ? 1.5511 1.0227 0.9886 0.5249 -0.4872 -0.1185 160 LYS A CE 1228 N NZ . LYS A 160 ? 1.5306 1.0355 0.9854 0.5533 -0.4776 -0.1543 160 LYS A NZ 1229 N N . ASN A 161 ? 1.2320 0.7779 0.7833 0.3028 -0.3487 -0.1207 161 ASN A N 1230 C CA . ASN A 161 ? 1.2222 0.7301 0.7774 0.3006 -0.3432 -0.1331 161 ASN A CA 1231 C C . ASN A 161 ? 1.3043 0.7348 0.8259 0.3529 -0.3801 -0.1452 161 ASN A C 1232 O O . ASN A 161 ? 1.3210 0.7947 0.8442 0.4054 -0.3903 -0.1711 161 ASN A O 1233 C CB . ASN A 161 ? 1.1527 0.7597 0.7439 0.2985 -0.3136 -0.1558 161 ASN A CB 1234 C CG . ASN A 161 ? 1.1367 0.7131 0.7349 0.2894 -0.3043 -0.1652 161 ASN A CG 1235 O OD1 . ASN A 161 ? 1.1708 0.6559 0.7487 0.2789 -0.3172 -0.1545 161 ASN A OD1 1236 N ND2 . ASN A 161 ? 1.0867 0.7435 0.7119 0.2903 -0.2824 -0.1840 161 ASN A ND2 1237 N N . THR A 162 ? 1.3598 0.6766 0.8483 0.3370 -0.4003 -0.1273 162 THR A N 1238 C CA . THR A 162 ? 1.4566 0.6750 0.9020 0.3802 -0.4384 -0.1364 162 THR A CA 1239 C C . THR A 162 ? 1.4564 0.6500 0.9030 0.3863 -0.4354 -0.1591 162 THR A C 1240 O O . THR A 162 ? 1.5402 0.6492 0.9488 0.4212 -0.4657 -0.1715 162 THR A O 1241 C CB . THR A 162 ? 1.5337 0.6332 0.9336 0.3552 -0.4656 -0.1046 162 THR A CB 1242 O OG1 . THR A 162 ? 1.4908 0.5731 0.9005 0.2888 -0.4452 -0.0844 162 THR A OG1 1243 C CG2 . THR A 162 ? 1.5524 0.6705 0.9438 0.3605 -0.4762 -0.0835 162 THR A CG2 1244 N N . ARG A 163 ? 1.3679 0.6315 0.8545 0.3533 -0.4002 -0.1647 163 ARG A N 1245 C CA . ARG A 163 ? 1.3619 0.6163 0.8533 0.3565 -0.3949 -0.1850 163 ARG A CA 1246 C C . ARG A 163 ? 1.3371 0.6831 0.8509 0.4037 -0.3881 -0.2196 163 ARG A C 1247 O O . ARG A 163 ? 1.3162 0.7427 0.8457 0.4272 -0.3835 -0.2261 163 ARG A O 1248 C CB . ARG A 163 ? 1.2912 0.5649 0.8091 0.2960 -0.3630 -0.1690 163 ARG A CB 1249 C CG . ARG A 163 ? 1.3314 0.5090 0.8204 0.2542 -0.3750 -0.1411 163 ARG A CG 1250 C CD . ARG A 163 ? 1.2607 0.4701 0.7770 0.1977 -0.3429 -0.1221 163 ARG A CD 1251 N NE . ARG A 163 ? 1.2220 0.4623 0.7590 0.1933 -0.3254 -0.1369 163 ARG A NE 1252 C CZ . ARG A 163 ? 1.1829 0.4292 0.7335 0.1518 -0.3053 -0.1227 163 ARG A CZ 1253 N NH1 . ARG A 163 ? 1.1770 0.4029 0.7230 0.1105 -0.2995 -0.0949 163 ARG A NH1 1254 N NH2 . ARG A 163 ? 1.1517 0.4305 0.7202 0.1529 -0.2913 -0.1363 163 ARG A NH2 1255 N N . LYS A 164 ? 1.3412 0.6818 0.8557 0.4149 -0.3875 -0.2415 164 LYS A N 1256 C CA . LYS A 164 ? 1.3304 0.7548 0.8607 0.4623 -0.3850 -0.2770 164 LYS A CA 1257 C C . LYS A 164 ? 1.2285 0.7726 0.8067 0.4339 -0.3464 -0.2809 164 LYS A C 1258 O O . LYS A 164 ? 1.2097 0.8382 0.8034 0.4653 -0.3416 -0.3081 164 LYS A O 1259 C CB . LYS A 164 ? 1.4001 0.7569 0.9011 0.4939 -0.4073 -0.3026 164 LYS A CB 1260 C CG . LYS A 164 ? 1.5197 0.7617 0.9658 0.5393 -0.4502 -0.3090 164 LYS A CG 1261 C CD . LYS A 164 ? 1.5849 0.8072 1.0081 0.5954 -0.4700 -0.3499 164 LYS A CD 1262 C CE . LYS A 164 ? 1.7214 0.8034 1.0800 0.6385 -0.5148 -0.3566 164 LYS A CE 1263 N NZ . LYS A 164 ? 1.7783 0.7272 1.0981 0.5940 -0.5282 -0.3422 164 LYS A NZ 1264 N N . SER A 165 ? 1.1661 0.7169 0.7644 0.3755 -0.3200 -0.2541 165 SER A N 1265 C CA . SER A 165 ? 1.0802 0.7294 0.7172 0.3453 -0.2844 -0.2537 165 SER A CA 1266 C C . SER A 165 ? 1.0338 0.7210 0.6860 0.3109 -0.2645 -0.2321 165 SER A C 1267 O O . SER A 165 ? 1.0552 0.6827 0.6918 0.2964 -0.2734 -0.2116 165 SER A O 1268 C CB . SER A 165 ? 1.0527 0.6757 0.6988 0.3090 -0.2681 -0.2452 165 SER A CB 1269 O OG . SER A 165 ? 1.0499 0.6062 0.6893 0.2667 -0.2628 -0.2156 165 SER A OG 1270 N N . PRO A 166 ? 0.9735 0.7595 0.6529 0.2944 -0.2381 -0.2366 166 PRO A N 1271 C CA . PRO A 166 ? 0.9397 0.7630 0.6289 0.2618 -0.2199 -0.2204 166 PRO A CA 1272 C C . PRO A 166 ? 0.9222 0.6812 0.6104 0.2140 -0.2049 -0.1930 166 PRO A C 1273 O O . PRO A 166 ? 0.9062 0.6348 0.6001 0.1933 -0.1932 -0.1863 166 PRO A O 1274 C CB . PRO A 166 ? 0.8911 0.8193 0.6038 0.2462 -0.1944 -0.2310 166 PRO A CB 1275 C CG . PRO A 166 ? 0.9021 0.8682 0.6177 0.2841 -0.2050 -0.2563 166 PRO A CG 1276 C CD . PRO A 166 ? 0.9422 0.8082 0.6406 0.3009 -0.2245 -0.2561 166 PRO A CD 1277 N N . ALA A 167 ? 0.9260 0.6715 0.6070 0.1985 -0.2056 -0.1777 167 ALA A N 1278 C CA . ALA A 167 ? 0.9103 0.6080 0.5903 0.1550 -0.1905 -0.1538 167 ALA A CA 1279 C C . ALA A 167 ? 0.8647 0.6191 0.5611 0.1182 -0.1578 -0.1501 167 ALA A C 1280 O O . ALA A 167 ? 0.8592 0.6743 0.5582 0.1176 -0.1537 -0.1565 167 ALA A O 1281 C CB . ALA A 167 ? 0.9484 0.5950 0.6073 0.1561 -0.2109 -0.1384 167 ALA A CB 1282 N N . LEU A 168 ? 0.8394 0.5728 0.5440 0.0878 -0.1353 -0.1401 168 LEU A N 1283 C CA . LEU A 168 ? 0.8106 0.5730 0.5224 0.0513 -0.1053 -0.1348 168 LEU A CA 1284 C C . LEU A 168 ? 0.8175 0.5487 0.5194 0.0285 -0.1020 -0.1198 168 LEU A C 1285 O O . LEU A 168 ? 0.8254 0.5015 0.5217 0.0205 -0.1052 -0.1054 168 LEU A O 1286 C CB . LEU A 168 ? 0.7901 0.5379 0.5111 0.0339 -0.0840 -0.1293 168 LEU A CB 1287 C CG . LEU A 168 ? 0.7764 0.5220 0.4970 -0.0027 -0.0542 -0.1204 168 LEU A CG 1288 C CD1 . LEU A 168 ? 0.7728 0.5763 0.4905 -0.0187 -0.0430 -0.1304 168 LEU A CD1 1289 C CD2 . LEU A 168 ? 0.7646 0.4949 0.4924 -0.0101 -0.0375 -0.1143 168 LEU A CD2 1290 N N . ILE A 169 ? 0.8155 0.5900 0.5143 0.0160 -0.0955 -0.1235 169 ILE A N 1291 C CA . ILE A 169 ? 0.8234 0.5809 0.5125 -0.0075 -0.0907 -0.1119 169 ILE A CA 1292 C C . ILE A 169 ? 0.8090 0.5804 0.4982 -0.0450 -0.0584 -0.1130 169 ILE A C 1293 O O . ILE A 169 ? 0.8005 0.6196 0.4916 -0.0551 -0.0458 -0.1245 169 ILE A O 1294 C CB . ILE A 169 ? 0.8403 0.6361 0.5216 0.0054 -0.1091 -0.1150 169 ILE A CB 1295 C CG1 . ILE A 169 ? 0.8686 0.6477 0.5446 0.0500 -0.1428 -0.1173 169 ILE A CG1 1296 C CG2 . ILE A 169 ? 0.8496 0.6264 0.5197 -0.0191 -0.1068 -0.1011 169 ILE A CG2 1297 C CD1 . ILE A 169 ? 0.8971 0.5958 0.5592 0.0537 -0.1618 -0.1001 169 ILE A CD1 1298 N N . VAL A 170 ? 0.8123 0.5416 0.4961 -0.0659 -0.0459 -0.1016 170 VAL A N 1299 C CA . VAL A 170 ? 0.8120 0.5389 0.4898 -0.0975 -0.0164 -0.1039 170 VAL A CA 1300 C C . VAL A 170 ? 0.8252 0.5481 0.4913 -0.1172 -0.0132 -0.0994 170 VAL A C 1301 O O . VAL A 170 ? 0.8303 0.5300 0.4949 -0.1112 -0.0272 -0.0873 170 VAL A O 1302 C CB . VAL A 170 ? 0.8077 0.4898 0.4892 -0.0998 -0.0002 -0.0967 170 VAL A CB 1303 C CG1 . VAL A 170 ? 0.8201 0.4836 0.4889 -0.1272 0.0277 -0.0984 170 VAL A CG1 1304 C CG2 . VAL A 170 ? 0.7977 0.4904 0.4892 -0.0866 0.0009 -0.1014 170 VAL A CG2 1305 N N . TRP A 171 ? 0.8353 0.5824 0.4905 -0.1441 0.0048 -0.1090 171 TRP A N 1306 C CA . TRP A 171 ? 0.8524 0.5964 0.4945 -0.1672 0.0132 -0.1077 171 TRP A CA 1307 C C . TRP A 171 ? 0.8704 0.6035 0.4965 -0.1979 0.0431 -0.1195 171 TRP A C 1308 O O . TRP A 171 ? 0.8724 0.6086 0.4954 -0.2048 0.0540 -0.1273 171 TRP A O 1309 C CB . TRP A 171 ? 0.8574 0.6509 0.4958 -0.1680 -0.0043 -0.1085 171 TRP A CB 1310 C CG . TRP A 171 ? 0.8585 0.7101 0.4934 -0.1788 -0.0001 -0.1226 171 TRP A CG 1311 C CD1 . TRP A 171 ? 0.8722 0.7561 0.4914 -0.2135 0.0159 -0.1333 171 TRP A CD1 1312 C CD2 . TRP A 171 ? 0.8502 0.7423 0.4958 -0.1576 -0.0120 -0.1287 171 TRP A CD2 1313 N NE1 . TRP A 171 ? 0.8705 0.8162 0.4898 -0.2181 0.0143 -0.1439 171 TRP A NE1 1314 C CE2 . TRP A 171 ? 0.8556 0.8112 0.4922 -0.1823 -0.0026 -0.1415 171 TRP A CE2 1315 C CE3 . TRP A 171 ? 0.8411 0.7255 0.5011 -0.1208 -0.0299 -0.1261 171 TRP A CE3 1316 C CZ2 . TRP A 171 ? 0.8501 0.8702 0.4939 -0.1708 -0.0100 -0.1505 171 TRP A CZ2 1317 C CZ3 . TRP A 171 ? 0.8358 0.7787 0.5027 -0.1060 -0.0371 -0.1371 171 TRP A CZ3 1318 C CH2 . TRP A 171 ? 0.8389 0.8536 0.4988 -0.1304 -0.0271 -0.1487 171 TRP A CH2 1319 N N . GLY A 172 ? 0.8900 0.6074 0.5027 -0.2168 0.0555 -0.1209 172 GLY A N 1320 C CA . GLY A 172 ? 0.9227 0.6137 0.5136 -0.2433 0.0833 -0.1338 172 GLY A CA 1321 C C . GLY A 172 ? 0.9466 0.6688 0.5177 -0.2751 0.0901 -0.1461 172 GLY A C 1322 O O . GLY A 172 ? 0.9356 0.7056 0.5124 -0.2753 0.0733 -0.1423 172 GLY A O 1323 N N . ILE A 173 ? 0.9877 0.6801 0.5323 -0.3023 0.1141 -0.1608 173 ILE A N 1324 C CA . ILE A 173 ? 1.0207 0.7323 0.5405 -0.3370 0.1245 -0.1754 173 ILE A CA 1325 C C . ILE A 173 ? 1.0676 0.7128 0.5600 -0.3487 0.1498 -0.1879 173 ILE A C 1326 O O . ILE A 173 ? 1.0937 0.6832 0.5731 -0.3469 0.1634 -0.1912 173 ILE A O 1327 C CB . ILE A 173 ? 1.0340 0.7910 0.5396 -0.3680 0.1253 -0.1863 173 ILE A CB 1328 C CG1 . ILE A 173 ? 0.9969 0.8332 0.5277 -0.3517 0.0993 -0.1769 173 ILE A CG1 1329 C CG2 . ILE A 173 ? 1.0765 0.8398 0.5485 -0.4108 0.1408 -0.2045 173 ILE A CG2 1330 C CD1 . ILE A 173 ? 0.9857 0.8615 0.5241 -0.3462 0.0846 -0.1703 173 ILE A CD1 1331 N N . HIS A 174 ? 1.0828 0.7342 0.5650 -0.3582 0.1554 -0.1947 174 HIS A N 1332 C CA . HIS A 174 ? 1.1333 0.7255 0.5894 -0.3614 0.1784 -0.2091 174 HIS A CA 1333 C C . HIS A 174 ? 1.1986 0.7685 0.6113 -0.4027 0.1969 -0.2339 174 HIS A C 1334 O O . HIS A 174 ? 1.2014 0.8244 0.6059 -0.4341 0.1921 -0.2410 174 HIS A O 1335 C CB . HIS A 174 ? 1.1199 0.7331 0.5855 -0.3497 0.1761 -0.2054 174 HIS A CB 1336 C CG . HIS A 174 ? 1.1647 0.7253 0.6076 -0.3423 0.1987 -0.2205 174 HIS A CG 1337 N ND1 . HIS A 174 ? 1.1881 0.7641 0.6130 -0.3561 0.2088 -0.2360 174 HIS A ND1 1338 C CD2 . HIS A 174 ? 1.1939 0.6890 0.6275 -0.3193 0.2130 -0.2235 174 HIS A CD2 1339 C CE1 . HIS A 174 ? 1.2309 0.7532 0.6364 -0.3392 0.2285 -0.2498 174 HIS A CE1 1340 N NE2 . HIS A 174 ? 1.2350 0.7059 0.6450 -0.3157 0.2311 -0.2416 174 HIS A NE2 1341 N N . HIS A 175 ? 1.2602 0.7494 0.6423 -0.4021 0.2173 -0.2468 175 HIS A N 1342 C CA . HIS A 175 ? 1.3363 0.7807 0.6674 -0.4412 0.2358 -0.2722 175 HIS A CA 1343 C C . HIS A 175 ? 1.3967 0.7800 0.7003 -0.4284 0.2549 -0.2905 175 HIS A C 1344 O O . HIS A 175 ? 1.4435 0.7447 0.7269 -0.4080 0.2676 -0.2943 175 HIS A O 1345 C CB . HIS A 175 ? 1.3739 0.7648 0.6816 -0.4570 0.2410 -0.2716 175 HIS A CB 1346 C CG . HIS A 175 ? 1.3295 0.7900 0.6595 -0.4726 0.2241 -0.2583 175 HIS A CG 1347 N ND1 . HIS A 175 ? 1.2985 0.8487 0.6394 -0.4964 0.2125 -0.2601 175 HIS A ND1 1348 C CD2 . HIS A 175 ? 1.3103 0.7710 0.6537 -0.4651 0.2167 -0.2435 175 HIS A CD2 1349 C CE1 . HIS A 175 ? 1.2641 0.8674 0.6241 -0.4997 0.1986 -0.2482 175 HIS A CE1 1350 N NE2 . HIS A 175 ? 1.2683 0.8198 0.6303 -0.4824 0.2012 -0.2388 175 HIS A NE2 1351 N N . SER A 176 ? 1.4009 0.8278 0.7023 -0.4386 0.2566 -0.3022 176 SER A N 1352 C CA . SER A 176 ? 1.4552 0.8416 0.7318 -0.4251 0.2744 -0.3229 176 SER A CA 1353 C C . SER A 176 ? 1.5612 0.8503 0.7760 -0.4457 0.2957 -0.3520 176 SER A C 1354 O O . SER A 176 ? 1.5960 0.8639 0.7818 -0.4871 0.2968 -0.3589 176 SER A O 1355 C CB . SER A 176 ? 1.4360 0.8986 0.7193 -0.4404 0.2713 -0.3306 176 SER A CB 1356 O OG . SER A 176 ? 1.3726 0.8915 0.6999 -0.4082 0.2581 -0.3082 176 SER A OG 1357 N N . VAL A 177 ? 1.6183 0.8499 0.8104 -0.4165 0.3119 -0.3693 177 VAL A N 1358 C CA . VAL A 177 ? 1.7355 0.8569 0.8623 -0.4269 0.3318 -0.3988 177 VAL A CA 1359 C C . VAL A 177 ? 1.7850 0.9135 0.8695 -0.4861 0.3378 -0.4256 177 VAL A C 1360 O O . VAL A 177 ? 1.8567 0.9160 0.8925 -0.5243 0.3438 -0.4379 177 VAL A O 1361 C CB . VAL A 177 ? 1.7856 0.8618 0.8969 -0.3785 0.3474 -0.4167 177 VAL A CB 1362 C CG1 . VAL A 177 ? 1.9175 0.8649 0.9540 -0.3852 0.3666 -0.4490 177 VAL A CG1 1363 C CG2 . VAL A 177 ? 1.7384 0.8208 0.8924 -0.3209 0.3417 -0.3896 177 VAL A CG2 1364 N N . SER A 178 ? 1.7479 0.9632 0.8494 -0.4967 0.3353 -0.4332 178 SER A N 1365 C CA . SER A 178 ? 1.7913 1.0274 0.8548 -0.5519 0.3413 -0.4597 178 SER A CA 1366 C C . SER A 178 ? 1.7136 1.0597 0.8104 -0.5894 0.3228 -0.4402 178 SER A C 1367 O O . SER A 178 ? 1.6279 1.0321 0.7775 -0.5683 0.3048 -0.4077 178 SER A O 1368 C CB . SER A 178 ? 1.8142 1.0754 0.8671 -0.5401 0.3527 -0.4850 178 SER A CB 1369 O OG . SER A 178 ? 1.8848 1.0536 0.9083 -0.4972 0.3694 -0.5044 178 SER A OG 1370 N N . THR A 179 ? 1.7497 1.1217 0.8117 -0.6441 0.3272 -0.4618 179 THR A N 1371 C CA . THR A 179 ? 1.6830 1.1759 0.7736 -0.6765 0.3111 -0.4481 179 THR A CA 1372 C C . THR A 179 ? 1.6359 1.2102 0.7550 -0.6598 0.3070 -0.4464 179 THR A C 1373 O O . THR A 179 ? 1.5633 1.2406 0.7208 -0.6650 0.2888 -0.4244 179 THR A O 1374 C CB . THR A 179 ? 1.7460 1.2444 0.7853 -0.7458 0.3180 -0.4723 179 THR A CB 1375 O OG1 . THR A 179 ? 1.8239 1.2837 0.8149 -0.7637 0.3365 -0.5096 179 THR A OG1 1376 C CG2 . THR A 179 ? 1.8047 1.2197 0.8069 -0.7716 0.3224 -0.4743 179 THR A CG2 1377 N N . ALA A 180 ? 1.6825 1.2098 0.7789 -0.6394 0.3236 -0.4700 180 ALA A N 1378 C CA . ALA A 180 ? 1.6475 1.2480 0.7670 -0.6221 0.3220 -0.4696 180 ALA A CA 1379 C C . ALA A 180 ? 1.5626 1.1957 0.7389 -0.5701 0.3076 -0.4349 180 ALA A C 1380 O O . ALA A 180 ? 1.5084 1.2272 0.7157 -0.5641 0.2963 -0.4193 180 ALA A O 1381 C CB . ALA A 180 ? 1.7371 1.2802 0.8095 -0.6167 0.3457 -0.5105 180 ALA A CB 1382 N N . GLU A 181 ? 1.5550 1.1200 0.7420 -0.5358 0.3074 -0.4219 181 GLU A N 1383 C CA . GLU A 181 ? 1.4782 1.0702 0.7160 -0.4899 0.2935 -0.3892 181 GLU A CA 1384 C C . GLU A 181 ? 1.3920 1.0556 0.6731 -0.4971 0.2670 -0.3540 181 GLU A C 1385 O O . GLU A 181 ? 1.3326 1.0477 0.6527 -0.4739 0.2511 -0.3275 181 GLU A O 1386 C CB . GLU A 181 ? 1.5040 1.0042 0.7379 -0.4505 0.3019 -0.3871 181 GLU A CB 1387 C CG . GLU A 181 ? 1.5738 1.0152 0.7764 -0.4215 0.3240 -0.4150 181 GLU A CG 1388 C CD . GLU A 181 ? 1.5450 1.0648 0.7681 -0.4040 0.3240 -0.4153 181 GLU A CD 1389 O OE1 . GLU A 181 ? 1.4787 1.0473 0.7461 -0.3759 0.3107 -0.3858 181 GLU A OE1 1390 O OE2 . GLU A 181 ? 1.5891 1.1251 0.7819 -0.4221 0.3367 -0.4450 181 GLU A OE2 1391 N N . GLN A 182 ? 1.3899 1.0573 0.6607 -0.5295 0.2619 -0.3544 182 GLN A N 1392 C CA . GLN A 182 ? 1.3200 1.0624 0.6266 -0.5352 0.2368 -0.3257 182 GLN A CA 1393 C C . GLN A 182 ? 1.2860 1.1222 0.6057 -0.5502 0.2245 -0.3178 182 GLN A C 1394 O O . GLN A 182 ? 1.2303 1.1218 0.5859 -0.5352 0.2008 -0.2877 182 GLN A O 1395 C CB . GLN A 182 ? 1.3377 1.0787 0.6270 -0.5692 0.2358 -0.3314 182 GLN A CB 1396 C CG . GLN A 182 ? 1.2795 1.1144 0.5995 -0.5768 0.2111 -0.3083 182 GLN A CG 1397 C CD . GLN A 182 ? 1.2898 1.1319 0.5995 -0.6016 0.2088 -0.3102 182 GLN A CD 1398 O OE1 . GLN A 182 ? 1.3054 1.0854 0.6105 -0.5919 0.2141 -0.3095 182 GLN A OE1 1399 N NE2 . GLN A 182 ? 1.2815 1.2081 0.5879 -0.6342 0.2000 -0.3111 182 GLN A NE2 1400 N N . THR A 183 ? 1.3238 1.1751 0.6113 -0.5799 0.2394 -0.3444 183 THR A N 1401 C CA . THR A 183 ? 1.2958 1.2401 0.5925 -0.5973 0.2286 -0.3368 183 THR A CA 1402 C C . THR A 183 ? 1.2612 1.2268 0.5825 -0.5663 0.2225 -0.3199 183 THR A C 1403 O O . THR A 183 ? 1.2139 1.2468 0.5622 -0.5633 0.2002 -0.2908 183 THR A O 1404 C CB . THR A 183 ? 1.3533 1.3166 0.6064 -0.6430 0.2464 -0.3720 183 THR A CB 1405 O OG1 . THR A 183 ? 1.4036 1.3180 0.6307 -0.6332 0.2688 -0.4003 183 THR A OG1 1406 C CG2 . THR A 183 ? 1.3951 1.3279 0.6157 -0.6799 0.2548 -0.3911 183 THR A CG2 1407 N N . LYS A 184 ? 1.7823 1.7978 0.6120 -0.7593 0.5337 -0.2503 184 LYS A N 1408 C CA . LYS A 184 ? 1.7549 1.7169 0.6302 -0.7049 0.5508 -0.2291 184 LYS A CA 1409 C C . LYS A 184 ? 1.6847 1.7062 0.6535 -0.6830 0.5571 -0.2330 184 LYS A C 1410 O O . LYS A 184 ? 1.6627 1.6881 0.6799 -0.6402 0.5777 -0.2251 184 LYS A O 1411 C CB . LYS A 184 ? 1.7962 1.6562 0.6257 -0.7063 0.5579 -0.2174 184 LYS A CB 1412 C CG . LYS A 184 ? 1.7586 1.5997 0.6484 -0.6603 0.5734 -0.2054 184 LYS A CG 1413 C CD . LYS A 184 ? 1.8135 1.5657 0.6438 -0.6469 0.5808 -0.1901 184 LYS A CD 1414 C CE . LYS A 184 ? 1.7717 1.5463 0.6694 -0.6091 0.5931 -0.1880 184 LYS A CE 1415 N NZ . LYS A 184 ? 1.8269 1.5264 0.6687 -0.5767 0.6038 -0.1687 184 LYS A NZ 1416 N N . LEU A 185 ? 1.6612 1.7213 0.6486 -0.7143 0.5451 -0.2468 185 LEU A N 1417 C CA . LEU A 185 ? 1.6007 1.7171 0.6732 -0.7018 0.5527 -0.2567 185 LEU A CA 1418 C C . LEU A 185 ? 1.5753 1.7586 0.6870 -0.6801 0.5612 -0.2601 185 LEU A C 1419 O O . LEU A 185 ? 1.5639 1.7344 0.7232 -0.6421 0.5906 -0.2559 185 LEU A O 1420 C CB . LEU A 185 ? 1.5838 1.7349 0.6612 -0.7383 0.5362 -0.2707 185 LEU A CB 1421 C CG . LEU A 185 ? 1.6122 1.7068 0.6561 -0.7394 0.5361 -0.2639 185 LEU A CG 1422 C CD1 . LEU A 185 ? 1.5880 1.7364 0.6516 -0.7616 0.5246 -0.2774 185 LEU A CD1 1423 C CD2 . LEU A 185 ? 1.6006 1.6682 0.6825 -0.6985 0.5557 -0.2575 185 LEU A CD2 1424 N N . TYR A 186 ? 1.5786 1.8311 0.6625 -0.7019 0.5414 -0.2681 186 TYR A N 1425 C CA . TYR A 186 ? 1.5587 1.8947 0.6734 -0.6731 0.5481 -0.2702 186 TYR A CA 1426 C C . TYR A 186 ? 1.5900 1.9823 0.6570 -0.6531 0.5414 -0.2651 186 TYR A C 1427 O O . TYR A 186 ? 1.5804 2.0666 0.6583 -0.6272 0.5418 -0.2672 186 TYR A O 1428 C CB . TYR A 186 ? 1.5246 1.9429 0.6659 -0.7077 0.5305 -0.2898 186 TYR A CB 1429 C CG . TYR A 186 ? 1.5026 1.8921 0.6675 -0.7435 0.5238 -0.3004 186 TYR A CG 1430 C CD1 . TYR A 186 ? 1.5319 1.8897 0.6422 -0.7896 0.5049 -0.3041 186 TYR A CD1 1431 C CD2 . TYR A 186 ? 1.4645 1.8613 0.6985 -0.7302 0.5413 -0.3087 186 TYR A CD2 1432 C CE1 . TYR A 186 ? 1.5225 1.8612 0.6438 -0.8087 0.5010 -0.3093 186 TYR A CE1 1433 C CE2 . TYR A 186 ? 1.4435 1.8399 0.6983 -0.7578 0.5328 -0.3210 186 TYR A CE2 1434 C CZ . TYR A 186 ? 1.4711 1.8414 0.6683 -0.7907 0.5113 -0.3180 186 TYR A CZ 1435 O OH . TYR A 186 ? 1.4601 1.8340 0.6673 -0.8043 0.5056 -0.3253 186 TYR A OH 1436 N N . GLY A 187 ? 1.6314 1.9766 0.6430 -0.6608 0.5366 -0.2595 187 GLY A N 1437 C CA . GLY A 187 ? 1.6655 2.0829 0.6286 -0.6483 0.5281 -0.2620 187 GLY A CA 1438 C C . GLY A 187 ? 1.6803 2.1837 0.6015 -0.7198 0.4999 -0.2938 187 GLY A C 1439 O O . GLY A 187 ? 1.6563 2.1862 0.5951 -0.7643 0.4886 -0.3096 187 GLY A O 1440 N N . SER A 188 ? 1.7251 2.2754 0.5888 -0.7353 0.4920 -0.3071 188 SER A N 1441 C CA . SER A 188 ? 1.7573 2.3851 0.5720 -0.8185 0.4740 -0.3471 188 SER A CA 1442 C C . SER A 188 ? 1.7260 2.5366 0.5685 -0.8177 0.4586 -0.3680 188 SER A C 1443 O O . SER A 188 ? 1.6928 2.5759 0.5760 -0.7391 0.4632 -0.3480 188 SER A O 1444 C CB . SER A 188 ? 1.8223 2.4534 0.5658 -0.8427 0.4751 -0.3639 188 SER A CB 1445 O OG . SER A 188 ? 1.8157 2.5743 0.5657 -0.7787 0.4719 -0.3601 188 SER A OG 1446 N N . GLY A 189 ? 1.7486 2.6272 0.5612 -0.9043 0.4461 -0.4081 189 GLY A N 1447 C CA . GLY A 189 ? 1.7238 2.7937 0.5580 -0.9155 0.4298 -0.4350 189 GLY A CA 1448 C C . GLY A 189 ? 1.6878 2.7436 0.5568 -0.9533 0.4251 -0.4398 189 GLY A C 1449 O O . GLY A 189 ? 1.6723 2.5848 0.5622 -0.9474 0.4341 -0.4157 189 GLY A O 1450 N N . ASN A 190 ? 1.6760 2.8945 0.5509 -0.9915 0.4108 -0.4733 190 ASN A N 1451 C CA . ASN A 190 ? 1.6414 2.8661 0.5489 -1.0275 0.4053 -0.4801 190 ASN A CA 1452 C C . ASN A 190 ? 1.5710 2.8030 0.5526 -0.9396 0.4061 -0.4451 190 ASN A C 1453 O O . ASN A 190 ? 1.5508 2.9013 0.5554 -0.8669 0.4049 -0.4355 190 ASN A O 1454 C CB . ASN A 190 ? 1.6578 3.0589 0.5462 -1.1035 0.3928 -0.5313 190 ASN A CB 1455 C CG . ASN A 190 ? 1.6573 3.2755 0.5439 -1.0674 0.3806 -0.5520 190 ASN A CG 1456 O OD1 . ASN A 190 ? 1.6402 3.2836 0.5455 -0.9671 0.3817 -0.5199 190 ASN A OD1 1457 N ND2 . ASN A 190 ? 1.6857 3.4679 0.5447 -1.1481 0.3727 -0.6078 190 ASN A ND2 1458 N N . LYS A 191 ? 1.5443 2.6499 0.5558 -0.9445 0.4129 -0.4277 191 LYS A N 1459 C CA . LYS A 191 ? 1.4907 2.5765 0.5691 -0.8735 0.4223 -0.4009 191 LYS A CA 1460 C C . LYS A 191 ? 1.4544 2.6304 0.5660 -0.9005 0.4104 -0.4178 191 LYS A C 1461 O O . LYS A 191 ? 1.4656 2.6364 0.5555 -0.9777 0.4003 -0.4398 191 LYS A O 1462 C CB . LYS A 191 ? 1.4832 2.3971 0.5802 -0.8610 0.4385 -0.3778 191 LYS A CB 1463 C CG . LYS A 191 ? 1.5279 2.3321 0.5775 -0.8647 0.4466 -0.3672 191 LYS A CG 1464 C CD . LYS A 191 ? 1.5442 2.3796 0.5836 -0.8009 0.4563 -0.3526 191 LYS A CD 1465 C CE . LYS A 191 ? 1.5353 2.2608 0.6081 -0.7337 0.4834 -0.3213 191 LYS A CE 1466 N NZ . LYS A 191 ? 1.5502 2.3235 0.6220 -0.6528 0.5012 -0.3026 191 LYS A NZ 1467 N N . LEU A 192 ? 1.4226 2.6717 0.5787 -0.8344 0.4170 -0.4063 192 LEU A N 1468 C CA . LEU A 192 ? 1.3877 2.7301 0.5766 -0.8506 0.4067 -0.4209 192 LEU A CA 1469 C C . LEU A 192 ? 1.3562 2.6307 0.6024 -0.7999 0.4276 -0.4021 192 LEU A C 1470 O O . LEU A 192 ? 1.3692 2.5969 0.6275 -0.7250 0.4554 -0.3787 192 LEU A O 1471 C CB . LEU A 192 ? 1.3916 2.9285 0.5695 -0.8222 0.3961 -0.4337 192 LEU A CB 1472 C CG . LEU A 192 ? 1.3577 3.0072 0.5715 -0.8111 0.3901 -0.4422 192 LEU A CG 1473 C CD1 . LEU A 192 ? 1.3400 2.9997 0.5571 -0.9104 0.3710 -0.4717 192 LEU A CD1 1474 C CD2 . LEU A 192 ? 1.3707 3.2228 0.5671 -0.7603 0.3831 -0.4494 192 LEU A CD2 1475 N N . VAL A 193 ? 1.3245 2.5927 0.6003 -0.8434 0.4190 -0.4152 193 VAL A N 1476 C CA . VAL A 193 ? 1.2946 2.5287 0.6260 -0.8079 0.4383 -0.4090 193 VAL A CA 1477 C C . VAL A 193 ? 1.2628 2.6138 0.6150 -0.8271 0.4233 -0.4265 193 VAL A C 1478 O O . VAL A 193 ? 1.2555 2.6607 0.5901 -0.8950 0.3977 -0.4462 193 VAL A O 1479 C CB . VAL A 193 ? 1.2833 2.3919 0.6395 -0.8358 0.4454 -0.4093 193 VAL A CB 1480 C CG1 . VAL A 193 ? 1.2577 2.3507 0.6735 -0.8108 0.4677 -0.4144 193 VAL A CG1 1481 C CG2 . VAL A 193 ? 1.3123 2.3104 0.6500 -0.8154 0.4612 -0.3926 193 VAL A CG2 1482 N N . THR A 194 ? 1.2535 2.6325 0.6365 -0.7667 0.4455 -0.4192 194 THR A N 1483 C CA . THR A 194 ? 1.2273 2.7183 0.6309 -0.7708 0.4355 -0.4328 194 THR A CA 1484 C C . THR A 194 ? 1.2140 2.6406 0.6653 -0.7415 0.4661 -0.4324 194 THR A C 1485 O O . THR A 194 ? 1.2385 2.5551 0.7005 -0.6998 0.5046 -0.4204 194 THR A O 1486 C CB . THR A 194 ? 1.2497 2.8875 0.6254 -0.7146 0.4342 -0.4271 194 THR A CB 1487 O OG1 . THR A 194 ? 1.2881 2.8800 0.6616 -0.6158 0.4779 -0.4009 194 THR A OG1 1488 C CG2 . THR A 194 ? 1.2713 2.9725 0.5998 -0.7347 0.4135 -0.4316 194 THR A CG2 1489 N N . VAL A 195 ? 1.1796 2.6759 0.6570 -0.7691 0.4524 -0.4496 195 VAL A N 1490 C CA . VAL A 195 ? 1.1682 2.6183 0.6907 -0.7543 0.4799 -0.4580 195 VAL A CA 1491 C C . VAL A 195 ? 1.1577 2.7255 0.6875 -0.7360 0.4755 -0.4651 195 VAL A C 1492 O O . VAL A 195 ? 1.1287 2.8100 0.6511 -0.7790 0.4376 -0.4769 195 VAL A O 1493 C CB . VAL A 195 ? 1.1311 2.5244 0.6875 -0.8198 0.4661 -0.4770 195 VAL A CB 1494 C CG1 . VAL A 195 ? 1.1195 2.4909 0.7257 -0.8129 0.4933 -0.4954 195 VAL A CG1 1495 C CG2 . VAL A 195 ? 1.1435 2.4277 0.6905 -0.8298 0.4723 -0.4690 195 VAL A CG2 1496 N N . GLY A 196 ? 1.1898 2.7228 0.7289 -0.6737 0.5202 -0.4594 196 GLY A N 1497 C CA . GLY A 196 ? 1.1974 2.8329 0.7330 -0.6356 0.5252 -0.4602 196 GLY A CA 1498 C C . GLY A 196 ? 1.2210 2.7796 0.7835 -0.6125 0.5727 -0.4706 196 GLY A C 1499 O O . GLY A 196 ? 1.2857 2.7268 0.8332 -0.5595 0.6319 -0.4601 196 GLY A O 1500 N N . SER A 197 ? 1.1756 2.7963 0.7736 -0.6568 0.5515 -0.4941 197 SER A N 1501 C CA . SER A 197 ? 1.2013 2.7811 0.8207 -0.6370 0.5940 -0.5094 197 SER A CA 1502 C C . SER A 197 ? 1.1826 2.9039 0.7995 -0.6257 0.5706 -0.5120 197 SER A C 1503 O O . SER A 197 ? 1.1396 2.9909 0.7484 -0.6524 0.5186 -0.5097 197 SER A O 1504 C CB . SER A 197 ? 1.1626 2.6751 0.8375 -0.7076 0.5951 -0.5435 197 SER A CB 1505 O OG . SER A 197 ? 1.0898 2.7008 0.7930 -0.7711 0.5401 -0.5604 197 SER A OG 1506 N N . SER A 198 ? 1.2224 2.9157 0.8433 -0.5904 0.6138 -0.5205 198 SER A N 1507 C CA . SER A 198 ? 1.2194 3.0387 0.8321 -0.5623 0.6026 -0.5201 198 SER A CA 1508 C C . SER A 198 ? 1.1311 3.1065 0.7688 -0.6313 0.5301 -0.5336 198 SER A C 1509 O O . SER A 198 ? 1.1284 3.2483 0.7449 -0.6039 0.5086 -0.5254 198 SER A O 1510 C CB . SER A 198 ? 1.2544 3.0043 0.8863 -0.5558 0.6508 -0.5425 198 SER A CB 1511 O OG . SER A 198 ? 1.3655 2.9691 0.9554 -0.4849 0.7328 -0.5302 198 SER A OG 1512 N N . ASN A 199 ? 1.0700 3.0183 0.7464 -0.7175 0.4978 -0.5546 199 ASN A N 1513 C CA . ASN A 199 ? 1.0065 3.0708 0.6951 -0.7879 0.4407 -0.5672 199 ASN A CA 1514 C C . ASN A 199 ? 0.9815 3.0106 0.6622 -0.8504 0.4094 -0.5665 199 ASN A C 1515 O O . ASN A 199 ? 0.9443 2.9959 0.6350 -0.9182 0.3785 -0.5802 199 ASN A O 1516 C CB . ASN A 199 ? 0.9723 3.0499 0.7032 -0.8261 0.4361 -0.5932 199 ASN A CB 1517 C CG . ASN A 199 ? 0.9715 2.9228 0.7385 -0.8469 0.4624 -0.6120 199 ASN A CG 1518 O OD1 . ASN A 199 ? 0.9761 2.8404 0.7414 -0.8595 0.4674 -0.6078 199 ASN A OD1 1519 N ND2 . ASN A 199 ? 0.9667 2.9195 0.7670 -0.8519 0.4804 -0.6368 199 ASN A ND2 1520 N N . TYR A 200 ? 1.0123 2.9800 0.6661 -0.8227 0.4218 -0.5484 200 TYR A N 1521 C CA . TYR A 200 ? 1.0024 2.9196 0.6407 -0.8743 0.3993 -0.5459 200 TYR A CA 1522 C C . TYR A 200 ? 1.0365 2.9756 0.6309 -0.8442 0.3982 -0.5272 200 TYR A C 1523 O O . TYR A 200 ? 1.0758 2.9858 0.6570 -0.7696 0.4305 -0.5094 200 TYR A O 1524 C CB . TYR A 200 ? 1.0005 2.7769 0.6655 -0.8836 0.4204 -0.5504 200 TYR A CB 1525 C CG . TYR A 200 ? 0.9955 2.7105 0.6404 -0.9292 0.4005 -0.5456 200 TYR A CG 1526 C CD1 . TYR A 200 ? 1.0242 2.6760 0.6410 -0.9060 0.4109 -0.5278 200 TYR A CD1 1527 C CD2 . TYR A 200 ? 0.9723 2.6863 0.6176 -0.9888 0.3756 -0.5562 200 TYR A CD2 1528 C CE1 . TYR A 200 ? 1.0289 2.6177 0.6210 -0.9442 0.3961 -0.5226 200 TYR A CE1 1529 C CE2 . TYR A 200 ? 0.9869 2.6309 0.5993 -1.0208 0.3650 -0.5478 200 TYR A CE2 1530 C CZ . TYR A 200 ? 1.0142 2.5953 0.6012 -1.0000 0.3749 -0.5319 200 TYR A CZ 1531 O OH . TYR A 200 ? 1.0356 2.5409 0.5841 -1.0290 0.3674 -0.5230 200 TYR A OH 1532 N N . GLN A 201 ? 1.0330 3.0190 0.5985 -0.9030 0.3662 -0.5328 201 GLN A N 1533 C CA . GLN A 201 ? 1.0644 3.0827 0.5872 -0.8916 0.3609 -0.5235 201 GLN A CA 1534 C C . GLN A 201 ? 1.0709 3.0280 0.5655 -0.9710 0.3425 -0.5314 201 GLN A C 1535 O O . GLN A 201 ? 1.0667 3.0716 0.5463 -1.0428 0.3229 -0.5501 201 GLN A O 1536 C CB . GLN A 201 ? 1.0710 3.2817 0.5724 -0.8817 0.3441 -0.5331 201 GLN A CB 1537 C CG . GLN A 201 ? 1.0755 3.3737 0.5912 -0.8013 0.3607 -0.5249 201 GLN A CG 1538 C CD . GLN A 201 ? 1.0888 3.5965 0.5759 -0.7714 0.3459 -0.5310 201 GLN A CD 1539 O OE1 . GLN A 201 ? 1.1077 3.6964 0.5906 -0.6867 0.3626 -0.5181 201 GLN A OE1 1540 N NE2 . GLN A 201 ? 1.0871 3.6880 0.5494 -0.8404 0.3186 -0.5534 201 GLN A NE2 1541 N N . GLN A 202 ? 1.0936 2.9369 0.5727 -0.9575 0.3542 -0.5167 202 GLN A N 1542 C CA . GLN A 202 ? 1.1171 2.8929 0.5559 -1.0239 0.3428 -0.5212 202 GLN A CA 1543 C C . GLN A 202 ? 1.1472 2.8479 0.5603 -0.9935 0.3542 -0.5047 202 GLN A C 1544 O O . GLN A 202 ? 1.1473 2.8036 0.5813 -0.9228 0.3758 -0.4865 202 GLN A O 1545 C CB . GLN A 202 ? 1.1069 2.7777 0.5575 -1.0623 0.3427 -0.5226 202 GLN A CB 1546 C CG . GLN A 202 ? 1.1396 2.8026 0.5385 -1.1446 0.3308 -0.5355 202 GLN A CG 1547 C CD . GLN A 202 ? 1.1308 2.7393 0.5403 -1.1671 0.3304 -0.5362 202 GLN A CD 1548 O OE1 . GLN A 202 ? 1.0910 2.7616 0.5462 -1.1542 0.3260 -0.5438 202 GLN A OE1 1549 N NE2 . GLN A 202 ? 1.1758 2.6707 0.5364 -1.1960 0.3371 -0.5275 202 GLN A NE2 1550 N N . SER A 203 ? 1.1831 2.8632 0.5444 -1.0492 0.3453 -0.5124 203 SER A N 1551 C CA . SER A 203 ? 1.2163 2.8337 0.5468 -1.0277 0.3537 -0.4995 203 SER A CA 1552 C C . SER A 203 ? 1.2577 2.7547 0.5389 -1.0905 0.3545 -0.5015 203 SER A C 1553 O O . SER A 203 ? 1.2815 2.7802 0.5291 -1.1617 0.3494 -0.5190 203 SER A O 1554 C CB . SER A 203 ? 1.2352 2.9987 0.5384 -1.0158 0.3459 -0.5108 203 SER A CB 1555 O OG . SER A 203 ? 1.2118 3.0874 0.5479 -0.9439 0.3494 -0.5038 203 SER A OG 1556 N N . PHE A 204 ? 1.2770 2.6618 0.5464 -1.0609 0.3665 -0.4823 204 PHE A N 1557 C CA . PHE A 204 ? 1.3266 2.5801 0.5428 -1.1046 0.3727 -0.4782 204 PHE A CA 1558 C C . PHE A 204 ? 1.3629 2.5627 0.5425 -1.0875 0.3805 -0.4684 204 PHE A C 1559 O O . PHE A 204 ? 1.3430 2.4962 0.5530 -1.0237 0.3904 -0.4475 204 PHE A O 1560 C CB . PHE A 204 ? 1.3090 2.4559 0.5539 -1.0852 0.3803 -0.4625 204 PHE A CB 1561 C CG . PHE A 204 ? 1.2649 2.4736 0.5607 -1.0841 0.3738 -0.4712 204 PHE A CG 1562 C CD1 . PHE A 204 ? 1.2827 2.5291 0.5504 -1.1415 0.3654 -0.4862 204 PHE A CD1 1563 C CD2 . PHE A 204 ? 1.2160 2.4427 0.5824 -1.0292 0.3814 -0.4673 204 PHE A CD2 1564 C CE1 . PHE A 204 ? 1.2402 2.5498 0.5547 -1.1389 0.3584 -0.4944 204 PHE A CE1 1565 C CE2 . PHE A 204 ? 1.1786 2.4637 0.5897 -1.0307 0.3773 -0.4790 204 PHE A CE2 1566 C CZ . PHE A 204 ? 1.1849 2.5167 0.5728 -1.0828 0.3625 -0.4913 204 PHE A CZ 1567 N N . VAL A 205 ? 1.4234 2.6295 0.5341 -1.1499 0.3806 -0.4873 205 VAL A N 1568 C CA . VAL A 205 ? 1.4732 2.6141 0.5343 -1.1505 0.3896 -0.4830 205 VAL A CA 1569 C C . VAL A 205 ? 1.5281 2.4925 0.5373 -1.1772 0.4057 -0.4694 205 VAL A C 1570 O O . VAL A 205 ? 1.5685 2.4927 0.5384 -1.2315 0.4128 -0.4789 205 VAL A O 1571 C CB . VAL A 205 ? 1.5236 2.7710 0.5301 -1.2143 0.3869 -0.5200 205 VAL A CB 1572 C CG1 . VAL A 205 ? 1.5715 2.7688 0.5318 -1.2078 0.3956 -0.5180 205 VAL A CG1 1573 C CG2 . VAL A 205 ? 1.4750 2.9293 0.5261 -1.1901 0.3695 -0.5371 205 VAL A CG2 1574 N N . PRO A 206 ? 1.5395 2.3976 0.5417 -1.1338 0.4152 -0.4452 206 PRO A N 1575 C CA . PRO A 206 ? 1.5967 2.2954 0.5450 -1.1442 0.4320 -0.4284 206 PRO A CA 1576 C C . PRO A 206 ? 1.7076 2.3298 0.5456 -1.2208 0.4516 -0.4451 206 PRO A C 1577 O O . PRO A 206 ? 1.7371 2.4409 0.5454 -1.2765 0.4514 -0.4771 206 PRO A O 1578 C CB . PRO A 206 ? 1.5827 2.2134 0.5506 -1.0807 0.4374 -0.4035 206 PRO A CB 1579 C CG . PRO A 206 ? 1.5553 2.2864 0.5496 -1.0571 0.4295 -0.4108 206 PRO A CG 1580 C CD . PRO A 206 ? 1.5087 2.3877 0.5459 -1.0675 0.4147 -0.4302 206 PRO A CD 1581 N N . SER A 207 ? 1.7774 2.2460 0.5501 -1.2215 0.4736 -0.4255 207 SER A N 1582 C CA . SER A 207 ? 1.9102 2.2622 0.5591 -1.2894 0.5068 -0.4371 207 SER A CA 1583 C C . SER A 207 ? 1.9853 2.1592 0.5640 -1.2519 0.5320 -0.4040 207 SER A C 1584 O O . SER A 207 ? 2.0359 2.1153 0.5691 -1.2359 0.5500 -0.3826 207 SER A O 1585 C CB . SER A 207 ? 1.9569 2.3049 0.5662 -1.3444 0.5209 -0.4507 207 SER A CB 1586 O OG . SER A 207 ? 1.9253 2.2356 0.5628 -1.2897 0.5170 -0.4204 207 SER A OG 1587 N N . PRO A 208 ? 1.9960 2.1301 0.5615 -1.2310 0.5343 -0.3980 208 PRO A N 1588 C CA . PRO A 208 ? 2.0750 2.0438 0.5677 -1.1934 0.5596 -0.3670 208 PRO A CA 1589 C C . PRO A 208 ? 2.2464 2.0518 0.5861 -1.2522 0.6090 -0.3720 208 PRO A C 1590 O O . PRO A 208 ? 2.3086 2.1305 0.5971 -1.3380 0.6263 -0.4084 208 PRO A O 1591 C CB . PRO A 208 ? 2.0425 2.0307 0.5635 -1.1659 0.5488 -0.3660 208 PRO A CB 1592 C CG . PRO A 208 ? 1.9950 2.1349 0.5589 -1.2088 0.5294 -0.4024 208 PRO A CG 1593 C CD . PRO A 208 ? 1.9323 2.1848 0.5551 -1.2261 0.5123 -0.4155 208 PRO A CD 1594 N N . GLY A 209 ? 2.3307 1.9792 0.5933 -1.2050 0.6367 -0.3371 209 GLY A N 1595 C CA . GLY A 209 ? 2.5190 1.9753 0.6177 -1.2407 0.6960 -0.3309 209 GLY A CA 1596 C C . GLY A 209 ? 2.5668 1.9140 0.6190 -1.1520 0.7134 -0.2805 209 GLY A C 1597 O O . GLY A 209 ? 2.4471 1.8960 0.6023 -1.0836 0.6775 -0.2616 209 GLY A O 1598 N N . ALA A 210 ? 2.7498 1.8952 0.6425 -1.1500 0.7722 -0.2606 210 ALA A N 1599 C CA . ALA A 210 ? 2.8125 1.8588 0.6452 -1.0495 0.7924 -0.2085 210 ALA A CA 1600 C C . ALA A 210 ? 2.8480 1.8932 0.6504 -1.0313 0.8061 -0.1932 210 ALA A C 1601 O O . ALA A 210 ? 2.9208 1.9311 0.6662 -1.1094 0.8334 -0.2167 210 ALA A O 1602 C CB . ALA A 210 ? 3.0114 1.8316 0.6716 -1.0387 0.8560 -0.1869 210 ALA A CB 1603 N N . ARG A 211 ? 2.7930 1.8927 0.6383 -0.9297 0.7869 -0.1577 211 ARG A N 1604 C CA . ARG A 211 ? 2.8296 1.9373 0.6420 -0.8911 0.7992 -0.1374 211 ARG A CA 1605 C C . ARG A 211 ? 2.9280 1.9490 0.6474 -0.7720 0.8279 -0.0845 211 ARG A C 1606 O O . ARG A 211 ? 2.9239 1.9226 0.6445 -0.7193 0.8239 -0.0681 211 ARG A O 1607 C CB . ARG A 211 ? 2.6272 1.9648 0.6194 -0.8850 0.7350 -0.1581 211 ARG A CB 1608 C CG . ARG A 211 ? 2.5570 1.9842 0.6171 -0.9870 0.7147 -0.2029 211 ARG A CG 1609 C CD . ARG A 211 ? 2.4710 1.9616 0.6105 -1.0410 0.6869 -0.2354 211 ARG A CD 1610 N NE . ARG A 211 ? 2.3377 1.9978 0.5994 -1.0950 0.6460 -0.2726 211 ARG A NE 1611 C CZ . ARG A 211 ? 2.2202 1.9977 0.5888 -1.1150 0.6094 -0.2975 211 ARG A CZ 1612 N NH1 . ARG A 211 ? 2.2073 1.9576 0.5868 -1.0898 0.6050 -0.2911 211 ARG A NH1 1613 N NH2 . ARG A 211 ? 2.1192 2.0435 0.5801 -1.1538 0.5794 -0.3265 211 ARG A NH2 1614 N N . PRO A 212 ? 3.0217 2.0011 0.6563 -0.7228 0.8581 -0.0562 212 PRO A N 1615 C CA . PRO A 212 ? 3.1262 2.0415 0.6624 -0.5943 0.8872 -0.0030 212 PRO A CA 1616 C C . PRO A 212 ? 2.9507 2.0702 0.6375 -0.5119 0.8269 -0.0015 212 PRO A C 1617 O O . PRO A 212 ? 2.7593 2.0798 0.6181 -0.5386 0.7683 -0.0356 212 PRO A O 1618 C CB . PRO A 212 ? 3.2246 2.1112 0.6745 -0.5620 0.9194 0.0193 212 PRO A CB 1619 C CG . PRO A 212 ? 3.2465 2.0856 0.6856 -0.6905 0.9344 -0.0179 212 PRO A CG 1620 C CD . PRO A 212 ? 3.0491 2.0378 0.6633 -0.7764 0.8709 -0.0697 212 PRO A CD 1621 N N . GLN A 213 ? 3.0247 2.0907 0.6422 -0.4150 0.8463 0.0351 213 GLN A N 1622 C CA . GLN A 213 ? 2.8751 2.1356 0.6267 -0.3416 0.7969 0.0315 213 GLN A CA 1623 C C . GLN A 213 ? 2.8120 2.2528 0.6210 -0.2710 0.7740 0.0346 213 GLN A C 1624 O O . GLN A 213 ? 2.9332 2.3481 0.6299 -0.1636 0.8056 0.0765 213 GLN A O 1625 C CB . GLN A 213 ? 2.9783 2.1430 0.6351 -0.2552 0.8257 0.0686 213 GLN A CB 1626 C CG . GLN A 213 ? 2.9671 2.0363 0.6350 -0.3219 0.8256 0.0526 213 GLN A CG 1627 C CD . GLN A 213 ? 3.0482 2.0451 0.6418 -0.2352 0.8478 0.0864 213 GLN A CD 1628 O OE1 . GLN A 213 ? 3.1000 2.1427 0.6459 -0.1191 0.8588 0.1204 213 GLN A OE1 1629 N NE2 . GLN A 213 ? 3.0606 1.9563 0.6432 -0.2873 0.8540 0.0761 213 GLN A NE2 1630 N N . VAL A 214 ? 2.6310 2.2549 0.6086 -0.3296 0.7222 -0.0103 214 VAL A N 1631 C CA . VAL A 214 ? 2.5374 2.3708 0.6047 -0.2764 0.6918 -0.0221 214 VAL A CA 1632 C C . VAL A 214 ? 2.3877 2.4112 0.6047 -0.2469 0.6512 -0.0501 214 VAL A C 1633 O O . VAL A 214 ? 2.2855 2.3239 0.6027 -0.3116 0.6289 -0.0794 214 VAL A O 1634 C CB . VAL A 214 ? 2.4348 2.3554 0.5972 -0.3606 0.6643 -0.0590 214 VAL A CB 1635 C CG1 . VAL A 214 ? 2.3328 2.4810 0.5962 -0.3104 0.6323 -0.0782 214 VAL A CG1 1636 C CG2 . VAL A 214 ? 2.5882 2.3251 0.6030 -0.3997 0.7092 -0.0367 214 VAL A CG2 1637 N N . ASN A 215 ? 2.3844 2.5562 0.6105 -0.1481 0.6460 -0.0426 215 ASN A N 1638 C CA . ASN A 215 ? 2.2757 2.6236 0.6189 -0.1123 0.6197 -0.0692 215 ASN A CA 1639 C C . ASN A 215 ? 2.3172 2.5392 0.6213 -0.1085 0.6347 -0.0519 215 ASN A C 1640 O O . ASN A 215 ? 2.2041 2.5327 0.6288 -0.1266 0.6121 -0.0843 215 ASN A O 1641 C CB . ASN A 215 ? 2.0790 2.6130 0.6240 -0.1936 0.5761 -0.1352 215 ASN A CB 1642 C CG . ASN A 215 ? 2.0259 2.7210 0.6252 -0.1889 0.5588 -0.1592 215 ASN A CG 1643 O OD1 . ASN A 215 ? 2.0947 2.8674 0.6274 -0.0980 0.5683 -0.1385 215 ASN A OD1 1644 N ND2 . ASN A 215 ? 1.9078 2.6604 0.6252 -0.2805 0.5345 -0.2025 215 ASN A ND2 1645 N N . GLY A 216 ? 2.4898 2.4787 0.6197 -0.0873 0.6781 -0.0026 216 GLY A N 1646 C CA . GLY A 216 ? 2.5459 2.3881 0.6226 -0.0926 0.6964 0.0143 216 GLY A CA 1647 C C . GLY A 216 ? 2.4672 2.2368 0.6171 -0.2122 0.6806 -0.0164 216 GLY A C 1648 O O . GLY A 216 ? 2.4955 2.1624 0.6179 -0.2235 0.6910 -0.0085 216 GLY A O 1649 N N . LEU A 217 ? 2.3754 2.2033 0.6121 -0.2951 0.6567 -0.0500 217 LEU A N 1650 C CA . LEU A 217 ? 2.2878 2.0917 0.6075 -0.3983 0.6375 -0.0822 217 LEU A CA 1651 C C . LEU A 217 ? 2.3531 2.0445 0.6039 -0.4745 0.6522 -0.0842 217 LEU A C 1652 O O . LEU A 217 ? 2.3867 2.0965 0.6036 -0.4690 0.6587 -0.0795 217 LEU A O 1653 C CB . LEU A 217 ? 2.0997 2.1080 0.6100 -0.4294 0.5948 -0.1293 217 LEU A CB 1654 C CG . LEU A 217 ? 2.0296 2.1744 0.6245 -0.3712 0.5839 -0.1413 217 LEU A CG 1655 C CD1 . LEU A 217 ? 1.8696 2.1989 0.6381 -0.4135 0.5549 -0.1939 217 LEU A CD1 1656 C CD2 . LEU A 217 ? 2.0570 2.1061 0.6273 -0.3636 0.5953 -0.1278 217 LEU A CD2 1657 N N . SER A 218 ? 1.0991 0.5544 0.5507 -0.5216 0.3736 -0.2538 218 SER A N 1658 C CA . SER A 218 ? 1.1046 0.5690 0.5465 -0.5327 0.3519 -0.2529 218 SER A CA 1659 C C . SER A 218 ? 1.0988 0.5867 0.5234 -0.5368 0.3098 -0.2390 218 SER A C 1660 O O . SER A 218 ? 1.1004 0.6024 0.5190 -0.5467 0.2882 -0.2386 218 SER A O 1661 C CB . SER A 218 ? 1.1709 0.5951 0.5629 -0.5634 0.3716 -0.2718 218 SER A CB 1662 O OG . SER A 218 ? 1.1748 0.5818 0.5919 -0.5565 0.4039 -0.2846 218 SER A OG 1663 N N . GLY A 219 ? 1.0954 0.5863 0.5119 -0.5298 0.2981 -0.2284 219 GLY A N 1664 C CA . GLY A 219 ? 1.0876 0.6023 0.4980 -0.5256 0.2557 -0.2133 219 GLY A CA 1665 C C . GLY A 219 ? 1.0177 0.5790 0.4940 -0.4939 0.2388 -0.2011 219 GLY A C 1666 O O . GLY A 219 ? 0.9797 0.5506 0.5007 -0.4753 0.2601 -0.2018 219 GLY A O 1667 N N . ARG A 220 ? 1.0055 0.5956 0.4881 -0.4878 0.2001 -0.1907 220 ARG A N 1668 C CA . ARG A 220 ? 0.9438 0.5789 0.4854 -0.4588 0.1825 -0.1801 220 ARG A CA 1669 C C . ARG A 220 ? 0.9442 0.5913 0.4785 -0.4490 0.1463 -0.1672 220 ARG A C 1670 O O . ARG A 220 ? 0.9898 0.6207 0.4777 -0.4657 0.1241 -0.1662 220 ARG A O 1671 C CB . ARG A 220 ? 0.9231 0.5921 0.4951 -0.4590 0.1719 -0.1844 220 ARG A CB 1672 C CG . ARG A 220 ? 0.9270 0.5823 0.5065 -0.4682 0.2039 -0.1959 220 ARG A CG 1673 C CD . ARG A 220 ? 0.8816 0.5448 0.5083 -0.4442 0.2256 -0.1922 220 ARG A CD 1674 N NE . ARG A 220 ? 0.8917 0.5374 0.5238 -0.4517 0.2527 -0.2022 220 ARG A NE 1675 C CZ . ARG A 220 ? 0.9305 0.5349 0.5395 -0.4619 0.2832 -0.2127 220 ARG A CZ 1676 N NH1 . ARG A 220 ? 0.9619 0.5398 0.5399 -0.4683 0.2938 -0.2157 220 ARG A NH1 1677 N NH2 . ARG A 220 ? 0.9403 0.5281 0.5564 -0.4666 0.3042 -0.2212 220 ARG A NH2 1678 N N . ILE A 221 ? 0.8950 0.5685 0.4739 -0.4218 0.1390 -0.1575 221 ILE A N 1679 C CA . ILE A 221 ? 0.8903 0.5794 0.4722 -0.4077 0.1025 -0.1458 221 ILE A CA 1680 C C . ILE A 221 ? 0.8394 0.5820 0.4795 -0.3866 0.0829 -0.1442 221 ILE A C 1681 O O . ILE A 221 ? 0.7917 0.5560 0.4776 -0.3699 0.0990 -0.1438 221 ILE A O 1682 C CB . ILE A 221 ? 0.8865 0.5563 0.4640 -0.3961 0.1094 -0.1366 221 ILE A CB 1683 C CG1 . ILE A 221 ? 0.9507 0.5685 0.4622 -0.4215 0.1231 -0.1387 221 ILE A CG1 1684 C CG2 . ILE A 221 ? 0.8731 0.5606 0.4634 -0.3764 0.0726 -0.1245 221 ILE A CG2 1685 C CD1 . ILE A 221 ? 0.9525 0.5487 0.4573 -0.4165 0.1390 -0.1331 221 ILE A CD1 1686 N N . ASP A 222 ? 0.8525 0.6168 0.4903 -0.3886 0.0484 -0.1444 222 ASP A N 1687 C CA . ASP A 222 ? 0.8092 0.6269 0.5016 -0.3677 0.0257 -0.1439 222 ASP A CA 1688 C C . ASP A 222 ? 0.7859 0.6087 0.4974 -0.3416 0.0113 -0.1326 222 ASP A C 1689 O O . ASP A 222 ? 0.8198 0.6069 0.4923 -0.3436 0.0023 -0.1246 222 ASP A O 1690 C CB . ASP A 222 ? 0.8372 0.6772 0.5227 -0.3759 -0.0104 -0.1483 222 ASP A CB 1691 C CG . ASP A 222 ? 0.8415 0.7016 0.5350 -0.3957 -0.0006 -0.1615 222 ASP A CG 1692 O OD1 . ASP A 222 ? 0.8710 0.6967 0.5301 -0.4178 0.0259 -0.1668 222 ASP A OD1 1693 O OD2 . ASP A 222 ? 0.8194 0.7290 0.5527 -0.3905 -0.0190 -0.1679 222 ASP A OD2 1694 N N . PHE A 223 ? 0.7326 0.5963 0.4999 -0.3193 0.0103 -0.1325 223 PHE A N 1695 C CA . PHE A 223 ? 0.7110 0.5854 0.5007 -0.2936 -0.0081 -0.1239 223 PHE A CA 1696 C C . PHE A 223 ? 0.6859 0.6141 0.5226 -0.2771 -0.0356 -0.1291 223 PHE A C 1697 O O . PHE A 223 ? 0.6599 0.6251 0.5311 -0.2793 -0.0259 -0.1383 223 PHE A O 1698 C CB . PHE A 223 ? 0.6716 0.5418 0.4844 -0.2806 0.0196 -0.1196 223 PHE A CB 1699 C CG . PHE A 223 ? 0.6970 0.5182 0.4700 -0.2913 0.0414 -0.1145 223 PHE A CG 1700 C CD1 . PHE A 223 ? 0.7295 0.5187 0.4665 -0.2915 0.0261 -0.1060 223 PHE A CD1 1701 C CD2 . PHE A 223 ? 0.6927 0.4994 0.4648 -0.3014 0.0775 -0.1190 223 PHE A CD2 1702 C CE1 . PHE A 223 ? 0.7562 0.5030 0.4571 -0.3041 0.0486 -0.1031 223 PHE A CE1 1703 C CE2 . PHE A 223 ? 0.7162 0.4831 0.4573 -0.3111 0.0992 -0.1173 223 PHE A CE2 1704 C CZ . PHE A 223 ? 0.7476 0.4862 0.4531 -0.3137 0.0860 -0.1098 223 PHE A CZ 1705 N N . HIS A 224 ? 0.7024 0.6324 0.5388 -0.2611 -0.0691 -0.1237 224 HIS A N 1706 C CA . HIS A 224 ? 0.6888 0.6678 0.5678 -0.2436 -0.1010 -0.1301 224 HIS A CA 1707 C C . HIS A 224 ? 0.6696 0.6541 0.5735 -0.2146 -0.1159 -0.1241 224 HIS A C 1708 O O . HIS A 224 ? 0.6853 0.6260 0.5570 -0.2115 -0.1145 -0.1126 224 HIS A O 1709 C CB . HIS A 224 ? 0.7431 0.7129 0.5913 -0.2518 -0.1373 -0.1303 224 HIS A CB 1710 C CG . HIS A 224 ? 0.7530 0.7532 0.6089 -0.2707 -0.1398 -0.1429 224 HIS A CG 1711 N ND1 . HIS A 224 ? 0.7990 0.7667 0.6032 -0.2991 -0.1360 -0.1434 224 HIS A ND1 1712 C CD2 . HIS A 224 ? 0.7256 0.7862 0.6341 -0.2670 -0.1456 -0.1566 224 HIS A CD2 1713 C CE1 . HIS A 224 ? 0.7992 0.8054 0.6239 -0.3119 -0.1403 -0.1564 224 HIS A CE1 1714 N NE2 . HIS A 224 ? 0.7535 0.8173 0.6422 -0.2934 -0.1455 -0.1647 224 HIS A NE2 1715 N N . TRP A 225 ? 0.6373 0.6742 0.5962 -0.1948 -0.1307 -0.1329 225 TRP A N 1716 C CA . TRP A 225 ? 0.6208 0.6643 0.6058 -0.1665 -0.1446 -0.1296 225 TRP A CA 1717 C C . TRP A 225 ? 0.6108 0.7086 0.6486 -0.1447 -0.1737 -0.1417 225 TRP A C 1718 O O . TRP A 225 ? 0.5937 0.7405 0.6657 -0.1506 -0.1728 -0.1556 225 TRP A O 1719 C CB . TRP A 225 ? 0.5729 0.6195 0.5785 -0.1611 -0.1105 -0.1277 225 TRP A CB 1720 C CG . TRP A 225 ? 0.5291 0.6250 0.5780 -0.1647 -0.0904 -0.1398 225 TRP A CG 1721 C CD1 . TRP A 225 ? 0.5226 0.6201 0.5636 -0.1870 -0.0647 -0.1434 225 TRP A CD1 1722 C CD2 . TRP A 225 ? 0.4916 0.6399 0.5955 -0.1470 -0.0941 -0.1507 225 TRP A CD2 1723 N NE1 . TRP A 225 ? 0.4854 0.6307 0.5701 -0.1856 -0.0526 -0.1543 225 TRP A NE1 1724 C CE2 . TRP A 225 ? 0.4655 0.6444 0.5895 -0.1620 -0.0693 -0.1596 225 TRP A CE2 1725 C CE3 . TRP A 225 ? 0.4816 0.6517 0.6180 -0.1206 -0.1149 -0.1546 225 TRP A CE3 1726 C CZ2 . TRP A 225 ? 0.4337 0.6649 0.6067 -0.1537 -0.0636 -0.1720 225 TRP A CZ2 1727 C CZ3 . TRP A 225 ? 0.4467 0.6715 0.6355 -0.1107 -0.1086 -0.1687 225 TRP A CZ3 1728 C CH2 . TRP A 225 ? 0.4234 0.6788 0.6290 -0.1284 -0.0827 -0.1771 225 TRP A CH2 1729 N N . LEU A 226 ? 0.6276 0.7158 0.6725 -0.1199 -0.1986 -0.1374 226 LEU A N 1730 C CA . LEU A 226 ? 0.6131 0.7521 0.7157 -0.0933 -0.2219 -0.1504 226 LEU A CA 1731 C C . LEU A 226 ? 0.6065 0.7291 0.7194 -0.0680 -0.2259 -0.1452 226 LEU A C 1732 O O . LEU A 226 ? 0.6223 0.6890 0.6913 -0.0706 -0.2212 -0.1298 226 LEU A O 1733 C CB . LEU A 226 ? 0.6540 0.8039 0.7582 -0.0864 -0.2661 -0.1549 226 LEU A CB 1734 C CG . LEU A 226 ? 0.7131 0.8118 0.7777 -0.0728 -0.3059 -0.1418 226 LEU A CG 1735 C CD1 . LEU A 226 ? 0.7547 0.7806 0.7413 -0.0963 -0.2960 -0.1229 226 LEU A CD1 1736 C CD2 . LEU A 226 ? 0.7092 0.8021 0.7973 -0.0407 -0.3206 -0.1408 226 LEU A CD2 1737 N N . MET A 227 ? 0.5829 0.7552 0.7539 -0.0450 -0.2341 -0.1596 227 MET A N 1738 C CA . MET A 227 ? 0.5818 0.7430 0.7674 -0.0189 -0.2413 -0.1581 227 MET A CA 1739 C C . MET A 227 ? 0.6254 0.7768 0.8144 0.0049 -0.2878 -0.1590 227 MET A C 1740 O O . MET A 227 ? 0.6194 0.8220 0.8565 0.0196 -0.3090 -0.1757 227 MET A O 1741 C CB . MET A 227 ? 0.5335 0.7522 0.7790 -0.0074 -0.2214 -0.1750 227 MET A CB 1742 C CG . MET A 227 ? 0.4980 0.7216 0.7398 -0.0274 -0.1780 -0.1726 227 MET A CG 1743 S SD . MET A 227 ? 0.5043 0.6670 0.7051 -0.0287 -0.1579 -0.1535 227 MET A SD 1744 C CE . MET A 227 ? 0.4732 0.6433 0.6662 -0.0565 -0.1149 -0.1512 227 MET A CE 1745 N N . LEU A 228 ? 0.6734 0.7584 0.8112 0.0082 -0.3039 -0.1415 228 LEU A N 1746 C CA . LEU A 228 ? 0.7286 0.7901 0.8595 0.0312 -0.3504 -0.1389 228 LEU A CA 1747 C C . LEU A 228 ? 0.7232 0.7927 0.8919 0.0628 -0.3580 -0.1463 228 LEU A C 1748 O O . LEU A 228 ? 0.7165 0.7515 0.8655 0.0626 -0.3392 -0.1375 228 LEU A O 1749 C CB . LEU A 228 ? 0.7881 0.7679 0.8391 0.0172 -0.3640 -0.1160 228 LEU A CB 1750 C CG . LEU A 228 ? 0.8537 0.7977 0.8834 0.0366 -0.4163 -0.1096 228 LEU A CG 1751 C CD1 . LEU A 228 ? 0.8647 0.8558 0.9255 0.0418 -0.4471 -0.1219 228 LEU A CD1 1752 C CD2 . LEU A 228 ? 0.9162 0.7742 0.8581 0.0167 -0.4233 -0.0859 228 LEU A CD2 1753 N N . ASN A 229 ? 0.7306 0.8463 0.9545 0.0894 -0.3858 -0.1639 229 ASN A N 1754 C CA . ASN A 229 ? 0.7270 0.8575 0.9942 0.1210 -0.3929 -0.1757 229 ASN A CA 1755 C C . ASN A 229 ? 0.7922 0.8486 1.0170 0.1382 -0.4210 -0.1601 229 ASN A C 1756 O O . ASN A 229 ? 0.8420 0.8428 1.0108 0.1305 -0.4466 -0.1427 229 ASN A O 1757 C CB . ASN A 229 ? 0.7166 0.9186 1.0575 0.1456 -0.4163 -0.2012 229 ASN A CB 1758 C CG . ASN A 229 ? 0.6542 0.9355 1.0501 0.1337 -0.3814 -0.2219 229 ASN A CG 1759 O OD1 . ASN A 229 ? 0.6170 0.9028 1.0105 0.1197 -0.3415 -0.2210 229 ASN A OD1 1760 N ND2 . ASN A 229 ? 0.6508 0.9947 1.0962 0.1387 -0.3976 -0.2410 229 ASN A ND2 1761 N N . PRO A 230 ? 0.7983 0.8510 1.0460 0.1596 -0.4157 -0.1666 230 PRO A N 1762 C CA . PRO A 230 ? 0.8666 0.8521 1.0816 0.1793 -0.4441 -0.1554 230 PRO A CA 1763 C C . PRO A 230 ? 0.9449 0.9171 1.1629 0.2035 -0.4987 -0.1564 230 PRO A C 1764 O O . PRO A 230 ? 0.9251 0.9606 1.2072 0.2242 -0.5154 -0.1777 230 PRO A O 1765 C CB . PRO A 230 ? 0.8287 0.8407 1.0921 0.2013 -0.4287 -0.1721 230 PRO A CB 1766 C CG . PRO A 230 ? 0.7569 0.8199 1.0439 0.1796 -0.3808 -0.1800 230 PRO A CG 1767 C CD . PRO A 230 ? 0.7392 0.8452 1.0372 0.1620 -0.3791 -0.1837 230 PRO A CD 1768 N N . ASN A 231 ? 1.0438 0.9340 1.1920 0.1997 -0.5258 -0.1336 231 ASN A N 1769 C CA . ASN A 231 ? 1.1436 1.0055 1.2777 0.2189 -0.5816 -0.1288 231 ASN A CA 1770 C C . ASN A 231 ? 1.1257 1.0231 1.2637 0.2058 -0.5975 -0.1307 231 ASN A C 1771 O O . ASN A 231 ? 1.1776 1.0598 1.3097 0.2223 -0.6462 -0.1283 231 ASN A O 1772 C CB . ASN A 231 ? 1.2056 1.0907 1.4017 0.2648 -0.6139 -0.1479 231 ASN A CB 1773 C CG . ASN A 231 ? 1.3031 1.1268 1.4759 0.2803 -0.6147 -0.1412 231 ASN A CG 1774 O OD1 . ASN A 231 ? 1.3357 1.0828 1.4337 0.2594 -0.6071 -0.1177 231 ASN A OD1 1775 N ND2 . ASN A 231 ? 1.3869 1.2445 1.6242 0.3161 -0.6231 -0.1633 231 ASN A ND2 1776 N N . ASP A 232 ? 1.0512 0.9924 1.1968 0.1761 -0.5585 -0.1348 232 ASP A N 1777 C CA . ASP A 232 ? 1.0455 1.0137 1.1859 0.1579 -0.5698 -0.1356 232 ASP A CA 1778 C C . ASP A 232 ? 1.0838 0.9757 1.1294 0.1244 -0.5682 -0.1089 232 ASP A C 1779 O O . ASP A 232 ? 1.0852 0.9229 1.0812 0.1086 -0.5424 -0.0938 232 ASP A O 1780 C CB . ASP A 232 ? 0.9646 1.0167 1.1601 0.1421 -0.5298 -0.1547 232 ASP A CB 1781 C CG . ASP A 232 ? 0.9687 1.0684 1.1844 0.1330 -0.5493 -0.1641 232 ASP A CG 1782 O OD1 . ASP A 232 ? 1.0262 1.0921 1.2079 0.1363 -0.5930 -0.1541 232 ASP A OD1 1783 O OD2 . ASP A 232 ? 0.9122 1.0821 1.1758 0.1210 -0.5214 -0.1815 232 ASP A OD2 1784 N N . THR A 233 ? 1.1105 0.9994 1.1317 0.1131 -0.5963 -0.1046 233 THR A N 1785 C CA . THR A 233 ? 1.1548 0.9744 1.0847 0.0795 -0.5968 -0.0819 233 THR A CA 1786 C C . THR A 233 ? 1.1193 0.9831 1.0531 0.0491 -0.5743 -0.0889 233 THR A C 1787 O O . THR A 233 ? 1.0864 1.0246 1.0846 0.0582 -0.5817 -0.1084 233 THR A O 1788 C CB . THR A 233 ? 1.2474 1.0062 1.1272 0.0912 -0.6568 -0.0670 233 THR A CB 1789 O OG1 . THR A 233 ? 1.2737 0.9999 1.1635 0.1255 -0.6821 -0.0646 233 THR A OG1 1790 C CG2 . THR A 233 ? 1.3094 0.9838 1.0839 0.0546 -0.6534 -0.0421 233 THR A CG2 1791 N N . VAL A 234 ? 1.1246 0.9429 0.9908 0.0124 -0.5452 -0.0744 234 VAL A N 1792 C CA . VAL A 234 ? 1.0954 0.9433 0.9547 -0.0194 -0.5209 -0.0798 234 VAL A CA 1793 C C . VAL A 234 ? 1.1658 0.9436 0.9325 -0.0491 -0.5345 -0.0613 234 VAL A C 1794 O O . VAL A 234 ? 1.2028 0.9072 0.9029 -0.0604 -0.5287 -0.0433 234 VAL A O 1795 C CB . VAL A 234 ? 1.0254 0.8981 0.9031 -0.0374 -0.4600 -0.0855 234 VAL A CB 1796 C CG1 . VAL A 234 ? 1.0428 0.8453 0.8573 -0.0546 -0.4327 -0.0677 234 VAL A CG1 1797 C CG2 . VAL A 234 ? 1.0018 0.9120 0.8839 -0.0656 -0.4378 -0.0945 234 VAL A CG2 1798 N N . THR A 235 ? 1.1775 0.9791 0.9396 -0.0637 -0.5513 -0.0668 235 THR A N 1799 C CA . THR A 235 ? 1.2515 0.9907 0.9260 -0.0920 -0.5696 -0.0514 235 THR A CA 1800 C C . THR A 235 ? 1.2294 0.9803 0.8812 -0.1309 -0.5309 -0.0564 235 THR A C 1801 O O . THR A 235 ? 1.1681 0.9887 0.8788 -0.1329 -0.5137 -0.0743 235 THR A O 1802 C CB . THR A 235 ? 1.3112 1.0567 0.9869 -0.0768 -0.6329 -0.0518 235 THR A CB 1803 O OG1 . THR A 235 ? 1.3341 1.0649 1.0314 -0.0380 -0.6716 -0.0478 235 THR A OG1 1804 C CG2 . THR A 235 ? 1.4012 1.0758 0.9771 -0.1083 -0.6540 -0.0345 235 THR A CG2 1805 N N . PHE A 236 ? 1.2797 0.9599 0.8439 -0.1626 -0.5175 -0.0412 236 PHE A N 1806 C CA . PHE A 236 ? 1.2777 0.9561 0.8087 -0.2009 -0.4821 -0.0453 236 PHE A CA 1807 C C . PHE A 236 ? 1.3673 0.9935 0.8153 -0.2269 -0.5128 -0.0351 236 PHE A C 1808 O O . PHE A 236 ? 1.4370 0.9861 0.8040 -0.2424 -0.5174 -0.0179 236 PHE A O 1809 C CB . PHE A 236 ? 1.2560 0.9002 0.7591 -0.2191 -0.4276 -0.0401 236 PHE A CB 1810 C CG . PHE A 236 ? 1.1674 0.8621 0.7460 -0.1994 -0.3933 -0.0502 236 PHE A CG 1811 C CD1 . PHE A 236 ? 1.1033 0.8570 0.7333 -0.2062 -0.3601 -0.0662 236 PHE A CD1 1812 C CD2 . PHE A 236 ? 1.1542 0.8337 0.7483 -0.1756 -0.3947 -0.0435 236 PHE A CD2 1813 C CE1 . PHE A 236 ? 1.0278 0.8239 0.7213 -0.1896 -0.3301 -0.0744 236 PHE A CE1 1814 C CE2 . PHE A 236 ? 1.0775 0.8021 0.7373 -0.1589 -0.3643 -0.0528 236 PHE A CE2 1815 C CZ . PHE A 236 ? 1.0154 0.7980 0.7238 -0.1660 -0.3324 -0.0678 236 PHE A CZ 1816 N N . SER A 237 ? 1.3699 1.0376 0.8361 -0.2334 -0.5341 -0.0462 237 SER A N 1817 C CA . SER A 237 ? 1.4509 1.0749 0.8384 -0.2636 -0.5577 -0.0391 237 SER A CA 1818 C C . SER A 237 ? 1.4367 1.0537 0.7924 -0.3031 -0.5050 -0.0460 237 SER A C 1819 O O . SER A 237 ? 1.3635 1.0407 0.7797 -0.3044 -0.4734 -0.0628 237 SER A O 1820 C CB . SER A 237 ? 1.4645 1.1390 0.8887 -0.2524 -0.6077 -0.0490 237 SER A CB 1821 O OG . SER A 237 ? 1.3976 1.1480 0.8866 -0.2594 -0.5811 -0.0704 237 SER A OG 1822 N N . PHE A 238 ? 1.5064 1.0486 0.7671 -0.3357 -0.4943 -0.0340 238 PHE A N 1823 C CA . PHE A 238 ? 1.5005 1.0317 0.7293 -0.3727 -0.4427 -0.0422 238 PHE A CA 1824 C C . PHE A 238 ? 1.5952 1.0542 0.7161 -0.4127 -0.4474 -0.0336 238 PHE A C 1825 O O . PHE A 238 ? 1.6696 1.0620 0.7206 -0.4177 -0.4699 -0.0162 238 PHE A O 1826 C CB . PHE A 238 ? 1.4439 0.9725 0.6948 -0.3709 -0.3858 -0.0437 238 PHE A CB 1827 C CG . PHE A 238 ? 1.4786 0.9475 0.6875 -0.3649 -0.3861 -0.0266 238 PHE A CG 1828 C CD1 . PHE A 238 ? 1.4608 0.9408 0.7107 -0.3283 -0.4144 -0.0194 238 PHE A CD1 1829 C CD2 . PHE A 238 ? 1.5280 0.9313 0.6588 -0.3968 -0.3553 -0.0196 238 PHE A CD2 1830 C CE1 . PHE A 238 ? 1.4941 0.9172 0.7044 -0.3244 -0.4138 -0.0041 238 PHE A CE1 1831 C CE2 . PHE A 238 ? 1.5602 0.9100 0.6528 -0.3943 -0.3534 -0.0049 238 PHE A CE2 1832 C CZ . PHE A 238 ? 1.5428 0.9012 0.6741 -0.3584 -0.3832 0.0035 238 PHE A CZ 1833 N N . ASN A 239 ? 1.5959 1.0675 0.7026 -0.4421 -0.4253 -0.0467 239 ASN A N 1834 C CA . ASN A 239 ? 1.6801 1.0889 0.6874 -0.4847 -0.4188 -0.0435 239 ASN A CA 1835 C C . ASN A 239 ? 1.6604 1.0464 0.6449 -0.5113 -0.3515 -0.0517 239 ASN A C 1836 O O . ASN A 239 ? 1.7274 1.0596 0.6295 -0.5483 -0.3365 -0.0515 239 ASN A O 1837 C CB . ASN A 239 ? 1.7083 1.1445 0.7100 -0.5015 -0.4460 -0.0543 239 ASN A CB 1838 C CG . ASN A 239 ? 1.8088 1.2001 0.7383 -0.5099 -0.5071 -0.0401 239 ASN A CG 1839 O OD1 . ASN A 239 ? 1.8630 1.1994 0.7444 -0.5025 -0.5309 -0.0213 239 ASN A OD1 1840 N ND2 . ASN A 239 ? 1.8393 1.2515 0.7586 -0.5263 -0.5340 -0.0489 239 ASN A ND2 1841 N N . GLY A 240 ? 1.5697 0.9963 0.6268 -0.4924 -0.3118 -0.0595 240 GLY A N 1842 C CA . GLY A 240 ? 1.5453 0.9564 0.5932 -0.5120 -0.2491 -0.0684 240 GLY A CA 1843 C C . GLY A 240 ? 1.4448 0.9200 0.5838 -0.4939 -0.2148 -0.0826 240 GLY A C 1844 O O . GLY A 240 ? 1.3904 0.9200 0.6023 -0.4627 -0.2348 -0.0834 240 GLY A O 1845 N N . ALA A 241 ? 1.4280 0.8943 0.5605 -0.5139 -0.1628 -0.0941 241 ALA A N 1846 C CA . ALA A 241 ? 1.3448 0.8609 0.5528 -0.5009 -0.1262 -0.1070 241 ALA A CA 1847 C C . ALA A 241 ? 1.2700 0.8187 0.5471 -0.4650 -0.1206 -0.1012 241 ALA A C 1848 O O . ALA A 241 ? 1.2029 0.7955 0.5446 -0.4514 -0.0971 -0.1101 241 ALA A O 1849 C CB . ALA A 241 ? 1.3251 0.8909 0.5707 -0.5017 -0.1425 -0.1187 241 ALA A CB 1850 N N . PHE A 242 ? 1.2878 0.8102 0.5461 -0.4521 -0.1406 -0.0865 242 PHE A N 1851 C CA . PHE A 242 ? 1.2298 0.7857 0.5508 -0.4155 -0.1537 -0.0799 242 PHE A CA 1852 C C . PHE A 242 ? 1.2091 0.7406 0.5300 -0.4105 -0.1204 -0.0744 242 PHE A C 1853 O O . PHE A 242 ? 1.2614 0.7373 0.5177 -0.4313 -0.1091 -0.0682 242 PHE A O 1854 C CB . PHE A 242 ? 1.2710 0.8201 0.5771 -0.4007 -0.2117 -0.0682 242 PHE A CB 1855 C CG . PHE A 242 ? 1.2304 0.8040 0.5906 -0.3637 -0.2297 -0.0613 242 PHE A CG 1856 C CD1 . PHE A 242 ? 1.1520 0.7909 0.5974 -0.3384 -0.2224 -0.0708 242 PHE A CD1 1857 C CD2 . PHE A 242 ? 1.2786 0.8066 0.6000 -0.3555 -0.2557 -0.0456 242 PHE A CD2 1858 C CE1 . PHE A 242 ? 1.1174 0.7775 0.6100 -0.3054 -0.2385 -0.0660 242 PHE A CE1 1859 C CE2 . PHE A 242 ? 1.2454 0.7922 0.6142 -0.3217 -0.2725 -0.0403 242 PHE A CE2 1860 C CZ . PHE A 242 ? 1.1626 0.7769 0.6182 -0.2962 -0.2635 -0.0512 242 PHE A CZ 1861 N N . ILE A 243 ? 1.1290 0.7037 0.5219 -0.3852 -0.1038 -0.0776 243 ILE A N 1862 C CA . ILE A 243 ? 1.1000 0.6620 0.5053 -0.3774 -0.0743 -0.0737 243 ILE A CA 1863 C C . ILE A 243 ? 1.0750 0.6500 0.5124 -0.3466 -0.1035 -0.0634 243 ILE A C 1864 O O . ILE A 243 ? 1.0159 0.6423 0.5187 -0.3213 -0.1132 -0.0675 243 ILE A O 1865 C CB . ILE A 243 ? 1.0336 0.6314 0.4944 -0.3725 -0.0317 -0.0853 243 ILE A CB 1866 C CG1 . ILE A 243 ? 1.0568 0.6415 0.4897 -0.4009 -0.0031 -0.0973 243 ILE A CG1 1867 C CG2 . ILE A 243 ? 1.0070 0.5952 0.4837 -0.3640 -0.0039 -0.0818 243 ILE A CG2 1868 C CD1 . ILE A 243 ? 1.1140 0.6428 0.4813 -0.4289 0.0226 -0.0977 243 ILE A CD1 1869 N N . ALA A 244 ? 1.1240 0.6500 0.5130 -0.3504 -0.1160 -0.0509 244 ALA A N 1870 C CA . ALA A 244 ? 1.1246 0.6501 0.5287 -0.3236 -0.1522 -0.0402 244 ALA A CA 1871 C C . ALA A 244 ? 1.0634 0.6088 0.5185 -0.3023 -0.1320 -0.0397 244 ALA A C 1872 O O . ALA A 244 ? 1.0605 0.5868 0.5041 -0.3150 -0.0958 -0.0401 244 ALA A O 1873 C CB . ALA A 244 ? 1.2149 0.6720 0.5381 -0.3382 -0.1779 -0.0256 244 ALA A CB 1874 N N . PRO A 245 ? 1.0194 0.6034 0.5307 -0.2704 -0.1560 -0.0399 245 PRO A N 1875 C CA . PRO A 245 ? 0.9725 0.5704 0.5256 -0.2510 -0.1406 -0.0387 245 PRO A CA 1876 C C . PRO A 245 ? 1.0208 0.5618 0.5260 -0.2544 -0.1495 -0.0255 245 PRO A C 1877 O O . PRO A 245 ? 1.0758 0.5830 0.5434 -0.2506 -0.1882 -0.0159 245 PRO A O 1878 C CB . PRO A 245 ? 0.9289 0.5783 0.5459 -0.2181 -0.1682 -0.0436 245 PRO A CB 1879 C CG . PRO A 245 ? 0.9716 0.6198 0.5695 -0.2176 -0.2090 -0.0430 245 PRO A CG 1880 C CD . PRO A 245 ? 1.0186 0.6336 0.5559 -0.2514 -0.1986 -0.0421 245 PRO A CD 1881 N N . ASP A 246 ? 1.0051 0.5350 0.5118 -0.2619 -0.1148 -0.0253 246 ASP A N 1882 C CA . ASP A 246 ? 1.0459 0.5260 0.5136 -0.2660 -0.1190 -0.0141 246 ASP A CA 1883 C C . ASP A 246 ? 1.0060 0.5076 0.5229 -0.2339 -0.1353 -0.0123 246 ASP A C 1884 O O . ASP A 246 ? 1.0509 0.5157 0.5402 -0.2252 -0.1657 -0.0022 246 ASP A O 1885 C CB . ASP A 246 ? 1.0488 0.5100 0.4976 -0.2907 -0.0735 -0.0167 246 ASP A CB 1886 C CG . ASP A 246 ? 1.1035 0.5090 0.5028 -0.3021 -0.0760 -0.0059 246 ASP A CG 1887 O OD1 . ASP A 246 ? 1.1829 0.5350 0.5153 -0.3150 -0.1024 0.0048 246 ASP A OD1 1888 O OD2 . ASP A 246 ? 1.0773 0.4906 0.5028 -0.2987 -0.0534 -0.0076 246 ASP A OD2 1889 N N . ARG A 247 ? 0.9274 0.4851 0.5136 -0.2171 -0.1154 -0.0222 247 ARG A N 1890 C CA . ARG A 247 ? 0.8861 0.4687 0.5215 -0.1879 -0.1269 -0.0230 247 ARG A CA 1891 C C . ARG A 247 ? 0.8257 0.4711 0.5257 -0.1634 -0.1385 -0.0335 247 ARG A C 1892 O O . ARG A 247 ? 0.7970 0.4759 0.5165 -0.1702 -0.1249 -0.0416 247 ARG A O 1893 C CB . ARG A 247 ? 0.8505 0.4419 0.5098 -0.1905 -0.0914 -0.0253 247 ARG A CB 1894 C CG . ARG A 247 ? 0.9020 0.4383 0.5068 -0.2144 -0.0761 -0.0175 247 ARG A CG 1895 C CD . ARG A 247 ? 0.8609 0.4187 0.4965 -0.2216 -0.0348 -0.0238 247 ARG A CD 1896 N NE . ARG A 247 ? 0.8502 0.4059 0.5050 -0.2101 -0.0346 -0.0214 247 ARG A NE 1897 C CZ . ARG A 247 ? 0.8083 0.3908 0.5017 -0.2091 -0.0062 -0.0271 247 ARG A CZ 1898 N NH1 . ARG A 247 ? 0.7724 0.3856 0.4920 -0.2167 0.0242 -0.0353 247 ARG A NH1 1899 N NH2 . ARG A 247 ? 0.8023 0.3792 0.5078 -0.2002 -0.0097 -0.0246 247 ARG A NH2 1900 N N . ALA A 248 ? 0.8075 0.4672 0.5397 -0.1360 -0.1625 -0.0343 248 ALA A N 1901 C CA . ALA A 248 ? 0.7510 0.4728 0.5487 -0.1120 -0.1709 -0.0463 248 ALA A CA 1902 C C . ALA A 248 ? 0.6880 0.4412 0.5329 -0.1009 -0.1454 -0.0518 248 ALA A C 1903 O O . ALA A 248 ? 0.6945 0.4191 0.5249 -0.1031 -0.1351 -0.0457 248 ALA A O 1904 C CB . ALA A 248 ? 0.7784 0.4981 0.5840 -0.0874 -0.2153 -0.0463 248 ALA A CB 1905 N N . SER A 249 ? 0.6294 0.4404 0.5283 -0.0907 -0.1359 -0.0635 249 SER A N 1906 C CA . SER A 249 ? 0.5725 0.4159 0.5157 -0.0799 -0.1145 -0.0692 249 SER A CA 1907 C C . SER A 249 ? 0.5494 0.4254 0.5361 -0.0521 -0.1355 -0.0780 249 SER A C 1908 O O . SER A 249 ? 0.5521 0.4551 0.5586 -0.0416 -0.1569 -0.0858 249 SER A O 1909 C CB . SER A 249 ? 0.5293 0.4101 0.4978 -0.0909 -0.0851 -0.0758 249 SER A CB 1910 O OG . SER A 249 ? 0.5472 0.3982 0.4797 -0.1146 -0.0632 -0.0698 249 SER A OG 1911 N N . PHE A 250 ? 0.5281 0.4027 0.5307 -0.0408 -0.1289 -0.0782 250 PHE A N 1912 C CA . PHE A 250 ? 0.5031 0.4112 0.5500 -0.0153 -0.1418 -0.0891 250 PHE A CA 1913 C C . PHE A 250 ? 0.4513 0.3945 0.5328 -0.0153 -0.1128 -0.0951 250 PHE A C 1914 O O . PHE A 250 ? 0.4418 0.3667 0.5083 -0.0281 -0.0907 -0.0877 250 PHE A O 1915 C CB . PHE A 250 ? 0.5396 0.4069 0.5684 -0.0007 -0.1653 -0.0843 250 PHE A CB 1916 C CG . PHE A 250 ? 0.5949 0.4269 0.5909 0.0032 -0.1998 -0.0784 250 PHE A CG 1917 C CD1 . PHE A 250 ? 0.6425 0.4183 0.5782 -0.0174 -0.2020 -0.0636 250 PHE A CD1 1918 C CD2 . PHE A 250 ? 0.6030 0.4588 0.6283 0.0269 -0.2305 -0.0885 250 PHE A CD2 1919 C CE1 . PHE A 250 ? 0.7007 0.4397 0.5999 -0.0153 -0.2360 -0.0567 250 PHE A CE1 1920 C CE2 . PHE A 250 ? 0.6591 0.4814 0.6542 0.0318 -0.2662 -0.0824 250 PHE A CE2 1921 C CZ . PHE A 250 ? 0.7094 0.4711 0.6385 0.0102 -0.2698 -0.0654 250 PHE A CZ 1922 N N . LEU A 251 ? 0.4197 0.4135 0.5467 -0.0019 -0.1132 -0.1090 251 LEU A N 1923 C CA . LEU A 251 ? 0.3758 0.4032 0.5322 -0.0034 -0.0870 -0.1146 251 LEU A CA 1924 C C . LEU A 251 ? 0.3742 0.3937 0.5401 0.0108 -0.0888 -0.1164 251 LEU A C 1925 O O . LEU A 251 ? 0.3913 0.4062 0.5653 0.0294 -0.1113 -0.1224 251 LEU A O 1926 C CB . LEU A 251 ? 0.3474 0.4313 0.5438 0.0003 -0.0836 -0.1294 251 LEU A CB 1927 C CG . LEU A 251 ? 0.3549 0.4533 0.5482 -0.0109 -0.0883 -0.1317 251 LEU A CG 1928 C CD1 . LEU A 251 ? 0.3254 0.4820 0.5601 -0.0103 -0.0800 -0.1475 251 LEU A CD1 1929 C CD2 . LEU A 251 ? 0.3607 0.4305 0.5190 -0.0343 -0.0699 -0.1193 251 LEU A CD2 1930 N N . ARG A 252 ? 0.3542 0.3730 0.5206 0.0026 -0.0657 -0.1122 252 ARG A N 1931 C CA . ARG A 252 ? 0.3576 0.3621 0.5253 0.0110 -0.0653 -0.1120 252 ARG A CA 1932 C C . ARG A 252 ? 0.3398 0.3820 0.5440 0.0266 -0.0653 -0.1265 252 ARG A C 1933 O O . ARG A 252 ? 0.3545 0.3843 0.5617 0.0405 -0.0769 -0.1311 252 ARG A O 1934 C CB . ARG A 252 ? 0.3443 0.3349 0.4993 -0.0048 -0.0421 -0.1021 252 ARG A CB 1935 C CG . ARG A 252 ? 0.3741 0.3204 0.4907 -0.0199 -0.0408 -0.0895 252 ARG A CG 1936 C CD . ARG A 252 ? 0.3624 0.3011 0.4748 -0.0334 -0.0178 -0.0829 252 ARG A CD 1937 N NE . ARG A 252 ? 0.3927 0.2927 0.4699 -0.0501 -0.0129 -0.0735 252 ARG A NE 1938 C CZ . ARG A 252 ? 0.4261 0.2860 0.4753 -0.0545 -0.0204 -0.0680 252 ARG A CZ 1939 N NH1 . ARG A 252 ? 0.4342 0.2847 0.4867 -0.0419 -0.0344 -0.0704 252 ARG A NH1 1940 N NH2 . ARG A 252 ? 0.4559 0.2829 0.4712 -0.0731 -0.0125 -0.0607 252 ARG A NH2 1941 N N . GLY A 253 ? 0.3147 0.4002 0.5438 0.0224 -0.0508 -0.1342 253 GLY A N 1942 C CA . GLY A 253 ? 0.3010 0.4232 0.5610 0.0326 -0.0457 -0.1487 253 GLY A CA 1943 C C . GLY A 253 ? 0.2801 0.4445 0.5590 0.0221 -0.0274 -0.1550 253 GLY A C 1944 O O . GLY A 253 ? 0.2826 0.4727 0.5753 0.0213 -0.0315 -0.1628 253 GLY A O 1945 N N . LYS A 254 ? 0.2677 0.4379 0.5455 0.0132 -0.0084 -0.1515 254 LYS A N 1946 C CA . LYS A 254 ? 0.2543 0.4589 0.5448 0.0022 0.0093 -0.1568 254 LYS A CA 1947 C C . LYS A 254 ? 0.2397 0.4276 0.5122 -0.0130 0.0263 -0.1420 254 LYS A C 1948 O O . LYS A 254 ? 0.2412 0.4046 0.5020 -0.0122 0.0274 -0.1330 254 LYS A O 1949 C CB . LYS A 254 ? 0.2580 0.4931 0.5696 0.0097 0.0134 -0.1722 254 LYS A CB 1950 C CG . LYS A 254 ? 0.2772 0.5428 0.6170 0.0241 0.0007 -0.1920 254 LYS A CG 1951 C CD . LYS A 254 ? 0.2837 0.5732 0.6426 0.0335 0.0050 -0.2091 254 LYS A CD 1952 C CE . LYS A 254 ? 0.3011 0.6134 0.6907 0.0539 -0.0115 -0.2295 254 LYS A CE 1953 N NZ . LYS A 254 ? 0.3010 0.6603 0.7184 0.0497 -0.0081 -0.2442 254 LYS A NZ 1954 N N . SER A 255 ? 0.2257 0.4267 0.4973 -0.0266 0.0389 -0.1403 255 SER A N 1955 C CA . SER A 255 ? 0.2183 0.4055 0.4763 -0.0391 0.0546 -0.1279 255 SER A CA 1956 C C . SER A 255 ? 0.2166 0.4262 0.4777 -0.0523 0.0677 -0.1317 255 SER A C 1957 O O . SER A 255 ? 0.2199 0.4584 0.4950 -0.0532 0.0659 -0.1446 255 SER A O 1958 C CB . SER A 255 ? 0.2230 0.3763 0.4628 -0.0445 0.0552 -0.1149 255 SER A CB 1959 O OG . SER A 255 ? 0.2283 0.3810 0.4632 -0.0499 0.0515 -0.1168 255 SER A OG 1960 N N . MET A 256 ? 0.2196 0.4145 0.4679 -0.0626 0.0804 -0.1206 256 MET A N 1961 C CA . MET A 256 ? 0.2257 0.4299 0.4687 -0.0774 0.0939 -0.1203 256 MET A CA 1962 C C . MET A 256 ? 0.2221 0.3962 0.4500 -0.0851 0.1003 -0.1077 256 MET A C 1963 O O . MET A 256 ? 0.2220 0.3720 0.4445 -0.0800 0.0996 -0.0977 256 MET A O 1964 C CB . MET A 256 ? 0.2417 0.4494 0.4805 -0.0794 0.1006 -0.1178 256 MET A CB 1965 C CG . MET A 256 ? 0.2682 0.4707 0.4920 -0.0954 0.1141 -0.1116 256 MET A CG 1966 S SD . MET A 256 ? 0.3055 0.5455 0.5335 -0.1091 0.1233 -0.1279 256 MET A SD 1967 C CE . MET A 256 ? 0.3228 0.5427 0.5292 -0.1299 0.1367 -0.1184 256 MET A CE 1968 N N . GLY A 257 ? 0.2195 0.3958 0.4418 -0.0977 0.1070 -0.1097 257 GLY A N 1969 C CA . GLY A 257 ? 0.2234 0.3704 0.4306 -0.1058 0.1148 -0.1002 257 GLY A CA 1970 C C . GLY A 257 ? 0.2299 0.3680 0.4255 -0.1190 0.1285 -0.0951 257 GLY A C 1971 O O . GLY A 257 ? 0.2324 0.3903 0.4280 -0.1295 0.1333 -0.1020 257 GLY A O 1972 N N . ILE A 258 ? 0.2342 0.3418 0.4203 -0.1187 0.1349 -0.0836 258 ILE A N 1973 C CA . ILE A 258 ? 0.2497 0.3396 0.4216 -0.1297 0.1460 -0.0770 258 ILE A CA 1974 C C . ILE A 258 ? 0.2627 0.3205 0.4255 -0.1331 0.1538 -0.0715 258 ILE A C 1975 O O . ILE A 258 ? 0.2550 0.3023 0.4226 -0.1257 0.1519 -0.0707 258 ILE A O 1976 C CB . ILE A 258 ? 0.2527 0.3360 0.4226 -0.1241 0.1448 -0.0681 258 ILE A CB 1977 C CG1 . ILE A 258 ? 0.2481 0.3114 0.4258 -0.1104 0.1413 -0.0592 258 ILE A CG1 1978 C CG2 . ILE A 258 ? 0.2408 0.3544 0.4186 -0.1205 0.1382 -0.0751 258 ILE A CG2 1979 C CD1 . ILE A 258 ? 0.2552 0.3118 0.4314 -0.1048 0.1372 -0.0499 258 ILE A CD1 1980 N N . GLN A 259 ? 0.2836 0.3244 0.4310 -0.1459 0.1635 -0.0688 259 GLN A N 1981 C CA . GLN A 259 ? 0.3034 0.3094 0.4414 -0.1485 0.1725 -0.0640 259 GLN A CA 1982 C C . GLN A 259 ? 0.3209 0.3033 0.4537 -0.1439 0.1743 -0.0526 259 GLN A C 1983 O O . GLN A 259 ? 0.3317 0.3176 0.4538 -0.1507 0.1735 -0.0493 259 GLN A O 1984 C CB . GLN A 259 ? 0.3231 0.3224 0.4448 -0.1674 0.1811 -0.0701 259 GLN A CB 1985 C CG . GLN A 259 ? 0.3111 0.3374 0.4375 -0.1735 0.1760 -0.0817 259 GLN A CG 1986 C CD . GLN A 259 ? 0.3324 0.3530 0.4433 -0.1937 0.1838 -0.0883 259 GLN A CD 1987 O OE1 . GLN A 259 ? 0.3483 0.3719 0.4499 -0.2078 0.1898 -0.0895 259 GLN A OE1 1988 N NE2 . GLN A 259 ? 0.3379 0.3491 0.4429 -0.1975 0.1842 -0.0930 259 GLN A NE2 1989 N N . SER A 260 ? 0.3269 0.2854 0.4668 -0.1329 0.1764 -0.0471 260 SER A N 1990 C CA . SER A 260 ? 0.3453 0.2824 0.4851 -0.1244 0.1738 -0.0359 260 SER A CA 1991 C C . SER A 260 ? 0.3570 0.2665 0.5070 -0.1143 0.1793 -0.0336 260 SER A C 1992 O O . SER A 260 ? 0.3468 0.2594 0.5083 -0.1112 0.1845 -0.0406 260 SER A O 1993 C CB . SER A 260 ? 0.3278 0.2860 0.4813 -0.1123 0.1614 -0.0317 260 SER A CB 1994 O OG . SER A 260 ? 0.3446 0.2829 0.5032 -0.1009 0.1560 -0.0212 260 SER A OG 1995 N N . GLY A 261 ? 0.3842 0.2660 0.5294 -0.1091 0.1776 -0.0243 261 GLY A N 1996 C CA . GLY A 261 ? 0.4009 0.2571 0.5613 -0.0961 0.1817 -0.0229 261 GLY A CA 1997 C C . GLY A 261 ? 0.4022 0.2581 0.5835 -0.0771 0.1691 -0.0141 261 GLY A C 1998 O O . GLY A 261 ? 0.4237 0.2570 0.6192 -0.0648 0.1703 -0.0123 261 GLY A O 1999 N N . VAL A 262 ? 0.3831 0.2646 0.5680 -0.0742 0.1566 -0.0098 262 VAL A N 2000 C CA . VAL A 262 ? 0.3858 0.2700 0.5899 -0.0575 0.1422 -0.0017 262 VAL A CA 2001 C C . VAL A 262 ? 0.3525 0.2710 0.5845 -0.0492 0.1378 -0.0074 262 VAL A C 2002 O O . VAL A 262 ? 0.3253 0.2642 0.5568 -0.0565 0.1436 -0.0159 262 VAL A O 2003 C CB . VAL A 262 ? 0.4061 0.2820 0.5852 -0.0616 0.1287 0.0106 262 VAL A CB 2004 C CG1 . VAL A 262 ? 0.4494 0.2847 0.5979 -0.0709 0.1328 0.0174 262 VAL A CG1 2005 C CG2 . VAL A 262 ? 0.3840 0.2897 0.5489 -0.0740 0.1273 0.0069 262 VAL A CG2 2006 N N . GLN A 263 ? 0.3576 0.2807 0.6131 -0.0342 0.1260 -0.0024 263 GLN A N 2007 C CA . GLN A 263 ? 0.3338 0.2861 0.6185 -0.0267 0.1228 -0.0083 263 GLN A CA 2008 C C . GLN A 263 ? 0.3116 0.2883 0.5863 -0.0324 0.1136 -0.0078 263 GLN A C 2009 O O . GLN A 263 ? 0.3233 0.2972 0.5751 -0.0373 0.1048 -0.0008 263 GLN A O 2010 C CB . GLN A 263 ? 0.3475 0.3008 0.6634 -0.0094 0.1114 -0.0040 263 GLN A CB 2011 C CG . GLN A 263 ? 0.3739 0.3091 0.7126 0.0009 0.1203 -0.0080 263 GLN A CG 2012 C CD . GLN A 263 ? 0.3990 0.3311 0.7648 0.0197 0.1035 -0.0011 263 GLN A CD 2013 O OE1 . GLN A 263 ? 0.3913 0.3473 0.7742 0.0256 0.0887 0.0014 263 GLN A OE1 2014 N NE2 . GLN A 263 ? 0.4355 0.3370 0.8049 0.0294 0.1039 0.0018 263 GLN A NE2 2015 N N . VAL A 264 ? 0.2849 0.2834 0.5761 -0.0319 0.1161 -0.0159 264 VAL A N 2016 C CA . VAL A 264 ? 0.2682 0.2890 0.5555 -0.0343 0.1067 -0.0172 264 VAL A CA 2017 C C . VAL A 264 ? 0.2707 0.3003 0.5739 -0.0246 0.0909 -0.0110 264 VAL A C 2018 O O . VAL A 264 ? 0.2788 0.3070 0.6086 -0.0144 0.0885 -0.0098 264 VAL A O 2019 C CB . VAL A 264 ? 0.2470 0.2810 0.5431 -0.0378 0.1140 -0.0273 264 VAL A CB 2020 C CG1 . VAL A 264 ? 0.2345 0.2877 0.5292 -0.0382 0.1035 -0.0293 264 VAL A CG1 2021 C CG2 . VAL A 264 ? 0.2473 0.2728 0.5237 -0.0479 0.1256 -0.0327 264 VAL A CG2 2022 N N . ASP A 265 ? 0.2690 0.3089 0.5566 -0.0281 0.0799 -0.0083 265 ASP A N 2023 C CA . ASP A 265 ? 0.2734 0.3215 0.5697 -0.0214 0.0627 -0.0024 265 ASP A CA 2024 C C . ASP A 265 ? 0.2529 0.3202 0.5406 -0.0267 0.0572 -0.0076 265 ASP A C 2025 O O . ASP A 265 ? 0.2553 0.3230 0.5164 -0.0351 0.0584 -0.0088 265 ASP A O 2026 C CB . ASP A 265 ? 0.3096 0.3375 0.5838 -0.0212 0.0526 0.0100 265 ASP A CB 2027 C CG . ASP A 265 ? 0.3289 0.3617 0.6095 -0.0140 0.0317 0.0178 265 ASP A CG 2028 O OD1 . ASP A 265 ? 0.3139 0.3693 0.6109 -0.0124 0.0257 0.0124 265 ASP A OD1 2029 O OD2 . ASP A 265 ? 0.3654 0.3771 0.6322 -0.0108 0.0201 0.0297 265 ASP A OD2 2030 N N . ALA A 266 ? 0.2329 0.3164 0.5439 -0.0227 0.0522 -0.0122 266 ALA A N 2031 C CA . ALA A 266 ? 0.2187 0.3169 0.5224 -0.0272 0.0469 -0.0184 266 ALA A CA 2032 C C . ALA A 266 ? 0.2310 0.3349 0.5274 -0.0265 0.0296 -0.0130 266 ALA A C 2033 O O . ALA A 266 ? 0.2220 0.3373 0.5146 -0.0297 0.0236 -0.0185 266 ALA A O 2034 C CB . ALA A 266 ? 0.2012 0.3095 0.5277 -0.0268 0.0516 -0.0267 266 ALA A CB 2035 N N . ASN A 267 ? 0.2546 0.3471 0.5463 -0.0227 0.0205 -0.0021 267 ASN A N 2036 C CA . ASN A 267 ? 0.2788 0.3719 0.5582 -0.0229 0.0017 0.0052 267 ASN A CA 2037 C C . ASN A 267 ? 0.3069 0.3891 0.5424 -0.0337 0.0013 0.0085 267 ASN A C 2038 O O . ASN A 267 ? 0.3218 0.4060 0.5386 -0.0383 -0.0115 0.0111 267 ASN A O 2039 C CB . ASN A 267 ? 0.2956 0.3799 0.5938 -0.0117 -0.0114 0.0160 267 ASN A CB 2040 C CG . ASN A 267 ? 0.3223 0.4024 0.6030 -0.0119 -0.0343 0.0261 267 ASN A CG 2041 O OD1 . ASN A 267 ? 0.3521 0.4085 0.6056 -0.0130 -0.0417 0.0378 267 ASN A OD1 2042 N ND2 . ASN A 267 ? 0.3139 0.4141 0.6061 -0.0126 -0.0461 0.0217 267 ASN A ND2 2043 N N . CYS A 268 ? 0.3208 0.3923 0.5395 -0.0396 0.0161 0.0073 268 CYS A N 2044 C CA . CYS A 268 ? 0.3526 0.4175 0.5321 -0.0526 0.0201 0.0073 268 CYS A CA 2045 C C . CYS A 268 ? 0.3347 0.4144 0.5123 -0.0588 0.0362 -0.0070 268 CYS A C 2046 O O . CYS A 268 ? 0.3135 0.3975 0.5118 -0.0543 0.0458 -0.0127 268 CYS A O 2047 C CB . CYS A 268 ? 0.3883 0.4259 0.5455 -0.0569 0.0218 0.0190 268 CYS A CB 2048 S SG . CYS A 268 ? 0.3862 0.4120 0.5656 -0.0505 0.0362 0.0188 268 CYS A SG 2049 N N . GLU A 269 ? 0.3745 0.5597 0.6814 -0.2966 -0.0041 0.0125 269 GLU A N 2050 C CA . GLU A 269 ? 0.3991 0.5008 0.6667 -0.2824 0.0132 0.0023 269 GLU A CA 2051 C C . GLU A 269 ? 0.3631 0.4522 0.6308 -0.2463 0.0077 0.0066 269 GLU A C 2052 O O . GLU A 269 ? 0.3538 0.4702 0.6259 -0.2455 -0.0077 0.0089 269 GLU A O 2053 C CB . GLU A 269 ? 0.4746 0.5201 0.6869 -0.3171 0.0225 -0.0148 269 GLU A CB 2054 C CG . GLU A 269 ? 0.5112 0.4725 0.6792 -0.2961 0.0424 -0.0212 269 GLU A CG 2055 C CD . GLU A 269 ? 0.5986 0.4893 0.7076 -0.3276 0.0634 -0.0359 269 GLU A CD 2056 O OE1 . GLU A 269 ? 0.6477 0.5460 0.7364 -0.3702 0.0573 -0.0461 269 GLU A OE1 2057 O OE2 . GLU A 269 ? 0.6372 0.4640 0.7164 -0.3102 0.0877 -0.0367 269 GLU A OE2 2058 N N . GLY A 270 ? 0.3431 0.3941 0.6052 -0.2177 0.0204 0.0083 270 GLY A N 2059 C CA . GLY A 270 ? 0.3160 0.3540 0.5742 -0.1882 0.0170 0.0114 270 GLY A CA 2060 C C . GLY A 270 ? 0.3189 0.3059 0.5530 -0.1689 0.0344 0.0098 270 GLY A C 2061 O O . GLY A 270 ? 0.3338 0.2999 0.5615 -0.1717 0.0490 0.0089 270 GLY A O 2062 N N . ASP A 271 ? 0.3070 0.2781 0.5277 -0.1490 0.0333 0.0111 271 ASP A N 2063 C CA . ASP A 271 ? 0.3094 0.2458 0.5094 -0.1272 0.0484 0.0136 271 ASP A CA 2064 C C . ASP A 271 ? 0.2673 0.2255 0.4838 -0.1027 0.0420 0.0209 271 ASP A C 2065 O O . ASP A 271 ? 0.2684 0.2127 0.4719 -0.0848 0.0519 0.0252 271 ASP A O 2066 C CB . ASP A 271 ? 0.3557 0.2435 0.5101 -0.1297 0.0599 0.0088 271 ASP A CB 2067 C CG . ASP A 271 ? 0.4110 0.2581 0.5350 -0.1539 0.0752 0.0006 271 ASP A CG 2068 O OD1 . ASP A 271 ? 0.4175 0.2617 0.5493 -0.1575 0.0851 0.0015 271 ASP A OD1 2069 O OD2 . ASP A 271 ? 0.4600 0.2737 0.5480 -0.1711 0.0792 -0.0074 271 ASP A OD2 2070 N N . CYS A 272 ? 0.2338 0.2272 0.4765 -0.1026 0.0271 0.0232 272 CYS A N 2071 C CA . CYS A 272 ? 0.2065 0.2152 0.4601 -0.0854 0.0231 0.0283 272 CYS A CA 2072 C C . CYS A 272 ? 0.1826 0.2160 0.4640 -0.0826 0.0213 0.0327 272 CYS A C 2073 O O . CYS A 272 ? 0.1771 0.2340 0.4769 -0.0887 0.0138 0.0353 272 CYS A O 2074 C CB . CYS A 272 ? 0.2036 0.2195 0.4533 -0.0839 0.0121 0.0281 272 CYS A CB 2075 S SG . CYS A 272 ? 0.1875 0.2154 0.4426 -0.0687 0.0102 0.0326 272 CYS A SG 2076 N N . TYR A 273 ? 0.1708 0.2005 0.4528 -0.0721 0.0293 0.0349 273 TYR A N 2077 C CA . TYR A 273 ? 0.1606 0.2032 0.4615 -0.0682 0.0326 0.0390 273 TYR A CA 2078 C C . TYR A 273 ? 0.1552 0.1962 0.4504 -0.0587 0.0344 0.0402 273 TYR A C 2079 O O . TYR A 273 ? 0.1564 0.1915 0.4350 -0.0561 0.0346 0.0382 273 TYR A O 2080 C CB . TYR A 273 ? 0.1649 0.1987 0.4666 -0.0688 0.0439 0.0393 273 TYR A CB 2081 C CG . TYR A 273 ? 0.1782 0.2061 0.4792 -0.0829 0.0466 0.0366 273 TYR A CG 2082 C CD1 . TYR A 273 ? 0.1758 0.2278 0.4981 -0.0954 0.0419 0.0389 273 TYR A CD1 2083 C CD2 . TYR A 273 ? 0.1974 0.1959 0.4734 -0.0844 0.0560 0.0331 273 TYR A CD2 2084 C CE1 . TYR A 273 ? 0.1951 0.2432 0.5134 -0.1154 0.0446 0.0349 273 TYR A CE1 2085 C CE2 . TYR A 273 ? 0.2233 0.2059 0.4902 -0.1016 0.0622 0.0289 273 TYR A CE2 2086 C CZ . TYR A 273 ? 0.2210 0.2291 0.5090 -0.1202 0.0556 0.0285 273 TYR A CZ 2087 O OH . TYR A 273 ? 0.2491 0.2441 0.5256 -0.1441 0.0614 0.0229 273 TYR A OH 2088 N N . HIS A 274 ? 0.1591 0.2061 0.4658 -0.0542 0.0375 0.0445 274 HIS A N 2089 C CA . HIS A 274 ? 0.1672 0.2026 0.4615 -0.0491 0.0442 0.0442 274 HIS A CA 2090 C C . HIS A 274 ? 0.1764 0.2098 0.4809 -0.0423 0.0554 0.0500 274 HIS A C 2091 O O . HIS A 274 ? 0.1723 0.2214 0.4976 -0.0417 0.0557 0.0552 274 HIS A O 2092 C CB . HIS A 274 ? 0.1709 0.2031 0.4567 -0.0485 0.0398 0.0442 274 HIS A CB 2093 C CG . HIS A 274 ? 0.1743 0.2180 0.4760 -0.0420 0.0381 0.0520 274 HIS A CG 2094 N ND1 . HIS A 274 ? 0.1915 0.2246 0.4890 -0.0317 0.0486 0.0586 274 HIS A ND1 2095 C CD2 . HIS A 274 ? 0.1698 0.2365 0.4887 -0.0441 0.0285 0.0557 274 HIS A CD2 2096 C CE1 . HIS A 274 ? 0.1896 0.2448 0.5049 -0.0236 0.0452 0.0687 274 HIS A CE1 2097 N NE2 . HIS A 274 ? 0.1747 0.2542 0.5041 -0.0333 0.0313 0.0664 274 HIS A NE2 2098 N N . SER A 275 ? 0.1917 0.2055 0.4793 -0.0387 0.0660 0.0495 275 SER A N 2099 C CA . SER A 275 ? 0.2067 0.2124 0.4986 -0.0300 0.0803 0.0555 275 SER A CA 2100 C C . SER A 275 ? 0.2058 0.2278 0.5198 -0.0179 0.0836 0.0682 275 SER A C 2101 O O . SER A 275 ? 0.2097 0.2436 0.5411 -0.0104 0.0916 0.0768 275 SER A O 2102 C CB . SER A 275 ? 0.2351 0.2080 0.4949 -0.0310 0.0937 0.0511 275 SER A CB 2103 O OG . SER A 275 ? 0.2559 0.2114 0.4978 -0.0315 0.0962 0.0503 275 SER A OG 2104 N N . GLY A 276 ? 0.2019 0.2300 0.5164 -0.0152 0.0776 0.0712 276 GLY A N 2105 C CA . GLY A 276 ? 0.2027 0.2552 0.5374 -0.0012 0.0798 0.0864 276 GLY A CA 2106 C C . GLY A 276 ? 0.1790 0.2780 0.5445 -0.0088 0.0643 0.0906 276 GLY A C 2107 O O . GLY A 276 ? 0.1816 0.3154 0.5679 0.0012 0.0642 0.1054 276 GLY A O 2108 N N . GLY A 277 ? 0.1609 0.2617 0.5264 -0.0265 0.0529 0.0789 277 GLY A N 2109 C CA . GLY A 277 ? 0.1491 0.2849 0.5349 -0.0398 0.0408 0.0800 277 GLY A CA 2110 C C . GLY A 277 ? 0.1438 0.2689 0.5156 -0.0566 0.0289 0.0671 277 GLY A C 2111 O O . GLY A 277 ? 0.1436 0.2389 0.4957 -0.0590 0.0315 0.0576 277 GLY A O 2112 N N . THR A 278 ? 0.1427 0.2941 0.5224 -0.0674 0.0168 0.0684 278 THR A N 2113 C CA . THR A 278 ? 0.1506 0.2883 0.5131 -0.0847 0.0085 0.0568 278 THR A CA 2114 C C . THR A 278 ? 0.1527 0.2982 0.5082 -0.0846 -0.0030 0.0570 278 THR A C 2115 O O . THR A 278 ? 0.1483 0.3289 0.5198 -0.0804 -0.0089 0.0672 278 THR A O 2116 C CB . THR A 278 ? 0.1612 0.3163 0.5310 -0.1074 0.0063 0.0543 278 THR A CB 2117 O OG1 . THR A 278 ? 0.1606 0.3095 0.5384 -0.1065 0.0184 0.0556 278 THR A OG1 2118 C CG2 . THR A 278 ? 0.1796 0.3040 0.5202 -0.1251 0.0036 0.0414 278 THR A CG2 2119 N N . ILE A 279 ? 0.1625 0.2778 0.4936 -0.0869 -0.0051 0.0477 279 ILE A N 2120 C CA . ILE A 279 ? 0.1711 0.2891 0.4919 -0.0877 -0.0152 0.0468 279 ILE A CA 2121 C C . ILE A 279 ? 0.1955 0.3097 0.5018 -0.1091 -0.0214 0.0388 279 ILE A C 2122 O O . ILE A 279 ? 0.2106 0.2899 0.4935 -0.1139 -0.0151 0.0304 279 ILE A O 2123 C CB . ILE A 279 ? 0.1692 0.2582 0.4705 -0.0771 -0.0122 0.0429 279 ILE A CB 2124 C CG1 . ILE A 279 ? 0.1614 0.2462 0.4681 -0.0627 -0.0037 0.0479 279 ILE A CG1 2125 C CG2 . ILE A 279 ? 0.1746 0.2652 0.4649 -0.0775 -0.0216 0.0425 279 ILE A CG2 2126 C CD1 . ILE A 279 ? 0.1612 0.2239 0.4484 -0.0585 -0.0004 0.0435 279 ILE A CD1 2127 N N . ILE A 280 ? 0.2089 0.3592 0.5259 -0.1222 -0.0318 0.0424 280 ILE A N 2128 C CA . ILE A 280 ? 0.2428 0.3886 0.5394 -0.1486 -0.0380 0.0332 280 ILE A CA 2129 C C . ILE A 280 ? 0.2534 0.4037 0.5373 -0.1464 -0.0489 0.0335 280 ILE A C 2130 O O . ILE A 280 ? 0.2481 0.4404 0.5515 -0.1383 -0.0579 0.0444 280 ILE A O 2131 C CB . ILE A 280 ? 0.2529 0.4454 0.5679 -0.1718 -0.0442 0.0366 280 ILE A CB 2132 C CG1 . ILE A 280 ? 0.2509 0.4400 0.5800 -0.1734 -0.0322 0.0375 280 ILE A CG1 2133 C CG2 . ILE A 280 ? 0.2903 0.4739 0.5757 -0.2064 -0.0500 0.0245 280 ILE A CG2 2134 C CD1 . ILE A 280 ? 0.2617 0.5000 0.6099 -0.1990 -0.0368 0.0414 280 ILE A CD1 2135 N N . SER A 281 ? 0.2772 0.3842 0.5271 -0.1510 -0.0460 0.0234 281 SER A N 2136 C CA . SER A 281 ? 0.2843 0.3882 0.5192 -0.1457 -0.0539 0.0235 281 SER A CA 2137 C C . SER A 281 ? 0.3193 0.3710 0.5118 -0.1536 -0.0468 0.0123 281 SER A C 2138 O O . SER A 281 ? 0.3233 0.3374 0.5006 -0.1497 -0.0326 0.0082 281 SER A O 2139 C CB . SER A 281 ? 0.2554 0.3599 0.5036 -0.1174 -0.0518 0.0318 281 SER A CB 2140 O OG . SER A 281 ? 0.2572 0.3620 0.4934 -0.1118 -0.0589 0.0334 281 SER A OG 2141 N N . ASN A 282 ? 0.3486 0.3981 0.5199 -0.1622 -0.0550 0.0092 282 ASN A N 2142 C CA . ASN A 282 ? 0.3897 0.3864 0.5176 -0.1629 -0.0459 0.0013 282 ASN A CA 2143 C C . ASN A 282 ? 0.3653 0.3563 0.4935 -0.1368 -0.0460 0.0077 282 ASN A C 2144 O O . ASN A 282 ? 0.3825 0.3348 0.4784 -0.1311 -0.0372 0.0049 282 ASN A O 2145 C CB . ASN A 282 ? 0.4453 0.4343 0.5402 -0.1926 -0.0522 -0.0082 282 ASN A CB 2146 C CG . ASN A 282 ? 0.4811 0.4824 0.5749 -0.2254 -0.0531 -0.0151 282 ASN A CG 2147 O OD1 . ASN A 282 ? 0.5110 0.4747 0.5896 -0.2320 -0.0372 -0.0209 282 ASN A OD1 2148 N ND2 . ASN A 282 ? 0.4860 0.5438 0.5956 -0.2462 -0.0710 -0.0129 282 ASN A ND2 2149 N N . LEU A 283 ? 0.3213 0.3481 0.4831 -0.1209 -0.0532 0.0172 283 LEU A N 2150 C CA . LEU A 283 ? 0.3022 0.3255 0.4632 -0.1014 -0.0532 0.0227 283 LEU A CA 2151 C C . LEU A 283 ? 0.2918 0.2906 0.4472 -0.0870 -0.0398 0.0237 283 LEU A C 2152 O O . LEU A 283 ? 0.2913 0.2880 0.4561 -0.0862 -0.0325 0.0234 283 LEU A O 2153 C CB . LEU A 283 ? 0.2764 0.3361 0.4671 -0.0900 -0.0602 0.0325 283 LEU A CB 2154 C CG . LEU A 283 ? 0.2848 0.3832 0.4853 -0.0984 -0.0734 0.0372 283 LEU A CG 2155 C CD1 . LEU A 283 ? 0.2690 0.3930 0.4906 -0.0782 -0.0744 0.0504 283 LEU A CD1 2156 C CD2 . LEU A 283 ? 0.3125 0.4031 0.4836 -0.1118 -0.0814 0.0316 283 LEU A CD2 2157 N N . PRO A 284 ? 0.2869 0.2717 0.4267 -0.0756 -0.0362 0.0261 284 PRO A N 2158 C CA . PRO A 284 ? 0.2777 0.2504 0.4117 -0.0624 -0.0237 0.0298 284 PRO A CA 2159 C C . PRO A 284 ? 0.2388 0.2352 0.3990 -0.0552 -0.0229 0.0347 284 PRO A C 2160 O O . PRO A 284 ? 0.2350 0.2321 0.3949 -0.0485 -0.0140 0.0378 284 PRO A O 2161 C CB . PRO A 284 ? 0.2920 0.2517 0.4041 -0.0536 -0.0212 0.0329 284 PRO A CB 2162 C CG . PRO A 284 ? 0.2913 0.2633 0.4081 -0.0588 -0.0341 0.0320 284 PRO A CG 2163 C CD . PRO A 284 ? 0.2962 0.2793 0.4218 -0.0744 -0.0428 0.0270 284 PRO A CD 2164 N N . PHE A 285 ? 0.2141 0.2283 0.3924 -0.0563 -0.0303 0.0362 285 PHE A N 2165 C CA . PHE A 285 ? 0.1904 0.2165 0.3841 -0.0527 -0.0267 0.0392 285 PHE A CA 2166 C C . PHE A 285 ? 0.1802 0.2172 0.3934 -0.0547 -0.0286 0.0400 285 PHE A C 2167 O O . PHE A 285 ? 0.1849 0.2312 0.4043 -0.0577 -0.0354 0.0409 285 PHE A O 2168 C CB . PHE A 285 ? 0.1889 0.2159 0.3771 -0.0487 -0.0265 0.0425 285 PHE A CB 2169 C CG . PHE A 285 ? 0.1956 0.2164 0.3660 -0.0448 -0.0250 0.0442 285 PHE A CG 2170 C CD1 . PHE A 285 ? 0.1932 0.2180 0.3575 -0.0412 -0.0176 0.0469 285 PHE A CD1 2171 C CD2 . PHE A 285 ? 0.2082 0.2216 0.3669 -0.0424 -0.0297 0.0450 285 PHE A CD2 2172 C CE1 . PHE A 285 ? 0.2035 0.2251 0.3512 -0.0334 -0.0133 0.0518 285 PHE A CE1 2173 C CE2 . PHE A 285 ? 0.2174 0.2225 0.3577 -0.0369 -0.0261 0.0476 285 PHE A CE2 2174 C CZ . PHE A 285 ? 0.2159 0.2249 0.3510 -0.0315 -0.0171 0.0516 285 PHE A CZ 2175 N N . GLN A 286 ? 0.1692 0.2076 0.3901 -0.0535 -0.0216 0.0408 286 GLN A N 2176 C CA . GLN A 286 ? 0.1651 0.2090 0.4007 -0.0512 -0.0188 0.0439 286 GLN A CA 2177 C C . GLN A 286 ? 0.1689 0.2015 0.3984 -0.0497 -0.0087 0.0447 286 GLN A C 2178 O O . GLN A 286 ? 0.1678 0.1963 0.3865 -0.0558 -0.0050 0.0411 286 GLN A O 2179 C CB . GLN A 286 ? 0.1604 0.2098 0.4076 -0.0549 -0.0172 0.0420 286 GLN A CB 2180 C CG . GLN A 286 ? 0.1582 0.2006 0.3987 -0.0572 -0.0107 0.0383 286 GLN A CG 2181 C CD . GLN A 286 ? 0.1568 0.1972 0.4012 -0.0570 -0.0022 0.0386 286 GLN A CD 2182 O OE1 . GLN A 286 ? 0.1647 0.2015 0.4135 -0.0536 0.0019 0.0415 286 GLN A OE1 2183 N NE2 . GLN A 286 ? 0.1548 0.1964 0.3939 -0.0592 0.0023 0.0366 286 GLN A NE2 2184 N N . ASN A 287 ? 0.1781 0.2063 0.4113 -0.0422 -0.0027 0.0505 287 ASN A N 2185 C CA . ASN A 287 ? 0.1999 0.2047 0.4182 -0.0419 0.0116 0.0508 287 ASN A CA 2186 C C . ASN A 287 ? 0.2112 0.2105 0.4365 -0.0356 0.0221 0.0547 287 ASN A C 2187 O O . ASN A 287 ? 0.2333 0.2097 0.4459 -0.0277 0.0370 0.0598 287 ASN A O 2188 C CB . ASN A 287 ? 0.2189 0.2102 0.4245 -0.0340 0.0163 0.0566 287 ASN A CB 2189 C CG . ASN A 287 ? 0.2521 0.2066 0.4323 -0.0361 0.0358 0.0560 287 ASN A CG 2190 O OD1 . ASN A 287 ? 0.2776 0.2144 0.4504 -0.0212 0.0488 0.0651 287 ASN A OD1 2191 N ND2 . ASN A 287 ? 0.2583 0.2016 0.4216 -0.0550 0.0396 0.0462 287 ASN A ND2 2192 N N . ILE A 288 ? 0.2008 0.2169 0.4428 -0.0381 0.0170 0.0530 288 ILE A N 2193 C CA . ILE A 288 ? 0.2110 0.2254 0.4618 -0.0315 0.0268 0.0576 288 ILE A CA 2194 C C . ILE A 288 ? 0.2219 0.2164 0.4581 -0.0408 0.0367 0.0499 288 ILE A C 2195 O O . ILE A 288 ? 0.2465 0.2180 0.4708 -0.0363 0.0522 0.0522 288 ILE A O 2196 C CB . ILE A 288 ? 0.1944 0.2403 0.4720 -0.0302 0.0172 0.0613 288 ILE A CB 2197 C CG1 . ILE A 288 ? 0.1947 0.2668 0.4850 -0.0225 0.0088 0.0710 288 ILE A CG1 2198 C CG2 . ILE A 288 ? 0.1985 0.2459 0.4868 -0.0240 0.0279 0.0665 288 ILE A CG2 2199 C CD1 . ILE A 288 ? 0.1817 0.2839 0.4881 -0.0335 -0.0058 0.0690 288 ILE A CD1 2200 N N . ASP A 289 ? 0.2103 0.2139 0.4446 -0.0524 0.0292 0.0421 289 ASP A N 2201 C CA . ASP A 289 ? 0.2169 0.2133 0.4396 -0.0616 0.0359 0.0363 289 ASP A CA 2202 C C . ASP A 289 ? 0.2016 0.2161 0.4197 -0.0708 0.0274 0.0320 289 ASP A C 2203 O O . ASP A 289 ? 0.1828 0.2133 0.4131 -0.0664 0.0196 0.0336 289 ASP A O 2204 C CB . ASP A 289 ? 0.2140 0.2155 0.4524 -0.0554 0.0394 0.0390 289 ASP A CB 2205 C CG . ASP A 289 ? 0.2289 0.2185 0.4517 -0.0627 0.0492 0.0341 289 ASP A CG 2206 O OD1 . ASP A 289 ? 0.2364 0.2263 0.4398 -0.0758 0.0489 0.0281 289 ASP A OD1 2207 O OD2 . ASP A 289 ? 0.2369 0.2209 0.4669 -0.0561 0.0572 0.0372 289 ASP A OD2 2208 N N . SER A 290 ? 0.2159 0.2277 0.4131 -0.0840 0.0313 0.0276 290 SER A N 2209 C CA . SER A 290 ? 0.2074 0.2466 0.4002 -0.0915 0.0247 0.0272 290 SER A CA 2210 C C . SER A 290 ? 0.1964 0.2549 0.3944 -0.0888 0.0245 0.0290 290 SER A C 2211 O O . SER A 290 ? 0.1930 0.2791 0.3906 -0.0874 0.0204 0.0332 290 SER A O 2212 C CB . SER A 290 ? 0.2314 0.2699 0.3999 -0.1115 0.0292 0.0224 290 SER A CB 2213 O OG . SER A 290 ? 0.2582 0.2821 0.4099 -0.1232 0.0388 0.0170 290 SER A OG 2214 N N . ARG A 291 ? 0.1973 0.2421 0.3988 -0.0858 0.0308 0.0277 291 ARG A N 2215 C CA . ARG A 291 ? 0.1897 0.2489 0.3949 -0.0816 0.0324 0.0299 291 ARG A CA 2216 C C . ARG A 291 ? 0.1793 0.2325 0.4037 -0.0676 0.0320 0.0334 291 ARG A C 2217 O O . ARG A 291 ? 0.1800 0.2351 0.4073 -0.0629 0.0368 0.0351 291 ARG A O 2218 C CB . ARG A 291 ? 0.2055 0.2531 0.3962 -0.0909 0.0415 0.0255 291 ARG A CB 2219 C CG . ARG A 291 ? 0.2235 0.2783 0.3878 -0.1123 0.0429 0.0201 291 ARG A CG 2220 C CD . ARG A 291 ? 0.2500 0.2856 0.3912 -0.1252 0.0536 0.0137 291 ARG A CD 2221 N NE . ARG A 291 ? 0.2389 0.2922 0.3861 -0.1178 0.0541 0.0172 291 ARG A NE 2222 C CZ . ARG A 291 ? 0.2356 0.2693 0.3950 -0.1033 0.0606 0.0193 291 ARG A CZ 2223 N NH1 . ARG A 291 ? 0.2407 0.2434 0.4098 -0.0941 0.0666 0.0197 291 ARG A NH1 2224 N NH2 . ARG A 291 ? 0.2300 0.2793 0.3921 -0.0971 0.0621 0.0228 291 ARG A NH2 2225 N N . ALA A 292 ? 0.1738 0.2205 0.4087 -0.0634 0.0269 0.0342 292 ALA A N 2226 C CA . ALA A 292 ? 0.1679 0.2111 0.4162 -0.0572 0.0259 0.0361 292 ALA A CA 2227 C C . ALA A 292 ? 0.1691 0.2170 0.4093 -0.0518 0.0285 0.0388 292 ALA A C 2228 O O . ALA A 292 ? 0.1674 0.2278 0.3963 -0.0494 0.0274 0.0418 292 ALA A O 2229 C CB . ALA A 292 ? 0.1671 0.2082 0.4221 -0.0576 0.0182 0.0361 292 ALA A CB 2230 N N . VAL A 293 ? 0.1725 0.2107 0.4170 -0.0488 0.0342 0.0395 293 VAL A N 2231 C CA . VAL A 293 ? 0.1844 0.2176 0.4156 -0.0402 0.0423 0.0438 293 VAL A CA 2232 C C . VAL A 293 ? 0.1997 0.2089 0.4274 -0.0429 0.0465 0.0417 293 VAL A C 2233 O O . VAL A 293 ? 0.1996 0.2060 0.4405 -0.0538 0.0411 0.0371 293 VAL A O 2234 C CB . VAL A 293 ? 0.1890 0.2290 0.4176 -0.0346 0.0510 0.0474 293 VAL A CB 2235 C CG1 . VAL A 293 ? 0.1827 0.2488 0.4057 -0.0367 0.0473 0.0490 293 VAL A CG1 2236 C CG2 . VAL A 293 ? 0.1874 0.2174 0.4303 -0.0399 0.0542 0.0438 293 VAL A CG2 2237 N N . GLY A 294 ? 0.2201 0.2133 0.4270 -0.0333 0.0578 0.0462 294 GLY A N 2238 C CA . GLY A 294 ? 0.2514 0.2108 0.4414 -0.0382 0.0660 0.0431 294 GLY A CA 2239 C C . GLY A 294 ? 0.2663 0.2154 0.4370 -0.0341 0.0649 0.0443 294 GLY A C 2240 O O . GLY A 294 ? 0.2612 0.2259 0.4250 -0.0189 0.0664 0.0526 294 GLY A O 2241 N N . LYS A 295 ? 0.2866 0.2133 0.4480 -0.0489 0.0623 0.0366 295 LYS A N 2242 C CA . LYS A 295 ? 0.3052 0.2169 0.4453 -0.0473 0.0613 0.0362 295 LYS A CA 2243 C C . LYS A 295 ? 0.2814 0.2181 0.4432 -0.0602 0.0412 0.0308 295 LYS A C 2244 O O . LYS A 295 ? 0.2955 0.2318 0.4640 -0.0789 0.0339 0.0236 295 LYS A O 2245 C CB . LYS A 295 ? 0.3572 0.2176 0.4605 -0.0566 0.0764 0.0309 295 LYS A CB 2246 C CG . LYS A 295 ? 0.3914 0.2190 0.4677 -0.0400 0.1015 0.0384 295 LYS A CG 2247 C CD . LYS A 295 ? 0.4550 0.2214 0.4905 -0.0554 0.1203 0.0305 295 LYS A CD 2248 C CE . LYS A 295 ? 0.4950 0.2240 0.5005 -0.0342 0.1494 0.0404 295 LYS A CE 2249 N NZ . LYS A 295 ? 0.5765 0.2292 0.5246 -0.0430 0.1755 0.0350 295 LYS A NZ 2250 N N . CYS A 296 ? 0.2559 0.2179 0.4281 -0.0507 0.0330 0.0354 296 CYS A N 2251 C CA . CYS A 296 ? 0.2312 0.2171 0.4249 -0.0583 0.0172 0.0327 296 CYS A CA 2252 C C . CYS A 296 ? 0.2329 0.2191 0.4158 -0.0550 0.0114 0.0338 296 CYS A C 2253 O O . CYS A 296 ? 0.2385 0.2172 0.4031 -0.0433 0.0192 0.0391 296 CYS A O 2254 C CB . CYS A 296 ? 0.2051 0.2162 0.4185 -0.0536 0.0150 0.0359 296 CYS A CB 2255 S SG . CYS A 296 ? 0.2010 0.2147 0.4298 -0.0561 0.0210 0.0352 296 CYS A SG 2256 N N . PRO A 297 ? 0.2256 0.2234 0.4200 -0.0629 -0.0009 0.0310 297 PRO A N 2257 C CA . PRO A 297 ? 0.2245 0.2278 0.4137 -0.0582 -0.0066 0.0332 297 PRO A CA 2258 C C . PRO A 297 ? 0.2109 0.2314 0.4067 -0.0502 -0.0039 0.0382 297 PRO A C 2259 O O . PRO A 297 ? 0.2023 0.2327 0.4102 -0.0511 -0.0013 0.0385 297 PRO A O 2260 C CB . PRO A 297 ? 0.2168 0.2341 0.4213 -0.0654 -0.0181 0.0318 297 PRO A CB 2261 C CG . PRO A 297 ? 0.2211 0.2420 0.4351 -0.0765 -0.0197 0.0288 297 PRO A CG 2262 C CD . PRO A 297 ? 0.2205 0.2321 0.4346 -0.0740 -0.0088 0.0284 297 PRO A CD 2263 N N . ARG A 298 ? 0.2157 0.2409 0.4016 -0.0447 -0.0038 0.0421 298 ARG A N 2264 C CA . ARG A 298 ? 0.2067 0.2543 0.3967 -0.0435 -0.0019 0.0464 298 ARG A CA 2265 C C . ARG A 298 ? 0.1864 0.2376 0.3873 -0.0524 -0.0065 0.0427 298 ARG A C 2266 O O . ARG A 298 ? 0.1841 0.2264 0.3863 -0.0533 -0.0116 0.0411 298 ARG A O 2267 C CB . ARG A 298 ? 0.2245 0.2815 0.4020 -0.0367 0.0001 0.0531 298 ARG A CB 2268 C CG . ARG A 298 ? 0.2491 0.3169 0.4160 -0.0232 0.0104 0.0629 298 ARG A CG 2269 C CD . ARG A 298 ? 0.2882 0.3228 0.4379 -0.0140 0.0188 0.0629 298 ARG A CD 2270 N NE . ARG A 298 ? 0.3210 0.3271 0.4588 -0.0186 0.0144 0.0565 298 ARG A NE 2271 C CZ . ARG A 298 ? 0.3595 0.3324 0.4837 -0.0246 0.0163 0.0494 298 ARG A CZ 2272 N NH1 . ARG A 298 ? 0.3636 0.3224 0.4846 -0.0257 0.0243 0.0476 298 ARG A NH1 2273 N NH2 . ARG A 298 ? 0.3781 0.3325 0.4897 -0.0319 0.0104 0.0437 298 ARG A NH2 2274 N N . TYR A 299 ? 0.1735 0.2355 0.3779 -0.0581 -0.0027 0.0421 299 TYR A N 2275 C CA . TYR A 299 ? 0.1733 0.2278 0.3782 -0.0664 -0.0014 0.0388 299 TYR A CA 2276 C C . TYR A 299 ? 0.1798 0.2369 0.3735 -0.0720 -0.0012 0.0396 299 TYR A C 2277 O O . TYR A 299 ? 0.1781 0.2567 0.3656 -0.0764 -0.0005 0.0426 299 TYR A O 2278 C CB . TYR A 299 ? 0.1750 0.2324 0.3786 -0.0745 0.0050 0.0361 299 TYR A CB 2279 C CG . TYR A 299 ? 0.1908 0.2277 0.3851 -0.0828 0.0117 0.0325 299 TYR A CG 2280 C CD1 . TYR A 299 ? 0.1978 0.2150 0.3987 -0.0749 0.0152 0.0335 299 TYR A CD1 2281 C CD2 . TYR A 299 ? 0.2070 0.2438 0.3829 -0.0985 0.0167 0.0294 299 TYR A CD2 2282 C CE1 . TYR A 299 ? 0.2221 0.2131 0.4087 -0.0773 0.0265 0.0328 299 TYR A CE1 2283 C CE2 . TYR A 299 ? 0.2359 0.2412 0.3939 -0.1069 0.0278 0.0255 299 TYR A CE2 2284 C CZ . TYR A 299 ? 0.2449 0.2238 0.4069 -0.0937 0.0341 0.0278 299 TYR A CZ 2285 O OH . TYR A 299 ? 0.2812 0.2220 0.4199 -0.0973 0.0500 0.0264 299 TYR A OH 2286 N N . VAL A 300 ? 0.1866 0.2252 0.3777 -0.0712 -0.0008 0.0389 300 VAL A N 2287 C CA . VAL A 300 ? 0.1989 0.2316 0.3761 -0.0782 0.0027 0.0390 300 VAL A CA 2288 C C . VAL A 300 ? 0.2218 0.2262 0.3879 -0.0831 0.0133 0.0365 300 VAL A C 2289 O O . VAL A 300 ? 0.2208 0.2129 0.3938 -0.0745 0.0162 0.0377 300 VAL A O 2290 C CB . VAL A 300 ? 0.1977 0.2278 0.3741 -0.0685 -0.0033 0.0427 300 VAL A CB 2291 C CG1 . VAL A 300 ? 0.1871 0.2336 0.3663 -0.0618 -0.0091 0.0455 300 VAL A CG1 2292 C CG2 . VAL A 300 ? 0.2021 0.2182 0.3848 -0.0578 -0.0059 0.0445 300 VAL A CG2 2293 N N . LYS A 301 ? 0.2469 0.2397 0.3930 -0.0965 0.0214 0.0342 301 LYS A N 2294 C CA . LYS A 301 ? 0.2880 0.2419 0.4117 -0.1031 0.0376 0.0315 301 LYS A CA 2295 C C . LYS A 301 ? 0.3011 0.2297 0.4215 -0.0848 0.0428 0.0383 301 LYS A C 2296 O O . LYS A 301 ? 0.3345 0.2276 0.4381 -0.0802 0.0590 0.0400 301 LYS A O 2297 C CB . LYS A 301 ? 0.3205 0.2676 0.4175 -0.1295 0.0465 0.0255 301 LYS A CB 2298 C CG . LYS A 301 ? 0.3269 0.2989 0.4187 -0.1527 0.0454 0.0193 301 LYS A CG 2299 C CD . LYS A 301 ? 0.3620 0.3373 0.4274 -0.1844 0.0524 0.0138 301 LYS A CD 2300 C CE . LYS A 301 ? 0.3579 0.3506 0.4293 -0.1808 0.0470 0.0197 301 LYS A CE 2301 N NZ . LYS A 301 ? 0.3832 0.3968 0.4357 -0.2136 0.0510 0.0164 301 LYS A NZ 2302 N N . GLN A 302 ? 0.2844 0.2299 0.4168 -0.0734 0.0313 0.0433 302 GLN A N 2303 C CA . GLN A 302 ? 0.3006 0.2307 0.4298 -0.0554 0.0345 0.0515 302 GLN A CA 2304 C C . GLN A 302 ? 0.2951 0.2378 0.4449 -0.0371 0.0293 0.0584 302 GLN A C 2305 O O . GLN A 302 ? 0.2651 0.2339 0.4351 -0.0385 0.0167 0.0560 302 GLN A O 2306 C CB . GLN A 302 ? 0.2891 0.2347 0.4210 -0.0516 0.0233 0.0540 302 GLN A CB 2307 C CG . GLN A 302 ? 0.2967 0.2405 0.4126 -0.0684 0.0272 0.0499 302 GLN A CG 2308 C CD . GLN A 302 ? 0.2698 0.2489 0.3978 -0.0781 0.0163 0.0468 302 GLN A CD 2309 O OE1 . GLN A 302 ? 0.2528 0.2469 0.3930 -0.0796 0.0119 0.0444 302 GLN A OE1 2310 N NE2 . GLN A 302 ? 0.2658 0.2583 0.3889 -0.0822 0.0142 0.0489 302 GLN A NE2 2311 N N . ARG A 303 ? 0.3257 0.2518 0.4690 -0.0196 0.0405 0.0686 303 ARG A N 2312 C CA . ARG A 303 ? 0.3247 0.2738 0.4893 -0.0012 0.0360 0.0791 303 ARG A CA 2313 C C . ARG A 303 ? 0.3002 0.2857 0.4816 0.0051 0.0165 0.0837 303 ARG A C 2314 O O . ARG A 303 ? 0.2804 0.2989 0.4836 0.0090 0.0053 0.0878 303 ARG A O 2315 C CB . ARG A 303 ? 0.3789 0.3027 0.5296 0.0200 0.0578 0.0928 303 ARG A CB 2316 C CG . ARG A 303 ? 0.4215 0.3294 0.5538 0.0351 0.0663 0.1030 303 ARG A CG 2317 C CD . ARG A 303 ? 0.4750 0.3698 0.5983 0.0658 0.0874 0.1231 303 ARG A CD 2318 N NE . ARG A 303 ? 0.4661 0.4194 0.6202 0.0862 0.0725 0.1394 303 ARG A NE 2319 C CZ . ARG A 303 ? 0.4728 0.4595 0.6505 0.0978 0.0714 0.1498 303 ARG A CZ 2320 N NH1 . ARG A 303 ? 0.4842 0.4472 0.6585 0.0951 0.0855 0.1463 303 ARG A NH1 2321 N NH2 . ARG A 303 ? 0.4669 0.5153 0.6715 0.1108 0.0557 0.1645 303 ARG A NH2 2322 N N . SER A 304 ? 0.2978 0.2766 0.4662 0.0035 0.0131 0.0825 304 SER A N 2323 C CA . SER A 304 ? 0.2854 0.2918 0.4611 0.0095 -0.0029 0.0871 304 SER A CA 2324 C C . SER A 304 ? 0.2822 0.2783 0.4429 0.0014 -0.0077 0.0809 304 SER A C 2325 O O . SER A 304 ? 0.2977 0.2664 0.4399 -0.0004 0.0047 0.0801 304 SER A O 2326 C CB . SER A 304 ? 0.3060 0.3210 0.4803 0.0327 0.0032 0.1043 304 SER A CB 2327 O OG . SER A 304 ? 0.3032 0.3419 0.4770 0.0366 -0.0111 0.1085 304 SER A OG 2328 N N . LEU A 305 ? 0.2636 0.2796 0.4292 -0.0043 -0.0239 0.0768 305 LEU A N 2329 C CA . LEU A 305 ? 0.2639 0.2717 0.4144 -0.0083 -0.0279 0.0730 305 LEU A CA 2330 C C . LEU A 305 ? 0.2650 0.2918 0.4137 -0.0067 -0.0428 0.0745 305 LEU A C 2331 O O . LEU A 305 ? 0.2563 0.2920 0.4075 -0.0171 -0.0520 0.0677 305 LEU A O 2332 C CB . LEU A 305 ? 0.2497 0.2527 0.3990 -0.0212 -0.0275 0.0637 305 LEU A CB 2333 C CG . LEU A 305 ? 0.2491 0.2410 0.3964 -0.0294 -0.0151 0.0609 305 LEU A CG 2334 C CD1 . LEU A 305 ? 0.2317 0.2346 0.3828 -0.0387 -0.0172 0.0555 305 LEU A CD1 2335 C CD2 . LEU A 305 ? 0.2653 0.2398 0.3953 -0.0304 -0.0048 0.0634 305 LEU A CD2 2336 N N . LEU A 306 ? 0.2796 0.3103 0.4197 0.0052 -0.0437 0.0835 306 LEU A N 2337 C CA . LEU A 306 ? 0.2860 0.3406 0.4217 0.0048 -0.0586 0.0859 306 LEU A CA 2338 C C . LEU A 306 ? 0.2931 0.3309 0.4066 -0.0031 -0.0635 0.0780 306 LEU A C 2339 O O . LEU A 306 ? 0.2968 0.3121 0.3975 0.0020 -0.0551 0.0785 306 LEU A O 2340 C CB . LEU A 306 ? 0.3007 0.3726 0.4354 0.0238 -0.0572 0.1017 306 LEU A CB 2341 C CG . LEU A 306 ? 0.3006 0.3908 0.4541 0.0373 -0.0494 0.1139 306 LEU A CG 2342 C CD1 . LEU A 306 ? 0.3216 0.4300 0.4705 0.0620 -0.0449 0.1336 306 LEU A CD1 2343 C CD2 . LEU A 306 ? 0.2863 0.4137 0.4614 0.0253 -0.0617 0.1116 306 LEU A CD2 2344 N N . LEU A 307 ? 0.2989 0.3459 0.4053 -0.0166 -0.0752 0.0709 307 LEU A N 2345 C CA . LEU A 307 ? 0.3151 0.3398 0.3935 -0.0242 -0.0773 0.0633 307 LEU A CA 2346 C C . LEU A 307 ? 0.3387 0.3793 0.3997 -0.0260 -0.0893 0.0663 307 LEU A C 2347 O O . LEU A 307 ? 0.3453 0.4176 0.4116 -0.0368 -0.1012 0.0666 307 LEU A O 2348 C CB . LEU A 307 ? 0.3175 0.3308 0.3900 -0.0405 -0.0779 0.0522 307 LEU A CB 2349 C CG . LEU A 307 ? 0.3459 0.3251 0.3824 -0.0471 -0.0743 0.0444 307 LEU A CG 2350 C CD1 . LEU A 307 ? 0.3390 0.2953 0.3710 -0.0337 -0.0602 0.0474 307 LEU A CD1 2351 C CD2 . LEU A 307 ? 0.3610 0.3280 0.3862 -0.0655 -0.0742 0.0341 307 LEU A CD2 2352 N N . ALA A 308 ? 0.3532 0.3763 0.3931 -0.0169 -0.0862 0.0691 308 ALA A N 2353 C CA . ALA A 308 ? 0.3771 0.4142 0.3959 -0.0181 -0.0973 0.0722 308 ALA A CA 2354 C C . ALA A 308 ? 0.4014 0.4337 0.3951 -0.0429 -0.1068 0.0595 308 ALA A C 2355 O O . ALA A 308 ? 0.4120 0.4062 0.3876 -0.0515 -0.0985 0.0489 308 ALA A O 2356 C CB . ALA A 308 ? 0.3910 0.4019 0.3881 -0.0045 -0.0897 0.0760 308 ALA A CB 2357 N N . THR A 309 ? 0.4136 0.4852 0.4037 -0.0548 -0.1224 0.0616 309 THR A N 2358 C CA . THR A 309 ? 0.4493 0.5157 0.4066 -0.0852 -0.1317 0.0482 309 THR A CA 2359 C C . THR A 309 ? 0.4819 0.5693 0.4116 -0.0903 -0.1444 0.0516 309 THR A C 2360 O O . THR A 309 ? 0.5152 0.6175 0.4191 -0.1197 -0.1566 0.0429 309 THR A O 2361 C CB . THR A 309 ? 0.4407 0.5443 0.4187 -0.1068 -0.1406 0.0449 309 THR A CB 2362 O OG1 . THR A 309 ? 0.4186 0.5884 0.4326 -0.0946 -0.1507 0.0619 309 THR A OG1 2363 C CG2 . THR A 309 ? 0.4171 0.4923 0.4138 -0.1043 -0.1273 0.0394 309 THR A CG2 2364 N N . GLY A 310 ? 0.4754 0.5625 0.4070 -0.0636 -0.1405 0.0638 310 GLY A N 2365 C CA . GLY A 310 ? 0.5057 0.6109 0.4105 -0.0630 -0.1507 0.0691 310 GLY A CA 2366 C C . GLY A 310 ? 0.5046 0.5756 0.4010 -0.0349 -0.1376 0.0767 310 GLY A C 2367 O O . GLY A 310 ? 0.4760 0.5219 0.3931 -0.0170 -0.1224 0.0799 310 GLY A O 2368 N N . MET A 311 ? 0.5376 0.6096 0.4016 -0.0335 -0.1435 0.0794 311 MET A N 2369 C CA . MET A 311 ? 0.5424 0.5854 0.3951 -0.0077 -0.1315 0.0878 311 MET A CA 2370 C C . MET A 311 ? 0.5180 0.5878 0.4060 0.0221 -0.1251 0.1072 311 MET A C 2371 O O . MET A 311 ? 0.4998 0.6150 0.4179 0.0252 -0.1311 0.1162 311 MET A O 2372 C CB . MET A 311 ? 0.5848 0.6296 0.3940 -0.0132 -0.1408 0.0876 311 MET A CB 2373 C CG . MET A 311 ? 0.5916 0.7083 0.4082 -0.0122 -0.1593 0.1014 311 MET A CG 2374 S SD . MET A 311 ? 0.6452 0.7647 0.4059 -0.0213 -0.1708 0.1003 311 MET A SD 2375 C CE . MET A 311 ? 0.6862 0.7812 0.4030 -0.0725 -0.1802 0.0729 311 MET A CE 2376 N N . LYS A 312 ? 0.5265 0.5646 0.4072 0.0438 -0.1104 0.1143 312 LYS A N 2377 C CA . LYS A 312 ? 0.5226 0.5718 0.4237 0.0719 -0.0993 0.1325 312 LYS A CA 2378 C C . LYS A 312 ? 0.5432 0.6452 0.4409 0.0851 -0.1108 0.1498 312 LYS A C 2379 O O . LYS A 312 ? 0.5714 0.6876 0.4404 0.0776 -0.1237 0.1486 312 LYS A O 2380 C CB . LYS A 312 ? 0.5355 0.5376 0.4214 0.0870 -0.0808 0.1351 312 LYS A CB 2381 C CG . LYS A 312 ? 0.5397 0.5376 0.4385 0.1127 -0.0636 0.1519 312 LYS A CG 2382 C CD . LYS A 312 ? 0.5637 0.5215 0.4401 0.1247 -0.0477 0.1555 312 LYS A CD 2383 C CE . LYS A 312 ? 0.5783 0.5207 0.4596 0.1471 -0.0262 0.1708 312 LYS A CE 2384 N NZ . LYS A 312 ? 0.5968 0.4945 0.4605 0.1498 -0.0079 0.1700 312 LYS A NZ 2385 N N . ASN A 313 ? 0.5339 0.6654 0.4582 0.1059 -0.1045 0.1671 313 ASN A N 2386 C CA . ASN A 313 ? 0.5530 0.7441 0.4783 0.1247 -0.1128 0.1890 313 ASN A CA 2387 C C . ASN A 313 ? 0.5799 0.7488 0.4863 0.1572 -0.0961 0.2061 313 ASN A C 2388 O O . ASN A 313 ? 0.5772 0.7059 0.4895 0.1772 -0.0719 0.2131 313 ASN A O 2389 C CB . ASN A 313 ? 0.5351 0.7712 0.4958 0.1360 -0.1112 0.2033 313 ASN A CB 2390 C CG . ASN A 313 ? 0.5522 0.8699 0.5174 0.1519 -0.1240 0.2276 313 ASN A CG 2391 O OD1 . ASN A 313 ? 0.5653 0.9292 0.5179 0.1303 -0.1476 0.2234 313 ASN A OD1 2392 N ND2 . ASN A 313 ? 0.5565 0.8928 0.5363 0.1896 -0.1070 0.2543 313 ASN A ND2 2393 N N . VAL A 314 ? 0.6106 0.8032 0.4902 0.1597 -0.1082 0.2120 314 VAL A N 2394 C CA . VAL A 314 ? 0.6407 0.8132 0.4971 0.1898 -0.0937 0.2282 314 VAL A CA 2395 C C . VAL A 314 ? 0.6657 0.9135 0.5181 0.2096 -0.1061 0.2530 314 VAL A C 2396 O O . VAL A 314 ? 0.6891 0.9630 0.5151 0.1997 -0.1236 0.2516 314 VAL A O 2397 C CB . VAL A 314 ? 0.6573 0.7812 0.4788 0.1764 -0.0942 0.2123 314 VAL A CB 2398 C CG1 . VAL A 314 ? 0.6837 0.7733 0.4850 0.2078 -0.0730 0.2279 314 VAL A CG1 2399 C CG2 . VAL A 314 ? 0.6352 0.7053 0.4620 0.1521 -0.0881 0.1883 314 VAL A CG2 2400 N N . PRO A 315 ? 0.6660 0.9505 0.5420 0.2389 -0.0957 0.2776 315 PRO A N 2401 C CA . PRO A 315 ? 0.6880 1.0609 0.5665 0.2596 -0.1082 0.3054 315 PRO A CA 2402 C C . PRO A 315 ? 0.7295 1.0997 0.5772 0.2939 -0.0976 0.3270 315 PRO A C 2403 O O . PRO A 315 ? 0.7426 1.0359 0.5684 0.3034 -0.0770 0.3209 315 PRO A O 2404 C CB . PRO A 315 ? 0.6764 1.0759 0.5879 0.2866 -0.0925 0.3270 315 PRO A CB 2405 C CG . PRO A 315 ? 0.6583 0.9707 0.5771 0.2824 -0.0683 0.3103 315 PRO A CG 2406 C CD . PRO A 315 ? 0.6562 0.8970 0.5506 0.2590 -0.0672 0.2839 315 PRO A CD 2407 N N . GLU A 316 ? 0.7535 1.2125 0.6002 0.3118 -0.1116 0.3531 316 GLU A N 2408 C CA . GLU A 316 ? 0.7977 1.2677 0.6159 0.3499 -0.1018 0.3793 316 GLU A CA 2409 C C . GLU A 316 ? 0.8195 1.2368 0.6351 0.4014 -0.0602 0.4042 316 GLU A C 2410 O O . GLU A 316 ? 0.8554 1.2399 0.6409 0.4311 -0.0420 0.4186 316 GLU A O 2411 C CB . GLU A 316 ? 0.8157 1.4090 0.6380 0.3586 -0.1268 0.4058 316 GLU A CB 2412 C CG . GLU A 316 ? 0.8313 1.4618 0.6255 0.3186 -0.1607 0.3882 316 GLU A CG 2413 C CD . GLU A 316 ? 0.8712 1.4761 0.6230 0.3410 -0.1536 0.3976 316 GLU A CD 2414 O OE1 . GLU A 316 ? 0.8980 1.5712 0.6433 0.3786 -0.1527 0.4329 316 GLU A OE1 2415 O OE2 . GLU A 316 ? 0.8772 1.3960 0.6016 0.3224 -0.1481 0.3714 316 GLU A OE2 2416 N N . ILE A 317 ? 0.8096 1.2116 0.6486 0.4144 -0.0416 0.4107 317 ILE A N 2417 N N . GLY B 1 ? 0.7856 1.1199 0.4336 -0.2905 -0.2098 0.3709 1 GLY B N 2418 C CA . GLY B 1 ? 0.7602 1.1376 0.4276 -0.2793 -0.1961 0.3683 1 GLY B CA 2419 C C . GLY B 1 ? 0.7523 1.2149 0.4411 -0.2838 -0.1869 0.3944 1 GLY B C 2420 O O . GLY B 1 ? 0.7670 1.2583 0.4585 -0.3030 -0.1914 0.4192 1 GLY B O 2421 N N . LEU B 2 ? 0.7340 1.2381 0.4338 -0.2626 -0.1731 0.3892 2 LEU B N 2422 C CA . LEU B 2 ? 0.7297 1.3281 0.4512 -0.2583 -0.1630 0.4139 2 LEU B CA 2423 C C . LEU B 2 ? 0.7311 1.3729 0.4446 -0.2367 -0.1436 0.4186 2 LEU B C 2424 O O . LEU B 2 ? 0.7364 1.4602 0.4671 -0.2425 -0.1370 0.4489 2 LEU B O 2425 C CB . LEU B 2 ? 0.7197 1.3419 0.4444 -0.2302 -0.1544 0.4022 2 LEU B CB 2426 C CG . LEU B 2 ? 0.7232 1.3159 0.4553 -0.2477 -0.1734 0.4011 2 LEU B CG 2427 C CD1 . LEU B 2 ? 0.7195 1.3196 0.4426 -0.2116 -0.1632 0.3831 2 LEU B CD1 2428 C CD2 . LEU B 2 ? 0.7345 1.3836 0.4978 -0.2883 -0.1934 0.4386 2 LEU B CD2 2429 N N . PHE B 3 ? 0.7310 1.3210 0.4173 -0.2128 -0.1354 0.3904 3 PHE B N 2430 C CA . PHE B 3 ? 0.7421 1.3593 0.4094 -0.1856 -0.1196 0.3894 3 PHE B CA 2431 C C . PHE B 3 ? 0.7556 1.3621 0.4168 -0.2044 -0.1253 0.4017 3 PHE B C 2432 O O . PHE B 3 ? 0.7713 1.3969 0.4129 -0.1831 -0.1141 0.4027 3 PHE B O 2433 C CB . PHE B 3 ? 0.7469 1.3133 0.3815 -0.1506 -0.1120 0.3538 3 PHE B CB 2434 C CG . PHE B 3 ? 0.7490 1.3233 0.3762 -0.1262 -0.1058 0.3437 3 PHE B CG 2435 C CD1 . PHE B 3 ? 0.7378 1.2711 0.3732 -0.1393 -0.1144 0.3323 3 PHE B CD1 2436 C CD2 . PHE B 3 ? 0.7694 1.3918 0.3754 -0.0856 -0.0919 0.3468 3 PHE B CD2 2437 C CE1 . PHE B 3 ? 0.7470 1.2828 0.3701 -0.1156 -0.1102 0.3234 3 PHE B CE1 2438 C CE2 . PHE B 3 ? 0.7804 1.4059 0.3719 -0.0578 -0.0884 0.3370 3 PHE B CE2 2439 C CZ . PHE B 3 ? 0.7687 1.3496 0.3694 -0.0745 -0.0981 0.3254 3 PHE B CZ 2440 N N . GLY B 4 ? 0.7620 1.3312 0.4313 -0.2408 -0.1446 0.4108 4 GLY B N 2441 C CA . GLY B 4 ? 0.7865 1.3464 0.4451 -0.2629 -0.1539 0.4300 4 GLY B CA 2442 C C . GLY B 4 ? 0.7952 1.3133 0.4266 -0.2427 -0.1520 0.4091 4 GLY B C 2443 O O . GLY B 4 ? 0.8189 1.3448 0.4353 -0.2488 -0.1531 0.4256 4 GLY B O 2444 N N . ALA B 5 ? 0.7806 1.2555 0.4049 -0.2213 -0.1506 0.3746 5 ALA B N 2445 C CA . ALA B 5 ? 0.7897 1.2301 0.3930 -0.2044 -0.1525 0.3536 5 ALA B CA 2446 C C . ALA B 5 ? 0.7925 1.1753 0.3953 -0.2161 -0.1702 0.3395 5 ALA B C 2447 O O . ALA B 5 ? 0.8143 1.1756 0.4016 -0.2214 -0.1821 0.3450 5 ALA B O 2448 C CB . ALA B 5 ? 0.7835 1.2198 0.3756 -0.1749 -0.1414 0.3277 5 ALA B CB 2449 N N . ILE B 6 ? 0.7763 1.1348 0.3912 -0.2162 -0.1716 0.3221 6 ILE B N 2450 C CA . ILE B 6 ? 0.7826 1.0949 0.3955 -0.2201 -0.1856 0.3093 6 ILE B CA 2451 C C . ILE B 6 ? 0.8098 1.0976 0.4133 -0.2417 -0.2026 0.3302 6 ILE B C 2452 O O . ILE B 6 ? 0.8083 1.1075 0.4208 -0.2567 -0.2032 0.3443 6 ILE B O 2453 C CB . ILE B 6 ? 0.7616 1.0598 0.3868 -0.2127 -0.1788 0.2873 6 ILE B CB 2454 C CG1 . ILE B 6 ? 0.7517 1.0603 0.3780 -0.1983 -0.1683 0.2675 6 ILE B CG1 2455 C CG2 . ILE B 6 ? 0.7715 1.0322 0.3928 -0.2113 -0.1907 0.2777 6 ILE B CG2 2456 C CD1 . ILE B 6 ? 0.7402 1.0372 0.3733 -0.1966 -0.1595 0.2514 6 ILE B CD1 2457 N N . ALA B 7 ? 0.8440 1.0932 0.4240 -0.2427 -0.2199 0.3318 7 ALA B N 2458 C CA . ALA B 7 ? 0.8907 1.1002 0.4442 -0.2656 -0.2425 0.3545 7 ALA B CA 2459 C C . ALA B 7 ? 0.8997 1.1523 0.4593 -0.2923 -0.2392 0.3878 7 ALA B C 2460 O O . ALA B 7 ? 0.9223 1.1681 0.4790 -0.3218 -0.2527 0.4110 7 ALA B O 2461 C CB . ALA B 7 ? 0.9018 1.0702 0.4491 -0.2709 -0.2546 0.3501 7 ALA B CB 2462 N N . GLY B 8 ? 0.8872 1.1873 0.4540 -0.2812 -0.2220 0.3907 8 GLY B N 2463 C CA . GLY B 8 ? 0.8964 1.2551 0.4701 -0.2982 -0.2123 0.4230 8 GLY B CA 2464 C C . GLY B 8 ? 0.9211 1.2845 0.4709 -0.2871 -0.2081 0.4280 8 GLY B C 2465 O O . GLY B 8 ? 0.9590 1.2664 0.4768 -0.2901 -0.2265 0.4268 8 GLY B O 2466 N N . PHE B 9 ? 0.9087 1.3330 0.4664 -0.2689 -0.1854 0.4322 9 PHE B N 2467 C CA . PHE B 9 ? 0.9383 1.3676 0.4674 -0.2555 -0.1807 0.4385 9 PHE B CA 2468 C C . PHE B 9 ? 0.9419 1.3180 0.4519 -0.2293 -0.1905 0.4039 9 PHE B C 2469 O O . PHE B 9 ? 0.9760 1.3311 0.4550 -0.2227 -0.1974 0.4073 9 PHE B O 2470 C CB . PHE B 9 ? 0.9326 1.4383 0.4654 -0.2353 -0.1542 0.4515 9 PHE B CB 2471 C CG . PHE B 9 ? 0.9091 1.4182 0.4414 -0.1952 -0.1420 0.4180 9 PHE B CG 2472 C CD1 . PHE B 9 ? 0.9277 1.4086 0.4292 -0.1668 -0.1434 0.3967 9 PHE B CD1 2473 C CD2 . PHE B 9 ? 0.8802 1.4152 0.4358 -0.1868 -0.1321 0.4091 9 PHE B CD2 2474 C CE1 . PHE B 9 ? 0.9200 1.3925 0.4122 -0.1354 -0.1378 0.3677 9 PHE B CE1 2475 C CE2 . PHE B 9 ? 0.8735 1.3975 0.4165 -0.1525 -0.1245 0.3797 9 PHE B CE2 2476 C CZ . PHE B 9 ? 0.8953 1.3855 0.4052 -0.1290 -0.1285 0.3596 9 PHE B CZ 2477 N N . ILE B 10 ? 0.9114 1.2700 0.4401 -0.2157 -0.1915 0.3727 10 ILE B N 2478 C CA . ILE B 10 ? 0.9164 1.2325 0.4366 -0.1995 -0.2051 0.3442 10 ILE B CA 2479 C C . ILE B 10 ? 0.9402 1.2070 0.4503 -0.2135 -0.2261 0.3474 10 ILE B C 2480 O O . ILE B 10 ? 0.9285 1.1841 0.4534 -0.2251 -0.2287 0.3469 10 ILE B O 2481 C CB . ILE B 10 ? 0.8814 1.2021 0.4249 -0.1841 -0.1986 0.3133 10 ILE B CB 2482 C CG1 . ILE B 10 ? 0.8790 1.2279 0.4148 -0.1659 -0.1840 0.3072 10 ILE B CG1 2483 C CG2 . ILE B 10 ? 0.8856 1.1791 0.4290 -0.1724 -0.2138 0.2893 10 ILE B CG2 2484 C CD1 . ILE B 10 ? 0.8623 1.2434 0.4103 -0.1665 -0.1668 0.3158 10 ILE B CD1 2485 N N . GLU B 11 ? 0.9834 1.2141 0.4597 -0.2083 -0.2427 0.3500 11 GLU B N 2486 C CA . GLU B 11 ? 1.0277 1.1964 0.4738 -0.2143 -0.2672 0.3536 11 GLU B CA 2487 C C . GLU B 11 ? 1.0058 1.1564 0.4685 -0.2003 -0.2727 0.3286 11 GLU B C 2488 O O . GLU B 11 ? 1.0262 1.1389 0.4759 -0.2120 -0.2844 0.3356 11 GLU B O 2489 C CB . GLU B 11 ? 1.0782 1.2120 0.4825 -0.1971 -0.2836 0.3506 11 GLU B CB 2490 C CG . GLU B 11 ? 1.1533 1.2097 0.5026 -0.2046 -0.3120 0.3636 11 GLU B CG 2491 C CD . GLU B 11 ? 1.2042 1.2431 0.5192 -0.2407 -0.3168 0.4034 11 GLU B CD 2492 O OE1 . GLU B 11 ? 1.1945 1.2563 0.5292 -0.2741 -0.3098 0.4262 11 GLU B OE1 2493 O OE2 . GLU B 11 ? 1.2592 1.2644 0.5273 -0.2367 -0.3283 0.4134 11 GLU B OE2 2494 N N . ASN B 12 ? 0.9703 1.1480 0.4586 -0.1762 -0.2654 0.3012 12 ASN B N 2495 C CA . ASN B 12 ? 0.9534 1.1271 0.4591 -0.1602 -0.2676 0.2793 12 ASN B CA 2496 C C . ASN B 12 ? 0.9070 1.1302 0.4532 -0.1485 -0.2542 0.2562 12 ASN B C 2497 O O . ASN B 12 ? 0.8967 1.1448 0.4488 -0.1485 -0.2486 0.2535 12 ASN B O 2498 C CB . ASN B 12 ? 1.0052 1.1321 0.4725 -0.1376 -0.2913 0.2733 12 ASN B CB 2499 C CG . ASN B 12 ? 1.0221 1.1581 0.4778 -0.1173 -0.3005 0.2643 12 ASN B CG 2500 O OD1 . ASN B 12 ? 1.0643 1.1698 0.4810 -0.1220 -0.3113 0.2795 12 ASN B OD1 2501 N ND2 . ASN B 12 ? 0.9939 1.1743 0.4832 -0.0969 -0.2971 0.2413 12 ASN B ND2 2502 N N . GLY B 13 ? 0.8887 1.1223 0.4571 -0.1393 -0.2508 0.2411 13 GLY B N 2503 C CA . GLY B 13 ? 0.8543 1.1342 0.4614 -0.1359 -0.2406 0.2226 13 GLY B CA 2504 C C . GLY B 13 ? 0.8668 1.1698 0.4802 -0.1148 -0.2539 0.2087 13 GLY B C 2505 O O . GLY B 13 ? 0.9022 1.1810 0.4869 -0.0947 -0.2703 0.2101 13 GLY B O 2506 N N . TRP B 14 ? 0.8448 1.1926 0.4924 -0.1200 -0.2496 0.1957 14 TRP B N 2507 C CA . TRP B 14 ? 0.8536 1.2404 0.5185 -0.1043 -0.2634 0.1829 14 TRP B CA 2508 C C . TRP B 14 ? 0.8390 1.2742 0.5419 -0.0979 -0.2562 0.1751 14 TRP B C 2509 O O . TRP B 14 ? 0.8144 1.2701 0.5445 -0.1192 -0.2408 0.1741 14 TRP B O 2510 C CB . TRP B 14 ? 0.8504 1.2558 0.5253 -0.1190 -0.2688 0.1760 14 TRP B CB 2511 C CG . TRP B 14 ? 0.8722 1.2376 0.5063 -0.1187 -0.2733 0.1841 14 TRP B CG 2512 C CD1 . TRP B 14 ? 0.8997 1.2290 0.4952 -0.1058 -0.2798 0.1960 14 TRP B CD1 2513 C CD2 . TRP B 14 ? 0.8776 1.2339 0.4985 -0.1302 -0.2719 0.1825 14 TRP B CD2 2514 N NE1 . TRP B 14 ? 0.9155 1.2255 0.4817 -0.1098 -0.2787 0.2041 14 TRP B NE1 2515 C CE2 . TRP B 14 ? 0.9035 1.2289 0.4823 -0.1203 -0.2738 0.1946 14 TRP B CE2 2516 C CE3 . TRP B 14 ? 0.8729 1.2379 0.5054 -0.1471 -0.2708 0.1728 14 TRP B CE3 2517 C CZ2 . TRP B 14 ? 0.9213 1.2322 0.4710 -0.1198 -0.2716 0.1965 14 TRP B CZ2 2518 C CZ3 . TRP B 14 ? 0.8983 1.2349 0.4940 -0.1463 -0.2731 0.1725 14 TRP B CZ3 2519 C CH2 . TRP B 14 ? 0.9202 1.2342 0.4760 -0.1294 -0.2721 0.1838 14 TRP B CH2 2520 N N . GLU B 15 ? 0.8626 1.3155 0.5621 -0.0657 -0.2670 0.1705 15 GLU B N 2521 C CA . GLU B 15 ? 0.8557 1.3689 0.5902 -0.0507 -0.2587 0.1648 15 GLU B CA 2522 C C . GLU B 15 ? 0.8401 1.4384 0.6284 -0.0621 -0.2628 0.1574 15 GLU B C 2523 O O . GLU B 15 ? 0.8252 1.4911 0.6557 -0.0643 -0.2510 0.1570 15 GLU B O 2524 C CB . GLU B 15 ? 0.8977 1.3949 0.5976 -0.0028 -0.2698 0.1627 15 GLU B CB 2525 C CG . GLU B 15 ? 0.9284 1.3351 0.5708 0.0030 -0.2706 0.1716 15 GLU B CG 2526 C CD . GLU B 15 ? 0.9904 1.3584 0.5795 0.0524 -0.2875 0.1686 15 GLU B CD 2527 O OE1 . GLU B 15 ? 1.0017 1.4291 0.6066 0.0902 -0.2890 0.1590 15 GLU B OE1 2528 O OE2 . GLU B 15 ? 1.0352 1.3122 0.5626 0.0538 -0.3008 0.1771 15 GLU B OE2 2529 N N . GLY B 16 ? 0.8517 1.4474 0.6363 -0.0709 -0.2807 0.1532 16 GLY B N 2530 C CA . GLY B 16 ? 0.8448 1.5117 0.6751 -0.0882 -0.2924 0.1467 16 GLY B CA 2531 C C . GLY B 16 ? 0.8293 1.4945 0.6786 -0.1364 -0.2844 0.1487 16 GLY B C 2532 O O . GLY B 16 ? 0.8284 1.5515 0.7173 -0.1612 -0.2939 0.1464 16 GLY B O 2533 N N . LEU B 17 ? 0.8237 1.4213 0.6412 -0.1501 -0.2698 0.1539 17 LEU B N 2534 C CA . LEU B 17 ? 0.8209 1.3996 0.6402 -0.1889 -0.2634 0.1548 17 LEU B CA 2535 C C . LEU B 17 ? 0.8036 1.4200 0.6571 -0.2071 -0.2434 0.1600 17 LEU B C 2536 O O . LEU B 17 ? 0.7946 1.3757 0.6324 -0.2059 -0.2238 0.1651 17 LEU B O 2537 C CB . LEU B 17 ? 0.8249 1.3252 0.5952 -0.1892 -0.2554 0.1587 17 LEU B CB 2538 C CG . LEU B 17 ? 0.8357 1.3008 0.5890 -0.2185 -0.2527 0.1574 17 LEU B CG 2539 C CD1 . LEU B 17 ? 0.8689 1.3305 0.6118 -0.2319 -0.2782 0.1489 17 LEU B CD1 2540 C CD2 . LEU B 17 ? 0.8351 1.2419 0.5463 -0.2092 -0.2399 0.1634 17 LEU B CD2 2541 N N . ILE B 18 ? 0.8050 1.4968 0.7054 -0.2253 -0.2494 0.1602 18 ILE B N 2542 C CA . ILE B 18 ? 0.7938 1.5341 0.7296 -0.2461 -0.2294 0.1686 18 ILE B CA 2543 C C . ILE B 18 ? 0.8094 1.5266 0.7426 -0.2990 -0.2323 0.1719 18 ILE B C 2544 O O . ILE B 18 ? 0.8097 1.5614 0.7677 -0.3252 -0.2174 0.1814 18 ILE B O 2545 C CB . ILE B 18 ? 0.7889 1.6438 0.7821 -0.2332 -0.2295 0.1724 18 ILE B CB 2546 C CG1 . ILE B 18 ? 0.8044 1.7138 0.8263 -0.2448 -0.2599 0.1678 18 ILE B CG1 2547 C CG2 . ILE B 18 ? 0.7838 1.6459 0.7643 -0.1750 -0.2209 0.1700 18 ILE B CG2 2548 C CD1 . ILE B 18 ? 0.8278 1.7360 0.8614 -0.3052 -0.2759 0.1711 18 ILE B CD1 2549 N N . ASP B 19 ? 0.8305 1.4821 0.7247 -0.3121 -0.2522 0.1648 19 ASP B N 2550 C CA . ASP B 19 ? 0.8664 1.4810 0.7425 -0.3590 -0.2656 0.1653 19 ASP B CA 2551 C C . ASP B 19 ? 0.8723 1.3997 0.6972 -0.3637 -0.2495 0.1659 19 ASP B C 2552 O O . ASP B 19 ? 0.9025 1.4049 0.7153 -0.4008 -0.2492 0.1705 19 ASP B O 2553 C CB . ASP B 19 ? 0.9048 1.4886 0.7541 -0.3630 -0.3000 0.1552 19 ASP B CB 2554 C CG . ASP B 19 ? 0.9616 1.5214 0.7976 -0.4156 -0.3257 0.1558 19 ASP B CG 2555 O OD1 . ASP B 19 ? 0.9766 1.5331 0.8176 -0.4522 -0.3159 0.1651 19 ASP B OD1 2556 O OD2 . ASP B 19 ? 1.0004 1.5375 0.8142 -0.4210 -0.3585 0.1474 19 ASP B OD2 2557 N N . GLY B 20 ? 0.8474 1.3297 0.6405 -0.3271 -0.2378 0.1627 20 GLY B N 2558 C CA . GLY B 20 ? 0.8497 1.2622 0.5990 -0.3241 -0.2223 0.1637 20 GLY B CA 2559 C C . GLY B 20 ? 0.8104 1.2141 0.5533 -0.2872 -0.2050 0.1665 20 GLY B C 2560 O O . GLY B 20 ? 0.7858 1.2292 0.5535 -0.2652 -0.2044 0.1680 20 GLY B O 2561 N N . TRP B 21 ? 0.8107 1.1599 0.5164 -0.2806 -0.1938 0.1678 21 TRP B N 2562 C CA . TRP B 21 ? 0.7806 1.1194 0.4788 -0.2534 -0.1809 0.1734 21 TRP B CA 2563 C C . TRP B 21 ? 0.7837 1.1086 0.4586 -0.2334 -0.1910 0.1739 21 TRP B C 2564 O O . TRP B 21 ? 0.7654 1.1014 0.4463 -0.2159 -0.1894 0.1804 21 TRP B O 2565 C CB . TRP B 21 ? 0.7849 1.0818 0.4566 -0.2545 -0.1663 0.1762 21 TRP B CB 2566 C CG . TRP B 21 ? 0.7759 1.0834 0.4659 -0.2663 -0.1515 0.1792 21 TRP B CG 2567 C CD1 . TRP B 21 ? 0.7773 1.1249 0.4988 -0.2855 -0.1495 0.1799 21 TRP B CD1 2568 C CD2 . TRP B 21 ? 0.7685 1.0502 0.4450 -0.2590 -0.1363 0.1834 21 TRP B CD2 2569 N NE1 . TRP B 21 ? 0.7739 1.1206 0.4990 -0.2887 -0.1313 0.1849 21 TRP B NE1 2570 C CE2 . TRP B 21 ? 0.7698 1.0707 0.4651 -0.2720 -0.1243 0.1857 21 TRP B CE2 2571 C CE3 . TRP B 21 ? 0.7642 1.0148 0.4160 -0.2426 -0.1322 0.1867 21 TRP B CE3 2572 C CZ2 . TRP B 21 ? 0.7699 1.0481 0.4527 -0.2668 -0.1092 0.1893 21 TRP B CZ2 2573 C CZ3 . TRP B 21 ? 0.7630 0.9946 0.4071 -0.2397 -0.1200 0.1899 21 TRP B CZ3 2574 C CH2 . TRP B 21 ? 0.7676 1.0073 0.4236 -0.2506 -0.1089 0.1901 21 TRP B CH2 2575 N N . TYR B 22 ? 0.8160 1.1105 0.4569 -0.2359 -0.2024 0.1681 22 TYR B N 2576 C CA . TYR B 22 ? 0.8290 1.1109 0.4406 -0.2147 -0.2101 0.1695 22 TYR B CA 2577 C C . TYR B 22 ? 0.8634 1.1427 0.4643 -0.2197 -0.2337 0.1596 22 TYR B C 2578 O O . TYR B 22 ? 0.8819 1.1616 0.4921 -0.2445 -0.2458 0.1523 22 TYR B O 2579 C CB . TYR B 22 ? 0.8487 1.0924 0.4149 -0.2009 -0.2016 0.1720 22 TYR B CB 2580 C CG . TYR B 22 ? 0.8229 1.0660 0.3980 -0.2009 -0.1827 0.1795 22 TYR B CG 2581 C CD1 . TYR B 22 ? 0.8351 1.0529 0.4030 -0.2156 -0.1780 0.1739 22 TYR B CD1 2582 C CD2 . TYR B 22 ? 0.7935 1.0574 0.3805 -0.1890 -0.1722 0.1934 22 TYR B CD2 2583 C CE1 . TYR B 22 ? 0.8163 1.0301 0.3884 -0.2130 -0.1625 0.1798 22 TYR B CE1 2584 C CE2 . TYR B 22 ? 0.7760 1.0380 0.3700 -0.1901 -0.1594 0.1999 22 TYR B CE2 2585 C CZ . TYR B 22 ? 0.7856 1.0229 0.3721 -0.1994 -0.1542 0.1920 22 TYR B CZ 2586 O OH . TYR B 22 ? 0.7714 1.0037 0.3610 -0.1980 -0.1431 0.1976 22 TYR B OH 2587 N N . GLY B 23 ? 0.8773 1.1539 0.4571 -0.1989 -0.2418 0.1610 23 GLY B N 2588 C CA . GLY B 23 ? 0.9168 1.1861 0.4805 -0.1998 -0.2672 0.1510 23 GLY B CA 2589 C C . GLY B 23 ? 0.9379 1.1979 0.4685 -0.1720 -0.2732 0.1542 23 GLY B C 2590 O O . GLY B 23 ? 0.9201 1.1865 0.4443 -0.1547 -0.2567 0.1675 23 GLY B O 2591 N N . PHE B 24 ? 0.9829 1.2278 0.4909 -0.1706 -0.2987 0.1435 24 PHE B N 2592 C CA . PHE B 24 ? 1.0164 1.2465 0.4843 -0.1433 -0.3076 0.1449 24 PHE B CA 2593 C C . PHE B 24 ? 1.0115 1.2752 0.5097 -0.1432 -0.3259 0.1413 24 PHE B C 2594 O O . PHE B 24 ? 1.0087 1.2975 0.5421 -0.1641 -0.3439 0.1315 24 PHE B O 2595 C CB . PHE B 24 ? 1.0872 1.2606 0.4892 -0.1342 -0.3278 0.1331 24 PHE B CB 2596 C CG . PHE B 24 ? 1.1133 1.2436 0.4761 -0.1328 -0.3181 0.1312 24 PHE B CG 2597 C CD1 . PHE B 24 ? 1.1209 1.2340 0.4959 -0.1648 -0.3263 0.1233 24 PHE B CD1 2598 C CD2 . PHE B 24 ? 1.1383 1.2463 0.4474 -0.0975 -0.3015 0.1384 24 PHE B CD2 2599 C CE1 . PHE B 24 ? 1.1574 1.2192 0.4851 -0.1603 -0.3203 0.1206 24 PHE B CE1 2600 C CE2 . PHE B 24 ? 1.1711 1.2391 0.4376 -0.0881 -0.2944 0.1352 24 PHE B CE2 2601 C CZ . PHE B 24 ? 1.1829 1.2208 0.4549 -0.1188 -0.3050 0.1252 24 PHE B CZ 2602 N N . ARG B 25 ? 1.0172 1.2838 0.5000 -0.1198 -0.3220 0.1507 25 ARG B N 2603 C CA . ARG B 25 ? 1.0311 1.3158 0.5229 -0.1098 -0.3429 0.1461 25 ARG B CA 2604 C C . ARG B 25 ? 1.0859 1.3337 0.5154 -0.0840 -0.3528 0.1475 25 ARG B C 2605 O O . ARG B 25 ? 1.0921 1.3270 0.4912 -0.0682 -0.3338 0.1641 25 ARG B O 2606 C CB . ARG B 25 ? 0.9966 1.3085 0.5185 -0.1039 -0.3314 0.1571 25 ARG B CB 2607 C CG . ARG B 25 ? 1.0128 1.3424 0.5410 -0.0877 -0.3539 0.1510 25 ARG B CG 2608 C CD . ARG B 25 ? 0.9885 1.3380 0.5420 -0.0804 -0.3462 0.1580 25 ARG B CD 2609 N NE . ARG B 25 ? 0.9530 1.3507 0.5632 -0.0942 -0.3423 0.1508 25 ARG B NE 2610 C CZ . ARG B 25 ? 0.9349 1.3496 0.5658 -0.0862 -0.3331 0.1551 25 ARG B CZ 2611 N NH1 . ARG B 25 ? 0.9525 1.3303 0.5490 -0.0683 -0.3309 0.1661 25 ARG B NH1 2612 N NH2 . ARG B 25 ? 0.9060 1.3707 0.5864 -0.0966 -0.3270 0.1497 25 ARG B NH2 2613 N N . HIS B 26 ? 1.1329 1.3661 0.5424 -0.0812 -0.3833 0.1320 26 HIS B N 2614 C CA . HIS B 26 ? 1.1964 1.3868 0.5370 -0.0534 -0.3955 0.1309 26 HIS B CA 2615 C C . HIS B 26 ? 1.2177 1.4178 0.5552 -0.0365 -0.4154 0.1289 26 HIS B C 2616 O O . HIS B 26 ? 1.1895 1.4310 0.5780 -0.0450 -0.4266 0.1238 26 HIS B O 2617 C CB . HIS B 26 ? 1.2542 1.4004 0.5526 -0.0569 -0.4215 0.1137 26 HIS B CB 2618 C CG . HIS B 26 ? 1.2641 1.4290 0.5969 -0.0809 -0.4589 0.0969 26 HIS B CG 2619 N ND1 . HIS B 26 ? 1.3088 1.4654 0.6198 -0.0679 -0.4928 0.0865 26 HIS B ND1 2620 C CD2 . HIS B 26 ? 1.2375 1.4363 0.6269 -0.1187 -0.4682 0.0909 26 HIS B CD2 2621 C CE1 . HIS B 26 ? 1.3079 1.4988 0.6657 -0.0980 -0.5227 0.0750 26 HIS B CE1 2622 N NE2 . HIS B 26 ? 1.2654 1.4846 0.6720 -0.1305 -0.5072 0.0788 26 HIS B NE2 2623 N N . GLN B 27 ? 1.2754 1.4372 0.5475 -0.0083 -0.4192 0.1334 27 GLN B N 2624 C CA . GLN B 27 ? 1.3118 1.4685 0.5637 0.0126 -0.4394 0.1319 27 GLN B CA 2625 C C . GLN B 27 ? 1.3905 1.4943 0.5616 0.0399 -0.4542 0.1275 27 GLN B C 2626 O O . GLN B 27 ? 1.4154 1.4944 0.5351 0.0581 -0.4301 0.1435 27 GLN B O 2627 C CB . GLN B 27 ? 1.2942 1.4580 0.5468 0.0201 -0.4166 0.1539 27 GLN B CB 2628 C CG . GLN B 27 ? 1.3466 1.4851 0.5537 0.0465 -0.4333 0.1574 27 GLN B CG 2629 C CD . GLN B 27 ? 1.3556 1.5151 0.5900 0.0534 -0.4696 0.1365 27 GLN B CD 2630 O OE1 . GLN B 27 ? 1.3872 1.5448 0.6149 0.0569 -0.4985 0.1176 27 GLN B OE1 2631 N NE2 . GLN B 27 ? 1.3376 1.5167 0.5984 0.0576 -0.4707 0.1401 27 GLN B NE2 2632 N N . ASN B 28 ? 1.4348 1.5258 0.5945 0.0436 -0.4944 0.1068 28 ASN B N 2633 C CA . ASN B 28 ? 1.5223 1.5535 0.5979 0.0714 -0.5159 0.0985 28 ASN B CA 2634 C C . ASN B 28 ? 1.5621 1.5900 0.6275 0.0852 -0.5566 0.0846 28 ASN B C 2635 O O . ASN B 28 ? 1.5248 1.5979 0.6419 0.0808 -0.5622 0.0849 28 ASN B O 2636 C CB . ASN B 28 ? 1.5611 1.5545 0.6097 0.0602 -0.5308 0.0838 28 ASN B CB 2637 C CG . ASN B 28 ? 1.5426 1.5654 0.6547 0.0194 -0.5628 0.0666 28 ASN B CG 2638 O OD1 . ASN B 28 ? 1.5160 1.5901 0.6851 0.0079 -0.5815 0.0615 28 ASN B OD1 2639 N ND2 . ASN B 28 ? 1.5636 1.5549 0.6623 -0.0016 -0.5698 0.0588 28 ASN B ND2 2640 N N . ALA B 29 ? 1.6449 1.6165 0.6380 0.1064 -0.5866 0.0717 29 ALA B N 2641 C CA . ALA B 29 ? 1.6914 1.6565 0.6698 0.1207 -0.6306 0.0565 29 ALA B CA 2642 C C . ALA B 29 ? 1.6559 1.6824 0.7189 0.0866 -0.6652 0.0400 29 ALA B C 2643 O O . ALA B 29 ? 1.6613 1.7202 0.7470 0.0965 -0.6920 0.0324 29 ALA B O 2644 C CB . ALA B 29 ? 1.7954 1.6804 0.6736 0.1488 -0.6587 0.0447 29 ALA B CB 2645 N N . GLN B 30 ? 1.6237 1.6702 0.7320 0.0475 -0.6639 0.0362 30 GLN B N 2646 C CA . GLN B 30 ? 1.5885 1.7064 0.7835 0.0081 -0.6917 0.0261 30 GLN B CA 2647 C C . GLN B 30 ? 1.4934 1.6998 0.7805 -0.0039 -0.6620 0.0371 30 GLN B C 2648 O O . GLN B 30 ? 1.4610 1.7434 0.8255 -0.0316 -0.6792 0.0320 30 GLN B O 2649 C CB . GLN B 30 ? 1.6124 1.7039 0.8060 -0.0328 -0.7072 0.0191 30 GLN B CB 2650 C CG . GLN B 30 ? 1.7218 1.7156 0.8162 -0.0216 -0.7456 0.0051 30 GLN B CG 2651 C CD . GLN B 30 ? 1.7612 1.7194 0.8485 -0.0668 -0.7711 -0.0026 30 GLN B CD 2652 O OE1 . GLN B 30 ? 1.8075 1.6840 0.8207 -0.0577 -0.7607 -0.0031 30 GLN B OE1 2653 N NE2 . GLN B 30 ? 1.7488 1.7696 0.9103 -0.1156 -0.8052 -0.0072 30 GLN B NE2 2654 N N . GLY B 31 ? 1.4547 1.6523 0.7308 0.0163 -0.6191 0.0533 31 GLY B N 2655 C CA . GLY B 31 ? 1.3808 1.6437 0.7255 0.0123 -0.5937 0.0632 31 GLY B CA 2656 C C . GLY B 31 ? 1.3245 1.5931 0.6969 -0.0119 -0.5536 0.0756 31 GLY B C 2657 O O . GLY B 31 ? 1.3404 1.5624 0.6763 -0.0219 -0.5429 0.0775 31 GLY B O 2658 N N . GLU B 32 ? 1.2759 1.5606 0.8553 0.1295 -0.5068 0.1236 32 GLU B N 2659 C CA . GLU B 32 ? 1.2191 1.4606 0.8310 0.1185 -0.4737 0.1092 32 GLU B CA 2660 C C . GLU B 32 ? 1.1293 1.4935 0.8331 0.1132 -0.4594 0.0921 32 GLU B C 2661 O O . GLU B 32 ? 1.1227 1.6103 0.8652 0.1440 -0.4788 0.0975 32 GLU B O 2662 C CB . GLU B 32 ? 1.2890 1.4190 0.8470 0.1750 -0.4830 0.1210 32 GLU B CB 2663 C CG . GLU B 32 ? 1.2379 1.3393 0.8323 0.1741 -0.4548 0.1068 32 GLU B CG 2664 C CD . GLU B 32 ? 1.3295 1.2732 0.8396 0.1966 -0.4644 0.1194 32 GLU B CD 2665 O OE1 . GLU B 32 ? 1.3799 1.2265 0.8256 0.1490 -0.4661 0.1353 32 GLU B OE1 2666 O OE2 . GLU B 32 ? 1.3620 1.2796 0.8624 0.2584 -0.4719 0.1148 32 GLU B OE2 2667 N N . GLY B 33 ? 1.0661 1.4043 0.8012 0.0716 -0.4266 0.0750 33 GLY B N 2668 C CA . GLY B 33 ? 0.9926 1.4202 0.8028 0.0601 -0.4116 0.0614 33 GLY B CA 2669 C C . GLY B 33 ? 0.9500 1.3033 0.7729 0.0473 -0.3786 0.0487 33 GLY B C 2670 O O . GLY B 33 ? 0.9685 1.2200 0.7482 0.0316 -0.3655 0.0496 33 GLY B O 2671 N N . THR B 34 ? 0.8954 1.3131 0.7776 0.0513 -0.3661 0.0404 34 THR B N 2672 C CA . THR B 34 ? 0.8556 1.2131 0.7534 0.0432 -0.3370 0.0293 34 THR B CA 2673 C C . THR B 34 ? 0.7962 1.2239 0.7494 0.0019 -0.3230 0.0169 34 THR B C 2674 O O . THR B 34 ? 0.7806 1.3268 0.7752 0.0023 -0.3356 0.0222 34 THR B O 2675 C CB . THR B 34 ? 0.8775 1.2025 0.7678 0.1075 -0.3383 0.0346 34 THR B CB 2676 O OG1 . THR B 34 ? 0.8311 1.2516 0.7823 0.1236 -0.3287 0.0281 34 THR B OG1 2677 C CG2 . THR B 34 ? 0.9594 1.2709 0.7986 0.1704 -0.3699 0.0500 34 THR B CG2 2678 N N . ALA B 35 ? 0.7712 1.1317 0.7201 -0.0338 -0.2991 0.0036 35 ALA B N 2679 C CA . ALA B 35 ? 0.7395 1.1335 0.7188 -0.0764 -0.2899 -0.0073 35 ALA B CA 2680 C C . ALA B 35 ? 0.7079 1.0341 0.6943 -0.0778 -0.2615 -0.0176 35 ALA B C 2681 O O . ALA B 35 ? 0.7155 0.9644 0.6725 -0.0694 -0.2475 -0.0194 35 ALA B O 2682 C CB . ALA B 35 ? 0.7789 1.1547 0.7184 -0.1299 -0.3017 -0.0157 35 ALA B CB 2683 N N . ALA B 36 ? 0.6767 1.0447 0.7012 -0.0931 -0.2545 -0.0208 36 ALA B N 2684 C CA . ALA B 36 ? 0.6461 0.9624 0.6820 -0.0914 -0.2300 -0.0286 36 ALA B CA 2685 C C . ALA B 36 ? 0.6689 0.9131 0.6687 -0.1285 -0.2207 -0.0428 36 ALA B C 2686 O O . ALA B 36 ? 0.7065 0.9523 0.6812 -0.1692 -0.2359 -0.0476 36 ALA B O 2687 C CB . ALA B 36 ? 0.6115 1.0051 0.6973 -0.0872 -0.2268 -0.0243 36 ALA B CB 2688 N N . ASP B 37 ? 0.6603 0.8402 0.6479 -0.1129 -0.1989 -0.0482 37 ASP B N 2689 C CA . ASP B 37 ? 0.6885 0.8032 0.6385 -0.1269 -0.1871 -0.0627 37 ASP B CA 2690 C C . ASP B 37 ? 0.6711 0.7826 0.6448 -0.1398 -0.1802 -0.0655 37 ASP B C 2691 O O . ASP B 37 ? 0.6243 0.7506 0.6370 -0.1206 -0.1657 -0.0598 37 ASP B O 2692 C CB . ASP B 37 ? 0.6862 0.7664 0.6178 -0.1008 -0.1661 -0.0625 37 ASP B CB 2693 C CG . ASP B 37 ? 0.7289 0.7533 0.6127 -0.0955 -0.1535 -0.0787 37 ASP B CG 2694 O OD1 . ASP B 37 ? 0.7941 0.7802 0.6159 -0.0981 -0.1618 -0.0914 37 ASP B OD1 2695 O OD2 . ASP B 37 ? 0.7069 0.7209 0.6059 -0.0831 -0.1371 -0.0797 37 ASP B OD2 2696 N N . TYR B 38 ? 0.7237 0.8046 0.6610 -0.1773 -0.1943 -0.0730 38 TYR B N 2697 C CA . TYR B 38 ? 0.7268 0.7946 0.6709 -0.2007 -0.1931 -0.0725 38 TYR B CA 2698 C C . TYR B 38 ? 0.7247 0.7222 0.6512 -0.1711 -0.1709 -0.0819 38 TYR B C 2699 O O . TYR B 38 ? 0.6747 0.6951 0.6443 -0.1622 -0.1574 -0.0758 38 TYR B O 2700 C CB . TYR B 38 ? 0.8187 0.8458 0.7008 -0.2604 -0.2222 -0.0746 38 TYR B CB 2701 C CG . TYR B 38 ? 0.8545 0.8488 0.7203 -0.2989 -0.2280 -0.0703 38 TYR B CG 2702 C CD1 . TYR B 38 ? 0.8121 0.9148 0.7391 -0.3318 -0.2320 -0.0503 38 TYR B CD1 2703 C CD2 . TYR B 38 ? 0.9454 0.8010 0.7248 -0.2985 -0.2309 -0.0851 38 TYR B CD2 2704 C CE1 . TYR B 38 ? 0.8504 0.9264 0.7572 -0.3751 -0.2384 -0.0422 38 TYR B CE1 2705 C CE2 . TYR B 38 ? 0.9938 0.8020 0.7442 -0.3366 -0.2406 -0.0786 38 TYR B CE2 2706 C CZ . TYR B 38 ? 0.9436 0.8629 0.7595 -0.3811 -0.2444 -0.0558 38 TYR B CZ 2707 O OH . TYR B 38 ? 0.9982 0.8734 0.7803 -0.4266 -0.2549 -0.0454 38 TYR B OH 2708 N N . LYS B 39 ? 0.7829 0.7050 0.6436 -0.1505 -0.1673 -0.0962 39 LYS B N 2709 C CA . LYS B 39 ? 0.8039 0.6676 0.6344 -0.1161 -0.1496 -0.1053 39 LYS B CA 2710 C C . LYS B 39 ? 0.7126 0.6405 0.6145 -0.0881 -0.1249 -0.0929 39 LYS B C 2711 O O . LYS B 39 ? 0.6940 0.6146 0.6142 -0.0847 -0.1170 -0.0902 39 LYS B O 2712 C CB . LYS B 39 ? 0.8852 0.6867 0.6335 -0.0801 -0.1464 -0.1222 39 LYS B CB 2713 C CG . LYS B 39 ? 1.0011 0.6813 0.6504 -0.0625 -0.1542 -0.1408 39 LYS B CG 2714 C CD . LYS B 39 ? 1.1043 0.6908 0.6769 -0.1202 -0.1916 -0.1473 39 LYS B CD 2715 C CE . LYS B 39 ? 1.2697 0.6893 0.6998 -0.0991 -0.2087 -0.1691 39 LYS B CE 2716 N NZ . LYS B 39 ? 1.3693 0.7246 0.7023 -0.0495 -0.2091 -0.1919 39 LYS B NZ 2717 N N . SER B 40 ? 0.6679 0.6498 0.5992 -0.0744 -0.1169 -0.0833 40 SER B N 2718 C CA . SER B 40 ? 0.6021 0.6310 0.5827 -0.0616 -0.1018 -0.0679 40 SER B CA 2719 C C . SER B 40 ? 0.5552 0.6041 0.5845 -0.0755 -0.1059 -0.0608 40 SER B C 2720 O O . SER B 40 ? 0.5282 0.5806 0.5790 -0.0694 -0.0953 -0.0558 40 SER B O 2721 C CB . SER B 40 ? 0.5913 0.6545 0.5751 -0.0599 -0.1031 -0.0549 40 SER B CB 2722 O OG . SER B 40 ? 0.5922 0.6623 0.5816 -0.0734 -0.1218 -0.0539 40 SER B OG 2723 N N . THR B 41 ? 0.5494 0.6223 0.5933 -0.0902 -0.1211 -0.0597 41 THR B N 2724 C CA . THR B 41 ? 0.5159 0.6271 0.6004 -0.0929 -0.1239 -0.0540 41 THR B CA 2725 C C . THR B 41 ? 0.5149 0.6106 0.6040 -0.1072 -0.1173 -0.0574 41 THR B C 2726 O O . THR B 41 ? 0.4845 0.5903 0.5988 -0.0978 -0.1081 -0.0531 41 THR B O 2727 C CB . THR B 41 ? 0.5223 0.6895 0.6189 -0.1033 -0.1414 -0.0512 41 THR B CB 2728 O OG1 . THR B 41 ? 0.5274 0.7059 0.6197 -0.0799 -0.1491 -0.0454 41 THR B OG1 2729 C CG2 . THR B 41 ? 0.4972 0.7291 0.6325 -0.1033 -0.1414 -0.0456 41 THR B CG2 2730 N N . GLN B 42 ? 0.5649 0.6212 0.6154 -0.1314 -0.1256 -0.0647 42 GLN B N 2731 C CA . GLN B 42 ? 0.5902 0.6138 0.6260 -0.1530 -0.1267 -0.0652 42 GLN B CA 2732 C C . GLN B 42 ? 0.5840 0.5657 0.6132 -0.1242 -0.1099 -0.0678 42 GLN B C 2733 O O . GLN B 42 ? 0.5736 0.5524 0.6150 -0.1313 -0.1057 -0.0633 42 GLN B O 2734 C CB . GLN B 42 ? 0.6827 0.6384 0.6478 -0.1894 -0.1480 -0.0718 42 GLN B CB 2735 C CG . GLN B 42 ? 0.7278 0.6598 0.6708 -0.2359 -0.1607 -0.0641 42 GLN B CG 2736 C CD . GLN B 42 ? 0.6781 0.7321 0.6852 -0.2685 -0.1639 -0.0464 42 GLN B CD 2737 O OE1 . GLN B 42 ? 0.6497 0.7887 0.6916 -0.2688 -0.1691 -0.0414 42 GLN B OE1 2738 N NE2 . GLN B 42 ? 0.6749 0.7468 0.6945 -0.2904 -0.1606 -0.0357 42 GLN B NE2 2739 N N . SER B 43 ? 0.5918 0.5559 0.6022 -0.0922 -0.1005 -0.0725 43 SER B N 2740 C CA . SER B 43 ? 0.5876 0.5415 0.5947 -0.0613 -0.0850 -0.0710 43 SER B CA 2741 C C . SER B 43 ? 0.5171 0.5241 0.5817 -0.0614 -0.0755 -0.0574 43 SER B C 2742 O O . SER B 43 ? 0.5075 0.5107 0.5789 -0.0534 -0.0685 -0.0534 43 SER B O 2743 C CB . SER B 43 ? 0.6130 0.5732 0.5913 -0.0276 -0.0759 -0.0744 43 SER B CB 2744 O OG . SER B 43 ? 0.6495 0.5925 0.5988 0.0100 -0.0655 -0.0773 43 SER B OG 2745 N N . ALA B 44 ? 0.4825 0.5263 0.5752 -0.0686 -0.0790 -0.0506 44 ALA B N 2746 C CA . ALA B 44 ? 0.4474 0.5121 0.5685 -0.0687 -0.0770 -0.0401 44 ALA B CA 2747 C C . ALA B 44 ? 0.4343 0.5047 0.5739 -0.0765 -0.0785 -0.0426 44 ALA B C 2748 O O . ALA B 44 ? 0.4231 0.4916 0.5724 -0.0747 -0.0734 -0.0382 44 ALA B O 2749 C CB . ALA B 44 ? 0.4490 0.5220 0.5673 -0.0675 -0.0862 -0.0332 44 ALA B CB 2750 N N . ILE B 45 ? 0.4410 0.5310 0.5842 -0.0883 -0.0863 -0.0471 45 ILE B N 2751 C CA . ILE B 45 ? 0.4312 0.5560 0.5932 -0.0997 -0.0864 -0.0452 45 ILE B CA 2752 C C . ILE B 45 ? 0.4444 0.5348 0.5946 -0.1149 -0.0811 -0.0441 45 ILE B C 2753 O O . ILE B 45 ? 0.4287 0.5344 0.5934 -0.1135 -0.0749 -0.0401 45 ILE B O 2754 C CB . ILE B 45 ? 0.4433 0.6209 0.6109 -0.1214 -0.0979 -0.0437 45 ILE B CB 2755 C CG1 . ILE B 45 ? 0.4321 0.6591 0.6150 -0.0927 -0.1034 -0.0429 45 ILE B CG1 2756 C CG2 . ILE B 45 ? 0.4429 0.6729 0.6251 -0.1477 -0.0975 -0.0359 45 ILE B CG2 2757 C CD1 . ILE B 45 ? 0.4417 0.7463 0.6358 -0.1100 -0.1165 -0.0379 45 ILE B CD1 2758 N N . ASP B 46 ? 0.4866 0.5209 0.5987 -0.1235 -0.0855 -0.0484 46 ASP B N 2759 C CA . ASP B 46 ? 0.5261 0.5047 0.6060 -0.1307 -0.0859 -0.0476 46 ASP B CA 2760 C C . ASP B 46 ? 0.4980 0.4765 0.5932 -0.1028 -0.0731 -0.0438 46 ASP B C 2761 O O . ASP B 46 ? 0.5082 0.4704 0.5977 -0.1096 -0.0721 -0.0388 46 ASP B O 2762 C CB . ASP B 46 ? 0.6081 0.5019 0.6182 -0.1297 -0.0973 -0.0567 46 ASP B CB 2763 C CG . ASP B 46 ? 0.6683 0.5373 0.6401 -0.1788 -0.1189 -0.0562 46 ASP B CG 2764 O OD1 . ASP B 46 ? 0.6367 0.5793 0.6472 -0.2145 -0.1225 -0.0451 46 ASP B OD1 2765 O OD2 . ASP B 46 ? 0.7596 0.5388 0.6550 -0.1817 -0.1342 -0.0657 46 ASP B OD2 2766 N N . GLN B 47 ? 0.4704 0.4719 0.5809 -0.0785 -0.0659 -0.0426 47 GLN B N 2767 C CA . GLN B 47 ? 0.4487 0.4690 0.5746 -0.0637 -0.0579 -0.0335 47 GLN B CA 2768 C C . GLN B 47 ? 0.4166 0.4583 0.5686 -0.0763 -0.0581 -0.0283 47 GLN B C 2769 O O . GLN B 47 ? 0.4114 0.4525 0.5666 -0.0763 -0.0556 -0.0222 47 GLN B O 2770 C CB . GLN B 47 ? 0.4398 0.4943 0.5697 -0.0491 -0.0537 -0.0268 47 GLN B CB 2771 C CG . GLN B 47 ? 0.4805 0.5277 0.5779 -0.0199 -0.0490 -0.0320 47 GLN B CG 2772 C CD . GLN B 47 ? 0.4705 0.5807 0.5759 -0.0107 -0.0427 -0.0209 47 GLN B CD 2773 O OE1 . GLN B 47 ? 0.4519 0.6220 0.5776 -0.0133 -0.0387 -0.0027 47 GLN B OE1 2774 N NE2 . GLN B 47 ? 0.4883 0.5921 0.5742 -0.0066 -0.0438 -0.0284 47 GLN B NE2 2775 N N . ILE B 48 ? 0.4058 0.4635 0.5674 -0.0800 -0.0624 -0.0315 48 ILE B N 2776 C CA . ILE B 48 ? 0.4004 0.4671 0.5672 -0.0765 -0.0639 -0.0308 48 ILE B CA 2777 C C . ILE B 48 ? 0.3996 0.4839 0.5737 -0.0853 -0.0590 -0.0321 48 ILE B C 2778 O O . ILE B 48 ? 0.4033 0.4852 0.5744 -0.0823 -0.0563 -0.0300 48 ILE B O 2779 C CB . ILE B 48 ? 0.4107 0.4850 0.5711 -0.0618 -0.0718 -0.0351 48 ILE B CB 2780 C CG1 . ILE B 48 ? 0.4350 0.4698 0.5679 -0.0596 -0.0820 -0.0281 48 ILE B CG1 2781 C CG2 . ILE B 48 ? 0.4207 0.5205 0.5802 -0.0434 -0.0711 -0.0406 48 ILE B CG2 2782 C CD1 . ILE B 48 ? 0.4304 0.4695 0.5640 -0.0734 -0.0815 -0.0192 48 ILE B CD1 2783 N N . THR B 49 ? 0.4072 0.5084 0.5832 -0.1030 -0.0604 -0.0329 49 THR B N 2784 C CA . THR B 49 ? 0.4163 0.5426 0.5930 -0.1260 -0.0585 -0.0274 49 THR B CA 2785 C C . THR B 49 ? 0.4325 0.5081 0.5894 -0.1344 -0.0572 -0.0220 49 THR B C 2786 O O . THR B 49 ? 0.4370 0.5281 0.5933 -0.1457 -0.0536 -0.0157 49 THR B O 2787 C CB . THR B 49 ? 0.4446 0.5908 0.6127 -0.1617 -0.0680 -0.0232 49 THR B CB 2788 O OG1 . THR B 49 ? 0.4855 0.5535 0.6170 -0.1688 -0.0768 -0.0272 49 THR B OG1 2789 C CG2 . THR B 49 ? 0.4259 0.6484 0.6187 -0.1528 -0.0704 -0.0249 49 THR B CG2 2790 N N . GLY B 50 ? 0.4472 0.4691 0.5837 -0.1234 -0.0601 -0.0237 50 GLY B N 2791 C CA . GLY B 50 ? 0.4708 0.4496 0.5847 -0.1158 -0.0603 -0.0183 50 GLY B CA 2792 C C . GLY B 50 ? 0.4370 0.4422 0.5725 -0.1042 -0.0541 -0.0128 50 GLY B C 2793 O O . GLY B 50 ? 0.4509 0.4408 0.5745 -0.1075 -0.0545 -0.0058 50 GLY B O 2794 N N . LYS B 51 ? 0.4058 0.4391 0.5612 -0.0947 -0.0525 -0.0148 51 LYS B N 2795 C CA . LYS B 51 ? 0.3972 0.4382 0.5545 -0.0936 -0.0536 -0.0099 51 LYS B CA 2796 C C . LYS B 51 ? 0.4034 0.4532 0.5563 -0.0987 -0.0504 -0.0131 51 LYS B C 2797 O O . LYS B 51 ? 0.4101 0.4532 0.5531 -0.1021 -0.0507 -0.0080 51 LYS B O 2798 C CB . LYS B 51 ? 0.3957 0.4364 0.5491 -0.0905 -0.0602 -0.0107 51 LYS B CB 2799 C CG . LYS B 51 ? 0.3939 0.4477 0.5497 -0.0938 -0.0640 0.0007 51 LYS B CG 2800 C CD . LYS B 51 ? 0.4160 0.4516 0.5495 -0.1061 -0.0773 0.0054 51 LYS B CD 2801 C CE . LYS B 51 ? 0.4172 0.4876 0.5529 -0.1217 -0.0819 0.0235 51 LYS B CE 2802 N NZ . LYS B 51 ? 0.4653 0.5036 0.5605 -0.1539 -0.1032 0.0373 51 LYS B NZ 2803 N N . LEU B 52 ? 0.4037 0.4820 0.5629 -0.0969 -0.0472 -0.0203 52 LEU B N 2804 C CA . LEU B 52 ? 0.4139 0.5317 0.5705 -0.0945 -0.0407 -0.0221 52 LEU B CA 2805 C C . LEU B 52 ? 0.4260 0.5496 0.5788 -0.1225 -0.0374 -0.0110 52 LEU B C 2806 O O . LEU B 52 ? 0.4362 0.5716 0.5783 -0.1218 -0.0327 -0.0084 52 LEU B O 2807 C CB . LEU B 52 ? 0.4111 0.5903 0.5813 -0.0845 -0.0380 -0.0271 52 LEU B CB 2808 C CG . LEU B 52 ? 0.4231 0.5889 0.5802 -0.0465 -0.0438 -0.0384 52 LEU B CG 2809 C CD1 . LEU B 52 ? 0.4182 0.6521 0.5943 -0.0359 -0.0436 -0.0402 52 LEU B CD1 2810 C CD2 . LEU B 52 ? 0.4624 0.6097 0.5814 -0.0119 -0.0440 -0.0471 52 LEU B CD2 2811 N N . ASN B 53 ? 0.4435 0.5443 0.5909 -0.1473 -0.0428 -0.0043 53 ASN B N 2812 C CA . ASN B 53 ? 0.4862 0.5631 0.6076 -0.1794 -0.0469 0.0091 53 ASN B CA 2813 C C . ASN B 53 ? 0.4972 0.5352 0.6044 -0.1669 -0.0472 0.0137 53 ASN B C 2814 O O . ASN B 53 ? 0.5153 0.5612 0.6079 -0.1840 -0.0456 0.0234 53 ASN B O 2815 C CB . ASN B 53 ? 0.5356 0.5488 0.6233 -0.2012 -0.0608 0.0127 53 ASN B CB 2816 C CG . ASN B 53 ? 0.5451 0.6017 0.6378 -0.2326 -0.0659 0.0143 53 ASN B CG 2817 O OD1 . ASN B 53 ? 0.5229 0.6757 0.6439 -0.2459 -0.0585 0.0196 53 ASN B OD1 2818 N ND2 . ASN B 53 ? 0.5866 0.5801 0.6471 -0.2412 -0.0795 0.0103 53 ASN B ND2 2819 N N . ARG B 54 ? 0.4889 0.4990 0.6009 -0.1399 -0.0499 0.0096 54 ARG B N 2820 C CA . ARG B 54 ? 0.4969 0.4943 0.6028 -0.1275 -0.0524 0.0166 54 ARG B CA 2821 C C . ARG B 54 ? 0.4872 0.5117 0.5955 -0.1293 -0.0487 0.0150 54 ARG B C 2822 O O . ARG B 54 ? 0.5038 0.5207 0.5964 -0.1350 -0.0507 0.0233 54 ARG B O 2823 C CB . ARG B 54 ? 0.4844 0.4867 0.6032 -0.1044 -0.0558 0.0169 54 ARG B CB 2824 C CG . ARG B 54 ? 0.5200 0.4987 0.6200 -0.0814 -0.0610 0.0248 54 ARG B CG 2825 C CD . ARG B 54 ? 0.5016 0.5329 0.6224 -0.0638 -0.0629 0.0344 54 ARG B CD 2826 N NE . ARG B 54 ? 0.4709 0.5337 0.6146 -0.0776 -0.0617 0.0305 54 ARG B NE 2827 C CZ . ARG B 54 ? 0.4597 0.5418 0.6073 -0.0987 -0.0686 0.0363 54 ARG B CZ 2828 N NH1 . ARG B 54 ? 0.4728 0.5599 0.6108 -0.1103 -0.0759 0.0460 54 ARG B NH1 2829 N NH2 . ARG B 54 ? 0.4518 0.5348 0.6000 -0.1104 -0.0721 0.0329 54 ARG B NH2 2830 N N . LEU B 55 ? 0.4776 0.5221 0.5933 -0.1194 -0.0458 0.0033 55 LEU B N 2831 C CA . LEU B 55 ? 0.5025 0.5433 0.5957 -0.1102 -0.0477 -0.0026 55 LEU B CA 2832 C C . LEU B 55 ? 0.5242 0.6011 0.6043 -0.1049 -0.0365 -0.0077 55 LEU B C 2833 O O . LEU B 55 ? 0.5477 0.6142 0.5974 -0.0991 -0.0373 -0.0099 55 LEU B O 2834 C CB . LEU B 55 ? 0.5139 0.5317 0.5939 -0.0952 -0.0561 -0.0127 55 LEU B CB 2835 C CG . LEU B 55 ? 0.5105 0.5091 0.5942 -0.1091 -0.0691 -0.0016 55 LEU B CG 2836 C CD1 . LEU B 55 ? 0.5370 0.5039 0.5972 -0.1059 -0.0810 -0.0068 55 LEU B CD1 2837 C CD2 . LEU B 55 ? 0.5320 0.5208 0.5968 -0.1256 -0.0796 0.0104 55 LEU B CD2 2838 N N . ILE B 56 ? 0.5241 0.6540 0.6239 -0.1083 -0.0270 -0.0080 56 ILE B N 2839 C CA . ILE B 56 ? 0.5500 0.7532 0.6437 -0.1014 -0.0140 -0.0088 56 ILE B CA 2840 C C . ILE B 56 ? 0.5765 0.7956 0.6639 -0.1397 -0.0107 0.0098 56 ILE B C 2841 O O . ILE B 56 ? 0.5806 0.8365 0.6781 -0.1771 -0.0100 0.0250 56 ILE B O 2842 C CB . ILE B 56 ? 0.5371 0.8211 0.6566 -0.0938 -0.0071 -0.0109 56 ILE B CB 2843 C CG1 . ILE B 56 ? 0.5373 0.7890 0.6525 -0.0530 -0.0138 -0.0280 56 ILE B CG1 2844 C CG2 . ILE B 56 ? 0.5548 0.9516 0.6713 -0.0790 0.0088 -0.0086 56 ILE B CG2 2845 C CD1 . ILE B 56 ? 0.5858 0.7796 0.6490 -0.0086 -0.0192 -0.0445 56 ILE B CD1 2846 N N . GLU B 57 ? 0.6134 0.7942 0.6735 -0.1361 -0.0134 0.0107 57 GLU B N 2847 C CA . GLU B 57 ? 0.6506 0.8463 0.6928 -0.1660 -0.0104 0.0280 57 GLU B CA 2848 C C . GLU B 57 ? 0.6824 0.8435 0.6899 -0.1512 -0.0134 0.0239 57 GLU B C 2849 O O . GLU B 57 ? 0.6815 0.7835 0.6792 -0.1354 -0.0257 0.0152 57 GLU B O 2850 C CB . GLU B 57 ? 0.6677 0.8093 0.7066 -0.2046 -0.0232 0.0472 57 GLU B CB 2851 C CG . GLU B 57 ? 0.6647 0.7280 0.7031 -0.1879 -0.0372 0.0450 57 GLU B CG 2852 C CD . GLU B 57 ? 0.7113 0.7165 0.7179 -0.2044 -0.0499 0.0637 57 GLU B CD 2853 O OE1 . GLU B 57 ? 0.7568 0.7413 0.7358 -0.2382 -0.0550 0.0783 57 GLU B OE1 2854 O OE2 . GLU B 57 ? 0.7093 0.6880 0.7106 -0.1855 -0.0581 0.0662 57 GLU B OE2 2855 N N . LYS B 58 ? 0.7178 0.9228 0.7025 -0.1629 -0.0040 0.0329 58 LYS B N 2856 C CA . LYS B 58 ? 0.7570 0.9242 0.7030 -0.1623 -0.0098 0.0353 58 LYS B CA 2857 C C . LYS B 58 ? 0.7783 0.9138 0.7189 -0.2039 -0.0198 0.0619 58 LYS B C 2858 O O . LYS B 58 ? 0.7778 0.9151 0.7291 -0.2345 -0.0220 0.0773 58 LYS B O 2859 C CB . LYS B 58 ? 0.7956 1.0251 0.7051 -0.1398 0.0067 0.0266 58 LYS B CB 2860 C CG . LYS B 58 ? 0.8012 1.1390 0.7187 -0.1686 0.0247 0.0467 58 LYS B CG 2861 C CD . LYS B 58 ? 0.8392 1.2661 0.7230 -0.1268 0.0457 0.0339 58 LYS B CD 2862 C CE . LYS B 58 ? 0.8385 1.4199 0.7421 -0.1554 0.0664 0.0574 58 LYS B CE 2863 N NZ . LYS B 58 ? 0.8672 1.5691 0.7503 -0.0896 0.0911 0.0398 58 LYS B NZ 2864 N N . THR B 59 ? 0.8136 0.9084 0.7248 -0.2046 -0.0303 0.0676 59 THR B N 2865 C CA . THR B 59 ? 0.8473 0.8968 0.7408 -0.2307 -0.0445 0.0924 59 THR B CA 2866 C C . THR B 59 ? 0.8959 0.9774 0.7542 -0.2642 -0.0373 0.1116 59 THR B C 2867 O O . THR B 59 ? 0.8997 1.0529 0.7491 -0.2597 -0.0193 0.1042 59 THR B O 2868 C CB . THR B 59 ? 0.8574 0.8647 0.7376 -0.2161 -0.0620 0.0942 59 THR B CB 2869 O OG1 . THR B 59 ? 0.8758 0.8995 0.7222 -0.2116 -0.0585 0.0854 59 THR B OG1 2870 C CG2 . THR B 59 ? 0.8181 0.8116 0.7312 -0.1940 -0.0711 0.0827 59 THR B CG2 2871 N N . ASN B 60 ? 0.7324 0.4806 0.5774 -0.2560 -0.0089 -0.0062 60 ASN B N 2872 C CA . ASN B 60 ? 0.7725 0.5006 0.5858 -0.2899 -0.0083 -0.0026 60 ASN B CA 2873 C C . ASN B 60 ? 0.7334 0.4589 0.5683 -0.2606 -0.0024 0.0024 60 ASN B C 2874 O O . ASN B 60 ? 0.7881 0.4844 0.5906 -0.2830 -0.0009 0.0064 60 ASN B O 2875 C CB . ASN B 60 ? 0.8960 0.5151 0.6133 -0.3209 -0.0091 -0.0062 60 ASN B CB 2876 C CG . ASN B 60 ? 0.9606 0.5787 0.6400 -0.3819 -0.0123 -0.0031 60 ASN B CG 2877 O OD1 . ASN B 60 ? 0.9271 0.6425 0.6544 -0.4072 -0.0151 0.0003 60 ASN B OD1 2878 N ND2 . ASN B 60 ? 1.0683 0.5752 0.6572 -0.4056 -0.0111 -0.0039 60 ASN B ND2 2879 N N . GLN B 61 ? 0.6487 0.4046 0.5343 -0.2149 0.0005 0.0028 61 GLN B N 2880 C CA . GLN B 61 ? 0.6131 0.3656 0.5155 -0.1879 0.0047 0.0073 61 GLN B CA 2881 C C . GLN B 61 ? 0.5366 0.3651 0.4870 -0.1978 0.0063 0.0100 61 GLN B C 2882 O O . GLN B 61 ? 0.4623 0.3616 0.4662 -0.1882 0.0063 0.0086 61 GLN B O 2883 C CB . GLN B 61 ? 0.5845 0.3403 0.5171 -0.1405 0.0069 0.0067 61 GLN B CB 2884 C CG . GLN B 61 ? 0.5784 0.3303 0.5223 -0.1157 0.0094 0.0119 61 GLN B CG 2885 C CD . GLN B 61 ? 0.6644 0.3385 0.5457 -0.1190 0.0097 0.0165 61 GLN B CD 2886 O OE1 . GLN B 61 ? 0.7389 0.3421 0.5643 -0.1191 0.0098 0.0150 61 GLN B OE1 2887 N NE2 . GLN B 61 ? 0.6699 0.3509 0.5541 -0.1209 0.0100 0.0222 61 GLN B NE2 2888 N N . GLN B 62 ? 0.5501 0.3592 0.4758 -0.2150 0.0084 0.0142 62 GLN B N 2889 C CA . GLN B 62 ? 0.5043 0.3810 0.4682 -0.2240 0.0121 0.0160 62 GLN B CA 2890 C C . GLN B 62 ? 0.4481 0.3382 0.4448 -0.1874 0.0155 0.0170 62 GLN B C 2891 O O . GLN B 62 ? 0.4629 0.3002 0.4357 -0.1679 0.0145 0.0200 62 GLN B O 2892 C CB . GLN B 62 ? 0.5630 0.4180 0.4826 -0.2658 0.0134 0.0203 62 GLN B CB 2893 C CG . GLN B 62 ? 0.5336 0.4719 0.4928 -0.2798 0.0190 0.0213 62 GLN B CG 2894 C CD . GLN B 62 ? 0.5979 0.5234 0.5131 -0.3276 0.0209 0.0262 62 GLN B CD 2895 O OE1 . GLN B 62 ? 0.6237 0.5318 0.5228 -0.3298 0.0251 0.0304 62 GLN B OE1 2896 N NE2 . GLN B 62 ? 0.6431 0.5755 0.5335 -0.3703 0.0173 0.0262 62 GLN B NE2 2897 N N . PHE B 63 ? 0.3853 0.3465 0.4334 -0.1781 0.0192 0.0146 63 PHE B N 2898 C CA . PHE B 63 ? 0.3512 0.3267 0.4237 -0.1533 0.0230 0.0144 63 PHE B CA 2899 C C . PHE B 63 ? 0.3481 0.3691 0.4309 -0.1706 0.0298 0.0142 63 PHE B C 2900 O O . PHE B 63 ? 0.3387 0.4122 0.4372 -0.1888 0.0327 0.0131 63 PHE B O 2901 C CB . PHE B 63 ? 0.3002 0.3055 0.4154 -0.1226 0.0231 0.0104 63 PHE B CB 2902 C CG . PHE B 63 ? 0.3029 0.2687 0.4093 -0.1033 0.0183 0.0110 63 PHE B CG 2903 C CD1 . PHE B 63 ? 0.3106 0.2703 0.4120 -0.1070 0.0151 0.0097 63 PHE B CD1 2904 C CD2 . PHE B 63 ? 0.3055 0.2465 0.4084 -0.0818 0.0173 0.0132 63 PHE B CD2 2905 C CE1 . PHE B 63 ? 0.3174 0.2432 0.4088 -0.0880 0.0128 0.0096 63 PHE B CE1 2906 C CE2 . PHE B 63 ? 0.3088 0.2245 0.4061 -0.0623 0.0145 0.0143 63 PHE B CE2 2907 C CZ . PHE B 63 ? 0.3163 0.2226 0.4071 -0.0645 0.0133 0.0120 63 PHE B CZ 2908 N N . GLU B 64 ? 0.3567 0.3624 0.4296 -0.1650 0.0325 0.0159 64 GLU B N 2909 C CA . GLU B 64 ? 0.3654 0.4106 0.4438 -0.1790 0.0406 0.0150 64 GLU B CA 2910 C C . GLU B 64 ? 0.3190 0.3955 0.4312 -0.1511 0.0461 0.0089 64 GLU B C 2911 O O . GLU B 64 ? 0.2934 0.3527 0.4181 -0.1260 0.0421 0.0070 64 GLU B O 2912 C CB . GLU B 64 ? 0.4266 0.4273 0.4589 -0.1981 0.0402 0.0217 64 GLU B CB 2913 C CG . GLU B 64 ? 0.4929 0.4169 0.4740 -0.2078 0.0321 0.0290 64 GLU B CG 2914 C CD . GLU B 64 ? 0.5443 0.4598 0.4979 -0.2449 0.0315 0.0305 64 GLU B CD 2915 O OE1 . GLU B 64 ? 0.5978 0.5301 0.5323 -0.2804 0.0361 0.0335 64 GLU B OE1 2916 O OE2 . GLU B 64 ? 0.5640 0.4546 0.5106 -0.2417 0.0263 0.0289 64 GLU B OE2 2917 N N . LEU B 65 ? 0.3103 0.4310 0.4321 -0.1580 0.0560 0.0057 65 LEU B N 2918 C CA . LEU B 65 ? 0.2912 0.4281 0.4295 -0.1355 0.0631 -0.0013 65 LEU B CA 2919 C C . LEU B 65 ? 0.3021 0.3907 0.4172 -0.1294 0.0577 0.0006 65 LEU B C 2920 O O . LEU B 65 ? 0.3287 0.3876 0.4114 -0.1465 0.0541 0.0076 65 LEU B O 2921 C CB . LEU B 65 ? 0.2972 0.4857 0.4396 -0.1460 0.0766 -0.0049 65 LEU B CB 2922 C CG . LEU B 65 ? 0.2818 0.5390 0.4561 -0.1431 0.0836 -0.0072 65 LEU B CG 2923 C CD1 . LEU B 65 ? 0.2946 0.6105 0.4706 -0.1565 0.0979 -0.0090 65 LEU B CD1 2924 C CD2 . LEU B 65 ? 0.2576 0.5244 0.4608 -0.1051 0.0852 -0.0136 65 LEU B CD2 2925 N N . ILE B 66 ? 0.2897 0.3706 0.4186 -0.1063 0.0562 -0.0044 66 ILE B N 2926 C CA . ILE B 66 ? 0.3052 0.3591 0.4160 -0.1026 0.0520 -0.0037 66 ILE B CA 2927 C C . ILE B 66 ? 0.3023 0.3707 0.4158 -0.0947 0.0611 -0.0141 66 ILE B C 2928 O O . ILE B 66 ? 0.3117 0.3628 0.4072 -0.0966 0.0579 -0.0146 66 ILE B O 2929 C CB . ILE B 66 ? 0.3039 0.3289 0.4155 -0.0896 0.0399 0.0013 66 ILE B CB 2930 C CG1 . ILE B 66 ? 0.2843 0.3157 0.4216 -0.0760 0.0385 -0.0009 66 ILE B CG1 2931 C CG2 . ILE B 66 ? 0.3312 0.3239 0.4158 -0.0965 0.0313 0.0127 66 ILE B CG2 2932 C CD1 . ILE B 66 ? 0.2762 0.3242 0.4325 -0.0633 0.0449 -0.0102 66 ILE B CD1 2933 N N . ASP B 67 ? 0.2946 0.3939 0.4264 -0.0849 0.0724 -0.0222 67 ASP B N 2934 C CA . ASP B 67 ? 0.3071 0.4133 0.4323 -0.0750 0.0842 -0.0333 67 ASP B CA 2935 C C . ASP B 67 ? 0.3125 0.4668 0.4476 -0.0736 0.0993 -0.0374 67 ASP B C 2936 O O . ASP B 67 ? 0.3156 0.4996 0.4607 -0.0880 0.0987 -0.0304 67 ASP B O 2937 C CB . ASP B 67 ? 0.3074 0.3913 0.4379 -0.0542 0.0836 -0.0404 67 ASP B CB 2938 C CG . ASP B 67 ? 0.2886 0.3855 0.4464 -0.0376 0.0827 -0.0387 67 ASP B CG 2939 O OD1 . ASP B 67 ? 0.2790 0.4114 0.4547 -0.0401 0.0843 -0.0341 67 ASP B OD1 2940 O OD2 . ASP B 67 ? 0.2910 0.3622 0.4491 -0.0245 0.0798 -0.0415 67 ASP B OD2 2941 N N . ASN B 68 ? 0.3251 0.4879 0.4540 -0.0575 0.1131 -0.0486 68 ASN B N 2942 C CA . ASN B 68 ? 0.3347 0.5496 0.4680 -0.0557 0.1299 -0.0527 68 ASN B CA 2943 C C . ASN B 68 ? 0.3504 0.5785 0.4903 -0.0197 0.1448 -0.0641 68 ASN B C 2944 O O . ASN B 68 ? 0.3803 0.5644 0.4956 -0.0050 0.1492 -0.0743 68 ASN B O 2945 C CB . ASN B 68 ? 0.3578 0.5671 0.4599 -0.0775 0.1351 -0.0541 68 ASN B CB 2946 C CG . ASN B 68 ? 0.3686 0.6393 0.4741 -0.0815 0.1533 -0.0569 68 ASN B CG 2947 O OD1 . ASN B 68 ? 0.3673 0.6835 0.4950 -0.0572 0.1661 -0.0623 68 ASN B OD1 2948 N ND2 . ASN B 68 ? 0.3850 0.6601 0.4669 -0.1109 0.1551 -0.0524 68 ASN B ND2 2949 N N . GLU B 69 ? 0.3413 0.6304 0.5105 -0.0063 0.1523 -0.0617 69 GLU B N 2950 C CA . GLU B 69 ? 0.3603 0.6692 0.5403 0.0352 0.1650 -0.0688 69 GLU B CA 2951 C C . GLU B 69 ? 0.3943 0.7366 0.5608 0.0510 0.1876 -0.0792 69 GLU B C 2952 O O . GLU B 69 ? 0.4258 0.7610 0.5842 0.0911 0.2010 -0.0885 69 GLU B O 2953 C CB . GLU B 69 ? 0.3372 0.7098 0.5576 0.0411 0.1607 -0.0588 69 GLU B CB 2954 C CG . GLU B 69 ? 0.3528 0.7424 0.5887 0.0873 0.1671 -0.0608 69 GLU B CG 2955 C CD . GLU B 69 ? 0.3236 0.7695 0.5976 0.0852 0.1563 -0.0484 69 GLU B CD 2956 O OE1 . GLU B 69 ? 0.2966 0.7162 0.5740 0.0577 0.1389 -0.0410 69 GLU B OE1 2957 O OE2 . GLU B 69 ? 0.3250 0.8441 0.6238 0.1116 0.1654 -0.0460 69 GLU B OE2 2958 N N . PHE B 70 ? 0.3952 0.7714 0.5555 0.0207 0.1927 -0.0773 70 PHE B N 2959 C CA . PHE B 70 ? 0.4265 0.8413 0.5727 0.0305 0.2154 -0.0868 70 PHE B CA 2960 C C . PHE B 70 ? 0.4663 0.8168 0.5642 0.0180 0.2187 -0.0967 70 PHE B C 2961 O O . PHE B 70 ? 0.5052 0.8664 0.5807 0.0327 0.2386 -0.1084 70 PHE B O 2962 C CB . PHE B 70 ? 0.4090 0.9107 0.5755 0.0001 0.2208 -0.0776 70 PHE B CB 2963 C CG . PHE B 70 ? 0.3770 0.9612 0.5900 0.0074 0.2194 -0.0681 70 PHE B CG 2964 C CD1 . PHE B 70 ? 0.3698 0.9609 0.6054 0.0511 0.2189 -0.0692 70 PHE B CD1 2965 C CD2 . PHE B 70 ? 0.3622 1.0169 0.5917 -0.0327 0.2178 -0.0570 70 PHE B CD2 2966 C CE1 . PHE B 70 ? 0.3442 1.0182 0.6220 0.0564 0.2158 -0.0591 70 PHE B CE1 2967 C CE2 . PHE B 70 ? 0.3389 1.0766 0.6091 -0.0319 0.2153 -0.0480 70 PHE B CE2 2968 C CZ . PHE B 70 ? 0.3284 1.0798 0.6251 0.0138 0.2138 -0.0489 70 PHE B CZ 2969 N N . ASN B 71 ? 0.4654 0.7534 0.5464 -0.0084 0.1993 -0.0919 71 ASN B N 2970 C CA . ASN B 71 ? 0.4998 0.7371 0.5366 -0.0271 0.1984 -0.0981 71 ASN B CA 2971 C C . ASN B 71 ? 0.4871 0.6559 0.5123 -0.0375 0.1768 -0.0945 71 ASN B C 2972 O O . ASN B 71 ? 0.4614 0.6222 0.4907 -0.0643 0.1597 -0.0819 71 ASN B O 2973 C CB . ASN B 71 ? 0.5085 0.7794 0.5374 -0.0642 0.1989 -0.0894 71 ASN B CB 2974 C CG . ASN B 71 ? 0.5611 0.8273 0.5497 -0.0687 0.2150 -0.1005 71 ASN B CG 2975 O OD1 . ASN B 71 ? 0.5989 0.8063 0.5513 -0.0645 0.2135 -0.1107 71 ASN B OD1 2976 N ND2 . ASN B 71 ? 0.5719 0.9022 0.5634 -0.0804 0.2309 -0.0988 71 ASN B ND2 2977 N N . GLU B 72 ? 0.5100 0.6289 0.5169 -0.0157 0.1785 -0.1054 72 GLU B N 2978 C CA . GLU B 72 ? 0.5000 0.5659 0.5028 -0.0226 0.1594 -0.1018 72 GLU B CA 2979 C C . GLU B 72 ? 0.4857 0.5323 0.4721 -0.0567 0.1426 -0.0938 72 GLU B C 2980 O O . GLU B 72 ? 0.5141 0.5526 0.4680 -0.0717 0.1467 -0.0986 72 GLU B O 2981 C CB . GLU B 72 ? 0.5564 0.5631 0.5258 -0.0024 0.1658 -0.1163 72 GLU B CB 2982 C CG . GLU B 72 ? 0.5523 0.5187 0.5278 -0.0045 0.1489 -0.1110 72 GLU B CG 2983 C CD . GLU B 72 ? 0.6209 0.5148 0.5488 0.0009 0.1521 -0.1244 72 GLU B CD 2984 O OE1 . GLU B 72 ? 0.6755 0.5386 0.5576 -0.0058 0.1613 -0.1373 72 GLU B OE1 2985 O OE2 . GLU B 72 ? 0.6316 0.4947 0.5629 0.0091 0.1453 -0.1220 72 GLU B OE2 2986 N N . VAL B 73 ? 0.4434 0.4852 0.4513 -0.0666 0.1238 -0.0810 73 VAL B N 2987 C CA . VAL B 73 ? 0.4374 0.4625 0.4308 -0.0913 0.1067 -0.0718 73 VAL B CA 2988 C C . VAL B 73 ? 0.4665 0.4498 0.4276 -0.0969 0.1020 -0.0807 73 VAL B C 2989 O O . VAL B 73 ? 0.4809 0.4371 0.4325 -0.0827 0.1091 -0.0920 73 VAL B O 2990 C CB . VAL B 73 ? 0.3970 0.4263 0.4187 -0.0946 0.0894 -0.0565 73 VAL B CB 2991 C CG1 . VAL B 73 ? 0.3747 0.4376 0.4192 -0.0959 0.0928 -0.0482 73 VAL B CG1 2992 C CG2 . VAL B 73 ? 0.3816 0.3927 0.4193 -0.0803 0.0841 -0.0587 73 VAL B CG2 2993 N N . GLU B 74 ? 0.4779 0.4550 0.4183 -0.1190 0.0893 -0.0745 74 GLU B N 2994 C CA . GLU B 74 ? 0.5127 0.4593 0.4215 -0.1332 0.0809 -0.0804 74 GLU B CA 2995 C C . GLU B 74 ? 0.5022 0.4286 0.4239 -0.1267 0.0743 -0.0818 74 GLU B C 2996 O O . GLU B 74 ? 0.4581 0.4010 0.4167 -0.1177 0.0668 -0.0711 74 GLU B O 2997 C CB . GLU B 74 ? 0.5159 0.4754 0.4147 -0.1546 0.0627 -0.0667 74 GLU B CB 2998 C CG . GLU B 74 ? 0.5578 0.4994 0.4222 -0.1758 0.0518 -0.0712 74 GLU B CG 2999 C CD . GLU B 74 ? 0.5416 0.4881 0.4254 -0.1801 0.0351 -0.0634 74 GLU B CD 3000 O OE1 . GLU B 74 ? 0.5026 0.4733 0.4245 -0.1684 0.0262 -0.0487 74 GLU B OE1 3001 O OE2 . GLU B 74 ? 0.5755 0.5004 0.4323 -0.1971 0.0314 -0.0723 74 GLU B OE2 3002 N N . LYS B 75 ? 0.5458 0.4319 0.4311 -0.1337 0.0777 -0.0953 75 LYS B N 3003 C CA . LYS B 75 ? 0.5518 0.4081 0.4385 -0.1287 0.0759 -0.0988 75 LYS B CA 3004 C C . LYS B 75 ? 0.5030 0.3821 0.4187 -0.1410 0.0558 -0.0835 75 LYS B C 3005 O O . LYS B 75 ? 0.4714 0.3533 0.4156 -0.1276 0.0547 -0.0785 75 LYS B O 3006 C CB . LYS B 75 ? 0.6358 0.4332 0.4636 -0.1414 0.0824 -0.1161 75 LYS B CB 3007 C CG . LYS B 75 ? 0.6761 0.4240 0.4909 -0.1247 0.0912 -0.1244 75 LYS B CG 3008 C CD . LYS B 75 ? 0.6982 0.4346 0.5114 -0.0861 0.1136 -0.1342 75 LYS B CD 3009 C CE . LYS B 75 ? 0.7341 0.4221 0.5363 -0.0635 0.1204 -0.1385 75 LYS B CE 3010 N NZ . LYS B 75 ? 0.8069 0.4464 0.5652 -0.0327 0.1434 -0.1556 75 LYS B NZ 3011 N N . GLN B 76 ? 0.4957 0.3960 0.4041 -0.1645 0.0403 -0.0755 76 GLN B N 3012 C CA . GLN B 76 ? 0.4583 0.3895 0.3934 -0.1732 0.0224 -0.0608 76 GLN B CA 3013 C C . GLN B 76 ? 0.3972 0.3587 0.3801 -0.1501 0.0201 -0.0472 76 GLN B C 3014 O O . GLN B 76 ? 0.3710 0.3388 0.3780 -0.1438 0.0163 -0.0422 76 GLN B O 3015 C CB . GLN B 76 ? 0.4689 0.4302 0.3909 -0.1966 0.0057 -0.0519 76 GLN B CB 3016 C CG . GLN B 76 ? 0.4413 0.4456 0.3936 -0.2009 -0.0115 -0.0361 76 GLN B CG 3017 C CD . GLN B 76 ? 0.4583 0.4996 0.3958 -0.2260 -0.0294 -0.0276 76 GLN B CD 3018 O OE1 . GLN B 76 ? 0.4702 0.5223 0.3917 -0.2292 -0.0339 -0.0236 76 GLN B OE1 3019 N NE2 . GLN B 76 ? 0.4607 0.5276 0.4042 -0.2448 -0.0403 -0.0233 76 GLN B NE2 3020 N N . ILE B 77 ? 0.3787 0.3555 0.3697 -0.1406 0.0225 -0.0415 77 ILE B N 3021 C CA . ILE B 77 ? 0.3363 0.3321 0.3618 -0.1228 0.0206 -0.0297 77 ILE B CA 3022 C C . ILE B 77 ? 0.3172 0.3009 0.3611 -0.1061 0.0328 -0.0369 77 ILE B C 3023 O O . ILE B 77 ? 0.2869 0.2799 0.3578 -0.0952 0.0291 -0.0299 77 ILE B O 3024 C CB . ILE B 77 ? 0.3369 0.3422 0.3561 -0.1220 0.0206 -0.0217 77 ILE B CB 3025 C CG1 . ILE B 77 ? 0.3102 0.3248 0.3534 -0.1084 0.0154 -0.0084 77 ILE B CG1 3026 C CG2 . ILE B 77 ? 0.3532 0.3496 0.3592 -0.1216 0.0376 -0.0328 77 ILE B CG2 3027 C CD1 . ILE B 77 ? 0.3043 0.3343 0.3554 -0.1039 -0.0007 0.0055 77 ILE B CD1 3028 N N . GLY B 78 ? 0.3404 0.3042 0.3669 -0.1022 0.0472 -0.0506 78 GLY B N 3029 C CA . GLY B 78 ? 0.3328 0.2885 0.3739 -0.0822 0.0589 -0.0567 78 GLY B CA 3030 C C . GLY B 78 ? 0.3291 0.2668 0.3770 -0.0786 0.0543 -0.0563 78 GLY B C 3031 O O . GLY B 78 ? 0.3010 0.2468 0.3747 -0.0634 0.0553 -0.0520 78 GLY B O 3032 N N . ASN B 79 ? 0.3607 0.2751 0.3824 -0.0964 0.0488 -0.0602 79 ASN B N 3033 C CA . ASN B 79 ? 0.3662 0.2634 0.3884 -0.1010 0.0436 -0.0585 79 ASN B CA 3034 C C . ASN B 79 ? 0.3206 0.2557 0.3789 -0.1020 0.0310 -0.0437 79 ASN B C 3035 O O . ASN B 79 ? 0.3067 0.2377 0.3792 -0.0951 0.0305 -0.0404 79 ASN B O 3036 C CB . ASN B 79 ? 0.4192 0.2836 0.3982 -0.1280 0.0402 -0.0662 79 ASN B CB 3037 C CG . ASN B 79 ? 0.4818 0.2867 0.4155 -0.1217 0.0553 -0.0829 79 ASN B CG 3038 O OD1 . ASN B 79 ? 0.4923 0.2783 0.4306 -0.0941 0.0670 -0.0867 79 ASN B OD1 3039 N ND2 . ASN B 79 ? 0.5344 0.3094 0.4212 -0.1457 0.0551 -0.0927 79 ASN B ND2 3040 N N . VAL B 80 ? 0.3020 0.2712 0.3711 -0.1082 0.0214 -0.0346 80 VAL B N 3041 C CA . VAL B 80 ? 0.2686 0.2714 0.3683 -0.1015 0.0117 -0.0209 80 VAL B CA 3042 C C . VAL B 80 ? 0.2442 0.2470 0.3675 -0.0798 0.0178 -0.0185 80 VAL B C 3043 O O . VAL B 80 ? 0.2273 0.2371 0.3694 -0.0721 0.0157 -0.0136 80 VAL B O 3044 C CB . VAL B 80 ? 0.2633 0.2961 0.3639 -0.1048 0.0011 -0.0104 80 VAL B CB 3045 C CG1 . VAL B 80 ? 0.2337 0.2916 0.3609 -0.0881 -0.0053 0.0027 80 VAL B CG1 3046 C CG2 . VAL B 80 ? 0.2870 0.3348 0.3694 -0.1284 -0.0087 -0.0096 80 VAL B CG2 3047 N N . ILE B 81 ? 0.2489 0.2472 0.3693 -0.0729 0.0255 -0.0221 81 ILE B N 3048 C CA . ILE B 81 ? 0.2328 0.2361 0.3723 -0.0581 0.0310 -0.0205 81 ILE B CA 3049 C C . ILE B 81 ? 0.2404 0.2326 0.3893 -0.0470 0.0365 -0.0250 81 ILE B C 3050 O O . ILE B 81 ? 0.2122 0.2126 0.3799 -0.0385 0.0342 -0.0196 81 ILE B O 3051 C CB . ILE B 81 ? 0.2384 0.2463 0.3701 -0.0584 0.0397 -0.0245 81 ILE B CB 3052 C CG1 . ILE B 81 ? 0.2403 0.2549 0.3624 -0.0677 0.0330 -0.0159 81 ILE B CG1 3053 C CG2 . ILE B 81 ? 0.2235 0.2439 0.3737 -0.0469 0.0468 -0.0251 81 ILE B CG2 3054 C CD1 . ILE B 81 ? 0.2571 0.2752 0.3625 -0.0759 0.0410 -0.0194 81 ILE B CD1 3055 N N . ASN B 82 ? 0.2860 0.2543 0.4159 -0.0462 0.0438 -0.0346 82 ASN B N 3056 C CA . ASN B 82 ? 0.3150 0.2637 0.4451 -0.0324 0.0493 -0.0379 82 ASN B CA 3057 C C . ASN B 82 ? 0.2962 0.2385 0.4317 -0.0388 0.0411 -0.0315 82 ASN B C 3058 O O . ASN B 82 ? 0.2726 0.2154 0.4217 -0.0272 0.0413 -0.0275 82 ASN B O 3059 C CB . ASN B 82 ? 0.3956 0.3064 0.4916 -0.0287 0.0596 -0.0500 82 ASN B CB 3060 C CG . ASN B 82 ? 0.4511 0.3752 0.5478 -0.0111 0.0722 -0.0564 82 ASN B CG 3061 O OD1 . ASN B 82 ? 0.4118 0.3755 0.5313 -0.0107 0.0721 -0.0518 82 ASN B OD1 3062 N ND2 . ASN B 82 ? 0.5694 0.4587 0.6366 0.0032 0.0840 -0.0670 82 ASN B ND2 3063 N N . TRP B 83 ? 0.3003 0.2428 0.4248 -0.0589 0.0337 -0.0297 83 TRP B N 3064 C CA . TRP B 83 ? 0.2923 0.2417 0.4230 -0.0694 0.0263 -0.0227 83 TRP B CA 3065 C C . TRP B 83 ? 0.2408 0.2230 0.4035 -0.0573 0.0220 -0.0131 83 TRP B C 3066 O O . TRP B 83 ? 0.2257 0.2076 0.3975 -0.0530 0.0217 -0.0091 83 TRP B O 3067 C CB . TRP B 83 ? 0.3112 0.2732 0.4283 -0.0943 0.0184 -0.0215 83 TRP B CB 3068 C CG . TRP B 83 ? 0.3125 0.3011 0.4397 -0.1082 0.0103 -0.0129 83 TRP B CG 3069 C CD1 . TRP B 83 ? 0.3410 0.3113 0.4524 -0.1253 0.0103 -0.0132 83 TRP B CD1 3070 C CD2 . TRP B 83 ? 0.2895 0.3303 0.4413 -0.1068 0.0017 -0.0021 83 TRP B CD2 3071 N NE1 . TRP B 83 ? 0.3288 0.3465 0.4582 -0.1373 0.0026 -0.0033 83 TRP B NE1 3072 C CE2 . TRP B 83 ? 0.2993 0.3626 0.4550 -0.1227 -0.0025 0.0036 83 TRP B CE2 3073 C CE3 . TRP B 83 ? 0.2727 0.3411 0.4395 -0.0923 -0.0024 0.0040 83 TRP B CE3 3074 C CZ2 . TRP B 83 ? 0.2815 0.4039 0.4611 -0.1206 -0.0097 0.0149 83 TRP B CZ2 3075 C CZ3 . TRP B 83 ? 0.2606 0.3759 0.4459 -0.0873 -0.0101 0.0154 83 TRP B CZ3 3076 C CH2 . TRP B 83 ? 0.2635 0.4104 0.4576 -0.0995 -0.0133 0.0206 83 TRP B CH2 3077 N N . THR B 84 ? 0.2193 0.2229 0.3924 -0.0524 0.0194 -0.0096 84 THR B N 3078 C CA . THR B 84 ? 0.1913 0.2134 0.3837 -0.0406 0.0163 -0.0018 84 THR B CA 3079 C C . THR B 84 ? 0.1830 0.1967 0.3845 -0.0283 0.0216 -0.0035 84 THR B C 3080 O O . THR B 84 ? 0.1721 0.1901 0.3837 -0.0224 0.0202 0.0006 84 THR B O 3081 C CB . THR B 84 ? 0.1876 0.2196 0.3771 -0.0388 0.0128 0.0025 84 THR B CB 3082 O OG1 . THR B 84 ? 0.1912 0.2397 0.3743 -0.0475 0.0056 0.0067 84 THR B OG1 3083 C CG2 . THR B 84 ? 0.1763 0.2115 0.3739 -0.0259 0.0108 0.0093 84 THR B CG2 3084 N N . ARG B 85 ? 0.1914 0.1985 0.3891 -0.0246 0.0279 -0.0094 85 ARG B N 3085 C CA . ARG B 85 ? 0.1858 0.1966 0.3942 -0.0132 0.0318 -0.0099 85 ARG B CA 3086 C C . ARG B 85 ? 0.1875 0.1848 0.3963 -0.0062 0.0323 -0.0091 85 ARG B C 3087 O O . ARG B 85 ? 0.1723 0.1770 0.3919 0.0000 0.0301 -0.0047 85 ARG B O 3088 C CB . ARG B 85 ? 0.2031 0.2205 0.4089 -0.0086 0.0397 -0.0158 85 ARG B CB 3089 C CG . ARG B 85 ? 0.2018 0.2393 0.4223 0.0030 0.0427 -0.0146 85 ARG B CG 3090 C CD . ARG B 85 ? 0.2216 0.2758 0.4414 0.0113 0.0524 -0.0204 85 ARG B CD 3091 N NE . ARG B 85 ? 0.2304 0.2996 0.4463 -0.0035 0.0540 -0.0211 85 ARG B NE 3092 C CZ . ARG B 85 ? 0.2523 0.3162 0.4531 -0.0073 0.0603 -0.0270 85 ARG B CZ 3093 N NH1 . ARG B 85 ? 0.2799 0.3201 0.4649 0.0029 0.0666 -0.0347 85 ARG B NH1 3094 N NH2 . ARG B 85 ? 0.2495 0.3269 0.4448 -0.0228 0.0608 -0.0254 85 ARG B NH2 3095 N N . ASP B 86 ? 0.2094 0.1816 0.4003 -0.0091 0.0351 -0.0134 86 ASP B N 3096 C CA . ASP B 86 ? 0.2262 0.1744 0.4077 -0.0054 0.0355 -0.0116 86 ASP B CA 3097 C C . ASP B 86 ? 0.2058 0.1659 0.3968 -0.0144 0.0291 -0.0039 86 ASP B C 3098 O O . ASP B 86 ? 0.1999 0.1556 0.3937 -0.0077 0.0286 0.0005 86 ASP B O 3099 C CB . ASP B 86 ? 0.2732 0.1802 0.4219 -0.0131 0.0395 -0.0180 86 ASP B CB 3100 C CG . ASP B 86 ? 0.3037 0.1934 0.4378 0.0033 0.0488 -0.0265 86 ASP B CG 3101 O OD1 . ASP B 86 ? 0.2899 0.2084 0.4442 0.0202 0.0521 -0.0261 86 ASP B OD1 3102 O OD2 . ASP B 86 ? 0.3566 0.2044 0.4560 -0.0017 0.0536 -0.0339 86 ASP B OD2 3103 N N . SER B 87 ? 0.1920 0.1713 0.3877 -0.0272 0.0246 -0.0017 87 SER B N 3104 C CA . SER B 87 ? 0.1801 0.1809 0.3869 -0.0314 0.0204 0.0056 87 SER B CA 3105 C C . SER B 87 ? 0.1622 0.1750 0.3840 -0.0167 0.0202 0.0089 87 SER B C 3106 O O . SER B 87 ? 0.1578 0.1733 0.3825 -0.0144 0.0201 0.0130 87 SER B O 3107 C CB . SER B 87 ? 0.1724 0.2010 0.3836 -0.0404 0.0157 0.0085 87 SER B CB 3108 O OG . SER B 87 ? 0.1953 0.2177 0.3903 -0.0597 0.0141 0.0057 87 SER B OG 3109 N N . ILE B 88 ? 0.1514 0.1688 0.3776 -0.0101 0.0203 0.0069 88 ILE B N 3110 C CA . ILE B 88 ? 0.1448 0.1668 0.3767 -0.0021 0.0197 0.0086 88 ILE B CA 3111 C C . ILE B 88 ? 0.1423 0.1600 0.3767 0.0039 0.0210 0.0086 88 ILE B C 3112 O O . ILE B 88 ? 0.1366 0.1573 0.3727 0.0070 0.0194 0.0116 88 ILE B O 3113 C CB . ILE B 88 ? 0.1494 0.1727 0.3783 -0.0033 0.0196 0.0068 88 ILE B CB 3114 C CG1 . ILE B 88 ? 0.1594 0.1836 0.3814 -0.0046 0.0169 0.0096 88 ILE B CG1 3115 C CG2 . ILE B 88 ? 0.1505 0.1735 0.3777 -0.0021 0.0187 0.0076 88 ILE B CG2 3116 C CD1 . ILE B 88 ? 0.1618 0.1901 0.3831 0.0039 0.0150 0.0146 88 ILE B CD1 3117 N N . THR B 89 ? 0.1505 0.1616 0.3827 0.0079 0.0241 0.0054 89 THR B N 3118 C CA . THR B 89 ? 0.1585 0.1674 0.3916 0.0194 0.0249 0.0073 89 THR B CA 3119 C C . THR B 89 ? 0.1713 0.1645 0.3967 0.0189 0.0231 0.0125 89 THR B C 3120 O O . THR B 89 ? 0.1725 0.1700 0.3997 0.0258 0.0207 0.0170 89 THR B O 3121 C CB . THR B 89 ? 0.1782 0.1759 0.4039 0.0299 0.0304 0.0031 89 THR B CB 3122 O OG1 . THR B 89 ? 0.1723 0.1942 0.4071 0.0306 0.0332 -0.0008 89 THR B OG1 3123 C CG2 . THR B 89 ? 0.1964 0.1878 0.4187 0.0482 0.0309 0.0072 89 THR B CG2 3124 N N . GLU B 90 ? 0.1818 0.1601 0.3968 0.0077 0.0239 0.0124 90 GLU B N 3125 C CA . GLU B 90 ? 0.2018 0.1672 0.4063 0.0012 0.0232 0.0178 90 GLU B CA 3126 C C . GLU B 90 ? 0.1772 0.1664 0.3928 0.0004 0.0211 0.0221 90 GLU B C 3127 O O . GLU B 90 ? 0.1813 0.1654 0.3913 0.0023 0.0205 0.0271 90 GLU B O 3128 C CB . GLU B 90 ? 0.2291 0.1823 0.4195 -0.0173 0.0241 0.0166 90 GLU B CB 3129 C CG . GLU B 90 ? 0.2802 0.1979 0.4439 -0.0272 0.0253 0.0202 90 GLU B CG 3130 C CD . GLU B 90 ? 0.3260 0.1983 0.4665 -0.0119 0.0282 0.0186 90 GLU B CD 3131 O OE1 . GLU B 90 ? 0.3315 0.2073 0.4798 0.0063 0.0303 0.0136 90 GLU B OE1 3132 O OE2 . GLU B 90 ? 0.3789 0.2113 0.4903 -0.0168 0.0290 0.0232 90 GLU B OE2 3133 N N . VAL B 91 ? 0.1509 0.1612 0.3773 -0.0003 0.0205 0.0203 91 VAL B N 3134 C CA . VAL B 91 ? 0.1420 0.1664 0.3717 0.0038 0.0203 0.0225 91 VAL B CA 3135 C C . VAL B 91 ? 0.1414 0.1619 0.3692 0.0106 0.0183 0.0225 91 VAL B C 3136 O O . VAL B 91 ? 0.1465 0.1678 0.3687 0.0116 0.0182 0.0256 91 VAL B O 3137 C CB . VAL B 91 ? 0.1345 0.1711 0.3677 0.0072 0.0203 0.0207 91 VAL B CB 3138 C CG1 . VAL B 91 ? 0.1365 0.1742 0.3635 0.0159 0.0217 0.0211 91 VAL B CG1 3139 C CG2 . VAL B 91 ? 0.1352 0.1903 0.3727 0.0011 0.0208 0.0231 91 VAL B CG2 3140 N N . TRP B 92 ? 0.1355 0.1570 0.3669 0.0129 0.0165 0.0194 92 TRP B N 3141 C CA . TRP B 92 ? 0.1357 0.1643 0.3662 0.0147 0.0130 0.0200 92 TRP B CA 3142 C C . TRP B 92 ? 0.1438 0.1726 0.3734 0.0214 0.0108 0.0254 92 TRP B C 3143 O O . TRP B 92 ? 0.1459 0.1816 0.3708 0.0212 0.0070 0.0283 92 TRP B O 3144 C CB . TRP B 92 ? 0.1320 0.1724 0.3677 0.0117 0.0119 0.0166 92 TRP B CB 3145 C CG . TRP B 92 ? 0.1386 0.1706 0.3647 0.0037 0.0123 0.0133 92 TRP B CG 3146 C CD1 . TRP B 92 ? 0.1375 0.1648 0.3627 0.0009 0.0143 0.0109 92 TRP B CD1 3147 C CD2 . TRP B 92 ? 0.1531 0.1720 0.3616 -0.0006 0.0110 0.0123 92 TRP B CD2 3148 N NE1 . TRP B 92 ? 0.1546 0.1649 0.3621 -0.0034 0.0138 0.0099 92 TRP B NE1 3149 C CE2 . TRP B 92 ? 0.1662 0.1677 0.3612 -0.0038 0.0124 0.0099 92 TRP B CE2 3150 C CE3 . TRP B 92 ? 0.1648 0.1803 0.3621 -0.0018 0.0089 0.0131 92 TRP B CE3 3151 C CZ2 . TRP B 92 ? 0.1938 0.1674 0.3609 -0.0058 0.0127 0.0080 92 TRP B CZ2 3152 C CZ3 . TRP B 92 ? 0.1901 0.1810 0.3606 -0.0062 0.0096 0.0096 92 TRP B CZ3 3153 C CH2 . TRP B 92 ? 0.2072 0.1741 0.3613 -0.0070 0.0118 0.0070 92 TRP B CH2 3154 N N . SER B 93 ? 0.1554 0.1716 0.3836 0.0276 0.0128 0.0269 93 SER B N 3155 C CA . SER B 93 ? 0.1772 0.1823 0.3965 0.0381 0.0109 0.0337 93 SER B CA 3156 C C . SER B 93 ? 0.1884 0.1823 0.3951 0.0312 0.0102 0.0393 93 SER B C 3157 O O . SER B 93 ? 0.1963 0.1906 0.3956 0.0369 0.0062 0.0459 93 SER B O 3158 C CB . SER B 93 ? 0.2014 0.1785 0.4097 0.0459 0.0150 0.0332 93 SER B CB 3159 O OG . SER B 93 ? 0.1976 0.1882 0.4160 0.0551 0.0174 0.0279 93 SER B OG 3160 N N . TYR B 94 ? 0.1838 0.1741 0.3886 0.0189 0.0142 0.0372 94 TYR B N 3161 C CA . TYR B 94 ? 0.1958 0.1861 0.3910 0.0108 0.0158 0.0417 94 TYR B CA 3162 C C . TYR B 94 ? 0.1883 0.1956 0.3847 0.0132 0.0142 0.0404 94 TYR B C 3163 O O . TYR B 94 ? 0.1988 0.2042 0.3837 0.0132 0.0124 0.0456 94 TYR B O 3164 C CB . TYR B 94 ? 0.1952 0.1931 0.3928 -0.0016 0.0208 0.0401 94 TYR B CB 3165 C CG . TYR B 94 ? 0.2028 0.2178 0.3965 -0.0086 0.0248 0.0437 94 TYR B CG 3166 C CD1 . TYR B 94 ? 0.2307 0.2361 0.4083 -0.0210 0.0267 0.0510 94 TYR B CD1 3167 C CD2 . TYR B 94 ? 0.1922 0.2304 0.3939 -0.0021 0.0278 0.0398 94 TYR B CD2 3168 C CE1 . TYR B 94 ? 0.2368 0.2659 0.4116 -0.0282 0.0321 0.0544 94 TYR B CE1 3169 C CE2 . TYR B 94 ? 0.1990 0.2572 0.3965 -0.0039 0.0337 0.0424 94 TYR B CE2 3170 C CZ . TYR B 94 ? 0.2199 0.2789 0.4067 -0.0176 0.0361 0.0496 94 TYR B CZ 3171 O OH . TYR B 94 ? 0.2293 0.3163 0.4130 -0.0201 0.0437 0.0522 94 TYR B OH 3172 N N . ASN B 95 ? 0.1763 0.1940 0.3804 0.0139 0.0148 0.0337 95 ASN B N 3173 C CA . ASN B 95 ? 0.1825 0.2035 0.3775 0.0138 0.0138 0.0304 95 ASN B CA 3174 C C . ASN B 95 ? 0.1902 0.2153 0.3794 0.0133 0.0066 0.0336 95 ASN B C 3175 O O . ASN B 95 ? 0.2033 0.2273 0.3774 0.0106 0.0055 0.0349 95 ASN B O 3176 C CB . ASN B 95 ? 0.1809 0.1996 0.3767 0.0135 0.0143 0.0235 95 ASN B CB 3177 C CG . ASN B 95 ? 0.1852 0.2038 0.3818 0.0182 0.0205 0.0215 95 ASN B CG 3178 O OD1 . ASN B 95 ? 0.1906 0.2197 0.3898 0.0198 0.0249 0.0248 95 ASN B OD1 3179 N ND2 . ASN B 95 ? 0.1926 0.2026 0.3853 0.0199 0.0205 0.0174 95 ASN B ND2 3180 N N . ALA B 96 ? 0.1830 0.2176 0.3838 0.0169 0.0019 0.0351 96 ALA B N 3181 C CA . ALA B 96 ? 0.1917 0.2444 0.3920 0.0188 -0.0063 0.0399 96 ALA B CA 3182 C C . ALA B 96 ? 0.2103 0.2567 0.3995 0.0252 -0.0092 0.0494 96 ALA B C 3183 O O . ALA B 96 ? 0.2149 0.2725 0.3935 0.0217 -0.0156 0.0529 96 ALA B O 3184 C CB . ALA B 96 ? 0.1821 0.2548 0.4001 0.0267 -0.0085 0.0406 96 ALA B CB 3185 N N . GLU B 97 ? 0.2236 0.2485 0.4100 0.0318 -0.0051 0.0538 97 GLU B N 3186 C CA . GLU B 97 ? 0.2545 0.2619 0.4225 0.0361 -0.0070 0.0643 97 GLU B CA 3187 C C . GLU B 97 ? 0.2556 0.2609 0.4081 0.0238 -0.0046 0.0650 97 GLU B C 3188 O O . GLU B 97 ? 0.2730 0.2782 0.4096 0.0245 -0.0097 0.0727 97 GLU B O 3189 C CB . GLU B 97 ? 0.2819 0.2558 0.4408 0.0381 -0.0015 0.0672 97 GLU B CB 3190 C CG . GLU B 97 ? 0.3329 0.2754 0.4637 0.0410 -0.0032 0.0794 97 GLU B CG 3191 C CD . GLU B 97 ? 0.3717 0.2966 0.4929 0.0650 -0.0082 0.0874 97 GLU B CD 3192 O OE1 . GLU B 97 ? 0.3710 0.2976 0.5045 0.0772 -0.0062 0.0819 97 GLU B OE1 3193 O OE2 . GLU B 97 ? 0.4169 0.3255 0.5155 0.0740 -0.0135 0.0996 97 GLU B OE2 3194 N N . LEU B 98 ? 0.2363 0.2422 0.3919 0.0148 0.0035 0.0575 98 LEU B N 3195 C CA . LEU B 98 ? 0.2446 0.2529 0.3857 0.0071 0.0090 0.0569 98 LEU B CA 3196 C C . LEU B 98 ? 0.2486 0.2649 0.3788 0.0058 0.0053 0.0520 98 LEU B C 3197 O O . LEU B 98 ? 0.2671 0.2821 0.3769 0.0016 0.0059 0.0546 98 LEU B O 3198 C CB . LEU B 98 ? 0.2335 0.2490 0.3829 0.0036 0.0191 0.0510 98 LEU B CB 3199 C CG . LEU B 98 ? 0.2467 0.2733 0.3833 0.0007 0.0279 0.0497 98 LEU B CG 3200 C CD1 . LEU B 98 ? 0.2683 0.2914 0.3882 -0.0088 0.0294 0.0599 98 LEU B CD1 3201 C CD2 . LEU B 98 ? 0.2360 0.2818 0.3857 0.0030 0.0371 0.0452 98 LEU B CD2 3202 N N . LEU B 99 ? 0.2350 0.2569 0.3737 0.0059 0.0018 0.0447 99 LEU B N 3203 C CA . LEU B 99 ? 0.2487 0.2714 0.3694 -0.0018 -0.0024 0.0388 99 LEU B CA 3204 C C . LEU B 99 ? 0.2633 0.2987 0.3739 -0.0052 -0.0132 0.0471 99 LEU B C 3205 O O . LEU B 99 ? 0.2836 0.3146 0.3688 -0.0129 -0.0143 0.0459 99 LEU B O 3206 C CB . LEU B 99 ? 0.2398 0.2656 0.3689 -0.0065 -0.0056 0.0319 99 LEU B CB 3207 C CG . LEU B 99 ? 0.2629 0.2879 0.3694 -0.0223 -0.0124 0.0264 99 LEU B CG 3208 C CD1 . LEU B 99 ? 0.2916 0.2823 0.3630 -0.0259 -0.0044 0.0166 99 LEU B CD1 3209 C CD2 . LEU B 99 ? 0.2538 0.2905 0.3731 -0.0305 -0.0166 0.0234 99 LEU B CD2 3210 N N . VAL B 100 ? 0.2562 0.3079 0.3846 0.0029 -0.0208 0.0557 100 VAL B N 3211 C CA . VAL B 100 ? 0.2728 0.3453 0.3952 0.0049 -0.0330 0.0660 100 VAL B CA 3212 C C . VAL B 100 ? 0.2986 0.3551 0.3984 0.0069 -0.0325 0.0753 100 VAL B C 3213 O O . VAL B 100 ? 0.3183 0.3846 0.3984 -0.0001 -0.0401 0.0791 100 VAL B O 3214 C CB . VAL B 100 ? 0.2634 0.3591 0.4099 0.0210 -0.0394 0.0736 100 VAL B CB 3215 C CG1 . VAL B 100 ? 0.2855 0.4070 0.4264 0.0305 -0.0523 0.0875 100 VAL B CG1 3216 C CG2 . VAL B 100 ? 0.2461 0.3675 0.4110 0.0131 -0.0407 0.0650 100 VAL B CG2 3217 N N . ALA B 101 ? 0.3013 0.3335 0.4002 0.0123 -0.0238 0.0788 101 ALA B N 3218 C CA . ALA B 101 ? 0.3331 0.3477 0.4072 0.0098 -0.0219 0.0886 101 ALA B CA 3219 C C . ALA B 101 ? 0.3492 0.3643 0.4020 -0.0039 -0.0155 0.0816 101 ALA B C 3220 O O . ALA B 101 ? 0.3732 0.3876 0.4009 -0.0086 -0.0197 0.0885 101 ALA B O 3221 C CB . ALA B 101 ? 0.3354 0.3241 0.4099 0.0109 -0.0132 0.0927 101 ALA B CB 3222 N N . MET B 102 ? 0.3399 0.3545 0.3994 -0.0075 -0.0050 0.0683 102 MET B N 3223 C CA . MET B 102 ? 0.3668 0.3781 0.4032 -0.0141 0.0036 0.0592 102 MET B CA 3224 C C . MET B 102 ? 0.3761 0.3887 0.3895 -0.0224 -0.0059 0.0550 102 MET B C 3225 O O . MET B 102 ? 0.4038 0.4115 0.3865 -0.0291 -0.0043 0.0550 102 MET B O 3226 C CB . MET B 102 ? 0.3783 0.3869 0.4255 -0.0092 0.0155 0.0467 102 MET B CB 3227 C CG . MET B 102 ? 0.4274 0.4274 0.4471 -0.0080 0.0270 0.0361 102 MET B CG 3228 S SD . MET B 102 ? 0.5056 0.4805 0.4956 -0.0134 0.0223 0.0220 102 MET B SD 3229 C CE . MET B 102 ? 0.4695 0.4362 0.4822 -0.0034 0.0264 0.0146 102 MET B CE 3230 N N . GLU B 103 ? 0.3529 0.3742 0.3781 -0.0251 -0.0155 0.0513 103 GLU B N 3231 C CA . GLU B 103 ? 0.3700 0.3977 0.3719 -0.0401 -0.0264 0.0477 103 GLU B CA 3232 C C . GLU B 103 ? 0.3803 0.4269 0.3704 -0.0427 -0.0390 0.0615 103 GLU B C 3233 O O . GLU B 103 ? 0.4083 0.4521 0.3642 -0.0567 -0.0433 0.0589 103 GLU B O 3234 C CB . GLU B 103 ? 0.3568 0.4017 0.3773 -0.0465 -0.0354 0.0444 103 GLU B CB 3235 C CG . GLU B 103 ? 0.3537 0.3742 0.3744 -0.0482 -0.0255 0.0308 103 GLU B CG 3236 C CD . GLU B 103 ? 0.3990 0.3842 0.3735 -0.0627 -0.0210 0.0170 103 GLU B CD 3237 O OE1 . GLU B 103 ? 0.4355 0.4143 0.3765 -0.0730 -0.0238 0.0160 103 GLU B OE1 3238 O OE2 . GLU B 103 ? 0.4108 0.3685 0.3772 -0.0629 -0.0139 0.0070 103 GLU B OE2 3239 N N . ASN B 104 ? 0.3580 0.4188 0.3711 -0.0281 -0.0449 0.0762 104 ASN B N 3240 C CA . ASN B 104 ? 0.3747 0.4526 0.3771 -0.0241 -0.0585 0.0926 104 ASN B CA 3241 C C . ASN B 104 ? 0.4023 0.4580 0.3707 -0.0292 -0.0526 0.0971 104 ASN B C 3242 O O . ASN B 104 ? 0.4314 0.4972 0.3736 -0.0369 -0.0627 0.1038 104 ASN B O 3243 C CB . ASN B 104 ? 0.3623 0.4475 0.3901 -0.0014 -0.0636 0.1069 104 ASN B CB 3244 C CG . ASN B 104 ? 0.3378 0.4582 0.3978 0.0053 -0.0710 0.1049 104 ASN B CG 3245 O OD1 . ASN B 104 ? 0.3293 0.4727 0.3917 -0.0117 -0.0751 0.0951 104 ASN B OD1 3246 N ND2 . ASN B 104 ? 0.3320 0.4541 0.4120 0.0289 -0.0720 0.1142 104 ASN B ND2 3247 N N . GLN B 105 ? 0.4512 0.4501 0.2933 0.0388 -0.0982 0.0392 105 GLN B N 3248 C CA . GLN B 105 ? 0.4709 0.4829 0.2926 0.0228 -0.0896 0.0376 105 GLN B CA 3249 C C . GLN B 105 ? 0.4596 0.4956 0.2904 0.0355 -0.0912 0.0295 105 GLN B C 3250 O O . GLN B 105 ? 0.4804 0.5120 0.2895 0.0306 -0.0904 0.0313 105 GLN B O 3251 C CB . GLN B 105 ? 0.4674 0.5181 0.2947 0.0022 -0.0780 0.0315 105 GLN B CB 3252 C CG . GLN B 105 ? 0.5008 0.5720 0.2966 -0.0285 -0.0668 0.0299 105 GLN B CG 3253 C CD . GLN B 105 ? 0.5636 0.5677 0.2990 -0.0602 -0.0630 0.0417 105 GLN B CD 3254 O OE1 . GLN B 105 ? 0.5818 0.5464 0.3012 -0.0681 -0.0634 0.0468 105 GLN B OE1 3255 N NE2 . GLN B 105 ? 0.6099 0.5904 0.2997 -0.0786 -0.0591 0.0458 105 GLN B NE2 3256 N N . HIS B 106 ? 0.4387 0.4882 0.2899 0.0518 -0.0936 0.0206 106 HIS B N 3257 C CA . HIS B 106 ? 0.4493 0.5010 0.2902 0.0656 -0.0946 0.0114 106 HIS B CA 3258 C C . HIS B 106 ? 0.4591 0.4840 0.2862 0.0626 -0.1030 0.0144 106 HIS B C 3259 O O . HIS B 106 ? 0.4767 0.5004 0.2849 0.0629 -0.1025 0.0108 106 HIS B O 3260 C CB . HIS B 106 ? 0.4524 0.5001 0.2939 0.0862 -0.0954 0.0016 106 HIS B CB 3261 C CG . HIS B 106 ? 0.4908 0.5178 0.2985 0.1054 -0.0960 -0.0090 106 HIS B CG 3262 N ND1 . HIS B 106 ? 0.5233 0.4935 0.2993 0.1046 -0.1023 -0.0121 106 HIS B ND1 3263 C CD2 . HIS B 106 ? 0.5139 0.5656 0.3041 0.1246 -0.0904 -0.0187 106 HIS B CD2 3264 C CE1 . HIS B 106 ? 0.5722 0.5153 0.3040 0.1233 -0.1007 -0.0222 106 HIS B CE1 3265 N NE2 . HIS B 106 ? 0.5640 0.5596 0.3071 0.1411 -0.0941 -0.0266 106 HIS B NE2 3266 N N . THR B 107 ? 0.4474 0.4623 0.2837 0.0592 -0.1107 0.0195 107 THR B N 3267 C CA . THR B 107 ? 0.4555 0.4721 0.2821 0.0545 -0.1194 0.0202 107 THR B CA 3268 C C . THR B 107 ? 0.4719 0.4931 0.2827 0.0562 -0.1212 0.0273 107 THR B C 3269 O O . THR B 107 ? 0.4856 0.5141 0.2815 0.0524 -0.1248 0.0241 107 THR B O 3270 C CB . THR B 107 ? 0.4398 0.4696 0.2820 0.0542 -0.1268 0.0225 107 THR B CB 3271 O OG1 . THR B 107 ? 0.4371 0.4557 0.2820 0.0459 -0.1259 0.0148 107 THR B OG1 3272 C CG2 . THR B 107 ? 0.4478 0.5101 0.2827 0.0523 -0.1364 0.0218 107 THR B CG2 3273 N N . ILE B 108 ? 0.4813 0.4896 0.2846 0.0590 -0.1184 0.0368 108 ILE B N 3274 C CA . ILE B 108 ? 0.5181 0.5096 0.2875 0.0607 -0.1197 0.0452 108 ILE B CA 3275 C C . ILE B 108 ? 0.5295 0.5275 0.2872 0.0486 -0.1118 0.0408 108 ILE B C 3276 O O . ILE B 108 ? 0.5487 0.5461 0.2858 0.0504 -0.1158 0.0424 108 ILE B O 3277 C CB . ILE B 108 ? 0.5520 0.5017 0.2913 0.0593 -0.1163 0.0559 108 ILE B CB 3278 C CG1 . ILE B 108 ? 0.5571 0.4978 0.2958 0.0829 -0.1265 0.0602 108 ILE B CG1 3279 C CG2 . ILE B 108 ? 0.6113 0.5209 0.2937 0.0535 -0.1144 0.0646 108 ILE B CG2 3280 C CD1 . ILE B 108 ? 0.6042 0.4850 0.3005 0.0842 -0.1235 0.0693 108 ILE B CD1 3281 N N . ASP B 109 ? 0.5189 0.5324 0.2888 0.0397 -0.1011 0.0339 109 ASP B N 3282 C CA . ASP B 109 ? 0.5319 0.5676 0.2921 0.0335 -0.0927 0.0264 109 ASP B CA 3283 C C . ASP B 109 ? 0.5329 0.5704 0.2917 0.0454 -0.0971 0.0169 109 ASP B C 3284 O O . ASP B 109 ? 0.5528 0.5945 0.2923 0.0430 -0.0952 0.0142 109 ASP B O 3285 C CB . ASP B 109 ? 0.5208 0.5959 0.2958 0.0299 -0.0815 0.0174 109 ASP B CB 3286 C CG . ASP B 109 ? 0.5386 0.6162 0.2998 0.0022 -0.0734 0.0241 109 ASP B CG 3287 O OD1 . ASP B 109 ? 0.5799 0.6209 0.3016 -0.0166 -0.0726 0.0343 109 ASP B OD1 3288 O OD2 . ASP B 109 ? 0.5245 0.6350 0.3045 -0.0025 -0.0677 0.0187 109 ASP B OD2 3289 N N . LEU B 110 ? 0.5226 0.5492 0.2922 0.0538 -0.1023 0.0116 110 LEU B N 3290 C CA . LEU B 110 ? 0.5453 0.5526 0.2935 0.0559 -0.1059 0.0019 110 LEU B CA 3291 C C . LEU B 110 ? 0.5568 0.5669 0.2915 0.0439 -0.1134 0.0056 110 LEU B C 3292 O O . LEU B 110 ? 0.5835 0.5847 0.2917 0.0401 -0.1127 -0.0013 110 LEU B O 3293 C CB . LEU B 110 ? 0.5469 0.5312 0.2959 0.0562 -0.1098 -0.0024 110 LEU B CB 3294 C CG . LEU B 110 ? 0.5893 0.5334 0.2980 0.0448 -0.1136 -0.0121 110 LEU B CG 3295 C CD1 . LEU B 110 ? 0.6021 0.5127 0.3017 0.0500 -0.1132 -0.0162 110 LEU B CD1 3296 C CD2 . LEU B 110 ? 0.5871 0.5534 0.2968 0.0190 -0.1220 -0.0097 110 LEU B CD2 3297 N N . ALA B 111 ? 0.5422 0.5675 0.2904 0.0424 -0.1210 0.0154 111 ALA B N 3298 C CA . ALA B 111 ? 0.5554 0.6000 0.2904 0.0400 -0.1300 0.0188 111 ALA B CA 3299 C C . ALA B 111 ? 0.5780 0.6156 0.2914 0.0426 -0.1266 0.0245 111 ALA B C 3300 O O . ALA B 111 ? 0.5950 0.6435 0.2898 0.0385 -0.1309 0.0225 111 ALA B O 3301 C CB . ALA B 111 ? 0.5452 0.6123 0.2919 0.0523 -0.1398 0.0266 111 ALA B CB 3302 N N . ASP B 112 ? 0.5827 0.6043 0.2934 0.0436 -0.1182 0.0310 112 ASP B N 3303 C CA . ASP B 112 ? 0.6138 0.6254 0.2950 0.0366 -0.1123 0.0361 112 ASP B CA 3304 C C . ASP B 112 ? 0.6185 0.6455 0.2949 0.0312 -0.1060 0.0242 112 ASP B C 3305 O O . ASP B 112 ? 0.6408 0.6677 0.2934 0.0275 -0.1077 0.0255 112 ASP B O 3306 C CB . ASP B 112 ? 0.6246 0.6229 0.2979 0.0243 -0.1015 0.0413 112 ASP B CB 3307 C CG . ASP B 112 ? 0.6768 0.6514 0.3011 0.0068 -0.0956 0.0494 112 ASP B CG 3308 O OD1 . ASP B 112 ? 0.7053 0.6648 0.3007 0.0129 -0.1024 0.0545 112 ASP B OD1 3309 O OD2 . ASP B 112 ? 0.6961 0.6685 0.3047 -0.0175 -0.0836 0.0500 112 ASP B OD2 3310 N N . SER B 113 ? 0.6049 0.6405 0.2965 0.0361 -0.0997 0.0122 113 SER B N 3311 C CA . SER B 113 ? 0.6250 0.6662 0.2997 0.0418 -0.0935 -0.0013 113 SER B CA 3312 C C . SER B 113 ? 0.6488 0.6687 0.2995 0.0378 -0.1011 -0.0065 113 SER B C 3313 O O . SER B 113 ? 0.6741 0.6935 0.2996 0.0368 -0.0980 -0.0124 113 SER B O 3314 C CB . SER B 113 ? 0.6223 0.6673 0.3033 0.0608 -0.0875 -0.0136 113 SER B CB 3315 O OG . SER B 113 ? 0.6347 0.6394 0.3047 0.0656 -0.0944 -0.0184 113 SER B OG 3316 N N . GLU B 114 ? 0.6443 0.6524 0.2990 0.0309 -0.1102 -0.0060 114 GLU B N 3317 C CA . GLU B 114 ? 0.6740 0.6724 0.3003 0.0144 -0.1168 -0.0129 114 GLU B CA 3318 C C . GLU B 114 ? 0.6793 0.7060 0.2999 0.0088 -0.1222 -0.0060 114 GLU B C 3319 O O . GLU B 114 ? 0.7104 0.7319 0.3007 -0.0026 -0.1227 -0.0135 114 GLU B O 3320 C CB . GLU B 114 ? 0.6687 0.6718 0.3012 -0.0013 -0.1248 -0.0144 114 GLU B CB 3321 C CG . GLU B 114 ? 0.6856 0.6431 0.3037 -0.0011 -0.1205 -0.0227 114 GLU B CG 3322 C CD . GLU B 114 ? 0.7549 0.6465 0.3078 -0.0053 -0.1153 -0.0371 114 GLU B CD 3323 O OE1 . GLU B 114 ? 0.7919 0.6760 0.3093 -0.0247 -0.1168 -0.0429 114 GLU B OE1 3324 O OE2 . GLU B 114 ? 0.7840 0.6254 0.3121 0.0139 -0.1102 -0.0432 114 GLU B OE2 3325 N N . MET B 115 ? 0.6613 0.7082 0.3001 0.0187 -0.1264 0.0081 115 MET B N 3326 C CA . MET B 115 ? 0.6814 0.7417 0.3015 0.0220 -0.1321 0.0169 115 MET B CA 3327 C C . MET B 115 ? 0.7033 0.7498 0.3014 0.0170 -0.1218 0.0143 115 MET B C 3328 O O . MET B 115 ? 0.7271 0.7811 0.3018 0.0113 -0.1250 0.0126 115 MET B O 3329 C CB . MET B 115 ? 0.6835 0.7368 0.3027 0.0392 -0.1370 0.0328 115 MET B CB 3330 C CG . MET B 115 ? 0.7245 0.7691 0.3041 0.0501 -0.1435 0.0442 115 MET B CG 3331 S SD . MET B 115 ? 0.7358 0.8363 0.3082 0.0694 -0.1637 0.0438 115 MET B SD 3332 C CE . MET B 115 ? 0.7450 0.8690 0.3063 0.0437 -0.1614 0.0318 115 MET B CE 3333 N N . ASP B 116 ? 0.6966 0.7345 0.3023 0.0184 -0.1095 0.0126 116 ASP B N 3334 C CA . ASP B 116 ? 0.7167 0.7615 0.3045 0.0136 -0.0978 0.0073 116 ASP B CA 3335 C C . ASP B 116 ? 0.7358 0.7766 0.3060 0.0173 -0.0954 -0.0090 116 ASP B C 3336 O O . ASP B 116 ? 0.7602 0.8065 0.3062 0.0127 -0.0921 -0.0123 116 ASP B O 3337 C CB . ASP B 116 ? 0.7036 0.7661 0.3066 0.0132 -0.0852 0.0050 116 ASP B CB 3338 C CG . ASP B 116 ? 0.7248 0.8182 0.3098 0.0033 -0.0722 -0.0011 116 ASP B CG 3339 O OD1 . ASP B 116 ? 0.7534 0.8377 0.3095 -0.0141 -0.0718 0.0080 116 ASP B OD1 3340 O OD2 . ASP B 116 ? 0.7198 0.8505 0.3148 0.0154 -0.0626 -0.0160 116 ASP B OD2 3341 N N . LYS B 117 ? 0.7369 0.7568 0.3075 0.0248 -0.0967 -0.0193 117 LYS B N 3342 C CA . LYS B 117 ? 0.7818 0.7682 0.3110 0.0287 -0.0945 -0.0355 117 LYS B CA 3343 C C . LYS B 117 ? 0.8094 0.7881 0.3104 0.0064 -0.1022 -0.0363 117 LYS B C 3344 O O . LYS B 117 ? 0.8522 0.8092 0.3120 0.0058 -0.0982 -0.0472 117 LYS B O 3345 C CB . LYS B 117 ? 0.7990 0.7411 0.3132 0.0368 -0.0954 -0.0443 117 LYS B CB 3346 C CG . LYS B 117 ? 0.8065 0.7471 0.3178 0.0718 -0.0861 -0.0534 117 LYS B CG 3347 C CD . LYS B 117 ? 0.7876 0.7153 0.3181 0.0804 -0.0883 -0.0513 117 LYS B CD 3348 C CE . LYS B 117 ? 0.8381 0.6896 0.3194 0.0692 -0.0940 -0.0578 117 LYS B CE 3349 N NZ . LYS B 117 ? 0.8395 0.6670 0.3214 0.0904 -0.0935 -0.0598 117 LYS B NZ 3350 N N . LEU B 118 ? 0.7881 0.7915 0.3085 -0.0091 -0.1134 -0.0263 118 LEU B N 3351 C CA . LEU B 118 ? 0.8085 0.8317 0.3084 -0.0294 -0.1223 -0.0270 118 LEU B CA 3352 C C . LEU B 118 ? 0.8157 0.8568 0.3087 -0.0231 -0.1209 -0.0197 118 LEU B C 3353 O O . LEU B 118 ? 0.8482 0.8873 0.3093 -0.0348 -0.1211 -0.0267 118 LEU B O 3354 C CB . LEU B 118 ? 0.7823 0.8515 0.3071 -0.0368 -0.1356 -0.0196 118 LEU B CB 3355 C CG . LEU B 118 ? 0.7975 0.9183 0.3077 -0.0530 -0.1474 -0.0210 118 LEU B CG 3356 C CD1 . LEU B 118 ? 0.8468 0.9454 0.3099 -0.0893 -0.1444 -0.0386 118 LEU B CD1 3357 C CD2 . LEU B 118 ? 0.7716 0.9580 0.3089 -0.0502 -0.1605 -0.0168 118 LEU B CD2 3358 N N . TYR B 119 ? 0.7957 0.8468 0.3092 -0.0091 -0.1187 -0.0060 119 TYR B N 3359 C CA . TYR B 119 ? 0.8154 0.8710 0.3099 -0.0088 -0.1157 0.0021 119 TYR B CA 3360 C C . TYR B 119 ? 0.8387 0.8885 0.3122 -0.0120 -0.1028 -0.0112 119 TYR B C 3361 O O . TYR B 119 ? 0.8650 0.9192 0.3117 -0.0195 -0.1033 -0.0120 119 TYR B O 3362 C CB . TYR B 119 ? 0.8103 0.8572 0.3106 -0.0032 -0.1123 0.0172 119 TYR B CB 3363 C CG . TYR B 119 ? 0.8506 0.8864 0.3124 -0.0108 -0.1093 0.0272 119 TYR B CG 3364 C CD1 . TYR B 119 ? 0.8847 0.9091 0.3144 -0.0023 -0.1227 0.0402 119 TYR B CD1 3365 C CD2 . TYR B 119 ? 0.8638 0.9055 0.3145 -0.0255 -0.0932 0.0224 119 TYR B CD2 3366 C CE1 . TYR B 119 ? 0.9369 0.9348 0.3159 -0.0098 -0.1202 0.0503 119 TYR B CE1 3367 C CE2 . TYR B 119 ? 0.9105 0.9385 0.3166 -0.0412 -0.0890 0.0310 119 TYR B CE2 3368 C CZ . TYR B 119 ? 0.9510 0.9464 0.3170 -0.0343 -0.1026 0.0461 119 TYR B CZ 3369 O OH . TYR B 119 ? 1.0136 0.9793 0.3205 -0.0504 -0.0987 0.0557 119 TYR B OH 3370 N N . GLU B 120 ? 0.8335 0.8778 0.3157 -0.0011 -0.0920 -0.0224 120 GLU B N 3371 C CA . GLU B 120 ? 0.8634 0.9124 0.3221 0.0084 -0.0797 -0.0376 120 GLU B CA 3372 C C . GLU B 120 ? 0.9092 0.9201 0.3246 0.0082 -0.0823 -0.0522 120 GLU B C 3373 O O . GLU B 120 ? 0.9409 0.9518 0.3249 0.0130 -0.0756 -0.0623 120 GLU B O 3374 C CB . GLU B 120 ? 0.8539 0.9197 0.3278 0.0313 -0.0690 -0.0478 120 GLU B CB 3375 C CG . GLU B 120 ? 0.8212 0.9278 0.3296 0.0232 -0.0636 -0.0371 120 GLU B CG 3376 C CD . GLU B 120 ? 0.8354 0.9758 0.3319 0.0001 -0.0556 -0.0307 120 GLU B CD 3377 O OE1 . GLU B 120 ? 0.8602 1.0287 0.3363 0.0032 -0.0470 -0.0426 120 GLU B OE1 3378 O OE2 . GLU B 120 ? 0.8353 0.9664 0.3325 -0.0218 -0.0575 -0.0139 120 GLU B OE2 3379 N N . ARG B 121 ? 0.9195 0.8958 0.3253 -0.0017 -0.0911 -0.0545 121 ARG B N 3380 C CA . ARG B 121 ? 0.9808 0.9083 0.3289 -0.0162 -0.0933 -0.0684 121 ARG B CA 3381 C C . ARG B 121 ? 0.9942 0.9468 0.3280 -0.0371 -0.0978 -0.0654 121 ARG B C 3382 O O . ARG B 121 ? 1.0472 0.9726 0.3329 -0.0384 -0.0926 -0.0777 121 ARG B O 3383 C CB . ARG B 121 ? 0.9891 0.8911 0.3291 -0.0401 -0.1021 -0.0695 121 ARG B CB 3384 C CG . ARG B 121 ? 1.0706 0.9116 0.3337 -0.0705 -0.1031 -0.0851 121 ARG B CG 3385 C CD . ARG B 121 ? 1.0650 0.9389 0.3330 -0.1159 -0.1144 -0.0830 121 ARG B CD 3386 N NE . ARG B 121 ? 1.0398 0.9136 0.3337 -0.1185 -0.1172 -0.0794 121 ARG B NE 3387 C CZ . ARG B 121 ? 1.0287 0.9468 0.3339 -0.1546 -0.1260 -0.0791 121 ARG B CZ 3388 N NH1 . ARG B 121 ? 1.0395 1.0157 0.3336 -0.1908 -0.1338 -0.0829 121 ARG B NH1 3389 N NH2 . ARG B 121 ? 1.0050 0.9213 0.3330 -0.1544 -0.1272 -0.0763 121 ARG B NH2 3390 N N . VAL B 122 ? 0.9550 0.9568 0.3243 -0.0482 -0.1082 -0.0495 122 VAL B N 3391 C CA . VAL B 122 ? 0.9683 1.0007 0.3235 -0.0632 -0.1157 -0.0449 122 VAL B CA 3392 C C . VAL B 122 ? 0.9816 1.0179 0.3252 -0.0527 -0.1064 -0.0430 122 VAL B C 3393 O O . VAL B 122 ? 1.0167 1.0489 0.3247 -0.0635 -0.1055 -0.0505 122 VAL B O 3394 C CB . VAL B 122 ? 0.9347 1.0174 0.3215 -0.0614 -0.1304 -0.0281 122 VAL B CB 3395 C CG1 . VAL B 122 ? 0.9553 1.0723 0.3216 -0.0660 -0.1395 -0.0223 122 VAL B CG1 3396 C CG2 . VAL B 122 ? 0.9243 1.0257 0.3223 -0.0767 -0.1394 -0.0333 122 VAL B CG2 3397 N N . LYS B 123 ? 0.9582 1.0054 0.3271 -0.0376 -0.0987 -0.0342 123 LYS B N 3398 C CA . LYS B 123 ? 0.9758 1.0370 0.3307 -0.0358 -0.0870 -0.0348 123 LYS B CA 3399 C C . LYS B 123 ? 1.0148 1.0615 0.3355 -0.0283 -0.0772 -0.0561 123 LYS B C 3400 O O . LYS B 123 ? 1.0407 1.0964 0.3340 -0.0348 -0.0734 -0.0598 123 LYS B O 3401 C CB . LYS B 123 ? 0.9529 1.0335 0.3333 -0.0294 -0.0763 -0.0297 123 LYS B CB 3402 C CG . LYS B 123 ? 0.9739 1.0818 0.3358 -0.0422 -0.0646 -0.0273 123 LYS B CG 3403 C CD . LYS B 123 ? 0.9718 1.1237 0.3427 -0.0316 -0.0473 -0.0444 123 LYS B CD 3404 C CE . LYS B 123 ? 0.9416 1.1142 0.3464 -0.0290 -0.0428 -0.0415 123 LYS B CE 3405 N NZ . LYS B 123 ? 0.9484 1.1220 0.3461 -0.0615 -0.0403 -0.0233 123 LYS B NZ 3406 N N . ARG B 124 ? 1.0280 1.0437 0.3405 -0.0110 -0.0735 -0.0704 124 ARG B N 3407 C CA . ARG B 124 ? 1.0885 1.0689 0.3485 0.0076 -0.0651 -0.0921 124 ARG B CA 3408 C C . ARG B 124 ? 1.1422 1.0766 0.3474 -0.0156 -0.0713 -0.0995 124 ARG B C 3409 O O . ARG B 124 ? 1.1949 1.1105 0.3525 -0.0070 -0.0643 -0.1133 124 ARG B O 3410 C CB . ARG B 124 ? 1.1094 1.0496 0.3553 0.0386 -0.0613 -0.1045 124 ARG B CB 3411 C CG . ARG B 124 ? 1.0699 1.0714 0.3595 0.0665 -0.0520 -0.1043 124 ARG B CG 3412 C CD . ARG B 124 ? 1.1007 1.0661 0.3680 0.1078 -0.0493 -0.1182 124 ARG B CD 3413 N NE . ARG B 124 ? 1.0609 1.1085 0.3725 0.1334 -0.0405 -0.1205 124 ARG B NE 3414 C CZ . ARG B 124 ? 1.0086 1.0839 0.3701 0.1291 -0.0424 -0.1101 124 ARG B CZ 3415 N NH1 . ARG B 124 ? 0.9877 1.0148 0.3647 0.1058 -0.0531 -0.0964 124 ARG B NH1 3416 N NH2 . ARG B 124 ? 0.9803 1.1417 0.3747 0.1466 -0.0330 -0.1154 124 ARG B NH2 3417 N N . GLN B 125 ? 1.1334 1.0583 0.3426 -0.0461 -0.0839 -0.0923 125 GLN B N 3418 C CA . GLN B 125 ? 1.1840 1.0843 0.3423 -0.0799 -0.0903 -0.0999 125 GLN B CA 3419 C C . GLN B 125 ? 1.1789 1.1247 0.3387 -0.0888 -0.0919 -0.0939 125 GLN B C 3420 O O . GLN B 125 ? 1.2365 1.1546 0.3416 -0.1009 -0.0890 -0.1065 125 GLN B O 3421 C CB . GLN B 125 ? 1.1669 1.0866 0.3407 -0.1137 -0.1039 -0.0937 125 GLN B CB 3422 C CG . GLN B 125 ? 1.1852 1.0525 0.3436 -0.1179 -0.1030 -0.1006 125 GLN B CG 3423 C CD . GLN B 125 ? 1.1547 1.0703 0.3417 -0.1511 -0.1157 -0.0941 125 GLN B CD 3424 O OE1 . GLN B 125 ? 1.1069 1.0399 0.3394 -0.1391 -0.1184 -0.0856 125 GLN B OE1 3425 N NE2 . GLN B 125 ? 1.1827 1.1311 0.3425 -0.1932 -0.1236 -0.0997 125 GLN B NE2 3426 N N . LEU B 126 ? 1.1217 1.1257 0.3330 -0.0829 -0.0963 -0.0746 126 LEU B N 3427 C CA . LEU B 126 ? 1.1246 1.1641 0.3301 -0.0910 -0.0999 -0.0653 126 LEU B CA 3428 C C . LEU B 126 ? 1.1486 1.1861 0.3323 -0.0799 -0.0850 -0.0729 126 LEU B C 3429 O O . LEU B 126 ? 1.1707 1.2226 0.3308 -0.0913 -0.0862 -0.0710 126 LEU B O 3430 C CB . LEU B 126 ? 1.0832 1.1601 0.3261 -0.0846 -0.1095 -0.0419 126 LEU B CB 3431 C CG . LEU B 126 ? 1.0611 1.1625 0.3254 -0.0886 -0.1263 -0.0347 126 LEU B CG 3432 C CD1 . LEU B 126 ? 1.0420 1.1636 0.3241 -0.0695 -0.1358 -0.0122 126 LEU B CD1 3433 C CD2 . LEU B 126 ? 1.0904 1.2188 0.3270 -0.1134 -0.1372 -0.0439 126 LEU B CD2 3434 N N . ARG B 127 ? 1.1456 1.1761 0.3363 -0.0561 -0.0714 -0.0825 127 ARG B N 3435 C CA . ARG B 127 ? 1.1726 1.2203 0.3413 -0.0414 -0.0562 -0.0951 127 ARG B CA 3436 C C . ARG B 127 ? 1.1599 1.2554 0.3387 -0.0588 -0.0535 -0.0803 127 ARG B C 3437 O O . ARG B 127 ? 1.1274 1.2425 0.3359 -0.0664 -0.0550 -0.0633 127 ARG B O 3438 C CB . ARG B 127 ? 1.2417 1.2413 0.3462 -0.0390 -0.0540 -0.1155 127 ARG B CB 3439 C CG . ARG B 127 ? 1.2897 1.2292 0.3541 -0.0072 -0.0478 -0.1362 127 ARG B CG 3440 C CD . ARG B 127 ? 1.3213 1.2844 0.3625 0.0344 -0.0322 -0.1546 127 ARG B CD 3441 N NE . ARG B 127 ? 1.4108 1.2876 0.3725 0.0704 -0.0284 -0.1779 127 ARG B NE 3442 C CZ . ARG B 127 ? 1.4758 1.3463 0.3829 0.1129 -0.0174 -0.1996 127 ARG B CZ 3443 N NH1 . ARG B 127 ? 1.4503 1.4134 0.3836 0.1186 -0.0077 -0.2023 127 ARG B NH1 3444 N NH2 . ARG B 127 ? 1.5789 1.3441 0.3933 0.1506 -0.0158 -0.2197 127 ARG B NH2 3445 N N . GLU B 128 ? 1.1986 1.3013 0.3415 -0.0676 -0.0495 -0.0865 128 GLU B N 3446 C CA . GLU B 128 ? 1.2034 1.3389 0.3397 -0.0881 -0.0462 -0.0730 128 GLU B CA 3447 C C . GLU B 128 ? 1.2168 1.3340 0.3354 -0.1066 -0.0634 -0.0556 128 GLU B C 3448 O O . GLU B 128 ? 1.2433 1.3688 0.3362 -0.1220 -0.0632 -0.0444 128 GLU B O 3449 C CB . GLU B 128 ? 1.2398 1.4055 0.3458 -0.0850 -0.0305 -0.0908 128 GLU B CB 3450 C CG . GLU B 128 ? 1.2361 1.4427 0.3538 -0.0559 -0.0138 -0.1118 128 GLU B CG 3451 C CD . GLU B 128 ? 1.2024 1.4668 0.3547 -0.0686 -0.0045 -0.1030 128 GLU B CD 3452 O OE1 . GLU B 128 ? 1.2124 1.4958 0.3533 -0.1049 -0.0011 -0.0885 128 GLU B OE1 3453 O OE2 . GLU B 128 ? 1.1771 1.4625 0.3585 -0.0452 -0.0004 -0.1111 128 GLU B OE2 3454 N N . ASN B 129 ? 1.2069 1.3049 0.3335 -0.1052 -0.0786 -0.0544 129 ASN B N 3455 C CA . ASN B 129 ? 1.2188 1.3235 0.3315 -0.1160 -0.0970 -0.0414 129 ASN B CA 3456 C C . ASN B 129 ? 1.1997 1.3077 0.3289 -0.1067 -0.1092 -0.0174 129 ASN B C 3457 O O . ASN B 129 ? 1.2154 1.3369 0.3296 -0.1029 -0.1265 -0.0058 129 ASN B O 3458 C CB . ASN B 129 ? 1.2268 1.3281 0.3330 -0.1262 -0.1070 -0.0547 129 ASN B CB 3459 C CG . ASN B 129 ? 1.2739 1.3465 0.3370 -0.1364 -0.0965 -0.0783 129 ASN B CG 3460 O OD1 . ASN B 129 ? 1.2913 1.3529 0.3403 -0.1244 -0.0809 -0.0876 129 ASN B OD1 3461 N ND2 . ASN B 129 ? 1.3047 1.3672 0.3388 -0.1599 -0.1047 -0.0896 129 ASN B ND2 3462 N N . ALA B 130 ? 1.1767 1.2732 0.3291 -0.0996 -0.1008 -0.0111 130 ALA B N 3463 C CA . ALA B 130 ? 1.1725 1.2531 0.3276 -0.0890 -0.1108 0.0105 130 ALA B CA 3464 C C . ALA B 130 ? 1.1745 1.2364 0.3272 -0.0979 -0.0951 0.0169 130 ALA B C 3465 O O . ALA B 130 ? 1.1645 1.2478 0.3280 -0.1086 -0.0771 0.0024 130 ALA B O 3466 C CB . ALA B 130 ? 1.1333 1.2253 0.3278 -0.0747 -0.1228 0.0091 130 ALA B CB 3467 N N . GLU B 131 ? 1.1974 1.2220 0.3275 -0.0930 -0.1021 0.0373 131 GLU B N 3468 C CA . GLU B 131 ? 1.2137 1.2136 0.3297 -0.1118 -0.0877 0.0440 131 GLU B CA 3469 C C . GLU B 131 ? 1.2094 1.1728 0.3313 -0.0945 -0.0976 0.0578 131 GLU B C 3470 O O . GLU B 131 ? 1.2181 1.1660 0.3313 -0.0652 -0.1173 0.0679 131 GLU B O 3471 C CB . GLU B 131 ? 1.2926 1.2532 0.3306 -0.1394 -0.0808 0.0562 131 GLU B CB 3472 C CG . GLU B 131 ? 1.2945 1.3025 0.3304 -0.1611 -0.0662 0.0399 131 GLU B CG 3473 C CD . GLU B 131 ? 1.3772 1.3487 0.3310 -0.1949 -0.0586 0.0511 131 GLU B CD 3474 O OE1 . GLU B 131 ? 1.4473 1.3404 0.3319 -0.2050 -0.0632 0.0723 131 GLU B OE1 3475 O OE2 . GLU B 131 ? 1.3817 1.3951 0.3302 -0.2114 -0.0478 0.0382 131 GLU B OE2 3476 N N . GLU B 132 ? 1.1983 1.1587 0.3347 -0.1112 -0.0838 0.0562 132 GLU B N 3477 C CA . GLU B 132 ? 1.1941 1.1183 0.3363 -0.0975 -0.0907 0.0672 132 GLU B CA 3478 C C . GLU B 132 ? 1.2898 1.1221 0.3404 -0.0969 -0.0986 0.0907 132 GLU B C 3479 O O . GLU B 132 ? 1.3647 1.1532 0.3439 -0.1315 -0.0875 0.0977 132 GLU B O 3480 C CB . GLU B 132 ? 1.1598 1.1111 0.3377 -0.1197 -0.0728 0.0576 132 GLU B CB 3481 C CG . GLU B 132 ? 1.0802 1.1005 0.3372 -0.1037 -0.0687 0.0362 132 GLU B CG 3482 C CD . GLU B 132 ? 1.0502 1.1009 0.3401 -0.1150 -0.0549 0.0282 132 GLU B CD 3483 O OE1 . GLU B 132 ? 1.0627 1.1580 0.3447 -0.1422 -0.0370 0.0183 132 GLU B OE1 3484 O OE2 . GLU B 132 ? 1.0143 1.0546 0.3377 -0.0974 -0.0618 0.0307 132 GLU B OE2 3485 N N . ASP B 133 ? 1.3000 1.0999 0.3426 -0.0565 -0.1175 0.1020 133 ASP B N 3486 C CA . ASP B 133 ? 1.4079 1.1031 0.3485 -0.0398 -0.1277 0.1240 133 ASP B CA 3487 C C . ASP B 133 ? 1.4448 1.0743 0.3494 -0.0693 -0.1142 0.1303 133 ASP B C 3488 O O . ASP B 133 ? 1.5559 1.0887 0.3540 -0.0991 -0.1066 0.1431 133 ASP B O 3489 C CB . ASP B 133 ? 1.4053 1.1090 0.3528 0.0235 -0.1534 0.1300 133 ASP B CB 3490 C CG . ASP B 133 ? 1.5366 1.1281 0.3615 0.0602 -0.1680 0.1519 133 ASP B CG 3491 O OD1 . ASP B 133 ? 1.5894 1.1014 0.3673 0.0683 -0.1674 0.1616 133 ASP B OD1 3492 O OD2 . ASP B 133 ? 1.5951 1.1725 0.3627 0.0848 -0.1808 0.1589 133 ASP B OD2 3493 N N . GLY B 134 ? 1.3599 1.0375 0.3448 -0.0656 -0.1108 0.1207 134 GLY B N 3494 C CA . GLY B 134 ? 1.3844 1.0140 0.3456 -0.0941 -0.0985 0.1243 134 GLY B CA 3495 C C . GLY B 134 ? 1.3828 0.9738 0.3459 -0.0502 -0.1132 0.1324 134 GLY B C 3496 O O . GLY B 134 ? 1.3828 0.9494 0.3469 -0.0692 -0.1043 0.1324 134 GLY B O 3497 N N . THR B 135 ? 1.3825 0.9784 0.3451 0.0083 -0.1357 0.1376 135 THR B N 3498 C CA . THR B 135 ? 1.3854 0.9610 0.3476 0.0597 -0.1519 0.1435 135 THR B CA 3499 C C . THR B 135 ? 1.2578 0.9562 0.3422 0.0817 -0.1598 0.1276 135 THR B C 3500 O O . THR B 135 ? 1.2450 0.9588 0.3454 0.1248 -0.1740 0.1287 135 THR B O 3501 C CB . THR B 135 ? 1.4948 0.9990 0.3553 0.1185 -0.1737 0.1592 135 THR B CB 3502 O OG1 . THR B 135 ? 1.4549 1.0447 0.3520 0.1400 -0.1857 0.1529 135 THR B OG1 3503 C CG2 . THR B 135 ? 1.6503 1.0024 0.3609 0.0954 -0.1666 0.1766 135 THR B CG2 3504 N N . GLY B 136 ? 1.1759 0.9557 0.3348 0.0512 -0.1499 0.1119 136 GLY B N 3505 C CA . GLY B 136 ? 1.0799 0.9570 0.3302 0.0619 -0.1561 0.0961 136 GLY B CA 3506 C C . GLY B 136 ? 1.0772 1.0089 0.3294 0.0762 -0.1689 0.0912 136 GLY B C 3507 O O . GLY B 136 ? 1.0321 1.0350 0.3292 0.0923 -0.1806 0.0818 136 GLY B O 3508 N N . CYS B 137 ? 1.2699 1.1907 0.7066 -0.0420 -0.1494 0.0384 137 CYS B N 3509 C CA . CYS B 137 ? 1.2363 1.2143 0.7005 -0.0074 -0.1544 0.0455 137 CYS B CA 3510 C C . CYS B 137 ? 1.2027 1.2219 0.6894 -0.0052 -0.1726 0.0446 137 CYS B C 3511 O O . CYS B 137 ? 1.2115 1.2138 0.6965 -0.0180 -0.1701 0.0474 137 CYS B O 3512 C CB . CYS B 137 ? 1.2714 1.2363 0.7229 0.0248 -0.1232 0.0650 137 CYS B CB 3513 S SG . CYS B 137 ? 1.3184 1.2334 0.7473 0.0334 -0.0895 0.0724 137 CYS B SG 3514 N N . PHE B 138 ? 1.1708 1.2409 0.6764 0.0092 -0.1884 0.0417 138 PHE B N 3515 C CA . PHE B 138 ? 1.1535 1.2532 0.6691 0.0134 -0.1992 0.0397 138 PHE B CA 3516 C C . PHE B 138 ? 1.1642 1.2945 0.6711 0.0410 -0.1961 0.0511 138 PHE B C 3517 O O . PHE B 138 ? 1.1547 1.3209 0.6671 0.0481 -0.2081 0.0509 138 PHE B O 3518 C CB . PHE B 138 ? 1.1221 1.2468 0.6563 -0.0016 -0.2204 0.0238 138 PHE B CB 3519 C CG . PHE B 138 ? 1.1116 1.2165 0.6591 -0.0279 -0.2265 0.0187 138 PHE B CG 3520 C CD1 . PHE B 138 ? 1.1085 1.2095 0.6709 -0.0380 -0.2257 0.0246 138 PHE B CD1 3521 C CD2 . PHE B 138 ? 1.1083 1.2008 0.6547 -0.0427 -0.2324 0.0122 138 PHE B CD2 3522 C CE1 . PHE B 138 ? 1.1005 1.1945 0.6812 -0.0638 -0.2349 0.0273 138 PHE B CE1 3523 C CE2 . PHE B 138 ? 1.1045 1.1827 0.6592 -0.0695 -0.2416 0.0110 138 PHE B CE2 3524 C CZ . PHE B 138 ? 1.0996 1.1828 0.6737 -0.0808 -0.2450 0.0202 138 PHE B CZ 3525 N N . GLU B 139 ? 1.1864 1.3047 0.6802 0.0547 -0.1808 0.0637 139 GLU B N 3526 C CA . GLU B 139 ? 1.2033 1.3519 0.6839 0.0794 -0.1797 0.0777 139 GLU B CA 3527 C C . GLU B 139 ? 1.1969 1.3718 0.6701 0.0722 -0.1979 0.0645 139 GLU B C 3528 O O . GLU B 139 ? 1.1951 1.3506 0.6694 0.0615 -0.1942 0.0554 139 GLU B O 3529 C CB . GLU B 139 ? 1.2340 1.3549 0.6995 0.0968 -0.1538 0.0960 139 GLU B CB 3530 C CG . GLU B 139 ? 1.2577 1.3481 0.7200 0.1084 -0.1286 0.1117 139 GLU B CG 3531 C CD . GLU B 139 ? 1.2939 1.3455 0.7398 0.1216 -0.0982 0.1277 139 GLU B CD 3532 O OE1 . GLU B 139 ? 1.2965 1.3472 0.7375 0.1216 -0.0978 0.1273 139 GLU B OE1 3533 O OE2 . GLU B 139 ? 1.3249 1.3413 0.7616 0.1325 -0.0699 0.1414 139 GLU B OE2 3534 N N . ILE B 140 ? 1.2017 1.4190 0.6672 0.0764 -0.2156 0.0656 140 ILE B N 3535 C CA . ILE B 140 ? 1.2094 1.4440 0.6563 0.0626 -0.2326 0.0489 140 ILE B CA 3536 C C . ILE B 140 ? 1.2519 1.5015 0.6608 0.0755 -0.2329 0.0615 140 ILE B C 3537 O O . ILE B 140 ? 1.2659 1.5504 0.6719 0.0911 -0.2388 0.0839 140 ILE B O 3538 C CB . ILE B 140 ? 1.1928 1.4638 0.6521 0.0480 -0.2562 0.0387 140 ILE B CB 3539 C CG1 . ILE B 140 ? 1.1576 1.4129 0.6513 0.0397 -0.2533 0.0316 140 ILE B CG1 3540 C CG2 . ILE B 140 ? 1.2078 1.4801 0.6420 0.0266 -0.2687 0.0158 140 ILE B CG2 3541 C CD1 . ILE B 140 ? 1.1407 1.4282 0.6519 0.0275 -0.2720 0.0235 140 ILE B CD1 3542 N N . PHE B 141 ? 1.2784 1.5010 0.6582 0.0699 -0.2243 0.0503 141 PHE B N 3543 C CA . PHE B 141 ? 1.3303 1.5549 0.6622 0.0800 -0.2212 0.0603 141 PHE B CA 3544 C C . PHE B 141 ? 1.3603 1.6268 0.6571 0.0660 -0.2500 0.0576 141 PHE B C 3545 O O . PHE B 141 ? 1.3870 1.6910 0.6677 0.0781 -0.2610 0.0814 141 PHE B O 3546 C CB . PHE B 141 ? 1.3582 1.5340 0.6651 0.0765 -0.1987 0.0482 141 PHE B CB 3547 C CG . PHE B 141 ? 1.3446 1.4878 0.6818 0.0903 -0.1716 0.0598 141 PHE B CG 3548 C CD1 . PHE B 141 ? 1.3643 1.5031 0.6941 0.1130 -0.1567 0.0827 141 PHE B CD1 3549 C CD2 . PHE B 141 ? 1.3161 1.4359 0.6912 0.0789 -0.1614 0.0507 141 PHE B CD2 3550 C CE1 . PHE B 141 ? 1.3554 1.4627 0.7119 0.1205 -0.1319 0.0927 141 PHE B CE1 3551 C CE2 . PHE B 141 ? 1.3053 1.4019 0.7105 0.0852 -0.1409 0.0643 141 PHE B CE2 3552 C CZ . PHE B 141 ? 1.3258 1.4141 0.7204 0.1043 -0.1261 0.0835 141 PHE B CZ 3553 N N . HIS B 142 ? 1.3618 1.6228 0.6469 0.0387 -0.2619 0.0309 142 HIS B N 3554 C CA . HIS B 142 ? 1.3976 1.6945 0.6451 0.0152 -0.2914 0.0244 142 HIS B CA 3555 C C . HIS B 142 ? 1.3630 1.7249 0.6559 0.0150 -0.3175 0.0406 142 HIS B C 3556 O O . HIS B 142 ? 1.3133 1.6798 0.6605 0.0326 -0.3081 0.0518 142 HIS B O 3557 C CB . HIS B 142 ? 1.4206 1.6797 0.6373 -0.0156 -0.2889 -0.0107 142 HIS B CB 3558 C CG . HIS B 142 ? 1.3663 1.6246 0.6358 -0.0249 -0.2899 -0.0256 142 HIS B CG 3559 N ND1 . HIS B 142 ? 1.3503 1.6516 0.6389 -0.0436 -0.3167 -0.0304 142 HIS B ND1 3560 C CD2 . HIS B 142 ? 1.3272 1.5493 0.6347 -0.0192 -0.2679 -0.0340 142 HIS B CD2 3561 C CE1 . HIS B 142 ? 1.3050 1.5910 0.6368 -0.0471 -0.3090 -0.0433 142 HIS B CE1 3562 N NE2 . HIS B 142 ? 1.2912 1.5312 0.6343 -0.0333 -0.2812 -0.0449 142 HIS B NE2 3563 N N . LYS B 143 ? 1.3965 1.8059 0.6644 -0.0073 -0.3490 0.0431 143 LYS B N 3564 C CA . LYS B 143 ? 1.3729 1.8566 0.6875 -0.0056 -0.3744 0.0684 143 LYS B CA 3565 C C . LYS B 143 ? 1.3382 1.8283 0.6881 -0.0280 -0.3843 0.0467 143 LYS B C 3566 O O . LYS B 143 ? 1.3680 1.8548 0.6843 -0.0637 -0.4008 0.0215 143 LYS B O 3567 C CB . LYS B 143 ? 1.4291 1.9750 0.7057 -0.0218 -0.4087 0.0898 143 LYS B CB 3568 C CG . LYS B 143 ? 1.4775 2.0179 0.7065 -0.0035 -0.4019 0.1115 143 LYS B CG 3569 C CD . LYS B 143 ? 1.4562 2.0453 0.7345 0.0382 -0.3955 0.1618 143 LYS B CD 3570 C CE . LYS B 143 ? 1.4003 1.9437 0.7304 0.0718 -0.3560 0.1620 143 LYS B CE 3571 N NZ . LYS B 143 ? 1.4022 1.9635 0.7566 0.1137 -0.3362 0.2065 143 LYS B NZ 3572 N N . CYS B 144 ? 1.2842 1.7768 0.6958 -0.0083 -0.3714 0.0560 144 CYS B N 3573 C CA . CYS B 144 ? 1.2509 1.7522 0.7004 -0.0252 -0.3788 0.0405 144 CYS B CA 3574 C C . CYS B 144 ? 1.2418 1.8211 0.7365 -0.0221 -0.3999 0.0722 144 CYS B C 3575 O O . CYS B 144 ? 1.2191 1.8152 0.7566 0.0092 -0.3851 0.1032 144 CYS B O 3576 C CB . CYS B 144 ? 1.2050 1.6567 0.6891 -0.0097 -0.3511 0.0310 144 CYS B CB 3577 S SG . CYS B 144 ? 1.1951 1.5788 0.6641 -0.0301 -0.3369 -0.0102 144 CYS B SG 3578 N N . ASP B 145 ? 1.2658 1.8901 0.7512 -0.0558 -0.4313 0.0664 145 ASP B N 3579 C CA . ASP B 145 ? 1.2530 1.9576 0.7943 -0.0578 -0.4525 0.0972 145 ASP B CA 3580 C C . ASP B 145 ? 1.2045 1.8889 0.7965 -0.0545 -0.4365 0.0846 145 ASP B C 3581 O O . ASP B 145 ? 1.1869 1.8016 0.7648 -0.0563 -0.4159 0.0514 145 ASP B O 3582 C CB . ASP B 145 ? 1.2998 2.0609 0.8129 -0.1028 -0.4948 0.0950 145 ASP B CB 3583 C CG . ASP B 145 ? 1.3198 2.0287 0.7885 -0.1455 -0.4982 0.0431 145 ASP B CG 3584 O OD1 . ASP B 145 ? 1.2989 1.9310 0.7575 -0.1373 -0.4684 0.0118 145 ASP B OD1 3585 O OD2 . ASP B 145 ? 1.3634 2.1083 0.8066 -0.1891 -0.5301 0.0359 145 ASP B OD2 3586 N N . ASP B 146 ? 1.1871 1.9342 0.8396 -0.0491 -0.4450 0.1145 146 ASP B N 3587 C CA . ASP B 146 ? 1.1481 1.8748 0.8463 -0.0444 -0.4273 0.1056 146 ASP B CA 3588 C C . ASP B 146 ? 1.1463 1.8319 0.8194 -0.0811 -0.4338 0.0574 146 ASP B C 3589 O O . ASP B 146 ? 1.1172 1.7533 0.8041 -0.0759 -0.4124 0.0384 146 ASP B O 3590 C CB . ASP B 146 ? 1.1382 1.9456 0.9068 -0.0360 -0.4357 0.1484 146 ASP B CB 3591 C CG . ASP B 146 ? 1.1389 1.9734 0.9433 0.0100 -0.4140 0.2007 146 ASP B CG 3592 O OD1 . ASP B 146 ? 1.1394 1.9127 0.9178 0.0368 -0.3844 0.1975 146 ASP B OD1 3593 O OD2 . ASP B 146 ? 1.1413 2.0592 1.0031 0.0191 -0.4243 0.2478 146 ASP B OD2 3594 N N . ASP B 147 ? 1.1854 1.8876 0.8168 -0.1190 -0.4613 0.0391 147 ASP B N 3595 C CA . ASP B 147 ? 1.1993 1.8490 0.7937 -0.1530 -0.4603 -0.0074 147 ASP B CA 3596 C C . ASP B 147 ? 1.1873 1.7515 0.7492 -0.1372 -0.4296 -0.0326 147 ASP B C 3597 O O . ASP B 147 ? 1.1639 1.6821 0.7362 -0.1391 -0.4120 -0.0549 147 ASP B O 3598 C CB . ASP B 147 ? 1.2653 1.9335 0.8018 -0.1978 -0.4895 -0.0222 147 ASP B CB 3599 C CG . ASP B 147 ? 1.2885 1.9143 0.7979 -0.2380 -0.4878 -0.0644 147 ASP B CG 3600 O OD1 . ASP B 147 ? 1.2688 1.8238 0.7727 -0.2284 -0.4578 -0.0906 147 ASP B OD1 3601 O OD2 . ASP B 147 ? 1.3308 1.9947 0.8243 -0.2809 -0.5160 -0.0693 147 ASP B OD2 3602 N N . CYS B 148 ? 1.2056 1.7536 0.7314 -0.1220 -0.4239 -0.0251 148 CYS B N 3603 C CA . CYS B 148 ? 1.1977 1.6741 0.6988 -0.1064 -0.3957 -0.0415 148 CYS B CA 3604 C C . CYS B 148 ? 1.1437 1.5931 0.6896 -0.0824 -0.3737 -0.0370 148 CYS B C 3605 O O . CYS B 148 ? 1.1298 1.5290 0.6734 -0.0859 -0.3573 -0.0576 148 CYS B O 3606 C CB . CYS B 148 ? 1.2237 1.6992 0.6930 -0.0874 -0.3922 -0.0237 148 CYS B CB 3607 S SG . CYS B 148 ? 1.2339 1.6284 0.6661 -0.0761 -0.3605 -0.0422 148 CYS B SG 3608 N N . MET B 149 ? 1.1200 1.6018 0.7043 -0.0591 -0.3718 -0.0073 149 MET B N 3609 C CA . MET B 149 ? 1.0853 1.5339 0.6989 -0.0395 -0.3489 -0.0021 149 MET B CA 3610 C C . MET B 149 ? 1.0613 1.4946 0.6958 -0.0560 -0.3479 -0.0219 149 MET B C 3611 O O . MET B 149 ? 1.0445 1.4296 0.6795 -0.0539 -0.3319 -0.0331 149 MET B O 3612 C CB . MET B 149 ? 1.0826 1.5632 0.7280 -0.0118 -0.3406 0.0351 149 MET B CB 3613 C CG . MET B 149 ? 1.1046 1.5948 0.7329 0.0105 -0.3351 0.0596 149 MET B CG 3614 S SD . MET B 149 ? 1.1074 1.5209 0.7039 0.0233 -0.3078 0.0490 149 MET B SD 3615 C CE . MET B 149 ? 1.1365 1.5749 0.7224 0.0525 -0.3004 0.0853 149 MET B CE 3616 N N . ALA B 150 ? 1.0625 1.5388 0.7136 -0.0748 -0.3661 -0.0242 150 ALA B N 3617 C CA . ALA B 150 ? 1.0443 1.5086 0.7154 -0.0914 -0.3644 -0.0425 150 ALA B CA 3618 C C . ALA B 150 ? 1.0500 1.4647 0.6912 -0.1106 -0.3586 -0.0752 150 ALA B C 3619 O O . ALA B 150 ? 1.0323 1.4169 0.6872 -0.1145 -0.3476 -0.0875 150 ALA B O 3620 C CB . ALA B 150 ? 1.0521 1.5784 0.7497 -0.1100 -0.3857 -0.0351 150 ALA B CB 3621 N N . SER B 151 ? 1.0795 1.4834 0.6793 -0.1209 -0.3626 -0.0864 151 SER B N 3622 C CA . SER B 151 ? 1.0935 1.4444 0.6653 -0.1336 -0.3481 -0.1119 151 SER B CA 3623 C C . SER B 151 ? 1.0658 1.3753 0.6487 -0.1134 -0.3277 -0.1069 151 SER B C 3624 O O . SER B 151 ? 1.0595 1.3351 0.6481 -0.1189 -0.3142 -0.1184 151 SER B O 3625 C CB . SER B 151 ? 1.1446 1.4844 0.6624 -0.1467 -0.3503 -0.1223 151 SER B CB 3626 O OG . SER B 151 ? 1.1453 1.4732 0.6492 -0.1240 -0.3419 -0.1080 151 SER B OG 3627 N N . ILE B 152 ? 1.0539 1.3679 0.6402 -0.0920 -0.3255 -0.0871 152 ILE B N 3628 C CA . ILE B 152 ? 1.0345 1.3135 0.6295 -0.0790 -0.3103 -0.0799 152 ILE B CA 3629 C C . ILE B 152 ? 1.0077 1.2777 0.6302 -0.0808 -0.3078 -0.0788 152 ILE B C 3630 O O . ILE B 152 ? 0.9958 1.2380 0.6253 -0.0861 -0.3003 -0.0828 152 ILE B O 3631 C CB . ILE B 152 ? 1.0385 1.3192 0.6257 -0.0589 -0.3061 -0.0598 152 ILE B CB 3632 C CG1 . ILE B 152 ? 1.0676 1.3484 0.6227 -0.0565 -0.3053 -0.0604 152 ILE B CG1 3633 C CG2 . ILE B 152 ? 1.0248 1.2698 0.6202 -0.0534 -0.2933 -0.0523 152 ILE B CG2 3634 C CD1 . ILE B 152 ? 1.0776 1.3698 0.6236 -0.0361 -0.3028 -0.0391 152 ILE B CD1 3635 N N . ARG B 153 ? 1.0016 1.2965 0.6397 -0.0760 -0.3130 -0.0700 153 ARG B N 3636 C CA . ARG B 153 ? 0.9869 1.2686 0.6442 -0.0770 -0.3071 -0.0686 153 ARG B CA 3637 C C . ARG B 153 ? 0.9790 1.2513 0.6461 -0.0945 -0.3084 -0.0864 153 ARG B C 3638 O O . ARG B 153 ? 0.9706 1.2152 0.6428 -0.0975 -0.3016 -0.0870 153 ARG B O 3639 C CB . ARG B 153 ? 0.9874 1.3019 0.6649 -0.0669 -0.3078 -0.0533 153 ARG B CB 3640 C CG . ARG B 153 ? 0.9990 1.3111 0.6713 -0.0443 -0.2962 -0.0298 153 ARG B CG 3641 C CD . ARG B 153 ? 1.0028 1.3351 0.7022 -0.0302 -0.2858 -0.0092 153 ARG B CD 3642 N NE . ARG B 153 ? 1.0019 1.4033 0.7292 -0.0303 -0.3030 0.0035 153 ARG B NE 3643 C CZ . ARG B 153 ? 1.0136 1.4565 0.7529 -0.0122 -0.3040 0.0319 153 ARG B CZ 3644 N NH1 . ARG B 153 ? 1.0284 1.4445 0.7536 0.0113 -0.2833 0.0496 153 ARG B NH1 3645 N NH2 . ARG B 153 ? 1.0152 1.5289 0.7809 -0.0195 -0.3261 0.0453 153 ARG B NH2 3646 N N . ASN B 154 ? 0.9906 1.2829 0.6553 -0.1080 -0.3162 -0.1001 154 ASN B N 3647 C CA . ASN B 154 ? 0.9917 1.2733 0.6648 -0.1250 -0.3130 -0.1173 154 ASN B CA 3648 C C . ASN B 154 ? 1.0015 1.2492 0.6597 -0.1309 -0.3008 -0.1282 154 ASN B C 3649 O O . ASN B 154 ? 1.0105 1.2437 0.6714 -0.1439 -0.2925 -0.1421 154 ASN B O 3650 C CB . ASN B 154 ? 1.0093 1.3273 0.6868 -0.1419 -0.3255 -0.1261 154 ASN B CB 3651 C CG . ASN B 154 ? 0.9968 1.3532 0.7056 -0.1344 -0.3327 -0.1090 154 ASN B CG 3652 O OD1 . ASN B 154 ? 1.0087 1.4125 0.7249 -0.1382 -0.3478 -0.0991 154 ASN B OD1 3653 N ND2 . ASN B 154 ? 0.9788 1.3147 0.7057 -0.1238 -0.3206 -0.1021 154 ASN B ND2 3654 N N . ASN B 155 ? 1.0025 1.2361 0.6481 -0.1200 -0.2957 -0.1192 155 ASN B N 3655 C CA . ASN B 155 ? 1.0107 1.2137 0.6533 -0.1197 -0.2790 -0.1198 155 ASN B CA 3656 C C . ASN B 155 ? 1.0503 1.2371 0.6645 -0.1304 -0.2670 -0.1371 155 ASN B C 3657 O O . ASN B 155 ? 1.0656 1.2211 0.6802 -0.1301 -0.2447 -0.1381 155 ASN B O 3658 C CB . ASN B 155 ? 0.9932 1.1814 0.6627 -0.1223 -0.2714 -0.1152 155 ASN B CB 3659 C CG . ASN B 155 ? 0.9856 1.1597 0.6697 -0.1146 -0.2627 -0.0954 155 ASN B CG 3660 O OD1 . ASN B 155 ? 1.0015 1.1643 0.6812 -0.1092 -0.2489 -0.0909 155 ASN B OD1 3661 N ND2 . ASN B 155 ? 0.9666 1.1414 0.6672 -0.1161 -0.2706 -0.0811 155 ASN B ND2 3662 N N . THR B 156 ? 1.0742 1.2801 0.6610 -0.1409 -0.2799 -0.1479 156 THR B N 3663 C CA . THR B 156 ? 1.1293 1.3126 0.6724 -0.1595 -0.2704 -0.1681 156 THR B CA 3664 C C . THR B 156 ? 1.1614 1.3358 0.6641 -0.1538 -0.2676 -0.1650 156 THR B C 3665 O O . THR B 156 ? 1.2194 1.3602 0.6740 -0.1686 -0.2533 -0.1812 156 THR B O 3666 C CB . THR B 156 ? 1.1498 1.3608 0.6810 -0.1859 -0.2900 -0.1834 156 THR B CB 3667 O OG1 . THR B 156 ? 1.1476 1.4074 0.6736 -0.1842 -0.3168 -0.1714 156 THR B OG1 3668 C CG2 . THR B 156 ? 1.1139 1.3390 0.6891 -0.1886 -0.2934 -0.1833 156 THR B CG2 3669 N N . TYR B 157 ? 1.1317 1.3291 0.6484 -0.1333 -0.2777 -0.1447 157 TYR B N 3670 C CA . TYR B 157 ? 1.1584 1.3525 0.6403 -0.1247 -0.2764 -0.1380 157 TYR B CA 3671 C C . TYR B 157 ? 1.1972 1.3382 0.6525 -0.1218 -0.2445 -0.1430 157 TYR B C 3672 O O . TYR B 157 ? 1.1741 1.2956 0.6626 -0.1082 -0.2251 -0.1314 157 TYR B O 3673 C CB . TYR B 157 ? 1.1176 1.3339 0.6273 -0.1008 -0.2837 -0.1137 157 TYR B CB 3674 C CG . TYR B 157 ? 1.1402 1.3499 0.6216 -0.0873 -0.2778 -0.1029 157 TYR B CG 3675 C CD1 . TYR B 157 ? 1.1435 1.3189 0.6274 -0.0751 -0.2543 -0.0953 157 TYR B CD1 3676 C CD2 . TYR B 157 ? 1.1592 1.4011 0.6162 -0.0855 -0.2953 -0.0957 157 TYR B CD2 3677 C CE1 . TYR B 157 ? 1.1664 1.3333 0.6255 -0.0618 -0.2461 -0.0847 157 TYR B CE1 3678 C CE2 . TYR B 157 ? 1.1829 1.4171 0.6121 -0.0716 -0.2884 -0.0843 157 TYR B CE2 3679 C CZ . TYR B 157 ? 1.1869 1.3804 0.6154 -0.0598 -0.2627 -0.0807 157 TYR B CZ 3680 O OH . TYR B 157 ? 1.2119 1.3952 0.6139 -0.0453 -0.2530 -0.0689 157 TYR B OH 3681 N N . ASP B 158 ? 1.2620 1.3803 0.6564 -0.1356 -0.2384 -0.1572 158 ASP B N 3682 C CA . ASP B 158 ? 1.3149 1.3732 0.6735 -0.1317 -0.2009 -0.1616 158 ASP B CA 3683 C C . ASP B 158 ? 1.3265 1.3853 0.6653 -0.1133 -0.1983 -0.1458 158 ASP B C 3684 O O . ASP B 158 ? 1.3599 1.4342 0.6520 -0.1221 -0.2167 -0.1494 158 ASP B O 3685 C CB . ASP B 158 ? 1.3985 1.4132 0.6863 -0.1630 -0.1886 -0.1908 158 ASP B CB 3686 C CG . ASP B 158 ? 1.4682 1.4058 0.7111 -0.1583 -0.1395 -0.1960 158 ASP B CG 3687 O OD1 . ASP B 158 ? 1.4437 1.3695 0.7230 -0.1290 -0.1152 -0.1735 158 ASP B OD1 3688 O OD2 . ASP B 158 ? 1.5549 1.4406 0.7239 -0.1861 -0.1229 -0.2217 158 ASP B OD2 3689 N N . HIS B 159 ? 1.3012 1.3459 0.6776 -0.0892 -0.1760 -0.1256 159 HIS B N 3690 C CA . HIS B 159 ? 1.3060 1.3507 0.6747 -0.0696 -0.1702 -0.1075 159 HIS B CA 3691 C C . HIS B 159 ? 1.3895 1.3844 0.6847 -0.0729 -0.1445 -0.1173 159 HIS B C 3692 O O . HIS B 159 ? 1.4089 1.4104 0.6736 -0.0645 -0.1503 -0.1093 159 HIS B O 3693 C CB . HIS B 159 ? 1.2623 1.3059 0.6941 -0.0487 -0.1526 -0.0817 159 HIS B CB 3694 C CG . HIS B 159 ? 1.2969 1.2925 0.7338 -0.0419 -0.1089 -0.0759 159 HIS B CG 3695 N ND1 . HIS B 159 ? 1.3005 1.2773 0.7569 -0.0490 -0.0920 -0.0814 159 HIS B ND1 3696 C CD2 . HIS B 159 ? 1.3332 1.2942 0.7613 -0.0259 -0.0738 -0.0613 159 HIS B CD2 3697 C CE1 . HIS B 159 ? 1.3383 1.2715 0.7997 -0.0361 -0.0465 -0.0684 159 HIS B CE1 3698 N NE2 . HIS B 159 ? 1.3583 1.2813 0.8036 -0.0221 -0.0346 -0.0560 159 HIS B NE2 3699 N N . SER B 160 ? 1.4464 1.3853 0.7088 -0.0849 -0.1121 -0.1338 160 SER B N 3700 C CA . SER B 160 ? 1.5414 1.4141 0.7249 -0.0889 -0.0771 -0.1442 160 SER B CA 3701 C C . SER B 160 ? 1.6057 1.4808 0.7014 -0.1164 -0.1040 -0.1650 160 SER B C 3702 O O . SER B 160 ? 1.6797 1.5132 0.7044 -0.1176 -0.0862 -0.1681 160 SER B O 3703 C CB . SER B 160 ? 1.5960 1.3982 0.7635 -0.0952 -0.0283 -0.1561 160 SER B CB 3704 O OG . SER B 160 ? 1.6001 1.4059 0.7588 -0.1229 -0.0437 -0.1798 160 SER B OG 3705 N N . LYS B 161 ? 1.5811 1.5072 0.6827 -0.1391 -0.1470 -0.1759 161 LYS B N 3706 C CA . LYS B 161 ? 1.6400 1.5844 0.6682 -0.1704 -0.1800 -0.1897 161 LYS B CA 3707 C C . LYS B 161 ? 1.6163 1.6183 0.6478 -0.1544 -0.2111 -0.1657 161 LYS B C 3708 O O . LYS B 161 ? 1.6751 1.6926 0.6412 -0.1768 -0.2360 -0.1693 161 LYS B O 3709 C CB . LYS B 161 ? 1.6241 1.6081 0.6671 -0.2014 -0.2131 -0.2049 161 LYS B CB 3710 C CG . LYS B 161 ? 1.6878 1.6032 0.6905 -0.2300 -0.1830 -0.2353 161 LYS B CG 3711 C CD . LYS B 161 ? 1.6526 1.6102 0.6932 -0.2538 -0.2113 -0.2460 161 LYS B CD 3712 C CE . LYS B 161 ? 1.7247 1.6077 0.7201 -0.2841 -0.1778 -0.2771 161 LYS B CE 3713 N NZ . LYS B 161 ? 1.6652 1.5819 0.7268 -0.2906 -0.1905 -0.2807 161 LYS B NZ 3714 N N . TYR B 162 ? 1.5370 1.5696 0.6416 -0.1181 -0.2095 -0.1397 162 TYR B N 3715 C CA . TYR B 162 ? 1.5184 1.5940 0.6285 -0.0974 -0.2281 -0.1144 162 TYR B CA 3716 C C . TYR B 162 ? 1.5132 1.5536 0.6351 -0.0655 -0.1934 -0.0975 162 TYR B C 3717 O O . TYR B 162 ? 1.4897 1.5592 0.6273 -0.0437 -0.2016 -0.0746 162 TYR B O 3718 C CB . TYR B 162 ? 1.4346 1.5818 0.6203 -0.0851 -0.2591 -0.0959 162 TYR B CB 3719 C CG . TYR B 162 ? 1.4237 1.6126 0.6210 -0.1117 -0.2902 -0.1069 162 TYR B CG 3720 C CD1 . TYR B 162 ? 1.4538 1.6950 0.6226 -0.1296 -0.3258 -0.0999 162 TYR B CD1 3721 C CD2 . TYR B 162 ? 1.3841 1.5652 0.6258 -0.1189 -0.2848 -0.1200 162 TYR B CD2 3722 C CE1 . TYR B 162 ? 1.4437 1.7293 0.6312 -0.1553 -0.3546 -0.1060 162 TYR B CE1 3723 C CE2 . TYR B 162 ? 1.3748 1.5931 0.6301 -0.1428 -0.3109 -0.1291 162 TYR B CE2 3724 C CZ . TYR B 162 ? 1.4040 1.6750 0.6342 -0.1615 -0.3454 -0.1221 162 TYR B CZ 3725 O OH . TYR B 162 ? 1.3954 1.7090 0.6463 -0.1867 -0.3715 -0.1275 162 TYR B OH 3726 N N . ARG B 163 ? 1.5371 1.5149 0.6541 -0.0621 -0.1519 -0.1056 163 ARG B N 3727 C CA . ARG B 163 ? 1.5179 1.4716 0.6713 -0.0320 -0.1183 -0.0844 163 ARG B CA 3728 C C . ARG B 163 ? 1.5688 1.5039 0.6694 -0.0183 -0.1065 -0.0730 163 ARG B C 3729 O O . ARG B 163 ? 1.5278 1.4912 0.6659 0.0044 -0.1112 -0.0497 163 ARG B O 3730 C CB . ARG B 163 ? 1.5405 1.4355 0.7056 -0.0298 -0.0726 -0.0890 163 ARG B CB 3731 C CG . ARG B 163 ? 1.5107 1.3959 0.7349 -0.0004 -0.0411 -0.0599 163 ARG B CG 3732 C CD . ARG B 163 ? 1.5261 1.3664 0.7797 0.0051 0.0041 -0.0548 163 ARG B CD 3733 N NE . ARG B 163 ? 1.4774 1.3339 0.8130 0.0293 0.0222 -0.0195 163 ARG B NE 3734 C CZ . ARG B 163 ? 1.4778 1.3131 0.8645 0.0408 0.0610 0.0004 163 ARG B CZ 3735 N NH1 . ARG B 163 ? 1.5273 1.3145 0.8888 0.0342 0.0926 -0.0130 163 ARG B NH1 3736 N NH2 . ARG B 163 ? 1.4331 1.2961 0.8982 0.0581 0.0696 0.0368 163 ARG B NH2 3737 N N . GLU B 164 ? 1.6655 1.5475 0.6734 -0.0341 -0.0892 -0.0900 164 GLU B N 3738 C CA . GLU B 164 ? 1.7295 1.5816 0.6750 -0.0220 -0.0720 -0.0801 164 GLU B CA 3739 C C . GLU B 164 ? 1.6993 1.6171 0.6508 -0.0119 -0.1111 -0.0603 164 GLU B C 3740 O O . GLU B 164 ? 1.6851 1.6045 0.6557 0.0159 -0.0971 -0.0373 164 GLU B O 3741 C CB . GLU B 164 ? 1.8540 1.6375 0.6795 -0.0503 -0.0548 -0.1057 164 GLU B CB 3742 C CG . GLU B 164 ? 1.9127 1.6052 0.7155 -0.0500 0.0056 -0.1185 164 GLU B CG 3743 C CD . GLU B 164 ? 1.9070 1.5877 0.7232 -0.0745 0.0057 -0.1416 164 GLU B CD 3744 O OE1 . GLU B 164 ? 1.8071 1.5480 0.7170 -0.0678 -0.0187 -0.1334 164 GLU B OE1 3745 O OE2 . GLU B 164 ? 2.0097 1.6150 0.7368 -0.1017 0.0327 -0.1685 164 GLU B OE2 3746 N N . GLU B 165 ? 1.6907 1.6634 0.6310 -0.0334 -0.1569 -0.0659 165 GLU B N 3747 C CA . GLU B 165 ? 1.6661 1.7067 0.6187 -0.0214 -0.1916 -0.0409 165 GLU B CA 3748 C C . GLU B 165 ? 1.5736 1.6490 0.6204 0.0114 -0.1892 -0.0163 165 GLU B C 3749 O O . GLU B 165 ? 1.5681 1.6663 0.6205 0.0343 -0.1911 0.0090 165 GLU B O 3750 C CB . GLU B 165 ? 1.6714 1.7729 0.6100 -0.0508 -0.2402 -0.0455 165 GLU B CB 3751 C CG . GLU B 165 ? 1.6081 1.7355 0.6096 -0.0644 -0.2548 -0.0590 165 GLU B CG 3752 C CD . GLU B 165 ? 1.6107 1.8071 0.6088 -0.0908 -0.3024 -0.0565 165 GLU B CD 3753 O OE1 . GLU B 165 ? 1.5954 1.8557 0.6116 -0.0772 -0.3278 -0.0263 165 GLU B OE1 3754 O OE2 . GLU B 165 ? 1.6297 1.8179 0.6112 -0.1246 -0.3123 -0.0818 165 GLU B OE2 3755 N N . ALA B 166 ? 1.5095 1.5846 0.6240 0.0115 -0.1834 -0.0233 166 ALA B N 3756 C CA . ALA B 166 ? 1.4348 1.5295 0.6278 0.0343 -0.1786 -0.0040 166 ALA B CA 3757 C C . ALA B 166 ? 1.4420 1.4935 0.6460 0.0547 -0.1405 0.0085 166 ALA B C 3758 O O . ALA B 166 ? 1.4200 1.4817 0.6505 0.0749 -0.1349 0.0300 166 ALA B O 3759 C CB . ALA B 166 ? 1.3758 1.4822 0.6276 0.0228 -0.1869 -0.0149 166 ALA B CB 3760 N N . MET B 167 ? 1.4771 1.4783 0.6623 0.0491 -0.1110 -0.0031 167 MET B N 3761 C CA . MET B 167 ? 1.4954 1.4547 0.6906 0.0681 -0.0702 0.0118 167 MET B CA 3762 C C . MET B 167 ? 1.5475 1.4937 0.6892 0.0845 -0.0599 0.0251 167 MET B C 3763 O O . MET B 167 ? 1.5326 1.4737 0.7064 0.1052 -0.0408 0.0467 167 MET B O 3764 C CB . MET B 167 ? 1.5433 1.4458 0.7156 0.0607 -0.0345 -0.0012 167 MET B CB 3765 C CG . MET B 167 ? 1.4907 1.3992 0.7355 0.0552 -0.0287 -0.0010 167 MET B CG 3766 S SD . MET B 167 ? 1.4393 1.3558 0.7778 0.0759 -0.0045 0.0344 167 MET B SD 3767 C CE . MET B 167 ? 1.4298 1.3289 0.8194 0.0704 0.0211 0.0373 167 MET B CE 3768 N N . GLN B 168 ? 1.6133 1.5544 0.6719 0.0725 -0.0733 0.0132 168 GLN B N 3769 C CA . GLN B 168 ? 1.6728 1.6044 0.6699 0.0859 -0.0676 0.0272 168 GLN B CA 3770 C C . GLN B 168 ? 1.6249 1.6077 0.6646 0.1077 -0.0851 0.0541 168 GLN B C 3771 O O . GLN B 168 ? 1.6548 1.6246 0.6739 0.1290 -0.0673 0.0736 168 GLN B O 3772 C CB . GLN B 168 ? 1.7537 1.6825 0.6525 0.0604 -0.0901 0.0110 168 GLN B CB 3773 C CG . GLN B 168 ? 1.8397 1.6917 0.6631 0.0396 -0.0596 -0.0154 168 GLN B CG 3774 C CD . GLN B 168 ? 1.9264 1.7116 0.6795 0.0539 -0.0175 -0.0084 168 GLN B CD 3775 O OE1 . GLN B 168 ? 1.9570 1.6750 0.7079 0.0621 0.0322 -0.0129 168 GLN B OE1 3776 N NE2 . GLN B 168 ? 1.9706 1.7741 0.6670 0.0587 -0.0346 0.0062 168 GLN B NE2 3777 N N . ASN B 169 ? 1.5583 1.5931 0.6540 0.1031 -0.1151 0.0559 169 ASN B N 3778 C CA . ASN B 169 ? 1.5169 1.5899 0.6560 0.1239 -0.1235 0.0812 169 ASN B CA 3779 C C . ASN B 169 ? 1.4684 1.5219 0.6740 0.1369 -0.0985 0.0914 169 ASN B C 3780 O O . ASN B 169 ? 1.4430 1.5131 0.6793 0.1517 -0.0981 0.1100 169 ASN B O 3781 C CB . ASN B 169 ? 1.4777 1.6084 0.6443 0.1140 -0.1607 0.0811 169 ASN B CB 3782 C CG . ASN B 169 ? 1.5266 1.6924 0.6351 0.0989 -0.1916 0.0798 169 ASN B CG 3783 O OD1 . ASN B 169 ? 1.5864 1.7509 0.6375 0.1058 -0.1907 0.0930 169 ASN B OD1 3784 N ND2 . ASN B 169 ? 1.5061 1.7053 0.6282 0.0758 -0.2204 0.0657 169 ASN B ND2 3785 N N . ARG B 170 ? 1.4622 1.4799 0.6888 0.1298 -0.0763 0.0818 170 ARG B N 3786 C CA . ARG B 170 ? 1.4232 1.4273 0.7141 0.1350 -0.0557 0.0945 170 ARG B CA 3787 C C . ARG B 170 ? 1.4099 1.4237 0.7206 0.1505 -0.0524 0.1155 170 ARG B C 3788 O O . ARG B 170 ? 1.3949 1.3925 0.7465 0.1525 -0.0334 0.1282 170 ARG B O 3789 C CB . ARG B 170 ? 1.4566 1.4166 0.7453 0.1419 -0.0172 0.1004 170 ARG B CB 3790 C CG . ARG B 170 ? 1.5116 1.4442 0.7574 0.1642 0.0095 0.1165 170 ARG B CG 3791 C CD . ARG B 170 ? 1.5793 1.5018 0.7342 0.1653 0.0031 0.1061 170 ARG B CD 3792 N NE . ARG B 170 ? 1.5993 1.5411 0.7239 0.1824 -0.0056 0.1235 170 ARG B NE 3793 C CZ . ARG B 170 ? 1.6340 1.5513 0.7426 0.2050 0.0229 0.1439 170 ARG B CZ 3794 N NH1 . ARG B 170 ? 1.6527 1.5254 0.7744 0.2128 0.0625 0.1498 170 ARG B NH1 3795 N NH2 . ARG B 170 ? 1.6521 1.5915 0.7354 0.2218 0.0141 0.1623 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 1 403 403 NAG NAG A . D 3 NAG 1 404 404 NAG NAG A . E 3 NAG 1 405 405 NAG NAG A . F 3 NAG 1 1123 1123 NAG NAG A . G 4 SO4 1 1317 1317 SO4 SO4 A . H 4 SO4 1 1318 1318 SO4 SO4 A . I 4 SO4 1 1319 1319 SO4 SO4 A . J 4 SO4 1 1320 1320 SO4 SO4 A . K 4 SO4 1 1321 1321 SO4 SO4 A . L 4 SO4 1 1322 1322 SO4 SO4 A . M 4 SO4 1 1323 1323 SO4 SO4 A . N 4 SO4 1 1324 1324 SO4 SO4 A . O 4 SO4 1 1325 1325 SO4 SO4 A . P 4 SO4 1 1326 1326 SO4 SO4 A . Q 3 NAG 1 201 201 NAG NAG B . R 3 NAG 2 202 202 NAG NAG B . S 4 SO4 1 1171 1171 SO4 SO4 B . T 4 SO4 1 1172 1172 SO4 SO4 B . U 4 SO4 1 1173 1173 SO4 SO4 B . V 4 SO4 1 1174 1174 SO4 SO4 B . W 5 HOH 1 2001 2001 HOH HOH A . W 5 HOH 2 2002 2002 HOH HOH A . W 5 HOH 3 2003 2003 HOH HOH A . W 5 HOH 4 2004 2004 HOH HOH A . W 5 HOH 5 2005 2005 HOH HOH A . W 5 HOH 6 2006 2006 HOH HOH A . W 5 HOH 7 2007 2007 HOH HOH A . W 5 HOH 8 2008 2008 HOH HOH A . W 5 HOH 9 2009 2009 HOH HOH A . W 5 HOH 10 2010 2010 HOH HOH A . W 5 HOH 11 2011 2011 HOH HOH A . W 5 HOH 12 2012 2012 HOH HOH A . W 5 HOH 13 2013 2013 HOH HOH A . W 5 HOH 14 2014 2014 HOH HOH A . W 5 HOH 15 2015 2015 HOH HOH A . W 5 HOH 16 2016 2016 HOH HOH A . W 5 HOH 17 2017 2017 HOH HOH A . W 5 HOH 18 2018 2018 HOH HOH A . W 5 HOH 19 2019 2019 HOH HOH A . W 5 HOH 20 2020 2020 HOH HOH A . W 5 HOH 21 2021 2021 HOH HOH A . W 5 HOH 22 2022 2022 HOH HOH A . W 5 HOH 23 2023 2023 HOH HOH A . W 5 HOH 24 2024 2024 HOH HOH A . W 5 HOH 25 2025 2025 HOH HOH A . W 5 HOH 26 2026 2026 HOH HOH A . W 5 HOH 27 2027 2027 HOH HOH A . W 5 HOH 28 2028 2028 HOH HOH A . W 5 HOH 29 2029 2029 HOH HOH A . W 5 HOH 30 2030 2030 HOH HOH A . W 5 HOH 31 2031 2031 HOH HOH A . W 5 HOH 32 2032 2032 HOH HOH A . W 5 HOH 33 2033 2033 HOH HOH A . W 5 HOH 34 2034 2034 HOH HOH A . W 5 HOH 35 2035 2035 HOH HOH A . W 5 HOH 36 2036 2036 HOH HOH A . W 5 HOH 37 2037 2037 HOH HOH A . W 5 HOH 38 2038 2038 HOH HOH A . W 5 HOH 39 2039 2039 HOH HOH A . W 5 HOH 40 2040 2040 HOH HOH A . W 5 HOH 41 2041 2041 HOH HOH A . W 5 HOH 42 2042 2042 HOH HOH A . W 5 HOH 43 2043 2043 HOH HOH A . W 5 HOH 44 2044 2044 HOH HOH A . W 5 HOH 45 2045 2045 HOH HOH A . W 5 HOH 46 2046 2046 HOH HOH A . W 5 HOH 47 2047 2047 HOH HOH A . W 5 HOH 48 2048 2048 HOH HOH A . W 5 HOH 49 2049 2049 HOH HOH A . W 5 HOH 50 2050 2050 HOH HOH A . W 5 HOH 51 2051 2051 HOH HOH A . W 5 HOH 52 2052 2052 HOH HOH A . W 5 HOH 53 2053 2053 HOH HOH A . W 5 HOH 54 2054 2054 HOH HOH A . W 5 HOH 55 2055 2055 HOH HOH A . W 5 HOH 56 2056 2056 HOH HOH A . W 5 HOH 57 2057 2057 HOH HOH A . W 5 HOH 58 2058 2058 HOH HOH A . W 5 HOH 59 2059 2059 HOH HOH A . W 5 HOH 60 2060 2060 HOH HOH A . W 5 HOH 61 2061 2061 HOH HOH A . W 5 HOH 62 2062 2062 HOH HOH A . W 5 HOH 63 2063 2063 HOH HOH A . W 5 HOH 64 2064 2064 HOH HOH A . W 5 HOH 65 2065 2065 HOH HOH A . W 5 HOH 66 2066 2066 HOH HOH A . W 5 HOH 67 2067 2067 HOH HOH A . W 5 HOH 68 2068 2068 HOH HOH A . W 5 HOH 69 2069 2069 HOH HOH A . W 5 HOH 70 2070 2070 HOH HOH A . W 5 HOH 71 2071 2071 HOH HOH A . W 5 HOH 72 2072 2072 HOH HOH A . W 5 HOH 73 2073 2073 HOH HOH A . W 5 HOH 74 2074 2074 HOH HOH A . W 5 HOH 75 2075 2075 HOH HOH A . W 5 HOH 76 2076 2076 HOH HOH A . W 5 HOH 77 2077 2077 HOH HOH A . W 5 HOH 78 2078 2078 HOH HOH A . W 5 HOH 79 2079 2079 HOH HOH A . W 5 HOH 80 2080 2080 HOH HOH A . W 5 HOH 81 2081 2081 HOH HOH A . W 5 HOH 82 2082 2082 HOH HOH A . W 5 HOH 83 2083 2083 HOH HOH A . W 5 HOH 84 2084 2084 HOH HOH A . W 5 HOH 85 2085 2085 HOH HOH A . W 5 HOH 86 2086 2086 HOH HOH A . W 5 HOH 87 2087 2087 HOH HOH A . W 5 HOH 88 2088 2088 HOH HOH A . W 5 HOH 89 2089 2089 HOH HOH A . W 5 HOH 90 2090 2090 HOH HOH A . W 5 HOH 91 2091 2091 HOH HOH A . W 5 HOH 92 2092 2092 HOH HOH A . W 5 HOH 93 2093 2093 HOH HOH A . W 5 HOH 94 2094 2094 HOH HOH A . W 5 HOH 95 2095 2095 HOH HOH A . W 5 HOH 96 2096 2096 HOH HOH A . W 5 HOH 97 2097 2097 HOH HOH A . W 5 HOH 98 2098 2098 HOH HOH A . W 5 HOH 99 2099 2099 HOH HOH A . W 5 HOH 100 2100 2100 HOH HOH A . W 5 HOH 101 2101 2101 HOH HOH A . W 5 HOH 102 2102 2102 HOH HOH A . W 5 HOH 103 2103 2103 HOH HOH A . W 5 HOH 104 2104 2104 HOH HOH A . W 5 HOH 105 2105 2105 HOH HOH A . W 5 HOH 106 2106 2106 HOH HOH A . W 5 HOH 107 2107 2107 HOH HOH A . W 5 HOH 108 2108 2108 HOH HOH A . W 5 HOH 109 2109 2109 HOH HOH A . W 5 HOH 110 2110 2110 HOH HOH A . W 5 HOH 111 2111 2111 HOH HOH A . W 5 HOH 112 2112 2112 HOH HOH A . W 5 HOH 113 2113 2113 HOH HOH A . W 5 HOH 114 2114 2114 HOH HOH A . W 5 HOH 115 2115 2115 HOH HOH A . W 5 HOH 116 2116 2116 HOH HOH A . W 5 HOH 117 2117 2117 HOH HOH A . W 5 HOH 118 2118 2118 HOH HOH A . W 5 HOH 119 2119 2119 HOH HOH A . W 5 HOH 120 2120 2120 HOH HOH A . W 5 HOH 121 2121 2121 HOH HOH A . W 5 HOH 122 2122 2122 HOH HOH A . W 5 HOH 123 2123 2123 HOH HOH A . W 5 HOH 124 2124 2124 HOH HOH A . W 5 HOH 125 2125 2125 HOH HOH A . W 5 HOH 126 2126 2126 HOH HOH A . W 5 HOH 127 2127 2127 HOH HOH A . W 5 HOH 128 2128 2128 HOH HOH A . W 5 HOH 129 2129 2129 HOH HOH A . W 5 HOH 130 2130 2130 HOH HOH A . W 5 HOH 131 2131 2131 HOH HOH A . W 5 HOH 132 2132 2132 HOH HOH A . W 5 HOH 133 2133 2133 HOH HOH A . W 5 HOH 134 2134 2134 HOH HOH A . W 5 HOH 135 2135 2135 HOH HOH A . W 5 HOH 136 2136 2136 HOH HOH A . W 5 HOH 137 2137 2137 HOH HOH A . W 5 HOH 138 2138 2138 HOH HOH A . W 5 HOH 139 2139 2139 HOH HOH A . W 5 HOH 140 2140 2140 HOH HOH A . W 5 HOH 141 2141 2141 HOH HOH A . W 5 HOH 142 2142 2142 HOH HOH A . W 5 HOH 143 2143 2143 HOH HOH A . W 5 HOH 144 2144 2144 HOH HOH A . W 5 HOH 145 2145 2145 HOH HOH A . W 5 HOH 146 2146 2146 HOH HOH A . W 5 HOH 147 2147 2147 HOH HOH A . W 5 HOH 148 2148 2148 HOH HOH A . W 5 HOH 149 2149 2149 HOH HOH A . W 5 HOH 150 2150 2150 HOH HOH A . W 5 HOH 151 2151 2151 HOH HOH A . W 5 HOH 152 2152 2152 HOH HOH A . W 5 HOH 153 2153 2153 HOH HOH A . W 5 HOH 154 2154 2154 HOH HOH A . W 5 HOH 155 2155 2155 HOH HOH A . W 5 HOH 156 2156 2156 HOH HOH A . W 5 HOH 157 2157 2157 HOH HOH A . W 5 HOH 158 2158 2158 HOH HOH A . W 5 HOH 159 2159 2159 HOH HOH A . W 5 HOH 160 2160 2160 HOH HOH A . W 5 HOH 161 2161 2161 HOH HOH A . W 5 HOH 162 2162 2162 HOH HOH A . W 5 HOH 163 2163 2163 HOH HOH A . W 5 HOH 164 2164 2164 HOH HOH A . W 5 HOH 165 2165 2165 HOH HOH A . W 5 HOH 166 2166 2166 HOH HOH A . W 5 HOH 167 2167 2167 HOH HOH A . W 5 HOH 168 2168 2168 HOH HOH A . W 5 HOH 169 2169 2169 HOH HOH A . W 5 HOH 170 2170 2170 HOH HOH A . W 5 HOH 171 2171 2171 HOH HOH A . W 5 HOH 172 2172 2172 HOH HOH A . W 5 HOH 173 2173 2173 HOH HOH A . W 5 HOH 174 2174 2174 HOH HOH A . W 5 HOH 175 2175 2175 HOH HOH A . W 5 HOH 176 2176 2176 HOH HOH A . W 5 HOH 177 2177 2177 HOH HOH A . W 5 HOH 178 2178 2178 HOH HOH A . W 5 HOH 179 2179 2179 HOH HOH A . W 5 HOH 180 2180 2180 HOH HOH A . W 5 HOH 181 2181 2181 HOH HOH A . W 5 HOH 182 2182 2182 HOH HOH A . W 5 HOH 183 2183 2183 HOH HOH A . W 5 HOH 184 2184 2184 HOH HOH A . W 5 HOH 185 2185 2185 HOH HOH A . W 5 HOH 186 2186 2186 HOH HOH A . W 5 HOH 187 2187 2187 HOH HOH A . W 5 HOH 188 2188 2188 HOH HOH A . W 5 HOH 189 2189 2189 HOH HOH A . W 5 HOH 190 2190 2190 HOH HOH A . W 5 HOH 191 2191 2191 HOH HOH A . W 5 HOH 192 2192 2192 HOH HOH A . W 5 HOH 193 2193 2193 HOH HOH A . W 5 HOH 194 2194 2194 HOH HOH A . W 5 HOH 195 2195 2195 HOH HOH A . W 5 HOH 196 2196 2196 HOH HOH A . W 5 HOH 197 2197 2197 HOH HOH A . W 5 HOH 198 2198 2198 HOH HOH A . W 5 HOH 199 2199 2199 HOH HOH A . W 5 HOH 200 2200 2200 HOH HOH A . X 5 HOH 1 2001 2001 HOH HOH B . X 5 HOH 2 2002 2002 HOH HOH B . X 5 HOH 3 2003 2003 HOH HOH B . X 5 HOH 4 2004 2004 HOH HOH B . X 5 HOH 5 2005 2005 HOH HOH B . X 5 HOH 6 2006 2006 HOH HOH B . X 5 HOH 7 2007 2007 HOH HOH B . X 5 HOH 8 2008 2008 HOH HOH B . X 5 HOH 9 2009 2009 HOH HOH B . X 5 HOH 10 2010 2010 HOH HOH B . X 5 HOH 11 2011 2011 HOH HOH B . X 5 HOH 12 2012 2012 HOH HOH B . X 5 HOH 13 2013 2013 HOH HOH B . X 5 HOH 14 2014 2014 HOH HOH B . X 5 HOH 15 2015 2015 HOH HOH B . X 5 HOH 16 2016 2016 HOH HOH B . X 5 HOH 17 2017 2017 HOH HOH B . X 5 HOH 18 2018 2018 HOH HOH B . X 5 HOH 19 2019 2019 HOH HOH B . X 5 HOH 20 2020 2020 HOH HOH B . X 5 HOH 21 2021 2021 HOH HOH B . X 5 HOH 22 2022 2022 HOH HOH B . X 5 HOH 23 2023 2023 HOH HOH B . X 5 HOH 24 2024 2024 HOH HOH B . X 5 HOH 25 2025 2025 HOH HOH B . X 5 HOH 26 2026 2026 HOH HOH B . X 5 HOH 27 2027 2027 HOH HOH B . X 5 HOH 28 2028 2028 HOH HOH B . X 5 HOH 29 2029 2029 HOH HOH B . X 5 HOH 30 2030 2030 HOH HOH B . X 5 HOH 31 2031 2031 HOH HOH B . X 5 HOH 32 2032 2032 HOH HOH B . X 5 HOH 33 2033 2033 HOH HOH B . X 5 HOH 34 2034 2034 HOH HOH B . X 5 HOH 35 2035 2035 HOH HOH B . X 5 HOH 36 2036 2036 HOH HOH B . X 5 HOH 37 2037 2037 HOH HOH B . X 5 HOH 38 2038 2038 HOH HOH B . X 5 HOH 39 2039 2039 HOH HOH B . X 5 HOH 40 2040 2040 HOH HOH B . X 5 HOH 41 2041 2041 HOH HOH B . X 5 HOH 42 2042 2042 HOH HOH B . X 5 HOH 43 2043 2043 HOH HOH B . X 5 HOH 44 2044 2044 HOH HOH B . X 5 HOH 45 2045 2045 HOH HOH B . X 5 HOH 46 2046 2046 HOH HOH B . X 5 HOH 47 2047 2047 HOH HOH B . X 5 HOH 48 2048 2048 HOH HOH B . X 5 HOH 49 2049 2049 HOH HOH B . X 5 HOH 50 2050 2050 HOH HOH B . X 5 HOH 51 2051 2051 HOH HOH B . X 5 HOH 52 2052 2052 HOH HOH B . X 5 HOH 53 2053 2053 HOH HOH B . X 5 HOH 54 2054 2054 HOH HOH B . X 5 HOH 55 2055 2055 HOH HOH B . X 5 HOH 56 2056 2056 HOH HOH B . X 5 HOH 57 2057 2057 HOH HOH B . X 5 HOH 58 2058 2058 HOH HOH B . X 5 HOH 59 2059 2059 HOH HOH B . X 5 HOH 60 2060 2060 HOH HOH B . X 5 HOH 61 2061 2061 HOH HOH B . X 5 HOH 62 2062 2062 HOH HOH B . X 5 HOH 63 2063 2063 HOH HOH B . X 5 HOH 64 2064 2064 HOH HOH B . X 5 HOH 65 2065 2065 HOH HOH B . X 5 HOH 66 2066 2066 HOH HOH B . X 5 HOH 67 2067 2067 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 # 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)' 43550 ? 1 MORE -603.4 ? 1 'SSA (A^2)' 58680 ? # 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 58.0650000000 0.8660254038 -0.5000000000 0.0000000000 -100.5715301415 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 116.1300000000 -0.8660254038 -0.5000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 2034 ? W HOH . 2 1 A HOH 2149 ? W HOH . 3 1 B HOH 2038 ? X HOH . 4 1 B HOH 2048 ? X HOH . # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2013-07-03 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 ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Database references' 2 2 'Structure model' 'Refinement description' # 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 37.5397 -36.3254 -3.6185 0.0947 0.1217 0.3114 -0.0553 0.0300 -0.0422 0.9976 1.2789 2.7717 0.1510 -0.9053 -0.5036 0.2212 0.0188 0.1453 0.1448 -0.0239 0.3082 -0.2268 0.0435 -0.1973 'X-RAY DIFFRACTION' 2 ? refined 40.4433 -44.9735 32.8493 0.7745 0.5024 0.3761 -0.2362 0.0163 -0.0638 3.4124 0.1932 7.3781 0.7569 0.9598 -0.0415 0.7256 -0.8659 -0.0534 0.2487 -0.1822 0.0419 -0.0567 0.4301 -0.5434 'X-RAY DIFFRACTION' 3 ? refined 47.8146 -36.7527 32.9282 1.3166 2.0041 0.4409 -1.0166 0.4277 -0.3933 4.6797 1.0777 12.9861 -1.9779 -6.6210 2.4198 -0.1409 0.0995 -0.2715 0.4426 0.4302 0.2175 -1.5451 1.7820 -0.2893 'X-RAY DIFFRACTION' 4 ? refined 42.0040 -45.0033 17.8708 0.3640 0.3230 0.3571 -0.1417 -0.0282 -0.0969 1.5337 2.9540 2.8554 1.2028 0.2774 1.1195 0.5099 -0.1894 -0.1832 0.9184 -0.0932 -0.3768 0.2472 0.6536 -0.4167 'X-RAY DIFFRACTION' 5 ? refined 41.0104 -31.0974 -17.2728 0.0790 0.1392 0.3035 -0.0516 -0.0410 0.0477 1.4960 1.4670 5.8737 0.1675 -2.6012 -1.5168 0.0614 0.2820 0.0612 -0.2050 0.0513 0.3276 0.0576 -0.4459 -0.1127 'X-RAY DIFFRACTION' 6 ? refined 40.6514 -28.9207 -51.8217 0.7261 1.0421 0.3119 -0.1506 -0.2310 0.2043 1.3381 3.5636 8.8946 -1.6939 2.4930 -1.3771 0.1210 0.4468 0.0029 -0.6075 -0.3810 0.4238 0.0436 -0.2397 0.2600 'X-RAY DIFFRACTION' 7 ? refined 41.6275 -39.1744 -36.7341 0.2848 0.3963 0.4560 -0.0983 -0.0737 -0.0408 3.1801 2.8733 17.5543 -0.1052 3.7636 -2.5889 0.0322 -0.0030 -0.1387 -0.2028 -0.0184 0.2588 0.4135 -1.0305 -0.0138 'X-RAY DIFFRACTION' 8 ? refined 50.6625 -30.9456 -5.5510 0.0192 0.0587 0.2493 -0.0052 0.0305 -0.0042 1.7248 1.8960 7.6134 0.6465 -0.2582 -0.6553 0.1244 -0.1290 0.1533 0.1635 -0.1013 0.1369 -0.1263 -0.3796 -0.0231 'X-RAY DIFFRACTION' 9 ? refined 49.6442 -34.3746 -53.1384 0.6679 0.7154 0.1885 -0.0002 -0.1014 -0.0033 0.8502 0.8887 14.2825 0.3278 -0.1104 1.6825 -0.1315 0.6898 -0.0235 -0.5962 0.1756 -0.0320 0.1412 0.0929 -0.0441 'X-RAY DIFFRACTION' 10 ? refined 43.5441 -37.9313 -68.7919 1.1173 1.3581 0.5071 -0.0348 -0.2807 -0.0487 2.7130 5.4365 4.6447 1.4348 -3.2831 -3.4927 -0.0231 1.0074 -0.0206 -1.1051 0.0572 -0.0142 0.3608 -0.9737 -0.0341 # 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 4BSA _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 GLOBAL INITIATIVE ON SHARING ALL INFLUENZA DATA (GISAID) GISAID-EPI439507 ; # loop_ _pdbx_validate_symm_contact.id _pdbx_validate_symm_contact.PDB_model_num _pdbx_validate_symm_contact.auth_atom_id_1 _pdbx_validate_symm_contact.auth_asym_id_1 _pdbx_validate_symm_contact.auth_comp_id_1 _pdbx_validate_symm_contact.auth_seq_id_1 _pdbx_validate_symm_contact.PDB_ins_code_1 _pdbx_validate_symm_contact.label_alt_id_1 _pdbx_validate_symm_contact.site_symmetry_1 _pdbx_validate_symm_contact.auth_atom_id_2 _pdbx_validate_symm_contact.auth_asym_id_2 _pdbx_validate_symm_contact.auth_comp_id_2 _pdbx_validate_symm_contact.auth_seq_id_2 _pdbx_validate_symm_contact.PDB_ins_code_2 _pdbx_validate_symm_contact.label_alt_id_2 _pdbx_validate_symm_contact.site_symmetry_2 _pdbx_validate_symm_contact.dist 1 1 O A HOH 2029 ? ? 1_555 O A HOH 2031 ? ? 6_555 1.84 2 1 O B HOH 2044 ? ? 1_555 O B HOH 2046 ? ? 3_655 2.13 # 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 THR A 18 ? ? -125.07 -167.82 2 1 PRO A 39 ? ? -80.40 45.22 3 1 GLU A 71 ? ? -141.43 41.53 4 1 CYS A 87 ? ? -109.86 -61.93 5 1 SER A 132 ? ? 46.14 77.44 6 1 SER A 135 ? ? -161.91 -156.68 7 1 SER A 198 ? ? -37.96 -37.97 8 1 SER A 207 ? ? -150.78 83.37 9 1 ALA A 241 ? ? 55.13 11.21 10 1 SER A 281 ? ? -171.20 148.88 11 1 ASP A 289 ? ? -164.41 119.55 12 1 ALA B 5 ? ? -103.80 -63.29 13 1 ASN B 71 ? ? -154.23 88.36 14 1 ARG B 127 ? ? 57.62 -125.63 # _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 2067 _pdbx_distant_solvent_atoms.PDB_ins_code ? _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 6.28 _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 'SULFATE ION' SO4 5 water HOH #