data_3FGR # _entry.id 3FGR # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 3FGR RCSB RCSB050570 WWPDB D_1000050570 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3FBX 'Crystal structure of the lysosomal 66.3 kDa protein from mouse solved by S-SAD' unspecified PDB 3FGT 'Two chain form of the 66.3 kDa protein from mouse lacking the linker peptide' unspecified PDB 3FGW 'One chain form of the 66.3 kDa protein' unspecified # _pdbx_database_status.entry_id 3FGR _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site PDBJ _pdbx_database_status.recvd_initial_deposition_date 2008-12-08 _pdbx_database_status.status_code REL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Lakomek, K.' 1 'Dickmanns, A.' 2 'Ficner, R.' 3 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography' 'Bmc Struct.Biol.' 9 56 56 2009 ? UK 1472-6807 ? ? 19706171 10.1186/1472-6807-9-56 1 'De novo sulfur SAD phasing of the lysosomal 66.3 kDa protein from mouse' 'Acta Crystallogr.,Sect.D' 65 220 228 2009 ABCRE6 DK 0907-4449 0766 ? 19237744 10.1107/S0907444908041814 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Lakomek, K.' 1 primary 'Dickmanns, A.' 2 primary 'Kettwig, M.' 3 primary 'Urlaub, H.' 4 primary 'Ficner, R.' 5 primary 'Luebke, T.' 6 1 'Lakomek, K.' 7 1 'Dickmanns, A.' 8 1 'Mueller, U.' 9 1 'Kollmann, K.' 10 1 'Deuschl, F.' 11 1 'Berndt, A.' 12 1 'Luebke, T.' 13 1 'Ficner, R.' 14 # _cell.entry_id 3FGR _cell.length_a 148.737 _cell.length_b 89.560 _cell.length_c 64.811 _cell.angle_alpha 90.00 _cell.angle_beta 98.69 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3FGR _symmetry.space_group_name_H-M 'C 1 2 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 5 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Putative phospholipase B-like 2 28 kDa form' 22774.531 1 3.1.1.- ? 'N-terminal domain, residues 47-248' ? 2 polymer man 'Putative phospholipase B-like 2 40 kDa form' 40476.836 1 3.1.1.- ? 'C-terminal domain, residues 249-594' ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 7 ? ? ? ? 4 non-polymer syn GLYCEROL 92.094 11 ? ? ? ? 5 non-polymer syn 'ACETATE ION' 59.044 2 ? ? ? ? 6 non-polymer syn XENON 131.293 1 ? ? ? ? 7 non-polymer syn 'SODIUM ION' 22.990 1 ? ? ? ? 8 water nat water 18.015 576 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'Lamina ancestor homolog 2, LAMA-like protein 2, 76 kDa protein, p76, 66.3 kDa protein' 2 'Lamina ancestor homolog 2, LAMA-like protein 2, 76 kDa protein, p76, 66.3 kDa protein' # 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 ;LPTLGPGWQRQNPDPPVSRTRSLLLDAASGQLRLEDGFHPDAVAWANLTNAIRETGWAYLDLSTNGRYNDSLQAYAAGVV EASVSEELIYMHWMNTVVNYCGPFEYEVGYCEKLKNFLEANLEWMQREMELNPDSPYWHQVRLTLLQLKGLEDSYEGRLT FPTGRFTIKPLGFLLLQISGDLEDLEPALNKTNTKPSLGSGS ; ;LPTLGPGWQRQNPDPPVSRTRSLLLDAASGQLRLEDGFHPDAVAWANLTNAIRETGWAYLDLSTNGRYNDSLQAYAAGVV EASVSEELIYMHWMNTVVNYCGPFEYEVGYCEKLKNFLEANLEWMQREMELNPDSPYWHQVRLTLLQLKGLEDSYEGRLT FPTGRFTIKPLGFLLLQISGDLEDLEPALNKTNTKPSLGSGS ; A ? 2 'polypeptide(L)' no yes ;(OCS)SALIKLLPGGHDLLVAHNTWNSYQNMLRIIKKYRLQFREGPQEEYPLVAGNNLVFSSYPGTIFSGDDFYILGSGL VTLETTIGNKNPALWKYVQPQGCVLEWIRNVVANRLALDGATWADVFKRFNSGTYNNQWMIVDYKAFLPNGPSPGSRVLT ILEQIPGMVVVADKTAELYKTTYWASYNIPYFETVFNASGLQALVAQYGDWFSYTKNPRAKIFQRDQSLVEDMDAMVRLM RYNDFLHDPLSLCEACNPKPNAENAISARSDLNPANGSYPFQALHQRAHGGIDVKVTSFTLAKYMSMLAASGPTWDQCPP FQWSKSPFHSMLHMGQPDLWMFSPIRVPWDGRGSHHHHHHG ; ;CSALIKLLPGGHDLLVAHNTWNSYQNMLRIIKKYRLQFREGPQEEYPLVAGNNLVFSSYPGTIFSGDDFYILGSGLVTLE TTIGNKNPALWKYVQPQGCVLEWIRNVVANRLALDGATWADVFKRFNSGTYNNQWMIVDYKAFLPNGPSPGSRVLTILEQ IPGMVVVADKTAELYKTTYWASYNIPYFETVFNASGLQALVAQYGDWFSYTKNPRAKIFQRDQSLVEDMDAMVRLMRYND FLHDPLSLCEACNPKPNAENAISARSDLNPANGSYPFQALHQRAHGGIDVKVTSFTLAKYMSMLAASGPTWDQCPPFQWS KSPFHSMLHMGQPDLWMFSPIRVPWDGRGSHHHHHHG ; B ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 LEU n 1 2 PRO n 1 3 THR n 1 4 LEU n 1 5 GLY n 1 6 PRO n 1 7 GLY n 1 8 TRP n 1 9 GLN n 1 10 ARG n 1 11 GLN n 1 12 ASN n 1 13 PRO n 1 14 ASP n 1 15 PRO n 1 16 PRO n 1 17 VAL n 1 18 SER n 1 19 ARG n 1 20 THR n 1 21 ARG n 1 22 SER n 1 23 LEU n 1 24 LEU n 1 25 LEU n 1 26 ASP n 1 27 ALA n 1 28 ALA n 1 29 SER n 1 30 GLY n 1 31 GLN n 1 32 LEU n 1 33 ARG n 1 34 LEU n 1 35 GLU n 1 36 ASP n 1 37 GLY n 1 38 PHE n 1 39 HIS n 1 40 PRO n 1 41 ASP n 1 42 ALA n 1 43 VAL n 1 44 ALA n 1 45 TRP n 1 46 ALA n 1 47 ASN n 1 48 LEU n 1 49 THR n 1 50 ASN n 1 51 ALA n 1 52 ILE n 1 53 ARG n 1 54 GLU n 1 55 THR n 1 56 GLY n 1 57 TRP n 1 58 ALA n 1 59 TYR n 1 60 LEU n 1 61 ASP n 1 62 LEU n 1 63 SER n 1 64 THR n 1 65 ASN n 1 66 GLY n 1 67 ARG n 1 68 TYR n 1 69 ASN n 1 70 ASP n 1 71 SER n 1 72 LEU n 1 73 GLN n 1 74 ALA n 1 75 TYR n 1 76 ALA n 1 77 ALA n 1 78 GLY n 1 79 VAL n 1 80 VAL n 1 81 GLU n 1 82 ALA n 1 83 SER n 1 84 VAL n 1 85 SER n 1 86 GLU n 1 87 GLU n 1 88 LEU n 1 89 ILE n 1 90 TYR n 1 91 MET n 1 92 HIS n 1 93 TRP n 1 94 MET n 1 95 ASN n 1 96 THR n 1 97 VAL n 1 98 VAL n 1 99 ASN n 1 100 TYR n 1 101 CYS n 1 102 GLY n 1 103 PRO n 1 104 PHE n 1 105 GLU n 1 106 TYR n 1 107 GLU n 1 108 VAL n 1 109 GLY n 1 110 TYR n 1 111 CYS n 1 112 GLU n 1 113 LYS n 1 114 LEU n 1 115 LYS n 1 116 ASN n 1 117 PHE n 1 118 LEU n 1 119 GLU n 1 120 ALA n 1 121 ASN n 1 122 LEU n 1 123 GLU n 1 124 TRP n 1 125 MET n 1 126 GLN n 1 127 ARG n 1 128 GLU n 1 129 MET n 1 130 GLU n 1 131 LEU n 1 132 ASN n 1 133 PRO n 1 134 ASP n 1 135 SER n 1 136 PRO n 1 137 TYR n 1 138 TRP n 1 139 HIS n 1 140 GLN n 1 141 VAL n 1 142 ARG n 1 143 LEU n 1 144 THR n 1 145 LEU n 1 146 LEU n 1 147 GLN n 1 148 LEU n 1 149 LYS n 1 150 GLY n 1 151 LEU n 1 152 GLU n 1 153 ASP n 1 154 SER n 1 155 TYR n 1 156 GLU n 1 157 GLY n 1 158 ARG n 1 159 LEU n 1 160 THR n 1 161 PHE n 1 162 PRO n 1 163 THR n 1 164 GLY n 1 165 ARG n 1 166 PHE n 1 167 THR n 1 168 ILE n 1 169 LYS n 1 170 PRO n 1 171 LEU n 1 172 GLY n 1 173 PHE n 1 174 LEU n 1 175 LEU n 1 176 LEU n 1 177 GLN n 1 178 ILE n 1 179 SER n 1 180 GLY n 1 181 ASP n 1 182 LEU n 1 183 GLU n 1 184 ASP n 1 185 LEU n 1 186 GLU n 1 187 PRO n 1 188 ALA n 1 189 LEU n 1 190 ASN n 1 191 LYS n 1 192 THR n 1 193 ASN n 1 194 THR n 1 195 LYS n 1 196 PRO n 1 197 SER n 1 198 LEU n 1 199 GLY n 1 200 SER n 1 201 GLY n 1 202 SER n 2 1 OCS n 2 2 SER n 2 3 ALA n 2 4 LEU n 2 5 ILE n 2 6 LYS n 2 7 LEU n 2 8 LEU n 2 9 PRO n 2 10 GLY n 2 11 GLY n 2 12 HIS n 2 13 ASP n 2 14 LEU n 2 15 LEU n 2 16 VAL n 2 17 ALA n 2 18 HIS n 2 19 ASN n 2 20 THR n 2 21 TRP n 2 22 ASN n 2 23 SER n 2 24 TYR n 2 25 GLN n 2 26 ASN n 2 27 MET n 2 28 LEU n 2 29 ARG n 2 30 ILE n 2 31 ILE n 2 32 LYS n 2 33 LYS n 2 34 TYR n 2 35 ARG n 2 36 LEU n 2 37 GLN n 2 38 PHE n 2 39 ARG n 2 40 GLU n 2 41 GLY n 2 42 PRO n 2 43 GLN n 2 44 GLU n 2 45 GLU n 2 46 TYR n 2 47 PRO n 2 48 LEU n 2 49 VAL n 2 50 ALA n 2 51 GLY n 2 52 ASN n 2 53 ASN n 2 54 LEU n 2 55 VAL n 2 56 PHE n 2 57 SER n 2 58 SER n 2 59 TYR n 2 60 PRO n 2 61 GLY n 2 62 THR n 2 63 ILE n 2 64 PHE n 2 65 SER n 2 66 GLY n 2 67 ASP n 2 68 ASP n 2 69 PHE n 2 70 TYR n 2 71 ILE n 2 72 LEU n 2 73 GLY n 2 74 SER n 2 75 GLY n 2 76 LEU n 2 77 VAL n 2 78 THR n 2 79 LEU n 2 80 GLU n 2 81 THR n 2 82 THR n 2 83 ILE n 2 84 GLY n 2 85 ASN n 2 86 LYS n 2 87 ASN n 2 88 PRO n 2 89 ALA n 2 90 LEU n 2 91 TRP n 2 92 LYS n 2 93 TYR n 2 94 VAL n 2 95 GLN n 2 96 PRO n 2 97 GLN n 2 98 GLY n 2 99 CYS n 2 100 VAL n 2 101 LEU n 2 102 GLU n 2 103 TRP n 2 104 ILE n 2 105 ARG n 2 106 ASN n 2 107 VAL n 2 108 VAL n 2 109 ALA n 2 110 ASN n 2 111 ARG n 2 112 LEU n 2 113 ALA n 2 114 LEU n 2 115 ASP n 2 116 GLY n 2 117 ALA n 2 118 THR n 2 119 TRP n 2 120 ALA n 2 121 ASP n 2 122 VAL n 2 123 PHE n 2 124 LYS n 2 125 ARG n 2 126 PHE n 2 127 ASN n 2 128 SER n 2 129 GLY n 2 130 THR n 2 131 TYR n 2 132 ASN n 2 133 ASN n 2 134 GLN n 2 135 TRP n 2 136 MET n 2 137 ILE n 2 138 VAL n 2 139 ASP n 2 140 TYR n 2 141 LYS n 2 142 ALA n 2 143 PHE n 2 144 LEU n 2 145 PRO n 2 146 ASN n 2 147 GLY n 2 148 PRO n 2 149 SER n 2 150 PRO n 2 151 GLY n 2 152 SER n 2 153 ARG n 2 154 VAL n 2 155 LEU n 2 156 THR n 2 157 ILE n 2 158 LEU n 2 159 GLU n 2 160 GLN n 2 161 ILE n 2 162 PRO n 2 163 GLY n 2 164 MET n 2 165 VAL n 2 166 VAL n 2 167 VAL n 2 168 ALA n 2 169 ASP n 2 170 LYS n 2 171 THR n 2 172 ALA n 2 173 GLU n 2 174 LEU n 2 175 TYR n 2 176 LYS n 2 177 THR n 2 178 THR n 2 179 TYR n 2 180 TRP n 2 181 ALA n 2 182 SER n 2 183 TYR n 2 184 ASN n 2 185 ILE n 2 186 PRO n 2 187 TYR n 2 188 PHE n 2 189 GLU n 2 190 THR n 2 191 VAL n 2 192 PHE n 2 193 ASN n 2 194 ALA n 2 195 SER n 2 196 GLY n 2 197 LEU n 2 198 GLN n 2 199 ALA n 2 200 LEU n 2 201 VAL n 2 202 ALA n 2 203 GLN n 2 204 TYR n 2 205 GLY n 2 206 ASP n 2 207 TRP n 2 208 PHE n 2 209 SER n 2 210 TYR n 2 211 THR n 2 212 LYS n 2 213 ASN n 2 214 PRO n 2 215 ARG n 2 216 ALA n 2 217 LYS n 2 218 ILE n 2 219 PHE n 2 220 GLN n 2 221 ARG n 2 222 ASP n 2 223 GLN n 2 224 SER n 2 225 LEU n 2 226 VAL n 2 227 GLU n 2 228 ASP n 2 229 MET n 2 230 ASP n 2 231 ALA n 2 232 MET n 2 233 VAL n 2 234 ARG n 2 235 LEU n 2 236 MET n 2 237 ARG n 2 238 TYR n 2 239 ASN n 2 240 ASP n 2 241 PHE n 2 242 LEU n 2 243 HIS n 2 244 ASP n 2 245 PRO n 2 246 LEU n 2 247 SER n 2 248 LEU n 2 249 CYS n 2 250 GLU n 2 251 ALA n 2 252 CYS n 2 253 ASN n 2 254 PRO n 2 255 LYS n 2 256 PRO n 2 257 ASN n 2 258 ALA n 2 259 GLU n 2 260 ASN n 2 261 ALA n 2 262 ILE n 2 263 SER n 2 264 ALA n 2 265 ARG n 2 266 SER n 2 267 ASP n 2 268 LEU n 2 269 ASN n 2 270 PRO n 2 271 ALA n 2 272 ASN n 2 273 GLY n 2 274 SER n 2 275 TYR n 2 276 PRO n 2 277 PHE n 2 278 GLN n 2 279 ALA n 2 280 LEU n 2 281 HIS n 2 282 GLN n 2 283 ARG n 2 284 ALA n 2 285 HIS n 2 286 GLY n 2 287 GLY n 2 288 ILE n 2 289 ASP n 2 290 VAL n 2 291 LYS n 2 292 VAL n 2 293 THR n 2 294 SER n 2 295 PHE n 2 296 THR n 2 297 LEU n 2 298 ALA n 2 299 LYS n 2 300 TYR n 2 301 MET n 2 302 SER n 2 303 MET n 2 304 LEU n 2 305 ALA n 2 306 ALA n 2 307 SER n 2 308 GLY n 2 309 PRO n 2 310 THR n 2 311 TRP n 2 312 ASP n 2 313 GLN n 2 314 CYS n 2 315 PRO n 2 316 PRO n 2 317 PHE n 2 318 GLN n 2 319 TRP n 2 320 SER n 2 321 LYS n 2 322 SER n 2 323 PRO n 2 324 PHE n 2 325 HIS n 2 326 SER n 2 327 MET n 2 328 LEU n 2 329 HIS n 2 330 MET n 2 331 GLY n 2 332 GLN n 2 333 PRO n 2 334 ASP n 2 335 LEU n 2 336 TRP n 2 337 MET n 2 338 PHE n 2 339 SER n 2 340 PRO n 2 341 ILE n 2 342 ARG n 2 343 VAL n 2 344 PRO n 2 345 TRP n 2 346 ASP n 2 347 GLY n 2 348 ARG n 2 349 GLY n 2 350 SER n 2 351 HIS n 2 352 HIS n 2 353 HIS n 2 354 HIS n 2 355 HIS n 2 356 HIS n 2 357 GLY 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 ? ? ? mouse ? AAG44101 ? C3H/RV ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? HT1080 ? ? 'fibrosarcoma cell' ? ? plasmid ? ? ? 'PCDNA3.1/HYGRO(+)' ? ? 2 1 sample ? ? ? mouse ? AAG44101 ? C3H/RV ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? human 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? HT1080 ? ? 'fibrosarcoma cell' ? ? plasmid ? ? ? 'PCDNA3.1/HYGRO(+)' ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP PLBL2_MOUSE Q3TCN2 1 ;LPTLGPGWQRQNPDPPVSRTRSLLLDAASGQLRLEDGFHPDAVAWANLTNAIRETGWAYLDLSTNGRYNDSLQAYAAGVV EASVSEELIYMHWMNTVVNYCGPFEYEVGYCEKLKNFLEANLEWMQREMELNPDSPYWHQVRLTLLQLKGLEDSYEGRLT FPTGRFTIKPLGFLLLQISGDLEDLEPALNKTNTKPSLGSGS ; 47 ? 2 UNP PLBL2_MOUSE Q3TCN2 2 ;CSALIKLLPGGHDLLVAHNTWNSYQNMLRIIKKYRLQFREGPQEEYPLVAGNNLVFSSYPGTIFSGDDFYILGSGLVTLE TTIGNKNPALWKYVQPQGCVLEWIRNVVANRLALDGATWADVFKRFNSGTYNNQWMIVDYKAFLPNGPSPGSRVLTILEQ IPGMVVVADKTAELYKTTYWASYNIPYFETVFNASGLQALVAQYGDWFSYTKNPRAKIFQRDQSLVEDMDAMVRLMRYND FLHDPLSLCEACNPKPNAENAISARSDLNPANGSYPFQALHQRAHGGIDVKVTSFTLAKYMSMLAASGPTWDQCPPFQWS KSPFHSMLHMGQPDLWMFSPIRVPWD ; 249 ? # 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 3FGR A 1 ? 202 ? Q3TCN2 47 ? 248 ? 47 248 2 2 3FGR B 1 ? 346 ? Q3TCN2 249 ? 594 ? 249 594 # 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 2 3FGR GLY B 347 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 595 1 2 3FGR ARG B 348 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 596 2 2 3FGR GLY B 349 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 597 3 2 3FGR SER B 350 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 598 4 2 3FGR HIS B 351 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 599 5 2 3FGR HIS B 352 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 600 6 2 3FGR HIS B 353 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 601 7 2 3FGR HIS B 354 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 602 8 2 3FGR HIS B 355 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 603 9 2 3FGR HIS B 356 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 604 10 2 3FGR GLY B 357 ? UNP Q3TCN2 ? ? 'EXPRESSION TAG' 605 11 # 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 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 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 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 OCS 'L-peptide linking' n 'CYSTEINESULFONIC ACID' ? 'C3 H7 N O5 S' 169.156 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 XE non-polymer . XENON ? Xe 131.293 # _exptl.entry_id 3FGR _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.37 _exptl_crystal.density_percent_sol 63.54 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.6 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '12% (w/v) PEG 4000, 200mM NH4AC, 100mM NaAc/HAc pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'MAR CCD 165 mm' _diffrn_detector.pdbx_collection_date 2008-03-07 _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 0.91841 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'BESSY BEAMLINE 14.2' _diffrn_source.pdbx_synchrotron_site BESSY _diffrn_source.pdbx_synchrotron_beamline 14.2 _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 0.91841 # _reflns.entry_id 3FGR _reflns.observed_criterion_sigma_I ? _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 50.000 _reflns.d_resolution_high 1.700 _reflns.number_obs 91683 _reflns.number_all ? _reflns.percent_possible_obs 99.500 _reflns.pdbx_Rmerge_I_obs 0.033 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 32.075 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.200 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.70 _reflns_shell.d_res_low 1.76 _reflns_shell.percent_possible_all 96.20 _reflns_shell.Rmerge_I_obs 0.419 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy 2.60 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all ? _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 3FGR _refine.ls_number_reflns_obs 77685 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.00 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 29.26 _refine.ls_d_res_high 1.80 _refine.ls_percent_reflns_obs 99.87 _refine.ls_R_factor_obs 0.15314 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.15163 _refine.ls_R_factor_R_free 0.18163 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.9 _refine.ls_number_reflns_R_work 73846 _refine.ls_number_reflns_R_free 3839 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min 0.10 _refine.occupancy_max 1.00 _refine.correlation_coeff_Fo_to_Fc 0.969 _refine.correlation_coeff_Fo_to_Fc_free 0.956 _refine.B_iso_mean 24.259 _refine.aniso_B[1][1] -0.51 _refine.aniso_B[2][2] -0.51 _refine.aniso_B[3][3] 0.89 _refine.aniso_B[1][2] 0.00 _refine.aniso_B[1][3] -0.44 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB ENTRY 3FBX' _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 0.085 _refine.pdbx_overall_ESU_R_Free 0.087 _refine.overall_SU_ML 0.052 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 1.607 _refine.overall_SU_R_Cruickshank_DPI 0.085 _refine.overall_SU_R_free 0.087 _refine.ls_wR_factor_R_work 0.157 _refine.ls_wR_factor_R_free 0.186 _refine.overall_FOM_work_R_set 0.899 _refine.B_iso_max 100.13 _refine.B_iso_min 9.63 _refine.ls_redundancy_reflns_obs ? _refine.overall_FOM_free_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _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 4180 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 174 _refine_hist.number_atoms_solvent 576 _refine_hist.number_atoms_total 4930 _refine_hist.d_res_high 1.80 _refine_hist.d_res_low 29.26 # 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 0.015 0.022 ? 4607 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.533 1.984 ? 6282 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.707 5.000 ? 567 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 34.654 23.944 ? 213 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 13.418 15.000 ? 723 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 21.962 15.000 ? 27 'X-RAY DIFFRACTION' ? r_chiral_restr 0.121 0.200 ? 681 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.007 0.020 ? 3506 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined 0.228 0.300 ? 2360 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined 0.323 0.500 ? 3157 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.207 0.500 ? 853 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.177 0.300 ? 40 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.170 0.500 ? 29 '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 0.955 1.500 ? 2688 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.777 2.000 ? 4353 'X-RAY DIFFRACTION' ? r_scbond_it 2.926 3.000 ? 2019 'X-RAY DIFFRACTION' ? r_scangle_it 4.534 4.500 ? 1906 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.800 _refine_ls_shell.d_res_low 1.847 _refine_ls_shell.number_reflns_R_work 5489 _refine_ls_shell.R_factor_R_work 0.203 _refine_ls_shell.percent_reflns_obs 99.79 _refine_ls_shell.R_factor_R_free 0.287 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 259 _refine_ls_shell.number_reflns_all 5748 _refine_ls_shell.R_factor_all ? _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.number_reflns_obs ? # _struct.entry_id 3FGR _struct.title 'Two chain form of the 66.3 kDa protein at 1.8 Angstroem' _struct.pdbx_descriptor 'Putative phospholipase B-like 2 28 kDa form (E.C.3.1.1.-), Putative phospholipase B-like 2 40 kDa form (E.C.3.1.1.-)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3FGR _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text ;alpha beta, glycosylated, disulphide bonds, N-terminal nucleophile hydrolase fold, two chain form, Glycoprotein, Hydrolase, Lipid degradation, Lysosome ; # 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 5 ? J N N 4 ? K N N 3 ? L N N 3 ? M N N 3 ? N N N 4 ? O N N 4 ? P N N 4 ? Q N N 4 ? R N N 4 ? S N N 4 ? T N N 4 ? U N N 4 ? V N N 5 ? W N N 6 ? X N N 7 ? Y N N 8 ? Z N N 8 ? # _struct_biol.id 1 _struct_biol.details 'author states that the biological unit is unknown' # 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 ALA A 51 ? GLY A 56 ? ALA A 97 GLY A 102 1 ? 6 HELX_P HELX_P2 2 ASN A 69 ? VAL A 97 ? ASN A 115 VAL A 143 1 ? 29 HELX_P HELX_P3 3 GLU A 107 ? ASN A 132 ? GLU A 153 ASN A 178 1 ? 26 HELX_P HELX_P4 4 SER A 135 ? GLY A 157 ? SER A 181 GLY A 203 1 ? 23 HELX_P HELX_P5 5 PHE A 173 ? ILE A 178 ? PHE A 219 ILE A 224 1 ? 6 HELX_P HELX_P6 6 ILE A 178 ? LEU A 189 ? ILE A 224 LEU A 235 1 ? 12 HELX_P HELX_P7 7 PRO B 9 ? HIS B 12 ? PRO B 257 HIS B 260 5 ? 4 HELX_P HELX_P8 8 GLN B 25 ? MET B 27 ? GLN B 273 MET B 275 5 ? 3 HELX_P HELX_P9 9 ASN B 87 ? VAL B 94 ? ASN B 335 VAL B 342 5 ? 8 HELX_P HELX_P10 10 LEU B 101 ? ALA B 113 ? LEU B 349 ALA B 361 1 ? 13 HELX_P HELX_P11 11 ASP B 115 ? LYS B 124 ? ASP B 363 LYS B 372 1 ? 10 HELX_P HELX_P12 12 LYS B 141 ? PHE B 143 ? LYS B 389 PHE B 391 5 ? 3 HELX_P HELX_P13 13 LYS B 170 ? THR B 178 ? LYS B 418 THR B 426 1 ? 9 HELX_P HELX_P14 14 PHE B 188 ? SER B 195 ? PHE B 436 SER B 443 1 ? 8 HELX_P HELX_P15 15 GLY B 196 ? GLY B 205 ? GLY B 444 GLY B 453 1 ? 10 HELX_P HELX_P16 16 ASP B 206 ? SER B 209 ? ASP B 454 SER B 457 5 ? 4 HELX_P HELX_P17 17 ASN B 213 ? GLN B 223 ? ASN B 461 GLN B 471 1 ? 11 HELX_P HELX_P18 18 SER B 224 ? VAL B 226 ? SER B 472 VAL B 474 5 ? 3 HELX_P HELX_P19 19 ASP B 228 ? ARG B 237 ? ASP B 476 ARG B 485 1 ? 10 HELX_P HELX_P20 20 ASP B 244 ? LEU B 248 ? ASP B 492 LEU B 496 5 ? 5 HELX_P HELX_P21 21 ARG B 265 ? ASN B 269 ? ARG B 513 ASN B 517 5 ? 5 HELX_P HELX_P22 22 PHE B 277 ? HIS B 281 ? PHE B 525 HIS B 529 5 ? 5 HELX_P HELX_P23 23 SER B 294 ? TYR B 300 ? SER B 542 TYR B 548 1 ? 7 HELX_P HELX_P24 24 SER B 320 ? SER B 322 ? SER B 568 SER B 570 5 ? 3 # _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 101 SG ? ? ? 1_555 A CYS 111 SG ? ? A CYS 147 A CYS 157 1_555 ? ? ? ? ? ? ? 2.112 ? disulf2 disulf ? ? B CYS 249 SG ? ? ? 1_555 B CYS 252 SG ? ? B CYS 497 B CYS 500 1_555 ? ? ? ? ? ? ? 2.121 ? covale1 covale ? ? A ASN 47 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 93 A NAG 1 1_555 ? ? ? ? ? ? ? 1.501 ? covale2 covale ? ? A ASN 69 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 115 A NAG 11 1_555 ? ? ? ? ? ? ? 1.343 ? covale3 covale ? ? A ASN 190 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 236 A NAG 21 1_555 ? ? ? ? ? ? ? 1.300 ? covale4 covale ? ? B ASN 193 ND2 ? ? ? 1_555 K NAG . C1 ? ? B ASN 441 B NAG 31 1_555 ? ? ? ? ? ? ? 1.322 ? covale5 covale ? ? B ASN 272 ND2 ? ? ? 1_555 M NAG . C1 ? ? B ASN 520 B NAG 41 1_555 ? ? ? ? ? ? ? 1.251 ? covale6 covale ? ? C NAG . O4 ? ? ? 1_555 D NAG . C1 ? ? A NAG 11 A NAG 12 1_555 ? ? ? ? ? ? ? 1.488 ? covale7 covale ? ? K NAG . O4 ? ? ? 1_555 L NAG . C1 ? ? B NAG 31 B NAG 32 1_555 ? ? ? ? ? ? ? 1.339 ? covale8 covale ? ? B OCS 1 C ? ? ? 1_555 B SER 2 N ? ? B OCS 249 B SER 250 1_555 ? ? ? ? ? ? ? 1.325 ? metalc1 metalc ? ? B OCS 1 OD1 ? ? ? 1_555 X NA . NA ? ? B OCS 249 B NA 607 1_555 ? ? ? ? ? ? ? 2.998 ? metalc2 metalc ? ? B OCS 1 OD2 ? ? ? 1_555 X NA . NA ? ? B OCS 249 B NA 607 1_555 ? ? ? ? ? ? ? 2.758 ? metalc3 metalc ? ? B ASP 67 O ? ? ? 1_555 X NA . NA ? ? B ASP 315 B NA 607 1_555 ? ? ? ? ? ? ? 2.861 ? metalc4 metalc ? ? B GLU 80 OE1 ? ? ? 1_555 X NA . NA ? ? B GLU 328 B NA 607 1_555 ? ? ? ? ? ? ? 2.759 ? metalc5 metalc ? ? B THR 82 OG1 ? ? ? 1_555 X NA . NA ? ? B THR 330 B NA 607 1_555 ? ? ? ? ? ? ? 2.819 ? metalc6 metalc ? ? B TYR 131 OH ? ? ? 1_555 X NA . NA ? ? B TYR 379 B NA 607 1_555 ? ? ? ? ? ? ? 2.837 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASP 67 B . ? ASP 315 B ASP 68 B ? ASP 316 B 1 -4.68 2 ASN 253 B . ? ASN 501 B PRO 254 B ? PRO 502 B 1 2.95 3 VAL 343 B . ? VAL 591 B PRO 344 B ? PRO 592 B 1 10.32 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 11 ? B ? 6 ? C ? 2 ? D ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel A 7 8 ? anti-parallel A 8 9 ? anti-parallel A 9 10 ? anti-parallel A 10 11 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel C 1 2 ? anti-parallel D 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 GLN A 31 ? ASP A 36 ? GLN A 77 ASP A 82 A 2 SER A 18 ? ASP A 26 ? SER A 64 ASP A 72 A 3 ALA A 44 ? ASN A 50 ? ALA A 90 ASN A 96 A 4 ALA A 58 ? THR A 64 ? ALA A 104 THR A 110 A 5 ILE B 30 ? ARG B 35 ? ILE B 278 ARG B 283 A 6 ASN B 53 ? SER B 58 ? ASN B 301 SER B 306 A 7 PHE B 69 ? LEU B 72 ? PHE B 317 LEU B 320 A 8 LEU B 76 ? THR B 82 ? LEU B 324 THR B 330 A 9 ASN B 133 ? ASP B 139 ? ASN B 381 ASP B 387 A 10 LEU B 155 ? ILE B 161 ? LEU B 403 ILE B 409 A 11 MET B 164 ? ASP B 169 ? MET B 412 ASP B 417 B 1 TYR B 179 ? SER B 182 ? TYR B 427 SER B 430 B 2 SER B 2 ? LEU B 7 ? SER B 250 LEU B 255 B 3 LEU B 14 ? ASN B 19 ? LEU B 262 ASN B 267 B 4 ASP B 289 ? THR B 293 ? ASP B 537 THR B 541 B 5 MET B 303 ? SER B 307 ? MET B 551 SER B 555 B 6 ILE B 341 ? VAL B 343 ? ILE B 589 VAL B 591 C 1 TRP B 21 ? SER B 23 ? TRP B 269 SER B 271 C 2 HIS B 285 ? GLY B 287 ? HIS B 533 GLY B 535 D 1 PHE B 317 ? GLN B 318 ? PHE B 565 GLN B 566 D 2 LEU B 335 ? TRP B 336 ? LEU B 583 TRP B 584 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 O ARG A 33 ? O ARG A 79 N LEU A 24 ? N LEU A 70 A 2 3 N LEU A 23 ? N LEU A 69 O ALA A 44 ? O ALA A 90 A 3 4 N TRP A 45 ? N TRP A 91 O SER A 63 ? O SER A 109 A 4 5 N ALA A 58 ? N ALA A 104 O ILE B 31 ? O ILE B 279 A 5 6 N TYR B 34 ? N TYR B 282 O LEU B 54 ? O LEU B 302 A 6 7 N VAL B 55 ? N VAL B 303 O ILE B 71 ? O ILE B 319 A 7 8 N LEU B 72 ? N LEU B 320 O LEU B 76 ? O LEU B 324 A 8 9 N LEU B 79 ? N LEU B 327 O MET B 136 ? O MET B 384 A 9 10 N TRP B 135 ? N TRP B 383 O LEU B 158 ? O LEU B 406 A 10 11 N ILE B 157 ? N ILE B 405 O ALA B 168 ? O ALA B 416 B 1 2 O TRP B 180 ? O TRP B 428 N ILE B 5 ? N ILE B 253 B 2 3 N SER B 2 ? N SER B 250 O ASN B 19 ? O ASN B 267 B 3 4 N VAL B 16 ? N VAL B 264 O THR B 293 ? O THR B 541 B 4 5 N VAL B 292 ? N VAL B 540 O LEU B 304 ? O LEU B 552 B 5 6 N MET B 303 ? N MET B 551 O VAL B 343 ? O VAL B 591 C 1 2 N ASN B 22 ? N ASN B 270 O GLY B 286 ? O GLY B 534 D 1 2 N PHE B 317 ? N PHE B 565 O TRP B 336 ? O TRP B 584 # 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 ? ? ? ? 9 'BINDING SITE FOR RESIDUE NAG A 11' AC2 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 12' AC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 21' AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG A 1' AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL A 9' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 10' AC7 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE ACT A 22' AC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 3' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG B 31' BC1 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 32' BC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NAG B 41' BC3 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL B 11' BC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL B 1' BC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL B 2' BC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE GOL B 4' BC7 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL B 5' BC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL B 6' BC9 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL B 7' CC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL B 8' CC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ACT B 21' CC3 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE XE B 606' CC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NA B 607' # 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 9 NAG D . ? NAG A 12 . ? 1_555 ? 2 AC1 9 ASN A 69 ? ASN A 115 . ? 1_555 ? 3 AC1 9 SER A 71 ? SER A 117 . ? 1_555 ? 4 AC1 9 PHE A 161 ? PHE A 207 . ? 1_555 ? 5 AC1 9 THR A 163 ? THR A 209 . ? 1_555 ? 6 AC1 9 HOH Y . ? HOH A 258 . ? 1_555 ? 7 AC1 9 HOH Y . ? HOH A 279 . ? 1_555 ? 8 AC1 9 HOH Y . ? HOH A 506 . ? 1_555 ? 9 AC1 9 HOH Y . ? HOH A 716 . ? 1_555 ? 10 AC2 7 NAG C . ? NAG A 11 . ? 1_555 ? 11 AC2 7 GLY A 30 ? GLY A 76 . ? 1_555 ? 12 AC2 7 PHE A 161 ? PHE A 207 . ? 1_555 ? 13 AC2 7 THR A 163 ? THR A 209 . ? 1_555 ? 14 AC2 7 HOH Y . ? HOH A 297 . ? 1_555 ? 15 AC2 7 HOH Y . ? HOH A 381 . ? 1_555 ? 16 AC2 7 HOH Y . ? HOH A 505 . ? 1_555 ? 17 AC3 3 LYS A 113 ? LYS A 159 . ? 1_555 ? 18 AC3 3 ASN A 190 ? ASN A 236 . ? 1_555 ? 19 AC3 3 GOL N . ? GOL B 11 . ? 1_555 ? 20 AC4 3 ASN A 47 ? ASN A 93 . ? 1_555 ? 21 AC4 3 THR A 49 ? THR A 95 . ? 1_555 ? 22 AC4 3 TYR A 59 ? TYR A 105 . ? 1_555 ? 23 AC5 5 ARG A 142 ? ARG A 188 . ? 1_555 ? 24 AC5 5 THR A 163 ? THR A 209 . ? 1_555 ? 25 AC5 5 HOH Y . ? HOH A 290 . ? 1_555 ? 26 AC5 5 HOH Y . ? HOH A 294 . ? 1_555 ? 27 AC5 5 HOH Y . ? HOH A 471 . ? 1_555 ? 28 AC6 6 ASN A 99 ? ASN A 145 . ? 1_555 ? 29 AC6 6 TYR A 100 ? TYR A 146 . ? 1_555 ? 30 AC6 6 CYS A 101 ? CYS A 147 . ? 1_555 ? 31 AC6 6 GLU A 105 ? GLU A 151 . ? 1_555 ? 32 AC6 6 GLU A 107 ? GLU A 153 . ? 1_555 ? 33 AC6 6 LYS A 191 ? LYS A 237 . ? 1_555 ? 34 AC7 8 TRP A 124 ? TRP A 170 . ? 1_555 ? 35 AC7 8 ARG A 127 ? ARG A 173 . ? 1_555 ? 36 AC7 8 GLU A 128 ? GLU A 174 . ? 1_555 ? 37 AC7 8 HOH Z . ? HOH B 14 . ? 4_546 ? 38 AC7 8 HOH Z . ? HOH B 127 . ? 4_546 ? 39 AC7 8 HOH Z . ? HOH B 185 . ? 4_546 ? 40 AC7 8 PRO B 9 ? PRO B 257 . ? 4_546 ? 41 AC7 8 HOH Z . ? HOH B 626 . ? 4_546 ? 42 AC8 8 HIS A 92 ? HIS A 138 . ? 1_555 ? 43 AC8 8 LEU A 176 ? LEU A 222 . ? 1_555 ? 44 AC8 8 SER A 179 ? SER A 225 . ? 1_555 ? 45 AC8 8 HOH Y . ? HOH A 659 . ? 1_555 ? 46 AC8 8 ASN B 22 ? ASN B 270 . ? 1_555 ? 47 AC8 8 ASN B 26 ? ASN B 274 . ? 1_555 ? 48 AC8 8 TYR B 59 ? TYR B 307 . ? 1_555 ? 49 AC8 8 THR B 62 ? THR B 310 . ? 1_555 ? 50 AC9 6 NAG L . ? NAG B 32 . ? 1_555 ? 51 AC9 6 ASN B 193 ? ASN B 441 . ? 1_555 ? 52 AC9 6 GLN B 198 ? GLN B 446 . ? 1_555 ? 53 AC9 6 HOH Z . ? HOH B 674 . ? 1_555 ? 54 AC9 6 HOH Z . ? HOH B 697 . ? 1_555 ? 55 AC9 6 HOH Z . ? HOH B 789 . ? 1_555 ? 56 BC1 1 NAG K . ? NAG B 31 . ? 1_555 ? 57 BC2 2 ASN B 272 ? ASN B 520 . ? 1_555 ? 58 BC2 2 HOH Z . ? HOH B 718 . ? 1_555 ? 59 BC3 9 NAG E . ? NAG A 21 . ? 1_555 ? 60 BC3 9 ALA A 188 ? ALA A 234 . ? 1_555 ? 61 BC3 9 LEU A 189 ? LEU A 235 . ? 1_555 ? 62 BC3 9 TRP B 91 ? TRP B 339 . ? 1_555 ? 63 BC3 9 LYS B 92 ? LYS B 340 . ? 1_555 ? 64 BC3 9 VAL B 94 ? VAL B 342 . ? 1_555 ? 65 BC3 9 GLN B 95 ? GLN B 343 . ? 1_555 ? 66 BC3 9 HOH Z . ? HOH B 695 . ? 1_555 ? 67 BC3 9 HOH Z . ? HOH B 734 . ? 1_555 ? 68 BC4 6 TYR A 137 ? TYR A 183 . ? 1_555 ? 69 BC4 6 HOH Z . ? HOH B 169 . ? 1_555 ? 70 BC4 6 ASP B 121 ? ASP B 369 . ? 1_555 ? 71 BC4 6 VAL B 122 ? VAL B 370 . ? 1_555 ? 72 BC4 6 ARG B 125 ? ARG B 373 . ? 1_555 ? 73 BC4 6 HOH Z . ? HOH B 790 . ? 1_555 ? 74 BC5 8 GLU A 183 ? GLU A 229 . ? 1_555 ? 75 BC5 8 ASP A 184 ? ASP A 230 . ? 1_555 ? 76 BC5 8 HOH Y . ? HOH A 277 . ? 1_555 ? 77 BC5 8 HOH Y . ? HOH A 692 . ? 1_555 ? 78 BC5 8 GLY B 84 ? GLY B 332 . ? 1_555 ? 79 BC5 8 ASN B 85 ? ASN B 333 . ? 1_555 ? 80 BC5 8 LYS B 86 ? LYS B 334 . ? 1_555 ? 81 BC5 8 HOH Z . ? HOH B 683 . ? 1_555 ? 82 BC6 5 TYR B 187 ? TYR B 435 . ? 1_555 ? 83 BC6 5 PHE B 188 ? PHE B 436 . ? 1_555 ? 84 BC6 5 GLU B 189 ? GLU B 437 . ? 1_555 ? 85 BC6 5 HOH Z . ? HOH B 636 . ? 1_555 ? 86 BC6 5 HOH Z . ? HOH B 849 . ? 1_555 ? 87 BC7 8 ARG B 125 ? ARG B 373 . ? 4_556 ? 88 BC7 8 ASP B 222 ? ASP B 470 . ? 1_555 ? 89 BC7 8 LEU B 225 ? LEU B 473 . ? 1_555 ? 90 BC7 8 ALA B 231 ? ALA B 479 . ? 1_555 ? 91 BC7 8 ARG B 234 ? ARG B 482 . ? 1_555 ? 92 BC7 8 LEU B 235 ? LEU B 483 . ? 1_555 ? 93 BC7 8 HOH Z . ? HOH B 741 . ? 1_555 ? 94 BC7 8 HOH Z . ? HOH B 822 . ? 1_555 ? 95 BC8 8 GLN A 147 ? GLN A 193 . ? 1_555 ? 96 BC8 8 HOH Y . ? HOH A 383 . ? 1_555 ? 97 BC8 8 TYR B 34 ? TYR B 282 . ? 1_555 ? 98 BC8 8 LEU B 36 ? LEU B 284 . ? 1_555 ? 99 BC8 8 ILE B 63 ? ILE B 311 . ? 1_555 ? 100 BC8 8 VAL B 107 ? VAL B 355 . ? 1_555 ? 101 BC8 8 ARG B 111 ? ARG B 359 . ? 1_555 ? 102 BC8 8 HOH Z . ? HOH B 616 . ? 1_555 ? 103 BC9 9 TRP B 21 ? TRP B 269 . ? 1_555 ? 104 BC9 9 ILE B 185 ? ILE B 433 . ? 1_555 ? 105 BC9 9 TRP B 207 ? TRP B 455 . ? 1_555 ? 106 BC9 9 ASN B 213 ? ASN B 461 . ? 1_555 ? 107 BC9 9 PRO B 214 ? PRO B 462 . ? 1_555 ? 108 BC9 9 ARG B 215 ? ARG B 463 . ? 1_555 ? 109 BC9 9 GLU B 259 ? GLU B 507 . ? 1_555 ? 110 BC9 9 ASN B 260 ? ASN B 508 . ? 1_555 ? 111 BC9 9 HOH Z . ? HOH B 743 . ? 1_555 ? 112 CC1 6 GLU B 45 ? GLU B 293 . ? 1_555 ? 113 CC1 6 TYR B 46 ? TYR B 294 . ? 1_555 ? 114 CC1 6 PRO B 245 ? PRO B 493 . ? 4_546 ? 115 CC1 6 HOH Z . ? HOH B 690 . ? 1_555 ? 116 CC1 6 HOH Z . ? HOH B 815 . ? 1_555 ? 117 CC1 6 HOH Z . ? HOH B 835 . ? 1_555 ? 118 CC2 5 ASP B 240 ? ASP B 488 . ? 1_555 ? 119 CC2 5 HIS B 243 ? HIS B 491 . ? 1_555 ? 120 CC2 5 ASP B 244 ? ASP B 492 . ? 1_555 ? 121 CC2 5 HOH Z . ? HOH B 765 . ? 1_555 ? 122 CC2 5 HOH Z . ? HOH B 867 . ? 1_555 ? 123 CC3 3 PHE A 117 ? PHE A 163 . ? 1_555 ? 124 CC3 3 ASN A 121 ? ASN A 167 . ? 1_555 ? 125 CC3 3 LEU B 101 ? LEU B 349 . ? 1_555 ? 126 CC4 6 SER A 200 ? SER A 246 . ? 1_555 ? 127 CC4 6 OCS B 1 ? OCS B 249 . ? 1_555 ? 128 CC4 6 ASP B 67 ? ASP B 315 . ? 1_555 ? 129 CC4 6 GLU B 80 ? GLU B 328 . ? 1_555 ? 130 CC4 6 THR B 82 ? THR B 330 . ? 1_555 ? 131 CC4 6 TYR B 131 ? TYR B 379 . ? 1_555 ? # _atom_sites.entry_id 3FGR _atom_sites.fract_transf_matrix[1][1] 0.006723 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.001028 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.011166 _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] 0.015609 _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 NA O S XE # 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 . VAL A 1 17 ? 3.626 66.932 51.190 1.00 41.43 ? 63 VAL A N 1 ATOM 2 C CA . VAL A 1 17 ? 5.000 67.150 50.626 1.00 41.00 ? 63 VAL A CA 1 ATOM 3 C C . VAL A 1 17 ? 6.000 66.094 51.132 1.00 40.41 ? 63 VAL A C 1 ATOM 4 O O . VAL A 1 17 ? 6.868 65.678 50.384 1.00 39.83 ? 63 VAL A O 1 ATOM 5 C CB . VAL A 1 17 ? 5.539 68.615 50.818 1.00 41.61 ? 63 VAL A CB 1 ATOM 6 C CG1 . VAL A 1 17 ? 4.393 69.634 50.683 1.00 42.44 ? 63 VAL A CG1 1 ATOM 7 C CG2 . VAL A 1 17 ? 6.287 68.797 52.146 1.00 41.93 ? 63 VAL A CG2 1 ATOM 8 N N . SER A 1 18 ? 5.848 65.638 52.376 1.00 38.90 ? 64 SER A N 1 ATOM 9 C CA . SER A 1 18 ? 6.760 64.624 52.920 1.00 37.94 ? 64 SER A CA 1 ATOM 10 C C . SER A 1 18 ? 6.038 63.440 53.579 1.00 36.52 ? 64 SER A C 1 ATOM 11 O O . SER A 1 18 ? 4.982 63.610 54.198 1.00 37.06 ? 64 SER A O 1 ATOM 12 C CB . SER A 1 18 ? 7.732 65.256 53.907 1.00 38.62 ? 64 SER A CB 1 ATOM 13 O OG . SER A 1 18 ? 8.621 64.265 54.389 1.00 40.90 ? 64 SER A OG 1 ATOM 14 N N . ARG A 1 19 ? 6.589 62.234 53.454 1.00 33.09 ? 65 ARG A N 1 ATOM 15 C CA . ARG A 1 19 ? 5.957 61.080 54.078 1.00 30.07 ? 65 ARG A CA 1 ATOM 16 C C . ARG A 1 19 ? 7.031 60.067 54.475 1.00 28.48 ? 65 ARG A C 1 ATOM 17 O O . ARG A 1 19 ? 7.916 59.803 53.674 1.00 26.00 ? 65 ARG A O 1 ATOM 18 C CB . ARG A 1 19 ? 4.968 60.427 53.111 1.00 30.66 ? 65 ARG A CB 1 ATOM 19 C CG . ARG A 1 19 ? 4.333 59.186 53.684 1.00 34.19 ? 65 ARG A CG 1 ATOM 20 C CD . ARG A 1 19 ? 3.489 58.460 52.667 1.00 39.74 ? 65 ARG A CD 1 ATOM 21 N NE . ARG A 1 19 ? 2.248 59.166 52.387 1.00 44.61 ? 65 ARG A NE 1 ATOM 22 C CZ . ARG A 1 19 ? 1.633 59.151 51.207 1.00 47.24 ? 65 ARG A CZ 1 ATOM 23 N NH1 . ARG A 1 19 ? 2.158 58.469 50.190 1.00 47.28 ? 65 ARG A NH1 1 ATOM 24 N NH2 . ARG A 1 19 ? 0.499 59.831 51.039 1.00 48.26 ? 65 ARG A NH2 1 ATOM 25 N N . THR A 1 20 ? 6.943 59.523 55.689 1.00 26.25 ? 66 THR A N 1 ATOM 26 C CA . THR A 1 20 ? 7.905 58.524 56.201 1.00 25.46 ? 66 THR A CA 1 ATOM 27 C C . THR A 1 20 ? 7.164 57.259 56.632 1.00 23.84 ? 66 THR A C 1 ATOM 28 O O . THR A 1 20 ? 6.125 57.327 57.317 1.00 23.40 ? 66 THR A O 1 ATOM 29 C CB . THR A 1 20 ? 8.726 59.089 57.390 1.00 26.20 ? 66 THR A CB 1 ATOM 30 O OG1 . THR A 1 20 ? 9.389 60.284 56.961 1.00 30.65 ? 66 THR A OG1 1 ATOM 31 C CG2 . THR A 1 20 ? 9.781 58.094 57.866 1.00 26.06 ? 66 THR A CG2 1 ATOM 32 N N . ARG A 1 21 ? 7.685 56.096 56.250 1.00 21.52 ? 67 ARG A N 1 ATOM 33 C CA A ARG A 1 21 ? 7.043 54.821 56.553 0.25 21.38 ? 67 ARG A CA 1 ATOM 34 C CA B ARG A 1 21 ? 7.059 54.837 56.623 0.75 21.78 ? 67 ARG A CA 1 ATOM 35 C C . ARG A 1 21 ? 8.107 53.801 56.932 1.00 21.33 ? 67 ARG A C 1 ATOM 36 O O . ARG A 1 21 ? 9.186 53.812 56.343 1.00 20.23 ? 67 ARG A O 1 ATOM 37 C CB A ARG A 1 21 ? 6.269 54.307 55.332 0.25 21.44 ? 67 ARG A CB 1 ATOM 38 C CB B ARG A 1 21 ? 6.132 54.308 55.531 0.75 22.61 ? 67 ARG A CB 1 ATOM 39 C CG A ARG A 1 21 ? 5.107 55.201 54.891 0.25 21.87 ? 67 ARG A CG 1 ATOM 40 C CG B ARG A 1 21 ? 4.904 55.185 55.378 0.75 24.99 ? 67 ARG A CG 1 ATOM 41 C CD A ARG A 1 21 ? 3.955 55.132 55.873 0.25 22.42 ? 67 ARG A CD 1 ATOM 42 C CD B ARG A 1 21 ? 3.637 54.384 55.396 0.75 30.27 ? 67 ARG A CD 1 ATOM 43 N NE A ARG A 1 21 ? 2.721 55.657 55.290 0.25 21.64 ? 67 ARG A NE 1 ATOM 44 N NE B ARG A 1 21 ? 2.846 54.729 54.228 0.75 37.38 ? 67 ARG A NE 1 ATOM 45 C CZ A ARG A 1 21 ? 2.241 56.881 55.492 0.25 23.42 ? 67 ARG A CZ 1 ATOM 46 C CZ B ARG A 1 21 ? 1.853 53.987 53.752 0.75 38.51 ? 67 ARG A CZ 1 ATOM 47 N NH1 A ARG A 1 21 ? 2.871 57.733 56.290 0.25 24.07 ? 67 ARG A NH1 1 ATOM 48 N NH1 B ARG A 1 21 ? 1.495 52.862 54.373 0.75 40.11 ? 67 ARG A NH1 1 ATOM 49 N NH2 A ARG A 1 21 ? 1.107 57.245 54.906 0.25 21.31 ? 67 ARG A NH2 1 ATOM 50 N NH2 B ARG A 1 21 ? 1.218 54.375 52.662 0.75 38.48 ? 67 ARG A NH2 1 ATOM 51 N N . SER A 1 22 ? 7.788 52.923 57.881 1.00 20.12 ? 68 SER A N 1 ATOM 52 C CA . SER A 1 22 ? 8.705 51.838 58.256 1.00 20.07 ? 68 SER A CA 1 ATOM 53 C C . SER A 1 22 ? 7.980 50.498 58.135 1.00 20.60 ? 68 SER A C 1 ATOM 54 O O . SER A 1 22 ? 6.763 50.427 58.371 1.00 21.08 ? 68 SER A O 1 ATOM 55 C CB . SER A 1 22 ? 9.217 52.015 59.708 1.00 19.41 ? 68 SER A CB 1 ATOM 56 O OG . SER A 1 22 ? 9.774 53.311 59.883 1.00 19.39 ? 68 SER A OG 1 ATOM 57 N N . LEU A 1 23 ? 8.723 49.440 57.779 1.00 19.49 ? 69 LEU A N 1 ATOM 58 C CA . LEU A 1 23 ? 8.163 48.092 57.690 1.00 19.64 ? 69 LEU A CA 1 ATOM 59 C C . LEU A 1 23 ? 8.701 47.246 58.832 1.00 20.94 ? 69 LEU A C 1 ATOM 60 O O . LEU A 1 23 ? 9.889 46.913 58.876 1.00 19.04 ? 69 LEU A O 1 ATOM 61 C CB . LEU A 1 23 ? 8.517 47.402 56.352 1.00 19.67 ? 69 LEU A CB 1 ATOM 62 C CG . LEU A 1 23 ? 7.838 46.031 56.170 1.00 18.77 ? 69 LEU A CG 1 ATOM 63 C CD1 . LEU A 1 23 ? 6.338 46.282 55.975 1.00 17.92 ? 69 LEU A CD1 1 ATOM 64 C CD2 . LEU A 1 23 ? 8.415 45.238 54.945 1.00 20.77 ? 69 LEU A CD2 1 ATOM 65 N N . LEU A 1 24 ? 7.809 46.892 59.757 1.00 22.60 ? 70 LEU A N 1 ATOM 66 C CA . LEU A 1 24 ? 8.189 46.091 60.903 1.00 24.36 ? 70 LEU A CA 1 ATOM 67 C C . LEU A 1 24 ? 7.875 44.625 60.697 1.00 24.86 ? 70 LEU A C 1 ATOM 68 O O . LEU A 1 24 ? 6.928 44.282 60.005 1.00 25.25 ? 70 LEU A O 1 ATOM 69 C CB . LEU A 1 24 ? 7.477 46.590 62.170 1.00 25.62 ? 70 LEU A CB 1 ATOM 70 C CG . LEU A 1 24 ? 8.102 47.885 62.713 1.00 28.13 ? 70 LEU A CG 1 ATOM 71 C CD1 . LEU A 1 24 ? 7.579 49.128 62.005 1.00 30.61 ? 70 LEU A CD1 1 ATOM 72 C CD2 . LEU A 1 24 ? 7.849 47.988 64.205 1.00 33.78 ? 70 LEU A CD2 1 ATOM 73 N N . LEU A 1 25 ? 8.691 43.786 61.317 1.00 26.24 ? 71 LEU A N 1 ATOM 74 C CA . LEU A 1 25 ? 8.415 42.369 61.418 1.00 28.85 ? 71 LEU A CA 1 ATOM 75 C C . LEU A 1 25 ? 7.912 42.073 62.838 1.00 31.51 ? 71 LEU A C 1 ATOM 76 O O . LEU A 1 25 ? 8.676 42.186 63.803 1.00 30.66 ? 71 LEU A O 1 ATOM 77 C CB . LEU A 1 25 ? 9.679 41.563 61.150 1.00 28.39 ? 71 LEU A CB 1 ATOM 78 C CG . LEU A 1 25 ? 9.498 40.054 61.364 1.00 29.91 ? 71 LEU A CG 1 ATOM 79 C CD1 . LEU A 1 25 ? 8.352 39.540 60.509 1.00 29.21 ? 71 LEU A CD1 1 ATOM 80 C CD2 . LEU A 1 25 ? 10.783 39.284 61.098 1.00 32.11 ? 71 LEU A CD2 1 ATOM 81 N N . ASP A 1 26 ? 6.631 41.718 62.938 1.00 34.62 ? 72 ASP A N 1 ATOM 82 C CA . ASP A 1 26 ? 6.027 41.314 64.206 1.00 38.91 ? 72 ASP A CA 1 ATOM 83 C C . ASP A 1 26 ? 6.480 39.894 64.498 1.00 40.19 ? 72 ASP A C 1 ATOM 84 O O . ASP A 1 26 ? 6.003 38.947 63.880 1.00 41.10 ? 72 ASP A O 1 ATOM 85 C CB . ASP A 1 26 ? 4.501 41.373 64.100 1.00 39.26 ? 72 ASP A CB 1 ATOM 86 C CG . ASP A 1 26 ? 3.813 41.134 65.435 1.00 44.10 ? 72 ASP A CG 1 ATOM 87 O OD1 . ASP A 1 26 ? 3.692 42.106 66.217 1.00 49.09 ? 72 ASP A OD1 1 ATOM 88 O OD2 . ASP A 1 26 ? 3.391 39.982 65.696 1.00 48.13 ? 72 ASP A OD2 1 ATOM 89 N N . ALA A 1 27 ? 7.443 39.752 65.398 1.00 42.84 ? 73 ALA A N 1 ATOM 90 C CA . ALA A 1 27 ? 8.006 38.434 65.698 1.00 45.43 ? 73 ALA A CA 1 ATOM 91 C C . ALA A 1 27 ? 6.925 37.498 66.254 1.00 46.91 ? 73 ALA A C 1 ATOM 92 O O . ALA A 1 27 ? 6.944 36.289 65.997 1.00 48.12 ? 73 ALA A O 1 ATOM 93 C CB . ALA A 1 27 ? 9.180 38.547 66.671 1.00 45.56 ? 73 ALA A CB 1 ATOM 94 N N . ALA A 1 28 ? 5.978 38.066 66.999 1.00 48.28 ? 74 ALA A N 1 ATOM 95 C CA . ALA A 1 28 ? 4.835 37.308 67.485 1.00 48.95 ? 74 ALA A CA 1 ATOM 96 C C . ALA A 1 28 ? 4.205 36.523 66.331 1.00 49.36 ? 74 ALA A C 1 ATOM 97 O O . ALA A 1 28 ? 4.290 35.287 66.283 1.00 50.25 ? 74 ALA A O 1 ATOM 98 C CB . ALA A 1 28 ? 3.807 38.247 68.121 1.00 49.20 ? 74 ALA A CB 1 ATOM 99 N N . SER A 1 29 ? 3.606 37.246 65.387 1.00 48.76 ? 75 SER A N 1 ATOM 100 C CA . SER A 1 29 ? 2.865 36.627 64.290 1.00 47.89 ? 75 SER A CA 1 ATOM 101 C C . SER A 1 29 ? 3.725 36.264 63.088 1.00 46.99 ? 75 SER A C 1 ATOM 102 O O . SER A 1 29 ? 3.308 35.470 62.242 1.00 47.01 ? 75 SER A O 1 ATOM 103 C CB . SER A 1 29 ? 1.739 37.551 63.833 1.00 48.26 ? 75 SER A CB 1 ATOM 104 O OG . SER A 1 29 ? 2.230 38.849 63.551 1.00 49.04 ? 75 SER A OG 1 ATOM 105 N N . GLY A 1 30 ? 4.914 36.861 62.994 1.00 45.75 ? 76 GLY A N 1 ATOM 106 C CA . GLY A 1 30 ? 5.757 36.693 61.801 1.00 43.47 ? 76 GLY A CA 1 ATOM 107 C C . GLY A 1 30 ? 5.174 37.455 60.625 1.00 41.60 ? 76 GLY A C 1 ATOM 108 O O . GLY A 1 30 ? 5.468 37.157 59.465 1.00 41.82 ? 76 GLY A O 1 ATOM 109 N N . GLN A 1 31 ? 4.332 38.438 60.928 1.00 39.64 ? 77 GLN A N 1 ATOM 110 C CA . GLN A 1 31 ? 3.672 39.220 59.905 1.00 37.87 ? 77 GLN A CA 1 ATOM 111 C C . GLN A 1 31 ? 4.465 40.503 59.706 1.00 35.54 ? 77 GLN A C 1 ATOM 112 O O . GLN A 1 31 ? 4.946 41.090 60.678 1.00 35.01 ? 77 GLN A O 1 ATOM 113 C CB . GLN A 1 31 ? 2.256 39.600 60.343 1.00 38.83 ? 77 GLN A CB 1 ATOM 114 C CG . GLN A 1 31 ? 1.295 38.417 60.556 1.00 42.95 ? 77 GLN A CG 1 ATOM 115 C CD . GLN A 1 31 ? 1.179 37.547 59.323 1.00 47.20 ? 77 GLN A CD 1 ATOM 116 O OE1 . GLN A 1 31 ? 0.813 38.028 58.243 1.00 50.81 ? 77 GLN A OE1 1 ATOM 117 N NE2 . GLN A 1 31 ? 1.491 36.260 59.470 1.00 48.52 ? 77 GLN A NE2 1 ATOM 118 N N . LEU A 1 32 ? 4.570 40.945 58.458 1.00 32.96 ? 78 LEU A N 1 ATOM 119 C CA . LEU A 1 32 ? 5.173 42.235 58.162 1.00 30.88 ? 78 LEU A CA 1 ATOM 120 C C . LEU A 1 32 ? 4.080 43.286 58.198 1.00 30.71 ? 78 LEU A C 1 ATOM 121 O O . LEU A 1 32 ? 2.972 43.040 57.717 1.00 31.52 ? 78 LEU A O 1 ATOM 122 C CB . LEU A 1 32 ? 5.827 42.208 56.781 1.00 30.51 ? 78 LEU A CB 1 ATOM 123 C CG . LEU A 1 32 ? 7.090 41.353 56.675 1.00 28.10 ? 78 LEU A CG 1 ATOM 124 C CD1 . LEU A 1 32 ? 7.404 41.107 55.181 1.00 27.04 ? 78 LEU A CD1 1 ATOM 125 C CD2 . LEU A 1 32 ? 8.256 42.029 57.380 1.00 25.50 ? 78 LEU A CD2 1 ATOM 126 N N . ARG A 1 33 ? 4.367 44.451 58.760 1.00 29.53 ? 79 ARG A N 1 ATOM 127 C CA . ARG A 1 33 ? 3.366 45.496 58.801 1.00 29.58 ? 79 ARG A CA 1 ATOM 128 C C . ARG A 1 33 ? 3.992 46.875 58.708 1.00 27.70 ? 79 ARG A C 1 ATOM 129 O O . ARG A 1 33 ? 5.034 47.161 59.322 1.00 26.65 ? 79 ARG A O 1 ATOM 130 C CB . ARG A 1 33 ? 2.487 45.369 60.055 1.00 31.21 ? 79 ARG A CB 1 ATOM 131 C CG . ARG A 1 33 ? 3.193 45.695 61.328 1.00 35.02 ? 79 ARG A CG 1 ATOM 132 C CD . ARG A 1 33 ? 2.227 45.652 62.539 1.00 41.07 ? 79 ARG A CD 1 ATOM 133 N NE . ARG A 1 33 ? 2.802 46.392 63.662 1.00 45.44 ? 79 ARG A NE 1 ATOM 134 C CZ . ARG A 1 33 ? 3.870 45.994 64.356 1.00 48.32 ? 79 ARG A CZ 1 ATOM 135 N NH1 . ARG A 1 33 ? 4.499 44.848 64.054 1.00 49.72 ? 79 ARG A NH1 1 ATOM 136 N NH2 . ARG A 1 33 ? 4.322 46.746 65.356 1.00 49.82 ? 79 ARG A NH2 1 ATOM 137 N N . LEU A 1 34 ? 3.343 47.715 57.917 1.00 27.50 ? 80 LEU A N 1 ATOM 138 C CA . LEU A 1 34 ? 3.775 49.075 57.702 1.00 27.41 ? 80 LEU A CA 1 ATOM 139 C C . LEU A 1 34 ? 3.286 49.944 58.832 1.00 28.33 ? 80 LEU A C 1 ATOM 140 O O . LEU A 1 34 ? 2.136 49.786 59.271 1.00 28.21 ? 80 LEU A O 1 ATOM 141 C CB . LEU A 1 34 ? 3.168 49.599 56.407 1.00 27.97 ? 80 LEU A CB 1 ATOM 142 C CG . LEU A 1 34 ? 3.881 49.189 55.126 1.00 28.54 ? 80 LEU A CG 1 ATOM 143 C CD1 . LEU A 1 34 ? 3.018 49.544 53.951 1.00 28.37 ? 80 LEU A CD1 1 ATOM 144 C CD2 . LEU A 1 34 ? 5.226 49.935 55.064 1.00 24.77 ? 80 LEU A CD2 1 ATOM 145 N N . GLU A 1 35 ? 4.137 50.857 59.286 1.00 27.70 ? 81 GLU A N 1 ATOM 146 C CA . GLU A 1 35 ? 3.767 51.859 60.280 1.00 28.79 ? 81 GLU A CA 1 ATOM 147 C C . GLU A 1 35 ? 4.196 53.234 59.790 1.00 28.45 ? 81 GLU A C 1 ATOM 148 O O . GLU A 1 35 ? 5.229 53.375 59.109 1.00 26.80 ? 81 GLU A O 1 ATOM 149 C CB . GLU A 1 35 ? 4.444 51.552 61.621 1.00 29.44 ? 81 GLU A CB 1 ATOM 150 C CG . GLU A 1 35 ? 3.946 50.268 62.282 1.00 34.88 ? 81 GLU A CG 1 ATOM 151 C CD . GLU A 1 35 ? 4.126 50.258 63.805 1.00 43.03 ? 81 GLU A CD 1 ATOM 152 O OE1 . GLU A 1 35 ? 4.976 51.030 64.321 1.00 45.56 ? 81 GLU A OE1 1 ATOM 153 O OE2 . GLU A 1 35 ? 3.408 49.473 64.486 1.00 47.04 ? 81 GLU A OE2 1 ATOM 154 N N . ASP A 1 36 ? 3.418 54.258 60.132 1.00 27.63 ? 82 ASP A N 1 ATOM 155 C CA . ASP A 1 36 ? 3.822 55.619 59.835 1.00 28.82 ? 82 ASP A CA 1 ATOM 156 C C . ASP A 1 36 ? 4.999 56.022 60.699 1.00 27.77 ? 82 ASP A C 1 ATOM 157 O O . ASP A 1 36 ? 5.145 55.551 61.845 1.00 28.22 ? 82 ASP A O 1 ATOM 158 C CB . ASP A 1 36 ? 2.677 56.604 60.085 1.00 29.94 ? 82 ASP A CB 1 ATOM 159 C CG . ASP A 1 36 ? 1.696 56.637 58.964 1.00 36.24 ? 82 ASP A CG 1 ATOM 160 O OD1 . ASP A 1 36 ? 1.837 55.835 58.005 1.00 41.86 ? 82 ASP A OD1 1 ATOM 161 O OD2 . ASP A 1 36 ? 0.757 57.469 59.046 1.00 43.89 ? 82 ASP A OD2 1 ATOM 162 N N . GLY A 1 37 ? 5.830 56.892 60.141 1.00 26.37 ? 83 GLY A N 1 ATOM 163 C CA . GLY A 1 37 ? 6.972 57.441 60.825 1.00 25.92 ? 83 GLY A CA 1 ATOM 164 C C . GLY A 1 37 ? 8.205 56.557 60.861 1.00 25.70 ? 83 GLY A C 1 ATOM 165 O O . GLY A 1 37 ? 8.261 55.485 60.262 1.00 25.21 ? 83 GLY A O 1 ATOM 166 N N . PHE A 1 38 ? 9.182 57.015 61.622 1.00 25.60 ? 84 PHE A N 1 ATOM 167 C CA . PHE A 1 38 ? 10.494 56.440 61.645 1.00 26.38 ? 84 PHE A CA 1 ATOM 168 C C . PHE A 1 38 ? 10.616 55.470 62.808 1.00 26.62 ? 84 PHE A C 1 ATOM 169 O O . PHE A 1 38 ? 10.431 55.852 63.962 1.00 25.95 ? 84 PHE A O 1 ATOM 170 C CB . PHE A 1 38 ? 11.476 57.601 61.798 1.00 27.10 ? 84 PHE A CB 1 ATOM 171 C CG . PHE A 1 38 ? 12.860 57.190 62.174 1.00 29.94 ? 84 PHE A CG 1 ATOM 172 C CD1 . PHE A 1 38 ? 13.606 56.372 61.336 1.00 32.09 ? 84 PHE A CD1 1 ATOM 173 C CD2 . PHE A 1 38 ? 13.451 57.673 63.345 1.00 31.30 ? 84 PHE A CD2 1 ATOM 174 C CE1 . PHE A 1 38 ? 14.881 56.003 61.669 1.00 33.05 ? 84 PHE A CE1 1 ATOM 175 C CE2 . PHE A 1 38 ? 14.740 57.311 63.682 1.00 32.47 ? 84 PHE A CE2 1 ATOM 176 C CZ . PHE A 1 38 ? 15.459 56.480 62.852 1.00 33.59 ? 84 PHE A CZ 1 ATOM 177 N N . HIS A 1 39 ? 10.915 54.211 62.515 1.00 26.36 ? 85 HIS A N 1 ATOM 178 C CA . HIS A 1 39 ? 11.099 53.216 63.547 1.00 26.97 ? 85 HIS A CA 1 ATOM 179 C C . HIS A 1 39 ? 12.392 52.490 63.209 1.00 28.20 ? 85 HIS A C 1 ATOM 180 O O . HIS A 1 39 ? 12.379 51.536 62.452 1.00 27.79 ? 85 HIS A O 1 ATOM 181 C CB . HIS A 1 39 ? 9.905 52.247 63.557 1.00 27.61 ? 85 HIS A CB 1 ATOM 182 C CG . HIS A 1 39 ? 8.597 52.933 63.792 1.00 29.20 ? 85 HIS A CG 1 ATOM 183 N ND1 . HIS A 1 39 ? 8.080 53.128 65.057 1.00 31.29 ? 85 HIS A ND1 1 ATOM 184 C CD2 . HIS A 1 39 ? 7.747 53.553 62.935 1.00 28.67 ? 85 HIS A CD2 1 ATOM 185 C CE1 . HIS A 1 39 ? 6.947 53.805 64.964 1.00 32.51 ? 85 HIS A CE1 1 ATOM 186 N NE2 . HIS A 1 39 ? 6.725 54.081 63.688 1.00 31.95 ? 85 HIS A NE2 1 ATOM 187 N N . PRO A 1 40 ? 13.529 52.974 63.722 1.00 29.48 ? 86 PRO A N 1 ATOM 188 C CA . PRO A 1 40 ? 14.827 52.369 63.365 1.00 29.70 ? 86 PRO A CA 1 ATOM 189 C C . PRO A 1 40 ? 14.980 50.884 63.788 1.00 29.38 ? 86 PRO A C 1 ATOM 190 O O . PRO A 1 40 ? 15.934 50.236 63.376 1.00 29.15 ? 86 PRO A O 1 ATOM 191 C CB . PRO A 1 40 ? 15.852 53.263 64.090 1.00 30.87 ? 86 PRO A CB 1 ATOM 192 C CG . PRO A 1 40 ? 15.077 53.884 65.237 1.00 30.80 ? 86 PRO A CG 1 ATOM 193 C CD . PRO A 1 40 ? 13.685 54.112 64.659 1.00 30.10 ? 86 PRO A CD 1 ATOM 194 N N . ASP A 1 41 ? 14.035 50.349 64.561 1.00 28.61 ? 87 ASP A N 1 ATOM 195 C CA . ASP A 1 41 ? 13.940 48.913 64.805 1.00 28.48 ? 87 ASP A CA 1 ATOM 196 C C . ASP A 1 41 ? 13.367 48.085 63.611 1.00 26.66 ? 87 ASP A C 1 ATOM 197 O O . ASP A 1 41 ? 13.446 46.861 63.576 1.00 26.51 ? 87 ASP A O 1 ATOM 198 C CB . ASP A 1 41 ? 13.071 48.662 66.050 1.00 30.66 ? 87 ASP A CB 1 ATOM 199 C CG . ASP A 1 41 ? 11.720 49.389 65.995 1.00 33.98 ? 87 ASP A CG 1 ATOM 200 O OD1 . ASP A 1 41 ? 11.691 50.637 66.018 1.00 38.38 ? 87 ASP A OD1 1 ATOM 201 O OD2 . ASP A 1 41 ? 10.671 48.704 65.941 1.00 41.38 ? 87 ASP A OD2 1 ATOM 202 N N . ALA A 1 42 ? 12.751 48.769 62.667 1.00 23.76 ? 88 ALA A N 1 ATOM 203 C CA . ALA A 1 42 ? 12.049 48.119 61.567 1.00 21.42 ? 88 ALA A CA 1 ATOM 204 C C . ALA A 1 42 ? 13.064 47.462 60.616 1.00 19.89 ? 88 ALA A C 1 ATOM 205 O O . ALA A 1 42 ? 14.275 47.709 60.718 1.00 18.95 ? 88 ALA A O 1 ATOM 206 C CB . ALA A 1 42 ? 11.255 49.160 60.826 1.00 21.81 ? 88 ALA A CB 1 ATOM 207 N N . VAL A 1 43 ? 12.556 46.638 59.693 1.00 18.32 ? 89 VAL A N 1 ATOM 208 C CA . VAL A 1 43 ? 13.426 46.018 58.682 1.00 17.57 ? 89 VAL A CA 1 ATOM 209 C C . VAL A 1 43 ? 13.937 47.076 57.701 1.00 16.39 ? 89 VAL A C 1 ATOM 210 O O . VAL A 1 43 ? 15.078 46.993 57.201 1.00 16.68 ? 89 VAL A O 1 ATOM 211 C CB . VAL A 1 43 ? 12.640 44.951 57.882 1.00 16.29 ? 89 VAL A CB 1 ATOM 212 C CG1 . VAL A 1 43 ? 13.561 44.261 56.889 1.00 16.31 ? 89 VAL A CG1 1 ATOM 213 C CG2 . VAL A 1 43 ? 12.009 43.889 58.820 1.00 17.81 ? 89 VAL A CG2 1 ATOM 214 N N . ALA A 1 44 ? 13.076 48.035 57.398 1.00 16.39 ? 90 ALA A N 1 ATOM 215 C CA . ALA A 1 44 ? 13.404 49.136 56.471 1.00 16.14 ? 90 ALA A CA 1 ATOM 216 C C . ALA A 1 44 ? 12.525 50.350 56.742 1.00 16.86 ? 90 ALA A C 1 ATOM 217 O O . ALA A 1 44 ? 11.431 50.224 57.315 1.00 16.37 ? 90 ALA A O 1 ATOM 218 C CB . ALA A 1 44 ? 13.236 48.660 54.959 1.00 16.79 ? 90 ALA A CB 1 ATOM 219 N N . TRP A 1 45 ? 12.996 51.522 56.325 1.00 17.54 ? 91 TRP A N 1 ATOM 220 C CA . TRP A 1 45 ? 12.198 52.723 56.337 1.00 18.60 ? 91 TRP A CA 1 ATOM 221 C C . TRP A 1 45 ? 12.578 53.616 55.168 1.00 17.88 ? 91 TRP A C 1 ATOM 222 O O . TRP A 1 45 ? 13.671 53.522 54.611 1.00 16.75 ? 91 TRP A O 1 ATOM 223 C CB . TRP A 1 45 ? 12.334 53.505 57.671 1.00 21.51 ? 91 TRP A CB 1 ATOM 224 C CG . TRP A 1 45 ? 13.733 53.772 58.064 1.00 23.36 ? 91 TRP A CG 1 ATOM 225 C CD1 . TRP A 1 45 ? 14.460 54.910 57.847 1.00 29.50 ? 91 TRP A CD1 1 ATOM 226 C CD2 . TRP A 1 45 ? 14.598 52.862 58.763 1.00 27.47 ? 91 TRP A CD2 1 ATOM 227 N NE1 . TRP A 1 45 ? 15.740 54.759 58.393 1.00 28.18 ? 91 TRP A NE1 1 ATOM 228 C CE2 . TRP A 1 45 ? 15.840 53.510 58.944 1.00 28.99 ? 91 TRP A CE2 1 ATOM 229 C CE3 . TRP A 1 45 ? 14.428 51.547 59.263 1.00 31.27 ? 91 TRP A CE3 1 ATOM 230 C CZ2 . TRP A 1 45 ? 16.940 52.875 59.591 1.00 31.22 ? 91 TRP A CZ2 1 ATOM 231 C CZ3 . TRP A 1 45 ? 15.499 50.916 59.930 1.00 30.37 ? 91 TRP A CZ3 1 ATOM 232 C CH2 . TRP A 1 45 ? 16.747 51.586 60.080 1.00 31.53 ? 91 TRP A CH2 1 ATOM 233 N N . ALA A 1 46 ? 11.665 54.496 54.814 1.00 17.73 ? 92 ALA A N 1 ATOM 234 C CA . ALA A 1 46 ? 11.902 55.394 53.709 1.00 17.36 ? 92 ALA A CA 1 ATOM 235 C C . ALA A 1 46 ? 11.161 56.679 53.973 1.00 18.55 ? 92 ALA A C 1 ATOM 236 O O . ALA A 1 46 ? 10.097 56.682 54.633 1.00 18.71 ? 92 ALA A O 1 ATOM 237 C CB . ALA A 1 46 ? 11.374 54.761 52.414 1.00 17.89 ? 92 ALA A CB 1 ATOM 238 N N . ASN A 1 47 ? 11.687 57.758 53.420 1.00 19.02 ? 93 ASN A N 1 ATOM 239 C CA . ASN A 1 47 ? 10.898 58.973 53.359 1.00 20.78 ? 93 ASN A CA 1 ATOM 240 C C . ASN A 1 47 ? 11.069 59.700 52.060 1.00 19.86 ? 93 ASN A C 1 ATOM 241 O O . ASN A 1 47 ? 12.171 59.746 51.503 1.00 20.06 ? 93 ASN A O 1 ATOM 242 C CB . ASN A 1 47 ? 11.086 59.884 54.570 1.00 23.02 ? 93 ASN A CB 1 ATOM 243 C CG . ASN A 1 47 ? 12.450 60.344 54.749 1.00 27.46 ? 93 ASN A CG 1 ATOM 244 O OD1 . ASN A 1 47 ? 13.413 59.663 54.398 1.00 35.77 ? 93 ASN A OD1 1 ATOM 245 N ND2 . ASN A 1 47 ? 12.583 61.523 55.364 1.00 31.62 ? 93 ASN A ND2 1 ATOM 246 N N . LEU A 1 48 ? 9.959 60.257 51.594 1.00 19.89 ? 94 LEU A N 1 ATOM 247 C CA . LEU A 1 48 ? 9.918 60.911 50.309 1.00 19.34 ? 94 LEU A CA 1 ATOM 248 C C . LEU A 1 48 ? 9.465 62.330 50.551 1.00 21.57 ? 94 LEU A C 1 ATOM 249 O O . LEU A 1 48 ? 8.470 62.537 51.284 1.00 21.92 ? 94 LEU A O 1 ATOM 250 C CB . LEU A 1 48 ? 8.915 60.208 49.415 1.00 19.27 ? 94 LEU A CB 1 ATOM 251 C CG . LEU A 1 48 ? 8.963 60.890 48.036 1.00 23.68 ? 94 LEU A CG 1 ATOM 252 C CD1 . LEU A 1 48 ? 9.431 59.982 46.936 1.00 26.11 ? 94 LEU A CD1 1 ATOM 253 C CD2 . LEU A 1 48 ? 7.658 61.616 47.728 1.00 27.38 ? 94 LEU A CD2 1 ATOM 254 N N . THR A 1 49 ? 10.208 63.275 49.982 1.00 21.62 ? 95 THR A N 1 ATOM 255 C CA . THR A 1 49 ? 9.816 64.683 49.942 1.00 24.42 ? 95 THR A CA 1 ATOM 256 C C . THR A 1 49 ? 9.572 65.043 48.494 1.00 23.97 ? 95 THR A C 1 ATOM 257 O O . THR A 1 49 ? 10.462 64.914 47.642 1.00 23.06 ? 95 THR A O 1 ATOM 258 C CB . THR A 1 49 ? 10.917 65.557 50.484 1.00 25.37 ? 95 THR A CB 1 ATOM 259 O OG1 . THR A 1 49 ? 11.229 65.134 51.820 1.00 29.96 ? 95 THR A OG1 1 ATOM 260 C CG2 . THR A 1 49 ? 10.505 67.027 50.494 1.00 28.47 ? 95 THR A CG2 1 ATOM 261 N N . ASN A 1 50 ? 8.342 65.445 48.203 1.00 24.12 ? 96 ASN A N 1 ATOM 262 C CA . ASN A 1 50 ? 7.980 65.797 46.839 1.00 23.30 ? 96 ASN A CA 1 ATOM 263 C C . ASN A 1 50 ? 8.156 67.312 46.668 1.00 23.90 ? 96 ASN A C 1 ATOM 264 O O . ASN A 1 50 ? 7.318 68.095 47.162 1.00 24.82 ? 96 ASN A O 1 ATOM 265 C CB . ASN A 1 50 ? 6.531 65.350 46.545 1.00 23.96 ? 96 ASN A CB 1 ATOM 266 C CG . ASN A 1 50 ? 6.117 65.606 45.111 1.00 25.48 ? 96 ASN A CG 1 ATOM 267 O OD1 . ASN A 1 50 ? 6.657 66.488 44.471 1.00 25.74 ? 96 ASN A OD1 1 ATOM 268 N ND2 . ASN A 1 50 ? 5.165 64.812 44.587 1.00 26.88 ? 96 ASN A ND2 1 ATOM 269 N N . ALA A 1 51 ? 9.232 67.726 45.997 1.00 21.21 ? 97 ALA A N 1 ATOM 270 C CA . ALA A 1 51 ? 9.482 69.123 45.696 1.00 21.09 ? 97 ALA A CA 1 ATOM 271 C C . ALA A 1 51 ? 9.365 69.366 44.209 1.00 19.88 ? 97 ALA A C 1 ATOM 272 O O . ALA A 1 51 ? 10.018 70.255 43.673 1.00 19.70 ? 97 ALA A O 1 ATOM 273 C CB . ALA A 1 51 ? 10.883 69.515 46.188 1.00 21.29 ? 97 ALA A CB 1 ATOM 274 N N . ILE A 1 52 ? 8.545 68.563 43.533 1.00 19.38 ? 98 ILE A N 1 ATOM 275 C CA . ILE A 1 52 ? 8.458 68.639 42.077 1.00 19.50 ? 98 ILE A CA 1 ATOM 276 C C . ILE A 1 52 ? 7.982 70.018 41.632 1.00 20.49 ? 98 ILE A C 1 ATOM 277 O O . ILE A 1 52 ? 8.534 70.597 40.708 1.00 19.24 ? 98 ILE A O 1 ATOM 278 C CB . ILE A 1 52 ? 7.619 67.495 41.496 1.00 20.41 ? 98 ILE A CB 1 ATOM 279 C CG1 . ILE A 1 52 ? 8.413 66.170 41.650 1.00 21.08 ? 98 ILE A CG1 1 ATOM 280 C CG2 . ILE A 1 52 ? 7.304 67.749 40.020 1.00 19.10 ? 98 ILE A CG2 1 ATOM 281 C CD1 . ILE A 1 52 ? 7.649 64.918 41.178 1.00 22.26 ? 98 ILE A CD1 1 ATOM 282 N N . ARG A 1 53 ? 6.958 70.561 42.305 1.00 20.52 ? 99 ARG A N 1 ATOM 283 C CA . ARG A 1 53 ? 6.467 71.891 41.923 1.00 23.24 ? 99 ARG A CA 1 ATOM 284 C C . ARG A 1 53 ? 7.542 72.990 41.990 1.00 22.24 ? 99 ARG A C 1 ATOM 285 O O . ARG A 1 53 ? 7.534 73.909 41.166 1.00 22.81 ? 99 ARG A O 1 ATOM 286 C CB . ARG A 1 53 ? 5.275 72.288 42.819 1.00 23.29 ? 99 ARG A CB 1 ATOM 287 C CG . ARG A 1 53 ? 4.674 73.620 42.442 1.00 30.88 ? 99 ARG A CG 1 ATOM 288 C CD . ARG A 1 53 ? 3.638 74.045 43.481 1.00 39.74 ? 99 ARG A CD 1 ATOM 289 N NE . ARG A 1 53 ? 3.289 75.448 43.279 1.00 47.95 ? 99 ARG A NE 1 ATOM 290 C CZ . ARG A 1 53 ? 3.812 76.459 43.975 1.00 52.38 ? 99 ARG A CZ 1 ATOM 291 N NH1 . ARG A 1 53 ? 4.705 76.223 44.937 1.00 54.28 ? 99 ARG A NH1 1 ATOM 292 N NH2 . ARG A 1 53 ? 3.438 77.709 43.716 1.00 54.44 ? 99 ARG A NH2 1 ATOM 293 N N . GLU A 1 54 ? 8.453 72.887 42.959 1.00 22.32 ? 100 GLU A N 1 ATOM 294 C CA . GLU A 1 54 ? 9.470 73.904 43.223 1.00 23.17 ? 100 GLU A CA 1 ATOM 295 C C . GLU A 1 54 ? 10.801 73.709 42.482 1.00 21.77 ? 100 GLU A C 1 ATOM 296 O O . GLU A 1 54 ? 11.499 74.682 42.149 1.00 20.89 ? 100 GLU A O 1 ATOM 297 C CB . GLU A 1 54 ? 9.757 73.953 44.722 1.00 25.06 ? 100 GLU A CB 1 ATOM 298 C CG . GLU A 1 54 ? 8.548 74.354 45.598 1.00 29.52 ? 100 GLU A CG 1 ATOM 299 C CD . GLU A 1 54 ? 7.467 73.273 45.778 1.00 36.78 ? 100 GLU A CD 1 ATOM 300 O OE1 . GLU A 1 54 ? 7.745 72.042 45.685 1.00 35.04 ? 100 GLU A OE1 1 ATOM 301 O OE2 . GLU A 1 54 ? 6.302 73.676 46.047 1.00 41.35 ? 100 GLU A OE2 1 ATOM 302 N N . THR A 1 55 ? 11.166 72.446 42.230 1.00 20.41 ? 101 THR A N 1 ATOM 303 C CA . THR A 1 55 ? 12.520 72.136 41.744 1.00 20.64 ? 101 THR A CA 1 ATOM 304 C C . THR A 1 55 ? 12.529 71.154 40.587 1.00 19.75 ? 101 THR A C 1 ATOM 305 O O . THR A 1 55 ? 13.582 70.906 39.995 1.00 19.93 ? 101 THR A O 1 ATOM 306 C CB . THR A 1 55 ? 13.400 71.472 42.840 1.00 20.99 ? 101 THR A CB 1 ATOM 307 O OG1 . THR A 1 55 ? 12.878 70.161 43.177 1.00 19.90 ? 101 THR A OG1 1 ATOM 308 C CG2 . THR A 1 55 ? 13.508 72.330 44.103 1.00 23.81 ? 101 THR A CG2 1 ATOM 309 N N . GLY A 1 56 ? 11.378 70.561 40.305 1.00 17.87 ? 102 GLY A N 1 ATOM 310 C CA . GLY A 1 56 ? 11.316 69.513 39.281 1.00 17.75 ? 102 GLY A CA 1 ATOM 311 C C . GLY A 1 56 ? 11.819 68.158 39.771 1.00 16.91 ? 102 GLY A C 1 ATOM 312 O O . GLY A 1 56 ? 11.854 67.216 38.974 1.00 16.51 ? 102 GLY A O 1 ATOM 313 N N . TRP A 1 57 ? 12.151 68.031 41.058 1.00 16.02 ? 103 TRP A N 1 ATOM 314 C CA . TRP A 1 57 ? 12.560 66.725 41.645 1.00 16.78 ? 103 TRP A CA 1 ATOM 315 C C . TRP A 1 57 ? 11.758 66.349 42.897 1.00 17.47 ? 103 TRP A C 1 ATOM 316 O O . TRP A 1 57 ? 11.366 67.228 43.705 1.00 17.30 ? 103 TRP A O 1 ATOM 317 C CB . TRP A 1 57 ? 14.041 66.783 42.102 1.00 16.20 ? 103 TRP A CB 1 ATOM 318 C CG . TRP A 1 57 ? 15.054 67.112 41.050 1.00 16.20 ? 103 TRP A CG 1 ATOM 319 C CD1 . TRP A 1 57 ? 15.654 68.320 40.838 1.00 15.83 ? 103 TRP A CD1 1 ATOM 320 C CD2 . TRP A 1 57 ? 15.630 66.197 40.099 1.00 16.06 ? 103 TRP A CD2 1 ATOM 321 N NE1 . TRP A 1 57 ? 16.571 68.222 39.811 1.00 17.11 ? 103 TRP A NE1 1 ATOM 322 C CE2 . TRP A 1 57 ? 16.566 66.935 39.325 1.00 15.07 ? 103 TRP A CE2 1 ATOM 323 C CE3 . TRP A 1 57 ? 15.423 64.831 39.810 1.00 16.19 ? 103 TRP A CE3 1 ATOM 324 C CZ2 . TRP A 1 57 ? 17.279 66.369 38.258 1.00 16.56 ? 103 TRP A CZ2 1 ATOM 325 C CZ3 . TRP A 1 57 ? 16.161 64.250 38.757 1.00 16.75 ? 103 TRP A CZ3 1 ATOM 326 C CH2 . TRP A 1 57 ? 17.078 65.023 37.991 1.00 16.63 ? 103 TRP A CH2 1 ATOM 327 N N . ALA A 1 58 ? 11.539 65.054 43.096 1.00 16.06 ? 104 ALA A N 1 ATOM 328 C CA . ALA A 1 58 ? 11.258 64.539 44.430 1.00 15.84 ? 104 ALA A CA 1 ATOM 329 C C . ALA A 1 58 ? 12.521 63.841 44.946 1.00 17.22 ? 104 ALA A C 1 ATOM 330 O O . ALA A 1 58 ? 13.447 63.563 44.162 1.00 16.42 ? 104 ALA A O 1 ATOM 331 C CB . ALA A 1 58 ? 10.077 63.576 44.412 1.00 15.89 ? 104 ALA A CB 1 ATOM 332 N N . TYR A 1 59 ? 12.574 63.596 46.253 1.00 16.82 ? 105 TYR A N 1 ATOM 333 C CA A TYR A 1 59 ? 13.766 63.021 46.881 0.50 17.65 ? 105 TYR A CA 1 ATOM 334 C CA B TYR A 1 59 ? 13.765 63.005 46.874 0.50 18.04 ? 105 TYR A CA 1 ATOM 335 C C . TYR A 1 59 ? 13.343 61.876 47.783 1.00 18.17 ? 105 TYR A C 1 ATOM 336 O O . TYR A 1 59 ? 12.425 62.027 48.617 1.00 18.45 ? 105 TYR A O 1 ATOM 337 C CB A TYR A 1 59 ? 14.531 64.071 47.703 0.50 18.62 ? 105 TYR A CB 1 ATOM 338 C CB B TYR A 1 59 ? 14.570 64.027 47.690 0.50 19.36 ? 105 TYR A CB 1 ATOM 339 C CG A TYR A 1 59 ? 14.626 65.417 47.021 0.50 18.72 ? 105 TYR A CG 1 ATOM 340 C CG B TYR A 1 59 ? 15.834 63.454 48.319 0.50 20.97 ? 105 TYR A CG 1 ATOM 341 C CD1 A TYR A 1 59 ? 15.634 65.695 46.112 0.50 19.13 ? 105 TYR A CD1 1 ATOM 342 C CD1 B TYR A 1 59 ? 16.825 62.853 47.535 0.50 24.71 ? 105 TYR A CD1 1 ATOM 343 C CD2 A TYR A 1 59 ? 13.694 66.409 47.287 0.50 21.45 ? 105 TYR A CD2 1 ATOM 344 C CD2 B TYR A 1 59 ? 16.052 63.528 49.696 0.50 23.27 ? 105 TYR A CD2 1 ATOM 345 C CE1 A TYR A 1 59 ? 15.700 66.933 45.485 0.50 21.48 ? 105 TYR A CE1 1 ATOM 346 C CE1 B TYR A 1 59 ? 17.974 62.330 48.106 0.50 24.11 ? 105 TYR A CE1 1 ATOM 347 C CE2 A TYR A 1 59 ? 13.756 67.624 46.665 0.50 20.83 ? 105 TYR A CE2 1 ATOM 348 C CE2 B TYR A 1 59 ? 17.206 63.013 50.272 0.50 24.15 ? 105 TYR A CE2 1 ATOM 349 C CZ A TYR A 1 59 ? 14.748 67.888 45.782 0.50 22.10 ? 105 TYR A CZ 1 ATOM 350 C CZ B TYR A 1 59 ? 18.160 62.426 49.479 0.50 25.81 ? 105 TYR A CZ 1 ATOM 351 O OH A TYR A 1 59 ? 14.763 69.131 45.194 0.50 25.55 ? 105 TYR A OH 1 ATOM 352 O OH B TYR A 1 59 ? 19.307 61.920 50.056 0.50 26.94 ? 105 TYR A OH 1 ATOM 353 N N . LEU A 1 60 ? 14.012 60.739 47.634 1.00 16.88 ? 106 LEU A N 1 ATOM 354 C CA . LEU A 1 60 ? 13.664 59.563 48.431 1.00 16.90 ? 106 LEU A CA 1 ATOM 355 C C . LEU A 1 60 ? 14.901 59.161 49.200 1.00 17.50 ? 106 LEU A C 1 ATOM 356 O O . LEU A 1 60 ? 16.001 59.066 48.621 1.00 16.43 ? 106 LEU A O 1 ATOM 357 C CB . LEU A 1 60 ? 13.228 58.394 47.511 1.00 17.00 ? 106 LEU A CB 1 ATOM 358 C CG . LEU A 1 60 ? 13.139 57.051 48.243 1.00 17.46 ? 106 LEU A CG 1 ATOM 359 C CD1 . LEU A 1 60 ? 11.856 57.010 49.073 1.00 18.98 ? 106 LEU A CD1 1 ATOM 360 C CD2 . LEU A 1 60 ? 13.141 55.873 47.253 1.00 21.14 ? 106 LEU A CD2 1 ATOM 361 N N . ASP A 1 61 ? 14.745 58.922 50.499 1.00 16.28 ? 107 ASP A N 1 ATOM 362 C CA . ASP A 1 61 ? 15.866 58.443 51.302 1.00 18.97 ? 107 ASP A CA 1 ATOM 363 C C . ASP A 1 61 ? 15.397 57.116 51.899 1.00 18.80 ? 107 ASP A C 1 ATOM 364 O O . ASP A 1 61 ? 14.308 57.039 52.459 1.00 20.48 ? 107 ASP A O 1 ATOM 365 C CB . ASP A 1 61 ? 16.184 59.488 52.376 1.00 20.95 ? 107 ASP A CB 1 ATOM 366 C CG . ASP A 1 61 ? 17.478 59.211 53.101 1.00 29.72 ? 107 ASP A CG 1 ATOM 367 O OD1 . ASP A 1 61 ? 17.962 60.137 53.802 1.00 40.21 ? 107 ASP A OD1 1 ATOM 368 O OD2 . ASP A 1 61 ? 18.036 58.106 52.973 1.00 35.53 ? 107 ASP A OD2 1 ATOM 369 N N . LEU A 1 62 ? 16.174 56.051 51.754 1.00 17.36 ? 108 LEU A N 1 ATOM 370 C CA . LEU A 1 62 ? 15.680 54.742 52.154 1.00 17.35 ? 108 LEU A CA 1 ATOM 371 C C . LEU A 1 62 ? 16.800 53.950 52.836 1.00 16.47 ? 108 LEU A C 1 ATOM 372 O O . LEU A 1 62 ? 17.941 53.992 52.360 1.00 16.26 ? 108 LEU A O 1 ATOM 373 C CB . LEU A 1 62 ? 15.198 54.003 50.897 1.00 17.91 ? 108 LEU A CB 1 ATOM 374 C CG . LEU A 1 62 ? 14.671 52.569 51.000 1.00 19.06 ? 108 LEU A CG 1 ATOM 375 C CD1 . LEU A 1 62 ? 13.655 52.332 49.859 1.00 19.84 ? 108 LEU A CD1 1 ATOM 376 C CD2 . LEU A 1 62 ? 15.790 51.510 50.929 1.00 20.54 ? 108 LEU A CD2 1 ATOM 377 N N . SER A 1 63 ? 16.488 53.250 53.940 1.00 16.14 ? 109 SER A N 1 ATOM 378 C CA . SER A 1 63 ? 17.516 52.510 54.668 1.00 17.34 ? 109 SER A CA 1 ATOM 379 C C . SER A 1 63 ? 16.995 51.128 55.003 1.00 16.83 ? 109 SER A C 1 ATOM 380 O O . SER A 1 63 ? 15.798 50.956 55.256 1.00 16.11 ? 109 SER A O 1 ATOM 381 C CB . SER A 1 63 ? 17.855 53.194 56.014 1.00 18.83 ? 109 SER A CB 1 ATOM 382 O OG . SER A 1 63 ? 18.540 54.423 55.815 1.00 24.64 ? 109 SER A OG 1 ATOM 383 N N . THR A 1 64 ? 17.896 50.151 55.043 1.00 16.30 ? 110 THR A N 1 ATOM 384 C CA . THR A 1 64 ? 17.516 48.841 55.582 1.00 17.49 ? 110 THR A CA 1 ATOM 385 C C . THR A 1 64 ? 18.335 48.503 56.827 1.00 17.48 ? 110 THR A C 1 ATOM 386 O O . THR A 1 64 ? 19.397 49.089 57.067 1.00 18.62 ? 110 THR A O 1 ATOM 387 C CB . THR A 1 64 ? 17.605 47.683 54.541 1.00 17.67 ? 110 THR A CB 1 ATOM 388 O OG1 . THR A 1 64 ? 18.955 47.518 54.096 1.00 18.15 ? 110 THR A OG1 1 ATOM 389 C CG2 . THR A 1 64 ? 16.719 47.987 53.325 1.00 16.83 ? 110 THR A CG2 1 ATOM 390 N N . ASN A 1 65 ? 17.842 47.525 57.586 1.00 18.20 ? 111 ASN A N 1 ATOM 391 C CA . ASN A 1 65 ? 18.393 47.176 58.909 1.00 18.32 ? 111 ASN A CA 1 ATOM 392 C C . ASN A 1 65 ? 19.148 45.843 58.842 1.00 17.96 ? 111 ASN A C 1 ATOM 393 O O . ASN A 1 65 ? 18.547 44.791 58.538 1.00 18.47 ? 111 ASN A O 1 ATOM 394 C CB . ASN A 1 65 ? 17.237 47.069 59.894 1.00 18.10 ? 111 ASN A CB 1 ATOM 395 C CG . ASN A 1 65 ? 17.703 46.876 61.327 1.00 20.26 ? 111 ASN A CG 1 ATOM 396 O OD1 . ASN A 1 65 ? 18.869 46.518 61.566 1.00 19.74 ? 111 ASN A OD1 1 ATOM 397 N ND2 . ASN A 1 65 ? 16.790 47.127 62.303 1.00 20.22 ? 111 ASN A ND2 1 ATOM 398 N N . GLY A 1 66 ? 20.454 45.935 59.098 1.00 18.72 ? 112 GLY A N 1 ATOM 399 C CA . GLY A 1 66 ? 21.426 44.817 59.013 1.00 20.23 ? 112 GLY A CA 1 ATOM 400 C C . GLY A 1 66 ? 21.184 43.763 60.082 1.00 20.99 ? 112 GLY A C 1 ATOM 401 O O . GLY A 1 66 ? 21.825 42.708 60.076 1.00 21.38 ? 112 GLY A O 1 ATOM 402 N N . ARG A 1 67 ? 20.272 44.039 61.014 1.00 20.22 ? 113 ARG A N 1 ATOM 403 C CA A ARG A 1 67 ? 19.923 43.003 61.971 0.50 21.04 ? 113 ARG A CA 1 ATOM 404 C CA B ARG A 1 67 ? 19.797 43.065 62.005 0.50 21.20 ? 113 ARG A CA 1 ATOM 405 C C . ARG A 1 67 ? 19.059 41.904 61.352 1.00 20.98 ? 113 ARG A C 1 ATOM 406 O O . ARG A 1 67 ? 18.920 40.830 61.942 1.00 20.97 ? 113 ARG A O 1 ATOM 407 C CB A ARG A 1 67 ? 19.283 43.608 63.216 0.50 21.28 ? 113 ARG A CB 1 ATOM 408 C CB B ARG A 1 67 ? 18.819 43.726 62.984 0.50 21.38 ? 113 ARG A CB 1 ATOM 409 C CG A ARG A 1 67 ? 20.218 44.574 63.938 0.50 24.00 ? 113 ARG A CG 1 ATOM 410 C CG B ARG A 1 67 ? 19.399 44.268 64.286 0.50 25.62 ? 113 ARG A CG 1 ATOM 411 C CD A ARG A 1 67 ? 21.170 43.843 64.869 0.50 30.80 ? 113 ARG A CD 1 ATOM 412 C CD B ARG A 1 67 ? 18.228 44.579 65.244 0.50 28.75 ? 113 ARG A CD 1 ATOM 413 N NE A ARG A 1 67 ? 20.517 43.499 66.130 0.50 36.33 ? 113 ARG A NE 1 ATOM 414 N NE B ARG A 1 67 ? 17.359 43.407 65.409 0.50 31.88 ? 113 ARG A NE 1 ATOM 415 C CZ A ARG A 1 67 ? 20.348 44.352 67.136 0.50 37.74 ? 113 ARG A CZ 1 ATOM 416 C CZ B ARG A 1 67 ? 16.028 43.424 65.431 0.50 32.89 ? 113 ARG A CZ 1 ATOM 417 N NH1 A ARG A 1 67 ? 20.784 45.603 67.032 0.50 39.15 ? 113 ARG A NH1 1 ATOM 418 N NH1 B ARG A 1 67 ? 15.347 44.563 65.296 0.50 35.14 ? 113 ARG A NH1 1 ATOM 419 N NH2 A ARG A 1 67 ? 19.740 43.958 68.243 0.50 39.05 ? 113 ARG A NH2 1 ATOM 420 N NH2 B ARG A 1 67 ? 15.373 42.283 65.575 0.50 33.64 ? 113 ARG A NH2 1 ATOM 421 N N . TYR A 1 68 ? 18.533 42.147 60.143 1.00 19.52 ? 114 TYR A N 1 ATOM 422 C CA . TYR A 1 68 ? 17.723 41.166 59.429 1.00 18.99 ? 114 TYR A CA 1 ATOM 423 C C . TYR A 1 68 ? 18.538 40.636 58.252 1.00 18.05 ? 114 TYR A C 1 ATOM 424 O O . TYR A 1 68 ? 19.489 41.297 57.831 1.00 17.82 ? 114 TYR A O 1 ATOM 425 C CB . TYR A 1 68 ? 16.445 41.814 58.905 1.00 19.46 ? 114 TYR A CB 1 ATOM 426 C CG . TYR A 1 68 ? 15.531 42.238 60.045 1.00 20.10 ? 114 TYR A CG 1 ATOM 427 C CD1 . TYR A 1 68 ? 14.678 41.311 60.641 1.00 21.98 ? 114 TYR A CD1 1 ATOM 428 C CD2 . TYR A 1 68 ? 15.562 43.544 60.538 1.00 22.30 ? 114 TYR A CD2 1 ATOM 429 C CE1 . TYR A 1 68 ? 13.840 41.688 61.703 1.00 24.36 ? 114 TYR A CE1 1 ATOM 430 C CE2 . TYR A 1 68 ? 14.738 43.931 61.594 1.00 23.19 ? 114 TYR A CE2 1 ATOM 431 C CZ . TYR A 1 68 ? 13.879 42.993 62.164 1.00 24.33 ? 114 TYR A CZ 1 ATOM 432 O OH . TYR A 1 68 ? 13.052 43.341 63.227 1.00 25.77 ? 114 TYR A OH 1 ATOM 433 N N . ASN A 1 69 ? 18.177 39.466 57.723 1.00 17.52 ? 115 ASN A N 1 ATOM 434 C CA . ASN A 1 69 ? 19.012 38.928 56.649 1.00 17.41 ? 115 ASN A CA 1 ATOM 435 C C . ASN A 1 69 ? 18.760 39.776 55.401 1.00 16.48 ? 115 ASN A C 1 ATOM 436 O O . ASN A 1 69 ? 17.743 40.504 55.342 1.00 15.09 ? 115 ASN A O 1 ATOM 437 C CB . ASN A 1 69 ? 18.783 37.426 56.384 1.00 17.37 ? 115 ASN A CB 1 ATOM 438 C CG . ASN A 1 69 ? 17.338 37.085 55.979 1.00 20.48 ? 115 ASN A CG 1 ATOM 439 O OD1 . ASN A 1 69 ? 16.783 37.656 55.051 1.00 18.24 ? 115 ASN A OD1 1 ATOM 440 N ND2 . ASN A 1 69 ? 16.751 36.084 56.654 1.00 18.26 ? 115 ASN A ND2 1 ATOM 441 N N . ASP A 1 70 ? 19.661 39.698 54.424 1.00 16.38 ? 116 ASP A N 1 ATOM 442 C CA . ASP A 1 70 ? 19.531 40.628 53.280 1.00 16.81 ? 116 ASP A CA 1 ATOM 443 C C . ASP A 1 70 ? 18.342 40.368 52.346 1.00 15.61 ? 116 ASP A C 1 ATOM 444 O O . ASP A 1 70 ? 17.885 41.278 51.660 1.00 16.10 ? 116 ASP A O 1 ATOM 445 C CB . ASP A 1 70 ? 20.860 40.900 52.526 1.00 17.77 ? 116 ASP A CB 1 ATOM 446 C CG . ASP A 1 70 ? 21.564 39.658 52.016 1.00 19.98 ? 116 ASP A CG 1 ATOM 447 O OD1 . ASP A 1 70 ? 21.052 38.543 52.154 1.00 21.19 ? 116 ASP A OD1 1 ATOM 448 O OD2 . ASP A 1 70 ? 22.686 39.806 51.432 1.00 22.55 ? 116 ASP A OD2 1 ATOM 449 N N . SER A 1 71 ? 17.847 39.132 52.320 1.00 15.04 ? 117 SER A N 1 ATOM 450 C CA . SER A 1 71 ? 16.655 38.807 51.521 1.00 15.09 ? 117 SER A CA 1 ATOM 451 C C . SER A 1 71 ? 15.459 39.589 52.042 1.00 15.49 ? 117 SER A C 1 ATOM 452 O O . SER A 1 71 ? 14.722 40.235 51.293 1.00 14.17 ? 117 SER A O 1 ATOM 453 C CB . SER A 1 71 ? 16.355 37.308 51.603 1.00 16.10 ? 117 SER A CB 1 ATOM 454 O OG . SER A 1 71 ? 17.402 36.625 50.943 1.00 18.48 ? 117 SER A OG 1 ATOM 455 N N . LEU A 1 72 ? 15.294 39.553 53.364 1.00 14.48 ? 118 LEU A N 1 ATOM 456 C CA . LEU A 1 72 ? 14.184 40.291 53.969 1.00 15.30 ? 118 LEU A CA 1 ATOM 457 C C . LEU A 1 72 ? 14.405 41.786 53.832 1.00 14.49 ? 118 LEU A C 1 ATOM 458 O O . LEU A 1 72 ? 13.478 42.494 53.529 1.00 15.05 ? 118 LEU A O 1 ATOM 459 C CB . LEU A 1 72 ? 14.036 39.905 55.459 1.00 16.21 ? 118 LEU A CB 1 ATOM 460 C CG . LEU A 1 72 ? 12.789 40.504 56.097 1.00 19.83 ? 118 LEU A CG 1 ATOM 461 C CD1 . LEU A 1 72 ? 11.544 39.829 55.517 1.00 22.90 ? 118 LEU A CD1 1 ATOM 462 C CD2 . LEU A 1 72 ? 12.845 40.350 57.668 1.00 19.75 ? 118 LEU A CD2 1 ATOM 463 N N . GLN A 1 73 ? 15.630 42.272 54.023 1.00 14.08 ? 119 GLN A N 1 ATOM 464 C CA . GLN A 1 73 ? 15.926 43.687 53.796 1.00 14.34 ? 119 GLN A CA 1 ATOM 465 C C . GLN A 1 73 ? 15.528 44.127 52.372 1.00 14.48 ? 119 GLN A C 1 ATOM 466 O O . GLN A 1 73 ? 14.922 45.183 52.175 1.00 13.14 ? 119 GLN A O 1 ATOM 467 C CB . GLN A 1 73 ? 17.420 43.924 53.925 1.00 14.87 ? 119 GLN A CB 1 ATOM 468 C CG . GLN A 1 73 ? 17.997 43.897 55.329 1.00 14.66 ? 119 GLN A CG 1 ATOM 469 C CD . GLN A 1 73 ? 19.492 44.146 55.228 1.00 16.69 ? 119 GLN A CD 1 ATOM 470 O OE1 . GLN A 1 73 ? 19.908 45.106 54.577 1.00 15.11 ? 119 GLN A OE1 1 ATOM 471 N NE2 . GLN A 1 73 ? 20.292 43.259 55.784 1.00 17.05 ? 119 GLN A NE2 1 ATOM 472 N N . ALA A 1 74 ? 15.886 43.311 51.374 1.00 13.59 ? 120 ALA A N 1 ATOM 473 C CA . ALA A 1 74 ? 15.598 43.671 49.968 1.00 14.57 ? 120 ALA A CA 1 ATOM 474 C C . ALA A 1 74 ? 14.099 43.767 49.689 1.00 14.51 ? 120 ALA A C 1 ATOM 475 O O . ALA A 1 74 ? 13.647 44.710 49.061 1.00 14.00 ? 120 ALA A O 1 ATOM 476 C CB . ALA A 1 74 ? 16.242 42.651 48.979 1.00 13.90 ? 120 ALA A CB 1 ATOM 477 N N . TYR A 1 75 ? 13.354 42.757 50.138 1.00 14.64 ? 121 TYR A N 1 ATOM 478 C CA . TYR A 1 75 ? 11.900 42.758 49.980 1.00 14.42 ? 121 TYR A CA 1 ATOM 479 C C . TYR A 1 75 ? 11.343 44.014 50.673 1.00 14.99 ? 121 TYR A C 1 ATOM 480 O O . TYR A 1 75 ? 10.554 44.754 50.096 1.00 14.60 ? 121 TYR A O 1 ATOM 481 C CB . TYR A 1 75 ? 11.322 41.454 50.566 1.00 14.33 ? 121 TYR A CB 1 ATOM 482 C CG . TYR A 1 75 ? 9.820 41.329 50.351 1.00 17.81 ? 121 TYR A CG 1 ATOM 483 C CD1 . TYR A 1 75 ? 9.300 40.954 49.115 1.00 16.61 ? 121 TYR A CD1 1 ATOM 484 C CD2 . TYR A 1 75 ? 8.916 41.655 51.380 1.00 19.99 ? 121 TYR A CD2 1 ATOM 485 C CE1 . TYR A 1 75 ? 7.918 40.861 48.902 1.00 16.85 ? 121 TYR A CE1 1 ATOM 486 C CE2 . TYR A 1 75 ? 7.530 41.554 51.180 1.00 19.80 ? 121 TYR A CE2 1 ATOM 487 C CZ . TYR A 1 75 ? 7.047 41.150 49.950 1.00 19.79 ? 121 TYR A CZ 1 ATOM 488 O OH . TYR A 1 75 ? 5.686 41.074 49.741 1.00 17.85 ? 121 TYR A OH 1 ATOM 489 N N . ALA A 1 76 ? 11.778 44.245 51.920 1.00 14.92 ? 122 ALA A N 1 ATOM 490 C CA . ALA A 1 76 ? 11.310 45.407 52.692 1.00 15.55 ? 122 ALA A CA 1 ATOM 491 C C . ALA A 1 76 ? 11.644 46.735 52.030 1.00 15.51 ? 122 ALA A C 1 ATOM 492 O O . ALA A 1 76 ? 10.861 47.696 52.112 1.00 15.62 ? 122 ALA A O 1 ATOM 493 C CB . ALA A 1 76 ? 11.889 45.365 54.097 1.00 15.34 ? 122 ALA A CB 1 ATOM 494 N N . ALA A 1 77 ? 12.812 46.815 51.391 1.00 15.32 ? 123 ALA A N 1 ATOM 495 C CA . ALA A 1 77 ? 13.190 48.035 50.687 1.00 15.13 ? 123 ALA A CA 1 ATOM 496 C C . ALA A 1 77 ? 12.166 48.354 49.594 1.00 15.38 ? 123 ALA A C 1 ATOM 497 O O . ALA A 1 77 ? 11.768 49.512 49.440 1.00 15.94 ? 123 ALA A O 1 ATOM 498 C CB . ALA A 1 77 ? 14.642 47.931 50.112 1.00 14.78 ? 123 ALA A CB 1 ATOM 499 N N . GLY A 1 78 ? 11.750 47.341 48.827 1.00 14.59 ? 124 GLY A N 1 ATOM 500 C CA . GLY A 1 78 ? 10.722 47.558 47.806 1.00 14.22 ? 124 GLY A CA 1 ATOM 501 C C . GLY A 1 78 ? 9.425 48.024 48.450 1.00 14.49 ? 124 GLY A C 1 ATOM 502 O O . GLY A 1 78 ? 8.776 48.961 47.989 1.00 14.58 ? 124 GLY A O 1 ATOM 503 N N . VAL A 1 79 ? 9.062 47.355 49.530 1.00 14.66 ? 125 VAL A N 1 ATOM 504 C CA . VAL A 1 79 ? 7.788 47.657 50.212 1.00 15.05 ? 125 VAL A CA 1 ATOM 505 C C . VAL A 1 79 ? 7.736 49.115 50.661 1.00 15.66 ? 125 VAL A C 1 ATOM 506 O O . VAL A 1 79 ? 6.740 49.823 50.388 1.00 15.85 ? 125 VAL A O 1 ATOM 507 C CB . VAL A 1 79 ? 7.552 46.718 51.417 1.00 15.13 ? 125 VAL A CB 1 ATOM 508 C CG1 . VAL A 1 79 ? 6.267 47.200 52.204 1.00 14.87 ? 125 VAL A CG1 1 ATOM 509 C CG2 . VAL A 1 79 ? 7.363 45.270 50.940 1.00 14.20 ? 125 VAL A CG2 1 ATOM 510 N N . VAL A 1 80 ? 8.759 49.553 51.396 1.00 15.92 ? 126 VAL A N 1 ATOM 511 C CA . VAL A 1 80 ? 8.719 50.919 51.929 1.00 17.01 ? 126 VAL A CA 1 ATOM 512 C C . VAL A 1 80 ? 8.846 51.973 50.830 1.00 16.90 ? 126 VAL A C 1 ATOM 513 O O . VAL A 1 80 ? 8.224 53.033 50.914 1.00 17.13 ? 126 VAL A O 1 ATOM 514 C CB . VAL A 1 80 ? 9.715 51.161 53.085 1.00 18.32 ? 126 VAL A CB 1 ATOM 515 C CG1 . VAL A 1 80 ? 9.377 50.223 54.269 1.00 18.55 ? 126 VAL A CG1 1 ATOM 516 C CG2 . VAL A 1 80 ? 11.195 50.983 52.615 1.00 15.76 ? 126 VAL A CG2 1 ATOM 517 N N . GLU A 1 81 ? 9.616 51.686 49.781 1.00 15.83 ? 127 GLU A N 1 ATOM 518 C CA . GLU A 1 81 ? 9.661 52.609 48.679 1.00 16.67 ? 127 GLU A CA 1 ATOM 519 C C . GLU A 1 81 ? 8.272 52.843 48.088 1.00 16.30 ? 127 GLU A C 1 ATOM 520 O O . GLU A 1 81 ? 7.882 54.010 47.882 1.00 16.73 ? 127 GLU A O 1 ATOM 521 C CB . GLU A 1 81 ? 10.633 52.161 47.565 1.00 16.80 ? 127 GLU A CB 1 ATOM 522 C CG . GLU A 1 81 ? 10.488 53.096 46.367 1.00 17.41 ? 127 GLU A CG 1 ATOM 523 C CD . GLU A 1 81 ? 11.724 53.152 45.447 1.00 20.14 ? 127 GLU A CD 1 ATOM 524 O OE1 . GLU A 1 81 ? 12.801 52.590 45.777 1.00 19.68 ? 127 GLU A OE1 1 ATOM 525 O OE2 . GLU A 1 81 ? 11.614 53.841 44.393 1.00 22.02 ? 127 GLU A OE2 1 ATOM 526 N N . ALA A 1 82 ? 7.547 51.759 47.790 1.00 16.17 ? 128 ALA A N 1 ATOM 527 C CA . ALA A 1 82 ? 6.205 51.880 47.183 1.00 17.31 ? 128 ALA A CA 1 ATOM 528 C C . ALA A 1 82 ? 5.289 52.630 48.154 1.00 18.28 ? 128 ALA A C 1 ATOM 529 O O . ALA A 1 82 ? 4.461 53.456 47.759 1.00 18.48 ? 128 ALA A O 1 ATOM 530 C CB . ALA A 1 82 ? 5.640 50.509 46.896 1.00 17.17 ? 128 ALA A CB 1 ATOM 531 N N . SER A 1 83 ? 5.427 52.314 49.436 1.00 18.33 ? 129 SER A N 1 ATOM 532 C CA A SER A 1 83 ? 4.578 52.901 50.476 0.50 18.42 ? 129 SER A CA 1 ATOM 533 C CA B SER A 1 83 ? 4.546 52.905 50.440 0.50 19.28 ? 129 SER A CA 1 ATOM 534 C C . SER A 1 83 ? 4.647 54.434 50.524 1.00 19.21 ? 129 SER A C 1 ATOM 535 O O . SER A 1 83 ? 3.660 55.090 50.850 1.00 21.64 ? 129 SER A O 1 ATOM 536 C CB A SER A 1 83 ? 4.913 52.282 51.849 0.50 17.89 ? 129 SER A CB 1 ATOM 537 C CB B SER A 1 83 ? 4.772 52.257 51.811 0.50 19.05 ? 129 SER A CB 1 ATOM 538 O OG A SER A 1 83 ? 6.000 52.938 52.489 0.50 14.50 ? 129 SER A OG 1 ATOM 539 O OG B SER A 1 83 ? 3.797 52.717 52.737 0.50 20.59 ? 129 SER A OG 1 ATOM 540 N N . VAL A 1 84 ? 5.811 55.022 50.252 1.00 17.46 ? 130 VAL A N 1 ATOM 541 C CA . VAL A 1 84 ? 5.942 56.483 50.333 1.00 18.25 ? 130 VAL A CA 1 ATOM 542 C C . VAL A 1 84 ? 5.788 57.174 48.978 1.00 18.97 ? 130 VAL A C 1 ATOM 543 O O . VAL A 1 84 ? 5.739 58.414 48.870 1.00 20.25 ? 130 VAL A O 1 ATOM 544 C CB . VAL A 1 84 ? 7.249 56.904 51.030 1.00 18.27 ? 130 VAL A CB 1 ATOM 545 C CG1 . VAL A 1 84 ? 7.260 56.291 52.460 1.00 19.57 ? 130 VAL A CG1 1 ATOM 546 C CG2 . VAL A 1 84 ? 8.479 56.433 50.235 1.00 17.83 ? 130 VAL A CG2 1 ATOM 547 N N . SER A 1 85 ? 5.713 56.377 47.925 1.00 18.18 ? 131 SER A N 1 ATOM 548 C CA . SER A 1 85 ? 5.619 56.954 46.593 1.00 18.51 ? 131 SER A CA 1 ATOM 549 C C . SER A 1 85 ? 4.422 56.482 45.757 1.00 18.55 ? 131 SER A C 1 ATOM 550 O O . SER A 1 85 ? 4.430 56.637 44.524 1.00 17.97 ? 131 SER A O 1 ATOM 551 C CB . SER A 1 85 ? 6.937 56.714 45.831 1.00 19.17 ? 131 SER A CB 1 ATOM 552 O OG . SER A 1 85 ? 7.145 55.336 45.602 1.00 18.95 ? 131 SER A OG 1 ATOM 553 N N . GLU A 1 86 ? 3.375 55.977 46.404 1.00 18.88 ? 132 GLU A N 1 ATOM 554 C CA . GLU A 1 86 ? 2.263 55.351 45.672 1.00 21.05 ? 132 GLU A CA 1 ATOM 555 C C . GLU A 1 86 ? 1.631 56.279 44.647 1.00 19.46 ? 132 GLU A C 1 ATOM 556 O O . GLU A 1 86 ? 1.321 55.860 43.538 1.00 19.06 ? 132 GLU A O 1 ATOM 557 C CB . GLU A 1 86 ? 1.194 54.768 46.634 1.00 22.70 ? 132 GLU A CB 1 ATOM 558 C CG . GLU A 1 86 ? 1.323 53.236 46.736 1.00 31.92 ? 132 GLU A CG 1 ATOM 559 C CD . GLU A 1 86 ? 1.018 52.677 48.115 1.00 40.76 ? 132 GLU A CD 1 ATOM 560 O OE1 . GLU A 1 86 ? 0.136 53.250 48.808 1.00 44.12 ? 132 GLU A OE1 1 ATOM 561 O OE2 . GLU A 1 86 ? 1.667 51.656 48.490 1.00 45.33 ? 132 GLU A OE2 1 ATOM 562 N N . GLU A 1 87 ? 1.383 57.531 45.025 1.00 19.04 ? 133 GLU A N 1 ATOM 563 C CA A GLU A 1 87 ? 0.784 58.520 44.130 0.50 18.79 ? 133 GLU A CA 1 ATOM 564 C CA B GLU A 1 87 ? 0.726 58.407 44.055 0.50 19.36 ? 133 GLU A CA 1 ATOM 565 C C . GLU A 1 87 ? 1.635 58.765 42.886 1.00 18.53 ? 133 GLU A C 1 ATOM 566 O O . GLU A 1 87 ? 1.155 58.804 41.758 1.00 17.26 ? 133 GLU A O 1 ATOM 567 C CB A GLU A 1 87 ? 0.608 59.833 44.901 0.50 18.84 ? 133 GLU A CB 1 ATOM 568 C CB B GLU A 1 87 ? 0.048 59.632 44.688 0.50 20.22 ? 133 GLU A CB 1 ATOM 569 C CG A GLU A 1 87 ? -0.374 59.680 46.065 0.50 20.41 ? 133 GLU A CG 1 ATOM 570 C CG B GLU A 1 87 ? -1.362 59.296 45.222 0.50 24.14 ? 133 GLU A CG 1 ATOM 571 C CD A GLU A 1 87 ? 0.276 59.367 47.423 0.50 23.77 ? 133 GLU A CD 1 ATOM 572 C CD B GLU A 1 87 ? -2.320 58.728 44.140 0.50 28.09 ? 133 GLU A CD 1 ATOM 573 O OE1 A GLU A 1 87 ? 1.457 58.891 47.512 0.50 17.93 ? 133 GLU A OE1 1 ATOM 574 O OE1 B GLU A 1 87 ? -2.769 59.510 43.265 0.50 30.71 ? 133 GLU A OE1 1 ATOM 575 O OE2 A GLU A 1 87 ? -0.448 59.602 48.422 0.50 25.48 ? 133 GLU A OE2 1 ATOM 576 O OE2 B GLU A 1 87 ? -2.633 57.506 44.172 0.50 28.27 ? 133 GLU A OE2 1 ATOM 577 N N . LEU A 1 88 ? 2.932 58.963 43.128 1.00 17.11 ? 134 LEU A N 1 ATOM 578 C CA . LEU A 1 88 ? 3.859 59.191 42.042 1.00 16.51 ? 134 LEU A CA 1 ATOM 579 C C . LEU A 1 88 ? 3.966 57.971 41.116 1.00 16.07 ? 134 LEU A C 1 ATOM 580 O O . LEU A 1 88 ? 4.101 58.133 39.905 1.00 15.47 ? 134 LEU A O 1 ATOM 581 C CB . LEU A 1 88 ? 5.229 59.572 42.589 1.00 16.94 ? 134 LEU A CB 1 ATOM 582 C CG . LEU A 1 88 ? 5.303 60.996 43.141 1.00 19.23 ? 134 LEU A CG 1 ATOM 583 C CD1 . LEU A 1 88 ? 6.651 61.226 43.873 1.00 21.15 ? 134 LEU A CD1 1 ATOM 584 C CD2 . LEU A 1 88 ? 5.086 62.033 42.013 1.00 21.85 ? 134 LEU A CD2 1 ATOM 585 N N . ILE A 1 89 ? 3.946 56.769 41.686 1.00 15.76 ? 135 ILE A N 1 ATOM 586 C CA . ILE A 1 89 ? 3.984 55.540 40.875 1.00 16.06 ? 135 ILE A CA 1 ATOM 587 C C . ILE A 1 89 ? 2.763 55.471 39.947 1.00 16.69 ? 135 ILE A C 1 ATOM 588 O O . ILE A 1 89 ? 2.867 55.212 38.737 1.00 16.14 ? 135 ILE A O 1 ATOM 589 C CB . ILE A 1 89 ? 4.081 54.282 41.750 1.00 16.23 ? 135 ILE A CB 1 ATOM 590 C CG1 . ILE A 1 89 ? 5.468 54.233 42.413 1.00 15.27 ? 135 ILE A CG1 1 ATOM 591 C CG2 . ILE A 1 89 ? 3.854 53.030 40.889 1.00 17.28 ? 135 ILE A CG2 1 ATOM 592 C CD1 . ILE A 1 89 ? 5.593 53.264 43.559 1.00 16.48 ? 135 ILE A CD1 1 ATOM 593 N N . TYR A 1 90 ? 1.593 55.767 40.522 1.00 16.21 ? 136 TYR A N 1 ATOM 594 C CA . TYR A 1 90 ? 0.374 55.701 39.748 1.00 16.19 ? 136 TYR A CA 1 ATOM 595 C C . TYR A 1 90 ? 0.431 56.677 38.568 1.00 15.64 ? 136 TYR A C 1 ATOM 596 O O . TYR A 1 90 ? 0.142 56.322 37.423 1.00 15.73 ? 136 TYR A O 1 ATOM 597 C CB . TYR A 1 90 ? -0.806 56.019 40.670 1.00 17.63 ? 136 TYR A CB 1 ATOM 598 C CG . TYR A 1 90 ? -2.059 56.246 39.868 1.00 19.03 ? 136 TYR A CG 1 ATOM 599 C CD1 . TYR A 1 90 ? -2.738 55.168 39.329 1.00 23.64 ? 136 TYR A CD1 1 ATOM 600 C CD2 . TYR A 1 90 ? -2.555 57.528 39.655 1.00 21.51 ? 136 TYR A CD2 1 ATOM 601 C CE1 . TYR A 1 90 ? -3.894 55.356 38.584 1.00 26.59 ? 136 TYR A CE1 1 ATOM 602 C CE2 . TYR A 1 90 ? -3.713 57.722 38.893 1.00 22.45 ? 136 TYR A CE2 1 ATOM 603 C CZ . TYR A 1 90 ? -4.356 56.631 38.367 1.00 25.49 ? 136 TYR A CZ 1 ATOM 604 O OH . TYR A 1 90 ? -5.508 56.771 37.610 1.00 28.03 ? 136 TYR A OH 1 ATOM 605 N N . MET A 1 91 ? 0.791 57.914 38.852 1.00 15.93 ? 137 MET A N 1 ATOM 606 C CA . MET A 1 91 ? 0.874 58.912 37.809 1.00 16.69 ? 137 MET A CA 1 ATOM 607 C C . MET A 1 91 ? 1.908 58.559 36.736 1.00 16.54 ? 137 MET A C 1 ATOM 608 O O . MET A 1 91 ? 1.665 58.718 35.530 1.00 15.57 ? 137 MET A O 1 ATOM 609 C CB . MET A 1 91 ? 1.196 60.273 38.433 1.00 17.53 ? 137 MET A CB 1 ATOM 610 C CG . MET A 1 91 ? -0.002 60.768 39.249 1.00 19.82 ? 137 MET A CG 1 ATOM 611 S SD . MET A 1 91 ? 0.272 62.403 39.916 1.00 29.30 ? 137 MET A SD 1 ATOM 612 C CE . MET A 1 91 ? 1.649 62.134 40.942 1.00 24.23 ? 137 MET A CE 1 ATOM 613 N N . HIS A 1 92 ? 3.090 58.107 37.173 1.00 16.89 ? 138 HIS A N 1 ATOM 614 C CA . HIS A 1 92 ? 4.138 57.720 36.209 1.00 16.09 ? 138 HIS A CA 1 ATOM 615 C C . HIS A 1 92 ? 3.677 56.548 35.339 1.00 16.71 ? 138 HIS A C 1 ATOM 616 O O . HIS A 1 92 ? 3.941 56.545 34.139 1.00 16.49 ? 138 HIS A O 1 ATOM 617 C CB . HIS A 1 92 ? 5.425 57.329 36.966 1.00 16.72 ? 138 HIS A CB 1 ATOM 618 C CG . HIS A 1 92 ? 6.648 57.244 36.087 1.00 18.11 ? 138 HIS A CG 1 ATOM 619 N ND1 . HIS A 1 92 ? 7.098 58.309 35.345 1.00 18.04 ? 138 HIS A ND1 1 ATOM 620 C CD2 . HIS A 1 92 ? 7.525 56.232 35.866 1.00 20.47 ? 138 HIS A CD2 1 ATOM 621 C CE1 . HIS A 1 92 ? 8.209 57.971 34.706 1.00 20.16 ? 138 HIS A CE1 1 ATOM 622 N NE2 . HIS A 1 92 ? 8.480 56.704 34.989 1.00 16.45 ? 138 HIS A NE2 1 ATOM 623 N N . TRP A 1 93 ? 2.999 55.566 35.940 1.00 15.79 ? 139 TRP A N 1 ATOM 624 C CA . TRP A 1 93 ? 2.442 54.427 35.192 1.00 16.89 ? 139 TRP A CA 1 ATOM 625 C C . TRP A 1 93 ? 1.477 54.946 34.110 1.00 16.84 ? 139 TRP A C 1 ATOM 626 O O . TRP A 1 93 ? 1.534 54.531 32.925 1.00 16.69 ? 139 TRP A O 1 ATOM 627 C CB . TRP A 1 93 ? 1.694 53.482 36.146 1.00 17.53 ? 139 TRP A CB 1 ATOM 628 C CG . TRP A 1 93 ? 1.153 52.262 35.465 1.00 22.21 ? 139 TRP A CG 1 ATOM 629 C CD1 . TRP A 1 93 ? -0.085 52.119 34.869 1.00 23.32 ? 139 TRP A CD1 1 ATOM 630 C CD2 . TRP A 1 93 ? 1.846 51.014 35.270 1.00 23.68 ? 139 TRP A CD2 1 ATOM 631 N NE1 . TRP A 1 93 ? -0.193 50.850 34.316 1.00 22.87 ? 139 TRP A NE1 1 ATOM 632 C CE2 . TRP A 1 93 ? 0.967 50.151 34.569 1.00 24.87 ? 139 TRP A CE2 1 ATOM 633 C CE3 . TRP A 1 93 ? 3.112 50.527 35.657 1.00 24.68 ? 139 TRP A CE3 1 ATOM 634 C CZ2 . TRP A 1 93 ? 1.329 48.836 34.216 1.00 24.80 ? 139 TRP A CZ2 1 ATOM 635 C CZ3 . TRP A 1 93 ? 3.462 49.205 35.309 1.00 23.77 ? 139 TRP A CZ3 1 ATOM 636 C CH2 . TRP A 1 93 ? 2.586 48.395 34.586 1.00 24.05 ? 139 TRP A CH2 1 ATOM 637 N N . MET A 1 94 ? 0.591 55.850 34.529 1.00 16.63 ? 140 MET A N 1 ATOM 638 C CA . MET A 1 94 ? -0.398 56.413 33.595 1.00 17.90 ? 140 MET A CA 1 ATOM 639 C C . MET A 1 94 ? 0.277 57.201 32.474 1.00 18.27 ? 140 MET A C 1 ATOM 640 O O . MET A 1 94 ? -0.151 57.154 31.312 1.00 19.53 ? 140 MET A O 1 ATOM 641 C CB . MET A 1 94 ? -1.424 57.276 34.348 1.00 17.95 ? 140 MET A CB 1 ATOM 642 C CG . MET A 1 94 ? -2.316 56.475 35.293 1.00 21.43 ? 140 MET A CG 1 ATOM 643 S SD . MET A 1 94 ? -3.491 55.438 34.347 1.00 28.89 ? 140 MET A SD 1 ATOM 644 C CE . MET A 1 94 ? -4.461 56.790 33.712 1.00 28.20 ? 140 MET A CE 1 ATOM 645 N N . ASN A 1 95 ? 1.329 57.948 32.808 1.00 17.45 ? 141 ASN A N 1 ATOM 646 C CA . ASN A 1 95 ? 2.028 58.757 31.833 1.00 17.11 ? 141 ASN A CA 1 ATOM 647 C C . ASN A 1 95 ? 2.852 57.958 30.821 1.00 18.12 ? 141 ASN A C 1 ATOM 648 O O . ASN A 1 95 ? 3.083 58.436 29.720 1.00 19.63 ? 141 ASN A O 1 ATOM 649 C CB . ASN A 1 95 ? 2.984 59.725 32.531 1.00 16.50 ? 141 ASN A CB 1 ATOM 650 C CG . ASN A 1 95 ? 2.260 60.815 33.315 1.00 17.85 ? 141 ASN A CG 1 ATOM 651 O OD1 . ASN A 1 95 ? 1.070 61.072 33.091 1.00 17.05 ? 141 ASN A OD1 1 ATOM 652 N ND2 . ASN A 1 95 ? 2.992 61.483 34.222 1.00 16.77 ? 141 ASN A ND2 1 ATOM 653 N N . THR A 1 96 ? 3.296 56.765 31.204 1.00 18.47 ? 142 THR A N 1 ATOM 654 C CA . THR A 1 96 ? 4.351 56.113 30.430 1.00 20.23 ? 142 THR A CA 1 ATOM 655 C C . THR A 1 96 ? 4.064 54.724 29.884 1.00 21.95 ? 142 THR A C 1 ATOM 656 O O . THR A 1 96 ? 4.589 54.401 28.812 1.00 25.10 ? 142 THR A O 1 ATOM 657 C CB . THR A 1 96 ? 5.695 56.047 31.223 1.00 19.23 ? 142 THR A CB 1 ATOM 658 O OG1 . THR A 1 96 ? 5.559 55.163 32.346 1.00 21.16 ? 142 THR A OG1 1 ATOM 659 C CG2 . THR A 1 96 ? 6.151 57.448 31.660 1.00 20.94 ? 142 THR A CG2 1 ATOM 660 N N . VAL A 1 97 ? 3.341 53.869 30.599 1.00 21.48 ? 143 VAL A N 1 ATOM 661 C CA . VAL A 1 97 ? 3.201 52.472 30.132 1.00 22.96 ? 143 VAL A CA 1 ATOM 662 C C . VAL A 1 97 ? 1.779 51.897 30.198 1.00 23.74 ? 143 VAL A C 1 ATOM 663 O O . VAL A 1 97 ? 1.551 50.749 29.821 1.00 22.63 ? 143 VAL A O 1 ATOM 664 C CB . VAL A 1 97 ? 4.165 51.492 30.876 1.00 23.95 ? 143 VAL A CB 1 ATOM 665 C CG1 . VAL A 1 97 ? 5.615 51.857 30.607 1.00 25.06 ? 143 VAL A CG1 1 ATOM 666 C CG2 . VAL A 1 97 ? 3.897 51.539 32.370 1.00 24.12 ? 143 VAL A CG2 1 ATOM 667 N N . VAL A 1 98 ? 0.821 52.690 30.671 1.00 24.56 ? 144 VAL A N 1 ATOM 668 C CA . VAL A 1 98 ? -0.555 52.187 30.802 1.00 26.43 ? 144 VAL A CA 1 ATOM 669 C C . VAL A 1 98 ? -1.104 51.564 29.498 1.00 27.78 ? 144 VAL A C 1 ATOM 670 O O . VAL A 1 98 ? -1.918 50.645 29.530 1.00 29.11 ? 144 VAL A O 1 ATOM 671 C CB . VAL A 1 98 ? -1.517 53.288 31.323 1.00 25.86 ? 144 VAL A CB 1 ATOM 672 C CG1 . VAL A 1 98 ? -1.643 54.390 30.308 1.00 24.29 ? 144 VAL A CG1 1 ATOM 673 C CG2 . VAL A 1 98 ? -2.879 52.671 31.690 1.00 27.28 ? 144 VAL A CG2 1 ATOM 674 N N . ASN A 1 99 ? -0.674 52.041 28.345 1.00 29.32 ? 145 ASN A N 1 ATOM 675 C CA . ASN A 1 99 ? -1.185 51.429 27.118 1.00 31.17 ? 145 ASN A CA 1 ATOM 676 C C . ASN A 1 99 ? -0.320 50.284 26.555 1.00 31.21 ? 145 ASN A C 1 ATOM 677 O O . ASN A 1 99 ? -0.723 49.613 25.594 1.00 31.55 ? 145 ASN A O 1 ATOM 678 C CB . ASN A 1 99 ? -1.442 52.491 26.054 1.00 31.90 ? 145 ASN A CB 1 ATOM 679 C CG . ASN A 1 99 ? -2.521 53.483 26.484 1.00 34.24 ? 145 ASN A CG 1 ATOM 680 O OD1 . ASN A 1 99 ? -3.567 53.085 26.998 1.00 39.18 ? 145 ASN A OD1 1 ATOM 681 N ND2 . ASN A 1 99 ? -2.252 54.769 26.303 1.00 36.55 ? 145 ASN A ND2 1 ATOM 682 N N . TYR A 1 100 ? 0.841 50.038 27.164 1.00 29.88 ? 146 TYR A N 1 ATOM 683 C CA . TYR A 1 100 ? 1.808 49.118 26.548 1.00 28.81 ? 146 TYR A CA 1 ATOM 684 C C . TYR A 1 100 ? 1.367 47.660 26.680 1.00 29.30 ? 146 TYR A C 1 ATOM 685 O O . TYR A 1 100 ? 1.278 47.132 27.778 1.00 29.36 ? 146 TYR A O 1 ATOM 686 C CB . TYR A 1 100 ? 3.206 49.317 27.155 1.00 27.76 ? 146 TYR A CB 1 ATOM 687 C CG . TYR A 1 100 ? 4.309 48.716 26.327 1.00 24.17 ? 146 TYR A CG 1 ATOM 688 C CD1 . TYR A 1 100 ? 4.903 49.435 25.290 1.00 24.09 ? 146 TYR A CD1 1 ATOM 689 C CD2 . TYR A 1 100 ? 4.753 47.424 26.580 1.00 24.77 ? 146 TYR A CD2 1 ATOM 690 C CE1 . TYR A 1 100 ? 5.922 48.877 24.498 1.00 24.08 ? 146 TYR A CE1 1 ATOM 691 C CE2 . TYR A 1 100 ? 5.748 46.858 25.815 1.00 22.38 ? 146 TYR A CE2 1 ATOM 692 C CZ . TYR A 1 100 ? 6.342 47.573 24.798 1.00 23.77 ? 146 TYR A CZ 1 ATOM 693 O OH . TYR A 1 100 ? 7.348 46.971 24.046 1.00 23.49 ? 146 TYR A OH 1 ATOM 694 N N . CYS A 1 101 ? 1.114 47.006 25.555 1.00 30.75 ? 147 CYS A N 1 ATOM 695 C CA . CYS A 1 101 ? 0.605 45.636 25.565 1.00 32.84 ? 147 CYS A CA 1 ATOM 696 C C . CYS A 1 101 ? -0.678 45.465 26.429 1.00 34.90 ? 147 CYS A C 1 ATOM 697 O O . CYS A 1 101 ? -0.843 44.458 27.138 1.00 35.88 ? 147 CYS A O 1 ATOM 698 C CB . CYS A 1 101 ? 1.722 44.646 25.951 1.00 33.58 ? 147 CYS A CB 1 ATOM 699 S SG . CYS A 1 101 ? 2.874 44.400 24.561 1.00 33.67 ? 147 CYS A SG 1 ATOM 700 N N . GLY A 1 102 ? -1.577 46.445 26.343 1.00 36.00 ? 148 GLY A N 1 ATOM 701 C CA . GLY A 1 102 ? -2.853 46.419 27.087 1.00 38.43 ? 148 GLY A CA 1 ATOM 702 C C . GLY A 1 102 ? -3.885 45.465 26.497 1.00 39.65 ? 148 GLY A C 1 ATOM 703 O O . GLY A 1 102 ? -3.614 44.789 25.509 1.00 39.60 ? 148 GLY A O 1 ATOM 704 N N . PRO A 1 103 ? -5.083 45.393 27.113 1.00 41.02 ? 149 PRO A N 1 ATOM 705 C CA . PRO A 1 103 ? -6.147 44.476 26.642 1.00 41.15 ? 149 PRO A CA 1 ATOM 706 C C . PRO A 1 103 ? -6.635 44.722 25.208 1.00 40.68 ? 149 PRO A C 1 ATOM 707 O O . PRO A 1 103 ? -7.184 43.809 24.586 1.00 41.14 ? 149 PRO A O 1 ATOM 708 C CB . PRO A 1 103 ? -7.298 44.713 27.638 1.00 41.38 ? 149 PRO A CB 1 ATOM 709 C CG . PRO A 1 103 ? -6.991 46.047 28.295 1.00 42.16 ? 149 PRO A CG 1 ATOM 710 C CD . PRO A 1 103 ? -5.484 46.145 28.318 1.00 41.46 ? 149 PRO A CD 1 ATOM 711 N N . PHE A 1 104 ? -6.455 45.932 24.685 1.00 39.56 ? 150 PHE A N 1 ATOM 712 C CA . PHE A 1 104 ? -6.968 46.242 23.351 1.00 38.81 ? 150 PHE A CA 1 ATOM 713 C C . PHE A 1 104 ? -5.869 46.358 22.298 1.00 38.93 ? 150 PHE A C 1 ATOM 714 O O . PHE A 1 104 ? -6.097 46.835 21.192 1.00 37.94 ? 150 PHE A O 1 ATOM 715 C CB . PHE A 1 104 ? -7.836 47.491 23.404 1.00 38.60 ? 150 PHE A CB 1 ATOM 716 C CG . PHE A 1 104 ? -8.924 47.390 24.416 1.00 37.76 ? 150 PHE A CG 1 ATOM 717 C CD1 . PHE A 1 104 ? -8.944 48.224 25.519 1.00 37.69 ? 150 PHE A CD1 1 ATOM 718 C CD2 . PHE A 1 104 ? -9.903 46.410 24.291 1.00 37.66 ? 150 PHE A CD2 1 ATOM 719 C CE1 . PHE A 1 104 ? -9.957 48.111 26.473 1.00 37.69 ? 150 PHE A CE1 1 ATOM 720 C CE2 . PHE A 1 104 ? -10.910 46.286 25.241 1.00 37.36 ? 150 PHE A CE2 1 ATOM 721 C CZ . PHE A 1 104 ? -10.929 47.141 26.334 1.00 35.85 ? 150 PHE A CZ 1 ATOM 722 N N . GLU A 1 105 ? -4.679 45.887 22.663 1.00 39.33 ? 151 GLU A N 1 ATOM 723 C CA A GLU A 1 105 ? -3.538 46.022 21.774 0.50 39.64 ? 151 GLU A CA 1 ATOM 724 C CA B GLU A 1 105 ? -3.477 45.879 21.819 0.50 39.73 ? 151 GLU A CA 1 ATOM 725 C C . GLU A 1 105 ? -3.745 45.348 20.407 1.00 39.82 ? 151 GLU A C 1 ATOM 726 O O . GLU A 1 105 ? -4.222 44.214 20.277 1.00 39.20 ? 151 GLU A O 1 ATOM 727 C CB A GLU A 1 105 ? -2.244 45.573 22.458 0.50 39.73 ? 151 GLU A CB 1 ATOM 728 C CB B GLU A 1 105 ? -2.465 44.934 22.483 0.50 39.86 ? 151 GLU A CB 1 ATOM 729 C CG A GLU A 1 105 ? -1.080 46.509 22.189 0.50 40.58 ? 151 GLU A CG 1 ATOM 730 C CG B GLU A 1 105 ? -3.019 43.499 22.607 0.50 40.70 ? 151 GLU A CG 1 ATOM 731 C CD A GLU A 1 105 ? -0.409 46.217 20.878 0.50 41.10 ? 151 GLU A CD 1 ATOM 732 C CD B GLU A 1 105 ? -2.287 42.606 23.602 0.50 42.29 ? 151 GLU A CD 1 ATOM 733 O OE1 A GLU A 1 105 ? -0.028 45.049 20.677 0.50 42.99 ? 151 GLU A OE1 1 ATOM 734 O OE1 B GLU A 1 105 ? -2.031 41.432 23.259 0.50 41.84 ? 151 GLU A OE1 1 ATOM 735 O OE2 A GLU A 1 105 ? -0.263 47.138 20.047 0.50 41.34 ? 151 GLU A OE2 1 ATOM 736 O OE2 B GLU A 1 105 ? -1.988 43.060 24.730 0.50 43.87 ? 151 GLU A OE2 1 ATOM 737 N N . TYR A 1 106 ? -3.417 46.107 19.361 1.00 40.12 ? 152 TYR A N 1 ATOM 738 C CA . TYR A 1 106 ? -3.526 45.587 17.999 1.00 40.22 ? 152 TYR A CA 1 ATOM 739 C C . TYR A 1 106 ? -2.411 44.566 17.688 1.00 39.50 ? 152 TYR A C 1 ATOM 740 O O . TYR A 1 106 ? -2.657 43.559 17.001 1.00 39.14 ? 152 TYR A O 1 ATOM 741 C CB . TYR A 1 106 ? -3.498 46.731 16.977 1.00 41.51 ? 152 TYR A CB 1 ATOM 742 C CG . TYR A 1 106 ? -3.322 46.263 15.541 1.00 42.99 ? 152 TYR A CG 1 ATOM 743 C CD1 . TYR A 1 106 ? -4.365 45.626 14.864 1.00 43.99 ? 152 TYR A CD1 1 ATOM 744 C CD2 . TYR A 1 106 ? -2.103 46.448 14.868 1.00 45.08 ? 152 TYR A CD2 1 ATOM 745 C CE1 . TYR A 1 106 ? -4.213 45.191 13.549 1.00 45.08 ? 152 TYR A CE1 1 ATOM 746 C CE2 . TYR A 1 106 ? -1.933 46.013 13.555 1.00 45.69 ? 152 TYR A CE2 1 ATOM 747 C CZ . TYR A 1 106 ? -2.993 45.386 12.897 1.00 46.37 ? 152 TYR A CZ 1 ATOM 748 O OH . TYR A 1 106 ? -2.835 44.957 11.590 1.00 44.98 ? 152 TYR A OH 1 ATOM 749 N N . GLU A 1 107 ? -1.194 44.829 18.194 1.00 38.36 ? 153 GLU A N 1 ATOM 750 C CA . GLU A 1 107 ? -0.027 43.960 17.938 1.00 37.49 ? 153 GLU A CA 1 ATOM 751 C C . GLU A 1 107 ? 0.003 42.728 18.847 1.00 36.76 ? 153 GLU A C 1 ATOM 752 O O . GLU A 1 107 ? 0.953 42.535 19.626 1.00 35.53 ? 153 GLU A O 1 ATOM 753 C CB . GLU A 1 107 ? 1.281 44.737 18.110 1.00 37.83 ? 153 GLU A CB 1 ATOM 754 C CG . GLU A 1 107 ? 1.614 45.678 16.968 1.00 41.12 ? 153 GLU A CG 1 ATOM 755 C CD . GLU A 1 107 ? 3.125 45.839 16.769 1.00 45.57 ? 153 GLU A CD 1 ATOM 756 O OE1 . GLU A 1 107 ? 3.776 44.947 16.153 1.00 46.00 ? 153 GLU A OE1 1 ATOM 757 O OE2 . GLU A 1 107 ? 3.655 46.868 17.231 1.00 48.44 ? 153 GLU A OE2 1 ATOM 758 N N . VAL A 1 108 ? -1.034 41.900 18.749 1.00 35.40 ? 154 VAL A N 1 ATOM 759 C CA . VAL A 1 108 ? -1.205 40.750 19.646 1.00 35.06 ? 154 VAL A CA 1 ATOM 760 C C . VAL A 1 108 ? -0.074 39.743 19.466 1.00 33.78 ? 154 VAL A C 1 ATOM 761 O O . VAL A 1 108 ? 0.363 39.092 20.432 1.00 34.25 ? 154 VAL A O 1 ATOM 762 C CB . VAL A 1 108 ? -2.571 40.049 19.413 1.00 35.30 ? 154 VAL A CB 1 ATOM 763 C CG1 . VAL A 1 108 ? -3.702 40.966 19.862 1.00 36.75 ? 154 VAL A CG1 1 ATOM 764 C CG2 . VAL A 1 108 ? -2.733 39.696 17.949 1.00 35.81 ? 154 VAL A CG2 1 ATOM 765 N N . GLY A 1 109 ? 0.417 39.644 18.236 1.00 32.08 ? 155 GLY A N 1 ATOM 766 C CA . GLY A 1 109 ? 1.563 38.818 17.937 1.00 30.76 ? 155 GLY A CA 1 ATOM 767 C C . GLY A 1 109 ? 2.756 39.233 18.790 1.00 29.44 ? 155 GLY A C 1 ATOM 768 O O . GLY A 1 109 ? 3.316 38.406 19.491 1.00 28.94 ? 155 GLY A O 1 ATOM 769 N N . TYR A 1 110 ? 3.140 40.510 18.719 1.00 27.65 ? 156 TYR A N 1 ATOM 770 C CA . TYR A 1 110 ? 4.312 40.987 19.470 1.00 26.97 ? 156 TYR A CA 1 ATOM 771 C C . TYR A 1 110 ? 4.091 40.847 20.974 1.00 26.47 ? 156 TYR A C 1 ATOM 772 O O . TYR A 1 110 ? 4.984 40.401 21.708 1.00 24.55 ? 156 TYR A O 1 ATOM 773 C CB . TYR A 1 110 ? 4.676 42.436 19.113 1.00 26.07 ? 156 TYR A CB 1 ATOM 774 C CG . TYR A 1 110 ? 5.608 43.052 20.163 1.00 26.01 ? 156 TYR A CG 1 ATOM 775 C CD1 . TYR A 1 110 ? 6.965 42.708 20.204 1.00 23.65 ? 156 TYR A CD1 1 ATOM 776 C CD2 . TYR A 1 110 ? 5.117 43.940 21.127 1.00 26.38 ? 156 TYR A CD2 1 ATOM 777 C CE1 . TYR A 1 110 ? 7.820 43.246 21.183 1.00 21.03 ? 156 TYR A CE1 1 ATOM 778 C CE2 . TYR A 1 110 ? 5.959 44.495 22.120 1.00 23.95 ? 156 TYR A CE2 1 ATOM 779 C CZ . TYR A 1 110 ? 7.311 44.128 22.140 1.00 23.67 ? 156 TYR A CZ 1 ATOM 780 O OH . TYR A 1 110 ? 8.148 44.650 23.116 1.00 21.78 ? 156 TYR A OH 1 ATOM 781 N N . CYS A 1 111 ? 2.919 41.252 21.452 1.00 25.72 ? 157 CYS A N 1 ATOM 782 C CA . CYS A 1 111 ? 2.689 41.210 22.887 1.00 27.27 ? 157 CYS A CA 1 ATOM 783 C C . CYS A 1 111 ? 2.761 39.788 23.439 1.00 26.50 ? 157 CYS A C 1 ATOM 784 O O . CYS A 1 111 ? 3.280 39.555 24.545 1.00 26.32 ? 157 CYS A O 1 ATOM 785 C CB . CYS A 1 111 ? 1.398 41.942 23.275 1.00 28.80 ? 157 CYS A CB 1 ATOM 786 S SG . CYS A 1 111 ? 1.571 43.735 23.038 1.00 35.85 ? 157 CYS A SG 1 ATOM 787 N N . GLU A 1 112 ? 2.271 38.823 22.673 1.00 25.71 ? 158 GLU A N 1 ATOM 788 C CA . GLU A 1 112 ? 2.367 37.436 23.095 1.00 26.09 ? 158 GLU A CA 1 ATOM 789 C C . GLU A 1 112 ? 3.824 36.975 23.133 1.00 23.62 ? 158 GLU A C 1 ATOM 790 O O . GLU A 1 112 ? 4.225 36.280 24.083 1.00 23.97 ? 158 GLU A O 1 ATOM 791 C CB . GLU A 1 112 ? 1.573 36.531 22.145 1.00 26.88 ? 158 GLU A CB 1 ATOM 792 C CG . GLU A 1 112 ? 1.718 35.063 22.444 1.00 33.89 ? 158 GLU A CG 1 ATOM 793 C CD . GLU A 1 112 ? 0.994 34.190 21.411 1.00 43.62 ? 158 GLU A CD 1 ATOM 794 O OE1 . GLU A 1 112 ? 0.293 33.231 21.825 1.00 47.45 ? 158 GLU A OE1 1 ATOM 795 O OE2 . GLU A 1 112 ? 1.118 34.467 20.187 1.00 47.84 ? 158 GLU A OE2 1 ATOM 796 N N . LYS A 1 113 ? 4.593 37.343 22.114 1.00 21.83 ? 159 LYS A N 1 ATOM 797 C CA . LYS A 1 113 ? 6.024 36.996 22.068 1.00 21.77 ? 159 LYS A CA 1 ATOM 798 C C . LYS A 1 113 ? 6.776 37.622 23.229 1.00 20.22 ? 159 LYS A C 1 ATOM 799 O O . LYS A 1 113 ? 7.669 36.985 23.814 1.00 19.97 ? 159 LYS A O 1 ATOM 800 C CB . LYS A 1 113 ? 6.666 37.472 20.779 1.00 22.56 ? 159 LYS A CB 1 ATOM 801 C CG . LYS A 1 113 ? 6.299 36.591 19.602 1.00 28.17 ? 159 LYS A CG 1 ATOM 802 C CD . LYS A 1 113 ? 6.732 37.238 18.306 1.00 34.98 ? 159 LYS A CD 1 ATOM 803 C CE . LYS A 1 113 ? 8.056 36.699 17.856 1.00 39.62 ? 159 LYS A CE 1 ATOM 804 N NZ . LYS A 1 113 ? 8.213 36.905 16.371 1.00 44.24 ? 159 LYS A NZ 1 ATOM 805 N N . LEU A 1 114 ? 6.446 38.875 23.519 1.00 19.37 ? 160 LEU A N 1 ATOM 806 C CA . LEU A 1 114 ? 7.112 39.584 24.633 1.00 18.90 ? 160 LEU A CA 1 ATOM 807 C C . LEU A 1 114 ? 6.795 38.889 25.939 1.00 19.31 ? 160 LEU A C 1 ATOM 808 O O . LEU A 1 114 ? 7.677 38.625 26.765 1.00 16.99 ? 160 LEU A O 1 ATOM 809 C CB . LEU A 1 114 ? 6.680 41.047 24.692 1.00 18.99 ? 160 LEU A CB 1 ATOM 810 C CG . LEU A 1 114 ? 7.267 41.817 25.884 1.00 18.64 ? 160 LEU A CG 1 ATOM 811 C CD1 . LEU A 1 114 ? 8.832 41.849 25.806 1.00 18.64 ? 160 LEU A CD1 1 ATOM 812 C CD2 . LEU A 1 114 ? 6.687 43.235 25.941 1.00 17.36 ? 160 LEU A CD2 1 ATOM 813 N N . LYS A 1 115 ? 5.511 38.614 26.156 1.00 18.66 ? 161 LYS A N 1 ATOM 814 C CA . LYS A 1 115 ? 5.119 37.976 27.397 1.00 20.51 ? 161 LYS A CA 1 ATOM 815 C C . LYS A 1 115 ? 5.801 36.625 27.548 1.00 20.47 ? 161 LYS A C 1 ATOM 816 O O . LYS A 1 115 ? 6.255 36.268 28.637 1.00 20.47 ? 161 LYS A O 1 ATOM 817 C CB . LYS A 1 115 ? 3.583 37.803 27.489 1.00 21.31 ? 161 LYS A CB 1 ATOM 818 C CG . LYS A 1 115 ? 3.183 37.207 28.814 1.00 26.95 ? 161 LYS A CG 1 ATOM 819 C CD . LYS A 1 115 ? 1.681 37.094 28.977 1.00 36.45 ? 161 LYS A CD 1 ATOM 820 C CE . LYS A 1 115 ? 1.196 35.741 28.456 1.00 39.74 ? 161 LYS A CE 1 ATOM 821 N NZ . LYS A 1 115 ? -0.269 35.580 28.780 1.00 44.33 ? 161 LYS A NZ 1 ATOM 822 N N . ASN A 1 116 ? 5.866 35.864 26.460 1.00 19.70 ? 162 ASN A N 1 ATOM 823 C CA . ASN A 1 116 ? 6.483 34.553 26.512 1.00 20.26 ? 162 ASN A CA 1 ATOM 824 C C . ASN A 1 116 ? 7.989 34.662 26.842 1.00 18.87 ? 162 ASN A C 1 ATOM 825 O O . ASN A 1 116 ? 8.530 33.835 27.602 1.00 17.39 ? 162 ASN A O 1 ATOM 826 C CB . ASN A 1 116 ? 6.298 33.840 25.170 1.00 21.31 ? 162 ASN A CB 1 ATOM 827 C CG . ASN A 1 116 ? 4.874 33.275 25.017 1.00 25.17 ? 162 ASN A CG 1 ATOM 828 O OD1 . ASN A 1 116 ? 4.150 33.119 26.016 1.00 27.91 ? 162 ASN A OD1 1 ATOM 829 N ND2 . ASN A 1 116 ? 4.485 32.948 23.789 1.00 29.46 ? 162 ASN A ND2 1 ATOM 830 N N . PHE A 1 117 ? 8.625 35.656 26.231 1.00 17.90 ? 163 PHE A N 1 ATOM 831 C CA . PHE A 1 117 ? 10.068 35.897 26.412 1.00 16.86 ? 163 PHE A CA 1 ATOM 832 C C . PHE A 1 117 ? 10.305 36.234 27.872 1.00 16.59 ? 163 PHE A C 1 ATOM 833 O O . PHE A 1 117 ? 11.162 35.616 28.534 1.00 15.79 ? 163 PHE A O 1 ATOM 834 C CB . PHE A 1 117 ? 10.552 37.033 25.508 1.00 17.45 ? 163 PHE A CB 1 ATOM 835 C CG . PHE A 1 117 ? 12.024 37.329 25.658 1.00 15.65 ? 163 PHE A CG 1 ATOM 836 C CD1 . PHE A 1 117 ? 12.936 36.838 24.740 1.00 18.26 ? 163 PHE A CD1 1 ATOM 837 C CD2 . PHE A 1 117 ? 12.486 38.056 26.765 1.00 18.88 ? 163 PHE A CD2 1 ATOM 838 C CE1 . PHE A 1 117 ? 14.325 37.125 24.885 1.00 21.08 ? 163 PHE A CE1 1 ATOM 839 C CE2 . PHE A 1 117 ? 13.879 38.328 26.929 1.00 20.13 ? 163 PHE A CE2 1 ATOM 840 C CZ . PHE A 1 117 ? 14.773 37.866 26.003 1.00 19.50 ? 163 PHE A CZ 1 ATOM 841 N N . LEU A 1 118 ? 9.542 37.196 28.392 1.00 16.05 ? 164 LEU A N 1 ATOM 842 C CA . LEU A 1 118 ? 9.739 37.623 29.798 1.00 16.32 ? 164 LEU A CA 1 ATOM 843 C C . LEU A 1 118 ? 9.428 36.504 30.785 1.00 16.97 ? 164 LEU A C 1 ATOM 844 O O . LEU A 1 118 ? 10.169 36.265 31.734 1.00 16.28 ? 164 LEU A O 1 ATOM 845 C CB . LEU A 1 118 ? 8.896 38.857 30.095 1.00 15.39 ? 164 LEU A CB 1 ATOM 846 C CG . LEU A 1 118 ? 9.329 40.116 29.335 1.00 16.85 ? 164 LEU A CG 1 ATOM 847 C CD1 . LEU A 1 118 ? 8.287 41.232 29.514 1.00 18.56 ? 164 LEU A CD1 1 ATOM 848 C CD2 . LEU A 1 118 ? 10.774 40.597 29.779 1.00 17.07 ? 164 LEU A CD2 1 ATOM 849 N N . GLU A 1 119 ? 8.316 35.787 30.572 1.00 16.72 ? 165 GLU A N 1 ATOM 850 C CA . GLU A 1 119 ? 8.015 34.669 31.485 1.00 17.39 ? 165 GLU A CA 1 ATOM 851 C C . GLU A 1 119 ? 9.137 33.601 31.483 1.00 16.71 ? 165 GLU A C 1 ATOM 852 O O . GLU A 1 119 ? 9.514 33.063 32.549 1.00 17.22 ? 165 GLU A O 1 ATOM 853 C CB . GLU A 1 119 ? 6.646 34.046 31.152 1.00 18.57 ? 165 GLU A CB 1 ATOM 854 C CG . GLU A 1 119 ? 5.485 34.986 31.473 1.00 21.93 ? 165 GLU A CG 1 ATOM 855 C CD . GLU A 1 119 ? 4.113 34.382 31.134 1.00 33.02 ? 165 GLU A CD 1 ATOM 856 O OE1 . GLU A 1 119 ? 3.110 34.785 31.785 1.00 37.49 ? 165 GLU A OE1 1 ATOM 857 O OE2 . GLU A 1 119 ? 4.047 33.515 30.222 1.00 33.97 ? 165 GLU A OE2 1 ATOM 858 N N . ALA A 1 120 ? 9.667 33.287 30.304 1.00 16.39 ? 166 ALA A N 1 ATOM 859 C CA . ALA A 1 120 ? 10.730 32.283 30.220 1.00 15.30 ? 166 ALA A CA 1 ATOM 860 C C . ALA A 1 120 ? 12.034 32.793 30.883 1.00 15.07 ? 166 ALA A C 1 ATOM 861 O O . ALA A 1 120 ? 12.762 32.032 31.544 1.00 15.27 ? 166 ALA A O 1 ATOM 862 C CB . ALA A 1 120 ? 10.987 31.940 28.763 1.00 16.46 ? 166 ALA A CB 1 ATOM 863 N N . ASN A 1 121 ? 12.303 34.075 30.694 1.00 14.49 ? 167 ASN A N 1 ATOM 864 C CA . ASN A 1 121 ? 13.526 34.671 31.283 1.00 13.87 ? 167 ASN A CA 1 ATOM 865 C C . ASN A 1 121 ? 13.433 34.699 32.813 1.00 13.68 ? 167 ASN A C 1 ATOM 866 O O . ASN A 1 121 ? 14.381 34.377 33.542 1.00 13.12 ? 167 ASN A O 1 ATOM 867 C CB . ASN A 1 121 ? 13.681 36.086 30.715 1.00 14.24 ? 167 ASN A CB 1 ATOM 868 C CG . ASN A 1 121 ? 14.900 36.791 31.285 1.00 15.43 ? 167 ASN A CG 1 ATOM 869 O OD1 . ASN A 1 121 ? 14.785 37.773 32.024 1.00 15.94 ? 167 ASN A OD1 1 ATOM 870 N ND2 . ASN A 1 121 ? 16.078 36.235 30.976 1.00 13.00 ? 167 ASN A ND2 1 ATOM 871 N N . LEU A 1 122 ? 12.273 35.086 33.326 1.00 14.06 ? 168 LEU A N 1 ATOM 872 C CA . LEU A 1 122 ? 12.051 35.089 34.779 1.00 14.58 ? 168 LEU A CA 1 ATOM 873 C C . LEU A 1 122 ? 12.141 33.662 35.327 1.00 14.64 ? 168 LEU A C 1 ATOM 874 O O . LEU A 1 122 ? 12.728 33.432 36.373 1.00 15.01 ? 168 LEU A O 1 ATOM 875 C CB . LEU A 1 122 ? 10.692 35.707 35.117 1.00 14.95 ? 168 LEU A CB 1 ATOM 876 C CG . LEU A 1 122 ? 10.564 37.208 34.717 1.00 14.97 ? 168 LEU A CG 1 ATOM 877 C CD1 . LEU A 1 122 ? 9.112 37.658 34.585 1.00 19.30 ? 168 LEU A CD1 1 ATOM 878 C CD2 . LEU A 1 122 ? 11.370 38.114 35.712 1.00 17.27 ? 168 LEU A CD2 1 ATOM 879 N N . GLU A 1 123 ? 11.555 32.712 34.619 1.00 14.92 ? 169 GLU A N 1 ATOM 880 C CA . GLU A 1 123 ? 11.613 31.329 35.081 1.00 16.62 ? 169 GLU A CA 1 ATOM 881 C C . GLU A 1 123 ? 13.057 30.824 35.098 1.00 15.32 ? 169 GLU A C 1 ATOM 882 O O . GLU A 1 123 ? 13.457 30.112 36.028 1.00 14.95 ? 169 GLU A O 1 ATOM 883 C CB . GLU A 1 123 ? 10.750 30.441 34.183 1.00 18.72 ? 169 GLU A CB 1 ATOM 884 C CG . GLU A 1 123 ? 11.013 28.949 34.320 1.00 24.00 ? 169 GLU A CG 1 ATOM 885 C CD . GLU A 1 123 ? 10.825 28.423 35.729 1.00 32.64 ? 169 GLU A CD 1 ATOM 886 O OE1 . GLU A 1 123 ? 10.011 29.018 36.472 1.00 35.65 ? 169 GLU A OE1 1 ATOM 887 O OE2 . GLU A 1 123 ? 11.494 27.403 36.088 1.00 36.01 ? 169 GLU A OE2 1 ATOM 888 N N . TRP A 1 124 ? 13.809 31.158 34.052 1.00 14.34 ? 170 TRP A N 1 ATOM 889 C CA . TRP A 1 124 ? 15.209 30.743 33.933 1.00 14.56 ? 170 TRP A CA 1 ATOM 890 C C . TRP A 1 124 ? 15.992 31.292 35.152 1.00 15.31 ? 170 TRP A C 1 ATOM 891 O O . TRP A 1 124 ? 16.768 30.555 35.788 1.00 14.85 ? 170 TRP A O 1 ATOM 892 C CB . TRP A 1 124 ? 15.819 31.212 32.595 1.00 14.93 ? 170 TRP A CB 1 ATOM 893 C CG . TRP A 1 124 ? 17.318 30.913 32.601 1.00 15.31 ? 170 TRP A CG 1 ATOM 894 C CD1 . TRP A 1 124 ? 17.920 29.686 32.661 1.00 17.55 ? 170 TRP A CD1 1 ATOM 895 C CD2 . TRP A 1 124 ? 18.372 31.886 32.707 1.00 13.69 ? 170 TRP A CD2 1 ATOM 896 N NE1 . TRP A 1 124 ? 19.301 29.827 32.737 1.00 16.50 ? 170 TRP A NE1 1 ATOM 897 C CE2 . TRP A 1 124 ? 19.595 31.172 32.779 1.00 16.92 ? 170 TRP A CE2 1 ATOM 898 C CE3 . TRP A 1 124 ? 18.396 33.299 32.745 1.00 16.77 ? 170 TRP A CE3 1 ATOM 899 C CZ2 . TRP A 1 124 ? 20.830 31.829 32.875 1.00 16.02 ? 170 TRP A CZ2 1 ATOM 900 C CZ3 . TRP A 1 124 ? 19.613 33.934 32.841 1.00 14.25 ? 170 TRP A CZ3 1 ATOM 901 C CH2 . TRP A 1 124 ? 20.813 33.193 32.913 1.00 15.44 ? 170 TRP A CH2 1 ATOM 902 N N . MET A 1 125 ? 15.796 32.565 35.489 1.00 13.00 ? 171 MET A N 1 ATOM 903 C CA . MET A 1 125 ? 16.459 33.095 36.678 1.00 15.06 ? 171 MET A CA 1 ATOM 904 C C . MET A 1 125 ? 16.071 32.368 37.959 1.00 14.40 ? 171 MET A C 1 ATOM 905 O O . MET A 1 125 ? 16.936 32.066 38.778 1.00 14.26 ? 171 MET A O 1 ATOM 906 C CB . MET A 1 125 ? 16.226 34.606 36.820 1.00 15.32 ? 171 MET A CB 1 ATOM 907 C CG . MET A 1 125 ? 16.929 35.387 35.694 1.00 14.33 ? 171 MET A CG 1 ATOM 908 S SD . MET A 1 125 ? 16.863 37.171 36.030 1.00 15.23 ? 171 MET A SD 1 ATOM 909 C CE . MET A 1 125 ? 15.089 37.489 35.824 1.00 15.87 ? 171 MET A CE 1 ATOM 910 N N . GLN A 1 126 ? 14.776 32.086 38.131 1.00 14.85 ? 172 GLN A N 1 ATOM 911 C CA . GLN A 1 126 ? 14.314 31.351 39.335 1.00 14.37 ? 172 GLN A CA 1 ATOM 912 C C . GLN A 1 126 ? 14.989 29.984 39.387 1.00 14.60 ? 172 GLN A C 1 ATOM 913 O O . GLN A 1 126 ? 15.429 29.541 40.462 1.00 14.99 ? 172 GLN A O 1 ATOM 914 C CB . GLN A 1 126 ? 12.785 31.181 39.332 1.00 14.96 ? 172 GLN A CB 1 ATOM 915 C CG . GLN A 1 126 ? 12.009 32.524 39.556 1.00 14.32 ? 172 GLN A CG 1 ATOM 916 C CD . GLN A 1 126 ? 12.257 33.143 40.928 1.00 18.78 ? 172 GLN A CD 1 ATOM 917 O OE1 . GLN A 1 126 ? 12.169 32.468 41.944 1.00 21.74 ? 172 GLN A OE1 1 ATOM 918 N NE2 . GLN A 1 126 ? 12.548 34.446 40.961 1.00 19.14 ? 172 GLN A NE2 1 ATOM 919 N N . ARG A 1 127 ? 15.078 29.312 38.242 1.00 14.50 ? 173 ARG A N 1 ATOM 920 C CA . ARG A 1 127 ? 15.763 28.006 38.211 1.00 15.41 ? 173 ARG A CA 1 ATOM 921 C C . ARG A 1 127 ? 17.235 28.106 38.577 1.00 14.84 ? 173 ARG A C 1 ATOM 922 O O . ARG A 1 127 ? 17.740 27.292 39.351 1.00 15.50 ? 173 ARG A O 1 ATOM 923 C CB . ARG A 1 127 ? 15.604 27.348 36.846 1.00 16.69 ? 173 ARG A CB 1 ATOM 924 C CG . ARG A 1 127 ? 16.045 25.871 36.904 1.00 20.76 ? 173 ARG A CG 1 ATOM 925 C CD . ARG A 1 127 ? 15.092 25.003 37.781 1.00 30.48 ? 173 ARG A CD 1 ATOM 926 N NE . ARG A 1 127 ? 15.531 23.597 37.759 1.00 37.76 ? 173 ARG A NE 1 ATOM 927 C CZ . ARG A 1 127 ? 15.537 22.791 38.810 1.00 40.44 ? 173 ARG A CZ 1 ATOM 928 N NH1 . ARG A 1 127 ? 15.133 23.248 39.998 1.00 42.94 ? 173 ARG A NH1 1 ATOM 929 N NH2 . ARG A 1 127 ? 15.964 21.527 38.678 1.00 45.22 ? 173 ARG A NH2 1 ATOM 930 N N . GLU A 1 128 ? 17.926 29.107 38.022 1.00 14.08 ? 174 GLU A N 1 ATOM 931 C CA . GLU A 1 128 ? 19.347 29.285 38.353 1.00 14.58 ? 174 GLU A CA 1 ATOM 932 C C . GLU A 1 128 ? 19.519 29.525 39.838 1.00 14.54 ? 174 GLU A C 1 ATOM 933 O O . GLU A 1 128 ? 20.458 29.011 40.438 1.00 14.88 ? 174 GLU A O 1 ATOM 934 C CB . GLU A 1 128 ? 19.975 30.415 37.548 1.00 14.69 ? 174 GLU A CB 1 ATOM 935 C CG . GLU A 1 128 ? 20.119 30.062 36.044 1.00 14.40 ? 174 GLU A CG 1 ATOM 936 C CD . GLU A 1 128 ? 21.325 29.133 35.736 1.00 19.23 ? 174 GLU A CD 1 ATOM 937 O OE1 . GLU A 1 128 ? 21.901 28.487 36.641 1.00 20.34 ? 174 GLU A OE1 1 ATOM 938 O OE2 . GLU A 1 128 ? 21.700 29.075 34.546 1.00 22.87 ? 174 GLU A OE2 1 ATOM 939 N N . MET A 1 129 ? 18.601 30.271 40.458 1.00 14.46 ? 175 MET A N 1 ATOM 940 C CA . MET A 1 129 ? 18.746 30.516 41.892 1.00 16.43 ? 175 MET A CA 1 ATOM 941 C C . MET A 1 129 ? 18.594 29.227 42.679 1.00 17.57 ? 175 MET A C 1 ATOM 942 O O . MET A 1 129 ? 19.363 28.969 43.609 1.00 18.31 ? 175 MET A O 1 ATOM 943 C CB . MET A 1 129 ? 17.712 31.528 42.376 1.00 17.49 ? 175 MET A CB 1 ATOM 944 C CG . MET A 1 129 ? 17.966 32.902 41.820 1.00 20.26 ? 175 MET A CG 1 ATOM 945 S SD . MET A 1 129 ? 16.459 33.934 42.036 1.00 26.04 ? 175 MET A SD 1 ATOM 946 C CE . MET A 1 129 ? 16.955 35.257 41.018 1.00 26.18 ? 175 MET A CE 1 ATOM 947 N N . GLU A 1 130 ? 17.608 28.427 42.292 1.00 17.69 ? 176 GLU A N 1 ATOM 948 C CA . GLU A 1 130 ? 17.348 27.154 42.970 1.00 19.76 ? 176 GLU A CA 1 ATOM 949 C C . GLU A 1 130 ? 18.548 26.204 42.813 1.00 18.81 ? 176 GLU A C 1 ATOM 950 O O . GLU A 1 130 ? 18.924 25.483 43.737 1.00 19.36 ? 176 GLU A O 1 ATOM 951 C CB . GLU A 1 130 ? 16.133 26.472 42.326 1.00 20.89 ? 176 GLU A CB 1 ATOM 952 C CG . GLU A 1 130 ? 14.817 27.095 42.679 1.00 27.97 ? 176 GLU A CG 1 ATOM 953 C CD . GLU A 1 130 ? 13.644 26.359 42.028 1.00 36.85 ? 176 GLU A CD 1 ATOM 954 O OE1 . GLU A 1 130 ? 13.855 25.687 40.982 1.00 38.53 ? 176 GLU A OE1 1 ATOM 955 O OE2 . GLU A 1 130 ? 12.510 26.462 42.573 1.00 41.32 ? 176 GLU A OE2 1 ATOM 956 N N . LEU A 1 131 ? 19.108 26.183 41.610 1.00 17.94 ? 177 LEU A N 1 ATOM 957 C CA . LEU A 1 131 ? 20.259 25.346 41.275 1.00 18.38 ? 177 LEU A CA 1 ATOM 958 C C . LEU A 1 131 ? 21.602 25.833 41.833 1.00 18.26 ? 177 LEU A C 1 ATOM 959 O O . LEU A 1 131 ? 22.606 25.110 41.781 1.00 19.00 ? 177 LEU A O 1 ATOM 960 C CB . LEU A 1 131 ? 20.388 25.244 39.759 1.00 17.80 ? 177 LEU A CB 1 ATOM 961 C CG . LEU A 1 131 ? 19.293 24.419 39.081 1.00 20.82 ? 177 LEU A CG 1 ATOM 962 C CD1 . LEU A 1 131 ? 19.561 24.527 37.599 1.00 24.17 ? 177 LEU A CD1 1 ATOM 963 C CD2 . LEU A 1 131 ? 19.316 22.978 39.554 1.00 23.42 ? 177 LEU A CD2 1 ATOM 964 N N . ASN A 1 132 ? 21.645 27.055 42.349 1.00 16.12 ? 178 ASN A N 1 ATOM 965 C CA . ASN A 1 132 ? 22.901 27.657 42.787 1.00 15.85 ? 178 ASN A CA 1 ATOM 966 C C . ASN A 1 132 ? 22.725 28.419 44.083 1.00 17.61 ? 178 ASN A C 1 ATOM 967 O O . ASN A 1 132 ? 23.007 29.605 44.147 1.00 17.30 ? 178 ASN A O 1 ATOM 968 C CB . ASN A 1 132 ? 23.440 28.580 41.679 1.00 15.13 ? 178 ASN A CB 1 ATOM 969 C CG . ASN A 1 132 ? 23.782 27.799 40.434 1.00 17.60 ? 178 ASN A CG 1 ATOM 970 O OD1 . ASN A 1 132 ? 24.825 27.160 40.386 1.00 18.74 ? 178 ASN A OD1 1 ATOM 971 N ND2 . ASN A 1 132 ? 22.897 27.805 39.440 1.00 14.93 ? 178 ASN A ND2 1 ATOM 972 N N . PRO A 1 133 ? 22.277 27.721 45.137 1.00 18.20 ? 179 PRO A N 1 ATOM 973 C CA . PRO A 1 133 ? 21.983 28.455 46.376 1.00 19.17 ? 179 PRO A CA 1 ATOM 974 C C . PRO A 1 133 ? 23.250 29.044 47.013 1.00 19.66 ? 179 PRO A C 1 ATOM 975 O O . PRO A 1 133 ? 23.156 29.922 47.876 1.00 20.11 ? 179 PRO A O 1 ATOM 976 C CB . PRO A 1 133 ? 21.345 27.376 47.272 1.00 19.37 ? 179 PRO A CB 1 ATOM 977 C CG . PRO A 1 133 ? 21.942 26.059 46.752 1.00 19.52 ? 179 PRO A CG 1 ATOM 978 C CD . PRO A 1 133 ? 21.982 26.269 45.254 1.00 18.97 ? 179 PRO A CD 1 ATOM 979 N N . ASP A 1 134 ? 24.441 28.583 46.618 1.00 18.29 ? 180 ASP A N 1 ATOM 980 C CA . ASP A 1 134 ? 25.656 29.166 47.212 1.00 19.21 ? 180 ASP A CA 1 ATOM 981 C C . ASP A 1 134 ? 26.359 30.214 46.357 1.00 17.91 ? 180 ASP A C 1 ATOM 982 O O . ASP A 1 134 ? 27.423 30.705 46.736 1.00 17.75 ? 180 ASP A O 1 ATOM 983 C CB . ASP A 1 134 ? 26.633 28.070 47.635 1.00 20.68 ? 180 ASP A CB 1 ATOM 984 C CG . ASP A 1 134 ? 26.015 27.138 48.659 1.00 25.43 ? 180 ASP A CG 1 ATOM 985 O OD1 . ASP A 1 134 ? 25.395 27.629 49.626 1.00 27.26 ? 180 ASP A OD1 1 ATOM 986 O OD2 . ASP A 1 134 ? 26.091 25.919 48.458 1.00 33.08 ? 180 ASP A OD2 1 ATOM 987 N N . SER A 1 135 ? 25.769 30.580 45.214 1.00 17.03 ? 181 SER A N 1 ATOM 988 C CA . SER A 1 135 ? 26.390 31.549 44.287 1.00 16.33 ? 181 SER A CA 1 ATOM 989 C C . SER A 1 135 ? 26.203 32.998 44.741 1.00 16.79 ? 181 SER A C 1 ATOM 990 O O . SER A 1 135 ? 25.051 33.427 44.899 1.00 16.44 ? 181 SER A O 1 ATOM 991 C CB . SER A 1 135 ? 25.732 31.431 42.896 1.00 17.13 ? 181 SER A CB 1 ATOM 992 O OG . SER A 1 135 ? 26.083 32.534 42.055 1.00 15.34 ? 181 SER A OG 1 ATOM 993 N N . PRO A 1 136 ? 27.299 33.758 44.905 1.00 16.86 ? 182 PRO A N 1 ATOM 994 C CA . PRO A 1 136 ? 27.145 35.228 45.183 1.00 16.20 ? 182 PRO A CA 1 ATOM 995 C C . PRO A 1 136 ? 26.431 35.963 44.055 1.00 16.13 ? 182 PRO A C 1 ATOM 996 O O . PRO A 1 136 ? 25.570 36.809 44.327 1.00 15.95 ? 182 PRO A O 1 ATOM 997 C CB . PRO A 1 136 ? 28.592 35.728 45.282 1.00 17.67 ? 182 PRO A CB 1 ATOM 998 C CG . PRO A 1 136 ? 29.360 34.463 45.777 1.00 17.75 ? 182 PRO A CG 1 ATOM 999 C CD . PRO A 1 136 ? 28.711 33.336 44.961 1.00 16.80 ? 182 PRO A CD 1 ATOM 1000 N N . TYR A 1 137 ? 26.747 35.605 42.808 1.00 14.21 ? 183 TYR A N 1 ATOM 1001 C CA . TYR A 1 137 ? 26.111 36.271 41.665 1.00 14.43 ? 183 TYR A CA 1 ATOM 1002 C C . TYR A 1 137 ? 24.612 36.102 41.736 1.00 13.80 ? 183 TYR A C 1 ATOM 1003 O O . TYR A 1 137 ? 23.864 37.083 41.623 1.00 13.98 ? 183 TYR A O 1 ATOM 1004 C CB . TYR A 1 137 ? 26.646 35.737 40.337 1.00 13.21 ? 183 TYR A CB 1 ATOM 1005 C CG . TYR A 1 137 ? 26.045 36.457 39.151 1.00 13.40 ? 183 TYR A CG 1 ATOM 1006 C CD1 . TYR A 1 137 ? 26.555 37.684 38.707 1.00 14.25 ? 183 TYR A CD1 1 ATOM 1007 C CD2 . TYR A 1 137 ? 24.902 35.950 38.522 1.00 15.04 ? 183 TYR A CD2 1 ATOM 1008 C CE1 . TYR A 1 137 ? 25.987 38.337 37.611 1.00 11.77 ? 183 TYR A CE1 1 ATOM 1009 C CE2 . TYR A 1 137 ? 24.341 36.577 37.410 1.00 13.84 ? 183 TYR A CE2 1 ATOM 1010 C CZ . TYR A 1 137 ? 24.861 37.777 36.984 1.00 14.17 ? 183 TYR A CZ 1 ATOM 1011 O OH . TYR A 1 137 ? 24.267 38.376 35.895 1.00 15.64 ? 183 TYR A OH 1 ATOM 1012 N N . TRP A 1 138 ? 24.150 34.856 41.850 1.00 12.97 ? 184 TRP A N 1 ATOM 1013 C CA . TRP A 1 138 ? 22.715 34.615 41.847 1.00 14.05 ? 184 TRP A CA 1 ATOM 1014 C C . TRP A 1 138 ? 22.059 35.129 43.127 1.00 13.82 ? 184 TRP A C 1 ATOM 1015 O O . TRP A 1 138 ? 20.881 35.465 43.093 1.00 14.71 ? 184 TRP A O 1 ATOM 1016 C CB . TRP A 1 138 ? 22.412 33.113 41.612 1.00 14.42 ? 184 TRP A CB 1 ATOM 1017 C CG . TRP A 1 138 ? 22.709 32.788 40.142 1.00 14.38 ? 184 TRP A CG 1 ATOM 1018 C CD1 . TRP A 1 138 ? 23.770 32.065 39.644 1.00 15.70 ? 184 TRP A CD1 1 ATOM 1019 C CD2 . TRP A 1 138 ? 21.986 33.277 39.010 1.00 15.27 ? 184 TRP A CD2 1 ATOM 1020 N NE1 . TRP A 1 138 ? 23.727 32.047 38.256 1.00 15.10 ? 184 TRP A NE1 1 ATOM 1021 C CE2 . TRP A 1 138 ? 22.645 32.785 37.841 1.00 14.32 ? 184 TRP A CE2 1 ATOM 1022 C CE3 . TRP A 1 138 ? 20.829 34.066 38.862 1.00 14.37 ? 184 TRP A CE3 1 ATOM 1023 C CZ2 . TRP A 1 138 ? 22.185 33.056 36.542 1.00 14.40 ? 184 TRP A CZ2 1 ATOM 1024 C CZ3 . TRP A 1 138 ? 20.382 34.356 37.559 1.00 15.64 ? 184 TRP A CZ3 1 ATOM 1025 C CH2 . TRP A 1 138 ? 21.051 33.837 36.418 1.00 14.95 ? 184 TRP A CH2 1 ATOM 1026 N N . HIS A 1 139 ? 22.821 35.224 44.224 1.00 13.91 ? 185 HIS A N 1 ATOM 1027 C CA . HIS A 1 139 ? 22.296 35.898 45.444 1.00 13.61 ? 185 HIS A CA 1 ATOM 1028 C C . HIS A 1 139 ? 21.972 37.366 45.136 1.00 13.76 ? 185 HIS A C 1 ATOM 1029 O O . HIS A 1 139 ? 20.915 37.861 45.507 1.00 13.96 ? 185 HIS A O 1 ATOM 1030 C CB . HIS A 1 139 ? 23.303 35.825 46.581 1.00 13.46 ? 185 HIS A CB 1 ATOM 1031 C CG . HIS A 1 139 ? 22.844 36.520 47.829 1.00 15.04 ? 185 HIS A CG 1 ATOM 1032 N ND1 . HIS A 1 139 ? 21.720 36.132 48.517 1.00 17.30 ? 185 HIS A ND1 1 ATOM 1033 C CD2 . HIS A 1 139 ? 23.375 37.565 48.515 1.00 16.19 ? 185 HIS A CD2 1 ATOM 1034 C CE1 . HIS A 1 139 ? 21.568 36.907 49.587 1.00 18.87 ? 185 HIS A CE1 1 ATOM 1035 N NE2 . HIS A 1 139 ? 22.559 37.787 49.606 1.00 17.56 ? 185 HIS A NE2 1 ATOM 1036 N N . GLN A 1 140 ? 22.849 38.042 44.411 1.00 13.85 ? 186 GLN A N 1 ATOM 1037 C CA . GLN A 1 140 ? 22.611 39.479 44.096 1.00 13.44 ? 186 GLN A CA 1 ATOM 1038 C C . GLN A 1 140 ? 21.425 39.620 43.153 1.00 12.99 ? 186 GLN A C 1 ATOM 1039 O O . GLN A 1 140 ? 20.630 40.570 43.270 1.00 12.49 ? 186 GLN A O 1 ATOM 1040 C CB . GLN A 1 140 ? 23.843 40.079 43.428 1.00 13.61 ? 186 GLN A CB 1 ATOM 1041 C CG . GLN A 1 140 ? 25.092 40.090 44.314 1.00 14.88 ? 186 GLN A CG 1 ATOM 1042 C CD . GLN A 1 140 ? 24.826 40.700 45.670 1.00 18.58 ? 186 GLN A CD 1 ATOM 1043 O OE1 . GLN A 1 140 ? 24.155 41.705 45.777 1.00 20.77 ? 186 GLN A OE1 1 ATOM 1044 N NE2 . GLN A 1 140 ? 25.355 40.075 46.713 1.00 18.35 ? 186 GLN A NE2 1 ATOM 1045 N N . VAL A 1 141 ? 21.269 38.675 42.231 1.00 12.71 ? 187 VAL A N 1 ATOM 1046 C CA . VAL A 1 141 ? 20.116 38.736 41.320 1.00 12.46 ? 187 VAL A CA 1 ATOM 1047 C C . VAL A 1 141 ? 18.828 38.555 42.124 1.00 12.52 ? 187 VAL A C 1 ATOM 1048 O O . VAL A 1 141 ? 17.844 39.305 41.929 1.00 12.06 ? 187 VAL A O 1 ATOM 1049 C CB . VAL A 1 141 ? 20.239 37.688 40.205 1.00 12.22 ? 187 VAL A CB 1 ATOM 1050 C CG1 . VAL A 1 141 ? 18.932 37.609 39.372 1.00 13.31 ? 187 VAL A CG1 1 ATOM 1051 C CG2 . VAL A 1 141 ? 21.461 38.036 39.315 1.00 11.28 ? 187 VAL A CG2 1 ATOM 1052 N N . ARG A 1 142 ? 18.850 37.599 43.045 1.00 12.88 ? 188 ARG A N 1 ATOM 1053 C CA . ARG A 1 142 ? 17.669 37.355 43.865 1.00 13.33 ? 188 ARG A CA 1 ATOM 1054 C C . ARG A 1 142 ? 17.304 38.581 44.704 1.00 13.39 ? 188 ARG A C 1 ATOM 1055 O O . ARG A 1 142 ? 16.118 38.907 44.823 1.00 12.88 ? 188 ARG A O 1 ATOM 1056 C CB . ARG A 1 142 ? 17.845 36.132 44.761 1.00 14.02 ? 188 ARG A CB 1 ATOM 1057 C CG . ARG A 1 142 ? 16.519 35.711 45.403 1.00 15.35 ? 188 ARG A CG 1 ATOM 1058 C CD . ARG A 1 142 ? 16.616 34.254 45.878 1.00 17.37 ? 188 ARG A CD 1 ATOM 1059 N NE . ARG A 1 142 ? 15.306 33.768 46.330 1.00 20.48 ? 188 ARG A NE 1 ATOM 1060 C CZ . ARG A 1 142 ? 14.815 33.998 47.552 1.00 20.30 ? 188 ARG A CZ 1 ATOM 1061 N NH1 . ARG A 1 142 ? 15.521 34.677 48.447 1.00 20.09 ? 188 ARG A NH1 1 ATOM 1062 N NH2 . ARG A 1 142 ? 13.615 33.544 47.876 1.00 20.66 ? 188 ARG A NH2 1 ATOM 1063 N N . LEU A 1 143 ? 18.297 39.245 45.302 1.00 12.64 ? 189 LEU A N 1 ATOM 1064 C CA . LEU A 1 143 ? 18.006 40.478 46.044 1.00 13.74 ? 189 LEU A CA 1 ATOM 1065 C C . LEU A 1 143 ? 17.306 41.530 45.175 1.00 13.14 ? 189 LEU A C 1 ATOM 1066 O O . LEU A 1 143 ? 16.386 42.202 45.639 1.00 12.66 ? 189 LEU A O 1 ATOM 1067 C CB . LEU A 1 143 ? 19.271 41.074 46.637 1.00 12.25 ? 189 LEU A CB 1 ATOM 1068 C CG . LEU A 1 143 ? 19.975 40.174 47.646 1.00 13.87 ? 189 LEU A CG 1 ATOM 1069 C CD1 . LEU A 1 143 ? 21.216 40.947 48.146 1.00 15.96 ? 189 LEU A CD1 1 ATOM 1070 C CD2 . LEU A 1 143 ? 19.008 39.835 48.803 1.00 16.56 ? 189 LEU A CD2 1 ATOM 1071 N N . THR A 1 144 ? 17.745 41.654 43.929 1.00 12.76 ? 190 THR A N 1 ATOM 1072 C CA . THR A 1 144 ? 17.179 42.646 43.021 1.00 13.35 ? 190 THR A CA 1 ATOM 1073 C C . THR A 1 144 ? 15.717 42.295 42.760 1.00 13.05 ? 190 THR A C 1 ATOM 1074 O O . THR A 1 144 ? 14.819 43.148 42.843 1.00 12.84 ? 190 THR A O 1 ATOM 1075 C CB . THR A 1 144 ? 17.997 42.717 41.719 1.00 12.25 ? 190 THR A CB 1 ATOM 1076 O OG1 . THR A 1 144 ? 19.395 42.913 42.051 1.00 15.57 ? 190 THR A OG1 1 ATOM 1077 C CG2 . THR A 1 144 ? 17.480 43.910 40.839 1.00 15.20 ? 190 THR A CG2 1 ATOM 1078 N N . LEU A 1 145 ? 15.456 41.022 42.460 1.00 13.12 ? 191 LEU A N 1 ATOM 1079 C CA . LEU A 1 145 ? 14.098 40.642 42.145 1.00 13.60 ? 191 LEU A CA 1 ATOM 1080 C C . LEU A 1 145 ? 13.187 40.677 43.399 1.00 13.86 ? 191 LEU A C 1 ATOM 1081 O O . LEU A 1 145 ? 11.988 40.885 43.266 1.00 14.07 ? 191 LEU A O 1 ATOM 1082 C CB . LEU A 1 145 ? 14.097 39.269 41.523 1.00 13.73 ? 191 LEU A CB 1 ATOM 1083 C CG . LEU A 1 145 ? 14.758 39.287 40.110 1.00 14.86 ? 191 LEU A CG 1 ATOM 1084 C CD1 . LEU A 1 145 ? 14.961 37.823 39.620 1.00 17.90 ? 191 LEU A CD1 1 ATOM 1085 C CD2 . LEU A 1 145 ? 13.928 40.088 39.142 1.00 16.40 ? 191 LEU A CD2 1 ATOM 1086 N N . LEU A 1 146 ? 13.741 40.410 44.578 1.00 13.00 ? 192 LEU A N 1 ATOM 1087 C CA . LEU A 1 146 ? 12.936 40.542 45.839 1.00 13.40 ? 192 LEU A CA 1 ATOM 1088 C C . LEU A 1 146 ? 12.501 41.973 46.030 1.00 13.37 ? 192 LEU A C 1 ATOM 1089 O O . LEU A 1 146 ? 11.372 42.226 46.408 1.00 13.98 ? 192 LEU A O 1 ATOM 1090 C CB . LEU A 1 146 ? 13.767 40.102 47.041 1.00 13.43 ? 192 LEU A CB 1 ATOM 1091 C CG . LEU A 1 146 ? 13.833 38.572 47.222 1.00 14.77 ? 192 LEU A CG 1 ATOM 1092 C CD1 . LEU A 1 146 ? 14.921 38.236 48.269 1.00 15.42 ? 192 LEU A CD1 1 ATOM 1093 C CD2 . LEU A 1 146 ? 12.464 37.996 47.612 1.00 16.69 ? 192 LEU A CD2 1 ATOM 1094 N N . GLN A 1 147 ? 13.388 42.932 45.745 1.00 13.39 ? 193 GLN A N 1 ATOM 1095 C CA . GLN A 1 147 ? 13.029 44.355 45.866 1.00 14.34 ? 193 GLN A CA 1 ATOM 1096 C C . GLN A 1 147 ? 11.894 44.705 44.895 1.00 14.72 ? 193 GLN A C 1 ATOM 1097 O O . GLN A 1 147 ? 10.930 45.401 45.252 1.00 14.58 ? 193 GLN A O 1 ATOM 1098 C CB . GLN A 1 147 ? 14.266 45.217 45.624 1.00 14.01 ? 193 GLN A CB 1 ATOM 1099 C CG . GLN A 1 147 ? 14.075 46.686 45.959 1.00 16.38 ? 193 GLN A CG 1 ATOM 1100 C CD . GLN A 1 147 ? 15.333 47.499 45.690 1.00 21.32 ? 193 GLN A CD 1 ATOM 1101 O OE1 . GLN A 1 147 ? 16.358 46.950 45.252 1.00 24.20 ? 193 GLN A OE1 1 ATOM 1102 N NE2 . GLN A 1 147 ? 15.255 48.812 45.912 1.00 19.80 ? 193 GLN A NE2 1 ATOM 1103 N N . LEU A 1 148 ? 11.998 44.206 43.662 1.00 13.88 ? 194 LEU A N 1 ATOM 1104 C CA . LEU A 1 148 ? 10.910 44.414 42.712 1.00 14.04 ? 194 LEU A CA 1 ATOM 1105 C C . LEU A 1 148 ? 9.581 43.779 43.234 1.00 14.83 ? 194 LEU A C 1 ATOM 1106 O O . LEU A 1 148 ? 8.509 44.406 43.164 1.00 16.16 ? 194 LEU A O 1 ATOM 1107 C CB . LEU A 1 148 ? 11.284 43.821 41.350 1.00 15.21 ? 194 LEU A CB 1 ATOM 1108 C CG . LEU A 1 148 ? 10.179 43.919 40.262 1.00 14.09 ? 194 LEU A CG 1 ATOM 1109 C CD1 . LEU A 1 148 ? 9.794 45.354 39.993 1.00 16.15 ? 194 LEU A CD1 1 ATOM 1110 C CD2 . LEU A 1 148 ? 10.728 43.245 38.958 1.00 16.00 ? 194 LEU A CD2 1 ATOM 1111 N N . LYS A 1 149 ? 9.650 42.549 43.732 1.00 15.26 ? 195 LYS A N 1 ATOM 1112 C CA A LYS A 1 149 ? 8.448 41.872 44.275 0.50 15.19 ? 195 LYS A CA 1 ATOM 1113 C CA B LYS A 1 149 ? 8.447 41.875 44.265 0.50 15.70 ? 195 LYS A CA 1 ATOM 1114 C C . LYS A 1 149 ? 7.831 42.692 45.415 1.00 15.66 ? 195 LYS A C 1 ATOM 1115 O O . LYS A 1 149 ? 6.607 42.871 45.466 1.00 16.03 ? 195 LYS A O 1 ATOM 1116 C CB A LYS A 1 149 ? 8.775 40.468 44.766 0.50 15.66 ? 195 LYS A CB 1 ATOM 1117 C CB B LYS A 1 149 ? 8.779 40.457 44.718 0.50 16.48 ? 195 LYS A CB 1 ATOM 1118 C CG A LYS A 1 149 ? 7.513 39.663 45.222 0.50 15.10 ? 195 LYS A CG 1 ATOM 1119 C CG B LYS A 1 149 ? 7.532 39.564 45.008 0.50 18.36 ? 195 LYS A CG 1 ATOM 1120 C CD A LYS A 1 149 ? 7.870 38.276 45.759 0.50 15.46 ? 195 LYS A CD 1 ATOM 1121 C CD B LYS A 1 149 ? 6.618 39.476 43.795 0.50 22.62 ? 195 LYS A CD 1 ATOM 1122 C CE A LYS A 1 149 ? 6.599 37.384 45.858 0.50 16.30 ? 195 LYS A CE 1 ATOM 1123 C CE B LYS A 1 149 ? 5.579 38.354 43.910 0.50 26.54 ? 195 LYS A CE 1 ATOM 1124 N NZ A LYS A 1 149 ? 5.636 37.863 46.880 0.50 17.07 ? 195 LYS A NZ 1 ATOM 1125 N NZ B LYS A 1 149 ? 4.907 38.320 45.243 0.50 28.19 ? 195 LYS A NZ 1 ATOM 1126 N N . GLY A 1 150 ? 8.674 43.213 46.316 1.00 14.84 ? 196 GLY A N 1 ATOM 1127 C CA . GLY A 1 150 ? 8.159 44.022 47.468 1.00 15.46 ? 196 GLY A CA 1 ATOM 1128 C C . GLY A 1 150 ? 7.540 45.320 47.008 1.00 15.68 ? 196 GLY A C 1 ATOM 1129 O O . GLY A 1 150 ? 6.512 45.749 47.548 1.00 14.86 ? 196 GLY A O 1 ATOM 1130 N N . LEU A 1 151 ? 8.128 45.953 45.986 1.00 14.97 ? 197 LEU A N 1 ATOM 1131 C CA . LEU A 1 151 ? 7.544 47.174 45.425 1.00 17.34 ? 197 LEU A CA 1 ATOM 1132 C C . LEU A 1 151 ? 6.113 46.923 44.900 1.00 17.37 ? 197 LEU A C 1 ATOM 1133 O O . LEU A 1 151 ? 5.156 47.674 45.208 1.00 17.36 ? 197 LEU A O 1 ATOM 1134 C CB . LEU A 1 151 ? 8.437 47.713 44.294 1.00 15.88 ? 197 LEU A CB 1 ATOM 1135 C CG . LEU A 1 151 ? 8.120 49.078 43.694 1.00 20.79 ? 197 LEU A CG 1 ATOM 1136 C CD1 . LEU A 1 151 ? 8.719 50.129 44.593 1.00 20.24 ? 197 LEU A CD1 1 ATOM 1137 C CD2 . LEU A 1 151 ? 8.743 49.180 42.277 1.00 23.93 ? 197 LEU A CD2 1 ATOM 1138 N N . GLU A 1 152 ? 5.974 45.880 44.092 1.00 17.51 ? 198 GLU A N 1 ATOM 1139 C CA . GLU A 1 152 ? 4.673 45.577 43.519 1.00 19.63 ? 198 GLU A CA 1 ATOM 1140 C C . GLU A 1 152 ? 3.678 45.116 44.598 1.00 19.18 ? 198 GLU A C 1 ATOM 1141 O O . GLU A 1 152 ? 2.515 45.562 44.603 1.00 20.47 ? 198 GLU A O 1 ATOM 1142 C CB . GLU A 1 152 ? 4.822 44.502 42.448 1.00 20.81 ? 198 GLU A CB 1 ATOM 1143 C CG . GLU A 1 152 ? 3.562 44.348 41.592 1.00 24.67 ? 198 GLU A CG 1 ATOM 1144 C CD . GLU A 1 152 ? 3.773 43.383 40.442 1.00 32.18 ? 198 GLU A CD 1 ATOM 1145 O OE1 . GLU A 1 152 ? 3.325 42.214 40.572 1.00 37.04 ? 198 GLU A OE1 1 ATOM 1146 O OE2 . GLU A 1 152 ? 4.420 43.762 39.438 1.00 29.13 ? 198 GLU A OE2 1 ATOM 1147 N N . ASP A 1 153 ? 4.109 44.228 45.489 1.00 18.73 ? 199 ASP A N 1 ATOM 1148 C CA . ASP A 1 153 ? 3.211 43.694 46.537 1.00 19.44 ? 199 ASP A CA 1 ATOM 1149 C C . ASP A 1 153 ? 2.683 44.852 47.398 1.00 19.44 ? 199 ASP A C 1 ATOM 1150 O O . ASP A 1 153 ? 1.494 44.895 47.747 1.00 20.40 ? 199 ASP A O 1 ATOM 1151 C CB . ASP A 1 153 ? 3.932 42.682 47.449 1.00 18.92 ? 199 ASP A CB 1 ATOM 1152 C CG . ASP A 1 153 ? 4.179 41.325 46.786 1.00 21.95 ? 199 ASP A CG 1 ATOM 1153 O OD1 . ASP A 1 153 ? 3.637 41.057 45.674 1.00 23.66 ? 199 ASP A OD1 1 ATOM 1154 O OD2 . ASP A 1 153 ? 4.895 40.491 47.392 1.00 22.74 ? 199 ASP A OD2 1 ATOM 1155 N N . SER A 1 154 ? 3.571 45.755 47.791 1.00 18.78 ? 200 SER A N 1 ATOM 1156 C CA . SER A 1 154 ? 3.200 46.903 48.624 1.00 19.85 ? 200 SER A CA 1 ATOM 1157 C C . SER A 1 154 ? 2.239 47.842 47.888 1.00 21.41 ? 200 SER A C 1 ATOM 1158 O O . SER A 1 154 ? 1.260 48.331 48.472 1.00 20.93 ? 200 SER A O 1 ATOM 1159 C CB . SER A 1 154 ? 4.466 47.642 49.076 1.00 20.46 ? 200 SER A CB 1 ATOM 1160 O OG . SER A 1 154 ? 4.158 48.798 49.847 1.00 21.19 ? 200 SER A OG 1 ATOM 1161 N N . TYR A 1 155 ? 2.491 48.078 46.600 1.00 20.38 ? 201 TYR A N 1 ATOM 1162 C CA . TYR A 1 155 ? 1.592 48.905 45.816 1.00 22.40 ? 201 TYR A CA 1 ATOM 1163 C C . TYR A 1 155 ? 0.195 48.271 45.757 1.00 23.27 ? 201 TYR A C 1 ATOM 1164 O O . TYR A 1 155 ? -0.819 48.982 45.779 1.00 23.89 ? 201 TYR A O 1 ATOM 1165 C CB . TYR A 1 155 ? 2.138 49.087 44.403 1.00 21.77 ? 201 TYR A CB 1 ATOM 1166 C CG . TYR A 1 155 ? 1.326 50.047 43.556 1.00 20.95 ? 201 TYR A CG 1 ATOM 1167 C CD1 . TYR A 1 155 ? 1.514 51.425 43.653 1.00 21.37 ? 201 TYR A CD1 1 ATOM 1168 C CD2 . TYR A 1 155 ? 0.358 49.561 42.670 1.00 22.97 ? 201 TYR A CD2 1 ATOM 1169 C CE1 . TYR A 1 155 ? 0.762 52.326 42.844 1.00 23.28 ? 201 TYR A CE1 1 ATOM 1170 C CE2 . TYR A 1 155 ? -0.385 50.425 41.876 1.00 23.72 ? 201 TYR A CE2 1 ATOM 1171 C CZ . TYR A 1 155 ? -0.185 51.805 41.972 1.00 25.13 ? 201 TYR A CZ 1 ATOM 1172 O OH . TYR A 1 155 ? -0.946 52.651 41.177 1.00 25.84 ? 201 TYR A OH 1 ATOM 1173 N N . GLU A 1 156 ? 0.148 46.946 45.681 1.00 24.75 ? 202 GLU A N 1 ATOM 1174 C CA . GLU A 1 156 ? -1.128 46.223 45.584 1.00 26.61 ? 202 GLU A CA 1 ATOM 1175 C C . GLU A 1 156 ? -1.746 46.012 46.963 1.00 27.32 ? 202 GLU A C 1 ATOM 1176 O O . GLU A 1 156 ? -2.887 45.542 47.069 1.00 28.19 ? 202 GLU A O 1 ATOM 1177 C CB . GLU A 1 156 ? -0.949 44.887 44.873 1.00 27.14 ? 202 GLU A CB 1 ATOM 1178 C CG . GLU A 1 156 ? -0.460 45.017 43.452 1.00 30.86 ? 202 GLU A CG 1 ATOM 1179 C CD . GLU A 1 156 ? -0.087 43.685 42.820 1.00 34.50 ? 202 GLU A CD 1 ATOM 1180 O OE1 . GLU A 1 156 ? 0.156 42.693 43.553 1.00 38.90 ? 202 GLU A OE1 1 ATOM 1181 O OE2 . GLU A 1 156 ? -0.003 43.645 41.580 1.00 37.21 ? 202 GLU A OE2 1 ATOM 1182 N N . GLY A 1 157 ? -1.005 46.355 48.013 1.00 27.73 ? 203 GLY A N 1 ATOM 1183 C CA . GLY A 1 157 ? -1.521 46.309 49.388 1.00 28.48 ? 203 GLY A CA 1 ATOM 1184 C C . GLY A 1 157 ? -1.565 44.932 50.033 1.00 30.38 ? 203 GLY A C 1 ATOM 1185 O O . GLY A 1 157 ? -2.351 44.702 50.971 1.00 30.62 ? 203 GLY A O 1 ATOM 1186 N N . ARG A 1 158 ? -0.757 43.987 49.553 1.00 30.25 ? 204 ARG A N 1 ATOM 1187 C CA A ARG A 1 158 ? -0.725 42.664 50.178 0.50 30.68 ? 204 ARG A CA 1 ATOM 1188 C CA B ARG A 1 158 ? -0.742 42.652 50.143 0.50 30.40 ? 204 ARG A CA 1 ATOM 1189 C C . ARG A 1 158 ? 0.654 42.068 50.131 1.00 30.51 ? 204 ARG A C 1 ATOM 1190 O O . ARG A 1 158 ? 1.147 41.673 49.069 1.00 30.12 ? 204 ARG A O 1 ATOM 1191 C CB A ARG A 1 158 ? -1.772 41.700 49.594 0.50 31.69 ? 204 ARG A CB 1 ATOM 1192 C CB B ARG A 1 158 ? -1.733 41.725 49.422 0.50 31.19 ? 204 ARG A CB 1 ATOM 1193 C CG A ARG A 1 158 ? -1.401 41.011 48.290 0.50 33.18 ? 204 ARG A CG 1 ATOM 1194 C CG B ARG A 1 158 ? -3.168 42.270 49.401 0.50 31.47 ? 204 ARG A CG 1 ATOM 1195 C CD A ARG A 1 158 ? -2.646 40.400 47.653 0.50 36.94 ? 204 ARG A CD 1 ATOM 1196 C CD B ARG A 1 158 ? -4.159 41.285 48.816 0.50 32.70 ? 204 ARG A CD 1 ATOM 1197 N NE A ARG A 1 158 ? -3.527 41.465 47.201 0.50 37.99 ? 204 ARG A NE 1 ATOM 1198 N NE B ARG A 1 158 ? -5.508 41.845 48.809 0.50 33.70 ? 204 ARG A NE 1 ATOM 1199 C CZ A ARG A 1 158 ? -3.368 42.090 46.047 0.50 38.04 ? 204 ARG A CZ 1 ATOM 1200 C CZ B ARG A 1 158 ? -6.370 41.729 49.816 0.50 34.42 ? 204 ARG A CZ 1 ATOM 1201 N NH1 A ARG A 1 158 ? -4.193 43.067 45.704 0.50 37.64 ? 204 ARG A NH1 1 ATOM 1202 N NH1 B ARG A 1 158 ? -6.019 41.071 50.917 0.50 34.55 ? 204 ARG A NH1 1 ATOM 1203 N NH2 A ARG A 1 158 ? -2.383 41.715 45.233 0.50 37.45 ? 204 ARG A NH2 1 ATOM 1204 N NH2 B ARG A 1 158 ? -7.586 42.272 49.723 0.50 33.55 ? 204 ARG A NH2 1 ATOM 1205 N N . LEU A 1 159 ? 1.263 42.016 51.317 1.00 29.81 ? 205 LEU A N 1 ATOM 1206 C CA . LEU A 1 159 ? 2.631 41.573 51.521 1.00 29.95 ? 205 LEU A CA 1 ATOM 1207 C C . LEU A 1 159 ? 2.764 40.060 51.658 1.00 30.34 ? 205 LEU A C 1 ATOM 1208 O O . LEU A 1 159 ? 2.008 39.431 52.402 1.00 30.81 ? 205 LEU A O 1 ATOM 1209 C CB . LEU A 1 159 ? 3.153 42.246 52.795 1.00 29.47 ? 205 LEU A CB 1 ATOM 1210 C CG . LEU A 1 159 ? 3.796 43.630 52.653 1.00 32.17 ? 205 LEU A CG 1 ATOM 1211 C CD1 . LEU A 1 159 ? 3.378 44.395 51.380 1.00 31.02 ? 205 LEU A CD1 1 ATOM 1212 C CD2 . LEU A 1 159 ? 3.700 44.462 53.921 1.00 32.79 ? 205 LEU A CD2 1 ATOM 1213 N N . THR A 1 160 ? 3.723 39.476 50.945 1.00 28.85 ? 206 THR A N 1 ATOM 1214 C CA A THR A 1 160 ? 4.042 38.058 51.114 0.50 28.50 ? 206 THR A CA 1 ATOM 1215 C CA B THR A 1 160 ? 4.020 38.058 51.048 0.50 28.66 ? 206 THR A CA 1 ATOM 1216 C C . THR A 1 160 ? 5.508 37.826 50.781 1.00 27.73 ? 206 THR A C 1 ATOM 1217 O O . THR A 1 160 ? 5.914 37.767 49.629 1.00 27.79 ? 206 THR A O 1 ATOM 1218 C CB A THR A 1 160 ? 3.167 37.086 50.267 0.50 28.89 ? 206 THR A CB 1 ATOM 1219 C CB B THR A 1 160 ? 3.173 37.237 50.033 0.50 28.98 ? 206 THR A CB 1 ATOM 1220 O OG1 A THR A 1 160 ? 1.777 37.321 50.514 0.50 29.70 ? 206 THR A OG1 1 ATOM 1221 O OG1 B THR A 1 160 ? 3.936 36.121 49.554 0.50 31.29 ? 206 THR A OG1 1 ATOM 1222 C CG2 A THR A 1 160 ? 3.492 35.637 50.646 0.50 29.52 ? 206 THR A CG2 1 ATOM 1223 C CG2 B THR A 1 160 ? 2.756 38.107 48.848 0.50 29.29 ? 206 THR A CG2 1 ATOM 1224 N N . PHE A 1 161 ? 6.301 37.688 51.830 1.00 26.77 ? 207 PHE A N 1 ATOM 1225 C CA . PHE A 1 161 ? 7.728 37.489 51.666 1.00 24.98 ? 207 PHE A CA 1 ATOM 1226 C C . PHE A 1 161 ? 8.014 36.048 51.250 1.00 24.11 ? 207 PHE A C 1 ATOM 1227 O O . PHE A 1 161 ? 7.678 35.106 51.973 1.00 24.64 ? 207 PHE A O 1 ATOM 1228 C CB . PHE A 1 161 ? 8.450 37.819 52.972 1.00 24.09 ? 207 PHE A CB 1 ATOM 1229 C CG . PHE A 1 161 ? 9.919 37.537 52.928 1.00 22.09 ? 207 PHE A CG 1 ATOM 1230 C CD1 . PHE A 1 161 ? 10.756 38.266 52.082 1.00 18.81 ? 207 PHE A CD1 1 ATOM 1231 C CD2 . PHE A 1 161 ? 10.460 36.544 53.721 1.00 22.37 ? 207 PHE A CD2 1 ATOM 1232 C CE1 . PHE A 1 161 ? 12.136 38.000 52.049 1.00 17.52 ? 207 PHE A CE1 1 ATOM 1233 C CE2 . PHE A 1 161 ? 11.815 36.257 53.692 1.00 21.05 ? 207 PHE A CE2 1 ATOM 1234 C CZ . PHE A 1 161 ? 12.667 36.999 52.834 1.00 19.48 ? 207 PHE A CZ 1 ATOM 1235 N N . PRO A 1 162 ? 8.651 35.854 50.082 1.00 24.08 ? 208 PRO A N 1 ATOM 1236 C CA . PRO A 1 162 ? 8.946 34.487 49.681 1.00 24.12 ? 208 PRO A CA 1 ATOM 1237 C C . PRO A 1 162 ? 10.267 33.957 50.225 1.00 25.67 ? 208 PRO A C 1 ATOM 1238 O O . PRO A 1 162 ? 11.295 34.624 50.159 1.00 25.43 ? 208 PRO A O 1 ATOM 1239 C CB . PRO A 1 162 ? 9.042 34.575 48.148 1.00 23.89 ? 208 PRO A CB 1 ATOM 1240 C CG . PRO A 1 162 ? 9.547 35.998 47.879 1.00 23.91 ? 208 PRO A CG 1 ATOM 1241 C CD . PRO A 1 162 ? 9.092 36.857 49.086 1.00 22.56 ? 208 PRO A CD 1 ATOM 1242 N N . THR A 1 163 ? 10.254 32.722 50.690 1.00 26.04 ? 209 THR A N 1 ATOM 1243 C CA A THR A 1 163 ? 11.455 32.082 51.195 0.50 27.11 ? 209 THR A CA 1 ATOM 1244 C CA B THR A 1 163 ? 11.474 32.096 51.191 0.50 26.03 ? 209 THR A CA 1 ATOM 1245 C C . THR A 1 163 ? 12.100 31.170 50.143 1.00 27.08 ? 209 THR A C 1 ATOM 1246 O O . THR A 1 163 ? 13.226 30.695 50.302 1.00 29.40 ? 209 THR A O 1 ATOM 1247 C CB A THR A 1 163 ? 11.109 31.338 52.504 0.50 27.43 ? 209 THR A CB 1 ATOM 1248 C CB B THR A 1 163 ? 11.187 31.332 52.498 0.50 26.20 ? 209 THR A CB 1 ATOM 1249 O OG1 A THR A 1 163 ? 11.625 32.081 53.616 0.50 28.45 ? 209 THR A OG1 1 ATOM 1250 O OG1 B THR A 1 163 ? 10.280 30.262 52.222 0.50 22.06 ? 209 THR A OG1 1 ATOM 1251 C CG2 A THR A 1 163 ? 11.657 29.934 52.509 0.50 28.01 ? 209 THR A CG2 1 ATOM 1252 C CG2 B THR A 1 163 ? 10.546 32.267 53.536 0.50 25.64 ? 209 THR A CG2 1 ATOM 1253 N N . GLY A 1 164 ? 11.400 30.943 49.043 1.00 27.28 ? 210 GLY A N 1 ATOM 1254 C CA . GLY A 1 164 ? 11.899 30.089 47.968 1.00 26.49 ? 210 GLY A CA 1 ATOM 1255 C C . GLY A 1 164 ? 11.593 30.738 46.630 1.00 25.87 ? 210 GLY A C 1 ATOM 1256 O O . GLY A 1 164 ? 11.818 31.948 46.443 1.00 25.92 ? 210 GLY A O 1 ATOM 1257 N N . ARG A 1 165 ? 11.074 29.970 45.680 1.00 25.19 ? 211 ARG A N 1 ATOM 1258 C CA . ARG A 1 165 ? 10.802 30.592 44.395 1.00 25.31 ? 211 ARG A CA 1 ATOM 1259 C C . ARG A 1 165 ? 9.603 31.540 44.452 1.00 24.40 ? 211 ARG A C 1 ATOM 1260 O O . ARG A 1 165 ? 8.737 31.434 45.332 1.00 22.55 ? 211 ARG A O 1 ATOM 1261 C CB . ARG A 1 165 ? 10.704 29.573 43.245 1.00 27.43 ? 211 ARG A CB 1 ATOM 1262 C CG . ARG A 1 165 ? 9.394 28.927 43.090 1.00 30.11 ? 211 ARG A CG 1 ATOM 1263 C CD . ARG A 1 165 ? 9.223 28.553 41.621 1.00 35.89 ? 211 ARG A CD 1 ATOM 1264 N NE . ARG A 1 165 ? 10.408 27.887 41.066 1.00 38.22 ? 211 ARG A NE 1 ATOM 1265 C CZ . ARG A 1 165 ? 10.685 27.878 39.766 1.00 36.41 ? 211 ARG A CZ 1 ATOM 1266 N NH1 . ARG A 1 165 ? 9.864 28.494 38.934 1.00 39.75 ? 211 ARG A NH1 1 ATOM 1267 N NH2 . ARG A 1 165 ? 11.750 27.252 39.298 1.00 37.02 ? 211 ARG A NH2 1 ATOM 1268 N N . PHE A 1 166 ? 9.584 32.501 43.540 1.00 22.43 ? 212 PHE A N 1 ATOM 1269 C CA . PHE A 1 166 ? 8.484 33.448 43.459 1.00 22.75 ? 212 PHE A CA 1 ATOM 1270 C C . PHE A 1 166 ? 8.297 33.883 42.021 1.00 23.12 ? 212 PHE A C 1 ATOM 1271 O O . PHE A 1 166 ? 9.231 33.769 41.202 1.00 21.99 ? 212 PHE A O 1 ATOM 1272 C CB . PHE A 1 166 ? 8.681 34.662 44.391 1.00 22.36 ? 212 PHE A CB 1 ATOM 1273 C CG . PHE A 1 166 ? 9.994 35.406 44.191 1.00 22.68 ? 212 PHE A CG 1 ATOM 1274 C CD1 . PHE A 1 166 ? 10.051 36.547 43.377 1.00 22.90 ? 212 PHE A CD1 1 ATOM 1275 C CD2 . PHE A 1 166 ? 11.158 34.990 44.847 1.00 22.62 ? 212 PHE A CD2 1 ATOM 1276 C CE1 . PHE A 1 166 ? 11.232 37.251 43.208 1.00 22.71 ? 212 PHE A CE1 1 ATOM 1277 C CE2 . PHE A 1 166 ? 12.353 35.698 44.681 1.00 21.50 ? 212 PHE A CE2 1 ATOM 1278 C CZ . PHE A 1 166 ? 12.388 36.825 43.868 1.00 20.66 ? 212 PHE A CZ 1 ATOM 1279 N N . THR A 1 167 ? 7.095 34.366 41.710 1.00 23.01 ? 213 THR A N 1 ATOM 1280 C CA . THR A 1 167 ? 6.734 34.682 40.326 1.00 24.79 ? 213 THR A CA 1 ATOM 1281 C C . THR A 1 167 ? 6.597 36.188 40.153 1.00 25.10 ? 213 THR A C 1 ATOM 1282 O O . THR A 1 167 ? 5.746 36.829 40.762 1.00 26.74 ? 213 THR A O 1 ATOM 1283 C CB . THR A 1 167 ? 5.391 33.974 39.942 1.00 25.86 ? 213 THR A CB 1 ATOM 1284 O OG1 . THR A 1 167 ? 5.599 32.555 39.993 1.00 28.86 ? 213 THR A OG1 1 ATOM 1285 C CG2 . THR A 1 167 ? 4.949 34.383 38.545 1.00 28.29 ? 213 THR A CG2 1 ATOM 1286 N N . ILE A 1 168 ? 7.455 36.777 39.349 1.00 23.25 ? 214 ILE A N 1 ATOM 1287 C CA . ILE A 1 168 ? 7.297 38.184 39.007 1.00 22.63 ? 214 ILE A CA 1 ATOM 1288 C C . ILE A 1 168 ? 6.337 38.228 37.803 1.00 22.31 ? 214 ILE A C 1 ATOM 1289 O O . ILE A 1 168 ? 6.540 37.499 36.826 1.00 21.88 ? 214 ILE A O 1 ATOM 1290 C CB . ILE A 1 168 ? 8.671 38.789 38.583 1.00 21.66 ? 214 ILE A CB 1 ATOM 1291 C CG1 . ILE A 1 168 ? 9.677 38.840 39.769 1.00 22.56 ? 214 ILE A CG1 1 ATOM 1292 C CG2 . ILE A 1 168 ? 8.499 40.163 37.922 1.00 20.37 ? 214 ILE A CG2 1 ATOM 1293 C CD1 . ILE A 1 168 ? 9.259 39.762 40.921 1.00 23.50 ? 214 ILE A CD1 1 ATOM 1294 N N . LYS A 1 169 ? 5.336 39.098 37.838 1.00 22.87 ? 215 LYS A N 1 ATOM 1295 C CA . LYS A 1 169 ? 4.422 39.280 36.678 1.00 24.45 ? 215 LYS A CA 1 ATOM 1296 C C . LYS A 1 169 ? 5.177 39.905 35.509 1.00 23.96 ? 215 LYS A C 1 ATOM 1297 O O . LYS A 1 169 ? 5.842 40.912 35.692 1.00 24.11 ? 215 LYS A O 1 ATOM 1298 C CB . LYS A 1 169 ? 3.255 40.203 37.072 1.00 25.97 ? 215 LYS A CB 1 ATOM 1299 C CG . LYS A 1 169 ? 2.456 39.661 38.260 1.00 31.12 ? 215 LYS A CG 1 ATOM 1300 C CD . LYS A 1 169 ? 1.263 40.549 38.715 1.00 38.92 ? 215 LYS A CD 1 ATOM 1301 C CE . LYS A 1 169 ? 1.374 42.012 38.292 1.00 40.66 ? 215 LYS A CE 1 ATOM 1302 N NZ . LYS A 1 169 ? 0.676 42.256 36.997 1.00 45.47 ? 215 LYS A NZ 1 ATOM 1303 N N . PRO A 1 170 ? 5.074 39.323 34.300 1.00 23.44 ? 216 PRO A N 1 ATOM 1304 C CA . PRO A 1 170 ? 5.867 39.888 33.210 1.00 23.45 ? 216 PRO A CA 1 ATOM 1305 C C . PRO A 1 170 ? 5.487 41.349 32.849 1.00 23.49 ? 216 PRO A C 1 ATOM 1306 O O . PRO A 1 170 ? 6.347 42.125 32.411 1.00 23.84 ? 216 PRO A O 1 ATOM 1307 C CB . PRO A 1 170 ? 5.588 38.931 32.029 1.00 23.66 ? 216 PRO A CB 1 ATOM 1308 C CG . PRO A 1 170 ? 4.393 38.166 32.404 1.00 24.80 ? 216 PRO A CG 1 ATOM 1309 C CD . PRO A 1 170 ? 4.281 38.145 33.881 1.00 24.07 ? 216 PRO A CD 1 ATOM 1310 N N . LEU A 1 171 ? 4.211 41.727 32.997 1.00 23.18 ? 217 LEU A N 1 ATOM 1311 C CA . LEU A 1 171 ? 3.772 43.053 32.576 1.00 23.20 ? 217 LEU A CA 1 ATOM 1312 C C . LEU A 1 171 ? 3.275 43.906 33.759 1.00 22.20 ? 217 LEU A C 1 ATOM 1313 O O . LEU A 1 171 ? 2.492 44.819 33.582 1.00 22.65 ? 217 LEU A O 1 ATOM 1314 C CB . LEU A 1 171 ? 2.698 42.974 31.465 1.00 24.36 ? 217 LEU A CB 1 ATOM 1315 C CG . LEU A 1 171 ? 3.053 42.273 30.146 1.00 28.50 ? 217 LEU A CG 1 ATOM 1316 C CD1 . LEU A 1 171 ? 1.867 42.382 29.136 1.00 32.89 ? 217 LEU A CD1 1 ATOM 1317 C CD2 . LEU A 1 171 ? 4.344 42.806 29.532 1.00 28.61 ? 217 LEU A CD2 1 ATOM 1318 N N . GLY A 1 172 ? 3.757 43.602 34.957 1.00 21.18 ? 218 GLY A N 1 ATOM 1319 C CA . GLY A 1 172 ? 3.518 44.454 36.126 1.00 19.87 ? 218 GLY A CA 1 ATOM 1320 C C . GLY A 1 172 ? 4.614 45.500 36.272 1.00 18.94 ? 218 GLY A C 1 ATOM 1321 O O . GLY A 1 172 ? 5.051 46.093 35.287 1.00 18.04 ? 218 GLY A O 1 ATOM 1322 N N . PHE A 1 173 ? 5.065 45.723 37.510 1.00 18.53 ? 219 PHE A N 1 ATOM 1323 C CA . PHE A 1 173 ? 6.124 46.711 37.728 1.00 18.28 ? 219 PHE A CA 1 ATOM 1324 C C . PHE A 1 173 ? 7.434 46.337 37.032 1.00 16.46 ? 219 PHE A C 1 ATOM 1325 O O . PHE A 1 173 ? 8.305 47.191 36.857 1.00 16.62 ? 219 PHE A O 1 ATOM 1326 C CB . PHE A 1 173 ? 6.350 46.962 39.208 1.00 19.92 ? 219 PHE A CB 1 ATOM 1327 C CG . PHE A 1 173 ? 5.320 47.889 39.815 1.00 23.67 ? 219 PHE A CG 1 ATOM 1328 C CD1 . PHE A 1 173 ? 4.237 48.344 39.045 1.00 30.13 ? 219 PHE A CD1 1 ATOM 1329 C CD2 . PHE A 1 173 ? 5.416 48.300 41.120 1.00 29.30 ? 219 PHE A CD2 1 ATOM 1330 C CE1 . PHE A 1 173 ? 3.264 49.203 39.594 1.00 31.61 ? 219 PHE A CE1 1 ATOM 1331 C CE2 . PHE A 1 173 ? 4.445 49.162 41.670 1.00 28.76 ? 219 PHE A CE2 1 ATOM 1332 C CZ . PHE A 1 173 ? 3.380 49.597 40.906 1.00 29.34 ? 219 PHE A CZ 1 ATOM 1333 N N . LEU A 1 174 ? 7.581 45.080 36.600 1.00 16.81 ? 220 LEU A N 1 ATOM 1334 C CA . LEU A 1 174 ? 8.737 44.801 35.717 1.00 15.64 ? 220 LEU A CA 1 ATOM 1335 C C . LEU A 1 174 ? 8.789 45.789 34.529 1.00 16.67 ? 220 LEU A C 1 ATOM 1336 O O . LEU A 1 174 ? 9.851 46.205 34.093 1.00 14.81 ? 220 LEU A O 1 ATOM 1337 C CB . LEU A 1 174 ? 8.697 43.355 35.187 1.00 15.66 ? 220 LEU A CB 1 ATOM 1338 C CG . LEU A 1 174 ? 9.902 42.964 34.317 1.00 15.34 ? 220 LEU A CG 1 ATOM 1339 C CD1 . LEU A 1 174 ? 11.205 43.013 35.134 1.00 14.04 ? 220 LEU A CD1 1 ATOM 1340 C CD2 . LEU A 1 174 ? 9.634 41.531 33.769 1.00 15.78 ? 220 LEU A CD2 1 ATOM 1341 N N . LEU A 1 175 ? 7.637 46.187 34.000 1.00 17.29 ? 221 LEU A N 1 ATOM 1342 C CA A LEU A 1 175 ? 7.622 47.085 32.854 0.50 17.62 ? 221 LEU A CA 1 ATOM 1343 C CA B LEU A 1 175 ? 7.613 47.112 32.862 0.50 17.76 ? 221 LEU A CA 1 ATOM 1344 C C . LEU A 1 175 ? 8.263 48.447 33.143 1.00 18.81 ? 221 LEU A C 1 ATOM 1345 O O . LEU A 1 175 ? 8.838 49.075 32.243 1.00 19.48 ? 221 LEU A O 1 ATOM 1346 C CB A LEU A 1 175 ? 6.180 47.220 32.337 0.50 17.48 ? 221 LEU A CB 1 ATOM 1347 C CB B LEU A 1 175 ? 6.180 47.355 32.369 0.50 17.95 ? 221 LEU A CB 1 ATOM 1348 C CG A LEU A 1 175 ? 5.830 47.854 31.000 0.50 16.69 ? 221 LEU A CG 1 ATOM 1349 C CG B LEU A 1 175 ? 5.554 46.237 31.560 0.50 17.21 ? 221 LEU A CG 1 ATOM 1350 C CD1 A LEU A 1 175 ? 6.596 47.213 29.839 0.50 15.79 ? 221 LEU A CD1 1 ATOM 1351 C CD1 B LEU A 1 175 ? 4.138 46.645 31.110 0.50 18.74 ? 221 LEU A CD1 1 ATOM 1352 C CD2 A LEU A 1 175 ? 4.308 47.701 30.823 0.50 15.96 ? 221 LEU A CD2 1 ATOM 1353 C CD2 B LEU A 1 175 ? 6.430 45.911 30.358 0.50 19.77 ? 221 LEU A CD2 1 ATOM 1354 N N . LEU A 1 176 ? 8.168 48.920 34.381 1.00 18.83 ? 222 LEU A N 1 ATOM 1355 C CA . LEU A 1 176 ? 8.866 50.154 34.755 1.00 19.40 ? 222 LEU A CA 1 ATOM 1356 C C . LEU A 1 176 ? 10.386 49.979 34.759 1.00 20.71 ? 222 LEU A C 1 ATOM 1357 O O . LEU A 1 176 ? 11.122 50.968 34.717 1.00 22.84 ? 222 LEU A O 1 ATOM 1358 C CB . LEU A 1 176 ? 8.399 50.656 36.134 1.00 18.75 ? 222 LEU A CB 1 ATOM 1359 C CG . LEU A 1 176 ? 6.936 51.149 36.190 1.00 20.65 ? 222 LEU A CG 1 ATOM 1360 C CD1 . LEU A 1 176 ? 6.619 51.632 37.607 1.00 22.12 ? 222 LEU A CD1 1 ATOM 1361 C CD2 . LEU A 1 176 ? 6.770 52.291 35.196 1.00 23.29 ? 222 LEU A CD2 1 ATOM 1362 N N . GLN A 1 177 ? 10.867 48.753 34.857 1.00 17.24 ? 223 GLN A N 1 ATOM 1363 C CA . GLN A 1 177 ? 12.327 48.548 34.933 1.00 16.85 ? 223 GLN A CA 1 ATOM 1364 C C . GLN A 1 177 ? 12.910 48.310 33.537 1.00 17.85 ? 223 GLN A C 1 ATOM 1365 O O . GLN A 1 177 ? 14.109 48.535 33.327 1.00 18.48 ? 223 GLN A O 1 ATOM 1366 C CB . GLN A 1 177 ? 12.699 47.344 35.799 1.00 15.92 ? 223 GLN A CB 1 ATOM 1367 C CG . GLN A 1 177 ? 11.837 47.094 37.068 1.00 15.66 ? 223 GLN A CG 1 ATOM 1368 C CD . GLN A 1 177 ? 11.726 48.335 37.935 1.00 16.17 ? 223 GLN A CD 1 ATOM 1369 O OE1 . GLN A 1 177 ? 12.702 49.078 38.117 1.00 15.24 ? 223 GLN A OE1 1 ATOM 1370 N NE2 . GLN A 1 177 ? 10.507 48.584 38.452 1.00 13.99 ? 223 GLN A NE2 1 ATOM 1371 N N . ILE A 1 178 ? 12.095 47.816 32.601 1.00 17.31 ? 224 ILE A N 1 ATOM 1372 C CA . ILE A 1 178 ? 12.670 47.344 31.313 1.00 17.10 ? 224 ILE A CA 1 ATOM 1373 C C . ILE A 1 178 ? 12.494 48.339 30.152 1.00 18.22 ? 224 ILE A C 1 ATOM 1374 O O . ILE A 1 178 ? 12.648 47.955 28.995 1.00 18.35 ? 224 ILE A O 1 ATOM 1375 C CB . ILE A 1 178 ? 12.144 45.915 30.970 1.00 16.91 ? 224 ILE A CB 1 ATOM 1376 C CG1 . ILE A 1 178 ? 10.618 45.957 30.741 1.00 15.03 ? 224 ILE A CG1 1 ATOM 1377 C CG2 . ILE A 1 178 ? 12.526 44.929 32.099 1.00 16.91 ? 224 ILE A CG2 1 ATOM 1378 C CD1 . ILE A 1 178 ? 10.008 44.679 30.033 1.00 16.94 ? 224 ILE A CD1 1 ATOM 1379 N N . SER A 1 179 ? 12.215 49.630 30.418 1.00 20.05 ? 225 SER A N 1 ATOM 1380 C CA A SER A 1 179 ? 12.027 50.580 29.316 0.50 20.77 ? 225 SER A CA 1 ATOM 1381 C CA B SER A 1 179 ? 12.024 50.574 29.309 0.50 20.77 ? 225 SER A CA 1 ATOM 1382 C C . SER A 1 179 ? 13.234 50.586 28.381 1.00 20.19 ? 225 SER A C 1 ATOM 1383 O O . SER A 1 179 ? 13.085 50.597 27.146 1.00 20.18 ? 225 SER A O 1 ATOM 1384 C CB A SER A 1 179 ? 11.727 52.003 29.812 0.50 22.10 ? 225 SER A CB 1 ATOM 1385 C CB B SER A 1 179 ? 11.689 52.003 29.777 0.50 22.06 ? 225 SER A CB 1 ATOM 1386 O OG A SER A 1 179 ? 12.777 52.469 30.641 0.50 24.85 ? 225 SER A OG 1 ATOM 1387 O OG B SER A 1 179 ? 10.671 51.993 30.758 0.50 24.90 ? 225 SER A OG 1 ATOM 1388 N N . GLY A 1 180 ? 14.439 50.543 28.969 1.00 18.67 ? 226 GLY A N 1 ATOM 1389 C CA . GLY A 1 180 ? 15.663 50.557 28.147 1.00 16.82 ? 226 GLY A CA 1 ATOM 1390 C C . GLY A 1 180 ? 15.856 49.226 27.410 1.00 15.32 ? 226 GLY A C 1 ATOM 1391 O O . GLY A 1 180 ? 16.258 49.189 26.246 1.00 15.99 ? 226 GLY A O 1 ATOM 1392 N N . ASP A 1 181 ? 15.607 48.131 28.118 1.00 15.12 ? 227 ASP A N 1 ATOM 1393 C CA . ASP A 1 181 ? 15.731 46.783 27.528 1.00 15.42 ? 227 ASP A CA 1 ATOM 1394 C C . ASP A 1 181 ? 14.758 46.632 26.380 1.00 16.50 ? 227 ASP A C 1 ATOM 1395 O O . ASP A 1 181 ? 15.079 46.012 25.372 1.00 16.45 ? 227 ASP A O 1 ATOM 1396 C CB . ASP A 1 181 ? 15.496 45.687 28.584 1.00 15.95 ? 227 ASP A CB 1 ATOM 1397 C CG . ASP A 1 181 ? 16.667 45.563 29.577 1.00 17.74 ? 227 ASP A CG 1 ATOM 1398 O OD1 . ASP A 1 181 ? 17.700 44.967 29.185 1.00 18.14 ? 227 ASP A OD1 1 ATOM 1399 O OD2 . ASP A 1 181 ? 16.560 46.039 30.745 1.00 17.25 ? 227 ASP A OD2 1 ATOM 1400 N N . LEU A 1 182 ? 13.585 47.255 26.503 1.00 16.33 ? 228 LEU A N 1 ATOM 1401 C CA . LEU A 1 182 ? 12.576 47.156 25.439 1.00 16.70 ? 228 LEU A CA 1 ATOM 1402 C C . LEU A 1 182 ? 13.009 47.816 24.120 1.00 17.02 ? 228 LEU A C 1 ATOM 1403 O O . LEU A 1 182 ? 12.555 47.419 23.023 1.00 18.31 ? 228 LEU A O 1 ATOM 1404 C CB . LEU A 1 182 ? 11.232 47.712 25.952 1.00 16.23 ? 228 LEU A CB 1 ATOM 1405 C CG . LEU A 1 182 ? 10.424 46.857 26.921 1.00 16.71 ? 228 LEU A CG 1 ATOM 1406 C CD1 . LEU A 1 182 ? 9.208 47.612 27.503 1.00 17.94 ? 228 LEU A CD1 1 ATOM 1407 C CD2 . LEU A 1 182 ? 9.977 45.543 26.193 1.00 19.65 ? 228 LEU A CD2 1 ATOM 1408 N N . GLU A 1 183 ? 13.909 48.791 24.180 1.00 16.71 ? 229 GLU A N 1 ATOM 1409 C CA . GLU A 1 183 ? 14.385 49.429 22.950 1.00 18.95 ? 229 GLU A CA 1 ATOM 1410 C C . GLU A 1 183 ? 14.967 48.389 22.007 1.00 19.61 ? 229 GLU A C 1 ATOM 1411 O O . GLU A 1 183 ? 14.881 48.519 20.789 1.00 18.54 ? 229 GLU A O 1 ATOM 1412 C CB . GLU A 1 183 ? 15.458 50.472 23.258 1.00 19.49 ? 229 GLU A CB 1 ATOM 1413 C CG . GLU A 1 183 ? 14.902 51.676 24.011 1.00 23.95 ? 229 GLU A CG 1 ATOM 1414 C CD . GLU A 1 183 ? 16.011 52.689 24.360 1.00 33.40 ? 229 GLU A CD 1 ATOM 1415 O OE1 . GLU A 1 183 ? 17.120 52.558 23.809 1.00 38.34 ? 229 GLU A OE1 1 ATOM 1416 O OE2 . GLU A 1 183 ? 15.776 53.596 25.187 1.00 36.31 ? 229 GLU A OE2 1 ATOM 1417 N N . ASP A 1 184 ? 15.539 47.343 22.586 1.00 18.98 ? 230 ASP A N 1 ATOM 1418 C CA . ASP A 1 184 ? 16.114 46.240 21.792 1.00 19.91 ? 230 ASP A CA 1 ATOM 1419 C C . ASP A 1 184 ? 15.216 45.021 21.716 1.00 19.86 ? 230 ASP A C 1 ATOM 1420 O O . ASP A 1 184 ? 15.209 44.323 20.702 1.00 20.30 ? 230 ASP A O 1 ATOM 1421 C CB . ASP A 1 184 ? 17.469 45.859 22.391 1.00 19.83 ? 230 ASP A CB 1 ATOM 1422 C CG . ASP A 1 184 ? 18.425 47.010 22.349 1.00 21.07 ? 230 ASP A CG 1 ATOM 1423 O OD1 . ASP A 1 184 ? 18.968 47.289 21.254 1.00 21.77 ? 230 ASP A OD1 1 ATOM 1424 O OD2 . ASP A 1 184 ? 18.671 47.667 23.402 1.00 23.00 ? 230 ASP A OD2 1 ATOM 1425 N N . LEU A 1 185 ? 14.461 44.740 22.774 1.00 19.54 ? 231 LEU A N 1 ATOM 1426 C CA . LEU A 1 185 ? 13.544 43.600 22.707 1.00 20.58 ? 231 LEU A CA 1 ATOM 1427 C C . LEU A 1 185 ? 12.512 43.765 21.608 1.00 21.20 ? 231 LEU A C 1 ATOM 1428 O O . LEU A 1 185 ? 12.126 42.778 20.983 1.00 21.56 ? 231 LEU A O 1 ATOM 1429 C CB . LEU A 1 185 ? 12.831 43.363 24.037 1.00 21.21 ? 231 LEU A CB 1 ATOM 1430 C CG . LEU A 1 185 ? 13.626 42.694 25.130 1.00 23.80 ? 231 LEU A CG 1 ATOM 1431 C CD1 . LEU A 1 185 ? 12.922 42.880 26.503 1.00 26.02 ? 231 LEU A CD1 1 ATOM 1432 C CD2 . LEU A 1 185 ? 13.831 41.172 24.762 1.00 23.48 ? 231 LEU A CD2 1 ATOM 1433 N N . GLU A 1 186 ? 12.027 44.986 21.416 1.00 20.76 ? 232 GLU A N 1 ATOM 1434 C CA . GLU A 1 186 ? 11.072 45.233 20.332 1.00 22.43 ? 232 GLU A CA 1 ATOM 1435 C C . GLU A 1 186 ? 11.568 44.736 18.949 1.00 21.70 ? 232 GLU A C 1 ATOM 1436 O O . GLU A 1 186 ? 10.949 43.857 18.378 1.00 23.22 ? 232 GLU A O 1 ATOM 1437 C CB . GLU A 1 186 ? 10.602 46.688 20.330 1.00 22.33 ? 232 GLU A CB 1 ATOM 1438 C CG . GLU A 1 186 ? 9.686 46.957 21.562 1.00 23.27 ? 232 GLU A CG 1 ATOM 1439 C CD . GLU A 1 186 ? 9.214 48.400 21.660 1.00 30.40 ? 232 GLU A CD 1 ATOM 1440 O OE1 . GLU A 1 186 ? 9.586 49.189 20.771 1.00 30.84 ? 232 GLU A OE1 1 ATOM 1441 O OE2 . GLU A 1 186 ? 8.481 48.742 22.624 1.00 31.41 ? 232 GLU A OE2 1 ATOM 1442 N N . PRO A 1 187 ? 12.681 45.284 18.418 1.00 22.03 ? 233 PRO A N 1 ATOM 1443 C CA . PRO A 1 187 ? 13.168 44.762 17.118 1.00 21.90 ? 233 PRO A CA 1 ATOM 1444 C C . PRO A 1 187 ? 13.602 43.303 17.175 1.00 22.88 ? 233 PRO A C 1 ATOM 1445 O O . PRO A 1 187 ? 13.451 42.574 16.182 1.00 23.28 ? 233 PRO A O 1 ATOM 1446 C CB . PRO A 1 187 ? 14.368 45.658 16.790 1.00 21.32 ? 233 PRO A CB 1 ATOM 1447 C CG . PRO A 1 187 ? 14.777 46.302 18.132 1.00 21.22 ? 233 PRO A CG 1 ATOM 1448 C CD . PRO A 1 187 ? 13.470 46.434 18.894 1.00 21.03 ? 233 PRO A CD 1 ATOM 1449 N N . ALA A 1 188 ? 14.113 42.859 18.319 1.00 22.34 ? 234 ALA A N 1 ATOM 1450 C CA . ALA A 1 188 ? 14.549 41.477 18.412 1.00 22.67 ? 234 ALA A CA 1 ATOM 1451 C C . ALA A 1 188 ? 13.338 40.528 18.300 1.00 24.03 ? 234 ALA A C 1 ATOM 1452 O O . ALA A 1 188 ? 13.484 39.387 17.862 1.00 23.94 ? 234 ALA A O 1 ATOM 1453 C CB . ALA A 1 188 ? 15.328 41.228 19.702 1.00 22.60 ? 234 ALA A CB 1 ATOM 1454 N N . LEU A 1 189 ? 12.159 40.991 18.722 1.00 23.31 ? 235 LEU A N 1 ATOM 1455 C CA . LEU A 1 189 ? 10.948 40.180 18.662 1.00 25.14 ? 235 LEU A CA 1 ATOM 1456 C C . LEU A 1 189 ? 10.101 40.594 17.455 1.00 27.73 ? 235 LEU A C 1 ATOM 1457 O O . LEU A 1 189 ? 8.909 40.293 17.391 1.00 27.91 ? 235 LEU A O 1 ATOM 1458 C CB . LEU A 1 189 ? 10.139 40.314 19.960 1.00 24.54 ? 235 LEU A CB 1 ATOM 1459 C CG . LEU A 1 189 ? 10.878 39.740 21.180 1.00 22.16 ? 235 LEU A CG 1 ATOM 1460 C CD1 . LEU A 1 189 ? 10.079 39.937 22.424 1.00 22.74 ? 235 LEU A CD1 1 ATOM 1461 C CD2 . LEU A 1 189 ? 11.255 38.268 21.040 1.00 26.72 ? 235 LEU A CD2 1 ATOM 1462 N N . ASN A 1 190 ? 10.732 41.325 16.538 1.00 30.64 ? 236 ASN A N 1 ATOM 1463 C CA . ASN A 1 190 ? 10.120 41.753 15.267 1.00 34.81 ? 236 ASN A CA 1 ATOM 1464 C C . ASN A 1 190 ? 8.870 42.634 15.398 1.00 36.32 ? 236 ASN A C 1 ATOM 1465 O O . ASN A 1 190 ? 7.905 42.484 14.636 1.00 37.12 ? 236 ASN A O 1 ATOM 1466 C CB . ASN A 1 190 ? 9.872 40.535 14.361 1.00 35.49 ? 236 ASN A CB 1 ATOM 1467 C CG . ASN A 1 190 ? 11.166 39.822 13.979 1.00 38.62 ? 236 ASN A CG 1 ATOM 1468 O OD1 . ASN A 1 190 ? 12.187 40.470 13.747 1.00 39.01 ? 236 ASN A OD1 1 ATOM 1469 N ND2 . ASN A 1 190 ? 11.135 38.480 13.927 1.00 46.23 ? 236 ASN A ND2 1 ATOM 1470 N N . LYS A 1 191 ? 8.879 43.552 16.357 1.00 37.81 ? 237 LYS A N 1 ATOM 1471 C CA . LYS A 1 191 ? 7.774 44.489 16.502 1.00 40.30 ? 237 LYS A CA 1 ATOM 1472 C C . LYS A 1 191 ? 7.749 45.461 15.316 1.00 42.24 ? 237 LYS A C 1 ATOM 1473 O O . LYS A 1 191 ? 8.806 45.834 14.795 1.00 42.77 ? 237 LYS A O 1 ATOM 1474 C CB . LYS A 1 191 ? 7.894 45.274 17.798 1.00 39.87 ? 237 LYS A CB 1 ATOM 1475 C CG . LYS A 1 191 ? 6.707 46.159 18.117 1.00 39.36 ? 237 LYS A CG 1 ATOM 1476 C CD . LYS A 1 191 ? 6.963 46.911 19.397 1.00 42.59 ? 237 LYS A CD 1 ATOM 1477 C CE . LYS A 1 191 ? 5.743 47.673 19.869 1.00 45.54 ? 237 LYS A CE 1 ATOM 1478 N NZ . LYS A 1 191 ? 5.470 48.866 19.007 1.00 48.30 ? 237 LYS A NZ 1 ATOM 1479 N N . THR A 1 192 ? 6.547 45.854 14.895 1.00 44.46 ? 238 THR A N 1 ATOM 1480 C CA . THR A 1 192 ? 6.376 46.846 13.813 1.00 46.51 ? 238 THR A CA 1 ATOM 1481 C C . THR A 1 192 ? 5.818 48.152 14.371 1.00 47.26 ? 238 THR A C 1 ATOM 1482 O O . THR A 1 192 ? 4.788 48.151 15.068 1.00 48.43 ? 238 THR A O 1 ATOM 1483 C CB . THR A 1 192 ? 5.418 46.343 12.715 1.00 46.59 ? 238 THR A CB 1 ATOM 1484 O OG1 . THR A 1 192 ? 4.213 45.845 13.322 1.00 49.20 ? 238 THR A OG1 1 ATOM 1485 C CG2 . THR A 1 192 ? 6.067 45.231 11.905 1.00 47.02 ? 238 THR A CG2 1 ATOM 1486 N N . GLY A 1 199 ? 12.305 55.919 23.546 1.00 42.12 ? 245 GLY A N 1 ATOM 1487 C CA . GLY A 1 199 ? 12.699 56.112 24.944 1.00 41.91 ? 245 GLY A CA 1 ATOM 1488 C C . GLY A 1 199 ? 13.989 56.914 25.116 1.00 41.95 ? 245 GLY A C 1 ATOM 1489 O O . GLY A 1 199 ? 14.175 57.955 24.480 1.00 40.57 ? 245 GLY A O 1 ATOM 1490 N N . SER A 1 200 ? 14.871 56.434 25.994 1.00 41.81 ? 246 SER A N 1 ATOM 1491 C CA . SER A 1 200 ? 16.146 57.112 26.239 1.00 42.24 ? 246 SER A CA 1 ATOM 1492 C C . SER A 1 200 ? 17.122 56.875 25.081 1.00 42.05 ? 246 SER A C 1 ATOM 1493 O O . SER A 1 200 ? 17.214 55.771 24.542 1.00 42.23 ? 246 SER A O 1 ATOM 1494 C CB . SER A 1 200 ? 16.761 56.658 27.568 1.00 42.72 ? 246 SER A CB 1 ATOM 1495 O OG . SER A 1 200 ? 17.837 57.518 27.955 1.00 44.19 ? 246 SER A OG 1 ATOM 1496 N N . GLY A 1 201 ? 17.859 57.915 24.704 1.00 41.55 ? 247 GLY A N 1 ATOM 1497 C CA . GLY A 1 201 ? 18.772 57.841 23.554 1.00 40.74 ? 247 GLY A CA 1 ATOM 1498 C C . GLY A 1 201 ? 18.517 59.042 22.662 1.00 40.32 ? 247 GLY A C 1 ATOM 1499 O O . GLY A 1 201 ? 17.757 59.939 23.044 1.00 39.93 ? 247 GLY A O 1 ATOM 1500 N N . SER A 1 202 ? 19.107 59.051 21.467 1.00 39.30 ? 248 SER A N 1 ATOM 1501 C CA . SER A 1 202 ? 18.904 60.169 20.521 1.00 38.48 ? 248 SER A CA 1 ATOM 1502 C C . SER A 1 202 ? 17.421 60.497 20.239 1.00 38.08 ? 248 SER A C 1 ATOM 1503 O O . SER A 1 202 ? 16.529 59.621 20.292 1.00 36.82 ? 248 SER A O 1 ATOM 1504 C CB . SER A 1 202 ? 19.641 59.897 19.207 1.00 39.10 ? 248 SER A CB 1 ATOM 1505 O OG . SER A 1 202 ? 21.016 59.589 19.441 1.00 40.56 ? 248 SER A OG 1 ATOM 1506 O OXT . SER A 1 202 ? 17.070 61.654 19.945 1.00 36.62 ? 248 SER A OXT 1 HETATM 1507 N N . OCS B 2 1 ? 21.256 60.699 25.095 1.00 22.28 ? 249 OCS B N 1 HETATM 1508 C CA . OCS B 2 1 ? 21.924 61.208 26.341 1.00 20.09 ? 249 OCS B CA 1 HETATM 1509 C CB . OCS B 2 1 ? 22.113 60.108 27.385 1.00 22.22 ? 249 OCS B CB 1 HETATM 1510 S SG . OCS B 2 1 ? 20.725 58.976 27.250 1.00 31.54 ? 249 OCS B SG 1 HETATM 1511 C C . OCS B 2 1 ? 23.285 61.692 25.968 1.00 17.44 ? 249 OCS B C 1 HETATM 1512 O O . OCS B 2 1 ? 23.934 61.118 25.071 1.00 15.28 ? 249 OCS B O 1 HETATM 1513 O OD1 . OCS B 2 1 ? 20.105 58.873 28.517 0.50 27.34 ? 249 OCS B OD1 1 HETATM 1514 O OD2 . OCS B 2 1 ? 21.147 57.736 26.651 0.50 26.35 ? 249 OCS B OD2 1 HETATM 1515 O OD3 . OCS B 2 1 ? 19.790 59.566 26.352 0.50 29.98 ? 249 OCS B OD3 1 ATOM 1516 N N . SER B 2 2 ? 23.736 62.703 26.696 1.00 14.59 ? 250 SER B N 1 ATOM 1517 C CA . SER B 2 2 ? 25.073 63.229 26.514 1.00 13.66 ? 250 SER B CA 1 ATOM 1518 C C . SER B 2 2 ? 25.785 63.090 27.877 1.00 13.41 ? 250 SER B C 1 ATOM 1519 O O . SER B 2 2 ? 25.137 63.209 28.931 1.00 13.69 ? 250 SER B O 1 ATOM 1520 C CB . SER B 2 2 ? 24.977 64.717 26.165 1.00 13.90 ? 250 SER B CB 1 ATOM 1521 O OG . SER B 2 2 ? 24.377 64.901 24.874 1.00 16.01 ? 250 SER B OG 1 ATOM 1522 N N . ALA B 2 3 ? 27.094 62.850 27.866 1.00 13.18 ? 251 ALA B N 1 ATOM 1523 C CA . ALA B 2 3 ? 27.856 62.770 29.127 1.00 12.07 ? 251 ALA B CA 1 ATOM 1524 C C . ALA B 2 3 ? 29.238 63.341 28.871 1.00 11.36 ? 251 ALA B C 1 ATOM 1525 O O . ALA B 2 3 ? 29.740 63.299 27.741 1.00 11.70 ? 251 ALA B O 1 ATOM 1526 C CB . ALA B 2 3 ? 28.000 61.303 29.611 1.00 12.00 ? 251 ALA B CB 1 ATOM 1527 N N . LEU B 2 4 ? 29.839 63.874 29.931 1.00 11.41 ? 252 LEU B N 1 ATOM 1528 C CA . LEU B 2 4 ? 31.183 64.444 29.828 1.00 12.27 ? 252 LEU B CA 1 ATOM 1529 C C . LEU B 2 4 ? 31.895 64.199 31.139 1.00 11.94 ? 252 LEU B C 1 ATOM 1530 O O . LEU B 2 4 ? 31.363 64.491 32.232 1.00 13.15 ? 252 LEU B O 1 ATOM 1531 C CB . LEU B 2 4 ? 31.114 65.967 29.523 1.00 11.60 ? 252 LEU B CB 1 ATOM 1532 C CG . LEU B 2 4 ? 32.476 66.647 29.374 1.00 12.93 ? 252 LEU B CG 1 ATOM 1533 C CD1 . LEU B 2 4 ? 33.219 66.089 28.220 1.00 14.13 ? 252 LEU B CD1 1 ATOM 1534 C CD2 . LEU B 2 4 ? 32.271 68.170 29.247 1.00 14.58 ? 252 LEU B CD2 1 ATOM 1535 N N . ILE B 2 5 ? 33.115 63.675 31.017 1.00 11.61 ? 253 ILE B N 1 ATOM 1536 C CA . ILE B 2 5 ? 34.024 63.512 32.141 1.00 12.51 ? 253 ILE B CA 1 ATOM 1537 C C . ILE B 2 5 ? 35.160 64.486 31.815 1.00 12.47 ? 253 ILE B C 1 ATOM 1538 O O . ILE B 2 5 ? 35.726 64.409 30.745 1.00 12.86 ? 253 ILE B O 1 ATOM 1539 C CB . ILE B 2 5 ? 34.549 62.063 32.185 1.00 12.88 ? 253 ILE B CB 1 ATOM 1540 C CG1 . ILE B 2 5 ? 33.334 61.143 32.471 1.00 15.58 ? 253 ILE B CG1 1 ATOM 1541 C CG2 . ILE B 2 5 ? 35.641 61.916 33.283 1.00 13.28 ? 253 ILE B CG2 1 ATOM 1542 C CD1 . ILE B 2 5 ? 33.621 59.632 32.209 1.00 17.41 ? 253 ILE B CD1 1 ATOM 1543 N N . LYS B 2 6 ? 35.455 65.406 32.729 1.00 13.79 ? 254 LYS B N 1 ATOM 1544 C CA . LYS B 2 6 ? 36.376 66.508 32.404 1.00 13.55 ? 254 LYS B CA 1 ATOM 1545 C C . LYS B 2 6 ? 37.416 66.645 33.503 1.00 12.71 ? 254 LYS B C 1 ATOM 1546 O O . LYS B 2 6 ? 37.070 66.817 34.666 1.00 13.41 ? 254 LYS B O 1 ATOM 1547 C CB . LYS B 2 6 ? 35.563 67.828 32.270 1.00 12.86 ? 254 LYS B CB 1 ATOM 1548 C CG . LYS B 2 6 ? 36.432 69.107 32.093 1.00 14.28 ? 254 LYS B CG 1 ATOM 1549 C CD . LYS B 2 6 ? 37.293 68.985 30.826 1.00 14.11 ? 254 LYS B CD 1 ATOM 1550 C CE . LYS B 2 6 ? 38.199 70.223 30.691 1.00 16.95 ? 254 LYS B CE 1 ATOM 1551 N NZ . LYS B 2 6 ? 39.262 69.952 29.659 1.00 15.05 ? 254 LYS B NZ 1 ATOM 1552 N N . LEU B 2 7 ? 38.681 66.526 33.126 1.00 14.03 ? 255 LEU B N 1 ATOM 1553 C CA . LEU B 2 7 ? 39.809 66.814 34.015 1.00 15.47 ? 255 LEU B CA 1 ATOM 1554 C C . LEU B 2 7 ? 40.030 68.322 33.966 1.00 15.19 ? 255 LEU B C 1 ATOM 1555 O O . LEU B 2 7 ? 40.276 68.863 32.872 1.00 15.87 ? 255 LEU B O 1 ATOM 1556 C CB . LEU B 2 7 ? 41.012 66.119 33.418 1.00 17.08 ? 255 LEU B CB 1 ATOM 1557 C CG . LEU B 2 7 ? 42.164 65.521 34.195 1.00 24.28 ? 255 LEU B CG 1 ATOM 1558 C CD1 . LEU B 2 7 ? 41.788 65.035 35.618 1.00 22.63 ? 255 LEU B CD1 1 ATOM 1559 C CD2 . LEU B 2 7 ? 42.770 64.371 33.283 1.00 26.96 ? 255 LEU B CD2 1 ATOM 1560 N N . LEU B 2 8 ? 39.900 69.001 35.104 1.00 15.79 ? 256 LEU B N 1 ATOM 1561 C CA . LEU B 2 8 ? 40.060 70.474 35.111 1.00 15.72 ? 256 LEU B CA 1 ATOM 1562 C C . LEU B 2 8 ? 41.544 70.800 34.937 1.00 18.06 ? 256 LEU B C 1 ATOM 1563 O O . LEU B 2 8 ? 42.416 69.950 35.151 1.00 18.00 ? 256 LEU B O 1 ATOM 1564 C CB . LEU B 2 8 ? 39.502 71.094 36.400 1.00 16.42 ? 256 LEU B CB 1 ATOM 1565 C CG . LEU B 2 8 ? 37.999 70.920 36.713 1.00 17.94 ? 256 LEU B CG 1 ATOM 1566 C CD1 . LEU B 2 8 ? 37.620 71.783 37.931 1.00 22.83 ? 256 LEU B CD1 1 ATOM 1567 C CD2 . LEU B 2 8 ? 37.134 71.303 35.477 1.00 20.03 ? 256 LEU B CD2 1 ATOM 1568 N N . PRO B 2 9 ? 41.848 72.036 34.510 1.00 18.40 ? 257 PRO B N 1 ATOM 1569 C CA . PRO B 2 9 ? 43.244 72.449 34.333 1.00 18.61 ? 257 PRO B CA 1 ATOM 1570 C C . PRO B 2 9 ? 44.089 72.098 35.560 1.00 18.61 ? 257 PRO B C 1 ATOM 1571 O O . PRO B 2 9 ? 43.626 72.245 36.688 1.00 18.86 ? 257 PRO B O 1 ATOM 1572 C CB . PRO B 2 9 ? 43.124 73.961 34.194 1.00 18.95 ? 257 PRO B CB 1 ATOM 1573 C CG . PRO B 2 9 ? 41.790 74.136 33.471 1.00 19.31 ? 257 PRO B CG 1 ATOM 1574 C CD . PRO B 2 9 ? 40.884 73.073 34.101 1.00 19.43 ? 257 PRO B CD 1 ATOM 1575 N N . GLY B 2 10 ? 45.314 71.654 35.318 1.00 19.58 ? 258 GLY B N 1 ATOM 1576 C CA . GLY B 2 10 ? 46.248 71.311 36.376 1.00 21.52 ? 258 GLY B CA 1 ATOM 1577 C C . GLY B 2 10 ? 45.823 70.045 37.117 1.00 21.77 ? 258 GLY B C 1 ATOM 1578 O O . GLY B 2 10 ? 46.361 69.746 38.193 1.00 22.07 ? 258 GLY B O 1 ATOM 1579 N N . GLY B 2 11 ? 44.800 69.360 36.593 1.00 21.21 ? 259 GLY B N 1 ATOM 1580 C CA . GLY B 2 11 ? 44.270 68.173 37.290 1.00 20.54 ? 259 GLY B CA 1 ATOM 1581 C C . GLY B 2 11 ? 43.600 68.544 38.612 1.00 19.88 ? 259 GLY B C 1 ATOM 1582 O O . GLY B 2 11 ? 43.545 67.722 39.523 1.00 20.25 ? 259 GLY B O 1 ATOM 1583 N N . HIS B 2 12 ? 43.083 69.772 38.730 1.00 19.04 ? 260 HIS B N 1 ATOM 1584 C CA . HIS B 2 12 ? 42.591 70.274 40.026 1.00 18.77 ? 260 HIS B CA 1 ATOM 1585 C C . HIS B 2 12 ? 41.366 69.502 40.519 1.00 18.44 ? 260 HIS B C 1 ATOM 1586 O O . HIS B 2 12 ? 41.118 69.386 41.725 1.00 19.27 ? 260 HIS B O 1 ATOM 1587 C CB . HIS B 2 12 ? 42.241 71.775 39.968 1.00 19.86 ? 260 HIS B CB 1 ATOM 1588 C CG . HIS B 2 12 ? 43.437 72.665 39.752 1.00 23.01 ? 260 HIS B CG 1 ATOM 1589 N ND1 . HIS B 2 12 ? 43.341 73.927 39.184 1.00 25.18 ? 260 HIS B ND1 1 ATOM 1590 C CD2 . HIS B 2 12 ? 44.755 72.463 39.998 1.00 25.29 ? 260 HIS B CD2 1 ATOM 1591 C CE1 . HIS B 2 12 ? 44.549 74.470 39.117 1.00 25.78 ? 260 HIS B CE1 1 ATOM 1592 N NE2 . HIS B 2 12 ? 45.426 73.601 39.599 1.00 26.16 ? 260 HIS B NE2 1 ATOM 1593 N N . ASP B 2 13 ? 40.613 68.955 39.577 1.00 16.38 ? 261 ASP B N 1 ATOM 1594 C CA . ASP B 2 13 ? 39.392 68.226 39.936 1.00 16.02 ? 261 ASP B CA 1 ATOM 1595 C C . ASP B 2 13 ? 39.028 67.371 38.729 1.00 13.99 ? 261 ASP B C 1 ATOM 1596 O O . ASP B 2 13 ? 39.617 67.512 37.653 1.00 13.02 ? 261 ASP B O 1 ATOM 1597 C CB . ASP B 2 13 ? 38.248 69.185 40.291 1.00 16.24 ? 261 ASP B CB 1 ATOM 1598 C CG . ASP B 2 13 ? 37.167 68.546 41.179 1.00 20.10 ? 261 ASP B CG 1 ATOM 1599 O OD1 . ASP B 2 13 ? 37.049 67.291 41.278 1.00 18.97 ? 261 ASP B OD1 1 ATOM 1600 O OD2 . ASP B 2 13 ? 36.386 69.315 41.790 1.00 22.63 ? 261 ASP B OD2 1 ATOM 1601 N N . LEU B 2 14 ? 38.067 66.467 38.909 1.00 13.50 ? 262 LEU B N 1 ATOM 1602 C CA . LEU B 2 14 ? 37.629 65.601 37.827 1.00 13.14 ? 262 LEU B CA 1 ATOM 1603 C C . LEU B 2 14 ? 36.091 65.620 37.939 1.00 12.73 ? 262 LEU B C 1 ATOM 1604 O O . LEU B 2 14 ? 35.531 65.182 38.953 1.00 13.32 ? 262 LEU B O 1 ATOM 1605 C CB . LEU B 2 14 ? 38.178 64.176 38.033 1.00 13.41 ? 262 LEU B CB 1 ATOM 1606 C CG . LEU B 2 14 ? 37.665 63.110 37.072 1.00 13.78 ? 262 LEU B CG 1 ATOM 1607 C CD1 . LEU B 2 14 ? 37.969 63.410 35.618 1.00 13.81 ? 262 LEU B CD1 1 ATOM 1608 C CD2 . LEU B 2 14 ? 38.254 61.697 37.491 1.00 15.91 ? 262 LEU B CD2 1 ATOM 1609 N N . LEU B 2 15 ? 35.433 66.245 36.967 1.00 12.66 ? 263 LEU B N 1 ATOM 1610 C CA . LEU B 2 15 ? 33.980 66.440 37.022 1.00 12.28 ? 263 LEU B CA 1 ATOM 1611 C C . LEU B 2 15 ? 33.343 65.364 36.146 1.00 13.22 ? 263 LEU B C 1 ATOM 1612 O O . LEU B 2 15 ? 33.901 64.998 35.116 1.00 13.28 ? 263 LEU B O 1 ATOM 1613 C CB . LEU B 2 15 ? 33.601 67.839 36.493 1.00 13.88 ? 263 LEU B CB 1 ATOM 1614 C CG . LEU B 2 15 ? 34.268 69.027 37.194 1.00 14.83 ? 263 LEU B CG 1 ATOM 1615 C CD1 . LEU B 2 15 ? 33.643 70.359 36.611 1.00 16.73 ? 263 LEU B CD1 1 ATOM 1616 C CD2 . LEU B 2 15 ? 33.956 68.883 38.670 1.00 16.70 ? 263 LEU B CD2 1 ATOM 1617 N N . VAL B 2 16 ? 32.176 64.878 36.561 1.00 12.13 ? 264 VAL B N 1 ATOM 1618 C CA . VAL B 2 16 ? 31.473 63.856 35.801 1.00 12.34 ? 264 VAL B CA 1 ATOM 1619 C C . VAL B 2 16 ? 30.041 64.362 35.658 1.00 12.30 ? 264 VAL B C 1 ATOM 1620 O O . VAL B 2 16 ? 29.390 64.643 36.693 1.00 13.56 ? 264 VAL B O 1 ATOM 1621 C CB . VAL B 2 16 ? 31.502 62.540 36.575 1.00 13.29 ? 264 VAL B CB 1 ATOM 1622 C CG1 . VAL B 2 16 ? 30.694 61.453 35.831 1.00 14.60 ? 264 VAL B CG1 1 ATOM 1623 C CG2 . VAL B 2 16 ? 32.961 62.088 36.771 1.00 13.00 ? 264 VAL B CG2 1 ATOM 1624 N N . ALA B 2 17 ? 29.535 64.418 34.425 1.00 13.22 ? 265 ALA B N 1 ATOM 1625 C CA . ALA B 2 17 ? 28.166 64.941 34.191 1.00 11.41 ? 265 ALA B CA 1 ATOM 1626 C C . ALA B 2 17 ? 27.403 64.098 33.175 1.00 12.12 ? 265 ALA B C 1 ATOM 1627 O O . ALA B 2 17 ? 27.995 63.460 32.263 1.00 11.41 ? 265 ALA B O 1 ATOM 1628 C CB . ALA B 2 17 ? 28.229 66.400 33.723 1.00 12.97 ? 265 ALA B CB 1 ATOM 1629 N N . HIS B 2 18 ? 26.076 64.093 33.314 1.00 12.27 ? 266 HIS B N 1 ATOM 1630 C CA . HIS B 2 18 ? 25.241 63.259 32.416 1.00 11.42 ? 266 HIS B CA 1 ATOM 1631 C C . HIS B 2 18 ? 23.940 64.022 32.204 1.00 12.90 ? 266 HIS B C 1 ATOM 1632 O O . HIS B 2 18 ? 23.393 64.588 33.157 1.00 13.70 ? 266 HIS B O 1 ATOM 1633 C CB . HIS B 2 18 ? 24.951 61.924 33.125 1.00 13.00 ? 266 HIS B CB 1 ATOM 1634 C CG . HIS B 2 18 ? 24.081 60.984 32.330 1.00 13.08 ? 266 HIS B CG 1 ATOM 1635 N ND1 . HIS B 2 18 ? 22.697 61.002 32.412 1.00 13.85 ? 266 HIS B ND1 1 ATOM 1636 C CD2 . HIS B 2 18 ? 24.400 59.995 31.466 1.00 14.53 ? 266 HIS B CD2 1 ATOM 1637 C CE1 . HIS B 2 18 ? 22.211 60.074 31.600 1.00 14.82 ? 266 HIS B CE1 1 ATOM 1638 N NE2 . HIS B 2 18 ? 23.221 59.457 31.007 1.00 12.87 ? 266 HIS B NE2 1 ATOM 1639 N N . ASN B 2 19 ? 23.462 64.021 30.966 1.00 12.79 ? 267 ASN B N 1 ATOM 1640 C CA . ASN B 2 19 ? 22.194 64.684 30.622 1.00 14.60 ? 267 ASN B CA 1 ATOM 1641 C C . ASN B 2 19 ? 21.339 63.617 29.940 1.00 14.27 ? 267 ASN B C 1 ATOM 1642 O O . ASN B 2 19 ? 21.647 63.136 28.833 1.00 14.33 ? 267 ASN B O 1 ATOM 1643 C CB . ASN B 2 19 ? 22.564 65.901 29.731 1.00 15.48 ? 267 ASN B CB 1 ATOM 1644 C CG . ASN B 2 19 ? 21.506 66.276 28.769 1.00 23.30 ? 267 ASN B CG 1 ATOM 1645 O OD1 . ASN B 2 19 ? 20.320 66.299 29.116 1.00 27.66 ? 267 ASN B OD1 1 ATOM 1646 N ND2 . ASN B 2 19 ? 21.914 66.486 27.494 1.00 29.19 ? 267 ASN B ND2 1 ATOM 1647 N N . THR B 2 20 ? 20.271 63.210 30.613 1.00 13.90 ? 268 THR B N 1 ATOM 1648 C CA . THR B 2 20 ? 19.389 62.167 30.081 1.00 14.49 ? 268 THR B CA 1 ATOM 1649 C C . THR B 2 20 ? 18.553 62.722 28.948 1.00 15.15 ? 268 THR B C 1 ATOM 1650 O O . THR B 2 20 ? 17.992 63.800 29.118 1.00 14.96 ? 268 THR B O 1 ATOM 1651 C CB . THR B 2 20 ? 18.387 61.791 31.146 1.00 15.86 ? 268 THR B CB 1 ATOM 1652 O OG1 . THR B 2 20 ? 19.085 61.378 32.326 1.00 15.69 ? 268 THR B OG1 1 ATOM 1653 C CG2 . THR B 2 20 ? 17.457 60.663 30.665 1.00 20.04 ? 268 THR B CG2 1 ATOM 1654 N N . TRP B 2 21 ? 18.470 62.014 27.825 1.00 14.17 ? 269 TRP B N 1 ATOM 1655 C CA . TRP B 2 21 ? 17.473 62.389 26.814 1.00 15.16 ? 269 TRP B CA 1 ATOM 1656 C C . TRP B 2 21 ? 16.364 61.366 26.895 1.00 16.38 ? 269 TRP B C 1 ATOM 1657 O O . TRP B 2 21 ? 16.625 60.145 26.954 1.00 17.92 ? 269 TRP B O 1 ATOM 1658 C CB . TRP B 2 21 ? 18.069 62.365 25.431 1.00 16.30 ? 269 TRP B CB 1 ATOM 1659 C CG . TRP B 2 21 ? 19.134 63.431 25.135 1.00 15.77 ? 269 TRP B CG 1 ATOM 1660 C CD1 . TRP B 2 21 ? 19.840 64.223 26.022 1.00 14.04 ? 269 TRP B CD1 1 ATOM 1661 C CD2 . TRP B 2 21 ? 19.582 63.780 23.834 1.00 14.31 ? 269 TRP B CD2 1 ATOM 1662 N NE1 . TRP B 2 21 ? 20.704 65.053 25.307 1.00 13.00 ? 269 TRP B NE1 1 ATOM 1663 C CE2 . TRP B 2 21 ? 20.552 64.806 23.973 1.00 13.76 ? 269 TRP B CE2 1 ATOM 1664 C CE3 . TRP B 2 21 ? 19.221 63.342 22.539 1.00 16.72 ? 269 TRP B CE3 1 ATOM 1665 C CZ2 . TRP B 2 21 ? 21.207 65.396 22.867 1.00 15.18 ? 269 TRP B CZ2 1 ATOM 1666 C CZ3 . TRP B 2 21 ? 19.894 63.922 21.419 1.00 17.15 ? 269 TRP B CZ3 1 ATOM 1667 C CH2 . TRP B 2 21 ? 20.870 64.943 21.609 1.00 15.70 ? 269 TRP B CH2 1 ATOM 1668 N N . ASN B 2 22 ? 15.127 61.837 26.936 1.00 15.02 ? 270 ASN B N 1 ATOM 1669 C CA . ASN B 2 22 ? 14.023 60.891 27.087 1.00 16.40 ? 270 ASN B CA 1 ATOM 1670 C C . ASN B 2 22 ? 12.765 61.600 26.614 1.00 16.46 ? 270 ASN B C 1 ATOM 1671 O O . ASN B 2 22 ? 12.792 62.798 26.268 1.00 16.68 ? 270 ASN B O 1 ATOM 1672 C CB . ASN B 2 22 ? 13.931 60.602 28.584 1.00 16.90 ? 270 ASN B CB 1 ATOM 1673 C CG . ASN B 2 22 ? 13.173 59.374 28.917 1.00 22.92 ? 270 ASN B CG 1 ATOM 1674 O OD1 . ASN B 2 22 ? 12.556 58.735 28.063 1.00 24.33 ? 270 ASN B OD1 1 ATOM 1675 N ND2 . ASN B 2 22 ? 13.220 59.016 30.220 1.00 27.10 ? 270 ASN B ND2 1 ATOM 1676 N N . SER B 2 23 ? 11.668 60.857 26.572 1.00 16.82 ? 271 SER B N 1 ATOM 1677 C CA . SER B 2 23 ? 10.392 61.460 26.246 1.00 17.39 ? 271 SER B CA 1 ATOM 1678 C C . SER B 2 23 ? 9.969 62.352 27.387 1.00 17.09 ? 271 SER B C 1 ATOM 1679 O O . SER B 2 23 ? 10.166 62.052 28.578 1.00 18.15 ? 271 SER B O 1 ATOM 1680 C CB . SER B 2 23 ? 9.327 60.373 26.032 1.00 18.46 ? 271 SER B CB 1 ATOM 1681 O OG . SER B 2 23 ? 9.625 59.711 24.810 1.00 22.25 ? 271 SER B OG 1 ATOM 1682 N N . TYR B 2 24 ? 9.335 63.463 27.029 1.00 16.76 ? 272 TYR B N 1 ATOM 1683 C CA . TYR B 2 24 ? 8.878 64.423 28.025 1.00 17.14 ? 272 TYR B CA 1 ATOM 1684 C C . TYR B 2 24 ? 7.828 63.857 28.972 1.00 17.10 ? 272 TYR B C 1 ATOM 1685 O O . TYR B 2 24 ? 7.744 64.300 30.133 1.00 16.65 ? 272 TYR B O 1 ATOM 1686 C CB . TYR B 2 24 ? 8.359 65.703 27.335 1.00 16.92 ? 272 TYR B CB 1 ATOM 1687 C CG . TYR B 2 24 ? 9.419 66.520 26.646 1.00 17.92 ? 272 TYR B CG 1 ATOM 1688 C CD1 . TYR B 2 24 ? 9.063 67.521 25.756 1.00 21.28 ? 272 TYR B CD1 1 ATOM 1689 C CD2 . TYR B 2 24 ? 10.798 66.275 26.846 1.00 18.14 ? 272 TYR B CD2 1 ATOM 1690 C CE1 . TYR B 2 24 ? 10.020 68.285 25.120 1.00 18.06 ? 272 TYR B CE1 1 ATOM 1691 C CE2 . TYR B 2 24 ? 11.776 67.041 26.206 1.00 17.98 ? 272 TYR B CE2 1 ATOM 1692 C CZ . TYR B 2 24 ? 11.370 68.058 25.349 1.00 17.45 ? 272 TYR B CZ 1 ATOM 1693 O OH . TYR B 2 24 ? 12.291 68.835 24.685 1.00 17.13 ? 272 TYR B OH 1 ATOM 1694 N N . GLN B 2 25 ? 7.055 62.858 28.521 1.00 17.83 ? 273 GLN B N 1 ATOM 1695 C CA . GLN B 2 25 ? 6.055 62.287 29.421 1.00 18.80 ? 273 GLN B CA 1 ATOM 1696 C C . GLN B 2 25 ? 6.719 61.539 30.587 1.00 17.65 ? 273 GLN B C 1 ATOM 1697 O O . GLN B 2 25 ? 6.031 61.207 31.545 1.00 18.60 ? 273 GLN B O 1 ATOM 1698 C CB . GLN B 2 25 ? 5.080 61.365 28.708 1.00 18.55 ? 273 GLN B CB 1 ATOM 1699 C CG . GLN B 2 25 ? 5.734 60.182 28.152 1.00 25.79 ? 273 GLN B CG 1 ATOM 1700 C CD . GLN B 2 25 ? 5.258 59.902 26.751 1.00 36.25 ? 273 GLN B CD 1 ATOM 1701 O OE1 . GLN B 2 25 ? 6.056 59.832 25.808 1.00 39.05 ? 273 GLN B OE1 1 ATOM 1702 N NE2 . GLN B 2 25 ? 3.928 59.793 26.592 1.00 36.40 ? 273 GLN B NE2 1 ATOM 1703 N N . ASN B 2 26 ? 8.047 61.313 30.530 1.00 16.70 ? 274 ASN B N 1 ATOM 1704 C CA . ASN B 2 26 ? 8.740 60.595 31.607 1.00 16.87 ? 274 ASN B CA 1 ATOM 1705 C C . ASN B 2 26 ? 9.256 61.484 32.726 1.00 17.48 ? 274 ASN B C 1 ATOM 1706 O O . ASN B 2 26 ? 9.881 60.997 33.656 1.00 18.54 ? 274 ASN B O 1 ATOM 1707 C CB . ASN B 2 26 ? 9.890 59.760 31.019 1.00 17.50 ? 274 ASN B CB 1 ATOM 1708 C CG . ASN B 2 26 ? 9.367 58.621 30.172 1.00 21.25 ? 274 ASN B CG 1 ATOM 1709 O OD1 . ASN B 2 26 ? 8.567 58.829 29.241 1.00 27.51 ? 274 ASN B OD1 1 ATOM 1710 N ND2 . ASN B 2 26 ? 9.717 57.438 30.530 1.00 25.42 ? 274 ASN B ND2 1 ATOM 1711 N N . MET B 2 27 ? 8.969 62.781 32.660 1.00 17.37 ? 275 MET B N 1 ATOM 1712 C CA . MET B 2 27 ? 9.544 63.749 33.599 1.00 17.11 ? 275 MET B CA 1 ATOM 1713 C C . MET B 2 27 ? 8.885 63.848 34.991 1.00 17.39 ? 275 MET B C 1 ATOM 1714 O O . MET B 2 27 ? 8.686 64.951 35.513 1.00 19.07 ? 275 MET B O 1 ATOM 1715 C CB . MET B 2 27 ? 9.630 65.146 32.972 1.00 18.58 ? 275 MET B CB 1 ATOM 1716 C CG . MET B 2 27 ? 10.527 65.202 31.762 1.00 18.69 ? 275 MET B CG 1 ATOM 1717 S SD . MET B 2 27 ? 10.883 66.855 31.137 1.00 20.91 ? 275 MET B SD 1 ATOM 1718 C CE . MET B 2 27 ? 9.229 67.457 30.732 1.00 20.05 ? 275 MET B CE 1 ATOM 1719 N N . LEU B 2 28 ? 8.502 62.729 35.576 1.00 16.41 ? 276 LEU B N 1 ATOM 1720 C CA . LEU B 2 28 ? 8.330 62.676 37.036 1.00 16.01 ? 276 LEU B CA 1 ATOM 1721 C C . LEU B 2 28 ? 9.605 62.047 37.602 1.00 15.24 ? 276 LEU B C 1 ATOM 1722 O O . LEU B 2 28 ? 9.915 60.871 37.280 1.00 14.76 ? 276 LEU B O 1 ATOM 1723 C CB . LEU B 2 28 ? 7.147 61.809 37.422 1.00 16.31 ? 276 LEU B CB 1 ATOM 1724 C CG . LEU B 2 28 ? 5.744 62.397 37.224 1.00 17.46 ? 276 LEU B CG 1 ATOM 1725 C CD1 . LEU B 2 28 ? 4.667 61.352 37.625 1.00 21.22 ? 276 LEU B CD1 1 ATOM 1726 C CD2 . LEU B 2 28 ? 5.553 63.736 38.022 1.00 18.79 ? 276 LEU B CD2 1 ATOM 1727 N N . ARG B 2 29 ? 10.326 62.801 38.418 1.00 15.11 ? 277 ARG B N 1 ATOM 1728 C CA . ARG B 2 29 ? 11.715 62.428 38.741 1.00 14.85 ? 277 ARG B CA 1 ATOM 1729 C C . ARG B 2 29 ? 11.893 62.284 40.224 1.00 15.89 ? 277 ARG B C 1 ATOM 1730 O O . ARG B 2 29 ? 11.345 63.053 41.035 1.00 15.19 ? 277 ARG B O 1 ATOM 1731 C CB . ARG B 2 29 ? 12.711 63.488 38.262 1.00 15.20 ? 277 ARG B CB 1 ATOM 1732 C CG . ARG B 2 29 ? 12.619 63.818 36.774 1.00 15.61 ? 277 ARG B CG 1 ATOM 1733 C CD . ARG B 2 29 ? 12.763 62.589 35.921 1.00 14.29 ? 277 ARG B CD 1 ATOM 1734 N NE . ARG B 2 29 ? 13.919 61.760 36.305 1.00 14.01 ? 277 ARG B NE 1 ATOM 1735 C CZ . ARG B 2 29 ? 15.157 61.943 35.846 1.00 17.60 ? 277 ARG B CZ 1 ATOM 1736 N NH1 . ARG B 2 29 ? 16.133 61.102 36.215 1.00 15.34 ? 277 ARG B NH1 1 ATOM 1737 N NH2 . ARG B 2 29 ? 15.409 62.993 35.062 1.00 16.07 ? 277 ARG B NH2 1 ATOM 1738 N N . ILE B 2 30 ? 12.670 61.285 40.602 1.00 15.26 ? 278 ILE B N 1 ATOM 1739 C CA . ILE B 2 30 ? 13.000 61.119 42.005 1.00 15.12 ? 278 ILE B CA 1 ATOM 1740 C C . ILE B 2 30 ? 14.506 60.886 42.086 1.00 16.50 ? 278 ILE B C 1 ATOM 1741 O O . ILE B 2 30 ? 15.027 59.998 41.399 1.00 15.90 ? 278 ILE B O 1 ATOM 1742 C CB . ILE B 2 30 ? 12.250 59.935 42.659 1.00 14.73 ? 278 ILE B CB 1 ATOM 1743 C CG1 . ILE B 2 30 ? 10.725 60.017 42.436 1.00 15.89 ? 278 ILE B CG1 1 ATOM 1744 C CG2 . ILE B 2 30 ? 12.634 59.853 44.148 1.00 14.50 ? 278 ILE B CG2 1 ATOM 1745 C CD1 . ILE B 2 30 ? 9.994 58.814 43.071 1.00 16.76 ? 278 ILE B CD1 1 ATOM 1746 N N . ILE B 2 31 ? 15.205 61.697 42.878 1.00 16.00 ? 279 ILE B N 1 ATOM 1747 C CA . ILE B 2 31 ? 16.598 61.395 43.229 1.00 16.51 ? 279 ILE B CA 1 ATOM 1748 C C . ILE B 2 31 ? 16.572 60.492 44.464 1.00 15.74 ? 279 ILE B C 1 ATOM 1749 O O . ILE B 2 31 ? 15.928 60.812 45.465 1.00 16.94 ? 279 ILE B O 1 ATOM 1750 C CB . ILE B 2 31 ? 17.404 62.668 43.457 1.00 17.27 ? 279 ILE B CB 1 ATOM 1751 C CG1 . ILE B 2 31 ? 17.578 63.378 42.090 1.00 20.94 ? 279 ILE B CG1 1 ATOM 1752 C CG2 . ILE B 2 31 ? 18.795 62.336 44.069 1.00 17.99 ? 279 ILE B CG2 1 ATOM 1753 C CD1 . ILE B 2 31 ? 18.183 64.699 42.138 1.00 26.34 ? 279 ILE B CD1 1 ATOM 1754 N N . LYS B 2 32 ? 17.237 59.348 44.394 1.00 13.97 ? 280 LYS B N 1 ATOM 1755 C CA . LYS B 2 32 ? 17.065 58.328 45.430 1.00 14.04 ? 280 LYS B CA 1 ATOM 1756 C C . LYS B 2 32 ? 18.388 58.094 46.132 1.00 15.12 ? 280 LYS B C 1 ATOM 1757 O O . LYS B 2 32 ? 19.442 58.036 45.480 1.00 15.27 ? 280 LYS B O 1 ATOM 1758 C CB . LYS B 2 32 ? 16.562 57.008 44.812 1.00 14.18 ? 280 LYS B CB 1 ATOM 1759 C CG . LYS B 2 32 ? 15.188 57.132 44.186 1.00 14.11 ? 280 LYS B CG 1 ATOM 1760 C CD . LYS B 2 32 ? 14.736 55.829 43.552 1.00 15.46 ? 280 LYS B CD 1 ATOM 1761 C CE . LYS B 2 32 ? 13.325 56.104 42.928 1.00 17.31 ? 280 LYS B CE 1 ATOM 1762 N NZ . LYS B 2 32 ? 12.777 54.871 42.290 1.00 17.21 ? 280 LYS B NZ 1 ATOM 1763 N N . LYS B 2 33 ? 18.339 57.974 47.463 1.00 15.09 ? 281 LYS B N 1 ATOM 1764 C CA . LYS B 2 33 ? 19.535 57.649 48.252 1.00 16.05 ? 281 LYS B CA 1 ATOM 1765 C C . LYS B 2 33 ? 19.189 56.348 48.953 1.00 16.80 ? 281 LYS B C 1 ATOM 1766 O O . LYS B 2 33 ? 18.195 56.290 49.715 1.00 16.27 ? 281 LYS B O 1 ATOM 1767 C CB . LYS B 2 33 ? 19.782 58.759 49.287 1.00 16.93 ? 281 LYS B CB 1 ATOM 1768 C CG . LYS B 2 33 ? 20.942 58.426 50.229 1.00 23.10 ? 281 LYS B CG 1 ATOM 1769 C CD . LYS B 2 33 ? 21.353 59.693 51.001 1.00 31.15 ? 281 LYS B CD 1 ATOM 1770 C CE . LYS B 2 33 ? 22.839 59.725 51.243 1.00 36.94 ? 281 LYS B CE 1 ATOM 1771 N NZ . LYS B 2 33 ? 23.309 58.535 51.996 1.00 40.62 ? 281 LYS B NZ 1 ATOM 1772 N N . TYR B 2 34 ? 19.951 55.287 48.670 1.00 15.28 ? 282 TYR B N 1 ATOM 1773 C CA . TYR B 2 34 ? 19.739 54.020 49.369 1.00 15.93 ? 282 TYR B CA 1 ATOM 1774 C C . TYR B 2 34 ? 20.900 53.775 50.339 1.00 15.83 ? 282 TYR B C 1 ATOM 1775 O O . TYR B 2 34 ? 22.064 53.996 49.976 1.00 16.32 ? 282 TYR B O 1 ATOM 1776 C CB . TYR B 2 34 ? 19.708 52.854 48.372 1.00 17.01 ? 282 TYR B CB 1 ATOM 1777 C CG . TYR B 2 34 ? 18.500 52.709 47.460 1.00 17.07 ? 282 TYR B CG 1 ATOM 1778 C CD1 . TYR B 2 34 ? 18.529 51.748 46.407 1.00 17.84 ? 282 TYR B CD1 1 ATOM 1779 C CD2 . TYR B 2 34 ? 17.336 53.475 47.613 1.00 17.37 ? 282 TYR B CD2 1 ATOM 1780 C CE1 . TYR B 2 34 ? 17.438 51.570 45.537 1.00 19.32 ? 282 TYR B CE1 1 ATOM 1781 C CE2 . TYR B 2 34 ? 16.198 53.271 46.736 1.00 18.83 ? 282 TYR B CE2 1 ATOM 1782 C CZ . TYR B 2 34 ? 16.277 52.313 45.703 1.00 18.08 ? 282 TYR B CZ 1 ATOM 1783 O OH . TYR B 2 34 ? 15.247 52.082 44.779 1.00 19.22 ? 282 TYR B OH 1 ATOM 1784 N N . ARG B 2 35 ? 20.589 53.337 51.556 1.00 15.53 ? 283 ARG B N 1 ATOM 1785 C CA . ARG B 2 35 ? 21.617 52.878 52.477 1.00 17.33 ? 283 ARG B CA 1 ATOM 1786 C C . ARG B 2 35 ? 21.254 51.471 52.908 1.00 17.07 ? 283 ARG B C 1 ATOM 1787 O O . ARG B 2 35 ? 20.426 51.291 53.824 1.00 16.33 ? 283 ARG B O 1 ATOM 1788 C CB . ARG B 2 35 ? 21.660 53.802 53.691 1.00 18.56 ? 283 ARG B CB 1 ATOM 1789 C CG . ARG B 2 35 ? 22.107 55.216 53.298 1.00 25.21 ? 283 ARG B CG 1 ATOM 1790 C CD . ARG B 2 35 ? 21.909 56.254 54.415 1.00 32.85 ? 283 ARG B CD 1 ATOM 1791 N NE . ARG B 2 35 ? 20.539 56.370 54.922 1.00 39.23 ? 283 ARG B NE 1 ATOM 1792 C CZ . ARG B 2 35 ? 19.416 56.568 54.201 1.00 41.71 ? 283 ARG B CZ 1 ATOM 1793 N NH1 . ARG B 2 35 ? 18.234 56.663 54.841 1.00 42.96 ? 283 ARG B NH1 1 ATOM 1794 N NH2 . ARG B 2 35 ? 19.435 56.664 52.868 1.00 34.95 ? 283 ARG B NH2 1 ATOM 1795 N N . LEU B 2 36 ? 21.867 50.482 52.251 1.00 16.22 ? 284 LEU B N 1 ATOM 1796 C CA . LEU B 2 36 ? 21.475 49.092 52.416 1.00 15.62 ? 284 LEU B CA 1 ATOM 1797 C C . LEU B 2 36 ? 22.478 48.361 53.289 1.00 15.50 ? 284 LEU B C 1 ATOM 1798 O O . LEU B 2 36 ? 23.519 48.925 53.658 1.00 15.72 ? 284 LEU B O 1 ATOM 1799 C CB . LEU B 2 36 ? 21.366 48.430 51.021 1.00 16.49 ? 284 LEU B CB 1 ATOM 1800 C CG . LEU B 2 36 ? 20.530 49.261 50.035 1.00 15.72 ? 284 LEU B CG 1 ATOM 1801 C CD1 . LEU B 2 36 ? 20.597 48.618 48.636 1.00 21.18 ? 284 LEU B CD1 1 ATOM 1802 C CD2 . LEU B 2 36 ? 19.124 49.319 50.563 1.00 19.50 ? 284 LEU B CD2 1 ATOM 1803 N N . GLN B 2 37 ? 22.160 47.122 53.669 1.00 15.70 ? 285 GLN B N 1 ATOM 1804 C CA . GLN B 2 37 ? 23.134 46.292 54.409 1.00 15.57 ? 285 GLN B CA 1 ATOM 1805 C C . GLN B 2 37 ? 23.205 44.890 53.804 1.00 15.05 ? 285 GLN B C 1 ATOM 1806 O O . GLN B 2 37 ? 23.106 43.853 54.511 1.00 14.40 ? 285 GLN B O 1 ATOM 1807 C CB . GLN B 2 37 ? 22.728 46.192 55.893 1.00 16.35 ? 285 GLN B CB 1 ATOM 1808 C CG . GLN B 2 37 ? 22.665 47.548 56.615 1.00 18.91 ? 285 GLN B CG 1 ATOM 1809 C CD . GLN B 2 37 ? 24.028 48.189 56.863 1.00 23.89 ? 285 GLN B CD 1 ATOM 1810 O OE1 . GLN B 2 37 ? 25.046 47.516 57.017 1.00 23.68 ? 285 GLN B OE1 1 ATOM 1811 N NE2 . GLN B 2 37 ? 24.033 49.532 56.936 1.00 25.92 ? 285 GLN B NE2 1 ATOM 1812 N N . PHE B 2 38 ? 23.336 44.844 52.484 1.00 14.97 ? 286 PHE B N 1 ATOM 1813 C CA . PHE B 2 38 ? 23.377 43.550 51.789 1.00 15.35 ? 286 PHE B CA 1 ATOM 1814 C C . PHE B 2 38 ? 24.778 42.947 51.878 1.00 16.36 ? 286 PHE B C 1 ATOM 1815 O O . PHE B 2 38 ? 25.769 43.676 52.001 1.00 15.56 ? 286 PHE B O 1 ATOM 1816 C CB . PHE B 2 38 ? 23.026 43.709 50.296 1.00 14.74 ? 286 PHE B CB 1 ATOM 1817 C CG . PHE B 2 38 ? 21.610 44.179 50.026 1.00 14.28 ? 286 PHE B CG 1 ATOM 1818 C CD1 . PHE B 2 38 ? 21.256 44.526 48.724 1.00 15.85 ? 286 PHE B CD1 1 ATOM 1819 C CD2 . PHE B 2 38 ? 20.652 44.313 51.042 1.00 16.33 ? 286 PHE B CD2 1 ATOM 1820 C CE1 . PHE B 2 38 ? 19.979 44.965 48.406 1.00 17.94 ? 286 PHE B CE1 1 ATOM 1821 C CE2 . PHE B 2 38 ? 19.370 44.772 50.733 1.00 18.95 ? 286 PHE B CE2 1 ATOM 1822 C CZ . PHE B 2 38 ? 19.027 45.096 49.410 1.00 18.05 ? 286 PHE B CZ 1 ATOM 1823 N N . ARG B 2 39 ? 24.856 41.622 51.755 1.00 16.17 ? 287 ARG B N 1 ATOM 1824 C CA . ARG B 2 39 ? 26.139 40.924 51.789 1.00 17.02 ? 287 ARG B CA 1 ATOM 1825 C C . ARG B 2 39 ? 26.435 40.342 50.408 1.00 18.59 ? 287 ARG B C 1 ATOM 1826 O O . ARG B 2 39 ? 25.527 40.210 49.568 1.00 17.83 ? 287 ARG B O 1 ATOM 1827 C CB . ARG B 2 39 ? 26.089 39.784 52.821 1.00 18.41 ? 287 ARG B CB 1 ATOM 1828 C CG . ARG B 2 39 ? 26.085 40.359 54.241 1.00 21.48 ? 287 ARG B CG 1 ATOM 1829 C CD . ARG B 2 39 ? 26.270 39.361 55.344 1.00 25.29 ? 287 ARG B CD 1 ATOM 1830 N NE . ARG B 2 39 ? 26.159 40.137 56.578 1.00 27.38 ? 287 ARG B NE 1 ATOM 1831 C CZ . ARG B 2 39 ? 27.175 40.729 57.197 1.00 29.11 ? 287 ARG B CZ 1 ATOM 1832 N NH1 . ARG B 2 39 ? 26.924 41.453 58.281 1.00 32.11 ? 287 ARG B NH1 1 ATOM 1833 N NH2 . ARG B 2 39 ? 28.433 40.568 56.787 1.00 26.37 ? 287 ARG B NH2 1 ATOM 1834 N N . GLU B 2 40 ? 27.707 40.018 50.178 1.00 18.07 ? 288 GLU B N 1 ATOM 1835 C CA . GLU B 2 40 ? 28.148 39.583 48.853 1.00 20.57 ? 288 GLU B CA 1 ATOM 1836 C C . GLU B 2 40 ? 27.542 38.241 48.507 1.00 21.34 ? 288 GLU B C 1 ATOM 1837 O O . GLU B 2 40 ? 27.297 37.932 47.333 1.00 23.84 ? 288 GLU B O 1 ATOM 1838 C CB . GLU B 2 40 ? 29.673 39.513 48.819 1.00 19.97 ? 288 GLU B CB 1 ATOM 1839 C CG . GLU B 2 40 ? 30.284 40.892 48.717 1.00 24.64 ? 288 GLU B CG 1 ATOM 1840 C CD . GLU B 2 40 ? 31.789 40.866 48.694 1.00 30.61 ? 288 GLU B CD 1 ATOM 1841 O OE1 . GLU B 2 40 ? 32.375 39.803 49.025 1.00 33.26 ? 288 GLU B OE1 1 ATOM 1842 O OE2 . GLU B 2 40 ? 32.377 41.923 48.367 1.00 31.29 ? 288 GLU B OE2 1 ATOM 1843 N N . GLY B 2 41 ? 27.266 37.440 49.526 1.00 20.99 ? 289 GLY B N 1 ATOM 1844 C CA . GLY B 2 41 ? 26.800 36.085 49.268 1.00 21.50 ? 289 GLY B CA 1 ATOM 1845 C C . GLY B 2 41 ? 25.709 35.685 50.244 1.00 22.60 ? 289 GLY B C 1 ATOM 1846 O O . GLY B 2 41 ? 25.375 36.443 51.166 1.00 21.39 ? 289 GLY B O 1 ATOM 1847 N N . PRO B 2 42 ? 25.126 34.496 50.031 1.00 23.90 ? 290 PRO B N 1 ATOM 1848 C CA . PRO B 2 42 ? 23.928 34.054 50.718 1.00 25.48 ? 290 PRO B CA 1 ATOM 1849 C C . PRO B 2 42 ? 24.119 33.595 52.147 1.00 27.35 ? 290 PRO B C 1 ATOM 1850 O O . PRO B 2 42 ? 23.188 33.069 52.731 1.00 28.68 ? 290 PRO B O 1 ATOM 1851 C CB . PRO B 2 42 ? 23.440 32.878 49.850 1.00 25.84 ? 290 PRO B CB 1 ATOM 1852 C CG . PRO B 2 42 ? 24.676 32.357 49.191 1.00 24.69 ? 290 PRO B CG 1 ATOM 1853 C CD . PRO B 2 42 ? 25.553 33.555 48.970 1.00 24.47 ? 290 PRO B CD 1 ATOM 1854 N N . GLN B 2 43 ? 25.315 33.765 52.693 1.00 28.17 ? 291 GLN B N 1 ATOM 1855 C CA . GLN B 2 43 ? 25.590 33.385 54.081 1.00 29.59 ? 291 GLN B CA 1 ATOM 1856 C C . GLN B 2 43 ? 26.068 34.631 54.863 1.00 30.20 ? 291 GLN B C 1 ATOM 1857 O O . GLN B 2 43 ? 26.736 35.499 54.303 1.00 29.17 ? 291 GLN B O 1 ATOM 1858 C CB . GLN B 2 43 ? 26.642 32.256 54.097 1.00 29.94 ? 291 GLN B CB 1 ATOM 1859 C CG . GLN B 2 43 ? 26.073 30.805 53.775 1.00 31.22 ? 291 GLN B CG 1 ATOM 1860 C CD . GLN B 2 43 ? 26.121 30.383 52.274 1.00 35.34 ? 291 GLN B CD 1 ATOM 1861 O OE1 . GLN B 2 43 ? 27.084 30.666 51.544 1.00 33.49 ? 291 GLN B OE1 1 ATOM 1862 N NE2 . GLN B 2 43 ? 25.076 29.670 51.829 1.00 37.23 ? 291 GLN B NE2 1 ATOM 1863 N N . GLU B 2 44 ? 25.730 34.702 56.150 1.00 30.86 ? 292 GLU B N 1 ATOM 1864 C CA . GLU B 2 44 ? 26.091 35.839 57.000 1.00 31.62 ? 292 GLU B CA 1 ATOM 1865 C C . GLU B 2 44 ? 27.604 36.081 57.088 1.00 30.68 ? 292 GLU B C 1 ATOM 1866 O O . GLU B 2 44 ? 28.042 37.192 57.388 1.00 30.74 ? 292 GLU B O 1 ATOM 1867 C CB . GLU B 2 44 ? 25.513 35.606 58.404 1.00 33.98 ? 292 GLU B CB 1 ATOM 1868 C CG . GLU B 2 44 ? 25.074 36.863 59.144 1.00 38.58 ? 292 GLU B CG 1 ATOM 1869 C CD . GLU B 2 44 ? 24.121 37.773 58.336 1.00 44.95 ? 292 GLU B CD 1 ATOM 1870 O OE1 . GLU B 2 44 ? 24.196 39.008 58.534 1.00 44.95 ? 292 GLU B OE1 1 ATOM 1871 O OE2 . GLU B 2 44 ? 23.288 37.268 57.530 1.00 49.97 ? 292 GLU B OE2 1 ATOM 1872 N N . GLU B 2 45 ? 28.400 35.047 56.822 1.00 28.89 ? 293 GLU B N 1 ATOM 1873 C CA . GLU B 2 45 ? 29.860 35.148 56.807 1.00 28.11 ? 293 GLU B CA 1 ATOM 1874 C C . GLU B 2 45 ? 30.432 36.004 55.686 1.00 26.42 ? 293 GLU B C 1 ATOM 1875 O O . GLU B 2 45 ? 31.550 36.503 55.796 1.00 25.50 ? 293 GLU B O 1 ATOM 1876 C CB . GLU B 2 45 ? 30.486 33.758 56.678 1.00 30.22 ? 293 GLU B CB 1 ATOM 1877 C CG . GLU B 2 45 ? 30.335 32.917 57.914 1.00 35.13 ? 293 GLU B CG 1 ATOM 1878 C CD . GLU B 2 45 ? 28.886 32.543 58.206 1.00 41.25 ? 293 GLU B CD 1 ATOM 1879 O OE1 . GLU B 2 45 ? 28.138 32.166 57.267 1.00 42.25 ? 293 GLU B OE1 1 ATOM 1880 O OE2 . GLU B 2 45 ? 28.498 32.620 59.394 1.00 46.47 ? 293 GLU B OE2 1 ATOM 1881 N N . TYR B 2 46 ? 29.691 36.152 54.586 1.00 22.84 ? 294 TYR B N 1 ATOM 1882 C CA . TYR B 2 46 ? 30.164 36.996 53.495 1.00 22.10 ? 294 TYR B CA 1 ATOM 1883 C C . TYR B 2 46 ? 30.279 38.438 53.948 1.00 20.90 ? 294 TYR B C 1 ATOM 1884 O O . TYR B 2 46 ? 29.467 38.887 54.754 1.00 20.71 ? 294 TYR B O 1 ATOM 1885 C CB . TYR B 2 46 ? 29.154 36.941 52.347 1.00 21.54 ? 294 TYR B CB 1 ATOM 1886 C CG . TYR B 2 46 ? 29.416 35.770 51.430 1.00 21.69 ? 294 TYR B CG 1 ATOM 1887 C CD1 . TYR B 2 46 ? 28.816 34.552 51.649 1.00 23.19 ? 294 TYR B CD1 1 ATOM 1888 C CD2 . TYR B 2 46 ? 30.304 35.891 50.372 1.00 22.15 ? 294 TYR B CD2 1 ATOM 1889 C CE1 . TYR B 2 46 ? 29.073 33.448 50.790 1.00 21.16 ? 294 TYR B CE1 1 ATOM 1890 C CE2 . TYR B 2 46 ? 30.569 34.810 49.519 1.00 22.99 ? 294 TYR B CE2 1 ATOM 1891 C CZ . TYR B 2 46 ? 29.922 33.601 49.732 1.00 23.69 ? 294 TYR B CZ 1 ATOM 1892 O OH . TYR B 2 46 ? 30.199 32.523 48.899 1.00 23.41 ? 294 TYR B OH 1 ATOM 1893 N N . PRO B 2 47 ? 31.255 39.170 53.402 1.00 21.20 ? 295 PRO B N 1 ATOM 1894 C CA . PRO B 2 47 ? 31.404 40.606 53.676 1.00 20.89 ? 295 PRO B CA 1 ATOM 1895 C C . PRO B 2 47 ? 30.194 41.376 53.166 1.00 20.09 ? 295 PRO B C 1 ATOM 1896 O O . PRO B 2 47 ? 29.509 40.913 52.220 1.00 19.03 ? 295 PRO B O 1 ATOM 1897 C CB . PRO B 2 47 ? 32.615 41.005 52.845 1.00 22.08 ? 295 PRO B CB 1 ATOM 1898 C CG . PRO B 2 47 ? 33.344 39.697 52.572 1.00 24.30 ? 295 PRO B CG 1 ATOM 1899 C CD . PRO B 2 47 ? 32.300 38.658 52.498 1.00 21.95 ? 295 PRO B CD 1 ATOM 1900 N N . LEU B 2 48 ? 29.953 42.541 53.758 1.00 18.79 ? 296 LEU B N 1 ATOM 1901 C CA . LEU B 2 48 ? 28.988 43.494 53.188 1.00 18.29 ? 296 LEU B CA 1 ATOM 1902 C C . LEU B 2 48 ? 29.437 43.884 51.767 1.00 17.91 ? 296 LEU B C 1 ATOM 1903 O O . LEU B 2 48 ? 30.635 44.001 51.499 1.00 18.61 ? 296 LEU B O 1 ATOM 1904 C CB . LEU B 2 48 ? 28.921 44.736 54.079 1.00 18.83 ? 296 LEU B CB 1 ATOM 1905 C CG . LEU B 2 48 ? 28.278 44.440 55.425 1.00 19.83 ? 296 LEU B CG 1 ATOM 1906 C CD1 . LEU B 2 48 ? 28.609 45.569 56.392 1.00 23.37 ? 296 LEU B CD1 1 ATOM 1907 C CD2 . LEU B 2 48 ? 26.758 44.279 55.226 1.00 19.95 ? 296 LEU B CD2 1 ATOM 1908 N N . VAL B 2 49 ? 28.486 44.083 50.849 1.00 17.28 ? 297 VAL B N 1 ATOM 1909 C CA . VAL B 2 49 ? 28.865 44.487 49.485 1.00 17.66 ? 297 VAL B CA 1 ATOM 1910 C C . VAL B 2 49 ? 29.533 45.880 49.481 1.00 17.80 ? 297 VAL B C 1 ATOM 1911 O O . VAL B 2 49 ? 29.310 46.698 50.372 1.00 18.87 ? 297 VAL B O 1 ATOM 1912 C CB . VAL B 2 49 ? 27.678 44.489 48.499 1.00 16.81 ? 297 VAL B CB 1 ATOM 1913 C CG1 . VAL B 2 49 ? 27.025 43.110 48.393 1.00 17.09 ? 297 VAL B CG1 1 ATOM 1914 C CG2 . VAL B 2 49 ? 26.593 45.532 48.890 1.00 17.16 ? 297 VAL B CG2 1 ATOM 1915 N N . ALA B 2 50 ? 30.293 46.169 48.427 1.00 17.03 ? 298 ALA B N 1 ATOM 1916 C CA . ALA B 2 50 ? 30.999 47.439 48.315 1.00 16.57 ? 298 ALA B CA 1 ATOM 1917 C C . ALA B 2 50 ? 30.047 48.602 48.065 1.00 16.95 ? 298 ALA B C 1 ATOM 1918 O O . ALA B 2 50 ? 30.344 49.728 48.472 1.00 17.09 ? 298 ALA B O 1 ATOM 1919 C CB . ALA B 2 50 ? 31.985 47.367 47.184 1.00 17.78 ? 298 ALA B CB 1 ATOM 1920 N N . GLY B 2 51 ? 28.944 48.308 47.363 1.00 16.80 ? 299 GLY B N 1 ATOM 1921 C CA . GLY B 2 51 ? 27.982 49.323 46.917 1.00 15.71 ? 299 GLY B CA 1 ATOM 1922 C C . GLY B 2 51 ? 26.717 49.398 47.768 1.00 16.92 ? 299 GLY B C 1 ATOM 1923 O O . GLY B 2 51 ? 25.632 49.551 47.219 1.00 16.22 ? 299 GLY B O 1 ATOM 1924 N N . ASN B 2 52 ? 26.809 49.283 49.104 1.00 15.74 ? 300 ASN B N 1 ATOM 1925 C CA . ASN B 2 52 ? 25.590 49.395 49.917 1.00 15.84 ? 300 ASN B CA 1 ATOM 1926 C C . ASN B 2 52 ? 25.007 50.796 49.988 1.00 16.81 ? 300 ASN B C 1 ATOM 1927 O O . ASN B 2 52 ? 23.807 50.970 50.313 1.00 17.78 ? 300 ASN B O 1 ATOM 1928 C CB . ASN B 2 52 ? 25.825 48.897 51.360 1.00 16.13 ? 300 ASN B CB 1 ATOM 1929 C CG . ASN B 2 52 ? 25.417 47.458 51.538 1.00 17.58 ? 300 ASN B CG 1 ATOM 1930 O OD1 . ASN B 2 52 ? 24.431 46.995 50.953 1.00 16.10 ? 300 ASN B OD1 1 ATOM 1931 N ND2 . ASN B 2 52 ? 26.165 46.744 52.356 1.00 16.33 ? 300 ASN B ND2 1 ATOM 1932 N N . ASN B 2 53 ? 25.840 51.813 49.744 1.00 15.01 ? 301 ASN B N 1 ATOM 1933 C CA . ASN B 2 53 ? 25.317 53.189 49.784 1.00 15.83 ? 301 ASN B CA 1 ATOM 1934 C C . ASN B 2 53 ? 25.347 53.739 48.364 1.00 15.19 ? 301 ASN B C 1 ATOM 1935 O O . ASN B 2 53 ? 26.378 53.630 47.682 1.00 16.43 ? 301 ASN B O 1 ATOM 1936 C CB . ASN B 2 53 ? 26.196 54.049 50.688 1.00 15.98 ? 301 ASN B CB 1 ATOM 1937 C CG . ASN B 2 53 ? 26.085 53.651 52.160 1.00 19.86 ? 301 ASN B CG 1 ATOM 1938 O OD1 . ASN B 2 53 ? 25.005 53.358 52.651 1.00 24.05 ? 301 ASN B OD1 1 ATOM 1939 N ND2 . ASN B 2 53 ? 27.214 53.675 52.876 1.00 25.39 ? 301 ASN B ND2 1 ATOM 1940 N N . LEU B 2 54 ? 24.259 54.345 47.916 1.00 14.74 ? 302 LEU B N 1 ATOM 1941 C CA . LEU B 2 54 ? 24.266 54.869 46.555 1.00 14.48 ? 302 LEU B CA 1 ATOM 1942 C C . LEU B 2 54 ? 23.237 55.982 46.450 1.00 14.74 ? 302 LEU B C 1 ATOM 1943 O O . LEU B 2 54 ? 22.228 55.991 47.173 1.00 15.62 ? 302 LEU B O 1 ATOM 1944 C CB . LEU B 2 54 ? 23.967 53.797 45.505 1.00 15.29 ? 302 LEU B CB 1 ATOM 1945 C CG . LEU B 2 54 ? 22.701 52.962 45.637 1.00 16.09 ? 302 LEU B CG 1 ATOM 1946 C CD1 . LEU B 2 54 ? 22.416 52.285 44.246 1.00 20.23 ? 302 LEU B CD1 1 ATOM 1947 C CD2 . LEU B 2 54 ? 22.820 51.892 46.735 1.00 18.37 ? 302 LEU B CD2 1 ATOM 1948 N N . VAL B 2 55 ? 23.533 56.934 45.576 1.00 14.03 ? 303 VAL B N 1 ATOM 1949 C CA A VAL B 2 55 ? 22.614 58.028 45.280 0.50 13.71 ? 303 VAL B CA 1 ATOM 1950 C CA B VAL B 2 55 ? 22.576 57.978 45.277 0.50 13.80 ? 303 VAL B CA 1 ATOM 1951 C C . VAL B 2 55 ? 22.506 58.046 43.770 1.00 13.70 ? 303 VAL B C 1 ATOM 1952 O O . VAL B 2 55 ? 23.537 57.924 43.073 1.00 12.90 ? 303 VAL B O 1 ATOM 1953 C CB A VAL B 2 55 ? 23.146 59.406 45.746 0.50 14.32 ? 303 VAL B CB 1 ATOM 1954 C CB B VAL B 2 55 ? 22.925 59.350 45.918 0.50 14.30 ? 303 VAL B CB 1 ATOM 1955 C CG1 A VAL B 2 55 ? 22.086 60.498 45.507 0.50 12.77 ? 303 VAL B CG1 1 ATOM 1956 C CG1 B VAL B 2 55 ? 22.754 59.276 47.424 0.50 15.56 ? 303 VAL B CG1 1 ATOM 1957 C CG2 A VAL B 2 55 ? 23.559 59.363 47.196 0.50 16.12 ? 303 VAL B CG2 1 ATOM 1958 C CG2 B VAL B 2 55 ? 24.330 59.828 45.530 0.50 14.25 ? 303 VAL B CG2 1 ATOM 1959 N N . PHE B 2 56 ? 21.289 58.183 43.247 1.00 13.06 ? 304 PHE B N 1 ATOM 1960 C CA . PHE B 2 56 ? 21.136 58.110 41.795 1.00 13.67 ? 304 PHE B CA 1 ATOM 1961 C C . PHE B 2 56 ? 19.886 58.827 41.303 1.00 13.65 ? 304 PHE B C 1 ATOM 1962 O O . PHE B 2 56 ? 18.939 58.982 42.058 1.00 13.78 ? 304 PHE B O 1 ATOM 1963 C CB . PHE B 2 56 ? 21.138 56.639 41.319 1.00 13.54 ? 304 PHE B CB 1 ATOM 1964 C CG . PHE B 2 56 ? 20.076 55.779 41.952 1.00 14.45 ? 304 PHE B CG 1 ATOM 1965 C CD1 . PHE B 2 56 ? 18.918 55.440 41.237 1.00 14.00 ? 304 PHE B CD1 1 ATOM 1966 C CD2 . PHE B 2 56 ? 20.266 55.243 43.225 1.00 14.73 ? 304 PHE B CD2 1 ATOM 1967 C CE1 . PHE B 2 56 ? 17.935 54.622 41.802 1.00 12.80 ? 304 PHE B CE1 1 ATOM 1968 C CE2 . PHE B 2 56 ? 19.311 54.418 43.804 1.00 14.35 ? 304 PHE B CE2 1 ATOM 1969 C CZ . PHE B 2 56 ? 18.134 54.088 43.087 1.00 14.70 ? 304 PHE B CZ 1 ATOM 1970 N N . SER B 2 57 ? 19.926 59.317 40.070 1.00 13.84 ? 305 SER B N 1 ATOM 1971 C CA . SER B 2 57 ? 18.737 59.942 39.502 1.00 13.08 ? 305 SER B CA 1 ATOM 1972 C C . SER B 2 57 ? 17.799 58.827 39.002 1.00 12.86 ? 305 SER B C 1 ATOM 1973 O O . SER B 2 57 ? 18.242 57.846 38.405 1.00 12.92 ? 305 SER B O 1 ATOM 1974 C CB . SER B 2 57 ? 19.110 60.922 38.374 1.00 13.24 ? 305 SER B CB 1 ATOM 1975 O OG . SER B 2 57 ? 20.015 60.302 37.436 1.00 15.56 ? 305 SER B OG 1 ATOM 1976 N N . SER B 2 58 ? 16.492 58.983 39.224 1.00 12.24 ? 306 SER B N 1 ATOM 1977 C CA . SER B 2 58 ? 15.569 57.881 38.950 1.00 12.59 ? 306 SER B CA 1 ATOM 1978 C C . SER B 2 58 ? 14.132 58.404 38.676 1.00 12.93 ? 306 SER B C 1 ATOM 1979 O O . SER B 2 58 ? 13.934 59.578 38.346 1.00 12.60 ? 306 SER B O 1 ATOM 1980 C CB . SER B 2 58 ? 15.611 56.909 40.146 1.00 13.26 ? 306 SER B CB 1 ATOM 1981 O OG . SER B 2 58 ? 14.885 55.701 39.927 1.00 14.17 ? 306 SER B OG 1 ATOM 1982 N N . TYR B 2 59 ? 13.156 57.513 38.836 1.00 12.15 ? 307 TYR B N 1 ATOM 1983 C CA . TYR B 2 59 ? 11.755 57.745 38.438 1.00 13.23 ? 307 TYR B CA 1 ATOM 1984 C C . TYR B 2 59 ? 10.905 56.974 39.429 1.00 12.97 ? 307 TYR B C 1 ATOM 1985 O O . TYR B 2 59 ? 11.388 56.044 40.093 1.00 13.18 ? 307 TYR B O 1 ATOM 1986 C CB . TYR B 2 59 ? 11.493 57.194 37.011 1.00 13.47 ? 307 TYR B CB 1 ATOM 1987 C CG . TYR B 2 59 ? 12.378 57.828 35.968 1.00 13.67 ? 307 TYR B CG 1 ATOM 1988 C CD1 . TYR B 2 59 ? 13.707 57.368 35.776 1.00 15.42 ? 307 TYR B CD1 1 ATOM 1989 C CD2 . TYR B 2 59 ? 11.930 58.920 35.213 1.00 14.11 ? 307 TYR B CD2 1 ATOM 1990 C CE1 . TYR B 2 59 ? 14.544 57.977 34.851 1.00 15.77 ? 307 TYR B CE1 1 ATOM 1991 C CE2 . TYR B 2 59 ? 12.743 59.513 34.280 1.00 14.93 ? 307 TYR B CE2 1 ATOM 1992 C CZ . TYR B 2 59 ? 14.069 59.033 34.110 1.00 16.63 ? 307 TYR B CZ 1 ATOM 1993 O OH . TYR B 2 59 ? 14.868 59.652 33.191 1.00 16.08 ? 307 TYR B OH 1 ATOM 1994 N N . PRO B 2 60 ? 9.601 57.316 39.537 1.00 12.61 ? 308 PRO B N 1 ATOM 1995 C CA . PRO B 2 60 ? 8.752 56.559 40.445 1.00 13.97 ? 308 PRO B CA 1 ATOM 1996 C C . PRO B 2 60 ? 8.681 55.076 40.057 1.00 14.49 ? 308 PRO B C 1 ATOM 1997 O O . PRO B 2 60 ? 8.541 54.751 38.883 1.00 15.16 ? 308 PRO B O 1 ATOM 1998 C CB . PRO B 2 60 ? 7.355 57.207 40.228 1.00 13.04 ? 308 PRO B CB 1 ATOM 1999 C CG . PRO B 2 60 ? 7.687 58.644 39.860 1.00 14.43 ? 308 PRO B CG 1 ATOM 2000 C CD . PRO B 2 60 ? 8.879 58.411 38.877 1.00 13.94 ? 308 PRO B CD 1 ATOM 2001 N N . GLY B 2 61 ? 8.803 54.205 41.048 1.00 14.89 ? 309 GLY B N 1 ATOM 2002 C CA . GLY B 2 61 ? 8.563 52.768 40.872 1.00 15.26 ? 309 GLY B CA 1 ATOM 2003 C C . GLY B 2 61 ? 9.715 52.069 40.133 1.00 15.76 ? 309 GLY B C 1 ATOM 2004 O O . GLY B 2 61 ? 9.571 50.919 39.737 1.00 17.06 ? 309 GLY B O 1 ATOM 2005 N N . THR B 2 62 ? 10.846 52.760 39.960 1.00 15.85 ? 310 THR B N 1 ATOM 2006 C CA . THR B 2 62 ? 11.947 52.255 39.113 1.00 15.50 ? 310 THR B CA 1 ATOM 2007 C C . THR B 2 62 ? 13.117 52.064 40.066 1.00 17.07 ? 310 THR B C 1 ATOM 2008 O O . THR B 2 62 ? 13.615 53.052 40.652 1.00 17.11 ? 310 THR B O 1 ATOM 2009 C CB . THR B 2 62 ? 12.319 53.278 38.025 1.00 17.59 ? 310 THR B CB 1 ATOM 2010 O OG1 . THR B 2 62 ? 11.160 53.550 37.217 1.00 17.84 ? 310 THR B OG1 1 ATOM 2011 C CG2 . THR B 2 62 ? 13.389 52.723 37.108 1.00 15.50 ? 310 THR B CG2 1 ATOM 2012 N N . ILE B 2 63 ? 13.530 50.809 40.272 1.00 16.06 ? 311 ILE B N 1 ATOM 2013 C CA . ILE B 2 63 ? 14.490 50.542 41.354 1.00 16.55 ? 311 ILE B CA 1 ATOM 2014 C C . ILE B 2 63 ? 15.941 50.560 40.862 1.00 17.50 ? 311 ILE B C 1 ATOM 2015 O O . ILE B 2 63 ? 16.810 49.849 41.385 1.00 19.66 ? 311 ILE B O 1 ATOM 2016 C CB . ILE B 2 63 ? 14.174 49.250 42.120 1.00 18.17 ? 311 ILE B CB 1 ATOM 2017 C CG1 . ILE B 2 63 ? 14.127 48.029 41.169 1.00 18.37 ? 311 ILE B CG1 1 ATOM 2018 C CG2 . ILE B 2 63 ? 12.863 49.440 42.900 1.00 16.33 ? 311 ILE B CG2 1 ATOM 2019 C CD1 . ILE B 2 63 ? 14.116 46.670 41.984 1.00 19.56 ? 311 ILE B CD1 1 ATOM 2020 N N . PHE B 2 64 ? 16.187 51.358 39.833 1.00 16.30 ? 312 PHE B N 1 ATOM 2021 C CA . PHE B 2 64 ? 17.548 51.643 39.394 1.00 15.57 ? 312 PHE B CA 1 ATOM 2022 C C . PHE B 2 64 ? 17.451 53.004 38.716 1.00 14.95 ? 312 PHE B C 1 ATOM 2023 O O . PHE B 2 64 ? 16.423 53.692 38.848 1.00 15.12 ? 312 PHE B O 1 ATOM 2024 C CB . PHE B 2 64 ? 18.092 50.553 38.445 1.00 14.90 ? 312 PHE B CB 1 ATOM 2025 C CG . PHE B 2 64 ? 17.491 50.573 37.067 1.00 15.88 ? 312 PHE B CG 1 ATOM 2026 C CD1 . PHE B 2 64 ? 16.127 50.358 36.868 1.00 20.47 ? 312 PHE B CD1 1 ATOM 2027 C CD2 . PHE B 2 64 ? 18.277 50.782 35.957 1.00 19.24 ? 312 PHE B CD2 1 ATOM 2028 C CE1 . PHE B 2 64 ? 15.578 50.407 35.583 1.00 18.49 ? 312 PHE B CE1 1 ATOM 2029 C CE2 . PHE B 2 64 ? 17.731 50.797 34.652 1.00 19.62 ? 312 PHE B CE2 1 ATOM 2030 C CZ . PHE B 2 64 ? 16.367 50.636 34.484 1.00 21.66 ? 312 PHE B CZ 1 ATOM 2031 N N . SER B 2 65 ? 18.524 53.444 38.084 1.00 14.79 ? 313 SER B N 1 ATOM 2032 C CA . SER B 2 65 ? 18.501 54.790 37.530 1.00 14.69 ? 313 SER B CA 1 ATOM 2033 C C . SER B 2 65 ? 17.697 54.861 36.221 1.00 16.04 ? 313 SER B C 1 ATOM 2034 O O . SER B 2 65 ? 16.702 55.576 36.159 1.00 17.91 ? 313 SER B O 1 ATOM 2035 C CB . SER B 2 65 ? 19.913 55.358 37.352 1.00 14.83 ? 313 SER B CB 1 ATOM 2036 O OG . SER B 2 65 ? 19.822 56.612 36.691 1.00 13.05 ? 313 SER B OG 1 ATOM 2037 N N . GLY B 2 66 ? 18.127 54.156 35.179 1.00 17.11 ? 314 GLY B N 1 ATOM 2038 C CA . GLY B 2 66 ? 17.479 54.273 33.853 1.00 18.77 ? 314 GLY B CA 1 ATOM 2039 C C . GLY B 2 66 ? 18.163 55.357 33.023 1.00 19.94 ? 314 GLY B C 1 ATOM 2040 O O . GLY B 2 66 ? 18.178 55.292 31.780 1.00 21.03 ? 314 GLY B O 1 ATOM 2041 N N . ASP B 2 67 ? 18.750 56.350 33.696 1.00 16.45 ? 315 ASP B N 1 ATOM 2042 C CA . ASP B 2 67 ? 19.400 57.465 32.972 1.00 15.83 ? 315 ASP B CA 1 ATOM 2043 C C . ASP B 2 67 ? 20.634 57.135 32.100 1.00 15.97 ? 315 ASP B C 1 ATOM 2044 O O . ASP B 2 67 ? 20.667 57.544 30.914 1.00 16.09 ? 315 ASP B O 1 ATOM 2045 C CB . ASP B 2 67 ? 19.733 58.604 33.944 1.00 15.75 ? 315 ASP B CB 1 ATOM 2046 C CG . ASP B 2 67 ? 18.489 59.393 34.379 1.00 19.02 ? 315 ASP B CG 1 ATOM 2047 O OD1 . ASP B 2 67 ? 17.374 59.078 33.878 1.00 19.75 ? 315 ASP B OD1 1 ATOM 2048 O OD2 . ASP B 2 67 ? 18.669 60.312 35.202 1.00 18.08 ? 315 ASP B OD2 1 ATOM 2049 N N . ASP B 2 68 ? 21.689 56.508 32.638 1.00 14.25 ? 316 ASP B N 1 ATOM 2050 C CA . ASP B 2 68 ? 21.866 56.152 34.075 1.00 13.74 ? 316 ASP B CA 1 ATOM 2051 C C . ASP B 2 68 ? 22.960 57.024 34.681 1.00 12.57 ? 316 ASP B C 1 ATOM 2052 O O . ASP B 2 68 ? 23.925 57.393 33.992 1.00 12.76 ? 316 ASP B O 1 ATOM 2053 C CB . ASP B 2 68 ? 22.392 54.704 34.204 1.00 14.46 ? 316 ASP B CB 1 ATOM 2054 C CG . ASP B 2 68 ? 21.343 53.687 33.869 1.00 16.39 ? 316 ASP B CG 1 ATOM 2055 O OD1 . ASP B 2 68 ? 21.171 53.372 32.684 1.00 21.35 ? 316 ASP B OD1 1 ATOM 2056 O OD2 . ASP B 2 68 ? 20.713 53.189 34.818 1.00 18.30 ? 316 ASP B OD2 1 ATOM 2057 N N . PHE B 2 69 ? 22.820 57.312 35.969 1.00 10.73 ? 317 PHE B N 1 ATOM 2058 C CA . PHE B 2 69 ? 23.851 58.082 36.692 1.00 11.26 ? 317 PHE B CA 1 ATOM 2059 C C . PHE B 2 69 ? 23.791 57.666 38.165 1.00 10.84 ? 317 PHE B C 1 ATOM 2060 O O . PHE B 2 69 ? 22.743 57.872 38.827 1.00 11.80 ? 317 PHE B O 1 ATOM 2061 C CB . PHE B 2 69 ? 23.536 59.583 36.542 1.00 11.54 ? 317 PHE B CB 1 ATOM 2062 C CG . PHE B 2 69 ? 24.544 60.485 37.205 1.00 12.82 ? 317 PHE B CG 1 ATOM 2063 C CD1 . PHE B 2 69 ? 25.710 60.842 36.548 1.00 15.15 ? 317 PHE B CD1 1 ATOM 2064 C CD2 . PHE B 2 69 ? 24.327 60.923 38.509 1.00 14.67 ? 317 PHE B CD2 1 ATOM 2065 C CE1 . PHE B 2 69 ? 26.640 61.727 37.179 1.00 15.96 ? 317 PHE B CE1 1 ATOM 2066 C CE2 . PHE B 2 69 ? 25.246 61.771 39.140 1.00 14.66 ? 317 PHE B CE2 1 ATOM 2067 C CZ . PHE B 2 69 ? 26.387 62.153 38.466 1.00 14.91 ? 317 PHE B CZ 1 ATOM 2068 N N . TYR B 2 70 ? 24.908 57.131 38.697 1.00 11.25 ? 318 TYR B N 1 ATOM 2069 C CA . TYR B 2 70 ? 24.956 56.640 40.083 1.00 11.41 ? 318 TYR B CA 1 ATOM 2070 C C . TYR B 2 70 ? 26.245 57.166 40.722 1.00 11.68 ? 318 TYR B C 1 ATOM 2071 O O . TYR B 2 70 ? 27.305 57.105 40.098 1.00 13.24 ? 318 TYR B O 1 ATOM 2072 C CB . TYR B 2 70 ? 25.103 55.109 40.147 1.00 12.21 ? 318 TYR B CB 1 ATOM 2073 C CG . TYR B 2 70 ? 23.978 54.341 39.466 1.00 12.80 ? 318 TYR B CG 1 ATOM 2074 C CD1 . TYR B 2 70 ? 24.052 54.045 38.078 1.00 11.55 ? 318 TYR B CD1 1 ATOM 2075 C CD2 . TYR B 2 70 ? 22.893 53.850 40.204 1.00 14.31 ? 318 TYR B CD2 1 ATOM 2076 C CE1 . TYR B 2 70 ? 23.002 53.308 37.440 1.00 11.95 ? 318 TYR B CE1 1 ATOM 2077 C CE2 . TYR B 2 70 ? 21.881 53.104 39.575 1.00 13.50 ? 318 TYR B CE2 1 ATOM 2078 C CZ . TYR B 2 70 ? 21.953 52.855 38.208 1.00 13.68 ? 318 TYR B CZ 1 ATOM 2079 O OH . TYR B 2 70 ? 20.966 52.108 37.600 1.00 16.10 ? 318 TYR B OH 1 ATOM 2080 N N . ILE B 2 71 ? 26.149 57.577 41.977 1.00 11.32 ? 319 ILE B N 1 ATOM 2081 C CA . ILE B 2 71 ? 27.339 57.829 42.812 1.00 12.72 ? 319 ILE B CA 1 ATOM 2082 C C . ILE B 2 71 ? 27.311 56.742 43.872 1.00 13.01 ? 319 ILE B C 1 ATOM 2083 O O . ILE B 2 71 ? 26.371 56.655 44.655 1.00 13.76 ? 319 ILE B O 1 ATOM 2084 C CB . ILE B 2 71 ? 27.206 59.214 43.442 1.00 13.30 ? 319 ILE B CB 1 ATOM 2085 C CG1 . ILE B 2 71 ? 27.122 60.262 42.311 1.00 15.12 ? 319 ILE B CG1 1 ATOM 2086 C CG2 . ILE B 2 71 ? 28.405 59.527 44.378 1.00 13.45 ? 319 ILE B CG2 1 ATOM 2087 C CD1 . ILE B 2 71 ? 26.885 61.705 42.867 1.00 17.67 ? 319 ILE B CD1 1 ATOM 2088 N N . LEU B 2 72 ? 28.339 55.912 43.877 1.00 12.94 ? 320 LEU B N 1 ATOM 2089 C CA . LEU B 2 72 ? 28.407 54.739 44.765 1.00 14.06 ? 320 LEU B CA 1 ATOM 2090 C C . LEU B 2 72 ? 29.347 54.958 45.957 1.00 14.92 ? 320 LEU B C 1 ATOM 2091 O O . LEU B 2 72 ? 30.387 55.617 45.821 1.00 15.26 ? 320 LEU B O 1 ATOM 2092 C CB . LEU B 2 72 ? 28.883 53.519 43.952 1.00 13.48 ? 320 LEU B CB 1 ATOM 2093 C CG . LEU B 2 72 ? 28.099 53.282 42.667 1.00 13.41 ? 320 LEU B CG 1 ATOM 2094 C CD1 . LEU B 2 72 ? 28.616 52.054 41.904 1.00 15.09 ? 320 LEU B CD1 1 ATOM 2095 C CD2 . LEU B 2 72 ? 26.601 53.072 42.995 1.00 13.79 ? 320 LEU B CD2 1 ATOM 2096 N N . GLY B 2 73 ? 28.998 54.367 47.096 1.00 15.29 ? 321 GLY B N 1 ATOM 2097 C CA . GLY B 2 73 ? 29.822 54.513 48.303 1.00 16.41 ? 321 GLY B CA 1 ATOM 2098 C C . GLY B 2 73 ? 31.164 53.810 48.197 1.00 17.24 ? 321 GLY B C 1 ATOM 2099 O O . GLY B 2 73 ? 32.061 54.031 49.042 1.00 17.91 ? 321 GLY B O 1 ATOM 2100 N N . SER B 2 74 ? 31.326 52.988 47.162 1.00 16.45 ? 322 SER B N 1 ATOM 2101 C CA . SER B 2 74 ? 32.604 52.348 46.830 1.00 16.42 ? 322 SER B CA 1 ATOM 2102 C C . SER B 2 74 ? 33.606 53.344 46.217 1.00 15.92 ? 322 SER B C 1 ATOM 2103 O O . SER B 2 74 ? 34.726 52.983 45.903 1.00 17.70 ? 322 SER B O 1 ATOM 2104 C CB . SER B 2 74 ? 32.342 51.223 45.827 1.00 16.65 ? 322 SER B CB 1 ATOM 2105 O OG . SER B 2 74 ? 31.676 51.765 44.676 1.00 17.25 ? 322 SER B OG 1 ATOM 2106 N N . GLY B 2 75 ? 33.188 54.593 46.019 1.00 14.63 ? 323 GLY B N 1 ATOM 2107 C CA . GLY B 2 75 ? 34.054 55.587 45.382 1.00 15.67 ? 323 GLY B CA 1 ATOM 2108 C C . GLY B 2 75 ? 33.931 55.612 43.864 1.00 15.58 ? 323 GLY B C 1 ATOM 2109 O O . GLY B 2 75 ? 34.696 56.307 43.195 1.00 17.15 ? 323 GLY B O 1 ATOM 2110 N N . LEU B 2 76 ? 32.955 54.878 43.306 1.00 14.52 ? 324 LEU B N 1 ATOM 2111 C CA . LEU B 2 76 ? 32.787 54.836 41.843 1.00 13.61 ? 324 LEU B CA 1 ATOM 2112 C C . LEU B 2 76 ? 31.641 55.769 41.447 1.00 13.04 ? 324 LEU B C 1 ATOM 2113 O O . LEU B 2 76 ? 30.693 55.938 42.226 1.00 13.66 ? 324 LEU B O 1 ATOM 2114 C CB . LEU B 2 76 ? 32.408 53.427 41.365 1.00 14.26 ? 324 LEU B CB 1 ATOM 2115 C CG . LEU B 2 76 ? 33.365 52.251 41.637 1.00 19.04 ? 324 LEU B CG 1 ATOM 2116 C CD1 . LEU B 2 76 ? 32.905 50.902 40.961 1.00 19.36 ? 324 LEU B CD1 1 ATOM 2117 C CD2 . LEU B 2 76 ? 34.753 52.635 41.242 1.00 22.87 ? 324 LEU B CD2 1 ATOM 2118 N N . VAL B 2 77 ? 31.711 56.328 40.244 1.00 12.78 ? 325 VAL B N 1 ATOM 2119 C CA . VAL B 2 77 ? 30.519 56.943 39.660 1.00 13.01 ? 325 VAL B CA 1 ATOM 2120 C C . VAL B 2 77 ? 30.290 56.187 38.350 1.00 12.68 ? 325 VAL B C 1 ATOM 2121 O O . VAL B 2 77 ? 31.242 55.972 37.539 1.00 14.03 ? 325 VAL B O 1 ATOM 2122 C CB . VAL B 2 77 ? 30.769 58.417 39.362 1.00 13.14 ? 325 VAL B CB 1 ATOM 2123 C CG1 . VAL B 2 77 ? 29.539 59.009 38.579 1.00 15.20 ? 325 VAL B CG1 1 ATOM 2124 C CG2 . VAL B 2 77 ? 31.059 59.152 40.649 1.00 14.85 ? 325 VAL B CG2 1 ATOM 2125 N N . THR B 2 78 ? 29.061 55.757 38.112 1.00 11.77 ? 326 THR B N 1 ATOM 2126 C CA . THR B 2 78 ? 28.807 54.972 36.892 1.00 11.05 ? 326 THR B CA 1 ATOM 2127 C C . THR B 2 78 ? 27.696 55.657 36.069 1.00 10.82 ? 326 THR B C 1 ATOM 2128 O O . THR B 2 78 ? 26.728 56.184 36.639 1.00 11.97 ? 326 THR B O 1 ATOM 2129 C CB . THR B 2 78 ? 28.427 53.494 37.219 1.00 11.40 ? 326 THR B CB 1 ATOM 2130 O OG1 . THR B 2 78 ? 27.215 53.422 37.962 1.00 14.19 ? 326 THR B OG1 1 ATOM 2131 C CG2 . THR B 2 78 ? 29.527 52.813 38.054 1.00 13.03 ? 326 THR B CG2 1 ATOM 2132 N N . LEU B 2 79 ? 27.870 55.688 34.768 1.00 10.90 ? 327 LEU B N 1 ATOM 2133 C CA . LEU B 2 79 ? 26.930 56.425 33.907 1.00 11.15 ? 327 LEU B CA 1 ATOM 2134 C C . LEU B 2 79 ? 27.044 55.882 32.515 1.00 11.34 ? 327 LEU B C 1 ATOM 2135 O O . LEU B 2 79 ? 28.041 55.221 32.182 1.00 12.59 ? 327 LEU B O 1 ATOM 2136 C CB . LEU B 2 79 ? 27.189 57.945 33.909 1.00 11.17 ? 327 LEU B CB 1 ATOM 2137 C CG . LEU B 2 79 ? 28.519 58.472 33.356 1.00 11.92 ? 327 LEU B CG 1 ATOM 2138 C CD1 . LEU B 2 79 ? 28.409 59.979 33.092 1.00 13.18 ? 327 LEU B CD1 1 ATOM 2139 C CD2 . LEU B 2 79 ? 29.724 58.197 34.345 1.00 12.68 ? 327 LEU B CD2 1 ATOM 2140 N N . GLU B 2 80 ? 26.017 56.113 31.687 1.00 11.92 ? 328 GLU B N 1 ATOM 2141 C CA . GLU B 2 80 ? 26.106 55.556 30.325 1.00 12.46 ? 328 GLU B CA 1 ATOM 2142 C C . GLU B 2 80 ? 25.355 56.422 29.346 1.00 12.20 ? 328 GLU B C 1 ATOM 2143 O O . GLU B 2 80 ? 24.471 57.170 29.775 1.00 13.06 ? 328 GLU B O 1 ATOM 2144 C CB . GLU B 2 80 ? 25.516 54.130 30.318 1.00 12.22 ? 328 GLU B CB 1 ATOM 2145 C CG . GLU B 2 80 ? 24.094 53.966 30.925 1.00 15.02 ? 328 GLU B CG 1 ATOM 2146 C CD . GLU B 2 80 ? 22.939 54.312 29.968 1.00 17.19 ? 328 GLU B CD 1 ATOM 2147 O OE1 . GLU B 2 80 ? 21.754 54.286 30.410 1.00 17.99 ? 328 GLU B OE1 1 ATOM 2148 O OE2 . GLU B 2 80 ? 23.174 54.572 28.775 1.00 16.11 ? 328 GLU B OE2 1 ATOM 2149 N N . THR B 2 81 ? 25.665 56.285 28.056 1.00 11.98 ? 329 THR B N 1 ATOM 2150 C CA . THR B 2 81 ? 24.740 56.763 27.035 1.00 12.75 ? 329 THR B CA 1 ATOM 2151 C C . THR B 2 81 ? 24.447 55.548 26.156 1.00 13.81 ? 329 THR B C 1 ATOM 2152 O O . THR B 2 81 ? 25.286 54.661 26.011 1.00 14.83 ? 329 THR B O 1 ATOM 2153 C CB . THR B 2 81 ? 25.273 57.961 26.208 1.00 12.67 ? 329 THR B CB 1 ATOM 2154 O OG1 . THR B 2 81 ? 26.279 57.528 25.269 1.00 14.74 ? 329 THR B OG1 1 ATOM 2155 C CG2 . THR B 2 81 ? 25.867 59.029 27.137 1.00 13.32 ? 329 THR B CG2 1 ATOM 2156 N N . THR B 2 82 ? 23.251 55.514 25.608 1.00 13.68 ? 330 THR B N 1 ATOM 2157 C CA . THR B 2 82 ? 22.772 54.339 24.888 1.00 14.78 ? 330 THR B CA 1 ATOM 2158 C C . THR B 2 82 ? 23.284 54.302 23.435 1.00 14.98 ? 330 THR B C 1 ATOM 2159 O O . THR B 2 82 ? 23.158 55.311 22.673 1.00 15.78 ? 330 THR B O 1 ATOM 2160 C CB . THR B 2 82 ? 21.218 54.285 24.947 1.00 14.85 ? 330 THR B CB 1 ATOM 2161 O OG1 . THR B 2 82 ? 20.810 54.249 26.325 1.00 17.64 ? 330 THR B OG1 1 ATOM 2162 C CG2 . THR B 2 82 ? 20.706 53.001 24.235 1.00 17.70 ? 330 THR B CG2 1 ATOM 2163 N N . ILE B 2 83 ? 23.802 53.142 23.016 1.00 14.50 ? 331 ILE B N 1 ATOM 2164 C CA . ILE B 2 83 ? 24.318 53.002 21.647 1.00 15.74 ? 331 ILE B CA 1 ATOM 2165 C C . ILE B 2 83 ? 23.378 52.201 20.729 1.00 16.89 ? 331 ILE B C 1 ATOM 2166 O O . ILE B 2 83 ? 23.392 52.416 19.503 1.00 17.80 ? 331 ILE B O 1 ATOM 2167 C CB . ILE B 2 83 ? 25.778 52.449 21.594 1.00 16.39 ? 331 ILE B CB 1 ATOM 2168 C CG1 . ILE B 2 83 ? 25.884 51.049 22.248 1.00 15.37 ? 331 ILE B CG1 1 ATOM 2169 C CG2 . ILE B 2 83 ? 26.788 53.479 22.239 1.00 14.51 ? 331 ILE B CG2 1 ATOM 2170 C CD1 . ILE B 2 83 ? 27.267 50.364 22.077 1.00 16.55 ? 331 ILE B CD1 1 ATOM 2171 N N . GLY B 2 84 ? 22.575 51.314 21.309 1.00 14.94 ? 332 GLY B N 1 ATOM 2172 C CA . GLY B 2 84 ? 21.606 50.493 20.539 1.00 16.69 ? 332 GLY B CA 1 ATOM 2173 C C . GLY B 2 84 ? 22.347 49.533 19.623 1.00 16.86 ? 332 GLY B C 1 ATOM 2174 O O . GLY B 2 84 ? 23.557 49.317 19.762 1.00 18.21 ? 332 GLY B O 1 ATOM 2175 N N . ASN B 2 85 ? 21.615 48.983 18.658 1.00 16.75 ? 333 ASN B N 1 ATOM 2176 C CA . ASN B 2 85 ? 22.185 48.074 17.673 1.00 16.65 ? 333 ASN B CA 1 ATOM 2177 C C . ASN B 2 85 ? 21.358 48.220 16.405 1.00 18.60 ? 333 ASN B C 1 ATOM 2178 O O . ASN B 2 85 ? 20.129 48.190 16.488 1.00 19.82 ? 333 ASN B O 1 ATOM 2179 C CB . ASN B 2 85 ? 22.040 46.610 18.134 1.00 16.91 ? 333 ASN B CB 1 ATOM 2180 C CG . ASN B 2 85 ? 22.376 45.629 17.018 1.00 17.16 ? 333 ASN B CG 1 ATOM 2181 O OD1 . ASN B 2 85 ? 23.421 45.763 16.344 1.00 18.58 ? 333 ASN B OD1 1 ATOM 2182 N ND2 . ASN B 2 85 ? 21.493 44.667 16.799 1.00 17.57 ? 333 ASN B ND2 1 ATOM 2183 N N . LYS B 2 86 ? 22.028 48.364 15.268 1.00 20.16 ? 334 LYS B N 1 ATOM 2184 C CA . LYS B 2 86 ? 21.353 48.472 13.969 1.00 22.35 ? 334 LYS B CA 1 ATOM 2185 C C . LYS B 2 86 ? 21.569 47.239 13.075 1.00 23.11 ? 334 LYS B C 1 ATOM 2186 O O . LYS B 2 86 ? 21.111 47.220 11.934 1.00 24.41 ? 334 LYS B O 1 ATOM 2187 C CB . LYS B 2 86 ? 21.838 49.708 13.214 1.00 22.77 ? 334 LYS B CB 1 ATOM 2188 C CG . LYS B 2 86 ? 21.585 51.009 13.919 1.00 27.75 ? 334 LYS B CG 1 ATOM 2189 C CD . LYS B 2 86 ? 20.116 51.262 14.084 1.00 33.42 ? 334 LYS B CD 1 ATOM 2190 C CE . LYS B 2 86 ? 19.840 52.780 14.315 1.00 38.13 ? 334 LYS B CE 1 ATOM 2191 N NZ . LYS B 2 86 ? 20.917 53.486 15.121 1.00 40.97 ? 334 LYS B NZ 1 ATOM 2192 N N . ASN B 2 87 ? 22.231 46.212 13.590 1.00 21.17 ? 335 ASN B N 1 ATOM 2193 C CA . ASN B 2 87 ? 22.533 45.022 12.779 1.00 21.14 ? 335 ASN B CA 1 ATOM 2194 C C . ASN B 2 87 ? 21.591 43.869 13.181 1.00 20.76 ? 335 ASN B C 1 ATOM 2195 O O . ASN B 2 87 ? 21.778 43.228 14.206 1.00 19.59 ? 335 ASN B O 1 ATOM 2196 C CB . ASN B 2 87 ? 24.012 44.656 12.942 1.00 20.02 ? 335 ASN B CB 1 ATOM 2197 C CG . ASN B 2 87 ? 24.407 43.413 12.176 1.00 21.18 ? 335 ASN B CG 1 ATOM 2198 O OD1 . ASN B 2 87 ? 23.572 42.798 11.498 1.00 20.12 ? 335 ASN B OD1 1 ATOM 2199 N ND2 . ASN B 2 87 ? 25.670 43.008 12.320 1.00 21.15 ? 335 ASN B ND2 1 ATOM 2200 N N . PRO B 2 88 ? 20.584 43.580 12.333 1.00 21.93 ? 336 PRO B N 1 ATOM 2201 C CA . PRO B 2 88 ? 19.567 42.581 12.677 1.00 22.24 ? 336 PRO B CA 1 ATOM 2202 C C . PRO B 2 88 ? 20.152 41.179 12.804 1.00 21.99 ? 336 PRO B C 1 ATOM 2203 O O . PRO B 2 88 ? 19.535 40.335 13.434 1.00 21.90 ? 336 PRO B O 1 ATOM 2204 C CB . PRO B 2 88 ? 18.587 42.647 11.506 1.00 23.17 ? 336 PRO B CB 1 ATOM 2205 C CG . PRO B 2 88 ? 19.438 43.119 10.355 1.00 24.92 ? 336 PRO B CG 1 ATOM 2206 C CD . PRO B 2 88 ? 20.394 44.125 10.981 1.00 22.67 ? 336 PRO B CD 1 ATOM 2207 N N . ALA B 2 89 ? 21.336 40.936 12.247 1.00 21.26 ? 337 ALA B N 1 ATOM 2208 C CA . ALA B 2 89 ? 21.963 39.617 12.401 1.00 21.47 ? 337 ALA B CA 1 ATOM 2209 C C . ALA B 2 89 ? 22.400 39.310 13.826 1.00 21.18 ? 337 ALA B C 1 ATOM 2210 O O . ALA B 2 89 ? 22.795 38.173 14.108 1.00 21.57 ? 337 ALA B O 1 ATOM 2211 C CB . ALA B 2 89 ? 23.167 39.449 11.436 1.00 21.66 ? 337 ALA B CB 1 ATOM 2212 N N . LEU B 2 90 ? 22.343 40.311 14.724 1.00 18.41 ? 338 LEU B N 1 ATOM 2213 C CA . LEU B 2 90 ? 22.785 40.099 16.094 1.00 17.26 ? 338 LEU B CA 1 ATOM 2214 C C . LEU B 2 90 ? 21.627 39.802 17.022 1.00 16.66 ? 338 LEU B C 1 ATOM 2215 O O . LEU B 2 90 ? 21.858 39.425 18.165 1.00 15.69 ? 338 LEU B O 1 ATOM 2216 C CB . LEU B 2 90 ? 23.573 41.324 16.613 1.00 17.16 ? 338 LEU B CB 1 ATOM 2217 C CG . LEU B 2 90 ? 24.787 41.812 15.799 1.00 19.26 ? 338 LEU B CG 1 ATOM 2218 C CD1 . LEU B 2 90 ? 25.535 42.915 16.564 1.00 17.85 ? 338 LEU B CD1 1 ATOM 2219 C CD2 . LEU B 2 90 ? 25.739 40.655 15.426 1.00 17.47 ? 338 LEU B CD2 1 ATOM 2220 N N . TRP B 2 91 ? 20.390 39.965 16.537 1.00 16.75 ? 339 TRP B N 1 ATOM 2221 C CA . TRP B 2 91 ? 19.243 39.722 17.409 1.00 18.05 ? 339 TRP B CA 1 ATOM 2222 C C . TRP B 2 91 ? 19.118 38.271 17.869 1.00 19.02 ? 339 TRP B C 1 ATOM 2223 O O . TRP B 2 91 ? 18.488 37.977 18.891 1.00 19.44 ? 339 TRP B O 1 ATOM 2224 C CB . TRP B 2 91 ? 17.940 40.185 16.767 1.00 18.41 ? 339 TRP B CB 1 ATOM 2225 C CG . TRP B 2 91 ? 17.833 41.673 16.512 1.00 20.11 ? 339 TRP B CG 1 ATOM 2226 C CD1 . TRP B 2 91 ? 17.353 42.262 15.361 1.00 20.42 ? 339 TRP B CD1 1 ATOM 2227 C CD2 . TRP B 2 91 ? 18.180 42.769 17.410 1.00 18.82 ? 339 TRP B CD2 1 ATOM 2228 N NE1 . TRP B 2 91 ? 17.363 43.640 15.494 1.00 21.47 ? 339 TRP B NE1 1 ATOM 2229 C CE2 . TRP B 2 91 ? 17.870 43.977 16.730 1.00 19.11 ? 339 TRP B CE2 1 ATOM 2230 C CE3 . TRP B 2 91 ? 18.695 42.838 18.715 1.00 17.33 ? 339 TRP B CE3 1 ATOM 2231 C CZ2 . TRP B 2 91 ? 18.082 45.245 17.305 1.00 17.86 ? 339 TRP B CZ2 1 ATOM 2232 C CZ3 . TRP B 2 91 ? 18.915 44.112 19.290 1.00 18.36 ? 339 TRP B CZ3 1 ATOM 2233 C CH2 . TRP B 2 91 ? 18.589 45.287 18.587 1.00 18.63 ? 339 TRP B CH2 1 ATOM 2234 N N . LYS B 2 92 ? 19.741 37.359 17.122 1.00 19.75 ? 340 LYS B N 1 ATOM 2235 C CA . LYS B 2 92 ? 19.739 35.969 17.548 1.00 20.69 ? 340 LYS B CA 1 ATOM 2236 C C . LYS B 2 92 ? 20.455 35.781 18.905 1.00 20.64 ? 340 LYS B C 1 ATOM 2237 O O . LYS B 2 92 ? 20.258 34.756 19.590 1.00 20.53 ? 340 LYS B O 1 ATOM 2238 C CB . LYS B 2 92 ? 20.384 35.092 16.459 1.00 21.64 ? 340 LYS B CB 1 ATOM 2239 C CG . LYS B 2 92 ? 21.838 35.405 16.188 1.00 23.80 ? 340 LYS B CG 1 ATOM 2240 C CD . LYS B 2 92 ? 22.397 34.376 15.189 1.00 31.83 ? 340 LYS B CD 1 ATOM 2241 C CE . LYS B 2 92 ? 23.897 34.419 15.111 1.00 35.18 ? 340 LYS B CE 1 ATOM 2242 N NZ . LYS B 2 92 ? 24.411 35.417 14.120 1.00 42.54 ? 340 LYS B NZ 1 ATOM 2243 N N . TYR B 2 93 ? 21.297 36.741 19.302 1.00 18.98 ? 341 TYR B N 1 ATOM 2244 C CA . TYR B 2 93 ? 21.950 36.646 20.626 1.00 18.54 ? 341 TYR B CA 1 ATOM 2245 C C . TYR B 2 93 ? 21.092 37.141 21.797 1.00 19.12 ? 341 TYR B C 1 ATOM 2246 O O . TYR B 2 93 ? 21.535 37.093 22.955 1.00 18.90 ? 341 TYR B O 1 ATOM 2247 C CB . TYR B 2 93 ? 23.282 37.409 20.625 1.00 19.45 ? 341 TYR B CB 1 ATOM 2248 C CG . TYR B 2 93 ? 24.222 36.871 19.572 1.00 20.53 ? 341 TYR B CG 1 ATOM 2249 C CD1 . TYR B 2 93 ? 24.665 37.667 18.528 1.00 22.64 ? 341 TYR B CD1 1 ATOM 2250 C CD2 . TYR B 2 93 ? 24.653 35.548 19.637 1.00 25.96 ? 341 TYR B CD2 1 ATOM 2251 C CE1 . TYR B 2 93 ? 25.539 37.165 17.569 1.00 27.46 ? 341 TYR B CE1 1 ATOM 2252 C CE2 . TYR B 2 93 ? 25.503 35.031 18.675 1.00 27.72 ? 341 TYR B CE2 1 ATOM 2253 C CZ . TYR B 2 93 ? 25.934 35.842 17.647 1.00 28.93 ? 341 TYR B CZ 1 ATOM 2254 O OH . TYR B 2 93 ? 26.789 35.322 16.703 1.00 30.83 ? 341 TYR B OH 1 ATOM 2255 N N . VAL B 2 94 ? 19.888 37.623 21.502 1.00 17.53 ? 342 VAL B N 1 ATOM 2256 C CA . VAL B 2 94 ? 18.966 38.017 22.551 1.00 17.11 ? 342 VAL B CA 1 ATOM 2257 C C . VAL B 2 94 ? 18.090 36.777 22.802 1.00 17.60 ? 342 VAL B C 1 ATOM 2258 O O . VAL B 2 94 ? 17.283 36.422 21.947 1.00 18.46 ? 342 VAL B O 1 ATOM 2259 C CB . VAL B 2 94 ? 18.116 39.219 22.105 1.00 16.70 ? 342 VAL B CB 1 ATOM 2260 C CG1 . VAL B 2 94 ? 17.156 39.637 23.214 1.00 18.39 ? 342 VAL B CG1 1 ATOM 2261 C CG2 . VAL B 2 94 ? 19.020 40.414 21.717 1.00 17.13 ? 342 VAL B CG2 1 ATOM 2262 N N . GLN B 2 95 ? 18.270 36.119 23.951 1.00 17.35 ? 343 GLN B N 1 ATOM 2263 C CA . GLN B 2 95 ? 17.559 34.854 24.276 1.00 17.82 ? 343 GLN B CA 1 ATOM 2264 C C . GLN B 2 95 ? 17.035 34.926 25.691 1.00 17.80 ? 343 GLN B C 1 ATOM 2265 O O . GLN B 2 95 ? 17.663 35.571 26.534 1.00 17.72 ? 343 GLN B O 1 ATOM 2266 C CB . GLN B 2 95 ? 18.566 33.699 24.189 1.00 19.30 ? 343 GLN B CB 1 ATOM 2267 C CG . GLN B 2 95 ? 19.081 33.487 22.781 1.00 19.61 ? 343 GLN B CG 1 ATOM 2268 C CD . GLN B 2 95 ? 17.983 32.922 21.886 1.00 23.36 ? 343 GLN B CD 1 ATOM 2269 O OE1 . GLN B 2 95 ? 17.100 32.187 22.360 1.00 27.53 ? 343 GLN B OE1 1 ATOM 2270 N NE2 . GLN B 2 95 ? 18.016 33.264 20.601 1.00 23.43 ? 343 GLN B NE2 1 ATOM 2271 N N . PRO B 2 96 ? 15.920 34.231 25.993 1.00 17.26 ? 344 PRO B N 1 ATOM 2272 C CA . PRO B 2 96 ? 15.407 34.297 27.341 1.00 17.17 ? 344 PRO B CA 1 ATOM 2273 C C . PRO B 2 96 ? 16.226 33.480 28.331 1.00 16.65 ? 344 PRO B C 1 ATOM 2274 O O . PRO B 2 96 ? 16.209 33.774 29.524 1.00 17.17 ? 344 PRO B O 1 ATOM 2275 C CB . PRO B 2 96 ? 13.975 33.764 27.212 1.00 17.72 ? 344 PRO B CB 1 ATOM 2276 C CG . PRO B 2 96 ? 13.984 32.884 26.009 1.00 17.07 ? 344 PRO B CG 1 ATOM 2277 C CD . PRO B 2 96 ? 15.040 33.465 25.079 1.00 18.11 ? 344 PRO B CD 1 ATOM 2278 N N . GLN B 2 97 ? 16.917 32.435 27.862 1.00 15.39 ? 345 GLN B N 1 ATOM 2279 C CA . GLN B 2 97 ? 17.773 31.669 28.783 1.00 16.81 ? 345 GLN B CA 1 ATOM 2280 C C . GLN B 2 97 ? 19.223 32.036 28.525 1.00 16.04 ? 345 GLN B C 1 ATOM 2281 O O . GLN B 2 97 ? 19.671 32.058 27.377 1.00 18.71 ? 345 GLN B O 1 ATOM 2282 C CB . GLN B 2 97 ? 17.597 30.145 28.623 1.00 16.79 ? 345 GLN B CB 1 ATOM 2283 C CG . GLN B 2 97 ? 16.220 29.610 29.004 1.00 20.03 ? 345 GLN B CG 1 ATOM 2284 C CD . GLN B 2 97 ? 15.290 29.493 27.825 1.00 26.28 ? 345 GLN B CD 1 ATOM 2285 O OE1 . GLN B 2 97 ? 15.731 29.393 26.672 1.00 30.20 ? 345 GLN B OE1 1 ATOM 2286 N NE2 . GLN B 2 97 ? 13.983 29.481 28.100 1.00 27.56 ? 345 GLN B NE2 1 ATOM 2287 N N . GLY B 2 98 ? 19.965 32.324 29.587 1.00 15.58 ? 346 GLY B N 1 ATOM 2288 C CA . GLY B 2 98 ? 21.378 32.641 29.433 1.00 15.30 ? 346 GLY B CA 1 ATOM 2289 C C . GLY B 2 98 ? 21.641 34.140 29.306 1.00 16.21 ? 346 GLY B C 1 ATOM 2290 O O . GLY B 2 98 ? 22.770 34.557 29.041 1.00 16.80 ? 346 GLY B O 1 ATOM 2291 N N . CYS B 2 99 ? 20.599 34.937 29.525 1.00 16.05 ? 347 CYS B N 1 ATOM 2292 C CA . CYS B 2 99 ? 20.674 36.416 29.413 1.00 15.41 ? 347 CYS B CA 1 ATOM 2293 C C . CYS B 2 99 ? 19.977 37.010 30.634 1.00 15.13 ? 347 CYS B C 1 ATOM 2294 O O . CYS B 2 99 ? 18.858 36.584 30.990 1.00 15.32 ? 347 CYS B O 1 ATOM 2295 C CB . CYS B 2 99 ? 19.954 36.890 28.142 1.00 16.55 ? 347 CYS B CB 1 ATOM 2296 S SG . CYS B 2 99 ? 20.701 36.347 26.604 1.00 20.25 ? 347 CYS B SG 1 ATOM 2297 N N . VAL B 2 100 ? 20.655 37.938 31.323 1.00 13.51 ? 348 VAL B N 1 ATOM 2298 C CA . VAL B 2 100 ? 20.036 38.674 32.431 1.00 13.20 ? 348 VAL B CA 1 ATOM 2299 C C . VAL B 2 100 ? 19.783 40.107 31.883 1.00 13.77 ? 348 VAL B C 1 ATOM 2300 O O . VAL B 2 100 ? 20.686 40.699 31.281 1.00 12.80 ? 348 VAL B O 1 ATOM 2301 C CB . VAL B 2 100 ? 20.969 38.692 33.712 1.00 12.93 ? 348 VAL B CB 1 ATOM 2302 C CG1 . VAL B 2 100 ? 20.396 39.608 34.862 1.00 12.55 ? 348 VAL B CG1 1 ATOM 2303 C CG2 . VAL B 2 100 ? 21.138 37.257 34.249 1.00 14.38 ? 348 VAL B CG2 1 ATOM 2304 N N . LEU B 2 101 ? 18.573 40.635 32.093 1.00 13.72 ? 349 LEU B N 1 ATOM 2305 C CA . LEU B 2 101 ? 18.230 41.944 31.536 1.00 14.54 ? 349 LEU B CA 1 ATOM 2306 C C . LEU B 2 101 ? 19.180 42.991 32.099 1.00 12.60 ? 349 LEU B C 1 ATOM 2307 O O . LEU B 2 101 ? 19.710 42.852 33.214 1.00 12.38 ? 349 LEU B O 1 ATOM 2308 C CB . LEU B 2 101 ? 16.758 42.312 31.787 1.00 15.41 ? 349 LEU B CB 1 ATOM 2309 C CG . LEU B 2 101 ? 15.845 41.519 30.780 1.00 19.93 ? 349 LEU B CG 1 ATOM 2310 C CD1 . LEU B 2 101 ? 14.457 42.073 30.728 1.00 25.81 ? 349 LEU B CD1 1 ATOM 2311 C CD2 . LEU B 2 101 ? 16.370 41.506 29.336 1.00 25.44 ? 349 LEU B CD2 1 ATOM 2312 N N . GLU B 2 102 ? 19.375 44.035 31.302 1.00 12.81 ? 350 GLU B N 1 ATOM 2313 C CA . GLU B 2 102 ? 20.462 44.963 31.582 1.00 12.93 ? 350 GLU B CA 1 ATOM 2314 C C . GLU B 2 102 ? 20.251 45.654 32.906 1.00 11.55 ? 350 GLU B C 1 ATOM 2315 O O . GLU B 2 102 ? 21.238 45.946 33.616 1.00 11.21 ? 350 GLU B O 1 ATOM 2316 C CB . GLU B 2 102 ? 20.548 45.955 30.428 1.00 12.19 ? 350 GLU B CB 1 ATOM 2317 C CG . GLU B 2 102 ? 21.837 46.787 30.372 1.00 14.76 ? 350 GLU B CG 1 ATOM 2318 C CD . GLU B 2 102 ? 21.787 48.042 31.180 1.00 17.51 ? 350 GLU B CD 1 ATOM 2319 O OE1 . GLU B 2 102 ? 22.808 48.762 31.157 1.00 18.14 ? 350 GLU B OE1 1 ATOM 2320 O OE2 . GLU B 2 102 ? 20.737 48.369 31.758 1.00 16.21 ? 350 GLU B OE2 1 ATOM 2321 N N . TRP B 2 103 ? 18.998 45.974 33.246 1.00 12.76 ? 351 TRP B N 1 ATOM 2322 C CA . TRP B 2 103 ? 18.781 46.731 34.484 1.00 13.27 ? 351 TRP B CA 1 ATOM 2323 C C . TRP B 2 103 ? 19.269 45.940 35.679 1.00 13.29 ? 351 TRP B C 1 ATOM 2324 O O . TRP B 2 103 ? 19.852 46.509 36.615 1.00 12.21 ? 351 TRP B O 1 ATOM 2325 C CB . TRP B 2 103 ? 17.304 47.171 34.638 1.00 13.78 ? 351 TRP B CB 1 ATOM 2326 C CG . TRP B 2 103 ? 16.350 46.061 34.956 1.00 13.38 ? 351 TRP B CG 1 ATOM 2327 C CD1 . TRP B 2 103 ? 15.765 45.197 34.070 1.00 14.78 ? 351 TRP B CD1 1 ATOM 2328 C CD2 . TRP B 2 103 ? 15.905 45.669 36.251 1.00 15.26 ? 351 TRP B CD2 1 ATOM 2329 N NE1 . TRP B 2 103 ? 14.960 44.294 34.745 1.00 16.68 ? 351 TRP B NE1 1 ATOM 2330 C CE2 . TRP B 2 103 ? 15.007 44.593 36.082 1.00 15.75 ? 351 TRP B CE2 1 ATOM 2331 C CE3 . TRP B 2 103 ? 16.155 46.151 37.550 1.00 15.55 ? 351 TRP B CE3 1 ATOM 2332 C CZ2 . TRP B 2 103 ? 14.382 43.958 37.154 1.00 14.88 ? 351 TRP B CZ2 1 ATOM 2333 C CZ3 . TRP B 2 103 ? 15.493 45.519 38.640 1.00 16.54 ? 351 TRP B CZ3 1 ATOM 2334 C CH2 . TRP B 2 103 ? 14.641 44.441 38.435 1.00 15.31 ? 351 TRP B CH2 1 ATOM 2335 N N . ILE B 2 104 ? 19.076 44.614 35.660 1.00 11.51 ? 352 ILE B N 1 ATOM 2336 C CA . ILE B 2 104 ? 19.584 43.779 36.752 1.00 11.40 ? 352 ILE B CA 1 ATOM 2337 C C . ILE B 2 104 ? 21.111 43.736 36.758 1.00 11.12 ? 352 ILE B C 1 ATOM 2338 O O . ILE B 2 104 ? 21.727 43.874 37.823 1.00 11.45 ? 352 ILE B O 1 ATOM 2339 C CB . ILE B 2 104 ? 19.022 42.333 36.698 1.00 11.29 ? 352 ILE B CB 1 ATOM 2340 C CG1 . ILE B 2 104 ? 17.487 42.389 36.802 1.00 12.90 ? 352 ILE B CG1 1 ATOM 2341 C CG2 . ILE B 2 104 ? 19.656 41.470 37.825 1.00 13.34 ? 352 ILE B CG2 1 ATOM 2342 C CD1 . ILE B 2 104 ? 16.761 41.052 36.513 1.00 15.06 ? 352 ILE B CD1 1 ATOM 2343 N N . ARG B 2 105 ? 21.725 43.509 35.593 1.00 10.69 ? 353 ARG B N 1 ATOM 2344 C CA . ARG B 2 105 ? 23.202 43.458 35.519 1.00 11.66 ? 353 ARG B CA 1 ATOM 2345 C C . ARG B 2 105 ? 23.818 44.759 36.044 1.00 11.61 ? 353 ARG B C 1 ATOM 2346 O O . ARG B 2 105 ? 24.831 44.740 36.772 1.00 11.68 ? 353 ARG B O 1 ATOM 2347 C CB . ARG B 2 105 ? 23.621 43.199 34.067 1.00 11.17 ? 353 ARG B CB 1 ATOM 2348 C CG . ARG B 2 105 ? 23.184 41.772 33.683 1.00 13.19 ? 353 ARG B CG 1 ATOM 2349 C CD . ARG B 2 105 ? 23.817 41.349 32.353 1.00 10.27 ? 353 ARG B CD 1 ATOM 2350 N NE . ARG B 2 105 ? 23.134 42.012 31.244 1.00 12.66 ? 353 ARG B NE 1 ATOM 2351 C CZ . ARG B 2 105 ? 23.666 42.932 30.449 1.00 12.78 ? 353 ARG B CZ 1 ATOM 2352 N NH1 . ARG B 2 105 ? 24.927 43.315 30.612 1.00 11.47 ? 353 ARG B NH1 1 ATOM 2353 N NH2 . ARG B 2 105 ? 22.927 43.447 29.445 1.00 12.93 ? 353 ARG B NH2 1 ATOM 2354 N N . ASN B 2 106 ? 23.179 45.880 35.715 1.00 12.26 ? 354 ASN B N 1 ATOM 2355 C CA . ASN B 2 106 ? 23.630 47.197 36.188 1.00 12.65 ? 354 ASN B CA 1 ATOM 2356 C C . ASN B 2 106 ? 23.562 47.268 37.727 1.00 12.09 ? 354 ASN B C 1 ATOM 2357 O O . ASN B 2 106 ? 24.533 47.676 38.387 1.00 12.47 ? 354 ASN B O 1 ATOM 2358 C CB . ASN B 2 106 ? 22.724 48.262 35.532 1.00 12.82 ? 354 ASN B CB 1 ATOM 2359 C CG . ASN B 2 106 ? 22.974 49.668 36.040 1.00 17.14 ? 354 ASN B CG 1 ATOM 2360 O OD1 . ASN B 2 106 ? 23.957 49.982 36.743 1.00 20.11 ? 354 ASN B OD1 1 ATOM 2361 N ND2 . ASN B 2 106 ? 22.119 50.528 35.620 1.00 13.61 ? 354 ASN B ND2 1 ATOM 2362 N N . VAL B 2 107 ? 22.440 46.857 38.304 1.00 12.56 ? 355 VAL B N 1 ATOM 2363 C CA . VAL B 2 107 ? 22.284 46.949 39.761 1.00 13.20 ? 355 VAL B CA 1 ATOM 2364 C C . VAL B 2 107 ? 23.286 46.037 40.469 1.00 13.83 ? 355 VAL B C 1 ATOM 2365 O O . VAL B 2 107 ? 23.933 46.452 41.459 1.00 12.33 ? 355 VAL B O 1 ATOM 2366 C CB . VAL B 2 107 ? 20.846 46.578 40.159 1.00 13.27 ? 355 VAL B CB 1 ATOM 2367 C CG1 . VAL B 2 107 ? 20.747 46.274 41.656 1.00 16.45 ? 355 VAL B CG1 1 ATOM 2368 C CG2 . VAL B 2 107 ? 19.874 47.752 39.719 1.00 14.49 ? 355 VAL B CG2 1 ATOM 2369 N N . VAL B 2 108 ? 23.438 44.809 39.944 1.00 12.99 ? 356 VAL B N 1 ATOM 2370 C CA . VAL B 2 108 ? 24.367 43.852 40.554 1.00 13.51 ? 356 VAL B CA 1 ATOM 2371 C C . VAL B 2 108 ? 25.825 44.336 40.449 1.00 12.89 ? 356 VAL B C 1 ATOM 2372 O O . VAL B 2 108 ? 26.582 44.257 41.431 1.00 12.14 ? 356 VAL B O 1 ATOM 2373 C CB . VAL B 2 108 ? 24.173 42.447 39.948 1.00 13.80 ? 356 VAL B CB 1 ATOM 2374 C CG1 . VAL B 2 108 ? 25.301 41.467 40.419 1.00 15.47 ? 356 VAL B CG1 1 ATOM 2375 C CG2 . VAL B 2 108 ? 22.754 41.928 40.348 1.00 14.55 ? 356 VAL B CG2 1 ATOM 2376 N N . ALA B 2 109 ? 26.228 44.809 39.265 1.00 11.95 ? 357 ALA B N 1 ATOM 2377 C CA . ALA B 2 109 ? 27.582 45.376 39.107 1.00 12.31 ? 357 ALA B CA 1 ATOM 2378 C C . ALA B 2 109 ? 27.810 46.559 40.062 1.00 12.61 ? 357 ALA B C 1 ATOM 2379 O O . ALA B 2 109 ? 28.883 46.650 40.676 1.00 12.06 ? 357 ALA B O 1 ATOM 2380 C CB . ALA B 2 109 ? 27.840 45.815 37.647 1.00 13.77 ? 357 ALA B CB 1 ATOM 2381 N N . ASN B 2 110 ? 26.821 47.459 40.186 1.00 11.83 ? 358 ASN B N 1 ATOM 2382 C CA . ASN B 2 110 ? 26.978 48.603 41.100 1.00 12.54 ? 358 ASN B CA 1 ATOM 2383 C C . ASN B 2 110 ? 27.147 48.161 42.537 1.00 13.28 ? 358 ASN B C 1 ATOM 2384 O O . ASN B 2 110 ? 27.895 48.767 43.295 1.00 13.68 ? 358 ASN B O 1 ATOM 2385 C CB . ASN B 2 110 ? 25.729 49.473 41.077 1.00 13.25 ? 358 ASN B CB 1 ATOM 2386 C CG . ASN B 2 110 ? 25.692 50.424 39.892 1.00 14.20 ? 358 ASN B CG 1 ATOM 2387 O OD1 . ASN B 2 110 ? 26.674 50.625 39.153 1.00 14.41 ? 358 ASN B OD1 1 ATOM 2388 N ND2 . ASN B 2 110 ? 24.517 51.027 39.712 1.00 13.35 ? 358 ASN B ND2 1 ATOM 2389 N N . ARG B 2 111 ? 26.503 47.059 42.901 1.00 13.45 ? 359 ARG B N 1 ATOM 2390 C CA . ARG B 2 111 ? 26.576 46.573 44.276 1.00 15.27 ? 359 ARG B CA 1 ATOM 2391 C C . ARG B 2 111 ? 27.922 45.909 44.569 1.00 14.59 ? 359 ARG B C 1 ATOM 2392 O O . ARG B 2 111 ? 28.500 46.130 45.621 1.00 15.09 ? 359 ARG B O 1 ATOM 2393 C CB . ARG B 2 111 ? 25.445 45.563 44.501 1.00 16.38 ? 359 ARG B CB 1 ATOM 2394 C CG . ARG B 2 111 ? 24.706 45.743 45.786 1.00 22.86 ? 359 ARG B CG 1 ATOM 2395 C CD . ARG B 2 111 ? 23.573 44.721 45.937 1.00 22.70 ? 359 ARG B CD 1 ATOM 2396 N NE . ARG B 2 111 ? 22.265 45.061 45.423 1.00 22.13 ? 359 ARG B NE 1 ATOM 2397 C CZ . ARG B 2 111 ? 21.461 44.189 44.816 1.00 24.11 ? 359 ARG B CZ 1 ATOM 2398 N NH1 . ARG B 2 111 ? 21.878 42.948 44.569 1.00 24.36 ? 359 ARG B NH1 1 ATOM 2399 N NH2 . ARG B 2 111 ? 20.260 44.548 44.399 1.00 24.17 ? 359 ARG B NH2 1 ATOM 2400 N N . LEU B 2 112 ? 28.456 45.130 43.635 1.00 13.78 ? 360 LEU B N 1 ATOM 2401 C CA . LEU B 2 112 ? 29.606 44.271 43.959 1.00 14.38 ? 360 LEU B CA 1 ATOM 2402 C C . LEU B 2 112 ? 30.955 44.918 43.661 1.00 15.89 ? 360 LEU B C 1 ATOM 2403 O O . LEU B 2 112 ? 31.980 44.555 44.295 1.00 17.41 ? 360 LEU B O 1 ATOM 2404 C CB . LEU B 2 112 ? 29.536 42.968 43.151 1.00 14.75 ? 360 LEU B CB 1 ATOM 2405 C CG . LEU B 2 112 ? 28.403 41.996 43.538 1.00 14.33 ? 360 LEU B CG 1 ATOM 2406 C CD1 . LEU B 2 112 ? 28.526 40.760 42.647 1.00 16.32 ? 360 LEU B CD1 1 ATOM 2407 C CD2 . LEU B 2 112 ? 28.544 41.601 45.050 1.00 15.13 ? 360 LEU B CD2 1 ATOM 2408 N N . ALA B 2 113 ? 30.991 45.829 42.681 1.00 15.07 ? 361 ALA B N 1 ATOM 2409 C CA . ALA B 2 113 ? 32.267 46.376 42.219 1.00 15.37 ? 361 ALA B CA 1 ATOM 2410 C C . ALA B 2 113 ? 33.045 47.162 43.266 1.00 16.59 ? 361 ALA B C 1 ATOM 2411 O O . ALA B 2 113 ? 32.492 48.004 43.980 1.00 16.35 ? 361 ALA B O 1 ATOM 2412 C CB . ALA B 2 113 ? 32.038 47.273 40.970 1.00 15.82 ? 361 ALA B CB 1 ATOM 2413 N N . LEU B 2 114 ? 34.353 46.928 43.297 1.00 17.12 ? 362 LEU B N 1 ATOM 2414 C CA . LEU B 2 114 ? 35.277 47.754 44.075 1.00 19.24 ? 362 LEU B CA 1 ATOM 2415 C C . LEU B 2 114 ? 35.995 48.755 43.169 1.00 17.41 ? 362 LEU B C 1 ATOM 2416 O O . LEU B 2 114 ? 36.584 49.701 43.647 1.00 18.41 ? 362 LEU B O 1 ATOM 2417 C CB . LEU B 2 114 ? 36.388 46.858 44.655 1.00 20.46 ? 362 LEU B CB 1 ATOM 2418 C CG . LEU B 2 114 ? 36.279 45.962 45.892 1.00 29.09 ? 362 LEU B CG 1 ATOM 2419 C CD1 . LEU B 2 114 ? 37.031 46.630 47.091 1.00 31.89 ? 362 LEU B CD1 1 ATOM 2420 C CD2 . LEU B 2 114 ? 34.846 45.573 46.259 1.00 31.47 ? 362 LEU B CD2 1 ATOM 2421 N N . ASP B 2 115 ? 36.010 48.494 41.866 1.00 16.54 ? 363 ASP B N 1 ATOM 2422 C CA . ASP B 2 115 ? 36.803 49.266 40.923 1.00 16.17 ? 363 ASP B CA 1 ATOM 2423 C C . ASP B 2 115 ? 36.225 49.052 39.540 1.00 15.38 ? 363 ASP B C 1 ATOM 2424 O O . ASP B 2 115 ? 35.283 48.278 39.386 1.00 15.51 ? 363 ASP B O 1 ATOM 2425 C CB . ASP B 2 115 ? 38.338 48.933 40.988 1.00 16.36 ? 363 ASP B CB 1 ATOM 2426 C CG . ASP B 2 115 ? 38.669 47.491 40.700 1.00 22.31 ? 363 ASP B CG 1 ATOM 2427 O OD1 . ASP B 2 115 ? 39.770 47.063 41.135 1.00 27.56 ? 363 ASP B OD1 1 ATOM 2428 O OD2 . ASP B 2 115 ? 37.910 46.767 40.030 1.00 22.98 ? 363 ASP B OD2 1 ATOM 2429 N N . GLY B 2 116 ? 36.752 49.762 38.548 1.00 14.21 ? 364 GLY B N 1 ATOM 2430 C CA . GLY B 2 116 ? 36.211 49.726 37.182 1.00 14.28 ? 364 GLY B CA 1 ATOM 2431 C C . GLY B 2 116 ? 36.326 48.337 36.559 1.00 14.94 ? 364 GLY B C 1 ATOM 2432 O O . GLY B 2 116 ? 35.389 47.838 35.940 1.00 14.83 ? 364 GLY B O 1 ATOM 2433 N N . ALA B 2 117 ? 37.480 47.697 36.746 1.00 14.63 ? 365 ALA B N 1 ATOM 2434 C CA . ALA B 2 117 ? 37.690 46.357 36.177 1.00 15.28 ? 365 ALA B CA 1 ATOM 2435 C C . ALA B 2 117 ? 36.652 45.355 36.712 1.00 15.27 ? 365 ALA B C 1 ATOM 2436 O O . ALA B 2 117 ? 36.069 44.571 35.937 1.00 15.09 ? 365 ALA B O 1 ATOM 2437 C CB . ALA B 2 117 ? 39.111 45.874 36.487 1.00 15.69 ? 365 ALA B CB 1 ATOM 2438 N N . THR B 2 118 ? 36.421 45.377 38.016 1.00 14.02 ? 366 THR B N 1 ATOM 2439 C CA A THR B 2 118 ? 35.467 44.436 38.602 0.50 14.15 ? 366 THR B CA 1 ATOM 2440 C CA B THR B 2 118 ? 35.459 44.467 38.654 0.50 15.10 ? 366 THR B CA 1 ATOM 2441 C C . THR B 2 118 ? 34.034 44.762 38.190 1.00 14.99 ? 366 THR B C 1 ATOM 2442 O O . THR B 2 118 ? 33.245 43.844 37.975 1.00 13.53 ? 366 THR B O 1 ATOM 2443 C CB A THR B 2 118 ? 35.630 44.285 40.123 0.50 14.90 ? 366 THR B CB 1 ATOM 2444 C CB B THR B 2 118 ? 35.496 44.580 40.181 0.50 15.78 ? 366 THR B CB 1 ATOM 2445 O OG1 A THR B 2 118 ? 35.520 45.564 40.778 0.50 11.65 ? 366 THR B OG1 1 ATOM 2446 O OG1 B THR B 2 118 ? 36.793 44.180 40.658 0.50 18.65 ? 366 THR B OG1 1 ATOM 2447 C CG2 A THR B 2 118 ? 37.029 43.669 40.408 0.50 14.94 ? 366 THR B CG2 1 ATOM 2448 C CG2 B THR B 2 118 ? 34.456 43.680 40.794 0.50 16.48 ? 366 THR B CG2 1 ATOM 2449 N N . TRP B 2 119 ? 33.708 46.064 38.096 1.00 12.90 ? 367 TRP B N 1 ATOM 2450 C CA . TRP B 2 119 ? 32.360 46.441 37.621 1.00 12.04 ? 367 TRP B CA 1 ATOM 2451 C C . TRP B 2 119 ? 32.118 45.786 36.257 1.00 12.25 ? 367 TRP B C 1 ATOM 2452 O O . TRP B 2 119 ? 31.074 45.154 36.012 1.00 12.50 ? 367 TRP B O 1 ATOM 2453 C CB . TRP B 2 119 ? 32.243 47.969 37.470 1.00 12.20 ? 367 TRP B CB 1 ATOM 2454 C CG . TRP B 2 119 ? 30.807 48.426 37.315 1.00 11.88 ? 367 TRP B CG 1 ATOM 2455 C CD1 . TRP B 2 119 ? 29.960 48.874 38.315 1.00 14.28 ? 367 TRP B CD1 1 ATOM 2456 C CD2 . TRP B 2 119 ? 30.071 48.491 36.102 1.00 11.42 ? 367 TRP B CD2 1 ATOM 2457 N NE1 . TRP B 2 119 ? 28.725 49.200 37.772 1.00 12.72 ? 367 TRP B NE1 1 ATOM 2458 C CE2 . TRP B 2 119 ? 28.779 49.007 36.417 1.00 13.92 ? 367 TRP B CE2 1 ATOM 2459 C CE3 . TRP B 2 119 ? 30.372 48.177 34.767 1.00 11.54 ? 367 TRP B CE3 1 ATOM 2460 C CZ2 . TRP B 2 119 ? 27.772 49.171 35.439 1.00 11.81 ? 367 TRP B CZ2 1 ATOM 2461 C CZ3 . TRP B 2 119 ? 29.373 48.367 33.781 1.00 13.57 ? 367 TRP B CZ3 1 ATOM 2462 C CH2 . TRP B 2 119 ? 28.095 48.858 34.134 1.00 11.23 ? 367 TRP B CH2 1 ATOM 2463 N N . ALA B 2 120 ? 33.112 45.908 35.374 1.00 12.43 ? 368 ALA B N 1 ATOM 2464 C CA . ALA B 2 120 ? 32.971 45.403 33.997 1.00 12.88 ? 368 ALA B CA 1 ATOM 2465 C C . ALA B 2 120 ? 32.832 43.877 33.994 1.00 14.93 ? 368 ALA B C 1 ATOM 2466 O O . ALA B 2 120 ? 31.981 43.311 33.280 1.00 13.49 ? 368 ALA B O 1 ATOM 2467 C CB . ALA B 2 120 ? 34.154 45.828 33.177 1.00 13.36 ? 368 ALA B CB 1 ATOM 2468 N N . ASP B 2 121 ? 33.650 43.232 34.825 1.00 14.67 ? 369 ASP B N 1 ATOM 2469 C CA A ASP B 2 121 ? 33.648 41.763 34.936 0.50 15.66 ? 369 ASP B CA 1 ATOM 2470 C CA B ASP B 2 121 ? 33.656 41.773 34.933 0.50 15.93 ? 369 ASP B CA 1 ATOM 2471 C C . ASP B 2 121 ? 32.276 41.260 35.352 1.00 14.70 ? 369 ASP B C 1 ATOM 2472 O O . ASP B 2 121 ? 31.791 40.260 34.819 1.00 15.82 ? 369 ASP B O 1 ATOM 2473 C CB A ASP B 2 121 ? 34.673 41.308 35.982 0.50 16.24 ? 369 ASP B CB 1 ATOM 2474 C CB B ASP B 2 121 ? 34.706 41.339 35.966 0.50 16.65 ? 369 ASP B CB 1 ATOM 2475 C CG A ASP B 2 121 ? 34.908 39.789 35.972 0.50 18.58 ? 369 ASP B CG 1 ATOM 2476 C CG B ASP B 2 121 ? 36.145 41.360 35.413 0.50 20.30 ? 369 ASP B CG 1 ATOM 2477 O OD1 A ASP B 2 121 ? 35.079 39.192 34.893 0.50 23.57 ? 369 ASP B OD1 1 ATOM 2478 O OD1 B ASP B 2 121 ? 36.346 41.549 34.192 0.50 25.67 ? 369 ASP B OD1 1 ATOM 2479 O OD2 A ASP B 2 121 ? 34.942 39.203 37.054 0.50 23.38 ? 369 ASP B OD2 1 ATOM 2480 O OD2 B ASP B 2 121 ? 37.090 41.162 36.222 0.50 24.49 ? 369 ASP B OD2 1 ATOM 2481 N N . VAL B 2 122 ? 31.651 41.940 36.323 1.00 13.06 ? 370 VAL B N 1 ATOM 2482 C CA . VAL B 2 122 ? 30.330 41.523 36.788 1.00 12.54 ? 370 VAL B CA 1 ATOM 2483 C C . VAL B 2 122 ? 29.239 41.829 35.755 1.00 13.01 ? 370 VAL B C 1 ATOM 2484 O O . VAL B 2 122 ? 28.389 40.998 35.423 1.00 12.41 ? 370 VAL B O 1 ATOM 2485 C CB . VAL B 2 122 ? 29.963 42.235 38.119 1.00 12.64 ? 370 VAL B CB 1 ATOM 2486 C CG1 . VAL B 2 122 ? 28.466 41.931 38.515 1.00 14.06 ? 370 VAL B CG1 1 ATOM 2487 C CG2 . VAL B 2 122 ? 30.967 41.786 39.260 1.00 13.87 ? 370 VAL B CG2 1 ATOM 2488 N N . PHE B 2 123 ? 29.307 43.033 35.207 1.00 11.95 ? 371 PHE B N 1 ATOM 2489 C CA . PHE B 2 123 ? 28.236 43.489 34.347 1.00 11.59 ? 371 PHE B CA 1 ATOM 2490 C C . PHE B 2 123 ? 28.155 42.655 33.083 1.00 13.53 ? 371 PHE B C 1 ATOM 2491 O O . PHE B 2 123 ? 27.079 42.481 32.544 1.00 14.12 ? 371 PHE B O 1 ATOM 2492 C CB . PHE B 2 123 ? 28.499 44.938 33.948 1.00 11.07 ? 371 PHE B CB 1 ATOM 2493 C CG . PHE B 2 123 ? 27.427 45.523 33.060 1.00 9.68 ? 371 PHE B CG 1 ATOM 2494 C CD1 . PHE B 2 123 ? 26.177 45.897 33.595 1.00 11.82 ? 371 PHE B CD1 1 ATOM 2495 C CD2 . PHE B 2 123 ? 27.668 45.702 31.687 1.00 11.57 ? 371 PHE B CD2 1 ATOM 2496 C CE1 . PHE B 2 123 ? 25.176 46.449 32.744 1.00 9.63 ? 371 PHE B CE1 1 ATOM 2497 C CE2 . PHE B 2 123 ? 26.671 46.245 30.840 1.00 11.62 ? 371 PHE B CE2 1 ATOM 2498 C CZ . PHE B 2 123 ? 25.437 46.620 31.375 1.00 12.43 ? 371 PHE B CZ 1 ATOM 2499 N N . LYS B 2 124 ? 29.297 42.199 32.574 1.00 13.05 ? 372 LYS B N 1 ATOM 2500 C CA . LYS B 2 124 ? 29.255 41.613 31.265 1.00 14.20 ? 372 LYS B CA 1 ATOM 2501 C C . LYS B 2 124 ? 28.762 40.175 31.279 1.00 15.22 ? 372 LYS B C 1 ATOM 2502 O O . LYS B 2 124 ? 28.547 39.572 30.195 1.00 15.48 ? 372 LYS B O 1 ATOM 2503 C CB . LYS B 2 124 ? 30.612 41.717 30.568 1.00 14.75 ? 372 LYS B CB 1 ATOM 2504 C CG . LYS B 2 124 ? 31.652 40.788 31.139 1.00 14.40 ? 372 LYS B CG 1 ATOM 2505 C CD . LYS B 2 124 ? 32.948 41.201 30.451 1.00 23.64 ? 372 LYS B CD 1 ATOM 2506 C CE . LYS B 2 124 ? 34.053 40.249 30.667 1.00 30.49 ? 372 LYS B CE 1 ATOM 2507 N NZ . LYS B 2 124 ? 35.240 40.921 30.001 1.00 36.32 ? 372 LYS B NZ 1 ATOM 2508 N N . ARG B 2 125 ? 28.605 39.592 32.472 1.00 14.00 ? 373 ARG B N 1 ATOM 2509 C CA . ARG B 2 125 ? 28.090 38.196 32.524 1.00 14.42 ? 373 ARG B CA 1 ATOM 2510 C C . ARG B 2 125 ? 26.653 38.104 32.026 1.00 12.47 ? 373 ARG B C 1 ATOM 2511 O O . ARG B 2 125 ? 25.838 38.982 32.338 1.00 13.96 ? 373 ARG B O 1 ATOM 2512 C CB . ARG B 2 125 ? 28.145 37.678 33.934 1.00 13.46 ? 373 ARG B CB 1 ATOM 2513 C CG . ARG B 2 125 ? 29.629 37.569 34.486 1.00 16.05 ? 373 ARG B CG 1 ATOM 2514 C CD . ARG B 2 125 ? 29.628 36.909 35.833 1.00 20.19 ? 373 ARG B CD 1 ATOM 2515 N NE . ARG B 2 125 ? 30.974 36.895 36.436 1.00 19.53 ? 373 ARG B NE 1 ATOM 2516 C CZ . ARG B 2 125 ? 31.969 36.073 36.057 1.00 24.01 ? 373 ARG B CZ 1 ATOM 2517 N NH1 . ARG B 2 125 ? 33.160 36.132 36.691 1.00 22.76 ? 373 ARG B NH1 1 ATOM 2518 N NH2 . ARG B 2 125 ? 31.815 35.206 35.050 1.00 20.49 ? 373 ARG B NH2 1 ATOM 2519 N N . PHE B 2 126 ? 26.334 37.041 31.269 1.00 12.66 ? 374 PHE B N 1 ATOM 2520 C CA . PHE B 2 126 ? 24.963 36.833 30.787 1.00 12.12 ? 374 PHE B CA 1 ATOM 2521 C C . PHE B 2 126 ? 24.456 38.077 30.037 1.00 12.35 ? 374 PHE B C 1 ATOM 2522 O O . PHE B 2 126 ? 23.295 38.467 30.173 1.00 12.22 ? 374 PHE B O 1 ATOM 2523 C CB . PHE B 2 126 ? 24.008 36.486 31.947 1.00 12.51 ? 374 PHE B CB 1 ATOM 2524 C CG . PHE B 2 126 ? 24.455 35.293 32.773 1.00 14.05 ? 374 PHE B CG 1 ATOM 2525 C CD1 . PHE B 2 126 ? 24.915 35.467 34.067 1.00 15.17 ? 374 PHE B CD1 1 ATOM 2526 C CD2 . PHE B 2 126 ? 24.429 34.003 32.219 1.00 13.72 ? 374 PHE B CD2 1 ATOM 2527 C CE1 . PHE B 2 126 ? 25.362 34.336 34.846 1.00 16.96 ? 374 PHE B CE1 1 ATOM 2528 C CE2 . PHE B 2 126 ? 24.831 32.874 32.997 1.00 15.95 ? 374 PHE B CE2 1 ATOM 2529 C CZ . PHE B 2 126 ? 25.300 33.054 34.282 1.00 16.01 ? 374 PHE B CZ 1 ATOM 2530 N N . ASN B 2 127 ? 25.314 38.620 29.184 1.00 13.27 ? 375 ASN B N 1 ATOM 2531 C CA . ASN B 2 127 ? 24.959 39.813 28.403 1.00 13.61 ? 375 ASN B CA 1 ATOM 2532 C C . ASN B 2 127 ? 23.689 39.543 27.613 1.00 14.18 ? 375 ASN B C 1 ATOM 2533 O O . ASN B 2 127 ? 23.642 38.610 26.806 1.00 15.30 ? 375 ASN B O 1 ATOM 2534 C CB . ASN B 2 127 ? 26.114 40.147 27.455 1.00 13.82 ? 375 ASN B CB 1 ATOM 2535 C CG . ASN B 2 127 ? 25.729 41.164 26.386 1.00 15.98 ? 375 ASN B CG 1 ATOM 2536 O OD1 . ASN B 2 127 ? 24.836 42.004 26.605 1.00 14.24 ? 375 ASN B OD1 1 ATOM 2537 N ND2 . ASN B 2 127 ? 26.425 41.103 25.228 1.00 15.29 ? 375 ASN B ND2 1 ATOM 2538 N N . SER B 2 128 ? 22.660 40.363 27.843 1.00 14.12 ? 376 SER B N 1 ATOM 2539 C CA . SER B 2 128 ? 21.348 40.189 27.182 1.00 14.49 ? 376 SER B CA 1 ATOM 2540 C C . SER B 2 128 ? 21.259 40.734 25.763 1.00 14.11 ? 376 SER B C 1 ATOM 2541 O O . SER B 2 128 ? 20.304 40.424 25.047 1.00 13.91 ? 376 SER B O 1 ATOM 2542 C CB . SER B 2 128 ? 20.259 40.884 28.019 1.00 14.51 ? 376 SER B CB 1 ATOM 2543 O OG . SER B 2 128 ? 20.541 42.283 28.176 1.00 14.63 ? 376 SER B OG 1 ATOM 2544 N N . GLY B 2 129 ? 22.189 41.612 25.388 1.00 13.13 ? 377 GLY B N 1 ATOM 2545 C CA . GLY B 2 129 ? 22.113 42.292 24.122 1.00 13.91 ? 377 GLY B CA 1 ATOM 2546 C C . GLY B 2 129 ? 20.925 43.261 24.100 1.00 14.70 ? 377 GLY B C 1 ATOM 2547 O O . GLY B 2 129 ? 20.436 43.619 23.042 1.00 14.06 ? 377 GLY B O 1 ATOM 2548 N N . THR B 2 130 ? 20.467 43.665 25.281 1.00 13.96 ? 378 THR B N 1 ATOM 2549 C CA . THR B 2 130 ? 19.365 44.633 25.389 1.00 15.00 ? 378 THR B CA 1 ATOM 2550 C C . THR B 2 130 ? 19.791 45.802 26.284 1.00 14.08 ? 378 THR B C 1 ATOM 2551 O O . THR B 2 130 ? 20.636 45.631 27.185 1.00 14.34 ? 378 THR B O 1 ATOM 2552 C CB . THR B 2 130 ? 18.090 44.000 25.902 1.00 14.77 ? 378 THR B CB 1 ATOM 2553 O OG1 . THR B 2 130 ? 18.295 43.513 27.244 1.00 15.73 ? 378 THR B OG1 1 ATOM 2554 C CG2 . THR B 2 130 ? 17.648 42.828 24.945 1.00 16.00 ? 378 THR B CG2 1 ATOM 2555 N N . TYR B 2 131 ? 19.202 46.970 26.011 1.00 14.26 ? 379 TYR B N 1 ATOM 2556 C CA . TYR B 2 131 ? 19.677 48.284 26.544 1.00 14.74 ? 379 TYR B CA 1 ATOM 2557 C C . TYR B 2 131 ? 21.186 48.394 26.333 1.00 14.18 ? 379 TYR B C 1 ATOM 2558 O O . TYR B 2 131 ? 21.974 48.455 27.303 1.00 14.69 ? 379 TYR B O 1 ATOM 2559 C CB . TYR B 2 131 ? 19.345 48.449 28.008 1.00 16.43 ? 379 TYR B CB 1 ATOM 2560 C CG . TYR B 2 131 ? 19.182 49.911 28.436 1.00 16.72 ? 379 TYR B CG 1 ATOM 2561 C CD1 . TYR B 2 131 ? 19.069 50.259 29.789 1.00 20.45 ? 379 TYR B CD1 1 ATOM 2562 C CD2 . TYR B 2 131 ? 19.061 50.914 27.487 1.00 20.69 ? 379 TYR B CD2 1 ATOM 2563 C CE1 . TYR B 2 131 ? 18.915 51.620 30.171 1.00 21.08 ? 379 TYR B CE1 1 ATOM 2564 C CE2 . TYR B 2 131 ? 18.864 52.248 27.851 1.00 22.87 ? 379 TYR B CE2 1 ATOM 2565 C CZ . TYR B 2 131 ? 18.807 52.593 29.193 1.00 24.40 ? 379 TYR B CZ 1 ATOM 2566 O OH . TYR B 2 131 ? 18.615 53.944 29.508 1.00 25.35 ? 379 TYR B OH 1 ATOM 2567 N N . ASN B 2 132 ? 21.571 48.370 25.060 1.00 13.49 ? 380 ASN B N 1 ATOM 2568 C CA . ASN B 2 132 ? 22.982 48.344 24.631 1.00 12.78 ? 380 ASN B CA 1 ATOM 2569 C C . ASN B 2 132 ? 23.602 49.734 24.810 1.00 13.21 ? 380 ASN B C 1 ATOM 2570 O O . ASN B 2 132 ? 23.211 50.685 24.133 1.00 14.36 ? 380 ASN B O 1 ATOM 2571 C CB . ASN B 2 132 ? 23.012 47.935 23.172 1.00 12.69 ? 380 ASN B CB 1 ATOM 2572 C CG . ASN B 2 132 ? 22.540 46.507 22.981 1.00 14.01 ? 380 ASN B CG 1 ATOM 2573 O OD1 . ASN B 2 132 ? 23.093 45.608 23.599 1.00 13.23 ? 380 ASN B OD1 1 ATOM 2574 N ND2 . ASN B 2 132 ? 21.500 46.296 22.175 1.00 13.91 ? 380 ASN B ND2 1 ATOM 2575 N N . ASN B 2 133 ? 24.518 49.857 25.757 1.00 12.26 ? 381 ASN B N 1 ATOM 2576 C CA . ASN B 2 133 ? 25.028 51.155 26.172 1.00 12.80 ? 381 ASN B CA 1 ATOM 2577 C C . ASN B 2 133 ? 26.551 51.229 26.105 1.00 13.84 ? 381 ASN B C 1 ATOM 2578 O O . ASN B 2 133 ? 27.214 50.191 26.068 1.00 14.00 ? 381 ASN B O 1 ATOM 2579 C CB . ASN B 2 133 ? 24.660 51.401 27.629 1.00 13.67 ? 381 ASN B CB 1 ATOM 2580 C CG . ASN B 2 133 ? 23.171 51.513 27.846 1.00 14.95 ? 381 ASN B CG 1 ATOM 2581 O OD1 . ASN B 2 133 ? 22.451 52.012 26.984 1.00 15.44 ? 381 ASN B OD1 1 ATOM 2582 N ND2 . ASN B 2 133 ? 22.708 51.117 29.027 1.00 16.52 ? 381 ASN B ND2 1 ATOM 2583 N N . GLN B 2 134 ? 27.082 52.461 26.102 1.00 12.35 ? 382 GLN B N 1 ATOM 2584 C CA . GLN B 2 134 ? 28.488 52.704 26.432 1.00 12.14 ? 382 GLN B CA 1 ATOM 2585 C C . GLN B 2 134 ? 28.488 53.157 27.881 1.00 12.66 ? 382 GLN B C 1 ATOM 2586 O O . GLN B 2 134 ? 27.930 54.216 28.211 1.00 12.42 ? 382 GLN B O 1 ATOM 2587 C CB . GLN B 2 134 ? 29.144 53.801 25.579 1.00 12.14 ? 382 GLN B CB 1 ATOM 2588 C CG . GLN B 2 134 ? 30.562 54.096 26.133 1.00 15.12 ? 382 GLN B CG 1 ATOM 2589 C CD . GLN B 2 134 ? 31.131 55.424 25.656 1.00 21.61 ? 382 GLN B CD 1 ATOM 2590 O OE1 . GLN B 2 134 ? 31.076 56.438 26.371 1.00 24.55 ? 382 GLN B OE1 1 ATOM 2591 N NE2 . GLN B 2 134 ? 31.621 55.430 24.452 1.00 21.86 ? 382 GLN B NE2 1 ATOM 2592 N N . TRP B 2 135 ? 29.100 52.339 28.734 1.00 11.11 ? 383 TRP B N 1 ATOM 2593 C CA . TRP B 2 135 ? 29.187 52.631 30.162 1.00 11.83 ? 383 TRP B CA 1 ATOM 2594 C C . TRP B 2 135 ? 30.549 53.293 30.434 1.00 12.42 ? 383 TRP B C 1 ATOM 2595 O O . TRP B 2 135 ? 31.565 52.839 29.928 1.00 13.49 ? 383 TRP B O 1 ATOM 2596 C CB . TRP B 2 135 ? 29.097 51.313 30.948 1.00 12.51 ? 383 TRP B CB 1 ATOM 2597 C CG . TRP B 2 135 ? 27.630 50.909 31.209 1.00 12.12 ? 383 TRP B CG 1 ATOM 2598 C CD1 . TRP B 2 135 ? 26.873 50.021 30.477 1.00 14.39 ? 383 TRP B CD1 1 ATOM 2599 C CD2 . TRP B 2 135 ? 26.788 51.409 32.247 1.00 13.08 ? 383 TRP B CD2 1 ATOM 2600 N NE1 . TRP B 2 135 ? 25.597 49.942 31.022 1.00 14.07 ? 383 TRP B NE1 1 ATOM 2601 C CE2 . TRP B 2 135 ? 25.532 50.760 32.127 1.00 12.32 ? 383 TRP B CE2 1 ATOM 2602 C CE3 . TRP B 2 135 ? 26.983 52.320 33.291 1.00 14.30 ? 383 TRP B CE3 1 ATOM 2603 C CZ2 . TRP B 2 135 ? 24.447 51.034 32.991 1.00 13.52 ? 383 TRP B CZ2 1 ATOM 2604 C CZ3 . TRP B 2 135 ? 25.918 52.571 34.180 1.00 16.63 ? 383 TRP B CZ3 1 ATOM 2605 C CH2 . TRP B 2 135 ? 24.669 51.933 34.019 1.00 13.96 ? 383 TRP B CH2 1 ATOM 2606 N N . MET B 2 136 ? 30.540 54.316 31.277 1.00 11.90 ? 384 MET B N 1 ATOM 2607 C CA . MET B 2 136 ? 31.771 54.918 31.811 1.00 12.26 ? 384 MET B CA 1 ATOM 2608 C C . MET B 2 136 ? 31.780 54.628 33.305 1.00 12.23 ? 384 MET B C 1 ATOM 2609 O O . MET B 2 136 ? 30.776 54.901 34.010 1.00 12.70 ? 384 MET B O 1 ATOM 2610 C CB . MET B 2 136 ? 31.728 56.449 31.575 1.00 12.94 ? 384 MET B CB 1 ATOM 2611 C CG . MET B 2 136 ? 31.889 56.862 30.106 1.00 15.15 ? 384 MET B CG 1 ATOM 2612 S SD . MET B 2 136 ? 30.802 58.319 29.785 1.00 18.85 ? 384 MET B SD 1 ATOM 2613 C CE . MET B 2 136 ? 29.202 57.460 29.425 1.00 16.10 ? 384 MET B CE 1 ATOM 2614 N N . ILE B 2 137 ? 32.891 54.093 33.820 1.00 11.74 ? 385 ILE B N 1 ATOM 2615 C CA A ILE B 2 137 ? 33.049 53.864 35.246 0.50 12.66 ? 385 ILE B CA 1 ATOM 2616 C CA B ILE B 2 137 ? 33.020 53.919 35.271 0.50 12.37 ? 385 ILE B CA 1 ATOM 2617 C C . ILE B 2 137 ? 34.226 54.723 35.709 1.00 12.36 ? 385 ILE B C 1 ATOM 2618 O O . ILE B 2 137 ? 35.366 54.487 35.251 1.00 12.71 ? 385 ILE B O 1 ATOM 2619 C CB A ILE B 2 137 ? 33.346 52.364 35.521 0.50 12.79 ? 385 ILE B CB 1 ATOM 2620 C CB B ILE B 2 137 ? 33.194 52.437 35.752 0.50 12.48 ? 385 ILE B CB 1 ATOM 2621 C CG1 A ILE B 2 137 ? 32.324 51.477 34.792 0.50 13.69 ? 385 ILE B CG1 1 ATOM 2622 C CG1 B ILE B 2 137 ? 32.128 51.509 35.146 0.50 12.58 ? 385 ILE B CG1 1 ATOM 2623 C CG2 A ILE B 2 137 ? 33.353 52.088 37.017 0.50 13.32 ? 385 ILE B CG2 1 ATOM 2624 C CG2 B ILE B 2 137 ? 33.201 52.388 37.297 0.50 12.49 ? 385 ILE B CG2 1 ATOM 2625 C CD1 A ILE B 2 137 ? 30.887 51.824 35.105 0.50 13.81 ? 385 ILE B CD1 1 ATOM 2626 C CD1 B ILE B 2 137 ? 32.545 50.890 33.822 0.50 11.07 ? 385 ILE B CD1 1 ATOM 2627 N N . VAL B 2 138 ? 33.953 55.708 36.546 1.00 12.24 ? 386 VAL B N 1 ATOM 2628 C CA . VAL B 2 138 ? 34.985 56.581 37.071 1.00 13.48 ? 386 VAL B CA 1 ATOM 2629 C C . VAL B 2 138 ? 35.280 56.144 38.496 1.00 13.34 ? 386 VAL B C 1 ATOM 2630 O O . VAL B 2 138 ? 34.368 56.055 39.337 1.00 13.65 ? 386 VAL B O 1 ATOM 2631 C CB . VAL B 2 138 ? 34.476 58.021 37.074 1.00 14.04 ? 386 VAL B CB 1 ATOM 2632 C CG1 . VAL B 2 138 ? 35.519 58.929 37.734 1.00 15.56 ? 386 VAL B CG1 1 ATOM 2633 C CG2 . VAL B 2 138 ? 34.259 58.466 35.643 1.00 16.50 ? 386 VAL B CG2 1 ATOM 2634 N N . ASP B 2 139 ? 36.555 55.872 38.784 1.00 13.82 ? 387 ASP B N 1 ATOM 2635 C CA . ASP B 2 139 ? 36.909 55.428 40.112 1.00 14.66 ? 387 ASP B CA 1 ATOM 2636 C C . ASP B 2 139 ? 37.660 56.577 40.823 1.00 14.41 ? 387 ASP B C 1 ATOM 2637 O O . ASP B 2 139 ? 38.842 56.796 40.558 1.00 16.45 ? 387 ASP B O 1 ATOM 2638 C CB . ASP B 2 139 ? 37.742 54.154 40.009 1.00 12.88 ? 387 ASP B CB 1 ATOM 2639 C CG . ASP B 2 139 ? 38.068 53.550 41.378 1.00 17.71 ? 387 ASP B CG 1 ATOM 2640 O OD1 . ASP B 2 139 ? 38.653 52.448 41.392 1.00 19.63 ? 387 ASP B OD1 1 ATOM 2641 O OD2 . ASP B 2 139 ? 37.741 54.164 42.425 1.00 16.88 ? 387 ASP B OD2 1 ATOM 2642 N N . TYR B 2 140 ? 36.972 57.314 41.676 1.00 14.74 ? 388 TYR B N 1 ATOM 2643 C CA . TYR B 2 140 ? 37.596 58.451 42.328 1.00 15.22 ? 388 TYR B CA 1 ATOM 2644 C C . TYR B 2 140 ? 38.691 58.023 43.305 1.00 16.80 ? 388 TYR B C 1 ATOM 2645 O O . TYR B 2 140 ? 39.550 58.850 43.677 1.00 17.98 ? 388 TYR B O 1 ATOM 2646 C CB . TYR B 2 140 ? 36.557 59.302 43.036 1.00 14.60 ? 388 TYR B CB 1 ATOM 2647 C CG . TYR B 2 140 ? 35.867 60.341 42.153 1.00 14.93 ? 388 TYR B CG 1 ATOM 2648 C CD1 . TYR B 2 140 ? 34.487 60.393 42.089 1.00 17.09 ? 388 TYR B CD1 1 ATOM 2649 C CD2 . TYR B 2 140 ? 36.595 61.292 41.420 1.00 17.27 ? 388 TYR B CD2 1 ATOM 2650 C CE1 . TYR B 2 140 ? 33.815 61.382 41.307 1.00 17.13 ? 388 TYR B CE1 1 ATOM 2651 C CE2 . TYR B 2 140 ? 35.947 62.302 40.638 1.00 17.35 ? 388 TYR B CE2 1 ATOM 2652 C CZ . TYR B 2 140 ? 34.542 62.324 40.586 1.00 15.88 ? 388 TYR B CZ 1 ATOM 2653 O OH . TYR B 2 140 ? 33.837 63.265 39.868 1.00 14.95 ? 388 TYR B OH 1 ATOM 2654 N N . LYS B 2 141 ? 38.685 56.750 43.713 1.00 15.78 ? 389 LYS B N 1 ATOM 2655 C CA . LYS B 2 141 ? 39.757 56.272 44.605 1.00 16.81 ? 389 LYS B CA 1 ATOM 2656 C C . LYS B 2 141 ? 41.112 56.348 43.902 1.00 17.15 ? 389 LYS B C 1 ATOM 2657 O O . LYS B 2 141 ? 42.180 56.379 44.579 1.00 18.87 ? 389 LYS B O 1 ATOM 2658 C CB . LYS B 2 141 ? 39.491 54.839 45.090 1.00 16.13 ? 389 LYS B CB 1 ATOM 2659 C CG . LYS B 2 141 ? 38.221 54.685 45.864 1.00 16.89 ? 389 LYS B CG 1 ATOM 2660 C CD . LYS B 2 141 ? 38.079 53.258 46.468 1.00 16.15 ? 389 LYS B CD 1 ATOM 2661 C CE . LYS B 2 141 ? 38.075 52.154 45.394 1.00 18.63 ? 389 LYS B CE 1 ATOM 2662 N NZ . LYS B 2 141 ? 37.042 52.409 44.326 1.00 17.33 ? 389 LYS B NZ 1 ATOM 2663 N N . ALA B 2 142 ? 41.108 56.322 42.572 1.00 16.24 ? 390 ALA B N 1 ATOM 2664 C CA . ALA B 2 142 ? 42.337 56.375 41.759 1.00 16.86 ? 390 ALA B CA 1 ATOM 2665 C C . ALA B 2 142 ? 42.684 57.808 41.311 1.00 17.65 ? 390 ALA B C 1 ATOM 2666 O O . ALA B 2 142 ? 43.705 58.045 40.667 1.00 18.17 ? 390 ALA B O 1 ATOM 2667 C CB . ALA B 2 142 ? 42.206 55.442 40.545 1.00 16.85 ? 390 ALA B CB 1 ATOM 2668 N N . PHE B 2 143 ? 41.821 58.759 41.652 1.00 17.46 ? 391 PHE B N 1 ATOM 2669 C CA . PHE B 2 143 ? 42.037 60.134 41.269 1.00 17.83 ? 391 PHE B CA 1 ATOM 2670 C C . PHE B 2 143 ? 42.754 60.910 42.378 1.00 19.32 ? 391 PHE B C 1 ATOM 2671 O O . PHE B 2 143 ? 42.223 61.045 43.504 1.00 20.22 ? 391 PHE B O 1 ATOM 2672 C CB . PHE B 2 143 ? 40.697 60.850 40.929 1.00 17.22 ? 391 PHE B CB 1 ATOM 2673 C CG . PHE B 2 143 ? 40.898 62.320 40.590 1.00 15.46 ? 391 PHE B CG 1 ATOM 2674 C CD1 . PHE B 2 143 ? 41.600 62.685 39.439 1.00 16.12 ? 391 PHE B CD1 1 ATOM 2675 C CD2 . PHE B 2 143 ? 40.435 63.303 41.461 1.00 17.08 ? 391 PHE B CD2 1 ATOM 2676 C CE1 . PHE B 2 143 ? 41.831 64.049 39.163 1.00 16.78 ? 391 PHE B CE1 1 ATOM 2677 C CE2 . PHE B 2 143 ? 40.653 64.678 41.193 1.00 18.31 ? 391 PHE B CE2 1 ATOM 2678 C CZ . PHE B 2 143 ? 41.354 65.031 40.048 1.00 14.83 ? 391 PHE B CZ 1 ATOM 2679 N N . LEU B 2 144 ? 43.930 61.455 42.050 1.00 20.51 ? 392 LEU B N 1 ATOM 2680 C CA . LEU B 2 144 ? 44.626 62.356 42.978 1.00 22.15 ? 392 LEU B CA 1 ATOM 2681 C C . LEU B 2 144 ? 44.565 63.803 42.487 1.00 22.17 ? 392 LEU B C 1 ATOM 2682 O O . LEU B 2 144 ? 45.134 64.108 41.454 1.00 21.28 ? 392 LEU B O 1 ATOM 2683 C CB . LEU B 2 144 ? 46.085 61.920 43.100 1.00 23.34 ? 392 LEU B CB 1 ATOM 2684 C CG . LEU B 2 144 ? 46.903 62.692 44.144 1.00 26.52 ? 392 LEU B CG 1 ATOM 2685 C CD1 . LEU B 2 144 ? 46.385 62.489 45.542 1.00 28.52 ? 392 LEU B CD1 1 ATOM 2686 C CD2 . LEU B 2 144 ? 48.375 62.222 44.056 1.00 29.49 ? 392 LEU B CD2 1 ATOM 2687 N N . PRO B 2 145 ? 43.859 64.674 43.210 1.00 23.10 ? 393 PRO B N 1 ATOM 2688 C CA . PRO B 2 145 ? 43.816 66.080 42.764 1.00 24.02 ? 393 PRO B CA 1 ATOM 2689 C C . PRO B 2 145 ? 45.242 66.622 42.575 1.00 25.15 ? 393 PRO B C 1 ATOM 2690 O O . PRO B 2 145 ? 46.122 66.360 43.419 1.00 25.43 ? 393 PRO B O 1 ATOM 2691 C CB . PRO B 2 145 ? 43.086 66.779 43.898 1.00 24.10 ? 393 PRO B CB 1 ATOM 2692 C CG . PRO B 2 145 ? 42.158 65.674 44.458 1.00 24.39 ? 393 PRO B CG 1 ATOM 2693 C CD . PRO B 2 145 ? 43.052 64.450 44.425 1.00 23.71 ? 393 PRO B CD 1 ATOM 2694 N N . ASN B 2 146 ? 45.463 67.289 41.444 1.00 25.47 ? 394 ASN B N 1 ATOM 2695 C CA . ASN B 2 146 ? 46.742 67.907 41.084 1.00 26.85 ? 394 ASN B CA 1 ATOM 2696 C C . ASN B 2 146 ? 47.792 66.901 40.628 1.00 27.17 ? 394 ASN B C 1 ATOM 2697 O O . ASN B 2 146 ? 48.867 67.273 40.161 1.00 26.72 ? 394 ASN B O 1 ATOM 2698 C CB . ASN B 2 146 ? 47.270 68.760 42.247 1.00 26.67 ? 394 ASN B CB 1 ATOM 2699 C CG . ASN B 2 146 ? 46.215 69.696 42.810 1.00 30.87 ? 394 ASN B CG 1 ATOM 2700 O OD1 . ASN B 2 146 ? 45.392 70.257 42.080 1.00 29.88 ? 394 ASN B OD1 1 ATOM 2701 N ND2 . ASN B 2 146 ? 46.224 69.855 44.133 1.00 34.53 ? 394 ASN B ND2 1 ATOM 2702 N N . GLY B 2 147 ? 47.474 65.616 40.734 1.00 27.18 ? 395 GLY B N 1 ATOM 2703 C CA . GLY B 2 147 ? 48.440 64.593 40.378 1.00 27.71 ? 395 GLY B CA 1 ATOM 2704 C C . GLY B 2 147 ? 48.550 64.361 38.897 1.00 27.85 ? 395 GLY B C 1 ATOM 2705 O O . GLY B 2 147 ? 47.655 64.749 38.128 1.00 27.83 ? 395 GLY B O 1 ATOM 2706 N N . PRO B 2 148 ? 49.645 63.699 38.478 1.00 27.35 ? 396 PRO B N 1 ATOM 2707 C CA . PRO B 2 148 ? 49.832 63.332 37.084 1.00 27.10 ? 396 PRO B CA 1 ATOM 2708 C C . PRO B 2 148 ? 48.975 62.088 36.769 1.00 26.49 ? 396 PRO B C 1 ATOM 2709 O O . PRO B 2 148 ? 48.368 61.543 37.693 1.00 27.56 ? 396 PRO B O 1 ATOM 2710 C CB . PRO B 2 148 ? 51.329 62.965 37.020 1.00 27.19 ? 396 PRO B CB 1 ATOM 2711 C CG . PRO B 2 148 ? 51.612 62.423 38.377 1.00 27.56 ? 396 PRO B CG 1 ATOM 2712 C CD . PRO B 2 148 ? 50.745 63.221 39.346 1.00 27.81 ? 396 PRO B CD 1 ATOM 2713 N N . SER B 2 149 ? 48.912 61.668 35.506 1.00 25.38 ? 397 SER B N 1 ATOM 2714 C CA . SER B 2 149 ? 48.204 60.424 35.171 1.00 25.62 ? 397 SER B CA 1 ATOM 2715 C C . SER B 2 149 ? 48.752 59.254 35.976 1.00 25.59 ? 397 SER B C 1 ATOM 2716 O O . SER B 2 149 ? 49.970 59.084 36.038 1.00 24.08 ? 397 SER B O 1 ATOM 2717 C CB . SER B 2 149 ? 48.331 60.089 33.701 1.00 26.53 ? 397 SER B CB 1 ATOM 2718 O OG . SER B 2 149 ? 47.693 58.853 33.430 1.00 26.11 ? 397 SER B OG 1 ATOM 2719 N N . PRO B 2 150 ? 47.858 58.466 36.617 1.00 25.24 ? 398 PRO B N 1 ATOM 2720 C CA . PRO B 2 150 ? 48.285 57.233 37.272 1.00 25.26 ? 398 PRO B CA 1 ATOM 2721 C C . PRO B 2 150 ? 48.373 56.068 36.296 1.00 24.93 ? 398 PRO B C 1 ATOM 2722 O O . PRO B 2 150 ? 48.762 54.939 36.679 1.00 27.14 ? 398 PRO B O 1 ATOM 2723 C CB . PRO B 2 150 ? 47.206 57.015 38.351 1.00 25.51 ? 398 PRO B CB 1 ATOM 2724 C CG . PRO B 2 150 ? 46.000 57.724 37.864 1.00 25.76 ? 398 PRO B CG 1 ATOM 2725 C CD . PRO B 2 150 ? 46.416 58.728 36.805 1.00 24.84 ? 398 PRO B CD 1 ATOM 2726 N N . GLY B 2 151 ? 48.000 56.322 35.048 1.00 23.83 ? 399 GLY B N 1 ATOM 2727 C CA . GLY B 2 151 ? 48.144 55.350 33.990 1.00 23.96 ? 399 GLY B CA 1 ATOM 2728 C C . GLY B 2 151 ? 47.007 54.351 33.878 1.00 22.22 ? 399 GLY B C 1 ATOM 2729 O O . GLY B 2 151 ? 46.806 53.768 32.818 1.00 24.07 ? 399 GLY B O 1 ATOM 2730 N N . SER B 2 152 ? 46.282 54.136 34.973 1.00 21.07 ? 400 SER B N 1 ATOM 2731 C CA . SER B 2 152 ? 45.200 53.158 34.989 1.00 19.50 ? 400 SER B CA 1 ATOM 2732 C C . SER B 2 152 ? 44.193 53.486 36.088 1.00 17.81 ? 400 SER B C 1 ATOM 2733 O O . SER B 2 152 ? 44.417 54.385 36.948 1.00 16.77 ? 400 SER B O 1 ATOM 2734 C CB . SER B 2 152 ? 45.751 51.727 35.215 1.00 20.35 ? 400 SER B CB 1 ATOM 2735 O OG . SER B 2 152 ? 46.277 51.643 36.545 1.00 21.76 ? 400 SER B OG 1 ATOM 2736 N N . ARG B 2 153 ? 43.064 52.771 36.002 1.00 16.37 ? 401 ARG B N 1 ATOM 2737 C CA A ARG B 2 153 ? 42.069 52.694 37.079 0.50 16.40 ? 401 ARG B CA 1 ATOM 2738 C CA B ARG B 2 153 ? 42.037 52.678 37.036 0.50 16.27 ? 401 ARG B CA 1 ATOM 2739 C C . ARG B 2 153 ? 41.043 53.830 37.140 1.00 15.63 ? 401 ARG B C 1 ATOM 2740 O O . ARG B 2 153 ? 39.947 53.621 37.632 1.00 16.47 ? 401 ARG B O 1 ATOM 2741 C CB A ARG B 2 153 ? 42.718 52.551 38.472 0.50 16.50 ? 401 ARG B CB 1 ATOM 2742 C CB B ARG B 2 153 ? 42.620 52.384 38.425 0.50 16.29 ? 401 ARG B CB 1 ATOM 2743 C CG A ARG B 2 153 ? 43.555 51.290 38.674 0.50 19.53 ? 401 ARG B CG 1 ATOM 2744 C CG B ARG B 2 153 ? 43.325 51.042 38.519 0.50 18.90 ? 401 ARG B CG 1 ATOM 2745 C CD A ARG B 2 153 ? 44.278 51.316 40.035 0.50 21.88 ? 401 ARG B CD 1 ATOM 2746 C CD B ARG B 2 153 ? 43.550 50.687 39.987 0.50 20.52 ? 401 ARG B CD 1 ATOM 2747 N NE A ARG B 2 153 ? 43.439 51.686 41.183 0.50 26.92 ? 401 ARG B NE 1 ATOM 2748 N NE B ARG B 2 153 ? 44.382 49.494 40.108 0.50 26.84 ? 401 ARG B NE 1 ATOM 2749 C CZ A ARG B 2 153 ? 43.734 52.651 42.063 0.50 26.53 ? 401 ARG B CZ 1 ATOM 2750 C CZ B ARG B 2 153 ? 45.707 49.489 39.962 0.50 29.52 ? 401 ARG B CZ 1 ATOM 2751 N NH1 A ARG B 2 153 ? 42.910 52.912 43.087 0.50 24.40 ? 401 ARG B NH1 1 ATOM 2752 N NH1 B ARG B 2 153 ? 46.387 48.353 40.082 0.50 29.98 ? 401 ARG B NH1 1 ATOM 2753 N NH2 A ARG B 2 153 ? 44.853 53.368 41.921 0.50 27.46 ? 401 ARG B NH2 1 ATOM 2754 N NH2 B ARG B 2 153 ? 46.354 50.617 39.698 0.50 31.37 ? 401 ARG B NH2 1 ATOM 2755 N N . VAL B 2 154 ? 41.411 55.024 36.661 1.00 14.38 ? 402 VAL B N 1 ATOM 2756 C CA . VAL B 2 154 ? 40.499 56.181 36.858 1.00 13.72 ? 402 VAL B CA 1 ATOM 2757 C C . VAL B 2 154 ? 39.248 56.018 35.978 1.00 12.66 ? 402 VAL B C 1 ATOM 2758 O O . VAL B 2 154 ? 38.138 56.287 36.452 1.00 15.29 ? 402 VAL B O 1 ATOM 2759 C CB . VAL B 2 154 ? 41.196 57.523 36.514 1.00 13.92 ? 402 VAL B CB 1 ATOM 2760 C CG1 . VAL B 2 154 ? 40.204 58.703 36.604 1.00 15.24 ? 402 VAL B CG1 1 ATOM 2761 C CG2 . VAL B 2 154 ? 42.421 57.719 37.480 1.00 14.88 ? 402 VAL B CG2 1 ATOM 2762 N N . LEU B 2 155 ? 39.440 55.634 34.732 1.00 12.40 ? 403 LEU B N 1 ATOM 2763 C CA . LEU B 2 155 ? 38.308 55.538 33.782 1.00 12.44 ? 403 LEU B CA 1 ATOM 2764 C C . LEU B 2 155 ? 38.321 54.207 33.048 1.00 13.02 ? 403 LEU B C 1 ATOM 2765 O O . LEU B 2 155 ? 39.310 53.827 32.393 1.00 13.72 ? 403 LEU B O 1 ATOM 2766 C CB . LEU B 2 155 ? 38.358 56.690 32.765 1.00 12.55 ? 403 LEU B CB 1 ATOM 2767 C CG . LEU B 2 155 ? 37.236 56.728 31.671 1.00 12.88 ? 403 LEU B CG 1 ATOM 2768 C CD1 . LEU B 2 155 ? 35.876 56.816 32.350 1.00 14.38 ? 403 LEU B CD1 1 ATOM 2769 C CD2 . LEU B 2 155 ? 37.537 57.870 30.662 1.00 15.22 ? 403 LEU B CD2 1 ATOM 2770 N N . THR B 2 156 ? 37.189 53.506 33.139 1.00 12.67 ? 404 THR B N 1 ATOM 2771 C CA . THR B 2 156 ? 37.002 52.268 32.398 1.00 13.52 ? 404 THR B CA 1 ATOM 2772 C C . THR B 2 156 ? 35.807 52.506 31.459 1.00 13.34 ? 404 THR B C 1 ATOM 2773 O O . THR B 2 156 ? 34.775 53.079 31.887 1.00 13.78 ? 404 THR B O 1 ATOM 2774 C CB . THR B 2 156 ? 36.664 51.142 33.381 1.00 14.86 ? 404 THR B CB 1 ATOM 2775 O OG1 . THR B 2 156 ? 37.723 51.056 34.365 1.00 16.33 ? 404 THR B OG1 1 ATOM 2776 C CG2 . THR B 2 156 ? 36.556 49.765 32.672 1.00 16.25 ? 404 THR B CG2 1 ATOM 2777 N N . ILE B 2 157 ? 35.931 52.029 30.231 1.00 11.89 ? 405 ILE B N 1 ATOM 2778 C CA . ILE B 2 157 ? 34.835 52.199 29.250 1.00 13.14 ? 405 ILE B CA 1 ATOM 2779 C C . ILE B 2 157 ? 34.437 50.784 28.811 1.00 12.97 ? 405 ILE B C 1 ATOM 2780 O O . ILE B 2 157 ? 35.294 49.930 28.498 1.00 14.25 ? 405 ILE B O 1 ATOM 2781 C CB . ILE B 2 157 ? 35.304 52.972 28.032 1.00 13.48 ? 405 ILE B CB 1 ATOM 2782 C CG1 . ILE B 2 157 ? 35.791 54.385 28.433 1.00 15.38 ? 405 ILE B CG1 1 ATOM 2783 C CG2 . ILE B 2 157 ? 34.216 53.015 26.924 1.00 14.92 ? 405 ILE B CG2 1 ATOM 2784 C CD1 . ILE B 2 157 ? 34.696 55.287 28.971 1.00 17.12 ? 405 ILE B CD1 1 ATOM 2785 N N . LEU B 2 158 ? 33.144 50.549 28.811 1.00 12.02 ? 406 LEU B N 1 ATOM 2786 C CA . LEU B 2 158 ? 32.552 49.256 28.404 1.00 11.84 ? 406 LEU B CA 1 ATOM 2787 C C . LEU B 2 158 ? 31.464 49.534 27.370 1.00 13.20 ? 406 LEU B C 1 ATOM 2788 O O . LEU B 2 158 ? 30.654 50.471 27.546 1.00 12.85 ? 406 LEU B O 1 ATOM 2789 C CB . LEU B 2 158 ? 31.975 48.550 29.647 1.00 11.60 ? 406 LEU B CB 1 ATOM 2790 C CG . LEU B 2 158 ? 31.223 47.216 29.392 1.00 13.89 ? 406 LEU B CG 1 ATOM 2791 C CD1 . LEU B 2 158 ? 31.379 46.271 30.629 1.00 14.09 ? 406 LEU B CD1 1 ATOM 2792 C CD2 . LEU B 2 158 ? 29.701 47.401 28.997 1.00 12.48 ? 406 LEU B CD2 1 ATOM 2793 N N . GLU B 2 159 ? 31.466 48.787 26.264 1.00 11.59 ? 407 GLU B N 1 ATOM 2794 C CA . GLU B 2 159 ? 30.400 48.916 25.286 1.00 13.06 ? 407 GLU B CA 1 ATOM 2795 C C . GLU B 2 159 ? 29.765 47.543 25.061 1.00 13.48 ? 407 GLU B C 1 ATOM 2796 O O . GLU B 2 159 ? 30.476 46.537 24.928 1.00 14.78 ? 407 GLU B O 1 ATOM 2797 C CB . GLU B 2 159 ? 30.902 49.544 23.957 1.00 13.39 ? 407 GLU B CB 1 ATOM 2798 C CG . GLU B 2 159 ? 31.355 51.009 24.203 1.00 16.41 ? 407 GLU B CG 1 ATOM 2799 C CD . GLU B 2 159 ? 31.771 51.788 22.970 1.00 22.23 ? 407 GLU B CD 1 ATOM 2800 O OE1 . GLU B 2 159 ? 32.159 51.145 21.965 1.00 21.25 ? 407 GLU B OE1 1 ATOM 2801 O OE2 . GLU B 2 159 ? 31.750 53.062 23.054 1.00 22.73 ? 407 GLU B OE2 1 ATOM 2802 N N . GLN B 2 160 ? 28.439 47.524 25.040 1.00 12.22 ? 408 GLN B N 1 ATOM 2803 C CA . GLN B 2 160 ? 27.705 46.259 24.905 1.00 12.22 ? 408 GLN B CA 1 ATOM 2804 C C . GLN B 2 160 ? 26.829 46.331 23.640 1.00 12.80 ? 408 GLN B C 1 ATOM 2805 O O . GLN B 2 160 ? 26.075 47.287 23.475 1.00 13.05 ? 408 GLN B O 1 ATOM 2806 C CB . GLN B 2 160 ? 26.779 46.105 26.100 1.00 11.18 ? 408 GLN B CB 1 ATOM 2807 C CG . GLN B 2 160 ? 25.849 44.910 26.009 1.00 12.22 ? 408 GLN B CG 1 ATOM 2808 C CD . GLN B 2 160 ? 24.685 45.059 26.937 1.00 12.03 ? 408 GLN B CD 1 ATOM 2809 O OE1 . GLN B 2 160 ? 24.854 45.127 28.161 1.00 13.62 ? 408 GLN B OE1 1 ATOM 2810 N NE2 . GLN B 2 160 ? 23.481 45.148 26.361 1.00 13.91 ? 408 GLN B NE2 1 ATOM 2811 N N . ILE B 2 161 ? 26.890 45.292 22.792 1.00 12.74 ? 409 ILE B N 1 ATOM 2812 C CA . ILE B 2 161 ? 25.844 45.040 21.808 1.00 13.78 ? 409 ILE B CA 1 ATOM 2813 C C . ILE B 2 161 ? 25.502 43.521 21.920 1.00 13.88 ? 409 ILE B C 1 ATOM 2814 O O . ILE B 2 161 ? 26.161 42.807 22.662 1.00 14.23 ? 409 ILE B O 1 ATOM 2815 C CB . ILE B 2 161 ? 26.345 45.409 20.383 1.00 14.14 ? 409 ILE B CB 1 ATOM 2816 C CG1 . ILE B 2 161 ? 27.635 44.634 20.033 1.00 15.63 ? 409 ILE B CG1 1 ATOM 2817 C CG2 . ILE B 2 161 ? 26.512 46.985 20.243 1.00 15.14 ? 409 ILE B CG2 1 ATOM 2818 C CD1 . ILE B 2 161 ? 28.082 44.920 18.571 1.00 18.21 ? 409 ILE B CD1 1 ATOM 2819 N N . PRO B 2 162 ? 24.482 43.033 21.202 1.00 15.07 ? 410 PRO B N 1 ATOM 2820 C CA . PRO B 2 162 ? 24.181 41.593 21.378 1.00 16.10 ? 410 PRO B CA 1 ATOM 2821 C C . PRO B 2 162 ? 25.388 40.742 20.963 1.00 16.19 ? 410 PRO B C 1 ATOM 2822 O O . PRO B 2 162 ? 25.982 40.993 19.906 1.00 17.00 ? 410 PRO B O 1 ATOM 2823 C CB . PRO B 2 162 ? 22.947 41.353 20.465 1.00 15.78 ? 410 PRO B CB 1 ATOM 2824 C CG . PRO B 2 162 ? 22.304 42.758 20.330 1.00 14.36 ? 410 PRO B CG 1 ATOM 2825 C CD . PRO B 2 162 ? 23.528 43.709 20.291 1.00 15.58 ? 410 PRO B CD 1 ATOM 2826 N N . GLY B 2 163 ? 25.764 39.793 21.815 1.00 17.41 ? 411 GLY B N 1 ATOM 2827 C CA . GLY B 2 163 ? 26.881 38.908 21.517 1.00 18.50 ? 411 GLY B CA 1 ATOM 2828 C C . GLY B 2 163 ? 28.289 39.456 21.708 1.00 18.03 ? 411 GLY B C 1 ATOM 2829 O O . GLY B 2 163 ? 29.264 38.731 21.504 1.00 18.38 ? 411 GLY B O 1 ATOM 2830 N N . MET B 2 164 ? 28.448 40.725 22.108 1.00 16.98 ? 412 MET B N 1 ATOM 2831 C CA . MET B 2 164 ? 29.800 41.290 22.181 1.00 17.71 ? 412 MET B CA 1 ATOM 2832 C C . MET B 2 164 ? 29.858 42.379 23.247 1.00 17.13 ? 412 MET B C 1 ATOM 2833 O O . MET B 2 164 ? 28.986 43.243 23.288 1.00 17.44 ? 412 MET B O 1 ATOM 2834 C CB . MET B 2 164 ? 30.217 41.860 20.798 1.00 18.00 ? 412 MET B CB 1 ATOM 2835 C CG . MET B 2 164 ? 31.573 42.592 20.760 1.00 23.68 ? 412 MET B CG 1 ATOM 2836 S SD . MET B 2 164 ? 31.802 43.453 19.176 1.00 30.12 ? 412 MET B SD 1 ATOM 2837 C CE . MET B 2 164 ? 31.469 42.113 18.055 1.00 29.27 ? 412 MET B CE 1 ATOM 2838 N N . VAL B 2 165 ? 30.863 42.312 24.123 1.00 15.78 ? 413 VAL B N 1 ATOM 2839 C CA . VAL B 2 165 ? 31.099 43.379 25.088 1.00 14.47 ? 413 VAL B CA 1 ATOM 2840 C C . VAL B 2 165 ? 32.593 43.656 25.000 1.00 16.61 ? 413 VAL B C 1 ATOM 2841 O O . VAL B 2 165 ? 33.420 42.717 25.027 1.00 15.63 ? 413 VAL B O 1 ATOM 2842 C CB . VAL B 2 165 ? 30.735 42.958 26.540 1.00 15.21 ? 413 VAL B CB 1 ATOM 2843 C CG1 . VAL B 2 165 ? 31.218 44.030 27.551 1.00 16.32 ? 413 VAL B CG1 1 ATOM 2844 C CG2 . VAL B 2 165 ? 29.180 42.675 26.697 1.00 14.32 ? 413 VAL B CG2 1 ATOM 2845 N N . VAL B 2 166 ? 32.947 44.926 24.883 1.00 14.23 ? 414 VAL B N 1 ATOM 2846 C CA . VAL B 2 166 ? 34.349 45.321 24.806 1.00 15.00 ? 414 VAL B CA 1 ATOM 2847 C C . VAL B 2 166 ? 34.622 46.267 25.952 1.00 15.24 ? 414 VAL B C 1 ATOM 2848 O O . VAL B 2 166 ? 33.772 47.127 26.279 1.00 14.22 ? 414 VAL B O 1 ATOM 2849 C CB . VAL B 2 166 ? 34.647 46.006 23.450 1.00 15.57 ? 414 VAL B CB 1 ATOM 2850 C CG1 . VAL B 2 166 ? 36.095 46.507 23.383 1.00 14.32 ? 414 VAL B CG1 1 ATOM 2851 C CG2 . VAL B 2 166 ? 34.337 45.034 22.278 1.00 16.91 ? 414 VAL B CG2 1 ATOM 2852 N N . VAL B 2 167 ? 35.774 46.063 26.600 1.00 13.91 ? 415 VAL B N 1 ATOM 2853 C CA . VAL B 2 167 ? 36.110 46.828 27.803 1.00 14.44 ? 415 VAL B CA 1 ATOM 2854 C C . VAL B 2 167 ? 37.537 47.329 27.664 1.00 14.97 ? 415 VAL B C 1 ATOM 2855 O O . VAL B 2 167 ? 38.417 46.570 27.211 1.00 15.07 ? 415 VAL B O 1 ATOM 2856 C CB . VAL B 2 167 ? 36.040 45.927 29.079 1.00 15.20 ? 415 VAL B CB 1 ATOM 2857 C CG1 . VAL B 2 167 ? 36.260 46.786 30.349 1.00 17.62 ? 415 VAL B CG1 1 ATOM 2858 C CG2 . VAL B 2 167 ? 34.721 45.179 29.196 1.00 16.80 ? 415 VAL B CG2 1 ATOM 2859 N N . ALA B 2 168 ? 37.809 48.567 28.086 1.00 13.53 ? 416 ALA B N 1 ATOM 2860 C CA . ALA B 2 168 ? 39.186 49.046 28.097 1.00 13.36 ? 416 ALA B CA 1 ATOM 2861 C C . ALA B 2 168 ? 39.365 50.083 29.185 1.00 14.74 ? 416 ALA B C 1 ATOM 2862 O O . ALA B 2 168 ? 38.428 50.819 29.485 1.00 15.14 ? 416 ALA B O 1 ATOM 2863 C CB . ALA B 2 168 ? 39.536 49.641 26.759 1.00 15.02 ? 416 ALA B CB 1 ATOM 2864 N N . ASP B 2 169 ? 40.560 50.128 29.775 1.00 13.89 ? 417 ASP B N 1 ATOM 2865 C CA . ASP B 2 169 ? 40.892 51.201 30.718 1.00 15.39 ? 417 ASP B CA 1 ATOM 2866 C C . ASP B 2 169 ? 41.317 52.388 29.835 1.00 16.15 ? 417 ASP B C 1 ATOM 2867 O O . ASP B 2 169 ? 42.255 52.278 29.021 1.00 17.07 ? 417 ASP B O 1 ATOM 2868 C CB . ASP B 2 169 ? 42.059 50.754 31.617 1.00 15.48 ? 417 ASP B CB 1 ATOM 2869 C CG . ASP B 2 169 ? 42.314 51.724 32.761 1.00 18.91 ? 417 ASP B CG 1 ATOM 2870 O OD1 . ASP B 2 169 ? 42.570 52.887 32.459 1.00 15.67 ? 417 ASP B OD1 1 ATOM 2871 O OD2 . ASP B 2 169 ? 42.249 51.337 33.949 1.00 22.82 ? 417 ASP B OD2 1 ATOM 2872 N N . LYS B 2 170 ? 40.651 53.515 30.000 1.00 15.58 ? 418 LYS B N 1 ATOM 2873 C CA . LYS B 2 170 ? 40.910 54.698 29.163 1.00 15.72 ? 418 LYS B CA 1 ATOM 2874 C C . LYS B 2 170 ? 41.514 55.843 29.968 1.00 14.94 ? 418 LYS B C 1 ATOM 2875 O O . LYS B 2 170 ? 41.420 57.004 29.580 1.00 15.70 ? 418 LYS B O 1 ATOM 2876 C CB . LYS B 2 170 ? 39.635 55.110 28.395 1.00 15.70 ? 418 LYS B CB 1 ATOM 2877 C CG . LYS B 2 170 ? 39.255 54.085 27.333 1.00 16.96 ? 418 LYS B CG 1 ATOM 2878 C CD . LYS B 2 170 ? 40.355 54.176 26.199 1.00 20.43 ? 418 LYS B CD 1 ATOM 2879 C CE . LYS B 2 170 ? 40.413 52.998 25.349 1.00 26.54 ? 418 LYS B CE 1 ATOM 2880 N NZ . LYS B 2 170 ? 41.526 53.292 24.316 1.00 24.81 ? 418 LYS B NZ 1 ATOM 2881 N N . THR B 2 171 ? 42.147 55.517 31.097 1.00 14.81 ? 419 THR B N 1 ATOM 2882 C CA . THR B 2 171 ? 42.737 56.550 31.960 1.00 14.82 ? 419 THR B CA 1 ATOM 2883 C C . THR B 2 171 ? 43.780 57.354 31.164 1.00 16.12 ? 419 THR B C 1 ATOM 2884 O O . THR B 2 171 ? 43.830 58.582 31.279 1.00 15.08 ? 419 THR B O 1 ATOM 2885 C CB . THR B 2 171 ? 43.416 55.923 33.208 1.00 16.29 ? 419 THR B CB 1 ATOM 2886 O OG1 . THR B 2 171 ? 42.424 55.214 33.980 1.00 14.81 ? 419 THR B OG1 1 ATOM 2887 C CG2 . THR B 2 171 ? 44.062 57.007 34.113 1.00 14.75 ? 419 THR B CG2 1 ATOM 2888 N N . ALA B 2 172 ? 44.643 56.676 30.411 1.00 15.46 ? 420 ALA B N 1 ATOM 2889 C CA . ALA B 2 172 ? 45.717 57.412 29.714 1.00 17.75 ? 420 ALA B CA 1 ATOM 2890 C C . ALA B 2 172 ? 45.112 58.401 28.706 1.00 17.55 ? 420 ALA B C 1 ATOM 2891 O O . ALA B 2 172 ? 45.572 59.564 28.596 1.00 17.26 ? 420 ALA B O 1 ATOM 2892 C CB . ALA B 2 172 ? 46.677 56.451 29.021 1.00 19.28 ? 420 ALA B CB 1 ATOM 2893 N N . GLU B 2 173 ? 44.067 57.952 28.002 1.00 17.69 ? 421 GLU B N 1 ATOM 2894 C CA . GLU B 2 173 ? 43.412 58.769 27.008 1.00 18.47 ? 421 GLU B CA 1 ATOM 2895 C C . GLU B 2 173 ? 42.723 59.972 27.672 1.00 17.49 ? 421 GLU B C 1 ATOM 2896 O O . GLU B 2 173 ? 42.739 61.092 27.124 1.00 17.34 ? 421 GLU B O 1 ATOM 2897 C CB . GLU B 2 173 ? 42.405 57.932 26.217 1.00 20.30 ? 421 GLU B CB 1 ATOM 2898 C CG . GLU B 2 173 ? 41.571 58.722 25.178 1.00 26.37 ? 421 GLU B CG 1 ATOM 2899 C CD . GLU B 2 173 ? 42.334 58.994 23.878 1.00 36.51 ? 421 GLU B CD 1 ATOM 2900 O OE1 . GLU B 2 173 ? 43.590 58.839 23.850 1.00 39.52 ? 421 GLU B OE1 1 ATOM 2901 O OE2 . GLU B 2 173 ? 41.669 59.387 22.876 1.00 42.00 ? 421 GLU B OE2 1 ATOM 2902 N N . LEU B 2 174 ? 42.111 59.746 28.830 1.00 16.10 ? 422 LEU B N 1 ATOM 2903 C CA . LEU B 2 174 ? 41.483 60.857 29.555 1.00 15.00 ? 422 LEU B CA 1 ATOM 2904 C C . LEU B 2 174 ? 42.529 61.883 29.949 1.00 15.93 ? 422 LEU B C 1 ATOM 2905 O O . LEU B 2 174 ? 42.312 63.095 29.834 1.00 15.64 ? 422 LEU B O 1 ATOM 2906 C CB . LEU B 2 174 ? 40.806 60.354 30.812 1.00 14.59 ? 422 LEU B CB 1 ATOM 2907 C CG . LEU B 2 174 ? 40.260 61.403 31.784 1.00 13.61 ? 422 LEU B CG 1 ATOM 2908 C CD1 . LEU B 2 174 ? 39.132 62.275 31.152 1.00 15.48 ? 422 LEU B CD1 1 ATOM 2909 C CD2 . LEU B 2 174 ? 39.705 60.688 33.074 1.00 15.24 ? 422 LEU B CD2 1 ATOM 2910 N N . TYR B 2 175 ? 43.656 61.413 30.460 1.00 15.24 ? 423 TYR B N 1 ATOM 2911 C CA . TYR B 2 175 ? 44.685 62.365 30.855 1.00 16.45 ? 423 TYR B CA 1 ATOM 2912 C C . TYR B 2 175 ? 45.352 63.056 29.668 1.00 16.42 ? 423 TYR B C 1 ATOM 2913 O O . TYR B 2 175 ? 45.762 64.211 29.789 1.00 18.55 ? 423 TYR B O 1 ATOM 2914 C CB . TYR B 2 175 ? 45.725 61.713 31.762 1.00 15.51 ? 423 TYR B CB 1 ATOM 2915 C CG . TYR B 2 175 ? 45.311 61.743 33.211 1.00 14.90 ? 423 TYR B CG 1 ATOM 2916 C CD1 . TYR B 2 175 ? 45.770 62.739 34.077 1.00 18.02 ? 423 TYR B CD1 1 ATOM 2917 C CD2 . TYR B 2 175 ? 44.402 60.798 33.714 1.00 14.37 ? 423 TYR B CD2 1 ATOM 2918 C CE1 . TYR B 2 175 ? 45.373 62.777 35.432 1.00 18.42 ? 423 TYR B CE1 1 ATOM 2919 C CE2 . TYR B 2 175 ? 44.013 60.823 35.045 1.00 16.22 ? 423 TYR B CE2 1 ATOM 2920 C CZ . TYR B 2 175 ? 44.490 61.817 35.896 1.00 18.56 ? 423 TYR B CZ 1 ATOM 2921 O OH . TYR B 2 175 ? 44.076 61.841 37.214 1.00 21.72 ? 423 TYR B OH 1 ATOM 2922 N N . LYS B 2 176 ? 45.423 62.377 28.541 1.00 16.74 ? 424 LYS B N 1 ATOM 2923 C CA . LYS B 2 176 ? 46.046 62.960 27.364 1.00 17.85 ? 424 LYS B CA 1 ATOM 2924 C C . LYS B 2 176 ? 45.155 64.061 26.767 1.00 18.40 ? 424 LYS B C 1 ATOM 2925 O O . LYS B 2 176 ? 45.653 65.141 26.417 1.00 18.57 ? 424 LYS B O 1 ATOM 2926 C CB . LYS B 2 176 ? 46.243 61.875 26.313 1.00 18.98 ? 424 LYS B CB 1 ATOM 2927 C CG . LYS B 2 176 ? 46.985 62.398 25.074 1.00 22.51 ? 424 LYS B CG 1 ATOM 2928 C CD . LYS B 2 176 ? 47.210 61.235 24.143 1.00 29.36 ? 424 LYS B CD 1 ATOM 2929 C CE . LYS B 2 176 ? 47.652 61.727 22.771 1.00 34.37 ? 424 LYS B CE 1 ATOM 2930 N NZ . LYS B 2 176 ? 47.733 60.552 21.839 1.00 38.09 ? 424 LYS B NZ 1 ATOM 2931 N N . THR B 2 177 ? 43.854 63.787 26.617 1.00 15.83 ? 425 THR B N 1 ATOM 2932 C CA . THR B 2 177 ? 42.964 64.764 25.912 1.00 16.01 ? 425 THR B CA 1 ATOM 2933 C C . THR B 2 177 ? 42.305 65.723 26.913 1.00 15.66 ? 425 THR B C 1 ATOM 2934 O O . THR B 2 177 ? 41.813 66.767 26.530 1.00 15.67 ? 425 THR B O 1 ATOM 2935 C CB . THR B 2 177 ? 41.853 64.033 25.137 1.00 16.67 ? 425 THR B CB 1 ATOM 2936 O OG1 . THR B 2 177 ? 40.977 63.414 26.091 1.00 16.20 ? 425 THR B OG1 1 ATOM 2937 C CG2 . THR B 2 177 ? 42.473 62.969 24.220 1.00 17.01 ? 425 THR B CG2 1 ATOM 2938 N N . THR B 2 178 ? 42.295 65.302 28.187 1.00 14.04 ? 426 THR B N 1 ATOM 2939 C CA . THR B 2 178 ? 41.679 65.967 29.351 1.00 13.60 ? 426 THR B CA 1 ATOM 2940 C C . THR B 2 178 ? 40.141 65.799 29.430 1.00 12.73 ? 426 THR B C 1 ATOM 2941 O O . THR B 2 178 ? 39.526 66.384 30.301 1.00 12.52 ? 426 THR B O 1 ATOM 2942 C CB . THR B 2 178 ? 42.032 67.504 29.527 1.00 14.95 ? 426 THR B CB 1 ATOM 2943 O OG1 . THR B 2 178 ? 41.324 68.302 28.557 1.00 15.36 ? 426 THR B OG1 1 ATOM 2944 C CG2 . THR B 2 178 ? 43.541 67.756 29.436 1.00 14.95 ? 426 THR B CG2 1 ATOM 2945 N N . TYR B 2 179 ? 39.549 64.996 28.541 1.00 12.00 ? 427 TYR B N 1 ATOM 2946 C CA . TYR B 2 179 ? 38.108 64.724 28.684 1.00 11.20 ? 427 TYR B CA 1 ATOM 2947 C C . TYR B 2 179 ? 37.710 63.418 28.044 1.00 12.50 ? 427 TYR B C 1 ATOM 2948 O O . TYR B 2 179 ? 38.449 62.866 27.191 1.00 12.20 ? 427 TYR B O 1 ATOM 2949 C CB . TYR B 2 179 ? 37.279 65.875 28.051 1.00 11.91 ? 427 TYR B CB 1 ATOM 2950 C CG . TYR B 2 179 ? 37.222 65.894 26.532 1.00 12.75 ? 427 TYR B CG 1 ATOM 2951 C CD1 . TYR B 2 179 ? 38.277 66.402 25.766 1.00 14.83 ? 427 TYR B CD1 1 ATOM 2952 C CD2 . TYR B 2 179 ? 36.076 65.441 25.860 1.00 14.03 ? 427 TYR B CD2 1 ATOM 2953 C CE1 . TYR B 2 179 ? 38.190 66.453 24.358 1.00 15.29 ? 427 TYR B CE1 1 ATOM 2954 C CE2 . TYR B 2 179 ? 35.968 65.483 24.461 1.00 17.11 ? 427 TYR B CE2 1 ATOM 2955 C CZ . TYR B 2 179 ? 37.025 65.997 23.721 1.00 14.79 ? 427 TYR B CZ 1 ATOM 2956 O OH . TYR B 2 179 ? 36.903 66.047 22.330 1.00 16.73 ? 427 TYR B OH 1 ATOM 2957 N N . TRP B 2 180 ? 36.506 62.959 28.411 1.00 11.74 ? 428 TRP B N 1 ATOM 2958 C CA . TRP B 2 180 ? 35.889 61.818 27.729 1.00 12.75 ? 428 TRP B CA 1 ATOM 2959 C C . TRP B 2 180 ? 34.439 62.231 27.522 1.00 12.13 ? 428 TRP B C 1 ATOM 2960 O O . TRP B 2 180 ? 33.746 62.473 28.512 1.00 13.24 ? 428 TRP B O 1 ATOM 2961 C CB . TRP B 2 180 ? 35.917 60.549 28.607 1.00 13.23 ? 428 TRP B CB 1 ATOM 2962 C CG . TRP B 2 180 ? 35.294 59.396 27.835 1.00 14.61 ? 428 TRP B CG 1 ATOM 2963 C CD1 . TRP B 2 180 ? 33.957 59.074 27.746 1.00 15.80 ? 428 TRP B CD1 1 ATOM 2964 C CD2 . TRP B 2 180 ? 35.982 58.503 26.963 1.00 14.55 ? 428 TRP B CD2 1 ATOM 2965 N NE1 . TRP B 2 180 ? 33.777 58.015 26.862 1.00 14.91 ? 428 TRP B NE1 1 ATOM 2966 C CE2 . TRP B 2 180 ? 35.009 57.651 26.374 1.00 15.35 ? 428 TRP B CE2 1 ATOM 2967 C CE3 . TRP B 2 180 ? 37.330 58.345 26.608 1.00 15.55 ? 428 TRP B CE3 1 ATOM 2968 C CZ2 . TRP B 2 180 ? 35.351 56.622 25.473 1.00 17.49 ? 428 TRP B CZ2 1 ATOM 2969 C CZ3 . TRP B 2 180 ? 37.666 57.300 25.698 1.00 17.33 ? 428 TRP B CZ3 1 ATOM 2970 C CH2 . TRP B 2 180 ? 36.679 56.475 25.144 1.00 16.60 ? 428 TRP B CH2 1 ATOM 2971 N N . ALA B 2 181 ? 34.007 62.325 26.275 1.00 11.63 ? 429 ALA B N 1 ATOM 2972 C CA . ALA B 2 181 ? 32.594 62.689 25.992 1.00 12.89 ? 429 ALA B CA 1 ATOM 2973 C C . ALA B 2 181 ? 31.871 61.456 25.458 1.00 12.83 ? 429 ALA B C 1 ATOM 2974 O O . ALA B 2 181 ? 32.487 60.586 24.812 1.00 13.78 ? 429 ALA B O 1 ATOM 2975 C CB . ALA B 2 181 ? 32.538 63.800 24.931 1.00 14.21 ? 429 ALA B CB 1 ATOM 2976 N N . SER B 2 182 ? 30.573 61.392 25.717 1.00 13.60 ? 430 SER B N 1 ATOM 2977 C CA . SER B 2 182 ? 29.766 60.281 25.240 1.00 12.66 ? 430 SER B CA 1 ATOM 2978 C C . SER B 2 182 ? 28.454 60.857 24.686 1.00 13.07 ? 430 SER B C 1 ATOM 2979 O O . SER B 2 182 ? 27.908 61.834 25.226 1.00 12.27 ? 430 SER B O 1 ATOM 2980 C CB . SER B 2 182 ? 29.495 59.281 26.392 1.00 14.31 ? 430 SER B CB 1 ATOM 2981 O OG . SER B 2 182 ? 28.884 58.097 25.884 1.00 16.07 ? 430 SER B OG 1 ATOM 2982 N N . TYR B 2 183 ? 27.969 60.262 23.601 1.00 12.39 ? 431 TYR B N 1 ATOM 2983 C CA . TYR B 2 183 ? 26.857 60.882 22.850 1.00 12.64 ? 431 TYR B CA 1 ATOM 2984 C C . TYR B 2 183 ? 26.206 59.821 21.927 1.00 12.92 ? 431 TYR B C 1 ATOM 2985 O O . TYR B 2 183 ? 25.944 60.079 20.756 1.00 13.07 ? 431 TYR B O 1 ATOM 2986 C CB . TYR B 2 183 ? 27.368 62.084 22.050 1.00 12.63 ? 431 TYR B CB 1 ATOM 2987 C CG . TYR B 2 183 ? 28.742 61.885 21.474 1.00 12.32 ? 431 TYR B CG 1 ATOM 2988 C CD1 . TYR B 2 183 ? 29.861 62.469 22.088 1.00 15.25 ? 431 TYR B CD1 1 ATOM 2989 C CD2 . TYR B 2 183 ? 28.948 61.131 20.335 1.00 14.94 ? 431 TYR B CD2 1 ATOM 2990 C CE1 . TYR B 2 183 ? 31.146 62.298 21.575 1.00 17.13 ? 431 TYR B CE1 1 ATOM 2991 C CE2 . TYR B 2 183 ? 30.258 60.924 19.832 1.00 14.14 ? 431 TYR B CE2 1 ATOM 2992 C CZ . TYR B 2 183 ? 31.339 61.505 20.461 1.00 15.19 ? 431 TYR B CZ 1 ATOM 2993 O OH . TYR B 2 183 ? 32.597 61.315 19.919 1.00 14.40 ? 431 TYR B OH 1 ATOM 2994 N N . ASN B 2 184 ? 25.913 58.650 22.496 1.00 12.65 ? 432 ASN B N 1 ATOM 2995 C CA . ASN B 2 184 ? 25.111 57.616 21.809 1.00 12.77 ? 432 ASN B CA 1 ATOM 2996 C C . ASN B 2 184 ? 25.754 56.935 20.589 1.00 13.98 ? 432 ASN B C 1 ATOM 2997 O O . ASN B 2 184 ? 25.055 56.305 19.786 1.00 15.73 ? 432 ASN B O 1 ATOM 2998 C CB . ASN B 2 184 ? 23.715 58.157 21.390 1.00 13.07 ? 432 ASN B CB 1 ATOM 2999 C CG . ASN B 2 184 ? 22.955 58.765 22.521 1.00 15.34 ? 432 ASN B CG 1 ATOM 3000 O OD1 . ASN B 2 184 ? 22.591 59.948 22.467 1.00 18.55 ? 432 ASN B OD1 1 ATOM 3001 N ND2 . ASN B 2 184 ? 22.700 57.995 23.565 1.00 15.40 ? 432 ASN B ND2 1 ATOM 3002 N N . ILE B 2 185 ? 27.063 57.039 20.446 1.00 13.39 ? 433 ILE B N 1 ATOM 3003 C CA . ILE B 2 185 ? 27.768 56.367 19.351 1.00 14.36 ? 433 ILE B CA 1 ATOM 3004 C C . ILE B 2 185 ? 28.952 55.607 19.944 1.00 14.04 ? 433 ILE B C 1 ATOM 3005 O O . ILE B 2 185 ? 29.725 56.174 20.770 1.00 14.34 ? 433 ILE B O 1 ATOM 3006 C CB . ILE B 2 185 ? 28.271 57.369 18.292 1.00 15.22 ? 433 ILE B CB 1 ATOM 3007 C CG1 . ILE B 2 185 ? 27.078 58.077 17.638 1.00 18.99 ? 433 ILE B CG1 1 ATOM 3008 C CG2 . ILE B 2 185 ? 29.125 56.650 17.230 1.00 13.29 ? 433 ILE B CG2 1 ATOM 3009 C CD1 . ILE B 2 185 ? 27.488 59.235 16.799 1.00 25.04 ? 433 ILE B CD1 1 ATOM 3010 N N . PRO B 2 186 ? 29.112 54.321 19.571 1.00 14.41 ? 434 PRO B N 1 ATOM 3011 C CA . PRO B 2 186 ? 30.206 53.565 20.214 1.00 15.13 ? 434 PRO B CA 1 ATOM 3012 C C . PRO B 2 186 ? 31.579 54.049 19.804 1.00 15.55 ? 434 PRO B C 1 ATOM 3013 O O . PRO B 2 186 ? 31.798 54.403 18.641 1.00 15.46 ? 434 PRO B O 1 ATOM 3014 C CB . PRO B 2 186 ? 29.998 52.108 19.739 1.00 15.68 ? 434 PRO B CB 1 ATOM 3015 C CG . PRO B 2 186 ? 29.144 52.227 18.509 1.00 16.33 ? 434 PRO B CG 1 ATOM 3016 C CD . PRO B 2 186 ? 28.293 53.475 18.668 1.00 14.53 ? 434 PRO B CD 1 ATOM 3017 N N . TYR B 2 187 ? 32.465 54.103 20.795 1.00 14.57 ? 435 TYR B N 1 ATOM 3018 C CA . TYR B 2 187 ? 33.885 54.468 20.605 1.00 15.21 ? 435 TYR B CA 1 ATOM 3019 C C . TYR B 2 187 ? 34.689 53.329 20.006 1.00 16.27 ? 435 TYR B C 1 ATOM 3020 O O . TYR B 2 187 ? 35.568 53.566 19.165 1.00 16.65 ? 435 TYR B O 1 ATOM 3021 C CB . TYR B 2 187 ? 34.462 54.838 21.964 1.00 16.64 ? 435 TYR B CB 1 ATOM 3022 C CG . TYR B 2 187 ? 35.955 54.866 22.032 1.00 17.27 ? 435 TYR B CG 1 ATOM 3023 C CD1 . TYR B 2 187 ? 36.661 53.767 22.525 1.00 17.68 ? 435 TYR B CD1 1 ATOM 3024 C CD2 . TYR B 2 187 ? 36.663 55.985 21.612 1.00 18.90 ? 435 TYR B CD2 1 ATOM 3025 C CE1 . TYR B 2 187 ? 38.067 53.782 22.602 1.00 19.43 ? 435 TYR B CE1 1 ATOM 3026 C CE2 . TYR B 2 187 ? 38.084 56.025 21.680 1.00 20.24 ? 435 TYR B CE2 1 ATOM 3027 C CZ . TYR B 2 187 ? 38.762 54.919 22.177 1.00 20.51 ? 435 TYR B CZ 1 ATOM 3028 O OH . TYR B 2 187 ? 40.142 54.951 22.260 1.00 23.24 ? 435 TYR B OH 1 ATOM 3029 N N . PHE B 2 188 ? 34.436 52.100 20.442 1.00 16.28 ? 436 PHE B N 1 ATOM 3030 C CA . PHE B 2 188 ? 35.259 50.978 19.948 1.00 15.83 ? 436 PHE B CA 1 ATOM 3031 C C . PHE B 2 188 ? 34.920 50.658 18.508 1.00 16.83 ? 436 PHE B C 1 ATOM 3032 O O . PHE B 2 188 ? 33.776 50.412 18.178 1.00 15.56 ? 436 PHE B O 1 ATOM 3033 C CB . PHE B 2 188 ? 35.066 49.731 20.818 1.00 16.62 ? 436 PHE B CB 1 ATOM 3034 C CG . PHE B 2 188 ? 35.538 49.904 22.250 1.00 15.16 ? 436 PHE B CG 1 ATOM 3035 C CD1 . PHE B 2 188 ? 34.624 49.834 23.303 1.00 16.66 ? 436 PHE B CD1 1 ATOM 3036 C CD2 . PHE B 2 188 ? 36.892 50.152 22.534 1.00 15.20 ? 436 PHE B CD2 1 ATOM 3037 C CE1 . PHE B 2 188 ? 35.059 49.954 24.636 1.00 16.30 ? 436 PHE B CE1 1 ATOM 3038 C CE2 . PHE B 2 188 ? 37.347 50.309 23.883 1.00 16.30 ? 436 PHE B CE2 1 ATOM 3039 C CZ . PHE B 2 188 ? 36.405 50.225 24.932 1.00 18.58 ? 436 PHE B CZ 1 ATOM 3040 N N . GLU B 2 189 ? 35.935 50.669 17.642 1.00 17.92 ? 437 GLU B N 1 ATOM 3041 C CA . GLU B 2 189 ? 35.695 50.411 16.216 1.00 19.05 ? 437 GLU B CA 1 ATOM 3042 C C . GLU B 2 189 ? 35.058 49.051 15.936 1.00 18.50 ? 437 GLU B C 1 ATOM 3043 O O . GLU B 2 189 ? 34.200 48.950 15.057 1.00 17.26 ? 437 GLU B O 1 ATOM 3044 C CB . GLU B 2 189 ? 36.993 50.585 15.423 1.00 20.22 ? 437 GLU B CB 1 ATOM 3045 C CG . GLU B 2 189 ? 37.399 52.037 15.377 1.00 25.56 ? 437 GLU B CG 1 ATOM 3046 C CD . GLU B 2 189 ? 38.584 52.289 14.482 1.00 35.72 ? 437 GLU B CD 1 ATOM 3047 O OE1 . GLU B 2 189 ? 38.832 53.479 14.172 1.00 39.23 ? 437 GLU B OE1 1 ATOM 3048 O OE2 . GLU B 2 189 ? 39.256 51.300 14.086 1.00 40.41 ? 437 GLU B OE2 1 ATOM 3049 N N . THR B 2 190 ? 35.436 48.005 16.678 1.00 17.30 ? 438 THR B N 1 ATOM 3050 C CA . THR B 2 190 ? 34.809 46.717 16.459 1.00 18.36 ? 438 THR B CA 1 ATOM 3051 C C . THR B 2 190 ? 33.314 46.744 16.734 1.00 18.21 ? 438 THR B C 1 ATOM 3052 O O . THR B 2 190 ? 32.562 46.076 16.050 1.00 18.45 ? 438 THR B O 1 ATOM 3053 C CB . THR B 2 190 ? 35.452 45.578 17.274 1.00 20.38 ? 438 THR B CB 1 ATOM 3054 O OG1 . THR B 2 190 ? 35.481 45.937 18.663 1.00 20.96 ? 438 THR B OG1 1 ATOM 3055 C CG2 . THR B 2 190 ? 36.878 45.339 16.771 1.00 21.51 ? 438 THR B CG2 1 ATOM 3056 N N . VAL B 2 191 ? 32.908 47.522 17.740 1.00 16.90 ? 439 VAL B N 1 ATOM 3057 C CA . VAL B 2 191 ? 31.485 47.629 18.123 1.00 15.23 ? 439 VAL B CA 1 ATOM 3058 C C . VAL B 2 191 ? 30.734 48.503 17.110 1.00 15.24 ? 439 VAL B C 1 ATOM 3059 O O . VAL B 2 191 ? 29.646 48.154 16.646 1.00 16.05 ? 439 VAL B O 1 ATOM 3060 C CB . VAL B 2 191 ? 31.356 48.216 19.571 1.00 14.95 ? 439 VAL B CB 1 ATOM 3061 C CG1 . VAL B 2 191 ? 29.861 48.433 19.938 1.00 15.78 ? 439 VAL B CG1 1 ATOM 3062 C CG2 . VAL B 2 191 ? 32.017 47.240 20.613 1.00 15.91 ? 439 VAL B CG2 1 ATOM 3063 N N . PHE B 2 192 ? 31.337 49.626 16.747 1.00 14.30 ? 440 PHE B N 1 ATOM 3064 C CA . PHE B 2 192 ? 30.780 50.506 15.717 1.00 14.48 ? 440 PHE B CA 1 ATOM 3065 C C . PHE B 2 192 ? 30.493 49.699 14.429 1.00 15.89 ? 440 PHE B C 1 ATOM 3066 O O . PHE B 2 192 ? 29.383 49.773 13.857 1.00 16.30 ? 440 PHE B O 1 ATOM 3067 C CB . PHE B 2 192 ? 31.755 51.649 15.469 1.00 15.05 ? 440 PHE B CB 1 ATOM 3068 C CG . PHE B 2 192 ? 31.230 52.727 14.532 1.00 14.94 ? 440 PHE B CG 1 ATOM 3069 C CD1 . PHE B 2 192 ? 31.309 52.567 13.135 1.00 16.36 ? 440 PHE B CD1 1 ATOM 3070 C CD2 . PHE B 2 192 ? 30.721 53.919 15.052 1.00 16.56 ? 440 PHE B CD2 1 ATOM 3071 C CE1 . PHE B 2 192 ? 30.858 53.565 12.260 1.00 17.43 ? 440 PHE B CE1 1 ATOM 3072 C CE2 . PHE B 2 192 ? 30.254 54.934 14.215 1.00 17.22 ? 440 PHE B CE2 1 ATOM 3073 C CZ . PHE B 2 192 ? 30.316 54.751 12.775 1.00 18.24 ? 440 PHE B CZ 1 ATOM 3074 N N . ASN B 2 193 ? 31.478 48.911 13.994 1.00 16.88 ? 441 ASN B N 1 ATOM 3075 C CA . ASN B 2 193 ? 31.307 48.107 12.774 1.00 18.10 ? 441 ASN B CA 1 ATOM 3076 C C . ASN B 2 193 ? 30.300 46.964 12.939 1.00 18.49 ? 441 ASN B C 1 ATOM 3077 O O . ASN B 2 193 ? 29.437 46.762 12.066 1.00 18.59 ? 441 ASN B O 1 ATOM 3078 C CB . ASN B 2 193 ? 32.670 47.549 12.318 1.00 18.12 ? 441 ASN B CB 1 ATOM 3079 C CG . ASN B 2 193 ? 33.533 48.605 11.650 1.00 19.92 ? 441 ASN B CG 1 ATOM 3080 O OD1 . ASN B 2 193 ? 33.282 49.814 11.750 1.00 19.50 ? 441 ASN B OD1 1 ATOM 3081 N ND2 . ASN B 2 193 ? 34.586 48.148 10.972 1.00 24.77 ? 441 ASN B ND2 1 ATOM 3082 N N . ALA B 2 194 ? 30.363 46.239 14.052 1.00 17.34 ? 442 ALA B N 1 ATOM 3083 C CA . ALA B 2 194 ? 29.485 45.073 14.237 1.00 18.53 ? 442 ALA B CA 1 ATOM 3084 C C . ALA B 2 194 ? 28.023 45.530 14.336 1.00 19.29 ? 442 ALA B C 1 ATOM 3085 O O . ALA B 2 194 ? 27.115 44.807 13.951 1.00 20.38 ? 442 ALA B O 1 ATOM 3086 C CB . ALA B 2 194 ? 29.870 44.281 15.468 1.00 18.24 ? 442 ALA B CB 1 ATOM 3087 N N . SER B 2 195 ? 27.796 46.751 14.822 1.00 18.70 ? 443 SER B N 1 ATOM 3088 C CA . SER B 2 195 ? 26.414 47.173 15.086 1.00 19.35 ? 443 SER B CA 1 ATOM 3089 C C . SER B 2 195 ? 25.770 47.886 13.909 1.00 19.50 ? 443 SER B C 1 ATOM 3090 O O . SER B 2 195 ? 24.651 48.347 14.003 1.00 20.35 ? 443 SER B O 1 ATOM 3091 C CB . SER B 2 195 ? 26.332 48.015 16.369 1.00 19.44 ? 443 SER B CB 1 ATOM 3092 O OG . SER B 2 195 ? 26.965 49.248 16.168 1.00 22.14 ? 443 SER B OG 1 ATOM 3093 N N . GLY B 2 196 ? 26.467 47.925 12.782 1.00 19.00 ? 444 GLY B N 1 ATOM 3094 C CA . GLY B 2 196 ? 25.846 48.375 11.538 1.00 19.92 ? 444 GLY B CA 1 ATOM 3095 C C . GLY B 2 196 ? 25.950 49.857 11.259 1.00 20.07 ? 444 GLY B C 1 ATOM 3096 O O . GLY B 2 196 ? 25.274 50.378 10.352 1.00 21.30 ? 444 GLY B O 1 ATOM 3097 N N . LEU B 2 197 ? 26.814 50.556 11.980 1.00 18.99 ? 445 LEU B N 1 ATOM 3098 C CA . LEU B 2 197 ? 26.857 52.010 11.801 1.00 19.05 ? 445 LEU B CA 1 ATOM 3099 C C . LEU B 2 197 ? 27.566 52.478 10.529 1.00 18.25 ? 445 LEU B C 1 ATOM 3100 O O . LEU B 2 197 ? 27.296 53.579 10.054 1.00 17.48 ? 445 LEU B O 1 ATOM 3101 C CB . LEU B 2 197 ? 27.455 52.717 13.027 1.00 19.24 ? 445 LEU B CB 1 ATOM 3102 C CG . LEU B 2 197 ? 26.457 52.592 14.187 1.00 21.81 ? 445 LEU B CG 1 ATOM 3103 C CD1 . LEU B 2 197 ? 27.131 52.960 15.488 1.00 21.22 ? 445 LEU B CD1 1 ATOM 3104 C CD2 . LEU B 2 197 ? 25.241 53.500 13.920 1.00 27.54 ? 445 LEU B CD2 1 ATOM 3105 N N . GLN B 2 198 ? 28.446 51.648 9.971 1.00 18.06 ? 446 GLN B N 1 ATOM 3106 C CA . GLN B 2 198 ? 29.141 52.064 8.736 1.00 18.95 ? 446 GLN B CA 1 ATOM 3107 C C . GLN B 2 198 ? 28.127 52.320 7.620 1.00 19.45 ? 446 GLN B C 1 ATOM 3108 O O . GLN B 2 198 ? 28.289 53.266 6.850 1.00 19.84 ? 446 GLN B O 1 ATOM 3109 C CB . GLN B 2 198 ? 30.192 51.024 8.298 1.00 19.02 ? 446 GLN B CB 1 ATOM 3110 C CG . GLN B 2 198 ? 31.405 50.937 9.251 1.00 20.65 ? 446 GLN B CG 1 ATOM 3111 C CD . GLN B 2 198 ? 32.337 52.158 9.219 1.00 24.53 ? 446 GLN B CD 1 ATOM 3112 O OE1 . GLN B 2 198 ? 32.138 53.120 8.451 1.00 26.82 ? 446 GLN B OE1 1 ATOM 3113 N NE2 . GLN B 2 198 ? 33.367 52.114 10.043 1.00 24.21 ? 446 GLN B NE2 1 ATOM 3114 N N . ALA B 2 199 ? 27.075 51.509 7.556 1.00 20.22 ? 447 ALA B N 1 ATOM 3115 C CA . ALA B 2 199 ? 26.077 51.645 6.471 1.00 21.29 ? 447 ALA B CA 1 ATOM 3116 C C . ALA B 2 199 ? 25.335 52.967 6.635 1.00 21.33 ? 447 ALA B C 1 ATOM 3117 O O . ALA B 2 199 ? 24.943 53.621 5.661 1.00 20.48 ? 447 ALA B O 1 ATOM 3118 C CB . ALA B 2 199 ? 25.081 50.474 6.513 1.00 22.33 ? 447 ALA B CB 1 ATOM 3119 N N . LEU B 2 200 ? 25.114 53.349 7.896 1.00 20.38 ? 448 LEU B N 1 ATOM 3120 C CA . LEU B 2 200 ? 24.410 54.578 8.193 1.00 20.23 ? 448 LEU B CA 1 ATOM 3121 C C . LEU B 2 200 ? 25.261 55.810 7.868 1.00 19.67 ? 448 LEU B C 1 ATOM 3122 O O . LEU B 2 200 ? 24.724 56.783 7.332 1.00 20.57 ? 448 LEU B O 1 ATOM 3123 C CB . LEU B 2 200 ? 23.932 54.604 9.658 1.00 20.56 ? 448 LEU B CB 1 ATOM 3124 C CG . LEU B 2 200 ? 22.707 53.720 9.948 1.00 23.17 ? 448 LEU B CG 1 ATOM 3125 C CD1 . LEU B 2 200 ? 22.370 53.781 11.418 1.00 25.48 ? 448 LEU B CD1 1 ATOM 3126 C CD2 . LEU B 2 200 ? 21.496 54.206 9.170 1.00 25.33 ? 448 LEU B CD2 1 ATOM 3127 N N . VAL B 2 201 ? 26.557 55.772 8.202 1.00 19.53 ? 449 VAL B N 1 ATOM 3128 C CA . VAL B 2 201 ? 27.499 56.824 7.772 1.00 20.50 ? 449 VAL B CA 1 ATOM 3129 C C . VAL B 2 201 ? 27.493 56.886 6.221 1.00 20.62 ? 449 VAL B C 1 ATOM 3130 O O . VAL B 2 201 ? 27.430 57.958 5.649 1.00 21.03 ? 449 VAL B O 1 ATOM 3131 C CB . VAL B 2 201 ? 28.941 56.588 8.298 1.00 20.39 ? 449 VAL B CB 1 ATOM 3132 C CG1 . VAL B 2 201 ? 29.915 57.625 7.744 1.00 21.82 ? 449 VAL B CG1 1 ATOM 3133 C CG2 . VAL B 2 201 ? 28.981 56.644 9.842 1.00 19.75 ? 449 VAL B CG2 1 ATOM 3134 N N . ALA B 2 202 ? 27.520 55.738 5.557 1.00 21.58 ? 450 ALA B N 1 ATOM 3135 C CA . ALA B 2 202 ? 27.542 55.737 4.075 1.00 21.83 ? 450 ALA B CA 1 ATOM 3136 C C . ALA B 2 202 ? 26.295 56.394 3.504 1.00 22.23 ? 450 ALA B C 1 ATOM 3137 O O . ALA B 2 202 ? 26.390 57.133 2.513 1.00 22.33 ? 450 ALA B O 1 ATOM 3138 C CB . ALA B 2 202 ? 27.702 54.329 3.528 1.00 22.28 ? 450 ALA B CB 1 ATOM 3139 N N . GLN B 2 203 ? 25.144 56.144 4.132 1.00 21.10 ? 451 GLN B N 1 ATOM 3140 C CA . GLN B 2 203 ? 23.861 56.618 3.615 1.00 22.05 ? 451 GLN B CA 1 ATOM 3141 C C . GLN B 2 203 ? 23.603 58.068 3.963 1.00 23.24 ? 451 GLN B C 1 ATOM 3142 O O . GLN B 2 203 ? 23.153 58.850 3.114 1.00 22.69 ? 451 GLN B O 1 ATOM 3143 C CB . GLN B 2 203 ? 22.705 55.749 4.091 1.00 22.74 ? 451 GLN B CB 1 ATOM 3144 C CG . GLN B 2 203 ? 21.338 56.159 3.495 1.00 24.03 ? 451 GLN B CG 1 ATOM 3145 C CD . GLN B 2 203 ? 20.195 55.252 3.905 1.00 26.32 ? 451 GLN B CD 1 ATOM 3146 O OE1 . GLN B 2 203 ? 20.394 54.251 4.585 1.00 28.35 ? 451 GLN B OE1 1 ATOM 3147 N NE2 . GLN B 2 203 ? 18.988 55.603 3.488 1.00 26.71 ? 451 GLN B NE2 1 ATOM 3148 N N . TYR B 2 204 ? 23.904 58.441 5.211 1.00 21.48 ? 452 TYR B N 1 ATOM 3149 C CA . TYR B 2 204 ? 23.451 59.731 5.750 1.00 22.68 ? 452 TYR B CA 1 ATOM 3150 C C . TYR B 2 204 ? 24.575 60.663 6.181 1.00 23.41 ? 452 TYR B C 1 ATOM 3151 O O . TYR B 2 204 ? 24.334 61.823 6.454 1.00 25.03 ? 452 TYR B O 1 ATOM 3152 C CB . TYR B 2 204 ? 22.566 59.509 6.960 1.00 22.73 ? 452 TYR B CB 1 ATOM 3153 C CG . TYR B 2 204 ? 21.248 58.823 6.707 1.00 23.79 ? 452 TYR B CG 1 ATOM 3154 C CD1 . TYR B 2 204 ? 20.975 57.575 7.279 1.00 22.26 ? 452 TYR B CD1 1 ATOM 3155 C CD2 . TYR B 2 204 ? 20.253 59.432 5.924 1.00 24.43 ? 452 TYR B CD2 1 ATOM 3156 C CE1 . TYR B 2 204 ? 19.743 56.940 7.069 1.00 26.03 ? 452 TYR B CE1 1 ATOM 3157 C CE2 . TYR B 2 204 ? 19.027 58.797 5.716 1.00 24.87 ? 452 TYR B CE2 1 ATOM 3158 C CZ . TYR B 2 204 ? 18.780 57.571 6.290 1.00 24.57 ? 452 TYR B CZ 1 ATOM 3159 O OH . TYR B 2 204 ? 17.581 56.930 6.103 1.00 27.72 ? 452 TYR B OH 1 ATOM 3160 N N . GLY B 2 205 ? 25.796 60.172 6.252 1.00 23.12 ? 453 GLY B N 1 ATOM 3161 C CA . GLY B 2 205 ? 26.918 61.046 6.529 1.00 22.84 ? 453 GLY B CA 1 ATOM 3162 C C . GLY B 2 205 ? 27.312 61.169 8.003 1.00 22.58 ? 453 GLY B C 1 ATOM 3163 O O . GLY B 2 205 ? 27.044 60.274 8.813 1.00 21.42 ? 453 GLY B O 1 ATOM 3164 N N . ASP B 2 206 ? 27.933 62.300 8.314 1.00 21.73 ? 454 ASP B N 1 ATOM 3165 C CA . ASP B 2 206 ? 28.661 62.502 9.591 1.00 22.14 ? 454 ASP B CA 1 ATOM 3166 C C . ASP B 2 206 ? 27.783 62.439 10.843 1.00 20.24 ? 454 ASP B C 1 ATOM 3167 O O . ASP B 2 206 ? 28.322 62.330 11.943 1.00 19.63 ? 454 ASP B O 1 ATOM 3168 C CB . ASP B 2 206 ? 29.367 63.879 9.616 1.00 23.97 ? 454 ASP B CB 1 ATOM 3169 C CG . ASP B 2 206 ? 30.521 64.010 8.629 1.00 27.68 ? 454 ASP B CG 1 ATOM 3170 O OD1 . ASP B 2 206 ? 31.080 63.004 8.157 1.00 32.77 ? 454 ASP B OD1 1 ATOM 3171 O OD2 . ASP B 2 206 ? 30.906 65.188 8.386 1.00 35.42 ? 454 ASP B OD2 1 ATOM 3172 N N . TRP B 2 207 ? 26.455 62.553 10.712 1.00 18.04 ? 455 TRP B N 1 ATOM 3173 C CA . TRP B 2 207 ? 25.596 62.483 11.902 1.00 18.44 ? 455 TRP B CA 1 ATOM 3174 C C . TRP B 2 207 ? 25.802 61.146 12.632 1.00 17.33 ? 455 TRP B C 1 ATOM 3175 O O . TRP B 2 207 ? 25.666 61.074 13.845 1.00 17.25 ? 455 TRP B O 1 ATOM 3176 C CB . TRP B 2 207 ? 24.125 62.623 11.501 1.00 19.22 ? 455 TRP B CB 1 ATOM 3177 C CG . TRP B 2 207 ? 23.202 63.033 12.600 1.00 20.64 ? 455 TRP B CG 1 ATOM 3178 C CD1 . TRP B 2 207 ? 22.869 64.338 12.974 1.00 21.66 ? 455 TRP B CD1 1 ATOM 3179 C CD2 . TRP B 2 207 ? 22.432 62.170 13.427 1.00 20.12 ? 455 TRP B CD2 1 ATOM 3180 N NE1 . TRP B 2 207 ? 21.950 64.302 13.998 1.00 21.65 ? 455 TRP B NE1 1 ATOM 3181 C CE2 . TRP B 2 207 ? 21.659 62.996 14.299 1.00 21.63 ? 455 TRP B CE2 1 ATOM 3182 C CE3 . TRP B 2 207 ? 22.305 60.768 13.529 1.00 22.06 ? 455 TRP B CE3 1 ATOM 3183 C CZ2 . TRP B 2 207 ? 20.779 62.458 15.250 1.00 22.48 ? 455 TRP B CZ2 1 ATOM 3184 C CZ3 . TRP B 2 207 ? 21.431 60.233 14.478 1.00 23.18 ? 455 TRP B CZ3 1 ATOM 3185 C CH2 . TRP B 2 207 ? 20.674 61.085 15.329 1.00 23.45 ? 455 TRP B CH2 1 ATOM 3186 N N . PHE B 2 208 ? 26.195 60.106 11.882 1.00 17.03 ? 456 PHE B N 1 ATOM 3187 C CA . PHE B 2 208 ? 26.417 58.796 12.474 1.00 17.51 ? 456 PHE B CA 1 ATOM 3188 C C . PHE B 2 208 ? 27.898 58.454 12.722 1.00 17.12 ? 456 PHE B C 1 ATOM 3189 O O . PHE B 2 208 ? 28.185 57.364 13.221 1.00 17.88 ? 456 PHE B O 1 ATOM 3190 C CB . PHE B 2 208 ? 25.775 57.701 11.614 1.00 17.27 ? 456 PHE B CB 1 ATOM 3191 C CG . PHE B 2 208 ? 24.276 57.809 11.543 1.00 17.22 ? 456 PHE B CG 1 ATOM 3192 C CD1 . PHE B 2 208 ? 23.674 58.543 10.539 1.00 16.42 ? 456 PHE B CD1 1 ATOM 3193 C CD2 . PHE B 2 208 ? 23.480 57.190 12.509 1.00 19.81 ? 456 PHE B CD2 1 ATOM 3194 C CE1 . PHE B 2 208 ? 22.295 58.658 10.489 1.00 17.64 ? 456 PHE B CE1 1 ATOM 3195 C CE2 . PHE B 2 208 ? 22.081 57.293 12.471 1.00 20.47 ? 456 PHE B CE2 1 ATOM 3196 C CZ . PHE B 2 208 ? 21.497 58.041 11.451 1.00 21.17 ? 456 PHE B CZ 1 ATOM 3197 N N . SER B 2 209 ? 28.798 59.388 12.402 1.00 16.94 ? 457 SER B N 1 ATOM 3198 C CA A SER B 2 209 ? 30.241 59.234 12.595 0.50 16.36 ? 457 SER B CA 1 ATOM 3199 C CA B SER B 2 209 ? 30.222 59.151 12.614 0.50 16.96 ? 457 SER B CA 1 ATOM 3200 C C . SER B 2 209 ? 30.585 59.443 14.073 1.00 16.51 ? 457 SER B C 1 ATOM 3201 O O . SER B 2 209 ? 30.001 60.332 14.717 1.00 17.32 ? 457 SER B O 1 ATOM 3202 C CB A SER B 2 209 ? 30.958 60.297 11.770 0.50 16.87 ? 457 SER B CB 1 ATOM 3203 C CB B SER B 2 209 ? 31.050 60.030 11.699 0.50 17.69 ? 457 SER B CB 1 ATOM 3204 O OG A SER B 2 209 ? 32.328 60.411 12.122 0.50 13.71 ? 457 SER B OG 1 ATOM 3205 O OG B SER B 2 209 ? 31.067 61.354 12.182 0.50 17.79 ? 457 SER B OG 1 ATOM 3206 N N . TYR B 2 210 ? 31.528 58.678 14.604 1.00 15.40 ? 458 TYR B N 1 ATOM 3207 C CA . TYR B 2 210 ? 31.926 58.852 15.984 1.00 14.43 ? 458 TYR B CA 1 ATOM 3208 C C . TYR B 2 210 ? 32.597 60.236 16.216 1.00 16.06 ? 458 TYR B C 1 ATOM 3209 O O . TYR B 2 210 ? 32.338 60.915 17.231 1.00 16.53 ? 458 TYR B O 1 ATOM 3210 C CB . TYR B 2 210 ? 32.883 57.707 16.428 1.00 14.11 ? 458 TYR B CB 1 ATOM 3211 C CG . TYR B 2 210 ? 33.279 57.891 17.883 1.00 14.39 ? 458 TYR B CG 1 ATOM 3212 C CD1 . TYR B 2 210 ? 34.530 58.405 18.228 1.00 15.05 ? 458 TYR B CD1 1 ATOM 3213 C CD2 . TYR B 2 210 ? 32.370 57.611 18.902 1.00 14.98 ? 458 TYR B CD2 1 ATOM 3214 C CE1 . TYR B 2 210 ? 34.885 58.644 19.577 1.00 15.34 ? 458 TYR B CE1 1 ATOM 3215 C CE2 . TYR B 2 210 ? 32.705 57.841 20.244 1.00 14.56 ? 458 TYR B CE2 1 ATOM 3216 C CZ . TYR B 2 210 ? 33.974 58.359 20.558 1.00 14.92 ? 458 TYR B CZ 1 ATOM 3217 O OH . TYR B 2 210 ? 34.309 58.554 21.901 1.00 15.74 ? 458 TYR B OH 1 ATOM 3218 N N . THR B 2 211 ? 33.449 60.668 15.290 1.00 17.27 ? 459 THR B N 1 ATOM 3219 C CA . THR B 2 211 ? 34.239 61.880 15.525 1.00 19.31 ? 459 THR B CA 1 ATOM 3220 C C . THR B 2 211 ? 33.626 63.127 14.907 1.00 19.13 ? 459 THR B C 1 ATOM 3221 O O . THR B 2 211 ? 33.954 64.229 15.326 1.00 19.06 ? 459 THR B O 1 ATOM 3222 C CB . THR B 2 211 ? 35.689 61.716 14.995 1.00 20.13 ? 459 THR B CB 1 ATOM 3223 O OG1 . THR B 2 211 ? 35.627 61.429 13.602 1.00 23.84 ? 459 THR B OG1 1 ATOM 3224 C CG2 . THR B 2 211 ? 36.404 60.570 15.724 1.00 20.62 ? 459 THR B CG2 1 ATOM 3225 N N . LYS B 2 212 ? 32.737 62.967 13.917 1.00 18.65 ? 460 LYS B N 1 ATOM 3226 C CA . LYS B 2 212 ? 32.246 64.113 13.139 1.00 19.63 ? 460 LYS B CA 1 ATOM 3227 C C . LYS B 2 212 ? 30.773 64.468 13.316 1.00 18.45 ? 460 LYS B C 1 ATOM 3228 O O . LYS B 2 212 ? 30.293 65.405 12.696 1.00 18.72 ? 460 LYS B O 1 ATOM 3229 C CB . LYS B 2 212 ? 32.575 63.925 11.652 1.00 19.86 ? 460 LYS B CB 1 ATOM 3230 C CG . LYS B 2 212 ? 34.057 63.786 11.428 1.00 24.58 ? 460 LYS B CG 1 ATOM 3231 C CD . LYS B 2 212 ? 34.387 63.724 9.938 1.00 32.33 ? 460 LYS B CD 1 ATOM 3232 C CE . LYS B 2 212 ? 35.887 63.820 9.719 1.00 38.58 ? 460 LYS B CE 1 ATOM 3233 N NZ . LYS B 2 212 ? 36.200 64.040 8.263 1.00 43.72 ? 460 LYS B NZ 1 ATOM 3234 N N . ASN B 2 213 ? 30.047 63.747 14.176 1.00 16.68 ? 461 ASN B N 1 ATOM 3235 C CA . ASN B 2 213 ? 28.655 64.119 14.432 1.00 16.41 ? 461 ASN B CA 1 ATOM 3236 C C . ASN B 2 213 ? 28.574 65.451 15.200 1.00 16.59 ? 461 ASN B C 1 ATOM 3237 O O . ASN B 2 213 ? 29.565 65.872 15.810 1.00 14.69 ? 461 ASN B O 1 ATOM 3238 C CB . ASN B 2 213 ? 27.960 63.010 15.214 1.00 16.43 ? 461 ASN B CB 1 ATOM 3239 C CG . ASN B 2 213 ? 28.442 62.918 16.608 1.00 19.65 ? 461 ASN B CG 1 ATOM 3240 O OD1 . ASN B 2 213 ? 27.970 63.669 17.496 1.00 18.13 ? 461 ASN B OD1 1 ATOM 3241 N ND2 . ASN B 2 213 ? 29.370 61.986 16.840 1.00 18.03 ? 461 ASN B ND2 1 ATOM 3242 N N . PRO B 2 214 ? 27.403 66.126 15.172 1.00 17.22 ? 462 PRO B N 1 ATOM 3243 C CA . PRO B 2 214 ? 27.273 67.464 15.801 1.00 16.38 ? 462 PRO B CA 1 ATOM 3244 C C . PRO B 2 214 ? 27.682 67.524 17.296 1.00 16.14 ? 462 PRO B C 1 ATOM 3245 O O . PRO B 2 214 ? 28.405 68.445 17.698 1.00 15.40 ? 462 PRO B O 1 ATOM 3246 C CB . PRO B 2 214 ? 25.779 67.783 15.654 1.00 17.56 ? 462 PRO B CB 1 ATOM 3247 C CG . PRO B 2 214 ? 25.361 67.042 14.414 1.00 17.88 ? 462 PRO B CG 1 ATOM 3248 C CD . PRO B 2 214 ? 26.151 65.730 14.482 1.00 17.69 ? 462 PRO B CD 1 ATOM 3249 N N . ARG B 2 215 ? 27.239 66.573 18.119 1.00 14.80 ? 463 ARG B N 1 ATOM 3250 C CA . ARG B 2 215 ? 27.652 66.632 19.534 1.00 13.71 ? 463 ARG B CA 1 ATOM 3251 C C . ARG B 2 215 ? 29.139 66.424 19.701 1.00 13.80 ? 463 ARG B C 1 ATOM 3252 O O . ARG B 2 215 ? 29.781 67.131 20.506 1.00 13.89 ? 463 ARG B O 1 ATOM 3253 C CB . ARG B 2 215 ? 26.845 65.661 20.406 1.00 14.94 ? 463 ARG B CB 1 ATOM 3254 C CG . ARG B 2 215 ? 25.466 66.194 20.737 1.00 15.47 ? 463 ARG B CG 1 ATOM 3255 C CD . ARG B 2 215 ? 24.733 65.217 21.639 1.00 16.82 ? 463 ARG B CD 1 ATOM 3256 N NE . ARG B 2 215 ? 24.161 64.120 20.848 1.00 16.56 ? 463 ARG B NE 1 ATOM 3257 C CZ . ARG B 2 215 ? 23.697 62.997 21.410 1.00 17.78 ? 463 ARG B CZ 1 ATOM 3258 N NH1 . ARG B 2 215 ? 23.831 62.807 22.721 1.00 15.64 ? 463 ARG B NH1 1 ATOM 3259 N NH2 . ARG B 2 215 ? 23.152 62.048 20.649 1.00 18.49 ? 463 ARG B NH2 1 ATOM 3260 N N . ALA B 2 216 ? 29.713 65.462 18.979 1.00 12.52 ? 464 ALA B N 1 ATOM 3261 C CA . ALA B 2 216 ? 31.173 65.297 19.021 1.00 13.67 ? 464 ALA B CA 1 ATOM 3262 C C . ALA B 2 216 ? 31.876 66.620 18.683 1.00 14.48 ? 464 ALA B C 1 ATOM 3263 O O . ALA B 2 216 ? 32.850 67.020 19.359 1.00 13.28 ? 464 ALA B O 1 ATOM 3264 C CB . ALA B 2 216 ? 31.628 64.209 18.052 1.00 14.38 ? 464 ALA B CB 1 ATOM 3265 N N . LYS B 2 217 ? 31.392 67.302 17.637 1.00 13.70 ? 465 LYS B N 1 ATOM 3266 C CA . LYS B 2 217 ? 32.052 68.564 17.224 1.00 15.11 ? 465 LYS B CA 1 ATOM 3267 C C . LYS B 2 217 ? 31.857 69.670 18.253 1.00 14.17 ? 465 LYS B C 1 ATOM 3268 O O . LYS B 2 217 ? 32.768 70.497 18.485 1.00 15.61 ? 465 LYS B O 1 ATOM 3269 C CB . LYS B 2 217 ? 31.525 69.002 15.850 1.00 14.53 ? 465 LYS B CB 1 ATOM 3270 C CG . LYS B 2 217 ? 31.977 68.019 14.752 1.00 18.89 ? 465 LYS B CG 1 ATOM 3271 C CD . LYS B 2 217 ? 31.847 68.694 13.380 1.00 26.86 ? 465 LYS B CD 1 ATOM 3272 C CE . LYS B 2 217 ? 32.649 67.928 12.329 1.00 32.56 ? 465 LYS B CE 1 ATOM 3273 N NZ . LYS B 2 217 ? 32.693 68.717 11.049 1.00 39.89 ? 465 LYS B NZ 1 ATOM 3274 N N . ILE B 2 218 ? 30.679 69.718 18.860 1.00 13.98 ? 466 ILE B N 1 ATOM 3275 C CA . ILE B 2 218 ? 30.416 70.745 19.884 1.00 13.91 ? 466 ILE B CA 1 ATOM 3276 C C . ILE B 2 218 ? 31.319 70.484 21.117 1.00 14.25 ? 466 ILE B C 1 ATOM 3277 O O . ILE B 2 218 ? 31.951 71.410 21.657 1.00 13.78 ? 466 ILE B O 1 ATOM 3278 C CB . ILE B 2 218 ? 28.928 70.791 20.298 1.00 14.68 ? 466 ILE B CB 1 ATOM 3279 C CG1 . ILE B 2 218 ? 28.056 71.265 19.124 1.00 14.00 ? 466 ILE B CG1 1 ATOM 3280 C CG2 . ILE B 2 218 ? 28.720 71.676 21.618 1.00 14.63 ? 466 ILE B CG2 1 ATOM 3281 C CD1 . ILE B 2 218 ? 26.547 71.003 19.416 1.00 17.02 ? 466 ILE B CD1 1 ATOM 3282 N N . PHE B 2 219 ? 31.413 69.227 21.549 1.00 13.88 ? 467 PHE B N 1 ATOM 3283 C CA . PHE B 2 219 ? 32.335 68.934 22.663 1.00 14.70 ? 467 PHE B CA 1 ATOM 3284 C C . PHE B 2 219 ? 33.791 69.270 22.291 1.00 15.60 ? 467 PHE B C 1 ATOM 3285 O O . PHE B 2 219 ? 34.556 69.819 23.126 1.00 15.63 ? 467 PHE B O 1 ATOM 3286 C CB . PHE B 2 219 ? 32.232 67.455 23.036 1.00 15.16 ? 467 PHE B CB 1 ATOM 3287 C CG . PHE B 2 219 ? 31.076 67.102 23.933 1.00 13.77 ? 467 PHE B CG 1 ATOM 3288 C CD1 . PHE B 2 219 ? 30.157 66.107 23.547 1.00 13.45 ? 467 PHE B CD1 1 ATOM 3289 C CD2 . PHE B 2 219 ? 30.925 67.695 25.188 1.00 15.26 ? 467 PHE B CD2 1 ATOM 3290 C CE1 . PHE B 2 219 ? 29.121 65.716 24.432 1.00 12.80 ? 467 PHE B CE1 1 ATOM 3291 C CE2 . PHE B 2 219 ? 29.880 67.344 26.037 1.00 16.38 ? 467 PHE B CE2 1 ATOM 3292 C CZ . PHE B 2 219 ? 28.964 66.320 25.666 1.00 14.90 ? 467 PHE B CZ 1 ATOM 3293 N N . GLN B 2 220 ? 34.223 68.907 21.087 1.00 15.54 ? 468 GLN B N 1 ATOM 3294 C CA . GLN B 2 220 ? 35.581 69.232 20.656 1.00 16.69 ? 468 GLN B CA 1 ATOM 3295 C C . GLN B 2 220 ? 35.839 70.740 20.707 1.00 16.84 ? 468 GLN B C 1 ATOM 3296 O O . GLN B 2 220 ? 36.937 71.169 21.081 1.00 17.09 ? 468 GLN B O 1 ATOM 3297 C CB . GLN B 2 220 ? 35.845 68.733 19.230 1.00 16.81 ? 468 GLN B CB 1 ATOM 3298 C CG . GLN B 2 220 ? 36.032 67.197 19.207 1.00 17.02 ? 468 GLN B CG 1 ATOM 3299 C CD . GLN B 2 220 ? 35.630 66.606 17.837 1.00 20.35 ? 468 GLN B CD 1 ATOM 3300 O OE1 . GLN B 2 220 ? 35.602 67.320 16.824 1.00 18.75 ? 468 GLN B OE1 1 ATOM 3301 N NE2 . GLN B 2 220 ? 35.303 65.293 17.815 1.00 20.98 ? 468 GLN B NE2 1 ATOM 3302 N N . ARG B 2 221 ? 34.846 71.523 20.279 1.00 15.89 ? 469 ARG B N 1 ATOM 3303 C CA . ARG B 2 221 ? 34.985 72.969 20.211 1.00 16.92 ? 469 ARG B CA 1 ATOM 3304 C C . ARG B 2 221 ? 34.991 73.576 21.606 1.00 17.03 ? 469 ARG B C 1 ATOM 3305 O O . ARG B 2 221 ? 35.768 74.519 21.887 1.00 17.30 ? 469 ARG B O 1 ATOM 3306 C CB . ARG B 2 221 ? 33.829 73.565 19.384 1.00 16.74 ? 469 ARG B CB 1 ATOM 3307 C CG . ARG B 2 221 ? 34.048 75.052 18.977 1.00 17.65 ? 469 ARG B CG 1 ATOM 3308 C CD . ARG B 2 221 ? 32.770 75.631 18.325 1.00 18.18 ? 469 ARG B CD 1 ATOM 3309 N NE . ARG B 2 221 ? 31.619 75.527 19.235 1.00 16.97 ? 469 ARG B NE 1 ATOM 3310 C CZ . ARG B 2 221 ? 30.347 75.623 18.841 1.00 20.05 ? 469 ARG B CZ 1 ATOM 3311 N NH1 . ARG B 2 221 ? 29.361 75.517 19.730 1.00 19.82 ? 469 ARG B NH1 1 ATOM 3312 N NH2 . ARG B 2 221 ? 30.054 75.846 17.548 1.00 18.85 ? 469 ARG B NH2 1 ATOM 3313 N N . ASP B 2 222 ? 34.129 73.057 22.487 1.00 16.08 ? 470 ASP B N 1 ATOM 3314 C CA . ASP B 2 222 ? 33.750 73.776 23.729 1.00 15.56 ? 470 ASP B CA 1 ATOM 3315 C C . ASP B 2 222 ? 34.147 73.144 25.079 1.00 15.16 ? 470 ASP B C 1 ATOM 3316 O O . ASP B 2 222 ? 34.004 73.775 26.118 1.00 15.12 ? 470 ASP B O 1 ATOM 3317 C CB . ASP B 2 222 ? 32.231 74.025 23.751 1.00 17.11 ? 470 ASP B CB 1 ATOM 3318 C CG . ASP B 2 222 ? 31.776 74.933 22.611 1.00 22.56 ? 470 ASP B CG 1 ATOM 3319 O OD1 . ASP B 2 222 ? 32.653 75.565 21.933 1.00 21.95 ? 470 ASP B OD1 1 ATOM 3320 O OD2 . ASP B 2 222 ? 30.544 75.015 22.404 1.00 23.80 ? 470 ASP B OD2 1 ATOM 3321 N N . GLN B 2 223 ? 34.602 71.894 25.082 1.00 14.31 ? 471 GLN B N 1 ATOM 3322 C CA . GLN B 2 223 ? 34.799 71.206 26.376 1.00 14.15 ? 471 GLN B CA 1 ATOM 3323 C C . GLN B 2 223 ? 35.852 71.916 27.237 1.00 14.76 ? 471 GLN B C 1 ATOM 3324 O O . GLN B 2 223 ? 35.765 71.899 28.469 1.00 14.20 ? 471 GLN B O 1 ATOM 3325 C CB . GLN B 2 223 ? 35.202 69.731 26.175 1.00 14.18 ? 471 GLN B CB 1 ATOM 3326 C CG . GLN B 2 223 ? 36.506 69.491 25.389 1.00 12.22 ? 471 GLN B CG 1 ATOM 3327 C CD . GLN B 2 223 ? 37.744 69.639 26.274 1.00 13.23 ? 471 GLN B CD 1 ATOM 3328 O OE1 . GLN B 2 223 ? 37.666 69.505 27.512 1.00 15.25 ? 471 GLN B OE1 1 ATOM 3329 N NE2 . GLN B 2 223 ? 38.880 69.938 25.656 1.00 15.12 ? 471 GLN B NE2 1 ATOM 3330 N N . SER B 2 224 ? 36.830 72.555 26.587 1.00 14.44 ? 472 SER B N 1 ATOM 3331 C CA . SER B 2 224 ? 37.892 73.198 27.399 1.00 15.36 ? 472 SER B CA 1 ATOM 3332 C C . SER B 2 224 ? 37.374 74.389 28.207 1.00 15.77 ? 472 SER B C 1 ATOM 3333 O O . SER B 2 224 ? 38.021 74.815 29.182 1.00 15.30 ? 472 SER B O 1 ATOM 3334 C CB . SER B 2 224 ? 39.077 73.609 26.524 1.00 16.73 ? 472 SER B CB 1 ATOM 3335 O OG . SER B 2 224 ? 38.795 74.819 25.856 1.00 19.81 ? 472 SER B OG 1 ATOM 3336 N N . LEU B 2 225 ? 36.194 74.911 27.855 1.00 14.57 ? 473 LEU B N 1 ATOM 3337 C CA . LEU B 2 225 ? 35.636 76.008 28.607 1.00 15.40 ? 473 LEU B CA 1 ATOM 3338 C C . LEU B 2 225 ? 35.039 75.533 29.935 1.00 15.75 ? 473 LEU B C 1 ATOM 3339 O O . LEU B 2 225 ? 34.589 76.333 30.757 1.00 16.28 ? 473 LEU B O 1 ATOM 3340 C CB . LEU B 2 225 ? 34.569 76.759 27.781 1.00 16.80 ? 473 LEU B CB 1 ATOM 3341 C CG . LEU B 2 225 ? 35.018 77.196 26.395 1.00 19.60 ? 473 LEU B CG 1 ATOM 3342 C CD1 . LEU B 2 225 ? 33.784 77.828 25.664 1.00 22.72 ? 473 LEU B CD1 1 ATOM 3343 C CD2 . LEU B 2 225 ? 36.180 78.168 26.534 1.00 22.34 ? 473 LEU B CD2 1 ATOM 3344 N N . VAL B 2 226 ? 34.984 74.217 30.146 1.00 15.64 ? 474 VAL B N 1 ATOM 3345 C CA . VAL B 2 226 ? 34.452 73.720 31.401 1.00 15.84 ? 474 VAL B CA 1 ATOM 3346 C C . VAL B 2 226 ? 35.562 73.850 32.430 1.00 17.65 ? 474 VAL B C 1 ATOM 3347 O O . VAL B 2 226 ? 36.510 73.027 32.475 1.00 17.91 ? 474 VAL B O 1 ATOM 3348 C CB . VAL B 2 226 ? 34.024 72.249 31.268 1.00 14.52 ? 474 VAL B CB 1 ATOM 3349 C CG1 . VAL B 2 226 ? 33.667 71.697 32.626 1.00 15.26 ? 474 VAL B CG1 1 ATOM 3350 C CG2 . VAL B 2 226 ? 32.846 72.191 30.303 1.00 15.17 ? 474 VAL B CG2 1 ATOM 3351 N N . GLU B 2 227 ? 35.471 74.895 33.243 1.00 18.19 ? 475 GLU B N 1 ATOM 3352 C CA . GLU B 2 227 ? 36.570 75.186 34.171 1.00 19.16 ? 475 GLU B CA 1 ATOM 3353 C C . GLU B 2 227 ? 36.088 74.997 35.615 1.00 18.82 ? 475 GLU B C 1 ATOM 3354 O O . GLU B 2 227 ? 36.869 75.082 36.564 1.00 18.19 ? 475 GLU B O 1 ATOM 3355 C CB . GLU B 2 227 ? 37.092 76.609 33.907 1.00 20.23 ? 475 GLU B CB 1 ATOM 3356 C CG . GLU B 2 227 ? 36.021 77.661 34.046 1.00 21.77 ? 475 GLU B CG 1 ATOM 3357 C CD . GLU B 2 227 ? 36.617 79.081 33.911 1.00 24.28 ? 475 GLU B CD 1 ATOM 3358 O OE1 . GLU B 2 227 ? 37.384 79.483 34.812 1.00 23.80 ? 475 GLU B OE1 1 ATOM 3359 O OE2 . GLU B 2 227 ? 36.286 79.777 32.944 1.00 20.58 ? 475 GLU B OE2 1 ATOM 3360 N N . ASP B 2 228 ? 34.803 74.702 35.773 1.00 18.20 ? 476 ASP B N 1 ATOM 3361 C CA . ASP B 2 228 ? 34.169 74.524 37.086 1.00 19.28 ? 476 ASP B CA 1 ATOM 3362 C C . ASP B 2 228 ? 32.774 73.907 36.959 1.00 19.54 ? 476 ASP B C 1 ATOM 3363 O O . ASP B 2 228 ? 32.297 73.659 35.849 1.00 18.51 ? 476 ASP B O 1 ATOM 3364 C CB . ASP B 2 228 ? 34.134 75.843 37.899 1.00 20.41 ? 476 ASP B CB 1 ATOM 3365 C CG . ASP B 2 228 ? 33.355 76.981 37.204 1.00 25.17 ? 476 ASP B CG 1 ATOM 3366 O OD1 . ASP B 2 228 ? 32.415 76.734 36.412 1.00 24.83 ? 476 ASP B OD1 1 ATOM 3367 O OD2 . ASP B 2 228 ? 33.685 78.176 37.456 1.00 30.77 ? 476 ASP B OD2 1 ATOM 3368 N N . MET B 2 229 ? 32.136 73.617 38.092 1.00 19.21 ? 477 MET B N 1 ATOM 3369 C CA . MET B 2 229 ? 30.801 72.972 38.061 1.00 21.20 ? 477 MET B CA 1 ATOM 3370 C C . MET B 2 229 ? 29.776 73.763 37.269 1.00 20.43 ? 477 MET B C 1 ATOM 3371 O O . MET B 2 229 ? 29.008 73.197 36.504 1.00 19.61 ? 477 MET B O 1 ATOM 3372 C CB . MET B 2 229 ? 30.279 72.812 39.485 1.00 22.03 ? 477 MET B CB 1 ATOM 3373 C CG . MET B 2 229 ? 31.157 71.942 40.310 1.00 28.38 ? 477 MET B CG 1 ATOM 3374 S SD . MET B 2 229 ? 30.726 70.233 39.993 1.00 37.13 ? 477 MET B SD 1 ATOM 3375 C CE . MET B 2 229 ? 29.103 70.116 40.727 1.00 32.01 ? 477 MET B CE 1 ATOM 3376 N N . ASP B 2 230 ? 29.703 75.069 37.512 1.00 21.04 ? 478 ASP B N 1 ATOM 3377 C CA . ASP B 2 230 ? 28.753 75.874 36.769 1.00 22.09 ? 478 ASP B CA 1 ATOM 3378 C C . ASP B 2 230 ? 28.974 75.832 35.255 1.00 20.43 ? 478 ASP B C 1 ATOM 3379 O O . ASP B 2 230 ? 28.007 75.768 34.502 1.00 19.06 ? 478 ASP B O 1 ATOM 3380 C CB . ASP B 2 230 ? 28.776 77.329 37.245 1.00 23.60 ? 478 ASP B CB 1 ATOM 3381 C CG . ASP B 2 230 ? 28.262 77.478 38.666 1.00 29.74 ? 478 ASP B CG 1 ATOM 3382 O OD1 . ASP B 2 230 ? 27.560 76.554 39.184 1.00 35.51 ? 478 ASP B OD1 1 ATOM 3383 O OD2 . ASP B 2 230 ? 28.580 78.537 39.271 1.00 38.17 ? 478 ASP B OD2 1 ATOM 3384 N N . ALA B 2 231 ? 30.230 75.894 34.816 1.00 17.69 ? 479 ALA B N 1 ATOM 3385 C CA . ALA B 2 231 ? 30.545 75.818 33.396 1.00 17.07 ? 479 ALA B CA 1 ATOM 3386 C C . ALA B 2 231 ? 30.123 74.446 32.853 1.00 16.87 ? 479 ALA B C 1 ATOM 3387 O O . ALA B 2 231 ? 29.677 74.334 31.701 1.00 15.53 ? 479 ALA B O 1 ATOM 3388 C CB . ALA B 2 231 ? 32.068 76.045 33.163 1.00 17.85 ? 479 ALA B CB 1 ATOM 3389 N N . MET B 2 232 ? 30.288 73.404 33.691 1.00 16.21 ? 480 MET B N 1 ATOM 3390 C CA . MET B 2 232 ? 29.848 72.064 33.280 1.00 15.76 ? 480 MET B CA 1 ATOM 3391 C C . MET B 2 232 ? 28.340 72.045 33.041 1.00 15.87 ? 480 MET B C 1 ATOM 3392 O O . MET B 2 232 ? 27.874 71.477 32.054 1.00 15.06 ? 480 MET B O 1 ATOM 3393 C CB . MET B 2 232 ? 30.227 70.977 34.311 1.00 16.26 ? 480 MET B CB 1 ATOM 3394 C CG . MET B 2 232 ? 29.714 69.585 33.881 1.00 17.45 ? 480 MET B CG 1 ATOM 3395 S SD . MET B 2 232 ? 30.480 68.957 32.366 1.00 19.55 ? 480 MET B SD 1 ATOM 3396 C CE . MET B 2 232 ? 31.876 67.965 33.008 1.00 19.86 ? 480 MET B CE 1 ATOM 3397 N N . VAL B 2 233 ? 27.577 72.593 33.988 1.00 15.76 ? 481 VAL B N 1 ATOM 3398 C CA . VAL B 2 233 ? 26.131 72.638 33.831 1.00 17.12 ? 481 VAL B CA 1 ATOM 3399 C C . VAL B 2 233 ? 25.767 73.383 32.536 1.00 17.36 ? 481 VAL B C 1 ATOM 3400 O O . VAL B 2 233 ? 24.882 72.933 31.780 1.00 17.26 ? 481 VAL B O 1 ATOM 3401 C CB . VAL B 2 233 ? 25.452 73.292 35.055 1.00 17.11 ? 481 VAL B CB 1 ATOM 3402 C CG1 . VAL B 2 233 ? 23.949 73.472 34.793 1.00 19.19 ? 481 VAL B CG1 1 ATOM 3403 C CG2 . VAL B 2 233 ? 25.703 72.420 36.326 1.00 17.49 ? 481 VAL B CG2 1 ATOM 3404 N N . ARG B 2 234 ? 26.433 74.518 32.272 1.00 16.40 ? 482 ARG B N 1 ATOM 3405 C CA . ARG B 2 234 ? 26.116 75.305 31.077 1.00 17.44 ? 482 ARG B CA 1 ATOM 3406 C C . ARG B 2 234 ? 26.343 74.514 29.785 1.00 16.59 ? 482 ARG B C 1 ATOM 3407 O O . ARG B 2 234 ? 25.534 74.565 28.858 1.00 16.52 ? 482 ARG B O 1 ATOM 3408 C CB . ARG B 2 234 ? 26.961 76.586 31.059 1.00 18.23 ? 482 ARG B CB 1 ATOM 3409 C CG . ARG B 2 234 ? 26.694 77.506 29.876 1.00 24.20 ? 482 ARG B CG 1 ATOM 3410 C CD . ARG B 2 234 ? 27.485 78.826 30.073 1.00 30.53 ? 482 ARG B CD 1 ATOM 3411 N NE . ARG B 2 234 ? 27.535 79.662 28.864 1.00 36.48 ? 482 ARG B NE 1 ATOM 3412 C CZ . ARG B 2 234 ? 28.205 80.822 28.790 1.00 38.70 ? 482 ARG B CZ 1 ATOM 3413 N NH1 . ARG B 2 234 ? 28.892 81.275 29.838 1.00 36.13 ? 482 ARG B NH1 1 ATOM 3414 N NH2 . ARG B 2 234 ? 28.186 81.535 27.673 1.00 40.34 ? 482 ARG B NH2 1 ATOM 3415 N N . LEU B 2 235 ? 27.453 73.782 29.713 1.00 15.03 ? 483 LEU B N 1 ATOM 3416 C CA . LEU B 2 235 ? 27.713 72.969 28.518 1.00 14.34 ? 483 LEU B CA 1 ATOM 3417 C C . LEU B 2 235 ? 26.701 71.824 28.405 1.00 13.58 ? 483 LEU B C 1 ATOM 3418 O O . LEU B 2 235 ? 26.227 71.490 27.297 1.00 15.23 ? 483 LEU B O 1 ATOM 3419 C CB . LEU B 2 235 ? 29.151 72.393 28.507 1.00 14.30 ? 483 LEU B CB 1 ATOM 3420 C CG . LEU B 2 235 ? 29.510 71.543 27.258 1.00 16.35 ? 483 LEU B CG 1 ATOM 3421 C CD1 . LEU B 2 235 ? 29.248 72.279 25.937 1.00 19.10 ? 483 LEU B CD1 1 ATOM 3422 C CD2 . LEU B 2 235 ? 30.983 71.122 27.351 1.00 21.18 ? 483 LEU B CD2 1 ATOM 3423 N N . MET B 2 236 ? 26.407 71.177 29.539 1.00 14.12 ? 484 MET B N 1 ATOM 3424 C CA . MET B 2 236 ? 25.522 70.005 29.487 1.00 15.83 ? 484 MET B CA 1 ATOM 3425 C C . MET B 2 236 ? 24.075 70.419 29.147 1.00 16.06 ? 484 MET B C 1 ATOM 3426 O O . MET B 2 236 ? 23.322 69.620 28.643 1.00 17.45 ? 484 MET B O 1 ATOM 3427 C CB . MET B 2 236 ? 25.593 69.202 30.780 1.00 15.95 ? 484 MET B CB 1 ATOM 3428 C CG . MET B 2 236 ? 27.026 68.605 30.987 1.00 17.91 ? 484 MET B CG 1 ATOM 3429 S SD . MET B 2 236 ? 27.628 67.635 29.555 1.00 21.68 ? 484 MET B SD 1 ATOM 3430 C CE . MET B 2 236 ? 26.435 66.313 29.731 1.00 18.21 ? 484 MET B CE 1 ATOM 3431 N N . ARG B 2 237 ? 23.720 71.668 29.439 1.00 16.58 ? 485 ARG B N 1 ATOM 3432 C CA . ARG B 2 237 ? 22.422 72.227 29.043 1.00 17.92 ? 485 ARG B CA 1 ATOM 3433 C C . ARG B 2 237 ? 22.452 72.914 27.684 1.00 17.10 ? 485 ARG B C 1 ATOM 3434 O O . ARG B 2 237 ? 21.457 73.564 27.294 1.00 16.86 ? 485 ARG B O 1 ATOM 3435 C CB . ARG B 2 237 ? 21.993 73.309 30.052 1.00 18.71 ? 485 ARG B CB 1 ATOM 3436 C CG . ARG B 2 237 ? 21.658 72.828 31.415 1.00 22.92 ? 485 ARG B CG 1 ATOM 3437 C CD . ARG B 2 237 ? 20.504 71.925 31.283 1.00 30.34 ? 485 ARG B CD 1 ATOM 3438 N NE . ARG B 2 237 ? 19.453 72.264 32.214 1.00 32.74 ? 485 ARG B NE 1 ATOM 3439 C CZ . ARG B 2 237 ? 18.289 71.632 32.197 1.00 34.35 ? 485 ARG B CZ 1 ATOM 3440 N NH1 . ARG B 2 237 ? 18.106 70.650 31.297 1.00 33.80 ? 485 ARG B NH1 1 ATOM 3441 N NH2 . ARG B 2 237 ? 17.345 71.964 33.075 1.00 36.96 ? 485 ARG B NH2 1 ATOM 3442 N N . TYR B 2 238 ? 23.555 72.803 26.951 1.00 15.87 ? 486 TYR B N 1 ATOM 3443 C CA . TYR B 2 238 ? 23.732 73.664 25.776 1.00 15.67 ? 486 TYR B CA 1 ATOM 3444 C C . TYR B 2 238 ? 22.855 73.310 24.576 1.00 15.92 ? 486 TYR B C 1 ATOM 3445 O O . TYR B 2 238 ? 22.853 72.183 24.094 1.00 15.67 ? 486 TYR B O 1 ATOM 3446 C CB . TYR B 2 238 ? 25.198 73.670 25.328 1.00 16.08 ? 486 TYR B CB 1 ATOM 3447 C CG . TYR B 2 238 ? 25.442 74.517 24.106 1.00 16.89 ? 486 TYR B CG 1 ATOM 3448 C CD1 . TYR B 2 238 ? 25.284 75.925 24.144 1.00 19.49 ? 486 TYR B CD1 1 ATOM 3449 C CD2 . TYR B 2 238 ? 25.850 73.934 22.925 1.00 17.53 ? 486 TYR B CD2 1 ATOM 3450 C CE1 . TYR B 2 238 ? 25.525 76.719 23.005 1.00 19.89 ? 486 TYR B CE1 1 ATOM 3451 C CE2 . TYR B 2 238 ? 26.084 74.727 21.778 1.00 20.08 ? 486 TYR B CE2 1 ATOM 3452 C CZ . TYR B 2 238 ? 25.925 76.107 21.850 1.00 19.52 ? 486 TYR B CZ 1 ATOM 3453 O OH . TYR B 2 238 ? 26.166 76.851 20.726 1.00 22.16 ? 486 TYR B OH 1 ATOM 3454 N N . ASN B 2 239 ? 22.111 74.304 24.084 1.00 16.58 ? 487 ASN B N 1 ATOM 3455 C CA . ASN B 2 239 ? 21.377 74.162 22.830 1.00 16.81 ? 487 ASN B CA 1 ATOM 3456 C C . ASN B 2 239 ? 21.152 75.580 22.321 1.00 17.87 ? 487 ASN B C 1 ATOM 3457 O O . ASN B 2 239 ? 20.416 76.327 22.932 1.00 18.88 ? 487 ASN B O 1 ATOM 3458 C CB . ASN B 2 239 ? 20.030 73.467 23.047 1.00 16.37 ? 487 ASN B CB 1 ATOM 3459 C CG . ASN B 2 239 ? 19.359 73.131 21.738 1.00 16.82 ? 487 ASN B CG 1 ATOM 3460 O OD1 . ASN B 2 239 ? 19.572 73.835 20.752 1.00 16.15 ? 487 ASN B OD1 1 ATOM 3461 N ND2 . ASN B 2 239 ? 18.614 72.034 21.685 1.00 15.63 ? 487 ASN B ND2 1 ATOM 3462 N N . ASP B 2 240 ? 21.827 75.945 21.247 1.00 18.65 ? 488 ASP B N 1 ATOM 3463 C CA . ASP B 2 240 ? 21.591 77.295 20.646 1.00 19.52 ? 488 ASP B CA 1 ATOM 3464 C C . ASP B 2 240 ? 21.377 77.019 19.174 1.00 18.51 ? 488 ASP B C 1 ATOM 3465 O O . ASP B 2 240 ? 22.039 77.596 18.303 1.00 19.28 ? 488 ASP B O 1 ATOM 3466 C CB . ASP B 2 240 ? 22.789 78.219 20.910 1.00 19.60 ? 488 ASP B CB 1 ATOM 3467 C CG . ASP B 2 240 ? 22.532 79.689 20.468 1.00 24.02 ? 488 ASP B CG 1 ATOM 3468 O OD1 . ASP B 2 240 ? 21.358 80.100 20.386 1.00 25.91 ? 488 ASP B OD1 1 ATOM 3469 O OD2 . ASP B 2 240 ? 23.520 80.418 20.247 1.00 25.84 ? 488 ASP B OD2 1 ATOM 3470 N N . PHE B 2 241 ? 20.483 76.062 18.884 1.00 18.20 ? 489 PHE B N 1 ATOM 3471 C CA . PHE B 2 241 ? 20.444 75.459 17.549 1.00 18.56 ? 489 PHE B CA 1 ATOM 3472 C C . PHE B 2 241 ? 20.110 76.474 16.455 1.00 19.69 ? 489 PHE B C 1 ATOM 3473 O O . PHE B 2 241 ? 20.445 76.250 15.301 1.00 19.64 ? 489 PHE B O 1 ATOM 3474 C CB . PHE B 2 241 ? 19.468 74.279 17.462 1.00 18.07 ? 489 PHE B CB 1 ATOM 3475 C CG . PHE B 2 241 ? 18.012 74.691 17.412 1.00 18.84 ? 489 PHE B CG 1 ATOM 3476 C CD1 . PHE B 2 241 ? 17.332 75.062 18.579 1.00 18.82 ? 489 PHE B CD1 1 ATOM 3477 C CD2 . PHE B 2 241 ? 17.326 74.688 16.202 1.00 20.57 ? 489 PHE B CD2 1 ATOM 3478 C CE1 . PHE B 2 241 ? 15.947 75.433 18.533 1.00 19.65 ? 489 PHE B CE1 1 ATOM 3479 C CE2 . PHE B 2 241 ? 15.960 75.042 16.142 1.00 21.16 ? 489 PHE B CE2 1 ATOM 3480 C CZ . PHE B 2 241 ? 15.286 75.423 17.294 1.00 19.14 ? 489 PHE B CZ 1 ATOM 3481 N N . LEU B 2 242 ? 19.443 77.570 16.817 1.00 20.58 ? 490 LEU B N 1 ATOM 3482 C CA . LEU B 2 242 ? 19.091 78.537 15.752 1.00 23.26 ? 490 LEU B CA 1 ATOM 3483 C C . LEU B 2 242 ? 20.283 79.317 15.260 1.00 23.92 ? 490 LEU B C 1 ATOM 3484 O O . LEU B 2 242 ? 20.250 79.881 14.153 1.00 25.42 ? 490 LEU B O 1 ATOM 3485 C CB . LEU B 2 242 ? 17.998 79.510 16.192 1.00 22.50 ? 490 LEU B CB 1 ATOM 3486 C CG . LEU B 2 242 ? 16.597 78.919 16.299 1.00 25.06 ? 490 LEU B CG 1 ATOM 3487 C CD1 . LEU B 2 242 ? 15.663 79.978 16.837 1.00 28.57 ? 490 LEU B CD1 1 ATOM 3488 C CD2 . LEU B 2 242 ? 16.115 78.322 14.949 1.00 25.61 ? 490 LEU B CD2 1 ATOM 3489 N N . HIS B 2 243 ? 21.347 79.349 16.058 1.00 23.80 ? 491 HIS B N 1 ATOM 3490 C CA . HIS B 2 243 ? 22.491 80.194 15.754 1.00 24.26 ? 491 HIS B CA 1 ATOM 3491 C C . HIS B 2 243 ? 23.812 79.454 15.629 1.00 24.21 ? 491 HIS B C 1 ATOM 3492 O O . HIS B 2 243 ? 24.786 79.990 15.103 1.00 25.21 ? 491 HIS B O 1 ATOM 3493 C CB . HIS B 2 243 ? 22.585 81.278 16.822 1.00 25.10 ? 491 HIS B CB 1 ATOM 3494 C CG . HIS B 2 243 ? 21.312 82.047 16.976 1.00 29.46 ? 491 HIS B CG 1 ATOM 3495 N ND1 . HIS B 2 243 ? 20.500 81.936 18.084 1.00 32.37 ? 491 HIS B ND1 1 ATOM 3496 C CD2 . HIS B 2 243 ? 20.669 82.876 16.115 1.00 32.57 ? 491 HIS B CD2 1 ATOM 3497 C CE1 . HIS B 2 243 ? 19.434 82.704 17.920 1.00 34.54 ? 491 HIS B CE1 1 ATOM 3498 N NE2 . HIS B 2 243 ? 19.513 83.281 16.735 1.00 33.94 ? 491 HIS B NE2 1 ATOM 3499 N N . ASP B 2 244 ? 23.855 78.222 16.102 1.00 22.05 ? 492 ASP B N 1 ATOM 3500 C CA . ASP B 2 244 ? 25.115 77.474 16.098 1.00 22.15 ? 492 ASP B CA 1 ATOM 3501 C C . ASP B 2 244 ? 25.286 76.770 14.763 1.00 21.53 ? 492 ASP B C 1 ATOM 3502 O O . ASP B 2 244 ? 24.435 75.939 14.363 1.00 21.64 ? 492 ASP B O 1 ATOM 3503 C CB . ASP B 2 244 ? 25.085 76.459 17.248 1.00 21.52 ? 492 ASP B CB 1 ATOM 3504 C CG . ASP B 2 244 ? 26.457 75.847 17.536 1.00 22.65 ? 492 ASP B CG 1 ATOM 3505 O OD1 . ASP B 2 244 ? 27.301 75.773 16.620 1.00 20.35 ? 492 ASP B OD1 1 ATOM 3506 O OD2 . ASP B 2 244 ? 26.678 75.454 18.704 1.00 26.03 ? 492 ASP B OD2 1 ATOM 3507 N N . PRO B 2 245 ? 26.387 77.055 14.061 1.00 22.00 ? 493 PRO B N 1 ATOM 3508 C CA . PRO B 2 245 ? 26.610 76.397 12.772 1.00 22.24 ? 493 PRO B CA 1 ATOM 3509 C C . PRO B 2 245 ? 26.701 74.884 12.913 1.00 21.35 ? 493 PRO B C 1 ATOM 3510 O O . PRO B 2 245 ? 26.344 74.172 11.994 1.00 20.30 ? 493 PRO B O 1 ATOM 3511 C CB . PRO B 2 245 ? 27.979 76.926 12.297 1.00 23.29 ? 493 PRO B CB 1 ATOM 3512 C CG . PRO B 2 245 ? 28.326 78.038 13.195 1.00 25.35 ? 493 PRO B CG 1 ATOM 3513 C CD . PRO B 2 245 ? 27.482 77.967 14.439 1.00 22.86 ? 493 PRO B CD 1 ATOM 3514 N N . LEU B 2 246 ? 27.162 74.394 14.070 1.00 19.07 ? 494 LEU B N 1 ATOM 3515 C CA . LEU B 2 246 ? 27.244 72.933 14.271 1.00 19.03 ? 494 LEU B CA 1 ATOM 3516 C C . LEU B 2 246 ? 25.873 72.256 14.372 1.00 19.72 ? 494 LEU B C 1 ATOM 3517 O O . LEU B 2 246 ? 25.798 71.006 14.310 1.00 20.06 ? 494 LEU B O 1 ATOM 3518 C CB . LEU B 2 246 ? 28.089 72.602 15.505 1.00 17.96 ? 494 LEU B CB 1 ATOM 3519 C CG . LEU B 2 246 ? 29.547 73.038 15.394 1.00 17.79 ? 494 LEU B CG 1 ATOM 3520 C CD1 . LEU B 2 246 ? 30.358 72.666 16.658 1.00 19.26 ? 494 LEU B CD1 1 ATOM 3521 C CD2 . LEU B 2 246 ? 30.194 72.426 14.163 1.00 19.51 ? 494 LEU B CD2 1 ATOM 3522 N N . SER B 2 247 ? 24.816 73.058 14.567 1.00 19.80 ? 495 SER B N 1 ATOM 3523 C CA . SER B 2 247 ? 23.461 72.530 14.632 1.00 20.36 ? 495 SER B CA 1 ATOM 3524 C C . SER B 2 247 ? 22.757 72.439 13.269 1.00 22.41 ? 495 SER B C 1 ATOM 3525 O O . SER B 2 247 ? 21.631 71.950 13.191 1.00 21.96 ? 495 SER B O 1 ATOM 3526 C CB . SER B 2 247 ? 22.586 73.269 15.643 1.00 20.42 ? 495 SER B CB 1 ATOM 3527 O OG . SER B 2 247 ? 23.171 73.274 16.943 1.00 20.93 ? 495 SER B OG 1 ATOM 3528 N N . LEU B 2 248 ? 23.422 72.897 12.204 1.00 23.10 ? 496 LEU B N 1 ATOM 3529 C CA . LEU B 2 248 ? 22.819 72.851 10.853 1.00 25.56 ? 496 LEU B CA 1 ATOM 3530 C C . LEU B 2 248 ? 22.776 71.426 10.313 1.00 26.70 ? 496 LEU B C 1 ATOM 3531 O O . LEU B 2 248 ? 23.761 70.685 10.403 1.00 27.05 ? 496 LEU B O 1 ATOM 3532 C CB . LEU B 2 248 ? 23.590 73.736 9.873 1.00 24.92 ? 496 LEU B CB 1 ATOM 3533 C CG . LEU B 2 248 ? 23.552 75.229 10.174 1.00 27.35 ? 496 LEU B CG 1 ATOM 3534 C CD1 . LEU B 2 248 ? 24.657 75.993 9.401 1.00 30.33 ? 496 LEU B CD1 1 ATOM 3535 C CD2 . LEU B 2 248 ? 22.188 75.799 9.816 1.00 26.39 ? 496 LEU B CD2 1 ATOM 3536 N N . CYS B 2 249 ? 21.638 71.041 9.755 1.00 27.76 ? 497 CYS B N 1 ATOM 3537 C CA . CYS B 2 249 ? 21.504 69.758 9.101 1.00 30.03 ? 497 CYS B CA 1 ATOM 3538 C C . CYS B 2 249 ? 21.312 70.113 7.629 1.00 30.08 ? 497 CYS B C 1 ATOM 3539 O O . CYS B 2 249 ? 20.270 70.621 7.253 1.00 28.33 ? 497 CYS B O 1 ATOM 3540 C CB . CYS B 2 249 ? 20.278 69.009 9.652 1.00 30.92 ? 497 CYS B CB 1 ATOM 3541 S SG . CYS B 2 249 ? 19.513 67.716 8.550 1.00 40.42 ? 497 CYS B SG 1 ATOM 3542 N N . GLU B 2 250 ? 22.325 69.875 6.807 1.00 30.27 ? 498 GLU B N 1 ATOM 3543 C CA . GLU B 2 250 ? 22.237 70.317 5.408 1.00 32.61 ? 498 GLU B CA 1 ATOM 3544 C C . GLU B 2 250 ? 21.129 69.613 4.611 1.00 32.20 ? 498 GLU B C 1 ATOM 3545 O O . GLU B 2 250 ? 20.588 70.171 3.645 1.00 33.72 ? 498 GLU B O 1 ATOM 3546 C CB . GLU B 2 250 ? 23.604 70.228 4.731 1.00 33.10 ? 498 GLU B CB 1 ATOM 3547 C CG . GLU B 2 250 ? 24.603 71.202 5.356 1.00 37.10 ? 498 GLU B CG 1 ATOM 3548 C CD . GLU B 2 250 ? 24.206 72.667 5.168 1.00 41.71 ? 498 GLU B CD 1 ATOM 3549 O OE1 . GLU B 2 250 ? 23.808 73.036 4.035 1.00 42.35 ? 498 GLU B OE1 1 ATOM 3550 O OE2 . GLU B 2 250 ? 24.281 73.446 6.150 1.00 42.13 ? 498 GLU B OE2 1 ATOM 3551 N N . ALA B 2 251 ? 20.768 68.409 5.034 1.00 32.20 ? 499 ALA B N 1 ATOM 3552 C CA . ALA B 2 251 ? 19.715 67.651 4.369 1.00 32.05 ? 499 ALA B CA 1 ATOM 3553 C C . ALA B 2 251 ? 18.307 68.026 4.834 1.00 32.07 ? 499 ALA B C 1 ATOM 3554 O O . ALA B 2 251 ? 17.334 67.501 4.304 1.00 32.98 ? 499 ALA B O 1 ATOM 3555 C CB . ALA B 2 251 ? 19.961 66.147 4.522 1.00 32.34 ? 499 ALA B CB 1 ATOM 3556 N N . CYS B 2 252 ? 18.191 68.908 5.828 1.00 30.73 ? 500 CYS B N 1 ATOM 3557 C CA . CYS B 2 252 ? 16.886 69.274 6.395 1.00 30.34 ? 500 CYS B CA 1 ATOM 3558 C C . CYS B 2 252 ? 16.393 70.615 5.867 1.00 30.00 ? 500 CYS B C 1 ATOM 3559 O O . CYS B 2 252 ? 17.184 71.494 5.494 1.00 29.32 ? 500 CYS B O 1 ATOM 3560 C CB . CYS B 2 252 ? 16.968 69.404 7.924 1.00 30.46 ? 500 CYS B CB 1 ATOM 3561 S SG . CYS B 2 252 ? 17.417 67.876 8.830 1.00 31.71 ? 500 CYS B SG 1 ATOM 3562 N N . ASN B 2 253 ? 15.082 70.792 5.916 1.00 29.53 ? 501 ASN B N 1 ATOM 3563 C CA . ASN B 2 253 ? 14.476 72.080 5.671 1.00 29.43 ? 501 ASN B CA 1 ATOM 3564 C C . ASN B 2 253 ? 13.447 72.263 6.753 1.00 28.02 ? 501 ASN B C 1 ATOM 3565 O O . ASN B 2 253 ? 12.462 71.508 6.789 1.00 28.43 ? 501 ASN B O 1 ATOM 3566 C CB . ASN B 2 253 ? 13.805 72.108 4.286 1.00 30.97 ? 501 ASN B CB 1 ATOM 3567 C CG . ASN B 2 253 ? 13.237 73.478 3.940 1.00 34.24 ? 501 ASN B CG 1 ATOM 3568 O OD1 . ASN B 2 253 ? 13.533 74.473 4.602 1.00 38.65 ? 501 ASN B OD1 1 ATOM 3569 N ND2 . ASN B 2 253 ? 12.417 73.533 2.889 1.00 36.94 ? 501 ASN B ND2 1 ATOM 3570 N N . PRO B 2 254 ? 13.675 73.225 7.665 1.00 26.51 ? 502 PRO B N 1 ATOM 3571 C CA . PRO B 2 254 ? 14.787 74.183 7.720 1.00 25.87 ? 502 PRO B CA 1 ATOM 3572 C C . PRO B 2 254 ? 16.105 73.508 8.104 1.00 24.59 ? 502 PRO B C 1 ATOM 3573 O O . PRO B 2 254 ? 16.082 72.364 8.561 1.00 23.69 ? 502 PRO B O 1 ATOM 3574 C CB . PRO B 2 254 ? 14.392 75.106 8.858 1.00 25.63 ? 502 PRO B CB 1 ATOM 3575 C CG . PRO B 2 254 ? 13.482 74.321 9.709 1.00 26.43 ? 502 PRO B CG 1 ATOM 3576 C CD . PRO B 2 254 ? 12.786 73.336 8.836 1.00 26.85 ? 502 PRO B CD 1 ATOM 3577 N N . LYS B 2 255 ? 17.234 74.195 7.947 1.00 23.49 ? 503 LYS B N 1 ATOM 3578 C CA . LYS B 2 255 ? 18.517 73.540 8.238 1.00 23.80 ? 503 LYS B CA 1 ATOM 3579 C C . LYS B 2 255 ? 18.849 73.441 9.744 1.00 23.49 ? 503 LYS B C 1 ATOM 3580 O O . LYS B 2 255 ? 19.322 72.386 10.179 1.00 23.52 ? 503 LYS B O 1 ATOM 3581 C CB . LYS B 2 255 ? 19.681 74.166 7.461 1.00 24.52 ? 503 LYS B CB 1 ATOM 3582 C CG . LYS B 2 255 ? 19.566 74.036 5.923 1.00 26.31 ? 503 LYS B CG 1 ATOM 3583 C CD . LYS B 2 255 ? 20.903 74.394 5.297 1.00 30.43 ? 503 LYS B CD 1 ATOM 3584 C CE . LYS B 2 255 ? 20.814 74.580 3.790 1.00 35.58 ? 503 LYS B CE 1 ATOM 3585 N NZ . LYS B 2 255 ? 20.190 73.400 3.171 1.00 38.28 ? 503 LYS B NZ 1 ATOM 3586 N N . PRO B 2 256 ? 18.630 74.521 10.530 1.00 23.36 ? 504 PRO B N 1 ATOM 3587 C CA . PRO B 2 256 ? 18.948 74.323 11.958 1.00 22.65 ? 504 PRO B CA 1 ATOM 3588 C C . PRO B 2 256 ? 18.041 73.256 12.558 1.00 22.48 ? 504 PRO B C 1 ATOM 3589 O O . PRO B 2 256 ? 16.823 73.267 12.327 1.00 21.35 ? 504 PRO B O 1 ATOM 3590 C CB . PRO B 2 256 ? 18.648 75.693 12.592 1.00 22.60 ? 504 PRO B CB 1 ATOM 3591 C CG . PRO B 2 256 ? 18.710 76.676 11.421 1.00 25.11 ? 504 PRO B CG 1 ATOM 3592 C CD . PRO B 2 256 ? 18.158 75.896 10.259 1.00 23.14 ? 504 PRO B CD 1 ATOM 3593 N N . ASN B 2 257 ? 18.618 72.351 13.353 1.00 20.52 ? 505 ASN B N 1 ATOM 3594 C CA . ASN B 2 257 ? 17.791 71.314 13.957 1.00 18.69 ? 505 ASN B CA 1 ATOM 3595 C C . ASN B 2 257 ? 18.094 71.200 15.459 1.00 18.39 ? 505 ASN B C 1 ATOM 3596 O O . ASN B 2 257 ? 19.248 71.105 15.872 1.00 17.41 ? 505 ASN B O 1 ATOM 3597 C CB . ASN B 2 257 ? 17.961 69.983 13.212 1.00 18.95 ? 505 ASN B CB 1 ATOM 3598 C CG . ASN B 2 257 ? 16.915 68.955 13.616 1.00 20.79 ? 505 ASN B CG 1 ATOM 3599 O OD1 . ASN B 2 257 ? 16.921 68.471 14.736 1.00 18.01 ? 505 ASN B OD1 1 ATOM 3600 N ND2 . ASN B 2 257 ? 16.012 68.615 12.698 1.00 19.71 ? 505 ASN B ND2 1 ATOM 3601 N N . ALA B 2 258 ? 17.038 71.228 16.252 1.00 17.37 ? 506 ALA B N 1 ATOM 3602 C CA . ALA B 2 258 ? 17.152 71.312 17.686 1.00 17.55 ? 506 ALA B CA 1 ATOM 3603 C C . ALA B 2 258 ? 17.585 69.980 18.314 1.00 16.97 ? 506 ALA B C 1 ATOM 3604 O O . ALA B 2 258 ? 17.793 69.918 19.539 1.00 17.62 ? 506 ALA B O 1 ATOM 3605 C CB . ALA B 2 258 ? 15.820 71.783 18.269 1.00 18.48 ? 506 ALA B CB 1 ATOM 3606 N N . GLU B 2 259 ? 17.737 68.935 17.499 1.00 16.84 ? 507 GLU B N 1 ATOM 3607 C CA . GLU B 2 259 ? 18.286 67.638 17.976 1.00 17.70 ? 507 GLU B CA 1 ATOM 3608 C C . GLU B 2 259 ? 19.824 67.724 18.058 1.00 18.45 ? 507 GLU B C 1 ATOM 3609 O O . GLU B 2 259 ? 20.505 66.897 18.709 1.00 18.66 ? 507 GLU B O 1 ATOM 3610 C CB . GLU B 2 259 ? 17.916 66.546 16.944 1.00 19.04 ? 507 GLU B CB 1 ATOM 3611 C CG . GLU B 2 259 ? 18.603 65.174 17.142 1.00 21.20 ? 507 GLU B CG 1 ATOM 3612 C CD . GLU B 2 259 ? 17.943 64.296 18.203 1.00 24.52 ? 507 GLU B CD 1 ATOM 3613 O OE1 . GLU B 2 259 ? 17.019 64.760 18.913 1.00 23.79 ? 507 GLU B OE1 1 ATOM 3614 O OE2 . GLU B 2 259 ? 18.389 63.122 18.339 1.00 25.51 ? 507 GLU B OE2 1 ATOM 3615 N N . ASN B 2 260 ? 20.376 68.712 17.369 1.00 18.17 ? 508 ASN B N 1 ATOM 3616 C CA . ASN B 2 260 ? 21.831 68.754 17.145 1.00 18.99 ? 508 ASN B CA 1 ATOM 3617 C C . ASN B 2 260 ? 22.466 69.674 18.176 1.00 18.75 ? 508 ASN B C 1 ATOM 3618 O O . ASN B 2 260 ? 22.893 70.788 17.861 1.00 19.17 ? 508 ASN B O 1 ATOM 3619 C CB . ASN B 2 260 ? 22.139 69.222 15.720 1.00 20.40 ? 508 ASN B CB 1 ATOM 3620 C CG . ASN B 2 260 ? 21.805 68.166 14.655 1.00 23.06 ? 508 ASN B CG 1 ATOM 3621 O OD1 . ASN B 2 260 ? 21.677 66.965 14.952 1.00 23.36 ? 508 ASN B OD1 1 ATOM 3622 N ND2 . ASN B 2 260 ? 21.651 68.620 13.405 1.00 20.76 ? 508 ASN B ND2 1 ATOM 3623 N N . ALA B 2 261 ? 22.474 69.224 19.431 1.00 16.76 ? 509 ALA B N 1 ATOM 3624 C CA . ALA B 2 261 ? 22.859 70.045 20.570 1.00 16.01 ? 509 ALA B CA 1 ATOM 3625 C C . ALA B 2 261 ? 23.288 69.089 21.670 1.00 15.88 ? 509 ALA B C 1 ATOM 3626 O O . ALA B 2 261 ? 22.988 67.876 21.592 1.00 15.23 ? 509 ALA B O 1 ATOM 3627 C CB . ALA B 2 261 ? 21.666 70.859 21.051 1.00 17.73 ? 509 ALA B CB 1 ATOM 3628 N N . ILE B 2 262 ? 23.956 69.604 22.696 1.00 15.10 ? 510 ILE B N 1 ATOM 3629 C CA . ILE B 2 262 ? 24.266 68.763 23.837 1.00 15.91 ? 510 ILE B CA 1 ATOM 3630 C C . ILE B 2 262 ? 22.978 68.329 24.562 1.00 17.31 ? 510 ILE B C 1 ATOM 3631 O O . ILE B 2 262 ? 22.867 67.155 24.969 1.00 17.53 ? 510 ILE B O 1 ATOM 3632 C CB . ILE B 2 262 ? 25.266 69.435 24.829 1.00 16.42 ? 510 ILE B CB 1 ATOM 3633 C CG1 . ILE B 2 262 ? 26.523 69.896 24.088 1.00 15.03 ? 510 ILE B CG1 1 ATOM 3634 C CG2 . ILE B 2 262 ? 25.635 68.449 25.955 1.00 16.95 ? 510 ILE B CG2 1 ATOM 3635 C CD1 . ILE B 2 262 ? 27.212 68.776 23.251 1.00 17.08 ? 510 ILE B CD1 1 ATOM 3636 N N . SER B 2 263 ? 22.005 69.257 24.693 1.00 17.95 ? 511 SER B N 1 ATOM 3637 C CA . SER B 2 263 ? 20.683 68.969 25.317 1.00 16.97 ? 511 SER B CA 1 ATOM 3638 C C . SER B 2 263 ? 19.557 69.201 24.288 1.00 16.67 ? 511 SER B C 1 ATOM 3639 O O . SER B 2 263 ? 19.128 70.352 24.080 1.00 15.71 ? 511 SER B O 1 ATOM 3640 C CB . SER B 2 263 ? 20.463 69.847 26.571 1.00 16.61 ? 511 SER B CB 1 ATOM 3641 O OG . SER B 2 263 ? 19.305 69.449 27.328 1.00 16.61 ? 511 SER B OG 1 ATOM 3642 N N . ALA B 2 264 ? 19.100 68.117 23.637 1.00 15.66 ? 512 ALA B N 1 ATOM 3643 C CA . ALA B 2 264 ? 18.154 68.234 22.491 1.00 16.19 ? 512 ALA B CA 1 ATOM 3644 C C . ALA B 2 264 ? 16.816 68.890 22.901 1.00 15.72 ? 512 ALA B C 1 ATOM 3645 O O . ALA B 2 264 ? 16.386 68.737 24.033 1.00 14.64 ? 512 ALA B O 1 ATOM 3646 C CB . ALA B 2 264 ? 17.885 66.845 21.891 1.00 16.22 ? 512 ALA B CB 1 ATOM 3647 N N . ARG B 2 265 ? 16.171 69.623 21.976 1.00 15.61 ? 513 ARG B N 1 ATOM 3648 C CA . ARG B 2 265 ? 14.800 70.151 22.227 1.00 15.89 ? 513 ARG B CA 1 ATOM 3649 C C . ARG B 2 265 ? 14.006 69.833 20.955 1.00 17.42 ? 513 ARG B C 1 ATOM 3650 O O . ARG B 2 265 ? 13.719 70.725 20.158 1.00 17.29 ? 513 ARG B O 1 ATOM 3651 C CB . ARG B 2 265 ? 14.815 71.673 22.494 1.00 15.67 ? 513 ARG B CB 1 ATOM 3652 C CG . ARG B 2 265 ? 15.289 72.090 23.890 1.00 16.10 ? 513 ARG B CG 1 ATOM 3653 C CD . ARG B 2 265 ? 14.247 71.773 24.994 1.00 16.83 ? 513 ARG B CD 1 ATOM 3654 N NE . ARG B 2 265 ? 12.899 72.314 24.692 1.00 16.62 ? 513 ARG B NE 1 ATOM 3655 C CZ . ARG B 2 265 ? 12.495 73.556 24.978 1.00 17.54 ? 513 ARG B CZ 1 ATOM 3656 N NH1 . ARG B 2 265 ? 13.287 74.385 25.639 1.00 16.18 ? 513 ARG B NH1 1 ATOM 3657 N NH2 . ARG B 2 265 ? 11.260 73.949 24.624 1.00 18.09 ? 513 ARG B NH2 1 ATOM 3658 N N . SER B 2 266 ? 13.664 68.572 20.767 1.00 16.77 ? 514 SER B N 1 ATOM 3659 C CA . SER B 2 266 ? 13.030 68.136 19.505 1.00 17.82 ? 514 SER B CA 1 ATOM 3660 C C . SER B 2 266 ? 11.629 68.763 19.346 1.00 18.27 ? 514 SER B C 1 ATOM 3661 O O . SER B 2 266 ? 11.094 68.793 18.234 1.00 19.15 ? 514 SER B O 1 ATOM 3662 C CB . SER B 2 266 ? 12.920 66.618 19.455 1.00 18.60 ? 514 SER B CB 1 ATOM 3663 O OG . SER B 2 266 ? 14.229 66.014 19.417 1.00 18.07 ? 514 SER B OG 1 ATOM 3664 N N . ASP B 2 267 ? 11.061 69.235 20.441 1.00 17.79 ? 515 ASP B N 1 ATOM 3665 C CA . ASP B 2 267 ? 9.724 69.856 20.413 1.00 18.95 ? 515 ASP B CA 1 ATOM 3666 C C . ASP B 2 267 ? 9.758 71.156 19.611 1.00 19.92 ? 515 ASP B C 1 ATOM 3667 O O . ASP B 2 267 ? 8.707 71.626 19.115 1.00 21.16 ? 515 ASP B O 1 ATOM 3668 C CB . ASP B 2 267 ? 9.237 70.125 21.835 1.00 18.55 ? 515 ASP B CB 1 ATOM 3669 C CG . ASP B 2 267 ? 10.196 71.035 22.637 1.00 20.16 ? 515 ASP B CG 1 ATOM 3670 O OD1 . ASP B 2 267 ? 11.380 70.630 22.909 1.00 18.66 ? 515 ASP B OD1 1 ATOM 3671 O OD2 . ASP B 2 267 ? 9.764 72.144 22.994 1.00 21.23 ? 515 ASP B OD2 1 ATOM 3672 N N . LEU B 2 268 ? 10.957 71.732 19.481 1.00 18.99 ? 516 LEU B N 1 ATOM 3673 C CA . LEU B 2 268 ? 11.146 73.021 18.777 1.00 19.39 ? 516 LEU B CA 1 ATOM 3674 C C . LEU B 2 268 ? 11.358 72.909 17.272 1.00 20.24 ? 516 LEU B C 1 ATOM 3675 O O . LEU B 2 268 ? 11.360 73.937 16.569 1.00 21.36 ? 516 LEU B O 1 ATOM 3676 C CB . LEU B 2 268 ? 12.277 73.841 19.421 1.00 19.17 ? 516 LEU B CB 1 ATOM 3677 C CG . LEU B 2 268 ? 12.019 74.217 20.900 1.00 19.28 ? 516 LEU B CG 1 ATOM 3678 C CD1 . LEU B 2 268 ? 13.205 74.958 21.528 1.00 18.37 ? 516 LEU B CD1 1 ATOM 3679 C CD2 . LEU B 2 268 ? 10.691 75.029 21.096 1.00 19.59 ? 516 LEU B CD2 1 ATOM 3680 N N . ASN B 2 269 ? 11.510 71.695 16.752 1.00 19.61 ? 517 ASN B N 1 ATOM 3681 C CA . ASN B 2 269 ? 11.642 71.525 15.317 1.00 20.25 ? 517 ASN B CA 1 ATOM 3682 C C . ASN B 2 269 ? 10.232 71.657 14.718 1.00 21.89 ? 517 ASN B C 1 ATOM 3683 O O . ASN B 2 269 ? 9.258 71.262 15.349 1.00 22.02 ? 517 ASN B O 1 ATOM 3684 C CB . ASN B 2 269 ? 12.171 70.130 15.000 1.00 20.33 ? 517 ASN B CB 1 ATOM 3685 C CG . ASN B 2 269 ? 13.675 70.000 15.244 1.00 19.62 ? 517 ASN B CG 1 ATOM 3686 O OD1 . ASN B 2 269 ? 14.414 70.973 15.148 1.00 18.21 ? 517 ASN B OD1 1 ATOM 3687 N ND2 . ASN B 2 269 ? 14.116 68.778 15.561 1.00 17.50 ? 517 ASN B ND2 1 ATOM 3688 N N . PRO B 2 270 ? 10.114 72.278 13.536 1.00 23.07 ? 518 PRO B N 1 ATOM 3689 C CA . PRO B 2 270 ? 8.746 72.383 12.979 1.00 23.66 ? 518 PRO B CA 1 ATOM 3690 C C . PRO B 2 270 ? 8.098 71.070 12.553 1.00 24.28 ? 518 PRO B C 1 ATOM 3691 O O . PRO B 2 270 ? 8.749 70.187 12.005 1.00 24.26 ? 518 PRO B O 1 ATOM 3692 C CB . PRO B 2 270 ? 8.933 73.313 11.776 1.00 24.22 ? 518 PRO B CB 1 ATOM 3693 C CG . PRO B 2 270 ? 10.367 73.085 11.346 1.00 24.56 ? 518 PRO B CG 1 ATOM 3694 C CD . PRO B 2 270 ? 11.112 72.962 12.695 1.00 22.85 ? 518 PRO B CD 1 ATOM 3695 N N . ALA B 2 271 ? 6.791 70.953 12.780 1.00 26.30 ? 519 ALA B N 1 ATOM 3696 C CA . ALA B 2 271 ? 6.069 69.739 12.432 1.00 27.74 ? 519 ALA B CA 1 ATOM 3697 C C . ALA B 2 271 ? 6.009 69.502 10.921 1.00 29.05 ? 519 ALA B C 1 ATOM 3698 O O . ALA B 2 271 ? 5.897 68.369 10.485 1.00 29.92 ? 519 ALA B O 1 ATOM 3699 C CB . ALA B 2 271 ? 4.660 69.769 13.023 1.00 28.70 ? 519 ALA B CB 1 ATOM 3700 N N . ASN B 2 272 ? 6.114 70.566 10.129 1.00 30.64 ? 520 ASN B N 1 ATOM 3701 C CA . ASN B 2 272 ? 6.060 70.425 8.674 1.00 31.69 ? 520 ASN B CA 1 ATOM 3702 C C . ASN B 2 272 ? 7.440 70.499 8.036 1.00 30.98 ? 520 ASN B C 1 ATOM 3703 O O . ASN B 2 272 ? 7.579 70.740 6.830 1.00 30.67 ? 520 ASN B O 1 ATOM 3704 C CB . ASN B 2 272 ? 5.132 71.481 8.055 1.00 33.31 ? 520 ASN B CB 1 ATOM 3705 C CG . ASN B 2 272 ? 5.618 72.894 8.291 1.00 37.12 ? 520 ASN B CG 1 ATOM 3706 O OD1 . ASN B 2 272 ? 6.647 73.117 8.939 1.00 37.89 ? 520 ASN B OD1 1 ATOM 3707 N ND2 . ASN B 2 272 ? 4.877 73.870 7.766 1.00 46.95 ? 520 ASN B ND2 1 ATOM 3708 N N . GLY B 2 273 ? 8.477 70.289 8.837 1.00 29.25 ? 521 GLY B N 1 ATOM 3709 C CA . GLY B 2 273 ? 9.823 70.288 8.294 1.00 27.83 ? 521 GLY B CA 1 ATOM 3710 C C . GLY B 2 273 ? 10.094 69.059 7.451 1.00 27.14 ? 521 GLY B C 1 ATOM 3711 O O . GLY B 2 273 ? 9.365 68.061 7.498 1.00 27.28 ? 521 GLY B O 1 ATOM 3712 N N . SER B 2 274 ? 11.149 69.146 6.655 1.00 26.55 ? 522 SER B N 1 ATOM 3713 C CA . SER B 2 274 ? 11.576 68.049 5.846 1.00 27.14 ? 522 SER B CA 1 ATOM 3714 C C . SER B 2 274 ? 12.857 67.504 6.502 1.00 26.68 ? 522 SER B C 1 ATOM 3715 O O . SER B 2 274 ? 13.837 68.249 6.641 1.00 26.57 ? 522 SER B O 1 ATOM 3716 C CB . SER B 2 274 ? 11.869 68.568 4.437 1.00 28.04 ? 522 SER B CB 1 ATOM 3717 O OG . SER B 2 274 ? 12.411 67.541 3.636 1.00 31.90 ? 522 SER B OG 1 ATOM 3718 N N . TYR B 2 275 ? 12.812 66.234 6.912 1.00 26.05 ? 523 TYR B N 1 ATOM 3719 C CA . TYR B 2 275 ? 13.921 65.590 7.639 1.00 25.44 ? 523 TYR B CA 1 ATOM 3720 C C . TYR B 2 275 ? 14.303 64.248 7.013 1.00 25.41 ? 523 TYR B C 1 ATOM 3721 O O . TYR B 2 275 ? 13.416 63.466 6.635 1.00 26.44 ? 523 TYR B O 1 ATOM 3722 C CB . TYR B 2 275 ? 13.479 65.346 9.093 1.00 24.64 ? 523 TYR B CB 1 ATOM 3723 C CG . TYR B 2 275 ? 12.903 66.574 9.767 1.00 22.39 ? 523 TYR B CG 1 ATOM 3724 C CD1 . TYR B 2 275 ? 13.708 67.678 10.054 1.00 22.50 ? 523 TYR B CD1 1 ATOM 3725 C CD2 . TYR B 2 275 ? 11.567 66.628 10.129 1.00 21.41 ? 523 TYR B CD2 1 ATOM 3726 C CE1 . TYR B 2 275 ? 13.202 68.814 10.651 1.00 20.41 ? 523 TYR B CE1 1 ATOM 3727 C CE2 . TYR B 2 275 ? 11.046 67.781 10.750 1.00 20.68 ? 523 TYR B CE2 1 ATOM 3728 C CZ . TYR B 2 275 ? 11.875 68.840 11.021 1.00 20.97 ? 523 TYR B CZ 1 ATOM 3729 O OH . TYR B 2 275 ? 11.360 69.952 11.611 1.00 23.16 ? 523 TYR B OH 1 ATOM 3730 N N . PRO B 2 276 ? 15.610 63.946 6.930 1.00 25.34 ? 524 PRO B N 1 ATOM 3731 C CA . PRO B 2 276 ? 16.041 62.682 6.298 1.00 24.99 ? 524 PRO B CA 1 ATOM 3732 C C . PRO B 2 276 ? 15.820 61.405 7.112 1.00 24.71 ? 524 PRO B C 1 ATOM 3733 O O . PRO B 2 276 ? 15.789 60.320 6.540 1.00 24.72 ? 524 PRO B O 1 ATOM 3734 C CB . PRO B 2 276 ? 17.527 62.901 6.036 1.00 24.97 ? 524 PRO B CB 1 ATOM 3735 C CG . PRO B 2 276 ? 17.963 63.908 7.065 1.00 25.44 ? 524 PRO B CG 1 ATOM 3736 C CD . PRO B 2 276 ? 16.751 64.790 7.338 1.00 25.19 ? 524 PRO B CD 1 ATOM 3737 N N . PHE B 2 277 ? 15.692 61.521 8.436 1.00 24.63 ? 525 PHE B N 1 ATOM 3738 C CA . PHE B 2 277 ? 15.415 60.371 9.299 1.00 23.84 ? 525 PHE B CA 1 ATOM 3739 C C . PHE B 2 277 ? 14.698 60.810 10.597 1.00 24.07 ? 525 PHE B C 1 ATOM 3740 O O . PHE B 2 277 ? 14.709 61.993 10.968 1.00 23.84 ? 525 PHE B O 1 ATOM 3741 C CB . PHE B 2 277 ? 16.683 59.505 9.578 1.00 24.22 ? 525 PHE B CB 1 ATOM 3742 C CG . PHE B 2 277 ? 17.904 60.300 9.976 1.00 23.05 ? 525 PHE B CG 1 ATOM 3743 C CD1 . PHE B 2 277 ? 18.858 60.660 9.028 1.00 22.91 ? 525 PHE B CD1 1 ATOM 3744 C CD2 . PHE B 2 277 ? 18.120 60.656 11.298 1.00 24.00 ? 525 PHE B CD2 1 ATOM 3745 C CE1 . PHE B 2 277 ? 19.993 61.415 9.376 1.00 24.61 ? 525 PHE B CE1 1 ATOM 3746 C CE2 . PHE B 2 277 ? 19.253 61.392 11.668 1.00 23.11 ? 525 PHE B CE2 1 ATOM 3747 C CZ . PHE B 2 277 ? 20.198 61.767 10.718 1.00 22.35 ? 525 PHE B CZ 1 ATOM 3748 N N . GLN B 2 278 ? 14.083 59.839 11.271 1.00 23.96 ? 526 GLN B N 1 ATOM 3749 C CA A GLN B 2 278 ? 13.141 60.150 12.353 0.50 23.69 ? 526 GLN B CA 1 ATOM 3750 C CA B GLN B 2 278 ? 13.163 60.076 12.385 0.50 23.82 ? 526 GLN B CA 1 ATOM 3751 C C . GLN B 2 278 ? 13.728 60.911 13.538 1.00 23.44 ? 526 GLN B C 1 ATOM 3752 O O . GLN B 2 278 ? 13.016 61.707 14.156 1.00 23.05 ? 526 GLN B O 1 ATOM 3753 C CB A GLN B 2 278 ? 12.418 58.889 12.857 0.50 24.20 ? 526 GLN B CB 1 ATOM 3754 C CB B GLN B 2 278 ? 12.673 58.726 12.935 0.50 24.18 ? 526 GLN B CB 1 ATOM 3755 C CG A GLN B 2 278 ? 11.597 59.089 14.145 0.50 24.11 ? 526 GLN B CG 1 ATOM 3756 C CG B GLN B 2 278 ? 12.055 57.794 11.877 0.50 25.16 ? 526 GLN B CG 1 ATOM 3757 C CD A GLN B 2 278 ? 10.343 59.932 13.957 0.50 26.85 ? 526 GLN B CD 1 ATOM 3758 C CD B GLN B 2 278 ? 10.946 58.449 11.095 0.50 27.32 ? 526 GLN B CD 1 ATOM 3759 O OE1 A GLN B 2 278 ? 9.807 60.503 14.925 0.50 27.80 ? 526 GLN B OE1 1 ATOM 3760 O OE1 B GLN B 2 278 ? 10.020 59.030 11.669 0.50 28.50 ? 526 GLN B OE1 1 ATOM 3761 N NE2 A GLN B 2 278 ? 9.857 60.011 12.717 0.50 27.18 ? 526 GLN B NE2 1 ATOM 3762 N NE2 B GLN B 2 278 ? 11.027 58.362 9.769 0.50 28.63 ? 526 GLN B NE2 1 ATOM 3763 N N . ALA B 2 279 ? 15.005 60.697 13.853 1.00 22.69 ? 527 ALA B N 1 ATOM 3764 C CA . ALA B 2 279 ? 15.569 61.352 15.048 1.00 21.95 ? 527 ALA B CA 1 ATOM 3765 C C . ALA B 2 279 ? 15.503 62.875 14.949 1.00 21.19 ? 527 ALA B C 1 ATOM 3766 O O . ALA B 2 279 ? 15.543 63.577 15.970 1.00 20.96 ? 527 ALA B O 1 ATOM 3767 C CB . ALA B 2 279 ? 17.013 60.911 15.260 1.00 21.99 ? 527 ALA B CB 1 ATOM 3768 N N . LEU B 2 280 ? 15.447 63.375 13.710 1.00 21.04 ? 528 LEU B N 1 ATOM 3769 C CA . LEU B 2 280 ? 15.457 64.793 13.458 1.00 21.29 ? 528 LEU B CA 1 ATOM 3770 C C . LEU B 2 280 ? 14.062 65.431 13.451 1.00 21.08 ? 528 LEU B C 1 ATOM 3771 O O . LEU B 2 280 ? 13.955 66.638 13.356 1.00 20.44 ? 528 LEU B O 1 ATOM 3772 C CB . LEU B 2 280 ? 16.190 65.063 12.135 1.00 21.23 ? 528 LEU B CB 1 ATOM 3773 C CG . LEU B 2 280 ? 17.702 64.737 12.201 1.00 22.39 ? 528 LEU B CG 1 ATOM 3774 C CD1 . LEU B 2 280 ? 18.282 64.692 10.778 1.00 24.82 ? 528 LEU B CD1 1 ATOM 3775 C CD2 . LEU B 2 280 ? 18.440 65.756 13.032 1.00 24.61 ? 528 LEU B CD2 1 ATOM 3776 N N . HIS B 2 281 ? 13.010 64.618 13.565 1.00 21.15 ? 529 HIS B N 1 ATOM 3777 C CA . HIS B 2 281 ? 11.644 65.155 13.580 1.00 22.11 ? 529 HIS B CA 1 ATOM 3778 C C . HIS B 2 281 ? 11.285 66.026 14.787 1.00 21.61 ? 529 HIS B C 1 ATOM 3779 O O . HIS B 2 281 ? 12.007 66.067 15.808 1.00 20.35 ? 529 HIS B O 1 ATOM 3780 C CB . HIS B 2 281 ? 10.634 64.023 13.465 1.00 22.93 ? 529 HIS B CB 1 ATOM 3781 C CG . HIS B 2 281 ? 10.632 63.364 12.124 1.00 25.40 ? 529 HIS B CG 1 ATOM 3782 N ND1 . HIS B 2 281 ? 9.484 62.848 11.554 1.00 30.90 ? 529 HIS B ND1 1 ATOM 3783 C CD2 . HIS B 2 281 ? 11.623 63.167 11.224 1.00 25.68 ? 529 HIS B CD2 1 ATOM 3784 C CE1 . HIS B 2 281 ? 9.776 62.349 10.364 1.00 31.00 ? 529 HIS B CE1 1 ATOM 3785 N NE2 . HIS B 2 281 ? 11.069 62.515 10.147 1.00 30.46 ? 529 HIS B NE2 1 ATOM 3786 N N . GLN B 2 282 ? 10.133 66.697 14.687 1.00 20.64 ? 530 GLN B N 1 ATOM 3787 C CA . GLN B 2 282 ? 9.534 67.291 15.866 1.00 19.93 ? 530 GLN B CA 1 ATOM 3788 C C . GLN B 2 282 ? 9.069 66.112 16.727 1.00 20.58 ? 530 GLN B C 1 ATOM 3789 O O . GLN B 2 282 ? 8.404 65.177 16.226 1.00 19.70 ? 530 GLN B O 1 ATOM 3790 C CB . GLN B 2 282 ? 8.308 68.165 15.520 1.00 20.46 ? 530 GLN B CB 1 ATOM 3791 C CG . GLN B 2 282 ? 7.748 68.849 16.729 1.00 19.94 ? 530 GLN B CG 1 ATOM 3792 C CD . GLN B 2 282 ? 6.407 69.521 16.445 1.00 23.92 ? 530 GLN B CD 1 ATOM 3793 O OE1 . GLN B 2 282 ? 5.376 68.857 16.442 1.00 25.10 ? 530 GLN B OE1 1 ATOM 3794 N NE2 . GLN B 2 282 ? 6.420 70.831 16.244 1.00 23.33 ? 530 GLN B NE2 1 ATOM 3795 N N . ARG B 2 283 ? 9.402 66.145 18.013 1.00 19.89 ? 531 ARG B N 1 ATOM 3796 C CA . ARG B 2 283 ? 9.115 65.010 18.908 1.00 20.16 ? 531 ARG B CA 1 ATOM 3797 C C . ARG B 2 283 ? 8.994 65.601 20.311 1.00 19.73 ? 531 ARG B C 1 ATOM 3798 O O . ARG B 2 283 ? 9.606 66.627 20.604 1.00 19.93 ? 531 ARG B O 1 ATOM 3799 C CB . ARG B 2 283 ? 10.274 63.980 18.907 1.00 19.86 ? 531 ARG B CB 1 ATOM 3800 C CG . ARG B 2 283 ? 10.718 63.391 17.534 1.00 22.86 ? 531 ARG B CG 1 ATOM 3801 C CD . ARG B 2 283 ? 12.216 62.893 17.539 1.00 25.19 ? 531 ARG B CD 1 ATOM 3802 N NE . ARG B 2 283 ? 12.471 61.841 18.543 1.00 24.88 ? 531 ARG B NE 1 ATOM 3803 C CZ . ARG B 2 283 ? 13.682 61.481 18.972 1.00 25.54 ? 531 ARG B CZ 1 ATOM 3804 N NH1 . ARG B 2 283 ? 14.757 62.100 18.496 1.00 22.23 ? 531 ARG B NH1 1 ATOM 3805 N NH2 . ARG B 2 283 ? 13.824 60.501 19.877 1.00 22.91 ? 531 ARG B NH2 1 ATOM 3806 N N . ALA B 2 284 ? 8.201 64.975 21.176 1.00 18.89 ? 532 ALA B N 1 ATOM 3807 C CA . ALA B 2 284 ? 8.133 65.430 22.572 1.00 19.08 ? 532 ALA B CA 1 ATOM 3808 C C . ALA B 2 284 ? 9.272 64.709 23.327 1.00 18.37 ? 532 ALA B C 1 ATOM 3809 O O . ALA B 2 284 ? 9.035 63.823 24.167 1.00 17.93 ? 532 ALA B O 1 ATOM 3810 C CB . ALA B 2 284 ? 6.782 65.066 23.180 1.00 20.42 ? 532 ALA B CB 1 ATOM 3811 N N . HIS B 2 285 ? 10.511 65.074 22.984 1.00 17.38 ? 533 HIS B N 1 ATOM 3812 C CA . HIS B 2 285 ? 11.654 64.278 23.414 1.00 17.07 ? 533 HIS B CA 1 ATOM 3813 C C . HIS B 2 285 ? 12.853 65.224 23.394 1.00 16.75 ? 533 HIS B C 1 ATOM 3814 O O . HIS B 2 285 ? 12.928 66.127 22.559 1.00 16.11 ? 533 HIS B O 1 ATOM 3815 C CB . HIS B 2 285 ? 11.876 63.165 22.395 1.00 17.83 ? 533 HIS B CB 1 ATOM 3816 C CG . HIS B 2 285 ? 12.907 62.153 22.790 1.00 18.62 ? 533 HIS B CG 1 ATOM 3817 N ND1 . HIS B 2 285 ? 14.258 62.334 22.556 1.00 19.95 ? 533 HIS B ND1 1 ATOM 3818 C CD2 . HIS B 2 285 ? 12.778 60.930 23.357 1.00 19.44 ? 533 HIS B CD2 1 ATOM 3819 C CE1 . HIS B 2 285 ? 14.919 61.271 22.993 1.00 21.82 ? 533 HIS B CE1 1 ATOM 3820 N NE2 . HIS B 2 285 ? 14.046 60.410 23.488 1.00 19.50 ? 533 HIS B NE2 1 ATOM 3821 N N . GLY B 2 286 ? 13.826 64.976 24.270 1.00 15.77 ? 534 GLY B N 1 ATOM 3822 C CA . GLY B 2 286 ? 15.024 65.815 24.271 1.00 15.13 ? 534 GLY B CA 1 ATOM 3823 C C . GLY B 2 286 ? 15.752 65.655 25.602 1.00 14.95 ? 534 GLY B C 1 ATOM 3824 O O . GLY B 2 286 ? 15.421 64.765 26.380 1.00 15.88 ? 534 GLY B O 1 ATOM 3825 N N . GLY B 2 287 ? 16.743 66.502 25.845 1.00 15.27 ? 535 GLY B N 1 ATOM 3826 C CA . GLY B 2 287 ? 17.413 66.499 27.152 1.00 15.37 ? 535 GLY B CA 1 ATOM 3827 C C . GLY B 2 287 ? 16.429 66.863 28.228 1.00 16.20 ? 535 GLY B C 1 ATOM 3828 O O . GLY B 2 287 ? 15.706 67.867 28.103 1.00 17.62 ? 535 GLY B O 1 ATOM 3829 N N . ILE B 2 288 ? 16.347 66.054 29.281 1.00 14.34 ? 536 ILE B N 1 ATOM 3830 C CA . ILE B 2 288 ? 15.383 66.314 30.354 1.00 14.81 ? 536 ILE B CA 1 ATOM 3831 C C . ILE B 2 288 ? 16.002 66.537 31.737 1.00 14.81 ? 536 ILE B C 1 ATOM 3832 O O . ILE B 2 288 ? 15.293 66.747 32.748 1.00 15.37 ? 536 ILE B O 1 ATOM 3833 C CB . ILE B 2 288 ? 14.295 65.196 30.470 1.00 15.00 ? 536 ILE B CB 1 ATOM 3834 C CG1 . ILE B 2 288 ? 14.934 63.839 30.872 1.00 16.14 ? 536 ILE B CG1 1 ATOM 3835 C CG2 . ILE B 2 288 ? 13.503 65.050 29.145 1.00 16.30 ? 536 ILE B CG2 1 ATOM 3836 C CD1 . ILE B 2 288 ? 13.930 62.854 31.559 1.00 17.64 ? 536 ILE B CD1 1 ATOM 3837 N N . ASP B 2 289 ? 17.332 66.512 31.815 1.00 15.33 ? 537 ASP B N 1 ATOM 3838 C CA . ASP B 2 289 ? 17.945 66.823 33.110 1.00 15.52 ? 537 ASP B CA 1 ATOM 3839 C C . ASP B 2 289 ? 19.452 67.033 32.911 1.00 16.21 ? 537 ASP B C 1 ATOM 3840 O O . ASP B 2 289 ? 19.970 66.911 31.776 1.00 16.50 ? 537 ASP B O 1 ATOM 3841 C CB . ASP B 2 289 ? 17.681 65.677 34.113 1.00 14.87 ? 537 ASP B CB 1 ATOM 3842 C CG . ASP B 2 289 ? 18.454 64.386 33.745 1.00 18.67 ? 537 ASP B CG 1 ATOM 3843 O OD1 . ASP B 2 289 ? 19.585 64.489 33.186 1.00 17.00 ? 537 ASP B OD1 1 ATOM 3844 O OD2 . ASP B 2 289 ? 17.930 63.296 34.060 1.00 20.16 ? 537 ASP B OD2 1 ATOM 3845 N N . VAL B 2 290 ? 20.144 67.393 33.992 1.00 15.40 ? 538 VAL B N 1 ATOM 3846 C CA A VAL B 2 290 ? 21.595 67.254 34.018 0.50 15.43 ? 538 VAL B CA 1 ATOM 3847 C CA B VAL B 2 290 ? 21.603 67.374 34.031 0.50 15.10 ? 538 VAL B CA 1 ATOM 3848 C C . VAL B 2 290 ? 21.948 66.923 35.457 1.00 14.51 ? 538 VAL B C 1 ATOM 3849 O O . VAL B 2 290 ? 21.284 67.365 36.401 1.00 14.64 ? 538 VAL B O 1 ATOM 3850 C CB A VAL B 2 290 ? 22.377 68.491 33.491 0.50 15.81 ? 538 VAL B CB 1 ATOM 3851 C CB B VAL B 2 290 ? 22.203 68.783 33.756 0.50 15.59 ? 538 VAL B CB 1 ATOM 3852 C CG1 A VAL B 2 290 ? 21.940 69.751 34.193 0.50 18.12 ? 538 VAL B CG1 1 ATOM 3853 C CG1 B VAL B 2 290 ? 23.679 68.826 34.103 0.50 16.11 ? 538 VAL B CG1 1 ATOM 3854 C CG2 A VAL B 2 290 ? 23.899 68.276 33.630 0.50 16.37 ? 538 VAL B CG2 1 ATOM 3855 C CG2 B VAL B 2 290 ? 21.986 69.194 32.303 0.50 15.71 ? 538 VAL B CG2 1 ATOM 3856 N N . LYS B 2 291 ? 22.933 66.043 35.634 1.00 13.73 ? 539 LYS B N 1 ATOM 3857 C CA . LYS B 2 291 ? 23.469 65.764 36.980 1.00 12.91 ? 539 LYS B CA 1 ATOM 3858 C C . LYS B 2 291 ? 24.987 65.957 36.865 1.00 13.09 ? 539 LYS B C 1 ATOM 3859 O O . LYS B 2 291 ? 25.594 65.558 35.863 1.00 12.82 ? 539 LYS B O 1 ATOM 3860 C CB . LYS B 2 291 ? 23.186 64.337 37.483 1.00 13.35 ? 539 LYS B CB 1 ATOM 3861 C CG . LYS B 2 291 ? 21.676 63.980 37.707 1.00 14.07 ? 539 LYS B CG 1 ATOM 3862 C CD . LYS B 2 291 ? 20.963 63.684 36.329 1.00 14.10 ? 539 LYS B CD 1 ATOM 3863 C CE . LYS B 2 291 ? 21.718 62.692 35.445 1.00 14.54 ? 539 LYS B CE 1 ATOM 3864 N NZ . LYS B 2 291 ? 20.851 62.286 34.285 1.00 14.56 ? 539 LYS B NZ 1 ATOM 3865 N N . VAL B 2 292 ? 25.609 66.578 37.867 1.00 13.59 ? 540 VAL B N 1 ATOM 3866 C CA . VAL B 2 292 ? 27.049 66.747 37.799 1.00 13.94 ? 540 VAL B CA 1 ATOM 3867 C C . VAL B 2 292 ? 27.629 66.429 39.169 1.00 13.97 ? 540 VAL B C 1 ATOM 3868 O O . VAL B 2 292 ? 27.062 66.860 40.199 1.00 14.11 ? 540 VAL B O 1 ATOM 3869 C CB . VAL B 2 292 ? 27.416 68.234 37.510 1.00 14.41 ? 540 VAL B CB 1 ATOM 3870 C CG1 . VAL B 2 292 ? 28.934 68.337 37.351 1.00 14.91 ? 540 VAL B CG1 1 ATOM 3871 C CG2 . VAL B 2 292 ? 26.711 68.737 36.220 1.00 14.34 ? 540 VAL B CG2 1 ATOM 3872 N N . THR B 2 293 ? 28.775 65.743 39.219 1.00 13.46 ? 541 THR B N 1 ATOM 3873 C CA . THR B 2 293 ? 29.439 65.588 40.506 1.00 14.27 ? 541 THR B CA 1 ATOM 3874 C C . THR B 2 293 ? 30.943 65.863 40.324 1.00 13.46 ? 541 THR B C 1 ATOM 3875 O O . THR B 2 293 ? 31.429 66.138 39.223 1.00 13.91 ? 541 THR B O 1 ATOM 3876 C CB . THR B 2 293 ? 29.144 64.211 41.147 1.00 15.53 ? 541 THR B CB 1 ATOM 3877 O OG1 . THR B 2 293 ? 29.543 64.190 42.532 1.00 17.38 ? 541 THR B OG1 1 ATOM 3878 C CG2 . THR B 2 293 ? 29.897 63.111 40.373 1.00 14.40 ? 541 THR B CG2 1 ATOM 3879 N N . SER B 2 294 ? 31.667 65.838 41.437 1.00 14.91 ? 542 SER B N 1 ATOM 3880 C CA . SER B 2 294 ? 33.112 66.136 41.441 1.00 14.65 ? 542 SER B CA 1 ATOM 3881 C C . SER B 2 294 ? 33.760 65.221 42.474 1.00 14.86 ? 542 SER B C 1 ATOM 3882 O O . SER B 2 294 ? 33.083 64.512 43.187 1.00 15.01 ? 542 SER B O 1 ATOM 3883 C CB . SER B 2 294 ? 33.374 67.582 41.884 1.00 15.55 ? 542 SER B CB 1 ATOM 3884 O OG . SER B 2 294 ? 32.915 67.792 43.233 1.00 16.06 ? 542 SER B OG 1 ATOM 3885 N N . PHE B 2 295 ? 35.087 65.256 42.536 1.00 15.45 ? 543 PHE B N 1 ATOM 3886 C CA . PHE B 2 295 ? 35.790 64.466 43.546 1.00 16.54 ? 543 PHE B CA 1 ATOM 3887 C C . PHE B 2 295 ? 35.220 64.752 44.946 1.00 17.82 ? 543 PHE B C 1 ATOM 3888 O O . PHE B 2 295 ? 34.839 63.826 45.668 1.00 17.70 ? 543 PHE B O 1 ATOM 3889 C CB . PHE B 2 295 ? 37.288 64.782 43.449 1.00 17.59 ? 543 PHE B CB 1 ATOM 3890 C CG . PHE B 2 295 ? 38.123 64.038 44.465 1.00 19.02 ? 543 PHE B CG 1 ATOM 3891 C CD1 . PHE B 2 295 ? 38.350 62.674 44.328 1.00 19.80 ? 543 PHE B CD1 1 ATOM 3892 C CD2 . PHE B 2 295 ? 38.675 64.720 45.543 1.00 24.06 ? 543 PHE B CD2 1 ATOM 3893 C CE1 . PHE B 2 295 ? 39.151 61.985 45.253 1.00 23.82 ? 543 PHE B CE1 1 ATOM 3894 C CE2 . PHE B 2 295 ? 39.461 64.046 46.490 1.00 24.56 ? 543 PHE B CE2 1 ATOM 3895 C CZ . PHE B 2 295 ? 39.695 62.683 46.337 1.00 24.44 ? 543 PHE B CZ 1 ATOM 3896 N N . THR B 2 296 ? 35.116 66.023 45.349 1.00 18.90 ? 544 THR B N 1 ATOM 3897 C CA . THR B 2 296 ? 34.569 66.287 46.681 1.00 21.89 ? 544 THR B CA 1 ATOM 3898 C C . THR B 2 296 ? 33.080 66.021 46.837 1.00 21.03 ? 544 THR B C 1 ATOM 3899 O O . THR B 2 296 ? 32.639 65.453 47.847 1.00 22.20 ? 544 THR B O 1 ATOM 3900 C CB . THR B 2 296 ? 34.857 67.723 47.143 1.00 22.83 ? 544 THR B CB 1 ATOM 3901 O OG1 . THR B 2 296 ? 36.274 67.902 47.163 1.00 26.53 ? 544 THR B OG1 1 ATOM 3902 C CG2 . THR B 2 296 ? 34.336 67.904 48.553 1.00 25.89 ? 544 THR B CG2 1 ATOM 3903 N N . LEU B 2 297 ? 32.282 66.432 45.863 1.00 18.97 ? 545 LEU B N 1 ATOM 3904 C CA . LEU B 2 297 ? 30.870 66.179 45.992 1.00 19.14 ? 545 LEU B CA 1 ATOM 3905 C C . LEU B 2 297 ? 30.585 64.679 46.117 1.00 18.14 ? 545 LEU B C 1 ATOM 3906 O O . LEU B 2 297 ? 29.778 64.274 46.951 1.00 17.89 ? 545 LEU B O 1 ATOM 3907 C CB . LEU B 2 297 ? 30.104 66.743 44.803 1.00 20.01 ? 545 LEU B CB 1 ATOM 3908 C CG . LEU B 2 297 ? 29.918 68.264 44.835 1.00 22.31 ? 545 LEU B CG 1 ATOM 3909 C CD1 . LEU B 2 297 ? 29.214 68.655 43.551 1.00 22.80 ? 545 LEU B CD1 1 ATOM 3910 C CD2 . LEU B 2 297 ? 29.063 68.636 46.027 1.00 26.18 ? 545 LEU B CD2 1 ATOM 3911 N N . ALA B 2 298 ? 31.237 63.868 45.290 1.00 17.26 ? 546 ALA B N 1 ATOM 3912 C CA . ALA B 2 298 ? 30.997 62.402 45.294 1.00 17.17 ? 546 ALA B CA 1 ATOM 3913 C C . ALA B 2 298 ? 31.402 61.788 46.641 1.00 20.19 ? 546 ALA B C 1 ATOM 3914 O O . ALA B 2 298 ? 30.777 60.848 47.154 1.00 19.96 ? 546 ALA B O 1 ATOM 3915 C CB . ALA B 2 298 ? 31.782 61.743 44.171 1.00 17.40 ? 546 ALA B CB 1 ATOM 3916 N N . LYS B 2 299 ? 32.464 62.319 47.214 1.00 21.35 ? 547 LYS B N 1 ATOM 3917 C CA . LYS B 2 299 ? 32.902 61.875 48.540 1.00 24.30 ? 547 LYS B CA 1 ATOM 3918 C C . LYS B 2 299 ? 31.784 62.025 49.570 1.00 24.76 ? 547 LYS B C 1 ATOM 3919 O O . LYS B 2 299 ? 31.635 61.174 50.465 1.00 26.12 ? 547 LYS B O 1 ATOM 3920 C CB . LYS B 2 299 ? 34.177 62.655 48.931 1.00 25.42 ? 547 LYS B CB 1 ATOM 3921 C CG . LYS B 2 299 ? 34.720 62.408 50.327 1.00 30.88 ? 547 LYS B CG 1 ATOM 3922 C CD . LYS B 2 299 ? 35.948 63.319 50.544 1.00 35.88 ? 547 LYS B CD 1 ATOM 3923 C CE . LYS B 2 299 ? 36.959 63.150 49.406 1.00 41.25 ? 547 LYS B CE 1 ATOM 3924 N NZ . LYS B 2 299 ? 38.206 63.952 49.612 1.00 45.36 ? 547 LYS B NZ 1 ATOM 3925 N N . TYR B 2 300 ? 30.977 63.076 49.427 1.00 23.89 ? 548 TYR B N 1 ATOM 3926 C CA . TYR B 2 300 ? 29.811 63.317 50.265 1.00 24.92 ? 548 TYR B CA 1 ATOM 3927 C C . TYR B 2 300 ? 28.483 62.866 49.658 1.00 23.98 ? 548 TYR B C 1 ATOM 3928 O O . TYR B 2 300 ? 27.415 63.331 50.063 1.00 22.96 ? 548 TYR B O 1 ATOM 3929 C CB . TYR B 2 300 ? 29.770 64.805 50.645 1.00 28.05 ? 548 TYR B CB 1 ATOM 3930 C CG . TYR B 2 300 ? 30.993 65.107 51.465 1.00 31.51 ? 548 TYR B CG 1 ATOM 3931 C CD1 . TYR B 2 300 ? 31.115 64.580 52.746 1.00 38.61 ? 548 TYR B CD1 1 ATOM 3932 C CD2 . TYR B 2 300 ? 32.055 65.837 50.948 1.00 35.38 ? 548 TYR B CD2 1 ATOM 3933 C CE1 . TYR B 2 300 ? 32.248 64.812 53.517 1.00 40.75 ? 548 TYR B CE1 1 ATOM 3934 C CE2 . TYR B 2 300 ? 33.204 66.070 51.706 1.00 38.79 ? 548 TYR B CE2 1 ATOM 3935 C CZ . TYR B 2 300 ? 33.289 65.553 52.989 1.00 40.84 ? 548 TYR B CZ 1 ATOM 3936 O OH . TYR B 2 300 ? 34.403 65.769 53.773 1.00 43.10 ? 548 TYR B OH 1 ATOM 3937 N N . MET B 2 301 ? 28.559 61.947 48.692 1.00 21.83 ? 549 MET B N 1 ATOM 3938 C CA . MET B 2 301 ? 27.366 61.386 48.045 1.00 21.91 ? 549 MET B CA 1 ATOM 3939 C C . MET B 2 301 ? 26.420 62.487 47.593 1.00 21.06 ? 549 MET B C 1 ATOM 3940 O O . MET B 2 301 ? 25.216 62.423 47.813 1.00 20.77 ? 549 MET B O 1 ATOM 3941 C CB . MET B 2 301 ? 26.679 60.380 49.006 1.00 23.55 ? 549 MET B CB 1 ATOM 3942 C CG . MET B 2 301 ? 27.701 59.369 49.557 1.00 26.80 ? 549 MET B CG 1 ATOM 3943 S SD . MET B 2 301 ? 28.107 58.086 48.316 1.00 39.46 ? 549 MET B SD 1 ATOM 3944 C CE . MET B 2 301 ? 26.497 57.357 48.155 1.00 34.14 ? 549 MET B CE 1 ATOM 3945 N N . SER B 2 302 ? 26.989 63.501 46.947 1.00 19.11 ? 550 SER B N 1 ATOM 3946 C CA A SER B 2 302 ? 26.249 64.696 46.546 0.50 19.28 ? 550 SER B CA 1 ATOM 3947 C CA B SER B 2 302 ? 26.219 64.665 46.529 0.50 19.20 ? 550 SER B CA 1 ATOM 3948 C C . SER B 2 302 ? 26.419 64.975 45.059 1.00 19.01 ? 550 SER B C 1 ATOM 3949 O O . SER B 2 302 ? 27.421 64.562 44.455 1.00 17.58 ? 550 SER B O 1 ATOM 3950 C CB A SER B 2 302 ? 26.774 65.917 47.313 0.50 19.61 ? 550 SER B CB 1 ATOM 3951 C CB B SER B 2 302 ? 26.647 65.879 47.346 0.50 19.68 ? 550 SER B CB 1 ATOM 3952 O OG A SER B 2 302 ? 25.960 67.050 47.052 0.50 21.15 ? 550 SER B OG 1 ATOM 3953 O OG B SER B 2 302 ? 26.287 65.690 48.694 0.50 20.55 ? 550 SER B OG 1 ATOM 3954 N N . MET B 2 303 ? 25.456 65.707 44.495 1.00 18.37 ? 551 MET B N 1 ATOM 3955 C CA . MET B 2 303 ? 25.531 66.150 43.106 1.00 19.13 ? 551 MET B CA 1 ATOM 3956 C C . MET B 2 303 ? 24.809 67.472 42.975 1.00 19.10 ? 551 MET B C 1 ATOM 3957 O O . MET B 2 303 ? 24.050 67.865 43.883 1.00 20.82 ? 551 MET B O 1 ATOM 3958 C CB . MET B 2 303 ? 24.846 65.118 42.169 1.00 18.82 ? 551 MET B CB 1 ATOM 3959 C CG . MET B 2 303 ? 23.316 65.133 42.304 1.00 21.11 ? 551 MET B CG 1 ATOM 3960 S SD . MET B 2 303 ? 22.514 63.815 41.331 1.00 25.51 ? 551 MET B SD 1 ATOM 3961 C CE . MET B 2 303 ? 22.973 62.400 42.311 1.00 28.78 ? 551 MET B CE 1 ATOM 3962 N N . LEU B 2 304 ? 25.027 68.148 41.853 1.00 18.29 ? 552 LEU B N 1 ATOM 3963 C CA . LEU B 2 304 ? 24.176 69.254 41.411 1.00 19.23 ? 552 LEU B CA 1 ATOM 3964 C C . LEU B 2 304 ? 23.241 68.646 40.363 1.00 19.39 ? 552 LEU B C 1 ATOM 3965 O O . LEU B 2 304 ? 23.678 67.859 39.520 1.00 19.69 ? 552 LEU B O 1 ATOM 3966 C CB . LEU B 2 304 ? 25.024 70.294 40.688 1.00 20.81 ? 552 LEU B CB 1 ATOM 3967 C CG . LEU B 2 304 ? 25.650 71.492 41.377 1.00 27.93 ? 552 LEU B CG 1 ATOM 3968 C CD1 . LEU B 2 304 ? 26.084 72.453 40.257 1.00 29.97 ? 552 LEU B CD1 1 ATOM 3969 C CD2 . LEU B 2 304 ? 24.600 72.149 42.297 1.00 30.94 ? 552 LEU B CD2 1 ATOM 3970 N N . ALA B 2 305 ? 21.963 68.970 40.410 1.00 17.91 ? 553 ALA B N 1 ATOM 3971 C CA . ALA B 2 305 ? 21.032 68.363 39.464 1.00 16.47 ? 553 ALA B CA 1 ATOM 3972 C C . ALA B 2 305 ? 20.013 69.403 39.010 1.00 18.57 ? 553 ALA B C 1 ATOM 3973 O O . ALA B 2 305 ? 19.541 70.220 39.842 1.00 19.05 ? 553 ALA B O 1 ATOM 3974 C CB . ALA B 2 305 ? 20.308 67.230 40.134 1.00 17.46 ? 553 ALA B CB 1 ATOM 3975 N N . ALA B 2 306 ? 19.672 69.365 37.726 1.00 16.78 ? 554 ALA B N 1 ATOM 3976 C CA . ALA B 2 306 ? 18.651 70.276 37.189 1.00 16.81 ? 554 ALA B CA 1 ATOM 3977 C C . ALA B 2 306 ? 17.631 69.443 36.432 1.00 17.29 ? 554 ALA B C 1 ATOM 3978 O O . ALA B 2 306 ? 18.011 68.551 35.637 1.00 15.93 ? 554 ALA B O 1 ATOM 3979 C CB . ALA B 2 306 ? 19.312 71.265 36.279 1.00 17.42 ? 554 ALA B CB 1 ATOM 3980 N N . SER B 2 307 ? 16.345 69.714 36.670 1.00 17.31 ? 555 SER B N 1 ATOM 3981 C CA . SER B 2 307 ? 15.288 68.918 36.076 1.00 17.49 ? 555 SER B CA 1 ATOM 3982 C C . SER B 2 307 ? 14.584 69.672 34.953 1.00 19.60 ? 555 SER B C 1 ATOM 3983 O O . SER B 2 307 ? 14.258 70.872 35.101 1.00 19.93 ? 555 SER B O 1 ATOM 3984 C CB . SER B 2 307 ? 14.269 68.547 37.140 1.00 18.74 ? 555 SER B CB 1 ATOM 3985 O OG . SER B 2 307 ? 13.308 67.662 36.588 1.00 17.92 ? 555 SER B OG 1 ATOM 3986 N N . GLY B 2 308 ? 14.360 68.987 33.837 1.00 18.69 ? 556 GLY B N 1 ATOM 3987 C CA . GLY B 2 308 ? 13.552 69.528 32.746 1.00 17.83 ? 556 GLY B CA 1 ATOM 3988 C C . GLY B 2 308 ? 14.365 69.933 31.531 1.00 17.17 ? 556 GLY B C 1 ATOM 3989 O O . GLY B 2 308 ? 15.602 69.946 31.573 1.00 17.17 ? 556 GLY B O 1 ATOM 3990 N N . PRO B 2 309 ? 13.667 70.207 30.418 1.00 16.75 ? 557 PRO B N 1 ATOM 3991 C CA . PRO B 2 309 ? 14.355 70.553 29.164 1.00 16.86 ? 557 PRO B CA 1 ATOM 3992 C C . PRO B 2 309 ? 15.114 71.878 29.312 1.00 17.08 ? 557 PRO B C 1 ATOM 3993 O O . PRO B 2 309 ? 14.743 72.704 30.149 1.00 16.50 ? 557 PRO B O 1 ATOM 3994 C CB . PRO B 2 309 ? 13.211 70.686 28.148 1.00 16.78 ? 557 PRO B CB 1 ATOM 3995 C CG . PRO B 2 309 ? 12.016 69.909 28.756 1.00 17.75 ? 557 PRO B CG 1 ATOM 3996 C CD . PRO B 2 309 ? 12.193 70.132 30.270 1.00 15.97 ? 557 PRO B CD 1 ATOM 3997 N N . THR B 2 310 ? 16.166 72.060 28.517 1.00 16.64 ? 558 THR B N 1 ATOM 3998 C CA . THR B 2 310 ? 17.033 73.227 28.661 1.00 16.63 ? 558 THR B CA 1 ATOM 3999 C C . THR B 2 310 ? 16.294 74.513 28.278 1.00 17.73 ? 558 THR B C 1 ATOM 4000 O O . THR B 2 310 ? 15.550 74.524 27.298 1.00 17.72 ? 558 THR B O 1 ATOM 4001 C CB . THR B 2 310 ? 18.306 73.112 27.808 1.00 16.66 ? 558 THR B CB 1 ATOM 4002 O OG1 . THR B 2 310 ? 19.102 74.284 28.003 1.00 17.24 ? 558 THR B OG1 1 ATOM 4003 C CG2 . THR B 2 310 ? 17.995 72.956 26.298 1.00 16.47 ? 558 THR B CG2 1 ATOM 4004 N N . TRP B 2 311 ? 16.551 75.573 29.034 1.00 18.41 ? 559 TRP B N 1 ATOM 4005 C CA . TRP B 2 311 ? 15.958 76.892 28.735 1.00 20.15 ? 559 TRP B CA 1 ATOM 4006 C C . TRP B 2 311 ? 17.012 78.007 28.859 1.00 21.61 ? 559 TRP B C 1 ATOM 4007 O O . TRP B 2 311 ? 16.661 79.186 29.013 1.00 20.93 ? 559 TRP B O 1 ATOM 4008 C CB . TRP B 2 311 ? 14.748 77.147 29.655 1.00 20.13 ? 559 TRP B CB 1 ATOM 4009 C CG . TRP B 2 311 ? 15.033 77.002 31.116 1.00 21.39 ? 559 TRP B CG 1 ATOM 4010 C CD1 . TRP B 2 311 ? 15.064 75.826 31.860 1.00 20.95 ? 559 TRP B CD1 1 ATOM 4011 C CD2 . TRP B 2 311 ? 15.319 78.061 32.037 1.00 23.39 ? 559 TRP B CD2 1 ATOM 4012 N NE1 . TRP B 2 311 ? 15.368 76.117 33.177 1.00 23.29 ? 559 TRP B NE1 1 ATOM 4013 C CE2 . TRP B 2 311 ? 15.511 77.475 33.309 1.00 23.85 ? 559 TRP B CE2 1 ATOM 4014 C CE3 . TRP B 2 311 ? 15.418 79.455 31.911 1.00 26.82 ? 559 TRP B CE3 1 ATOM 4015 C CZ2 . TRP B 2 311 ? 15.815 78.232 34.445 1.00 24.19 ? 559 TRP B CZ2 1 ATOM 4016 C CZ3 . TRP B 2 311 ? 15.709 80.207 33.051 1.00 23.25 ? 559 TRP B CZ3 1 ATOM 4017 C CH2 . TRP B 2 311 ? 15.913 79.588 34.294 1.00 24.34 ? 559 TRP B CH2 1 ATOM 4018 N N . ASP B 2 312 ? 18.295 77.639 28.764 1.00 21.07 ? 560 ASP B N 1 ATOM 4019 C CA . ASP B 2 312 ? 19.376 78.619 28.813 1.00 24.06 ? 560 ASP B CA 1 ATOM 4020 C C . ASP B 2 312 ? 19.294 79.592 27.645 1.00 24.29 ? 560 ASP B C 1 ATOM 4021 O O . ASP B 2 312 ? 19.430 80.815 27.835 1.00 25.67 ? 560 ASP B O 1 ATOM 4022 C CB . ASP B 2 312 ? 20.761 77.934 28.814 1.00 23.89 ? 560 ASP B CB 1 ATOM 4023 C CG . ASP B 2 312 ? 21.101 77.290 30.157 1.00 28.53 ? 560 ASP B CG 1 ATOM 4024 O OD1 . ASP B 2 312 ? 22.228 76.744 30.290 1.00 29.12 ? 560 ASP B OD1 1 ATOM 4025 O OD2 . ASP B 2 312 ? 20.265 77.364 31.096 1.00 28.29 ? 560 ASP B OD2 1 ATOM 4026 N N . GLN B 2 313 ? 19.097 79.059 26.453 1.00 24.72 ? 561 GLN B N 1 ATOM 4027 C CA . GLN B 2 313 ? 19.035 79.855 25.233 1.00 25.40 ? 561 GLN B CA 1 ATOM 4028 C C . GLN B 2 313 ? 17.814 79.500 24.386 1.00 26.63 ? 561 GLN B C 1 ATOM 4029 O O . GLN B 2 313 ? 17.582 80.100 23.342 1.00 29.27 ? 561 GLN B O 1 ATOM 4030 C CB . GLN B 2 313 ? 20.318 79.655 24.434 1.00 25.45 ? 561 GLN B CB 1 ATOM 4031 C CG . GLN B 2 313 ? 21.516 80.294 25.126 1.00 25.62 ? 561 GLN B CG 1 ATOM 4032 C CD . GLN B 2 313 ? 22.800 79.970 24.432 1.00 28.14 ? 561 GLN B CD 1 ATOM 4033 O OE1 . GLN B 2 313 ? 23.315 78.870 24.561 1.00 26.36 ? 561 GLN B OE1 1 ATOM 4034 N NE2 . GLN B 2 313 ? 23.325 80.929 23.670 1.00 29.37 ? 561 GLN B NE2 1 ATOM 4035 N N . CYS B 2 314 ? 17.074 78.484 24.801 1.00 24.80 ? 562 CYS B N 1 ATOM 4036 C CA . CYS B 2 314 ? 15.831 78.101 24.158 1.00 24.18 ? 562 CYS B CA 1 ATOM 4037 C C . CYS B 2 314 ? 14.695 78.569 25.067 1.00 23.13 ? 562 CYS B C 1 ATOM 4038 O O . CYS B 2 314 ? 14.879 78.673 26.287 1.00 21.68 ? 562 CYS B O 1 ATOM 4039 C CB . CYS B 2 314 ? 15.791 76.552 24.044 1.00 22.73 ? 562 CYS B CB 1 ATOM 4040 S SG . CYS B 2 314 ? 16.866 75.911 22.725 1.00 26.93 ? 562 CYS B SG 1 ATOM 4041 N N . PRO B 2 315 ? 13.495 78.804 24.495 1.00 23.38 ? 563 PRO B N 1 ATOM 4042 C CA . PRO B 2 315 ? 12.366 79.160 25.355 1.00 23.60 ? 563 PRO B CA 1 ATOM 4043 C C . PRO B 2 315 ? 11.986 77.941 26.223 1.00 22.99 ? 563 PRO B C 1 ATOM 4044 O O . PRO B 2 315 ? 12.043 76.796 25.723 1.00 22.05 ? 563 PRO B O 1 ATOM 4045 C CB . PRO B 2 315 ? 11.240 79.452 24.358 1.00 23.69 ? 563 PRO B CB 1 ATOM 4046 C CG . PRO B 2 315 ? 11.596 78.686 23.122 1.00 24.39 ? 563 PRO B CG 1 ATOM 4047 C CD . PRO B 2 315 ? 13.117 78.670 23.075 1.00 23.97 ? 563 PRO B CD 1 ATOM 4048 N N . PRO B 2 316 ? 11.632 78.170 27.501 1.00 22.74 ? 564 PRO B N 1 ATOM 4049 C CA . PRO B 2 316 ? 11.280 77.060 28.398 1.00 21.89 ? 564 PRO B CA 1 ATOM 4050 C C . PRO B 2 316 ? 10.149 76.226 27.835 1.00 21.95 ? 564 PRO B C 1 ATOM 4051 O O . PRO B 2 316 ? 9.207 76.757 27.197 1.00 21.17 ? 564 PRO B O 1 ATOM 4052 C CB . PRO B 2 316 ? 10.835 77.754 29.695 1.00 22.43 ? 564 PRO B CB 1 ATOM 4053 C CG . PRO B 2 316 ? 11.230 79.143 29.592 1.00 24.30 ? 564 PRO B CG 1 ATOM 4054 C CD . PRO B 2 316 ? 11.593 79.481 28.183 1.00 23.40 ? 564 PRO B CD 1 ATOM 4055 N N . PHE B 2 317 ? 10.247 74.911 28.021 1.00 19.86 ? 565 PHE B N 1 ATOM 4056 C CA . PHE B 2 317 ? 9.192 74.032 27.603 1.00 18.86 ? 565 PHE B CA 1 ATOM 4057 C C . PHE B 2 317 ? 7.969 74.257 28.472 1.00 19.18 ? 565 PHE B C 1 ATOM 4058 O O . PHE B 2 317 ? 8.091 74.352 29.690 1.00 17.81 ? 565 PHE B O 1 ATOM 4059 C CB . PHE B 2 317 ? 9.645 72.549 27.679 1.00 17.75 ? 565 PHE B CB 1 ATOM 4060 C CG . PHE B 2 317 ? 8.539 71.574 27.353 1.00 19.01 ? 565 PHE B CG 1 ATOM 4061 C CD1 . PHE B 2 317 ? 8.098 71.417 26.042 1.00 17.92 ? 565 PHE B CD1 1 ATOM 4062 C CD2 . PHE B 2 317 ? 7.920 70.853 28.360 1.00 19.74 ? 565 PHE B CD2 1 ATOM 4063 C CE1 . PHE B 2 317 ? 7.077 70.528 25.741 1.00 20.71 ? 565 PHE B CE1 1 ATOM 4064 C CE2 . PHE B 2 317 ? 6.877 69.964 28.058 1.00 20.38 ? 565 PHE B CE2 1 ATOM 4065 C CZ . PHE B 2 317 ? 6.451 69.831 26.741 1.00 19.25 ? 565 PHE B CZ 1 ATOM 4066 N N . GLN B 2 318 ? 6.789 74.300 27.852 1.00 19.78 ? 566 GLN B N 1 ATOM 4067 C CA . GLN B 2 318 ? 5.546 74.426 28.619 1.00 19.55 ? 566 GLN B CA 1 ATOM 4068 C C . GLN B 2 318 ? 4.469 73.576 27.962 1.00 19.75 ? 566 GLN B C 1 ATOM 4069 O O . GLN B 2 318 ? 4.134 73.826 26.807 1.00 20.48 ? 566 GLN B O 1 ATOM 4070 C CB . GLN B 2 318 ? 5.083 75.899 28.652 1.00 21.27 ? 566 GLN B CB 1 ATOM 4071 C CG . GLN B 2 318 ? 3.916 76.089 29.617 1.00 22.96 ? 566 GLN B CG 1 ATOM 4072 C CD . GLN B 2 318 ? 3.562 77.555 29.873 1.00 27.25 ? 566 GLN B CD 1 ATOM 4073 O OE1 . GLN B 2 318 ? 4.123 78.456 29.252 1.00 27.55 ? 566 GLN B OE1 1 ATOM 4074 N NE2 . GLN B 2 318 ? 2.626 77.784 30.786 1.00 26.80 ? 566 GLN B NE2 1 ATOM 4075 N N . TRP B 2 319 ? 3.940 72.580 28.673 1.00 19.29 ? 567 TRP B N 1 ATOM 4076 C CA . TRP B 2 319 ? 3.035 71.597 28.088 1.00 20.27 ? 567 TRP B CA 1 ATOM 4077 C C . TRP B 2 319 ? 1.875 72.270 27.391 1.00 21.40 ? 567 TRP B C 1 ATOM 4078 O O . TRP B 2 319 ? 1.616 71.999 26.218 1.00 21.79 ? 567 TRP B O 1 ATOM 4079 C CB . TRP B 2 319 ? 2.480 70.665 29.161 1.00 20.51 ? 567 TRP B CB 1 ATOM 4080 C CG . TRP B 2 319 ? 3.421 69.554 29.544 1.00 19.17 ? 567 TRP B CG 1 ATOM 4081 C CD1 . TRP B 2 319 ? 4.152 69.456 30.695 1.00 20.50 ? 567 TRP B CD1 1 ATOM 4082 C CD2 . TRP B 2 319 ? 3.686 68.368 28.784 1.00 19.45 ? 567 TRP B CD2 1 ATOM 4083 N NE1 . TRP B 2 319 ? 4.881 68.266 30.689 1.00 18.71 ? 567 TRP B NE1 1 ATOM 4084 C CE2 . TRP B 2 319 ? 4.607 67.587 29.529 1.00 18.54 ? 567 TRP B CE2 1 ATOM 4085 C CE3 . TRP B 2 319 ? 3.240 67.891 27.537 1.00 18.98 ? 567 TRP B CE3 1 ATOM 4086 C CZ2 . TRP B 2 319 ? 5.067 66.337 29.075 1.00 18.95 ? 567 TRP B CZ2 1 ATOM 4087 C CZ3 . TRP B 2 319 ? 3.699 66.644 27.082 1.00 19.75 ? 567 TRP B CZ3 1 ATOM 4088 C CH2 . TRP B 2 319 ? 4.621 65.895 27.854 1.00 19.46 ? 567 TRP B CH2 1 ATOM 4089 N N . SER B 2 320 ? 1.243 73.192 28.106 1.00 23.93 ? 568 SER B N 1 ATOM 4090 C CA . SER B 2 320 ? 0.005 73.823 27.597 1.00 25.58 ? 568 SER B CA 1 ATOM 4091 C C . SER B 2 320 ? 0.258 74.730 26.397 1.00 27.40 ? 568 SER B C 1 ATOM 4092 O O . SER B 2 320 ? -0.685 75.032 25.655 1.00 29.14 ? 568 SER B O 1 ATOM 4093 C CB . SER B 2 320 ? -0.708 74.581 28.705 1.00 24.88 ? 568 SER B CB 1 ATOM 4094 O OG . SER B 2 320 ? 0.059 75.681 29.127 1.00 25.00 ? 568 SER B OG 1 ATOM 4095 N N . LYS B 2 321 ? 1.510 75.170 26.215 1.00 28.18 ? 569 LYS B N 1 ATOM 4096 C CA . LYS B 2 321 ? 1.908 75.960 25.055 1.00 29.28 ? 569 LYS B CA 1 ATOM 4097 C C . LYS B 2 321 ? 2.920 75.187 24.220 1.00 29.50 ? 569 LYS B C 1 ATOM 4098 O O . LYS B 2 321 ? 4.000 75.707 23.881 1.00 31.50 ? 569 LYS B O 1 ATOM 4099 C CB . LYS B 2 321 ? 2.509 77.287 25.495 1.00 29.47 ? 569 LYS B CB 1 ATOM 4100 C CG . LYS B 2 321 ? 1.538 78.075 26.328 1.00 32.83 ? 569 LYS B CG 1 ATOM 4101 C CD . LYS B 2 321 ? 2.083 79.401 26.810 1.00 37.37 ? 569 LYS B CD 1 ATOM 4102 C CE . LYS B 2 321 ? 1.030 80.044 27.710 1.00 41.46 ? 569 LYS B CE 1 ATOM 4103 N NZ . LYS B 2 321 ? 1.513 81.295 28.359 1.00 46.15 ? 569 LYS B NZ 1 ATOM 4104 N N . SER B 2 322 ? 2.616 73.925 23.958 1.00 27.67 ? 570 SER B N 1 ATOM 4105 C CA . SER B 2 322 ? 3.451 73.118 23.091 1.00 26.84 ? 570 SER B CA 1 ATOM 4106 C C . SER B 2 322 ? 2.517 72.367 22.174 1.00 27.25 ? 570 SER B C 1 ATOM 4107 O O . SER B 2 322 ? 1.308 72.323 22.433 1.00 28.33 ? 570 SER B O 1 ATOM 4108 C CB . SER B 2 322 ? 4.254 72.114 23.920 1.00 25.94 ? 570 SER B CB 1 ATOM 4109 O OG . SER B 2 322 ? 3.425 71.036 24.314 1.00 24.00 ? 570 SER B OG 1 ATOM 4110 N N . PRO B 2 323 ? 3.059 71.748 21.123 1.00 27.57 ? 571 PRO B N 1 ATOM 4111 C CA . PRO B 2 323 ? 2.253 70.864 20.268 1.00 27.91 ? 571 PRO B CA 1 ATOM 4112 C C . PRO B 2 323 ? 1.706 69.643 21.011 1.00 27.83 ? 571 PRO B C 1 ATOM 4113 O O . PRO B 2 323 ? 0.897 68.898 20.453 1.00 28.31 ? 571 PRO B O 1 ATOM 4114 C CB . PRO B 2 323 ? 3.259 70.392 19.195 1.00 28.34 ? 571 PRO B CB 1 ATOM 4115 C CG . PRO B 2 323 ? 4.422 71.363 19.262 1.00 28.78 ? 571 PRO B CG 1 ATOM 4116 C CD . PRO B 2 323 ? 4.458 71.877 20.664 1.00 28.04 ? 571 PRO B CD 1 ATOM 4117 N N . PHE B 2 324 ? 2.145 69.434 22.256 1.00 26.86 ? 572 PHE B N 1 ATOM 4118 C CA . PHE B 2 324 ? 1.936 68.156 22.947 1.00 26.58 ? 572 PHE B CA 1 ATOM 4119 C C . PHE B 2 324 ? 1.021 68.259 24.166 1.00 27.33 ? 572 PHE B C 1 ATOM 4120 O O . PHE B 2 324 ? 0.977 67.363 25.020 1.00 26.96 ? 572 PHE B O 1 ATOM 4121 C CB . PHE B 2 324 ? 3.312 67.558 23.313 1.00 25.89 ? 572 PHE B CB 1 ATOM 4122 C CG . PHE B 2 324 ? 4.221 67.413 22.120 1.00 25.55 ? 572 PHE B CG 1 ATOM 4123 C CD1 . PHE B 2 324 ? 3.895 66.548 21.084 1.00 24.84 ? 572 PHE B CD1 1 ATOM 4124 C CD2 . PHE B 2 324 ? 5.387 68.178 22.013 1.00 26.18 ? 572 PHE B CD2 1 ATOM 4125 C CE1 . PHE B 2 324 ? 4.710 66.417 19.966 1.00 26.02 ? 572 PHE B CE1 1 ATOM 4126 C CE2 . PHE B 2 324 ? 6.206 68.066 20.880 1.00 26.21 ? 572 PHE B CE2 1 ATOM 4127 C CZ . PHE B 2 324 ? 5.879 67.184 19.868 1.00 26.75 ? 572 PHE B CZ 1 ATOM 4128 N N . HIS B 2 325 ? 0.254 69.346 24.212 1.00 27.94 ? 573 HIS B N 1 ATOM 4129 C CA . HIS B 2 325 ? -0.603 69.655 25.350 1.00 29.75 ? 573 HIS B CA 1 ATOM 4130 C C . HIS B 2 325 ? -1.609 68.540 25.706 1.00 29.77 ? 573 HIS B C 1 ATOM 4131 O O . HIS B 2 325 ? -2.045 68.441 26.861 1.00 31.16 ? 573 HIS B O 1 ATOM 4132 C CB . HIS B 2 325 ? -1.324 70.975 25.074 1.00 30.53 ? 573 HIS B CB 1 ATOM 4133 C CG . HIS B 2 325 ? -2.147 70.956 23.822 1.00 33.24 ? 573 HIS B CG 1 ATOM 4134 N ND1 . HIS B 2 325 ? -3.428 70.443 23.783 1.00 36.72 ? 573 HIS B ND1 1 ATOM 4135 C CD2 . HIS B 2 325 ? -1.870 71.371 22.562 1.00 36.51 ? 573 HIS B CD2 1 ATOM 4136 C CE1 . HIS B 2 325 ? -3.905 70.543 22.556 1.00 36.96 ? 573 HIS B CE1 1 ATOM 4137 N NE2 . HIS B 2 325 ? -2.986 71.116 21.797 1.00 38.91 ? 573 HIS B NE2 1 ATOM 4138 N N . SER B 2 326 ? -1.956 67.686 24.748 1.00 28.92 ? 574 SER B N 1 ATOM 4139 C CA A SER B 2 326 ? -2.933 66.623 25.003 0.50 29.12 ? 574 SER B CA 1 ATOM 4140 C CA B SER B 2 326 ? -2.935 66.623 24.995 0.50 29.10 ? 574 SER B CA 1 ATOM 4141 C C . SER B 2 326 ? -2.347 65.332 25.577 1.00 29.05 ? 574 SER B C 1 ATOM 4142 O O . SER B 2 326 ? -3.097 64.448 26.029 1.00 29.01 ? 574 SER B O 1 ATOM 4143 C CB A SER B 2 326 ? -3.721 66.295 23.731 0.50 29.33 ? 574 SER B CB 1 ATOM 4144 C CB B SER B 2 326 ? -3.723 66.301 23.715 0.50 29.30 ? 574 SER B CB 1 ATOM 4145 O OG A SER B 2 326 ? -4.616 67.339 23.407 0.50 30.13 ? 574 SER B OG 1 ATOM 4146 O OG B SER B 2 326 ? -2.896 65.706 22.725 0.50 29.93 ? 574 SER B OG 1 ATOM 4147 N N . MET B 2 327 ? -1.017 65.189 25.543 1.00 27.00 ? 575 MET B N 1 ATOM 4148 C CA . MET B 2 327 ? -0.406 64.009 26.113 1.00 26.64 ? 575 MET B CA 1 ATOM 4149 C C . MET B 2 327 ? -0.575 63.971 27.629 1.00 26.12 ? 575 MET B C 1 ATOM 4150 O O . MET B 2 327 ? -0.555 65.015 28.294 1.00 26.60 ? 575 MET B O 1 ATOM 4151 C CB . MET B 2 327 ? 1.093 63.976 25.796 1.00 26.03 ? 575 MET B CB 1 ATOM 4152 C CG . MET B 2 327 ? 1.403 63.703 24.374 1.00 28.80 ? 575 MET B CG 1 ATOM 4153 S SD . MET B 2 327 ? 3.210 63.644 24.192 1.00 32.10 ? 575 MET B SD 1 ATOM 4154 C CE . MET B 2 327 ? 3.262 63.285 22.453 1.00 33.23 ? 575 MET B CE 1 ATOM 4155 N N . LEU B 2 328 ? -0.743 62.773 28.181 1.00 25.53 ? 576 LEU B N 1 ATOM 4156 C CA . LEU B 2 328 ? -0.855 62.663 29.624 1.00 24.94 ? 576 LEU B CA 1 ATOM 4157 C C . LEU B 2 328 ? 0.460 63.060 30.278 1.00 23.73 ? 576 LEU B C 1 ATOM 4158 O O . LEU B 2 328 ? 1.511 62.571 29.878 1.00 22.73 ? 576 LEU B O 1 ATOM 4159 C CB . LEU B 2 328 ? -1.191 61.242 30.053 1.00 26.08 ? 576 LEU B CB 1 ATOM 4160 C CG . LEU B 2 328 ? -2.654 60.871 30.284 1.00 30.01 ? 576 LEU B CG 1 ATOM 4161 C CD1 . LEU B 2 328 ? -2.758 59.667 31.243 1.00 31.79 ? 576 LEU B CD1 1 ATOM 4162 C CD2 . LEU B 2 328 ? -3.420 62.051 30.862 1.00 32.13 ? 576 LEU B CD2 1 ATOM 4163 N N . HIS B 2 329 ? 0.384 63.930 31.286 1.00 21.73 ? 577 HIS B N 1 ATOM 4164 C CA . HIS B 2 329 ? 1.556 64.307 32.081 1.00 21.12 ? 577 HIS B CA 1 ATOM 4165 C C . HIS B 2 329 ? 1.148 64.578 33.525 1.00 20.63 ? 577 HIS B C 1 ATOM 4166 O O . HIS B 2 329 ? 1.530 65.589 34.104 1.00 19.85 ? 577 HIS B O 1 ATOM 4167 C CB . HIS B 2 329 ? 2.324 65.494 31.462 1.00 20.56 ? 577 HIS B CB 1 ATOM 4168 C CG . HIS B 2 329 ? 1.479 66.704 31.180 1.00 23.21 ? 577 HIS B CG 1 ATOM 4169 N ND1 . HIS B 2 329 ? 0.695 66.816 30.049 1.00 25.66 ? 577 HIS B ND1 1 ATOM 4170 C CD2 . HIS B 2 329 ? 1.331 67.868 31.859 1.00 23.23 ? 577 HIS B CD2 1 ATOM 4171 C CE1 . HIS B 2 329 ? 0.097 67.995 30.042 1.00 24.75 ? 577 HIS B CE1 1 ATOM 4172 N NE2 . HIS B 2 329 ? 0.459 68.652 31.132 1.00 25.06 ? 577 HIS B NE2 1 ATOM 4173 N N . MET B 2 330 ? 0.372 63.642 34.090 1.00 20.06 ? 578 MET B N 1 ATOM 4174 C CA . MET B 2 330 ? -0.118 63.746 35.458 1.00 21.14 ? 578 MET B CA 1 ATOM 4175 C C . MET B 2 330 ? 0.990 64.021 36.439 1.00 20.65 ? 578 MET B C 1 ATOM 4176 O O . MET B 2 330 ? 2.052 63.378 36.388 1.00 19.17 ? 578 MET B O 1 ATOM 4177 C CB . MET B 2 330 ? -0.813 62.429 35.871 1.00 21.93 ? 578 MET B CB 1 ATOM 4178 C CG . MET B 2 330 ? -1.900 61.977 34.947 1.00 26.42 ? 578 MET B CG 1 ATOM 4179 S SD . MET B 2 330 ? -2.663 60.462 35.657 1.00 30.06 ? 578 MET B SD 1 ATOM 4180 C CE . MET B 2 330 ? -3.081 61.028 37.286 1.00 32.32 ? 578 MET B CE 1 ATOM 4181 N N . GLY B 2 331 ? 0.769 64.982 37.333 1.00 19.56 ? 579 GLY B N 1 ATOM 4182 C CA . GLY B 2 331 ? 1.751 65.278 38.359 1.00 20.22 ? 579 GLY B CA 1 ATOM 4183 C C . GLY B 2 331 ? 2.866 66.228 37.962 1.00 19.98 ? 579 GLY B C 1 ATOM 4184 O O . GLY B 2 331 ? 3.634 66.701 38.814 1.00 20.72 ? 579 GLY B O 1 ATOM 4185 N N . GLN B 2 332 ? 3.004 66.481 36.670 1.00 19.88 ? 580 GLN B N 1 ATOM 4186 C CA . GLN B 2 332 ? 4.121 67.306 36.201 1.00 20.57 ? 580 GLN B CA 1 ATOM 4187 C C . GLN B 2 332 ? 3.758 68.772 36.233 1.00 21.62 ? 580 GLN B C 1 ATOM 4188 O O . GLN B 2 332 ? 2.613 69.129 35.909 1.00 21.43 ? 580 GLN B O 1 ATOM 4189 C CB . GLN B 2 332 ? 4.493 66.962 34.758 1.00 19.93 ? 580 GLN B CB 1 ATOM 4190 C CG . GLN B 2 332 ? 5.193 65.595 34.605 1.00 17.65 ? 580 GLN B CG 1 ATOM 4191 C CD . GLN B 2 332 ? 5.748 65.407 33.197 1.00 18.62 ? 580 GLN B CD 1 ATOM 4192 O OE1 . GLN B 2 332 ? 6.044 66.376 32.508 1.00 17.65 ? 580 GLN B OE1 1 ATOM 4193 N NE2 . GLN B 2 332 ? 5.902 64.148 32.777 1.00 19.65 ? 580 GLN B NE2 1 ATOM 4194 N N . PRO B 2 333 ? 4.742 69.631 36.520 1.00 22.05 ? 581 PRO B N 1 ATOM 4195 C CA . PRO B 2 333 ? 4.560 71.066 36.255 1.00 22.67 ? 581 PRO B CA 1 ATOM 4196 C C . PRO B 2 333 ? 4.181 71.336 34.791 1.00 22.76 ? 581 PRO B C 1 ATOM 4197 O O . PRO B 2 333 ? 4.588 70.599 33.869 1.00 22.59 ? 581 PRO B O 1 ATOM 4198 C CB . PRO B 2 333 ? 5.956 71.642 36.557 1.00 23.09 ? 581 PRO B CB 1 ATOM 4199 C CG . PRO B 2 333 ? 6.521 70.710 37.566 1.00 23.04 ? 581 PRO B CG 1 ATOM 4200 C CD . PRO B 2 333 ? 6.073 69.350 37.095 1.00 22.19 ? 581 PRO B CD 1 ATOM 4201 N N . ASP B 2 334 ? 3.397 72.399 34.557 1.00 22.04 ? 582 ASP B N 1 ATOM 4202 C CA . ASP B 2 334 ? 3.131 72.830 33.206 1.00 22.11 ? 582 ASP B CA 1 ATOM 4203 C C . ASP B 2 334 ? 4.378 73.470 32.591 1.00 21.52 ? 582 ASP B C 1 ATOM 4204 O O . ASP B 2 334 ? 4.818 73.076 31.503 1.00 21.84 ? 582 ASP B O 1 ATOM 4205 C CB . ASP B 2 334 ? 1.956 73.825 33.189 1.00 22.58 ? 582 ASP B CB 1 ATOM 4206 C CG . ASP B 2 334 ? 1.535 74.198 31.798 1.00 23.71 ? 582 ASP B CG 1 ATOM 4207 O OD1 . ASP B 2 334 ? 1.474 73.304 30.918 1.00 23.04 ? 582 ASP B OD1 1 ATOM 4208 O OD2 . ASP B 2 334 ? 1.241 75.400 31.589 1.00 26.03 ? 582 ASP B OD2 1 ATOM 4209 N N . LEU B 2 335 ? 4.926 74.475 33.269 1.00 21.48 ? 583 LEU B N 1 ATOM 4210 C CA . LEU B 2 335 ? 6.075 75.210 32.748 1.00 20.65 ? 583 LEU B CA 1 ATOM 4211 C C . LEU B 2 335 ? 7.328 74.660 33.386 1.00 20.90 ? 583 LEU B C 1 ATOM 4212 O O . LEU B 2 335 ? 7.354 74.426 34.586 1.00 21.08 ? 583 LEU B O 1 ATOM 4213 C CB . LEU B 2 335 ? 5.965 76.691 33.113 1.00 21.78 ? 583 LEU B CB 1 ATOM 4214 C CG . LEU B 2 335 ? 7.139 77.628 32.757 1.00 22.22 ? 583 LEU B CG 1 ATOM 4215 C CD1 . LEU B 2 335 ? 7.284 77.813 31.244 1.00 24.40 ? 583 LEU B CD1 1 ATOM 4216 C CD2 . LEU B 2 335 ? 6.874 78.964 33.488 1.00 26.55 ? 583 LEU B CD2 1 ATOM 4217 N N . TRP B 2 336 ? 8.352 74.446 32.571 1.00 19.91 ? 584 TRP B N 1 ATOM 4218 C CA . TRP B 2 336 ? 9.610 73.873 33.067 1.00 21.21 ? 584 TRP B CA 1 ATOM 4219 C C . TRP B 2 336 ? 10.690 74.930 32.979 1.00 21.28 ? 584 TRP B C 1 ATOM 4220 O O . TRP B 2 336 ? 11.292 75.143 31.925 1.00 22.94 ? 584 TRP B O 1 ATOM 4221 C CB . TRP B 2 336 ? 9.977 72.629 32.223 1.00 20.21 ? 584 TRP B CB 1 ATOM 4222 C CG . TRP B 2 336 ? 9.093 71.473 32.593 1.00 20.34 ? 584 TRP B CG 1 ATOM 4223 C CD1 . TRP B 2 336 ? 7.814 71.203 32.146 1.00 20.12 ? 584 TRP B CD1 1 ATOM 4224 C CD2 . TRP B 2 336 ? 9.413 70.453 33.538 1.00 19.30 ? 584 TRP B CD2 1 ATOM 4225 N NE1 . TRP B 2 336 ? 7.331 70.072 32.776 1.00 21.98 ? 584 TRP B NE1 1 ATOM 4226 C CE2 . TRP B 2 336 ? 8.291 69.589 33.629 1.00 21.99 ? 584 TRP B CE2 1 ATOM 4227 C CE3 . TRP B 2 336 ? 10.525 70.216 34.353 1.00 18.10 ? 584 TRP B CE3 1 ATOM 4228 C CZ2 . TRP B 2 336 ? 8.276 68.467 34.481 1.00 22.20 ? 584 TRP B CZ2 1 ATOM 4229 C CZ3 . TRP B 2 336 ? 10.521 69.120 35.195 1.00 18.08 ? 584 TRP B CZ3 1 ATOM 4230 C CH2 . TRP B 2 336 ? 9.398 68.251 35.259 1.00 19.79 ? 584 TRP B CH2 1 ATOM 4231 N N . MET B 2 337 ? 10.927 75.595 34.100 1.00 21.67 ? 585 MET B N 1 ATOM 4232 C CA A MET B 2 337 ? 11.913 76.648 34.181 0.50 22.52 ? 585 MET B CA 1 ATOM 4233 C CA B MET B 2 337 ? 11.962 76.622 34.151 0.50 22.57 ? 585 MET B CA 1 ATOM 4234 C C . MET B 2 337 ? 12.726 76.491 35.470 1.00 23.04 ? 585 MET B C 1 ATOM 4235 O O . MET B 2 337 ? 12.855 77.449 36.251 1.00 23.87 ? 585 MET B O 1 ATOM 4236 C CB A MET B 2 337 ? 11.165 77.984 34.214 0.50 22.90 ? 585 MET B CB 1 ATOM 4237 C CB B MET B 2 337 ? 11.338 78.026 33.988 0.50 23.21 ? 585 MET B CB 1 ATOM 4238 C CG A MET B 2 337 ? 11.731 79.044 33.328 0.50 23.83 ? 585 MET B CG 1 ATOM 4239 C CG B MET B 2 337 ? 12.346 79.158 33.858 0.50 24.16 ? 585 MET B CG 1 ATOM 4240 S SD A MET B 2 337 ? 10.556 80.431 33.280 0.50 24.34 ? 585 MET B SD 1 ATOM 4241 S SD B MET B 2 337 ? 11.607 80.727 33.264 0.50 28.94 ? 585 MET B SD 1 ATOM 4242 C CE A MET B 2 337 ? 10.360 80.780 35.004 0.50 24.25 ? 585 MET B CE 1 ATOM 4243 C CE B MET B 2 337 ? 12.967 81.864 33.434 0.50 28.07 ? 585 MET B CE 1 ATOM 4244 N N . PHE B 2 338 ? 13.242 75.285 35.729 1.00 22.01 ? 586 PHE B N 1 ATOM 4245 C CA . PHE B 2 338 ? 13.928 75.030 36.996 1.00 21.29 ? 586 PHE B CA 1 ATOM 4246 C C . PHE B 2 338 ? 15.434 75.234 36.867 1.00 22.41 ? 586 PHE B C 1 ATOM 4247 O O . PHE B 2 338 ? 16.012 74.994 35.821 1.00 22.79 ? 586 PHE B O 1 ATOM 4248 C CB . PHE B 2 338 ? 13.629 73.614 37.529 1.00 20.01 ? 586 PHE B CB 1 ATOM 4249 C CG . PHE B 2 338 ? 12.152 73.356 37.792 1.00 20.25 ? 586 PHE B CG 1 ATOM 4250 C CD1 . PHE B 2 338 ? 11.489 73.977 38.854 1.00 19.31 ? 586 PHE B CD1 1 ATOM 4251 C CD2 . PHE B 2 338 ? 11.431 72.517 36.956 1.00 19.44 ? 586 PHE B CD2 1 ATOM 4252 C CE1 . PHE B 2 338 ? 10.105 73.748 39.093 1.00 20.10 ? 586 PHE B CE1 1 ATOM 4253 C CE2 . PHE B 2 338 ? 10.038 72.267 37.184 1.00 21.78 ? 586 PHE B CE2 1 ATOM 4254 C CZ . PHE B 2 338 ? 9.381 72.900 38.233 1.00 21.46 ? 586 PHE B CZ 1 ATOM 4255 N N . SER B 2 339 ? 16.069 75.648 37.960 1.00 23.20 ? 587 SER B N 1 ATOM 4256 C CA . SER B 2 339 ? 17.524 75.826 37.974 1.00 24.36 ? 587 SER B CA 1 ATOM 4257 C C . SER B 2 339 ? 18.146 74.671 38.745 1.00 23.45 ? 587 SER B C 1 ATOM 4258 O O . SER B 2 339 ? 17.438 73.964 39.466 1.00 23.45 ? 587 SER B O 1 ATOM 4259 C CB . SER B 2 339 ? 17.872 77.139 38.677 1.00 24.86 ? 587 SER B CB 1 ATOM 4260 O OG . SER B 2 339 ? 17.490 78.234 37.859 1.00 30.23 ? 587 SER B OG 1 ATOM 4261 N N . PRO B 2 340 ? 19.469 74.476 38.604 1.00 23.51 ? 588 PRO B N 1 ATOM 4262 C CA . PRO B 2 340 ? 20.105 73.369 39.313 1.00 23.70 ? 588 PRO B CA 1 ATOM 4263 C C . PRO B 2 340 ? 19.993 73.518 40.821 1.00 23.61 ? 588 PRO B C 1 ATOM 4264 O O . PRO B 2 340 ? 19.970 74.653 41.344 1.00 23.79 ? 588 PRO B O 1 ATOM 4265 C CB . PRO B 2 340 ? 21.586 73.453 38.905 1.00 23.45 ? 588 PRO B CB 1 ATOM 4266 C CG . PRO B 2 340 ? 21.649 74.424 37.765 1.00 24.02 ? 588 PRO B CG 1 ATOM 4267 C CD . PRO B 2 340 ? 20.412 75.260 37.786 1.00 24.22 ? 588 PRO B CD 1 ATOM 4268 N N . ILE B 2 341 ? 19.911 72.397 41.516 1.00 23.21 ? 589 ILE B N 1 ATOM 4269 C CA . ILE B 2 341 ? 19.907 72.397 42.968 1.00 24.22 ? 589 ILE B CA 1 ATOM 4270 C C . ILE B 2 341 ? 20.984 71.431 43.446 1.00 25.04 ? 589 ILE B C 1 ATOM 4271 O O . ILE B 2 341 ? 21.360 70.516 42.726 1.00 23.25 ? 589 ILE B O 1 ATOM 4272 C CB . ILE B 2 341 ? 18.563 71.965 43.554 1.00 24.80 ? 589 ILE B CB 1 ATOM 4273 C CG1 . ILE B 2 341 ? 18.164 70.578 43.016 1.00 26.01 ? 589 ILE B CG1 1 ATOM 4274 C CG2 . ILE B 2 341 ? 17.466 72.988 43.234 1.00 25.67 ? 589 ILE B CG2 1 ATOM 4275 C CD1 . ILE B 2 341 ? 17.173 69.851 43.864 1.00 31.89 ? 589 ILE B CD1 1 ATOM 4276 N N . ARG B 2 342 ? 21.476 71.640 44.668 1.00 25.90 ? 590 ARG B N 1 ATOM 4277 C CA . ARG B 2 342 ? 22.396 70.694 45.288 1.00 28.59 ? 590 ARG B CA 1 ATOM 4278 C C . ARG B 2 342 ? 21.610 69.594 45.968 1.00 29.64 ? 590 ARG B C 1 ATOM 4279 O O . ARG B 2 342 ? 20.646 69.856 46.705 1.00 28.84 ? 590 ARG B O 1 ATOM 4280 C CB . ARG B 2 342 ? 23.262 71.415 46.313 1.00 29.23 ? 590 ARG B CB 1 ATOM 4281 C CG . ARG B 2 342 ? 24.049 70.487 47.204 1.00 35.20 ? 590 ARG B CG 1 ATOM 4282 C CD . ARG B 2 342 ? 25.401 70.122 46.575 1.00 42.87 ? 590 ARG B CD 1 ATOM 4283 N NE . ARG B 2 342 ? 26.396 69.677 47.566 1.00 49.29 ? 590 ARG B NE 1 ATOM 4284 C CZ . ARG B 2 342 ? 26.120 69.036 48.707 1.00 51.49 ? 590 ARG B CZ 1 ATOM 4285 N NH1 . ARG B 2 342 ? 24.857 68.742 49.029 1.00 53.74 ? 590 ARG B NH1 1 ATOM 4286 N NH2 . ARG B 2 342 ? 27.116 68.663 49.519 1.00 51.91 ? 590 ARG B NH2 1 ATOM 4287 N N . VAL B 2 343 ? 21.994 68.348 45.721 1.00 30.93 ? 591 VAL B N 1 ATOM 4288 C CA . VAL B 2 343 ? 21.234 67.218 46.199 1.00 35.28 ? 591 VAL B CA 1 ATOM 4289 C C . VAL B 2 343 ? 22.212 66.251 46.831 1.00 38.51 ? 591 VAL B C 1 ATOM 4290 O O . VAL B 2 343 ? 23.066 65.706 46.123 1.00 38.48 ? 591 VAL B O 1 ATOM 4291 C CB . VAL B 2 343 ? 20.516 66.480 45.036 1.00 35.08 ? 591 VAL B CB 1 ATOM 4292 C CG1 . VAL B 2 343 ? 19.632 65.396 45.600 1.00 37.78 ? 591 VAL B CG1 1 ATOM 4293 C CG2 . VAL B 2 343 ? 19.654 67.454 44.218 1.00 36.64 ? 591 VAL B CG2 1 ATOM 4294 N N . PRO B 2 344 ? 22.091 66.013 48.157 1.00 40.82 ? 592 PRO B N 1 ATOM 4295 C CA . PRO B 2 344 ? 20.978 66.433 49.010 1.00 42.25 ? 592 PRO B CA 1 ATOM 4296 C C . PRO B 2 344 ? 21.110 67.867 49.482 1.00 43.22 ? 592 PRO B C 1 ATOM 4297 O O . PRO B 2 344 ? 20.095 68.461 49.879 1.00 45.65 ? 592 PRO B O 1 ATOM 4298 C CB . PRO B 2 344 ? 21.086 65.473 50.204 1.00 42.53 ? 592 PRO B CB 1 ATOM 4299 C CG . PRO B 2 344 ? 22.566 65.250 50.351 1.00 42.28 ? 592 PRO B CG 1 ATOM 4300 C CD . PRO B 2 344 ? 23.119 65.278 48.927 1.00 41.58 ? 592 PRO B CD 1 HETATM 4301 C C1 . NAG C 3 . ? 15.501 35.683 56.370 1.00 20.08 ? 11 NAG A C1 1 HETATM 4302 C C2 . NAG C 3 . ? 15.391 34.155 56.200 1.00 21.30 ? 11 NAG A C2 1 HETATM 4303 C C3 . NAG C 3 . ? 13.937 33.669 56.075 1.00 23.77 ? 11 NAG A C3 1 HETATM 4304 C C4 . NAG C 3 . ? 13.074 34.252 57.181 1.00 23.53 ? 11 NAG A C4 1 HETATM 4305 C C5 . NAG C 3 . ? 13.313 35.764 57.333 1.00 22.06 ? 11 NAG A C5 1 HETATM 4306 C C6 . NAG C 3 . ? 12.517 36.354 58.510 1.00 26.42 ? 11 NAG A C6 1 HETATM 4307 C C7 . NAG C 3 . ? 15.866 34.020 53.785 1.00 21.54 ? 11 NAG A C7 1 HETATM 4308 C C8 . NAG C 3 . ? 16.759 33.480 52.707 1.00 21.83 ? 11 NAG A C8 1 HETATM 4309 N N2 . NAG C 3 . ? 16.161 33.705 55.054 1.00 21.53 ? 11 NAG A N2 1 HETATM 4310 O O3 . NAG C 3 . ? 13.879 32.236 56.070 1.00 23.79 ? 11 NAG A O3 1 HETATM 4311 O O4 . NAG C 3 . ? 11.710 34.067 56.831 1.00 23.85 ? 11 NAG A O4 1 HETATM 4312 O O5 . NAG C 3 . ? 14.702 36.023 57.504 1.00 22.51 ? 11 NAG A O5 1 HETATM 4313 O O6 . NAG C 3 . ? 12.879 35.666 59.697 1.00 27.36 ? 11 NAG A O6 1 HETATM 4314 O O7 . NAG C 3 . ? 14.918 34.712 53.446 1.00 21.13 ? 11 NAG A O7 1 HETATM 4315 C C1 . NAG D 3 . ? 10.935 33.061 57.607 1.00 34.38 ? 12 NAG A C1 1 HETATM 4316 C C2 . NAG D 3 . ? 9.461 33.382 57.397 1.00 35.02 ? 12 NAG A C2 1 HETATM 4317 C C3 . NAG D 3 . ? 8.667 32.308 58.125 1.00 37.59 ? 12 NAG A C3 1 HETATM 4318 C C4 . NAG D 3 . ? 9.059 30.955 57.563 1.00 38.84 ? 12 NAG A C4 1 HETATM 4319 C C5 . NAG D 3 . ? 10.577 30.751 57.459 1.00 38.90 ? 12 NAG A C5 1 HETATM 4320 C C6 . NAG D 3 . ? 10.823 29.544 56.570 1.00 39.32 ? 12 NAG A C6 1 HETATM 4321 C C7 . NAG D 3 . ? 8.478 35.595 57.067 1.00 33.18 ? 12 NAG A C7 1 HETATM 4322 C C8 . NAG D 3 . ? 8.238 36.974 57.621 1.00 35.12 ? 12 NAG A C8 1 HETATM 4323 N N2 . NAG D 3 . ? 9.128 34.725 57.836 1.00 33.02 ? 12 NAG A N2 1 HETATM 4324 O O3 . NAG D 3 . ? 7.306 32.501 57.854 1.00 38.05 ? 12 NAG A O3 1 HETATM 4325 O O4 . NAG D 3 . ? 8.481 29.943 58.362 1.00 44.53 ? 12 NAG A O4 1 HETATM 4326 O O5 . NAG D 3 . ? 11.255 31.883 56.899 1.00 34.28 ? 12 NAG A O5 1 HETATM 4327 O O6 . NAG D 3 . ? 12.199 29.276 56.594 1.00 44.19 ? 12 NAG A O6 1 HETATM 4328 O O7 . NAG D 3 . ? 8.057 35.330 55.942 1.00 35.55 ? 12 NAG A O7 1 HETATM 4329 C C1 . NAG E 3 . ? 12.024 37.642 13.483 1.00 57.11 ? 21 NAG A C1 1 HETATM 4330 C C2 . NAG E 3 . ? 12.125 36.272 14.155 1.00 59.33 ? 21 NAG A C2 1 HETATM 4331 C C3 . NAG E 3 . ? 13.223 35.399 13.555 1.00 60.54 ? 21 NAG A C3 1 HETATM 4332 C C4 . NAG E 3 . ? 13.129 35.348 12.034 1.00 62.01 ? 21 NAG A C4 1 HETATM 4333 C C5 . NAG E 3 . ? 13.042 36.769 11.480 1.00 61.71 ? 21 NAG A C5 1 HETATM 4334 C C6 . NAG E 3 . ? 12.843 36.724 9.968 1.00 63.25 ? 21 NAG A C6 1 HETATM 4335 C C7 . NAG E 3 . ? 11.444 36.160 16.463 1.00 58.96 ? 21 NAG A C7 1 HETATM 4336 C C8 . NAG E 3 . ? 11.840 36.066 17.908 1.00 57.55 ? 21 NAG A C8 1 HETATM 4337 N N2 . NAG E 3 . ? 12.397 36.403 15.573 1.00 59.31 ? 21 NAG A N2 1 HETATM 4338 O O3 . NAG E 3 . ? 13.152 34.105 14.119 1.00 60.66 ? 21 NAG A O3 1 HETATM 4339 O O4 . NAG E 3 . ? 14.268 34.691 11.505 1.00 62.95 ? 21 NAG A O4 1 HETATM 4340 O O5 . NAG E 3 . ? 11.963 37.477 12.071 1.00 61.38 ? 21 NAG A O5 1 HETATM 4341 O O6 . NAG E 3 . ? 13.633 37.720 9.351 1.00 64.68 ? 21 NAG A O6 1 HETATM 4342 O O7 . NAG E 3 . ? 10.279 36.023 16.120 1.00 59.23 ? 21 NAG A O7 1 HETATM 4343 C C1 . NAG F 3 . ? 13.880 62.184 55.731 1.00 99.05 ? 1 NAG A C1 1 HETATM 4344 C C2 . NAG F 3 . ? 14.221 63.447 54.944 1.00 98.56 ? 1 NAG A C2 1 HETATM 4345 C C3 . NAG F 3 . ? 15.476 64.132 55.475 1.00 99.46 ? 1 NAG A C3 1 HETATM 4346 C C4 . NAG F 3 . ? 15.435 64.234 56.993 1.00 100.00 ? 1 NAG A C4 1 HETATM 4347 C C5 . NAG F 3 . ? 15.115 62.872 57.588 1.00 100.13 ? 1 NAG A C5 1 HETATM 4348 C C6 . NAG F 3 . ? 15.118 62.950 59.107 1.00 100.12 ? 1 NAG A C6 1 HETATM 4349 C C7 . NAG F 3 . ? 13.415 63.230 52.666 1.00 95.41 ? 1 NAG A C7 1 HETATM 4350 C C8 . NAG F 3 . ? 13.592 62.529 51.356 1.00 95.30 ? 1 NAG A C8 1 HETATM 4351 N N2 . NAG F 3 . ? 14.407 63.114 53.545 1.00 96.90 ? 1 NAG A N2 1 HETATM 4352 O O3 . NAG F 3 . ? 15.583 65.424 54.923 1.00 99.71 ? 1 NAG A O3 1 HETATM 4353 O O4 . NAG F 3 . ? 16.673 64.696 57.487 1.00 100.07 ? 1 NAG A O4 1 HETATM 4354 O O5 . NAG F 3 . ? 13.852 62.463 57.115 1.00 99.74 ? 1 NAG A O5 1 HETATM 4355 O O6 . NAG F 3 . ? 16.244 63.695 59.512 1.00 99.53 ? 1 NAG A O6 1 HETATM 4356 O O7 . NAG F 3 . ? 12.394 63.875 52.890 1.00 93.53 ? 1 NAG A O7 1 HETATM 4357 C C1 . GOL G 4 . ? 16.989 31.256 48.073 1.00 61.32 ? 9 GOL A C1 1 HETATM 4358 O O1 . GOL G 4 . ? 16.740 31.335 49.462 1.00 58.41 ? 9 GOL A O1 1 HETATM 4359 C C2 . GOL G 4 . ? 16.361 30.012 47.434 1.00 61.46 ? 9 GOL A C2 1 HETATM 4360 O O2 . GOL G 4 . ? 17.386 29.074 47.176 1.00 62.72 ? 9 GOL A O2 1 HETATM 4361 C C3 . GOL G 4 . ? 15.703 30.397 46.107 1.00 61.75 ? 9 GOL A C3 1 HETATM 4362 O O3 . GOL G 4 . ? 14.894 29.348 45.616 1.00 61.46 ? 9 GOL A O3 1 HETATM 4363 C C1 . GOL H 4 . ? 2.575 47.467 22.732 1.00 59.02 ? 10 GOL A C1 1 HETATM 4364 O O1 . GOL H 4 . ? 1.361 48.026 23.195 1.00 56.35 ? 10 GOL A O1 1 HETATM 4365 C C2 . GOL H 4 . ? 3.066 48.232 21.510 1.00 60.04 ? 10 GOL A C2 1 HETATM 4366 O O2 . GOL H 4 . ? 2.408 47.752 20.354 1.00 60.27 ? 10 GOL A O2 1 HETATM 4367 C C3 . GOL H 4 . ? 2.803 49.727 21.678 1.00 60.67 ? 10 GOL A C3 1 HETATM 4368 O O3 . GOL H 4 . ? 4.007 50.412 21.955 1.00 61.50 ? 10 GOL A O3 1 HETATM 4369 C C . ACT I 5 . ? 19.229 26.215 33.300 1.00 38.27 ? 22 ACT A C 1 HETATM 4370 O O . ACT I 5 . ? 20.193 26.835 32.794 1.00 37.91 ? 22 ACT A O 1 HETATM 4371 O OXT . ACT I 5 . ? 18.790 25.238 32.649 1.00 38.52 ? 22 ACT A OXT 1 HETATM 4372 C CH3 . ACT I 5 . ? 18.647 26.603 34.624 1.00 38.22 ? 22 ACT A CH3 1 HETATM 4373 C C1 . GOL J 4 . ? 12.432 55.214 31.879 1.00 42.94 ? 3 GOL A C1 1 HETATM 4374 O O1 . GOL J 4 . ? 12.604 56.397 31.127 1.00 43.55 ? 3 GOL A O1 1 HETATM 4375 C C2 . GOL J 4 . ? 11.780 55.619 33.187 1.00 42.83 ? 3 GOL A C2 1 HETATM 4376 O O2 . GOL J 4 . ? 10.654 56.403 32.870 1.00 41.60 ? 3 GOL A O2 1 HETATM 4377 C C3 . GOL J 4 . ? 11.415 54.360 33.982 1.00 41.66 ? 3 GOL A C3 1 HETATM 4378 O O3 . GOL J 4 . ? 10.298 54.564 34.819 1.00 36.92 ? 3 GOL A O3 1 HETATM 4379 C C1 . NAG K 3 . ? 35.276 48.975 10.206 1.00 33.10 ? 31 NAG B C1 1 HETATM 4380 C C2 . NAG K 3 . ? 36.717 48.498 9.988 1.00 37.10 ? 31 NAG B C2 1 HETATM 4381 C C3 . NAG K 3 . ? 37.459 49.395 9.004 1.00 39.01 ? 31 NAG B C3 1 HETATM 4382 C C4 . NAG K 3 . ? 36.638 49.654 7.751 1.00 40.23 ? 31 NAG B C4 1 HETATM 4383 C C5 . NAG K 3 . ? 35.240 50.125 8.140 1.00 38.94 ? 31 NAG B C5 1 HETATM 4384 C C6 . NAG K 3 . ? 34.385 50.416 6.905 1.00 39.56 ? 31 NAG B C6 1 HETATM 4385 C C7 . NAG K 3 . ? 37.514 47.482 12.030 1.00 39.56 ? 31 NAG B C7 1 HETATM 4386 C C8 . NAG K 3 . ? 38.321 47.644 13.282 1.00 39.70 ? 31 NAG B C8 1 HETATM 4387 N N2 . NAG K 3 . ? 37.425 48.549 11.247 1.00 35.90 ? 31 NAG B N2 1 HETATM 4388 O O3 . NAG K 3 . ? 38.699 48.810 8.668 1.00 40.90 ? 31 NAG B O3 1 HETATM 4389 O O4 . NAG K 3 . ? 37.285 50.664 7.010 1.00 47.31 ? 31 NAG B O4 1 HETATM 4390 O O5 . NAG K 3 . ? 34.635 49.131 8.953 1.00 34.98 ? 31 NAG B O5 1 HETATM 4391 O O6 . NAG K 3 . ? 34.242 49.250 6.116 1.00 40.87 ? 31 NAG B O6 1 HETATM 4392 O O7 . NAG K 3 . ? 36.956 46.413 11.764 1.00 41.75 ? 31 NAG B O7 1 HETATM 4393 C C1 . NAG L 3 . ? 37.634 50.313 5.766 1.00 61.64 ? 32 NAG B C1 1 HETATM 4394 C C2 . NAG L 3 . ? 37.902 51.567 4.935 1.00 64.38 ? 32 NAG B C2 1 HETATM 4395 C C3 . NAG L 3 . ? 38.437 51.163 3.572 1.00 66.49 ? 32 NAG B C3 1 HETATM 4396 C C4 . NAG L 3 . ? 39.697 50.328 3.778 1.00 67.59 ? 32 NAG B C4 1 HETATM 4397 C C5 . NAG L 3 . ? 39.347 49.115 4.646 1.00 67.33 ? 32 NAG B C5 1 HETATM 4398 C C6 . NAG L 3 . ? 40.562 48.216 4.892 1.00 68.48 ? 32 NAG B C6 1 HETATM 4399 C C7 . NAG L 3 . ? 36.389 53.369 5.567 1.00 63.86 ? 32 NAG B C7 1 HETATM 4400 C C8 . NAG L 3 . ? 37.493 53.941 6.410 1.00 63.30 ? 32 NAG B C8 1 HETATM 4401 N N2 . NAG L 3 . ? 36.696 52.348 4.767 1.00 63.56 ? 32 NAG B N2 1 HETATM 4402 O O3 . NAG L 3 . ? 38.713 52.314 2.803 1.00 67.18 ? 32 NAG B O3 1 HETATM 4403 O O4 . NAG L 3 . ? 40.240 49.934 2.528 1.00 69.53 ? 32 NAG B O4 1 HETATM 4404 O O5 . NAG L 3 . ? 38.817 49.550 5.887 1.00 65.29 ? 32 NAG B O5 1 HETATM 4405 O O6 . NAG L 3 . ? 41.549 48.913 5.631 1.00 70.01 ? 32 NAG B O6 1 HETATM 4406 O O7 . NAG L 3 . ? 35.250 53.836 5.630 1.00 64.19 ? 32 NAG B O7 1 HETATM 4407 C C1 . NAG M 3 . ? 5.169 75.086 7.783 1.00 63.93 ? 41 NAG B C1 1 HETATM 4408 C C2 . NAG M 3 . ? 4.868 76.169 6.764 1.00 69.00 ? 41 NAG B C2 1 HETATM 4409 C C3 . NAG M 3 . ? 4.901 77.583 7.294 1.00 70.14 ? 41 NAG B C3 1 HETATM 4410 C C4 . NAG M 3 . ? 4.123 77.655 8.576 1.00 70.88 ? 41 NAG B C4 1 HETATM 4411 C C5 . NAG M 3 . ? 4.639 76.565 9.482 1.00 70.05 ? 41 NAG B C5 1 HETATM 4412 C C6 . NAG M 3 . ? 4.064 76.704 10.885 1.00 71.28 ? 41 NAG B C6 1 HETATM 4413 C C7 . NAG M 3 . ? 5.299 75.302 4.721 1.00 70.61 ? 41 NAG B C7 1 HETATM 4414 C C8 . NAG M 3 . ? 6.207 74.892 3.610 1.00 70.78 ? 41 NAG B C8 1 HETATM 4415 N N2 . NAG M 3 . ? 5.769 76.060 5.668 1.00 69.67 ? 41 NAG B N2 1 HETATM 4416 O O3 . NAG M 3 . ? 4.181 78.383 6.395 1.00 70.90 ? 41 NAG B O3 1 HETATM 4417 O O4 . NAG M 3 . ? 4.324 78.913 9.141 1.00 72.41 ? 41 NAG B O4 1 HETATM 4418 O O5 . NAG M 3 . ? 4.346 75.323 8.883 1.00 68.87 ? 41 NAG B O5 1 HETATM 4419 O O6 . NAG M 3 . ? 2.692 77.014 10.902 1.00 72.57 ? 41 NAG B O6 1 HETATM 4420 O O7 . NAG M 3 . ? 4.145 74.931 4.762 1.00 70.68 ? 41 NAG B O7 1 HETATM 4421 C C1 . GOL N 4 . ? 14.448 36.658 20.268 1.00 50.39 ? 11 GOL B C1 1 HETATM 4422 O O1 . GOL N 4 . ? 14.768 35.577 21.129 1.00 48.24 ? 11 GOL B O1 1 HETATM 4423 C C2 . GOL N 4 . ? 15.652 37.015 19.398 1.00 50.31 ? 11 GOL B C2 1 HETATM 4424 O O2 . GOL N 4 . ? 16.535 35.920 19.381 1.00 51.67 ? 11 GOL B O2 1 HETATM 4425 C C3 . GOL N 4 . ? 15.252 37.389 17.966 1.00 52.78 ? 11 GOL B C3 1 HETATM 4426 O O3 . GOL N 4 . ? 15.836 36.540 16.991 1.00 53.22 ? 11 GOL B O3 1 HETATM 4427 C C1 . GOL O 4 . ? 30.710 38.086 39.164 1.00 37.76 ? 1 GOL B C1 1 HETATM 4428 O O1 . GOL O 4 . ? 31.938 38.425 38.548 1.00 35.24 ? 1 GOL B O1 1 HETATM 4429 C C2 . GOL O 4 . ? 31.027 37.488 40.514 1.00 39.28 ? 1 GOL B C2 1 HETATM 4430 O O2 . GOL O 4 . ? 29.854 37.251 41.266 1.00 39.23 ? 1 GOL B O2 1 HETATM 4431 C C3 . GOL O 4 . ? 31.769 36.173 40.292 1.00 41.91 ? 1 GOL B C3 1 HETATM 4432 O O3 . GOL O 4 . ? 33.143 36.388 40.032 1.00 45.63 ? 1 GOL B O3 1 HETATM 4433 C C1 . GOL P 4 . ? 17.499 49.133 19.132 1.00 40.35 ? 2 GOL B C1 1 HETATM 4434 O O1 . GOL P 4 . ? 18.842 49.299 19.538 1.00 29.48 ? 2 GOL B O1 1 HETATM 4435 C C2 . GOL P 4 . ? 17.072 50.303 18.252 1.00 45.70 ? 2 GOL B C2 1 HETATM 4436 O O2 . GOL P 4 . ? 15.780 50.056 17.727 1.00 49.73 ? 2 GOL B O2 1 HETATM 4437 C C3 . GOL P 4 . ? 18.053 50.434 17.092 1.00 47.46 ? 2 GOL B C3 1 HETATM 4438 O O3 . GOL P 4 . ? 19.070 51.356 17.428 1.00 49.80 ? 2 GOL B O3 1 HETATM 4439 C C1 . GOL Q 4 . ? 38.342 52.425 19.052 1.00 46.47 ? 4 GOL B C1 1 HETATM 4440 O O1 . GOL Q 4 . ? 38.632 51.196 18.436 1.00 38.45 ? 4 GOL B O1 1 HETATM 4441 C C2 . GOL Q 4 . ? 39.562 53.326 19.105 1.00 48.72 ? 4 GOL B C2 1 HETATM 4442 O O2 . GOL Q 4 . ? 39.838 53.780 17.797 1.00 49.76 ? 4 GOL B O2 1 HETATM 4443 C C3 . GOL Q 4 . ? 40.749 52.594 19.740 1.00 50.07 ? 4 GOL B C3 1 HETATM 4444 O O3 . GOL Q 4 . ? 40.286 51.473 20.477 1.00 52.38 ? 4 GOL B O3 1 HETATM 4445 C C1 . GOL R 4 . ? 30.463 77.847 28.667 1.00 38.91 ? 5 GOL B C1 1 HETATM 4446 O O1 . GOL R 4 . ? 30.633 78.220 30.022 1.00 37.87 ? 5 GOL B O1 1 HETATM 4447 C C2 . GOL R 4 . ? 30.342 76.322 28.627 1.00 39.06 ? 5 GOL B C2 1 HETATM 4448 O O2 . GOL R 4 . ? 30.933 75.789 29.787 1.00 34.06 ? 5 GOL B O2 1 HETATM 4449 C C3 . GOL R 4 . ? 31.036 75.837 27.347 1.00 40.67 ? 5 GOL B C3 1 HETATM 4450 O O3 . GOL R 4 . ? 31.698 74.612 27.522 1.00 36.99 ? 5 GOL B O3 1 HETATM 4451 C C1 . GOL S 4 . ? 20.733 48.703 44.912 1.00 36.68 ? 6 GOL B C1 1 HETATM 4452 O O1 . GOL S 4 . ? 21.661 47.779 45.455 1.00 35.74 ? 6 GOL B O1 1 HETATM 4453 C C2 . GOL S 4 . ? 19.579 47.904 44.345 1.00 41.85 ? 6 GOL B C2 1 HETATM 4454 O O2 . GOL S 4 . ? 19.006 47.108 45.348 1.00 38.48 ? 6 GOL B O2 1 HETATM 4455 C C3 . GOL S 4 . ? 18.532 48.757 43.629 1.00 40.44 ? 6 GOL B C3 1 HETATM 4456 O O3 . GOL S 4 . ? 17.667 47.848 42.975 1.00 44.03 ? 6 GOL B O3 1 HETATM 4457 C C1 . GOL T 4 . ? 22.845 64.672 17.324 1.00 31.41 ? 7 GOL B C1 1 HETATM 4458 O O1 . GOL T 4 . ? 22.752 65.382 18.524 1.00 29.44 ? 7 GOL B O1 1 HETATM 4459 C C2 . GOL T 4 . ? 24.051 63.721 17.440 1.00 32.12 ? 7 GOL B C2 1 HETATM 4460 O O2 . GOL T 4 . ? 25.230 64.515 17.497 1.00 28.66 ? 7 GOL B O2 1 HETATM 4461 C C3 . GOL T 4 . ? 24.079 62.830 16.191 1.00 30.41 ? 7 GOL B C3 1 HETATM 4462 O O3 . GOL T 4 . ? 25.162 61.954 16.237 1.00 29.02 ? 7 GOL B O3 1 HETATM 4463 C C1 . GOL U 4 . ? 32.508 34.337 52.905 1.00 47.69 ? 8 GOL B C1 1 HETATM 4464 O O1 . GOL U 4 . ? 33.506 35.089 52.248 1.00 45.68 ? 8 GOL B O1 1 HETATM 4465 C C2 . GOL U 4 . ? 32.809 32.839 52.958 1.00 47.12 ? 8 GOL B C2 1 HETATM 4466 O O2 . GOL U 4 . ? 31.864 32.273 53.826 1.00 50.80 ? 8 GOL B O2 1 HETATM 4467 C C3 . GOL U 4 . ? 32.587 32.194 51.588 1.00 47.83 ? 8 GOL B C3 1 HETATM 4468 O O3 . GOL U 4 . ? 33.247 30.942 51.463 1.00 42.60 ? 8 GOL B O3 1 HETATM 4469 C C . ACT V 5 . ? 27.559 80.130 17.670 1.00 56.90 ? 21 ACT B C 1 HETATM 4470 O O . ACT V 5 . ? 28.369 79.261 18.063 1.00 56.49 ? 21 ACT B O 1 HETATM 4471 O OXT . ACT V 5 . ? 26.404 80.042 18.145 1.00 57.07 ? 21 ACT B OXT 1 HETATM 4472 C CH3 . ACT V 5 . ? 27.940 81.211 16.698 1.00 56.85 ? 21 ACT B CH3 1 HETATM 4473 XE XE . XE W 6 . ? 16.953 39.042 28.859 0.10 19.26 ? 606 XE B XE 1 HETATM 4474 NA NA . NA X 7 . ? 20.455 55.896 28.585 1.00 27.96 ? 607 NA B NA 1 HETATM 4475 O O . HOH Y 8 . ? 4.276 33.705 19.992 1.00 64.49 ? 8 HOH A O 1 HETATM 4476 O O . HOH Y 8 . ? 25.795 40.305 34.761 1.00 12.04 ? 13 HOH A O 1 HETATM 4477 O O . HOH Y 8 . ? 9.620 65.636 38.171 1.00 16.26 ? 19 HOH A O 1 HETATM 4478 O O . HOH Y 8 . ? 14.977 39.246 15.175 1.00 49.30 ? 25 HOH A O 1 HETATM 4479 O O . HOH Y 8 . ? 9.265 55.093 43.634 1.00 20.31 ? 27 HOH A O 1 HETATM 4480 O O . HOH Y 8 . ? 22.799 32.261 45.635 1.00 24.45 ? 28 HOH A O 1 HETATM 4481 O O . HOH Y 8 . ? 16.631 39.067 33.417 1.00 16.70 ? 34 HOH A O 1 HETATM 4482 O O . HOH Y 8 . ? 25.437 26.778 44.740 1.00 23.56 ? 37 HOH A O 1 HETATM 4483 O O . HOH Y 8 . ? 6.143 42.812 37.487 1.00 18.28 ? 38 HOH A O 1 HETATM 4484 O O . HOH Y 8 . ? 27.173 28.603 40.241 1.00 20.49 ? 39 HOH A O 1 HETATM 4485 O O . HOH Y 8 . ? 12.893 50.108 46.657 1.00 22.19 ? 40 HOH A O 1 HETATM 4486 O O . HOH Y 8 . ? 15.819 48.668 31.194 1.00 18.32 ? 42 HOH A O 1 HETATM 4487 O O . HOH Y 8 . ? 23.704 27.664 33.882 1.00 25.14 ? 44 HOH A O 1 HETATM 4488 O O . HOH Y 8 . ? 20.503 40.047 64.068 1.00 45.17 ? 45 HOH A O 1 HETATM 4489 O O . HOH Y 8 . ? 16.113 71.355 39.093 1.00 16.40 ? 249 HOH A O 1 HETATM 4490 O O . HOH Y 8 . ? 19.441 36.431 52.874 1.00 20.86 ? 250 HOH A O 1 HETATM 4491 O O . HOH Y 8 . ? 0.815 48.083 30.252 1.00 31.46 ? 251 HOH A O 1 HETATM 4492 O O . HOH Y 8 . ? 23.287 26.091 36.690 1.00 15.72 ? 252 HOH A O 1 HETATM 4493 O O . HOH Y 8 . ? 20.872 30.197 49.601 1.00 35.92 ? 253 HOH A O 1 HETATM 4494 O O . HOH Y 8 . ? 22.976 22.604 40.517 1.00 20.24 ? 254 HOH A O 1 HETATM 4495 O O . HOH Y 8 . ? 10.800 45.052 62.931 1.00 21.93 ? 255 HOH A O 1 HETATM 4496 O O . HOH Y 8 . ? 7.920 33.161 34.682 1.00 22.03 ? 256 HOH A O 1 HETATM 4497 O O . HOH Y 8 . ? 10.300 28.442 30.739 1.00 33.10 ? 257 HOH A O 1 HETATM 4498 O O . HOH Y 8 . ? 14.008 34.604 50.905 1.00 21.86 ? 258 HOH A O 1 HETATM 4499 O O . HOH Y 8 . ? 8.781 34.848 22.644 1.00 22.79 ? 259 HOH A O 1 HETATM 4500 O O . HOH Y 8 . ? 12.475 35.685 38.246 1.00 18.95 ? 260 HOH A O 1 HETATM 4501 O O . HOH Y 8 . ? 21.317 50.947 56.532 1.00 26.86 ? 261 HOH A O 1 HETATM 4502 O O . HOH Y 8 . ? 6.174 35.326 35.020 1.00 25.75 ? 262 HOH A O 1 HETATM 4503 O O . HOH Y 8 . ? 19.591 49.902 23.170 1.00 31.61 ? 263 HOH A O 1 HETATM 4504 O O . HOH Y 8 . ? 1.402 53.885 27.518 1.00 41.89 ? 264 HOH A O 1 HETATM 4505 O O . HOH Y 8 . ? -5.355 48.450 19.037 1.00 59.73 ? 265 HOH A O 1 HETATM 4506 O O . HOH Y 8 . ? 28.389 30.604 49.170 1.00 23.87 ? 266 HOH A O 1 HETATM 4507 O O . HOH Y 8 . ? 14.874 57.168 55.777 1.00 41.37 ? 267 HOH A O 1 HETATM 4508 O O . HOH Y 8 . ? 9.737 35.066 38.822 1.00 22.40 ? 268 HOH A O 1 HETATM 4509 O O . HOH Y 8 . ? 7.464 31.363 28.136 1.00 28.78 ? 269 HOH A O 1 HETATM 4510 O O . HOH Y 8 . ? 28.432 32.200 41.072 1.00 22.11 ? 270 HOH A O 1 HETATM 4511 O O . HOH Y 8 . ? 19.880 33.114 45.470 1.00 26.96 ? 271 HOH A O 1 HETATM 4512 O O . HOH Y 8 . ? 19.975 34.125 47.861 1.00 26.23 ? 272 HOH A O 1 HETATM 4513 O O . HOH Y 8 . ? 12.707 39.344 32.600 1.00 27.83 ? 273 HOH A O 1 HETATM 4514 O O . HOH Y 8 . ? 1.153 53.886 61.481 1.00 43.32 ? 274 HOH A O 1 HETATM 4515 O O . HOH Y 8 . ? 13.842 32.448 44.348 1.00 32.16 ? 275 HOH A O 1 HETATM 4516 O O . HOH Y 8 . ? 1.717 40.456 33.640 1.00 29.59 ? 276 HOH A O 1 HETATM 4517 O O . HOH Y 8 . ? 18.630 51.795 21.337 1.00 34.51 ? 277 HOH A O 1 HETATM 4518 O O . HOH Y 8 . ? 12.747 51.535 32.769 1.00 38.88 ? 278 HOH A O 1 HETATM 4519 O O . HOH Y 8 . ? 15.884 38.296 58.970 1.00 22.56 ? 279 HOH A O 1 HETATM 4520 O O . HOH Y 8 . ? 13.160 26.019 34.088 1.00 50.08 ? 280 HOH A O 1 HETATM 4521 O O . HOH Y 8 . ? 6.768 33.081 21.824 1.00 32.41 ? 281 HOH A O 1 HETATM 4522 O O . HOH Y 8 . ? 2.027 34.728 47.277 1.00 57.29 ? 282 HOH A O 1 HETATM 4523 O O . HOH Y 8 . ? -0.325 57.814 28.720 1.00 35.79 ? 283 HOH A O 1 HETATM 4524 O O . HOH Y 8 . ? 14.419 58.259 16.494 1.00 40.69 ? 284 HOH A O 1 HETATM 4525 O O . HOH Y 8 . ? 17.911 36.181 48.327 1.00 25.68 ? 285 HOH A O 1 HETATM 4526 O O . HOH Y 8 . ? 13.156 43.609 13.739 1.00 37.76 ? 286 HOH A O 1 HETATM 4527 O O . HOH Y 8 . ? 8.168 31.027 38.792 1.00 54.08 ? 287 HOH A O 1 HETATM 4528 O O . HOH Y 8 . ? 8.631 31.093 48.031 1.00 29.03 ? 288 HOH A O 1 HETATM 4529 O O . HOH Y 8 . ? 19.548 32.395 50.059 1.00 35.65 ? 290 HOH A O 1 HETATM 4530 O O . HOH Y 8 . ? 9.155 32.886 37.265 1.00 28.16 ? 291 HOH A O 1 HETATM 4531 O O . HOH Y 8 . ? 8.253 41.724 67.161 1.00 55.22 ? 292 HOH A O 1 HETATM 4532 O O . HOH Y 8 . ? 11.268 51.568 25.565 1.00 40.72 ? 293 HOH A O 1 HETATM 4533 O O . HOH Y 8 . ? 18.848 30.619 45.814 1.00 39.00 ? 294 HOH A O 1 HETATM 4534 O O . HOH Y 8 . ? 6.297 31.018 34.358 1.00 46.18 ? 295 HOH A O 1 HETATM 4535 O O . HOH Y 8 . ? 7.421 33.721 54.318 1.00 41.64 ? 297 HOH A O 1 HETATM 4536 O O . HOH Y 8 . ? 8.152 53.927 32.224 1.00 28.06 ? 298 HOH A O 1 HETATM 4537 O O . HOH Y 8 . ? -2.390 51.480 39.223 1.00 42.18 ? 299 HOH A O 1 HETATM 4538 O O . HOH Y 8 . ? 11.028 47.437 16.607 1.00 38.37 ? 300 HOH A O 1 HETATM 4539 O O . HOH Y 8 . ? 30.692 28.854 49.038 1.00 31.32 ? 301 HOH A O 1 HETATM 4540 O O . HOH Y 8 . ? 17.827 34.870 58.913 1.00 28.85 ? 303 HOH A O 1 HETATM 4541 O O . HOH Y 8 . ? 17.988 25.600 46.250 1.00 35.46 ? 306 HOH A O 1 HETATM 4542 O O . HOH Y 8 . ? 8.776 59.726 62.556 1.00 37.23 ? 311 HOH A O 1 HETATM 4543 O O . HOH Y 8 . ? -0.138 42.757 53.773 1.00 38.96 ? 312 HOH A O 1 HETATM 4544 O O . HOH Y 8 . ? 0.709 46.809 56.688 1.00 43.26 ? 313 HOH A O 1 HETATM 4545 O O . HOH Y 8 . ? 0.946 49.036 61.973 1.00 47.75 ? 320 HOH A O 1 HETATM 4546 O O . HOH Y 8 . ? 6.546 32.605 19.228 1.00 55.48 ? 322 HOH A O 1 HETATM 4547 O O . HOH Y 8 . ? 1.362 53.003 57.459 1.00 49.54 ? 323 HOH A O 1 HETATM 4548 O O . HOH Y 8 . ? -0.883 49.330 55.249 1.00 55.79 ? 324 HOH A O 1 HETATM 4549 O O . HOH Y 8 . ? 7.769 31.448 50.818 1.00 36.46 ? 330 HOH A O 1 HETATM 4550 O O . HOH Y 8 . ? 1.154 36.165 32.522 1.00 55.02 ? 333 HOH A O 1 HETATM 4551 O O . HOH Y 8 . ? 8.982 50.835 24.823 1.00 45.42 ? 346 HOH A O 1 HETATM 4552 O O . HOH Y 8 . ? 7.363 50.810 27.500 1.00 53.36 ? 352 HOH A O 1 HETATM 4553 O O . HOH Y 8 . ? 28.292 24.888 48.408 1.00 29.13 ? 354 HOH A O 1 HETATM 4554 O O . HOH Y 8 . ? -2.401 48.354 24.035 1.00 48.53 ? 364 HOH A O 1 HETATM 4555 O O . HOH Y 8 . ? 3.565 39.326 56.072 1.00 38.64 ? 367 HOH A O 1 HETATM 4556 O O . HOH Y 8 . ? 20.275 23.009 44.188 1.00 35.67 ? 368 HOH A O 1 HETATM 4557 O O . HOH Y 8 . ? 3.721 68.403 42.801 1.00 50.09 ? 371 HOH A O 1 HETATM 4558 O O . HOH Y 8 . ? 3.041 35.693 18.769 1.00 38.57 ? 374 HOH A O 1 HETATM 4559 O O . HOH Y 8 . ? 9.805 35.403 60.476 1.00 42.18 ? 381 HOH A O 1 HETATM 4560 O O . HOH Y 8 . ? 17.669 44.900 45.888 1.00 35.71 ? 383 HOH A O 1 HETATM 4561 O O . HOH Y 8 . ? 11.431 60.993 63.589 1.00 36.33 ? 388 HOH A O 1 HETATM 4562 O O . HOH Y 8 . ? 3.739 31.992 36.112 1.00 58.00 ? 393 HOH A O 1 HETATM 4563 O O . HOH Y 8 . ? 15.890 39.833 64.264 1.00 62.02 ? 395 HOH A O 1 HETATM 4564 O O . HOH Y 8 . ? 5.195 40.666 40.397 1.00 39.58 ? 407 HOH A O 1 HETATM 4565 O O . HOH Y 8 . ? 21.206 21.329 42.053 1.00 29.36 ? 438 HOH A O 1 HETATM 4566 O O . HOH Y 8 . ? 20.069 37.740 60.289 1.00 53.08 ? 439 HOH A O 1 HETATM 4567 O O . HOH Y 8 . ? 28.763 25.555 51.299 1.00 52.97 ? 444 HOH A O 1 HETATM 4568 O O . HOH Y 8 . ? 4.012 62.609 46.087 1.00 34.58 ? 458 HOH A O 1 HETATM 4569 O O . HOH Y 8 . ? -0.186 42.516 34.728 1.00 50.91 ? 462 HOH A O 1 HETATM 4570 O O . HOH Y 8 . ? 9.322 57.859 65.615 1.00 33.95 ? 463 HOH A O 1 HETATM 4571 O O . HOH Y 8 . ? 12.921 29.397 30.967 1.00 20.60 ? 465 HOH A O 1 HETATM 4572 O O . HOH Y 8 . ? 11.320 41.655 64.307 1.00 36.81 ? 469 HOH A O 1 HETATM 4573 O O . HOH Y 8 . ? 14.281 30.366 42.988 1.00 28.39 ? 471 HOH A O 1 HETATM 4574 O O . HOH Y 8 . ? 19.068 28.292 49.968 1.00 49.11 ? 472 HOH A O 1 HETATM 4575 O O . HOH Y 8 . ? 17.496 47.166 65.361 1.00 47.34 ? 483 HOH A O 1 HETATM 4576 O O . HOH Y 8 . ? 16.287 47.848 67.523 1.00 40.94 ? 484 HOH A O 1 HETATM 4577 O O . HOH Y 8 . ? 8.260 30.017 31.062 1.00 42.67 ? 485 HOH A O 1 HETATM 4578 O O . HOH Y 8 . ? 6.409 50.622 66.447 1.00 51.70 ? 499 HOH A O 1 HETATM 4579 O O . HOH Y 8 . ? 13.289 28.204 54.515 1.00 54.44 ? 505 HOH A O 1 HETATM 4580 O O . HOH Y 8 . ? 14.830 30.715 53.981 1.00 42.09 ? 506 HOH A O 1 HETATM 4581 O O . HOH Y 8 . ? 14.796 27.587 32.363 1.00 29.15 ? 508 HOH A O 1 HETATM 4582 O O . HOH Y 8 . ? 0.670 37.947 34.746 1.00 48.02 ? 510 HOH A O 1 HETATM 4583 O O . HOH Y 8 . ? 5.762 74.263 39.095 1.00 31.31 ? 522 HOH A O 1 HETATM 4584 O O . HOH Y 8 . ? 18.381 50.468 63.354 1.00 50.52 ? 534 HOH A O 1 HETATM 4585 O O . HOH Y 8 . ? -0.632 44.373 30.319 1.00 57.10 ? 538 HOH A O 1 HETATM 4586 O O . HOH Y 8 . ? -0.130 45.053 34.359 1.00 49.41 ? 539 HOH A O 1 HETATM 4587 O O . HOH Y 8 . ? 0.678 46.044 31.678 1.00 35.91 ? 540 HOH A O 1 HETATM 4588 O O . HOH Y 8 . ? 6.594 30.778 42.107 1.00 47.96 ? 542 HOH A O 1 HETATM 4589 O O . HOH Y 8 . ? 3.712 34.651 34.973 1.00 27.85 ? 543 HOH A O 1 HETATM 4590 O O . HOH Y 8 . ? 22.796 58.267 17.710 1.00 47.84 ? 558 HOH A O 1 HETATM 4591 O O . HOH Y 8 . ? 10.107 45.748 65.404 1.00 52.36 ? 566 HOH A O 1 HETATM 4592 O O . HOH Y 8 . ? 5.106 34.371 43.766 1.00 29.93 ? 582 HOH A O 1 HETATM 4593 O O . HOH Y 8 . ? 5.195 37.264 54.642 1.00 39.77 ? 583 HOH A O 1 HETATM 4594 O O . HOH Y 8 . ? 1.769 33.501 58.626 1.00 62.99 ? 584 HOH A O 1 HETATM 4595 O O . HOH Y 8 . ? 7.320 30.800 53.751 1.00 47.87 ? 585 HOH A O 1 HETATM 4596 O O . HOH Y 8 . ? -3.396 46.876 53.034 1.00 66.42 ? 587 HOH A O 1 HETATM 4597 O O . HOH Y 8 . ? -1.300 49.945 49.028 1.00 50.36 ? 588 HOH A O 1 HETATM 4598 O O . HOH Y 8 . ? 9.415 51.848 67.071 1.00 47.79 ? 593 HOH A O 1 HETATM 4599 O O . HOH Y 8 . ? 12.521 52.258 66.287 1.00 60.65 ? 594 HOH A O 1 HETATM 4600 O O . HOH Y 8 . ? 21.890 48.282 60.156 1.00 27.39 ? 595 HOH A O 1 HETATM 4601 O O . HOH Y 8 . ? 4.529 60.292 57.215 1.00 40.41 ? 596 HOH A O 1 HETATM 4602 O O . HOH Y 8 . ? 15.655 34.303 60.354 1.00 47.34 ? 599 HOH A O 1 HETATM 4603 O O . HOH Y 8 . ? 17.226 38.017 61.923 1.00 62.43 ? 600 HOH A O 1 HETATM 4604 O O . HOH Y 8 . ? -4.945 48.022 25.171 1.00 45.25 ? 601 HOH A O 1 HETATM 4605 O O . HOH Y 8 . ? 19.930 54.970 57.850 1.00 45.65 ? 602 HOH A O 1 HETATM 4606 O O . HOH Y 8 . ? 5.587 69.397 44.597 1.00 28.51 ? 603 HOH A O 1 HETATM 4607 O O . HOH Y 8 . ? 2.972 62.640 55.573 1.00 59.98 ? 605 HOH A O 1 HETATM 4608 O O . HOH Y 8 . ? 5.274 56.958 64.511 1.00 50.23 ? 606 HOH A O 1 HETATM 4609 O O . HOH Y 8 . ? 14.840 23.758 34.376 1.00 51.18 ? 616 HOH A O 1 HETATM 4610 O O . HOH Y 8 . ? -4.574 49.479 33.629 1.00 67.27 ? 617 HOH A O 1 HETATM 4611 O O . HOH Y 8 . ? 2.244 36.267 36.676 1.00 42.54 ? 620 HOH A O 1 HETATM 4612 O O . HOH Y 8 . ? -2.267 55.005 44.244 1.00 56.59 ? 649 HOH A O 1 HETATM 4613 O O . HOH Y 8 . ? -6.363 49.893 20.693 1.00 49.94 ? 656 HOH A O 1 HETATM 4614 O O . HOH Y 8 . ? 6.162 40.133 16.697 1.00 43.56 ? 657 HOH A O 1 HETATM 4615 O O . HOH Y 8 . ? 14.661 55.447 31.962 1.00 40.13 ? 659 HOH A O 1 HETATM 4616 O O . HOH Y 8 . ? 8.543 50.457 29.993 1.00 43.62 ? 660 HOH A O 1 HETATM 4617 O O . HOH Y 8 . ? 3.807 59.746 45.935 1.00 26.50 ? 669 HOH A O 1 HETATM 4618 O O . HOH Y 8 . ? 1.917 63.243 44.554 1.00 47.40 ? 670 HOH A O 1 HETATM 4619 O O . HOH Y 8 . ? 10.239 27.036 46.278 1.00 49.12 ? 675 HOH A O 1 HETATM 4620 O O . HOH Y 8 . ? 16.247 58.272 18.111 1.00 42.61 ? 690 HOH A O 1 HETATM 4621 O O . HOH Y 8 . ? 13.636 50.046 19.242 1.00 32.83 ? 692 HOH A O 1 HETATM 4622 O O . HOH Y 8 . ? 2.077 41.997 16.512 1.00 40.93 ? 698 HOH A O 1 HETATM 4623 O O . HOH Y 8 . ? 19.078 19.827 41.584 1.00 41.94 ? 707 HOH A O 1 HETATM 4624 O O . HOH Y 8 . ? 0.408 41.171 46.230 1.00 53.35 ? 710 HOH A O 1 HETATM 4625 O O . HOH Y 8 . ? 15.139 51.400 31.511 1.00 41.86 ? 711 HOH A O 1 HETATM 4626 O O . HOH Y 8 . ? 21.029 31.573 44.439 1.00 42.21 ? 712 HOH A O 1 HETATM 4627 O O . HOH Y 8 . ? 24.004 42.645 58.335 1.00 38.75 ? 713 HOH A O 1 HETATM 4628 O O . HOH Y 8 . ? -2.168 49.362 33.080 1.00 50.25 ? 715 HOH A O 1 HETATM 4629 O O . HOH Y 8 . ? 18.530 32.378 55.856 1.00 40.92 ? 716 HOH A O 1 HETATM 4630 O O . HOH Y 8 . ? 16.601 50.358 67.092 1.00 47.97 ? 720 HOH A O 1 HETATM 4631 O O . HOH Y 8 . ? 2.553 52.426 25.540 1.00 48.25 ? 725 HOH A O 1 HETATM 4632 O O . HOH Y 8 . ? 5.510 60.213 59.512 1.00 46.99 ? 728 HOH A O 1 HETATM 4633 O O . HOH Y 8 . ? 5.477 52.454 26.971 1.00 38.60 ? 732 HOH A O 1 HETATM 4634 O O . HOH Y 8 . ? 2.309 56.631 49.269 1.00 41.29 ? 756 HOH A O 1 HETATM 4635 O O . HOH Y 8 . ? 2.267 50.552 50.235 1.00 39.46 ? 757 HOH A O 1 HETATM 4636 O O . HOH Y 8 . ? 15.826 57.587 21.745 1.00 47.14 ? 758 HOH A O 1 HETATM 4637 O O . HOH Y 8 . ? 14.575 51.984 67.321 1.00 40.15 ? 759 HOH A O 1 HETATM 4638 O O . HOH Z 8 . ? 7.735 60.899 18.465 1.00 38.02 ? 3 HOH B O 1 HETATM 4639 O O . HOH Z 8 . ? 36.626 59.354 23.073 1.00 30.59 ? 9 HOH B O 1 HETATM 4640 O O . HOH Z 8 . ? 32.523 37.350 30.936 1.00 46.09 ? 10 HOH B O 1 HETATM 4641 O O . HOH Z 8 . ? 16.345 58.135 13.377 1.00 26.35 ? 12 HOH B O 1 HETATM 4642 O O . HOH Z 8 . ? 47.260 68.144 30.297 1.00 27.73 ? 14 HOH B O 1 HETATM 4643 O O . HOH Z 8 . ? 44.751 53.775 30.180 1.00 20.03 ? 15 HOH B O 1 HETATM 4644 O O . HOH Z 8 . ? 39.141 51.378 38.939 1.00 16.07 ? 16 HOH B O 1 HETATM 4645 O O . HOH Z 8 . ? 23.661 38.991 23.775 1.00 18.89 ? 18 HOH B O 1 HETATM 4646 O O . HOH Z 8 . ? 5.820 60.770 34.244 1.00 19.36 ? 20 HOH B O 1 HETATM 4647 O O . HOH Z 8 . ? 37.410 52.942 36.387 1.00 15.57 ? 23 HOH B O 1 HETATM 4648 O O . HOH Z 8 . ? 33.099 56.915 12.902 1.00 21.14 ? 26 HOH B O 1 HETATM 4649 O O . HOH Z 8 . ? 24.646 48.111 28.205 1.00 13.91 ? 29 HOH B O 1 HETATM 4650 O O . HOH Z 8 . ? 32.314 58.244 23.577 1.00 16.33 ? 30 HOH B O 1 HETATM 4651 O O . HOH Z 8 . ? 33.462 44.184 14.324 1.00 25.60 ? 33 HOH B O 1 HETATM 4652 O O . HOH Z 8 . ? 47.344 66.353 35.864 1.00 38.00 ? 35 HOH B O 1 HETATM 4653 O O . HOH Z 8 . ? 31.219 43.862 46.925 1.00 17.94 ? 36 HOH B O 1 HETATM 4654 O O . HOH Z 8 . ? 19.173 76.239 25.843 1.00 20.11 ? 43 HOH B O 1 HETATM 4655 O O . HOH Z 8 . ? 14.436 65.908 16.749 1.00 21.12 ? 46 HOH B O 1 HETATM 4656 O O . HOH Z 8 . ? 49.368 64.487 28.490 1.00 47.25 ? 47 HOH B O 1 HETATM 4657 O O . HOH Z 8 . ? 7.184 73.012 22.727 1.00 23.09 ? 48 HOH B O 1 HETATM 4658 O O . HOH Z 8 . ? 12.256 74.017 29.666 1.00 19.36 ? 49 HOH B O 1 HETATM 4659 O O . HOH Z 8 . ? 34.891 62.927 19.431 1.00 47.32 ? 50 HOH B O 1 HETATM 4660 O O . HOH Z 8 . ? 22.048 76.756 25.724 1.00 18.90 ? 53 HOH B O 1 HETATM 4661 O O . HOH Z 8 . ? 31.634 39.417 24.585 1.00 39.31 ? 55 HOH B O 1 HETATM 4662 O O . HOH Z 8 . ? 37.352 43.649 25.932 1.00 21.91 ? 56 HOH B O 1 HETATM 4663 O O . HOH Z 8 . ? 40.180 49.759 34.650 1.00 28.64 ? 57 HOH B O 1 HETATM 4664 O O . HOH Z 8 . ? 18.310 75.309 31.363 1.00 24.57 ? 58 HOH B O 1 HETATM 4665 O O . HOH Z 8 . ? 20.783 50.621 33.150 1.00 19.85 ? 59 HOH B O 1 HETATM 4666 O O . HOH Z 8 . ? 33.894 54.193 16.847 1.00 20.75 ? 60 HOH B O 1 HETATM 4667 O O . HOH Z 8 . ? 13.572 73.163 33.612 1.00 30.22 ? 61 HOH B O 1 HETATM 4668 O O . HOH Z 8 . ? 28.556 39.001 25.143 1.00 29.63 ? 62 HOH B O 1 HETATM 4669 O O . HOH Z 8 . ? 22.265 50.272 41.319 1.00 21.68 ? 64 HOH B O 1 HETATM 4670 O O . HOH Z 8 . ? 34.300 54.611 14.231 1.00 23.31 ? 65 HOH B O 1 HETATM 4671 O O . HOH Z 8 . ? 40.012 49.011 37.632 1.00 17.57 ? 66 HOH B O 1 HETATM 4672 O O . HOH Z 8 . ? 20.891 59.704 1.849 1.00 38.94 ? 67 HOH B O 1 HETATM 4673 O O . HOH Z 8 . ? 27.787 37.392 28.425 1.00 26.59 ? 68 HOH B O 1 HETATM 4674 O O . HOH Z 8 . ? 43.786 55.074 27.431 1.00 19.29 ? 70 HOH B O 1 HETATM 4675 O O . HOH Z 8 . ? 38.662 62.955 24.197 1.00 22.21 ? 71 HOH B O 1 HETATM 4676 O O . HOH Z 8 . ? 38.896 69.613 22.264 1.00 22.78 ? 72 HOH B O 1 HETATM 4677 O O . HOH Z 8 . ? 38.375 46.694 20.341 1.00 54.38 ? 73 HOH B O 1 HETATM 4678 O O . HOH Z 8 . ? 28.227 40.292 18.371 1.00 26.19 ? 76 HOH B O 1 HETATM 4679 O O . HOH Z 8 . ? 34.377 71.381 16.502 1.00 21.47 ? 77 HOH B O 1 HETATM 4680 O O . HOH Z 8 . ? 15.761 70.868 10.870 1.00 27.66 ? 79 HOH B O 1 HETATM 4681 O O . HOH Z 8 . ? 22.850 76.411 32.926 1.00 44.68 ? 80 HOH B O 1 HETATM 4682 O O . HOH Z 8 . ? 39.020 67.261 21.097 1.00 23.27 ? 82 HOH B O 1 HETATM 4683 O O . HOH Z 8 . ? 21.788 32.682 25.664 1.00 25.87 ? 83 HOH B O 1 HETATM 4684 O O . HOH Z 8 . ? 24.737 68.523 7.800 1.00 39.81 ? 84 HOH B O 1 HETATM 4685 O O . HOH Z 8 . ? -5.150 69.896 26.017 1.00 55.75 ? 85 HOH B O 1 HETATM 4686 O O . HOH Z 8 . ? 23.732 76.457 28.258 1.00 20.61 ? 86 HOH B O 1 HETATM 4687 O O . HOH Z 8 . ? -0.760 74.615 22.242 1.00 55.05 ? 90 HOH B O 1 HETATM 4688 O O . HOH Z 8 . ? 49.201 62.324 30.084 1.00 31.97 ? 91 HOH B O 1 HETATM 4689 O O . HOH Z 8 . ? 37.085 55.469 17.882 1.00 32.16 ? 92 HOH B O 1 HETATM 4690 O O . HOH Z 8 . ? 28.925 48.721 10.269 1.00 20.00 ? 93 HOH B O 1 HETATM 4691 O O . HOH Z 8 . ? 37.015 75.060 39.465 1.00 46.43 ? 95 HOH B O 1 HETATM 4692 O O . HOH Z 8 . ? 19.405 37.658 14.223 1.00 26.35 ? 96 HOH B O 1 HETATM 4693 O O . HOH Z 8 . ? 23.986 50.886 16.578 1.00 37.97 ? 100 HOH B O 1 HETATM 4694 O O . HOH Z 8 . ? 14.419 73.351 13.389 1.00 30.12 ? 102 HOH B O 1 HETATM 4695 O O . HOH Z 8 . ? 26.577 72.702 7.602 1.00 56.55 ? 103 HOH B O 1 HETATM 4696 O O . HOH Z 8 . ? 15.506 64.413 21.200 1.00 19.17 ? 104 HOH B O 1 HETATM 4697 O O . HOH Z 8 . ? 35.488 61.037 45.817 1.00 21.65 ? 105 HOH B O 1 HETATM 4698 O O . HOH Z 8 . ? 42.504 48.175 29.018 1.00 25.74 ? 107 HOH B O 1 HETATM 4699 O O . HOH Z 8 . ? 3.692 65.803 41.780 1.00 32.96 ? 108 HOH B O 1 HETATM 4700 O O . HOH Z 8 . ? 25.633 77.092 35.013 1.00 30.01 ? 109 HOH B O 1 HETATM 4701 O O . HOH Z 8 . ? 35.724 49.568 47.102 1.00 39.17 ? 110 HOH B O 1 HETATM 4702 O O . HOH Z 8 . ? 32.625 56.924 10.339 1.00 23.99 ? 112 HOH B O 1 HETATM 4703 O O . HOH Z 8 . ? 24.649 51.341 54.259 1.00 22.42 ? 113 HOH B O 1 HETATM 4704 O O . HOH Z 8 . ? 3.559 75.666 35.659 1.00 27.84 ? 114 HOH B O 1 HETATM 4705 O O . HOH Z 8 . ? 14.857 81.125 27.917 1.00 32.63 ? 115 HOH B O 1 HETATM 4706 O O . HOH Z 8 . ? 34.795 79.087 30.885 1.00 19.59 ? 116 HOH B O 1 HETATM 4707 O O . HOH Z 8 . ? 18.740 78.844 19.346 1.00 27.05 ? 118 HOH B O 1 HETATM 4708 O O . HOH Z 8 . ? 43.451 51.623 26.345 1.00 43.60 ? 119 HOH B O 1 HETATM 4709 O O . HOH Z 8 . ? 28.091 44.720 10.395 1.00 45.68 ? 120 HOH B O 1 HETATM 4710 O O . HOH Z 8 . ? 40.595 51.384 42.734 1.00 25.73 ? 122 HOH B O 1 HETATM 4711 O O . HOH Z 8 . ? 25.049 45.153 58.610 1.00 30.74 ? 123 HOH B O 1 HETATM 4712 O O . HOH Z 8 . ? 22.095 76.454 13.239 1.00 26.60 ? 124 HOH B O 1 HETATM 4713 O O . HOH Z 8 . ? 23.522 74.308 19.507 1.00 26.09 ? 125 HOH B O 1 HETATM 4714 O O . HOH Z 8 . ? 44.359 68.742 33.158 1.00 33.54 ? 127 HOH B O 1 HETATM 4715 O O . HOH Z 8 . ? 35.580 54.639 10.057 1.00 50.72 ? 128 HOH B O 1 HETATM 4716 O O . HOH Z 8 . ? 9.199 76.058 24.370 1.00 21.80 ? 130 HOH B O 1 HETATM 4717 O O . HOH Z 8 . ? 30.887 53.906 6.161 1.00 27.12 ? 132 HOH B O 1 HETATM 4718 O O . HOH Z 8 . ? 10.457 31.653 24.909 1.00 46.12 ? 133 HOH B O 1 HETATM 4719 O O . HOH Z 8 . ? 19.763 51.281 42.036 1.00 22.49 ? 135 HOH B O 1 HETATM 4720 O O . HOH Z 8 . ? 28.090 64.296 6.165 1.00 31.57 ? 136 HOH B O 1 HETATM 4721 O O . HOH Z 8 . ? 30.347 49.662 43.937 1.00 25.79 ? 139 HOH B O 1 HETATM 4722 O O . HOH Z 8 . ? 24.113 67.527 10.861 1.00 30.56 ? 140 HOH B O 1 HETATM 4723 O O . HOH Z 8 . ? 18.897 48.268 10.866 1.00 52.30 ? 141 HOH B O 1 HETATM 4724 O O . HOH Z 8 . ? -1.428 67.668 34.165 1.00 50.84 ? 142 HOH B O 1 HETATM 4725 O O . HOH Z 8 . ? 43.468 48.274 43.382 1.00 52.62 ? 144 HOH B O 1 HETATM 4726 O O . HOH Z 8 . ? 24.983 63.563 8.344 1.00 28.63 ? 146 HOH B O 1 HETATM 4727 O O . HOH Z 8 . ? 2.049 73.667 36.829 1.00 30.73 ? 148 HOH B O 1 HETATM 4728 O O . HOH Z 8 . ? 48.954 52.282 35.991 1.00 37.96 ? 149 HOH B O 1 HETATM 4729 O O . HOH Z 8 . ? 37.395 43.923 33.541 1.00 28.38 ? 150 HOH B O 1 HETATM 4730 O O . HOH Z 8 . ? 14.298 76.319 40.213 1.00 36.84 ? 153 HOH B O 1 HETATM 4731 O O . HOH Z 8 . ? 33.224 70.442 43.832 1.00 32.87 ? 155 HOH B O 1 HETATM 4732 O O . HOH Z 8 . ? 2.789 68.979 15.851 1.00 34.30 ? 156 HOH B O 1 HETATM 4733 O O . HOH Z 8 . ? 39.515 75.332 36.080 1.00 27.86 ? 157 HOH B O 1 HETATM 4734 O O . HOH Z 8 . ? 22.076 52.592 5.474 1.00 50.24 ? 158 HOH B O 1 HETATM 4735 O O . HOH Z 8 . ? 28.567 48.263 53.460 1.00 30.73 ? 159 HOH B O 1 HETATM 4736 O O . HOH Z 8 . ? 10.148 64.813 7.077 1.00 36.49 ? 163 HOH B O 1 HETATM 4737 O O . HOH Z 8 . ? 24.691 33.333 28.102 1.00 31.47 ? 164 HOH B O 1 HETATM 4738 O O . HOH Z 8 . ? 14.325 41.102 34.100 1.00 25.88 ? 165 HOH B O 1 HETATM 4739 O O . HOH Z 8 . ? 46.535 65.720 31.789 1.00 26.17 ? 167 HOH B O 1 HETATM 4740 O O . HOH Z 8 . ? 48.865 53.600 31.164 1.00 35.71 ? 168 HOH B O 1 HETATM 4741 O O . HOH Z 8 . ? 29.547 34.561 41.922 1.00 22.69 ? 169 HOH B O 1 HETATM 4742 O O . HOH Z 8 . ? 24.915 75.763 38.177 1.00 40.25 ? 170 HOH B O 1 HETATM 4743 O O . HOH Z 8 . ? 28.801 51.707 49.727 1.00 21.09 ? 172 HOH B O 1 HETATM 4744 O O . HOH Z 8 . ? 32.789 78.249 21.239 1.00 31.34 ? 174 HOH B O 1 HETATM 4745 O O . HOH Z 8 . ? 28.004 69.693 12.973 1.00 29.57 ? 177 HOH B O 1 HETATM 4746 O O . HOH Z 8 . ? 8.306 66.480 12.398 1.00 26.04 ? 180 HOH B O 1 HETATM 4747 O O . HOH Z 8 . ? 5.367 73.251 13.672 1.00 36.05 ? 181 HOH B O 1 HETATM 4748 O O . HOH Z 8 . ? 33.806 59.068 45.870 1.00 29.69 ? 184 HOH B O 1 HETATM 4749 O O . HOH Z 8 . ? 42.111 70.346 31.544 1.00 27.32 ? 185 HOH B O 1 HETATM 4750 O O . HOH Z 8 . ? 48.851 58.106 31.318 1.00 29.90 ? 186 HOH B O 1 HETATM 4751 O O . HOH Z 8 . ? -1.364 67.533 21.847 1.00 31.56 ? 187 HOH B O 1 HETATM 4752 O O . HOH Z 8 . ? 5.181 66.172 15.972 1.00 38.07 ? 189 HOH B O 1 HETATM 4753 O O . HOH Z 8 . ? 26.095 66.010 10.846 1.00 41.65 ? 193 HOH B O 1 HETATM 4754 O O . HOH Z 8 . ? 8.093 66.693 9.542 1.00 36.86 ? 195 HOH B O 1 HETATM 4755 O O . HOH Z 8 . ? 12.516 61.354 8.010 1.00 34.99 ? 196 HOH B O 1 HETATM 4756 O O . HOH Z 8 . ? 34.805 52.169 13.018 1.00 37.55 ? 199 HOH B O 1 HETATM 4757 O O . HOH Z 8 . ? 38.876 73.885 31.497 1.00 25.96 ? 200 HOH B O 1 HETATM 4758 O O . HOH Z 8 . ? 30.798 58.094 47.207 1.00 40.78 ? 201 HOH B O 1 HETATM 4759 O O . HOH Z 8 . ? 29.307 37.663 18.212 1.00 52.74 ? 203 HOH B O 1 HETATM 4760 O O . HOH Z 8 . ? 6.742 74.599 24.891 1.00 26.32 ? 204 HOH B O 1 HETATM 4761 O O . HOH Z 8 . ? 24.976 36.383 26.045 1.00 37.64 ? 206 HOH B O 1 HETATM 4762 O O . HOH Z 8 . ? 36.662 40.548 38.606 1.00 46.73 ? 207 HOH B O 1 HETATM 4763 O O . HOH Z 8 . ? 36.543 56.141 15.201 1.00 45.78 ? 214 HOH B O 1 HETATM 4764 O O . HOH Z 8 . ? 26.210 80.649 22.822 1.00 43.55 ? 216 HOH B O 1 HETATM 4765 O O . HOH Z 8 . ? 1.284 67.459 17.978 1.00 53.41 ? 217 HOH B O 1 HETATM 4766 O O . HOH Z 8 . ? 25.364 49.935 44.508 1.00 21.04 ? 218 HOH B O 1 HETATM 4767 O O . HOH Z 8 . ? 17.701 69.558 48.496 1.00 66.36 ? 221 HOH B O 1 HETATM 4768 O O . HOH Z 8 . ? 21.532 63.157 6.030 1.00 35.79 ? 222 HOH B O 1 HETATM 4769 O O . HOH Z 8 . ? 25.426 55.389 55.387 1.00 49.63 ? 224 HOH B O 1 HETATM 4770 O O . HOH Z 8 . ? 17.083 30.736 25.096 1.00 29.60 ? 225 HOH B O 1 HETATM 4771 O O . HOH Z 8 . ? 35.054 41.389 22.859 1.00 37.01 ? 229 HOH B O 1 HETATM 4772 O O . HOH Z 8 . ? 45.785 56.080 41.359 1.00 40.45 ? 230 HOH B O 1 HETATM 4773 O O . HOH Z 8 . ? 3.255 73.248 39.154 1.00 43.34 ? 232 HOH B O 1 HETATM 4774 O O . HOH Z 8 . ? 8.046 79.178 27.060 1.00 31.63 ? 233 HOH B O 1 HETATM 4775 O O . HOH Z 8 . ? 29.792 54.724 51.900 1.00 39.16 ? 234 HOH B O 1 HETATM 4776 O O . HOH Z 8 . ? 18.671 78.741 32.669 1.00 46.31 ? 235 HOH B O 1 HETATM 4777 O O . HOH Z 8 . ? 36.390 38.417 30.265 1.00 52.45 ? 236 HOH B O 1 HETATM 4778 O O . HOH Z 8 . ? 48.292 71.047 39.496 1.00 36.52 ? 237 HOH B O 1 HETATM 4779 O O . HOH Z 8 . ? 28.176 67.155 12.057 1.00 27.27 ? 239 HOH B O 1 HETATM 4780 O O . HOH Z 8 . ? 47.662 61.117 40.043 1.00 27.60 ? 241 HOH B O 1 HETATM 4781 O O . HOH Z 8 . ? 31.598 57.907 44.477 1.00 23.58 ? 243 HOH B O 1 HETATM 4782 O O . HOH Z 8 . ? 49.749 59.426 40.796 1.00 49.61 ? 244 HOH B O 1 HETATM 4783 O O . HOH Z 8 . ? 39.890 48.925 44.783 1.00 48.35 ? 246 HOH B O 1 HETATM 4784 O O . HOH Z 8 . ? 45.761 55.061 25.526 1.00 56.16 ? 608 HOH B O 1 HETATM 4785 O O . HOH Z 8 . ? 41.373 56.907 21.213 1.00 37.58 ? 609 HOH B O 1 HETATM 4786 O O . HOH Z 8 . ? 29.027 41.517 13.487 1.00 43.22 ? 610 HOH B O 1 HETATM 4787 O O . HOH Z 8 . ? 29.296 40.696 15.972 1.00 39.14 ? 611 HOH B O 1 HETATM 4788 O O . HOH Z 8 . ? 38.339 57.686 18.244 1.00 44.14 ? 612 HOH B O 1 HETATM 4789 O O . HOH Z 8 . ? 28.023 37.637 14.868 1.00 48.37 ? 613 HOH B O 1 HETATM 4790 O O . HOH Z 8 . ? 23.692 42.257 8.860 1.00 44.80 ? 614 HOH B O 1 HETATM 4791 O O . HOH Z 8 . ? 50.447 66.944 36.540 1.00 57.66 ? 615 HOH B O 1 HETATM 4792 O O . HOH Z 8 . ? 23.106 48.584 43.189 1.00 17.24 ? 616 HOH B O 1 HETATM 4793 O O . HOH Z 8 . ? 16.690 69.820 26.647 1.00 15.55 ? 617 HOH B O 1 HETATM 4794 O O . HOH Z 8 . ? 29.635 58.230 22.414 1.00 18.61 ? 618 HOH B O 1 HETATM 4795 O O . HOH Z 8 . ? 33.642 41.407 56.191 1.00 45.14 ? 619 HOH B O 1 HETATM 4796 O O . HOH Z 8 . ? 14.838 57.495 7.418 1.00 48.40 ? 620 HOH B O 1 HETATM 4797 O O . HOH Z 8 . ? -0.276 71.312 31.377 1.00 33.25 ? 621 HOH B O 1 HETATM 4798 O O . HOH Z 8 . ? 35.307 43.017 51.914 1.00 54.43 ? 622 HOH B O 1 HETATM 4799 O O . HOH Z 8 . ? 32.631 50.187 49.700 1.00 26.45 ? 623 HOH B O 1 HETATM 4800 O O . HOH Z 8 . ? 0.517 70.172 34.295 1.00 46.52 ? 624 HOH B O 1 HETATM 4801 O O . HOH Z 8 . ? 23.319 36.991 53.053 1.00 26.40 ? 625 HOH B O 1 HETATM 4802 O O . HOH Z 8 . ? 47.337 71.269 33.333 1.00 37.59 ? 626 HOH B O 1 HETATM 4803 O O . HOH Z 8 . ? 18.186 55.829 10.975 1.00 55.72 ? 627 HOH B O 1 HETATM 4804 O O . HOH Z 8 . ? 16.726 53.718 4.312 1.00 42.23 ? 628 HOH B O 1 HETATM 4805 O O . HOH Z 8 . ? 28.798 47.964 5.773 1.00 47.73 ? 629 HOH B O 1 HETATM 4806 O O . HOH Z 8 . ? 29.576 77.850 22.713 1.00 56.00 ? 630 HOH B O 1 HETATM 4807 O O . HOH Z 8 . ? 27.319 48.605 8.065 1.00 25.18 ? 631 HOH B O 1 HETATM 4808 O O . HOH Z 8 . ? 22.964 49.363 9.499 1.00 37.26 ? 632 HOH B O 1 HETATM 4809 O O . HOH Z 8 . ? 48.655 68.900 34.738 1.00 48.09 ? 633 HOH B O 1 HETATM 4810 O O . HOH Z 8 . ? 28.375 75.127 41.778 1.00 64.95 ? 634 HOH B O 1 HETATM 4811 O O . HOH Z 8 . ? 31.678 79.550 35.487 1.00 44.11 ? 635 HOH B O 1 HETATM 4812 O O . HOH Z 8 . ? 40.719 51.063 23.089 1.00 36.33 ? 636 HOH B O 1 HETATM 4813 O O . HOH Z 8 . ? 35.021 39.624 49.134 1.00 43.15 ? 637 HOH B O 1 HETATM 4814 O O . HOH Z 8 . ? 46.062 66.037 46.209 1.00 43.05 ? 638 HOH B O 1 HETATM 4815 O O . HOH Z 8 . ? 18.283 80.526 12.512 1.00 36.90 ? 639 HOH B O 1 HETATM 4816 O O . HOH Z 8 . ? -3.130 74.047 25.841 1.00 48.54 ? 640 HOH B O 1 HETATM 4817 O O . HOH Z 8 . ? 11.337 82.656 26.211 1.00 51.67 ? 641 HOH B O 1 HETATM 4818 O O . HOH Z 8 . ? 9.535 78.563 20.113 1.00 49.88 ? 642 HOH B O 1 HETATM 4819 O O . HOH Z 8 . ? 6.728 74.822 20.667 1.00 30.05 ? 643 HOH B O 1 HETATM 4820 O O . HOH Z 8 . ? 22.532 77.850 6.442 1.00 50.27 ? 644 HOH B O 1 HETATM 4821 O O . HOH Z 8 . ? 20.611 79.247 9.593 1.00 43.28 ? 645 HOH B O 1 HETATM 4822 O O . HOH Z 8 . ? 17.045 76.710 6.802 1.00 31.41 ? 646 HOH B O 1 HETATM 4823 O O . HOH Z 8 . ? 22.055 78.765 11.991 1.00 32.54 ? 647 HOH B O 1 HETATM 4824 O O . HOH Z 8 . ? 10.114 60.617 19.977 1.00 39.95 ? 648 HOH B O 1 HETATM 4825 O O . HOH Z 8 . ? 21.703 32.375 19.537 1.00 43.16 ? 649 HOH B O 1 HETATM 4826 O O . HOH Z 8 . ? 20.351 75.600 34.168 1.00 41.77 ? 650 HOH B O 1 HETATM 4827 O O . HOH Z 8 . ? 41.160 59.342 46.030 1.00 43.47 ? 651 HOH B O 1 HETATM 4828 O O . HOH Z 8 . ? 24.789 54.337 17.972 1.00 24.13 ? 652 HOH B O 1 HETATM 4829 O O . HOH Z 8 . ? 20.311 62.613 3.699 1.00 38.09 ? 653 HOH B O 1 HETATM 4830 O O . HOH Z 8 . ? 22.629 67.011 2.123 1.00 61.27 ? 654 HOH B O 1 HETATM 4831 O O . HOH Z 8 . ? 50.786 60.978 26.167 1.00 59.32 ? 655 HOH B O 1 HETATM 4832 O O . HOH Z 8 . ? 9.193 77.346 18.129 1.00 57.83 ? 656 HOH B O 1 HETATM 4833 O O . HOH Z 8 . ? 36.274 68.386 44.168 1.00 33.23 ? 657 HOH B O 1 HETATM 4834 O O . HOH Z 8 . ? 42.747 70.615 43.438 1.00 36.43 ? 658 HOH B O 1 HETATM 4835 O O . HOH Z 8 . ? 22.269 38.743 55.286 1.00 28.38 ? 659 HOH B O 1 HETATM 4836 O O . HOH Z 8 . ? 7.483 73.850 18.352 1.00 37.61 ? 660 HOH B O 1 HETATM 4837 O O . HOH Z 8 . ? 7.189 57.022 27.927 1.00 49.30 ? 661 HOH B O 1 HETATM 4838 O O . HOH Z 8 . ? 16.752 48.027 15.165 1.00 61.26 ? 662 HOH B O 1 HETATM 4839 O O . HOH Z 8 . ? 39.029 60.042 23.908 1.00 49.93 ? 663 HOH B O 1 HETATM 4840 O O . HOH Z 8 . ? 35.316 66.387 14.229 1.00 32.18 ? 664 HOH B O 1 HETATM 4841 O O . HOH Z 8 . ? 37.303 62.648 19.297 1.00 57.25 ? 665 HOH B O 1 HETATM 4842 O O . HOH Z 8 . ? 22.087 64.481 8.681 1.00 43.92 ? 666 HOH B O 1 HETATM 4843 O O . HOH Z 8 . ? 23.836 65.819 4.342 1.00 56.31 ? 667 HOH B O 1 HETATM 4844 O O . HOH Z 8 . ? 28.941 59.446 4.011 1.00 37.58 ? 668 HOH B O 1 HETATM 4845 O O . HOH Z 8 . ? 19.093 78.036 35.547 1.00 37.51 ? 669 HOH B O 1 HETATM 4846 O O . HOH Z 8 . ? 29.199 70.809 11.071 1.00 41.68 ? 670 HOH B O 1 HETATM 4847 O O . HOH Z 8 . ? 24.991 78.693 27.274 1.00 37.83 ? 671 HOH B O 1 HETATM 4848 O O . HOH Z 8 . ? 33.516 73.602 40.622 1.00 35.17 ? 672 HOH B O 1 HETATM 4849 O O . HOH Z 8 . ? 24.839 79.128 11.757 1.00 36.47 ? 673 HOH B O 1 HETATM 4850 O O . HOH Z 8 . ? 34.670 45.397 10.368 1.00 38.18 ? 674 HOH B O 1 HETATM 4851 O O . HOH Z 8 . ? 8.672 81.575 25.819 1.00 44.71 ? 675 HOH B O 1 HETATM 4852 O O . HOH Z 8 . ? 31.139 79.345 39.111 1.00 54.24 ? 676 HOH B O 1 HETATM 4853 O O . HOH Z 8 . ? 21.825 66.671 11.061 1.00 49.79 ? 677 HOH B O 1 HETATM 4854 O O . HOH Z 8 . ? 23.364 82.945 20.016 1.00 40.15 ? 678 HOH B O 1 HETATM 4855 O O . HOH Z 8 . ? 1.788 60.504 28.094 1.00 26.97 ? 679 HOH B O 1 HETATM 4856 O O . HOH Z 8 . ? 27.243 50.829 54.617 1.00 41.69 ? 680 HOH B O 1 HETATM 4857 O O . HOH Z 8 . ? 29.836 80.989 37.508 1.00 58.65 ? 681 HOH B O 1 HETATM 4858 O O . HOH Z 8 . ? 52.343 60.052 34.680 1.00 44.33 ? 682 HOH B O 1 HETATM 4859 O O . HOH Z 8 . ? 21.859 52.289 17.103 1.00 44.42 ? 683 HOH B O 1 HETATM 4860 O O . HOH Z 8 . ? 6.682 62.719 25.634 1.00 29.96 ? 684 HOH B O 1 HETATM 4861 O O . HOH Z 8 . ? 32.583 79.893 32.637 1.00 41.65 ? 685 HOH B O 1 HETATM 4862 O O . HOH Z 8 . ? 29.964 39.266 27.970 1.00 42.34 ? 686 HOH B O 1 HETATM 4863 O O . HOH Z 8 . ? 4.108 69.403 40.055 1.00 38.52 ? 687 HOH B O 1 HETATM 4864 O O . HOH Z 8 . ? 17.739 66.604 49.362 1.00 54.94 ? 688 HOH B O 1 HETATM 4865 O O . HOH Z 8 . ? 4.502 73.050 11.269 1.00 44.37 ? 689 HOH B O 1 HETATM 4866 O O . HOH Z 8 . ? 35.316 35.609 53.872 1.00 63.03 ? 690 HOH B O 1 HETATM 4867 O O . HOH Z 8 . ? 20.583 55.794 20.747 1.00 47.13 ? 691 HOH B O 1 HETATM 4868 O O . HOH Z 8 . ? 46.999 52.788 29.282 1.00 58.98 ? 692 HOH B O 1 HETATM 4869 O O . HOH Z 8 . ? 43.206 62.701 47.851 1.00 38.40 ? 693 HOH B O 1 HETATM 4870 O O . HOH Z 8 . ? 13.316 82.034 30.232 1.00 38.22 ? 694 HOH B O 1 HETATM 4871 O O . HOH Z 8 . ? 13.112 34.064 22.064 1.00 39.87 ? 695 HOH B O 1 HETATM 4872 O O . HOH Z 8 . ? 12.000 29.644 26.137 1.00 36.71 ? 696 HOH B O 1 HETATM 4873 O O . HOH Z 8 . ? 32.018 48.272 6.504 1.00 49.69 ? 697 HOH B O 1 HETATM 4874 O O . HOH Z 8 . ? 20.379 77.814 7.474 1.00 48.42 ? 698 HOH B O 1 HETATM 4875 O O . HOH Z 8 . ? 39.582 68.111 43.648 1.00 34.74 ? 699 HOH B O 1 HETATM 4876 O O . HOH Z 8 . ? 33.686 42.549 43.757 1.00 48.06 ? 700 HOH B O 1 HETATM 4877 O O . HOH Z 8 . ? 39.810 46.491 24.730 1.00 40.79 ? 701 HOH B O 1 HETATM 4878 O O . HOH Z 8 . ? 39.574 63.868 21.923 1.00 40.97 ? 702 HOH B O 1 HETATM 4879 O O . HOH Z 8 . ? 43.187 69.933 46.011 1.00 41.38 ? 703 HOH B O 1 HETATM 4880 O O . HOH Z 8 . ? -2.941 66.240 29.414 1.00 49.46 ? 704 HOH B O 1 HETATM 4881 O O . HOH Z 8 . ? 35.540 41.960 26.891 1.00 50.80 ? 705 HOH B O 1 HETATM 4882 O O . HOH Z 8 . ? 39.733 68.619 18.747 1.00 39.16 ? 706 HOH B O 1 HETATM 4883 O O . HOH Z 8 . ? 24.219 52.817 56.471 1.00 49.73 ? 707 HOH B O 1 HETATM 4884 O O . HOH Z 8 . ? 18.442 63.602 2.144 1.00 56.44 ? 708 HOH B O 1 HETATM 4885 O O . HOH Z 8 . ? 46.103 53.596 39.179 1.00 33.01 ? 709 HOH B O 1 HETATM 4886 O O . HOH Z 8 . ? 19.432 72.082 47.650 1.00 53.52 ? 710 HOH B O 1 HETATM 4887 O O . HOH Z 8 . ? 41.308 74.432 37.645 1.00 37.38 ? 711 HOH B O 1 HETATM 4888 O O . HOH Z 8 . ? 15.481 78.609 20.339 1.00 50.24 ? 712 HOH B O 1 HETATM 4889 O O . HOH Z 8 . ? 33.332 55.462 8.521 1.00 40.74 ? 713 HOH B O 1 HETATM 4890 O O . HOH Z 8 . ? 9.121 61.018 22.346 1.00 36.64 ? 714 HOH B O 1 HETATM 4891 O O . HOH Z 8 . ? 37.907 61.767 12.500 1.00 54.15 ? 715 HOH B O 1 HETATM 4892 O O . HOH Z 8 . ? 23.202 41.605 56.177 1.00 43.59 ? 716 HOH B O 1 HETATM 4893 O O . HOH Z 8 . ? 16.349 39.461 12.834 1.00 55.98 ? 717 HOH B O 1 HETATM 4894 O O . HOH Z 8 . ? 1.756 76.180 13.307 1.00 68.11 ? 718 HOH B O 1 HETATM 4895 O O . HOH Z 8 . ? 26.714 40.498 11.321 1.00 38.40 ? 719 HOH B O 1 HETATM 4896 O O . HOH Z 8 . ? 8.026 80.996 29.410 1.00 45.74 ? 720 HOH B O 1 HETATM 4897 O O . HOH Z 8 . ? 34.330 65.113 21.376 1.00 36.72 ? 721 HOH B O 1 HETATM 4898 O O . HOH Z 8 . ? 29.105 48.973 51.132 1.00 41.18 ? 722 HOH B O 1 HETATM 4899 O O . HOH Z 8 . ? 14.674 77.778 11.399 1.00 42.36 ? 723 HOH B O 1 HETATM 4900 O O . HOH Z 8 . ? 5.399 79.023 26.677 1.00 40.25 ? 724 HOH B O 1 HETATM 4901 O O . HOH Z 8 . ? 40.424 44.946 40.077 1.00 40.83 ? 725 HOH B O 1 HETATM 4902 O O . HOH Z 8 . ? 31.677 39.006 57.221 1.00 53.51 ? 726 HOH B O 1 HETATM 4903 O O . HOH Z 8 . ? 24.303 32.485 57.053 1.00 42.68 ? 727 HOH B O 1 HETATM 4904 O O . HOH Z 8 . ? 14.500 31.596 21.726 1.00 44.07 ? 728 HOH B O 1 HETATM 4905 O O . HOH Z 8 . ? 9.199 54.884 29.276 1.00 43.28 ? 729 HOH B O 1 HETATM 4906 O O . HOH Z 8 . ? 10.481 55.994 15.110 1.00 42.11 ? 730 HOH B O 1 HETATM 4907 O O . HOH Z 8 . ? 19.798 53.637 19.654 1.00 42.37 ? 731 HOH B O 1 HETATM 4908 O O . HOH Z 8 . ? 13.210 78.074 19.394 1.00 37.80 ? 732 HOH B O 1 HETATM 4909 O O . HOH Z 8 . ? 45.651 51.102 31.703 1.00 50.54 ? 733 HOH B O 1 HETATM 4910 O O . HOH Z 8 . ? 16.973 36.833 14.930 1.00 43.53 ? 734 HOH B O 1 HETATM 4911 O O . HOH Z 8 . ? 34.920 53.766 49.462 1.00 40.94 ? 735 HOH B O 1 HETATM 4912 O O . HOH Z 8 . ? 15.121 65.943 4.412 1.00 46.54 ? 736 HOH B O 1 HETATM 4913 O O . HOH Z 8 . ? 24.018 45.724 9.744 1.00 49.76 ? 737 HOH B O 1 HETATM 4914 O O . HOH Z 8 . ? 27.909 71.990 46.875 1.00 59.07 ? 738 HOH B O 1 HETATM 4915 O O . HOH Z 8 . ? 28.915 36.005 20.741 1.00 44.06 ? 739 HOH B O 1 HETATM 4916 O O . HOH Z 8 . ? 30.049 42.617 58.417 1.00 46.98 ? 740 HOH B O 1 HETATM 4917 O O . HOH Z 8 . ? 30.405 79.276 32.183 1.00 37.09 ? 741 HOH B O 1 HETATM 4918 O O . HOH Z 8 . ? 38.628 71.361 43.887 1.00 58.77 ? 742 HOH B O 1 HETATM 4919 O O . HOH Z 8 . ? 24.243 60.297 18.294 1.00 32.82 ? 743 HOH B O 1 HETATM 4920 O O . HOH Z 8 . ? 46.842 57.696 25.522 1.00 44.78 ? 744 HOH B O 1 HETATM 4921 O O . HOH Z 8 . ? 32.020 43.816 12.156 1.00 46.98 ? 745 HOH B O 1 HETATM 4922 O O . HOH Z 8 . ? 0.702 69.038 39.466 1.00 59.13 ? 746 HOH B O 1 HETATM 4923 O O . HOH Z 8 . ? 48.072 59.951 29.368 1.00 23.17 ? 747 HOH B O 1 HETATM 4924 O O . HOH Z 8 . ? 49.174 58.864 26.828 1.00 38.89 ? 748 HOH B O 1 HETATM 4925 O O . HOH Z 8 . ? 13.661 65.341 34.402 1.00 22.71 ? 749 HOH B O 1 HETATM 4926 O O . HOH Z 8 . ? 44.935 60.502 39.521 1.00 28.24 ? 750 HOH B O 1 HETATM 4927 O O . HOH Z 8 . ? 45.041 64.208 38.548 1.00 26.31 ? 751 HOH B O 1 HETATM 4928 O O . HOH Z 8 . ? 31.517 79.268 18.854 1.00 38.23 ? 752 HOH B O 1 HETATM 4929 O O . HOH Z 8 . ? 32.199 81.971 16.016 1.00 53.65 ? 753 HOH B O 1 HETATM 4930 O O . HOH Z 8 . ? 15.577 54.097 30.294 1.00 43.93 ? 754 HOH B O 1 HETATM 4931 O O . HOH Z 8 . ? 42.687 60.673 46.074 1.00 43.10 ? 755 HOH B O 1 HETATM 4932 O O . HOH Z 8 . ? 2.329 71.095 39.494 1.00 50.08 ? 756 HOH B O 1 HETATM 4933 O O . HOH Z 8 . ? 41.855 47.465 38.718 1.00 39.45 ? 757 HOH B O 1 HETATM 4934 O O . HOH Z 8 . ? 36.120 42.786 31.677 1.00 35.97 ? 758 HOH B O 1 HETATM 4935 O O . HOH Z 8 . ? 15.086 74.472 41.047 1.00 38.57 ? 759 HOH B O 1 HETATM 4936 O O . HOH Z 8 . ? 10.478 71.275 2.598 1.00 62.83 ? 760 HOH B O 1 HETATM 4937 O O . HOH Z 8 . ? -0.559 60.262 26.812 1.00 37.58 ? 761 HOH B O 1 HETATM 4938 O O . HOH Z 8 . ? 36.456 57.890 46.881 1.00 44.92 ? 762 HOH B O 1 HETATM 4939 O O . HOH Z 8 . ? 25.317 59.206 53.455 1.00 49.85 ? 763 HOH B O 1 HETATM 4940 O O . HOH Z 8 . ? 37.539 42.783 22.778 1.00 50.65 ? 764 HOH B O 1 HETATM 4941 O O . HOH Z 8 . ? 25.956 79.474 20.338 1.00 44.30 ? 765 HOH B O 1 HETATM 4942 O O . HOH Z 8 . ? 24.946 81.799 27.253 1.00 60.53 ? 766 HOH B O 1 HETATM 4943 O O . HOH Z 8 . ? 34.106 47.757 50.624 1.00 54.67 ? 767 HOH B O 1 HETATM 4944 O O . HOH Z 8 . ? 22.569 66.598 6.535 1.00 46.18 ? 768 HOH B O 1 HETATM 4945 O O . HOH Z 8 . ? 0.333 76.940 33.432 1.00 54.12 ? 769 HOH B O 1 HETATM 4946 O O . HOH Z 8 . ? 15.226 81.308 20.739 1.00 50.73 ? 770 HOH B O 1 HETATM 4947 O O . HOH Z 8 . ? 21.034 35.836 12.665 1.00 47.34 ? 771 HOH B O 1 HETATM 4948 O O . HOH Z 8 . ? 24.114 62.560 50.699 1.00 45.01 ? 772 HOH B O 1 HETATM 4949 O O . HOH Z 8 . ? 5.643 77.950 24.190 1.00 44.36 ? 773 HOH B O 1 HETATM 4950 O O . HOH Z 8 . ? 15.076 79.150 40.834 1.00 52.47 ? 774 HOH B O 1 HETATM 4951 O O . HOH Z 8 . ? 45.339 49.794 29.102 1.00 52.99 ? 775 HOH B O 1 HETATM 4952 O O . HOH Z 8 . ? 26.235 60.596 2.309 1.00 60.35 ? 776 HOH B O 1 HETATM 4953 O O . HOH Z 8 . ? 41.582 48.913 41.969 1.00 41.39 ? 777 HOH B O 1 HETATM 4954 O O . HOH Z 8 . ? 41.913 73.141 43.548 1.00 53.85 ? 778 HOH B O 1 HETATM 4955 O O . HOH Z 8 . ? 33.292 40.531 42.076 1.00 52.00 ? 779 HOH B O 1 HETATM 4956 O O . HOH Z 8 . ? 24.317 84.738 18.086 1.00 65.58 ? 780 HOH B O 1 HETATM 4957 O O . HOH Z 8 . ? 7.453 62.612 15.996 1.00 43.50 ? 781 HOH B O 1 HETATM 4958 O O . HOH Z 8 . ? 48.304 72.714 41.026 1.00 54.18 ? 782 HOH B O 1 HETATM 4959 O O . HOH Z 8 . ? 19.628 82.217 21.605 1.00 53.65 ? 783 HOH B O 1 HETATM 4960 O O . HOH Z 8 . ? 28.370 57.115 0.772 1.00 36.19 ? 784 HOH B O 1 HETATM 4961 O O . HOH Z 8 . ? -1.170 78.009 29.064 1.00 38.66 ? 785 HOH B O 1 HETATM 4962 O O . HOH Z 8 . ? 31.214 55.851 4.379 1.00 37.72 ? 786 HOH B O 1 HETATM 4963 O O . HOH Z 8 . ? 33.018 57.604 48.472 1.00 44.56 ? 787 HOH B O 1 HETATM 4964 O O . HOH Z 8 . ? 36.198 78.921 37.881 1.00 44.41 ? 788 HOH B O 1 HETATM 4965 O O . HOH Z 8 . ? 35.709 44.759 13.239 1.00 45.73 ? 789 HOH B O 1 HETATM 4966 O O . HOH Z 8 . ? 31.156 38.130 43.657 1.00 53.19 ? 790 HOH B O 1 HETATM 4967 O O . HOH Z 8 . ? 39.269 43.949 28.449 1.00 51.43 ? 791 HOH B O 1 HETATM 4968 O O . HOH Z 8 . ? 4.031 72.428 15.731 1.00 37.83 ? 792 HOH B O 1 HETATM 4969 O O . HOH Z 8 . ? 25.874 64.300 4.386 1.00 57.89 ? 793 HOH B O 1 HETATM 4970 O O . HOH Z 8 . ? 39.873 60.697 26.328 1.00 30.79 ? 794 HOH B O 1 HETATM 4971 O O . HOH Z 8 . ? 33.389 59.789 9.715 1.00 46.24 ? 795 HOH B O 1 HETATM 4972 O O . HOH Z 8 . ? 40.317 45.775 29.803 1.00 52.55 ? 796 HOH B O 1 HETATM 4973 O O . HOH Z 8 . ? 20.528 33.776 52.462 1.00 45.89 ? 797 HOH B O 1 HETATM 4974 O O . HOH Z 8 . ? 49.922 55.639 30.317 1.00 37.78 ? 798 HOH B O 1 HETATM 4975 O O . HOH Z 8 . ? 39.280 46.428 32.599 1.00 48.65 ? 799 HOH B O 1 HETATM 4976 O O . HOH Z 8 . ? 36.018 55.907 48.340 1.00 40.92 ? 800 HOH B O 1 HETATM 4977 O O . HOH Z 8 . ? 23.867 80.573 29.525 1.00 47.24 ? 801 HOH B O 1 HETATM 4978 O O . HOH Z 8 . ? 42.173 52.308 45.775 1.00 65.71 ? 802 HOH B O 1 HETATM 4979 O O . HOH Z 8 . ? 14.156 30.055 23.631 1.00 44.99 ? 803 HOH B O 1 HETATM 4980 O O . HOH Z 8 . ? 40.676 68.311 46.018 1.00 53.07 ? 804 HOH B O 1 HETATM 4981 O O . HOH Z 8 . ? 33.048 43.792 49.814 1.00 55.46 ? 805 HOH B O 1 HETATM 4982 O O . HOH Z 8 . ? 43.556 75.187 42.448 1.00 47.10 ? 806 HOH B O 1 HETATM 4983 O O . HOH Z 8 . ? 26.331 79.396 9.658 1.00 50.36 ? 807 HOH B O 1 HETATM 4984 O O . HOH Z 8 . ? 36.222 41.809 54.000 1.00 56.82 ? 808 HOH B O 1 HETATM 4985 O O . HOH Z 8 . ? 27.130 36.854 24.777 1.00 59.36 ? 809 HOH B O 1 HETATM 4986 O O . HOH Z 8 . ? 13.631 75.691 13.084 1.00 45.46 ? 810 HOH B O 1 HETATM 4987 O O . HOH Z 8 . ? 35.816 61.819 24.030 1.00 22.07 ? 811 HOH B O 1 HETATM 4988 O O . HOH Z 8 . ? 33.006 38.288 33.453 1.00 23.34 ? 812 HOH B O 1 HETATM 4989 O O . HOH Z 8 . ? 45.336 66.627 34.192 1.00 38.63 ? 813 HOH B O 1 HETATM 4990 O O . HOH Z 8 . ? 47.466 66.572 28.214 1.00 28.13 ? 814 HOH B O 1 HETATM 4991 O O . HOH Z 8 . ? 32.824 31.700 48.803 1.00 31.92 ? 815 HOH B O 1 HETATM 4992 O O . HOH Z 8 . ? 6.582 75.485 36.983 1.00 28.58 ? 816 HOH B O 1 HETATM 4993 O O . HOH Z 8 . ? 49.864 63.172 33.161 1.00 40.05 ? 817 HOH B O 1 HETATM 4994 O O . HOH Z 8 . ? 22.762 34.973 24.024 1.00 37.82 ? 818 HOH B O 1 HETATM 4995 O O . HOH Z 8 . ? 37.211 60.293 47.632 1.00 42.42 ? 819 HOH B O 1 HETATM 4996 O O . HOH Z 8 . ? 23.779 56.674 50.670 1.00 32.10 ? 820 HOH B O 1 HETATM 4997 O O . HOH Z 8 . ? 17.217 73.381 3.557 1.00 51.47 ? 821 HOH B O 1 HETATM 4998 O O . HOH Z 8 . ? 28.384 76.601 26.508 1.00 58.90 ? 822 HOH B O 1 HETATM 4999 O O . HOH Z 8 . ? 37.746 66.396 49.256 1.00 51.12 ? 823 HOH B O 1 HETATM 5000 O O . HOH Z 8 . ? 7.153 62.678 13.167 1.00 44.72 ? 824 HOH B O 1 HETATM 5001 O O . HOH Z 8 . ? -5.072 64.852 28.717 1.00 54.24 ? 825 HOH B O 1 HETATM 5002 O O . HOH Z 8 . ? 41.244 54.746 48.665 1.00 50.38 ? 826 HOH B O 1 HETATM 5003 O O . HOH Z 8 . ? 42.179 56.407 47.385 1.00 44.38 ? 827 HOH B O 1 HETATM 5004 O O . HOH Z 8 . ? 38.512 55.510 49.481 1.00 55.18 ? 828 HOH B O 1 HETATM 5005 O O . HOH Z 8 . ? 32.464 81.529 18.265 1.00 52.15 ? 829 HOH B O 1 HETATM 5006 O O . HOH Z 8 . ? 1.773 71.147 15.645 1.00 42.80 ? 830 HOH B O 1 HETATM 5007 O O . HOH Z 8 . ? 33.013 46.397 5.241 1.00 59.33 ? 831 HOH B O 1 HETATM 5008 O O . HOH Z 8 . ? 31.452 47.477 8.872 1.00 45.31 ? 832 HOH B O 1 HETATM 5009 O O . HOH Z 8 . ? 10.898 33.733 23.971 1.00 28.01 ? 833 HOH B O 1 HETATM 5010 O O . HOH Z 8 . ? 32.848 44.935 52.953 1.00 49.33 ? 834 HOH B O 1 HETATM 5011 O O . HOH Z 8 . ? 34.019 36.089 49.990 1.00 36.82 ? 835 HOH B O 1 HETATM 5012 O O . HOH Z 8 . ? 31.804 43.327 55.824 1.00 25.36 ? 836 HOH B O 1 HETATM 5013 O O . HOH Z 8 . ? 14.322 57.225 10.144 1.00 40.42 ? 837 HOH B O 1 HETATM 5014 O O . HOH Z 8 . ? 18.465 57.356 13.994 1.00 58.60 ? 838 HOH B O 1 HETATM 5015 O O . HOH Z 8 . ? 9.642 75.951 36.677 1.00 28.46 ? 839 HOH B O 1 HETATM 5016 O O . HOH Z 8 . ? 14.591 78.984 37.771 1.00 34.77 ? 840 HOH B O 1 HETATM 5017 O O . HOH Z 8 . ? 2.504 77.941 35.005 1.00 53.99 ? 841 HOH B O 1 HETATM 5018 O O . HOH Z 8 . ? 1.124 80.425 31.107 1.00 61.84 ? 842 HOH B O 1 HETATM 5019 O O . HOH Z 8 . ? 3.304 80.169 33.776 1.00 61.75 ? 843 HOH B O 1 HETATM 5020 O O . HOH Z 8 . ? 34.674 62.588 21.650 1.00 33.61 ? 844 HOH B O 1 HETATM 5021 O O . HOH Z 8 . ? 34.934 58.764 13.262 1.00 27.98 ? 845 HOH B O 1 HETATM 5022 O O . HOH Z 8 . ? 18.239 73.852 33.974 1.00 37.35 ? 846 HOH B O 1 HETATM 5023 O O . HOH Z 8 . ? 37.158 51.781 11.972 1.00 46.24 ? 847 HOH B O 1 HETATM 5024 O O . HOH Z 8 . ? 39.449 47.518 22.348 1.00 59.31 ? 848 HOH B O 1 HETATM 5025 O O . HOH Z 8 . ? 37.755 48.237 18.570 1.00 31.49 ? 849 HOH B O 1 HETATM 5026 O O . HOH Z 8 . ? 44.480 48.932 33.115 1.00 52.00 ? 850 HOH B O 1 HETATM 5027 O O . HOH Z 8 . ? 51.432 58.792 38.831 1.00 49.81 ? 851 HOH B O 1 HETATM 5028 O O . HOH Z 8 . ? 51.541 61.389 42.179 1.00 56.43 ? 852 HOH B O 1 HETATM 5029 O O . HOH Z 8 . ? 49.115 54.284 39.348 1.00 61.89 ? 853 HOH B O 1 HETATM 5030 O O . HOH Z 8 . ? 23.114 55.786 16.089 1.00 45.03 ? 854 HOH B O 1 HETATM 5031 O O . HOH Z 8 . ? 25.762 50.674 18.343 1.00 29.73 ? 855 HOH B O 1 HETATM 5032 O O . HOH Z 8 . ? 33.415 63.813 6.582 1.00 47.08 ? 856 HOH B O 1 HETATM 5033 O O . HOH Z 8 . ? 26.581 65.681 7.892 1.00 48.81 ? 857 HOH B O 1 HETATM 5034 O O . HOH Z 8 . ? 33.227 57.699 6.072 1.00 58.93 ? 858 HOH B O 1 HETATM 5035 O O . HOH Z 8 . ? 37.294 44.095 20.233 1.00 46.37 ? 859 HOH B O 1 HETATM 5036 O O . HOH Z 8 . ? -3.698 72.428 28.225 1.00 55.83 ? 860 HOH B O 1 HETATM 5037 O O . HOH Z 8 . ? -1.539 70.817 28.607 1.00 35.23 ? 861 HOH B O 1 HETATM 5038 O O . HOH Z 8 . ? -1.883 65.451 31.963 1.00 28.50 ? 862 HOH B O 1 HETATM 5039 O O . HOH Z 8 . ? 0.215 60.007 23.651 1.00 57.68 ? 863 HOH B O 1 HETATM 5040 O O . HOH Z 8 . ? 20.906 74.026 46.268 1.00 43.75 ? 864 HOH B O 1 HETATM 5041 O O . HOH Z 8 . ? 31.050 76.473 39.681 1.00 25.83 ? 865 HOH B O 1 HETATM 5042 O O . HOH Z 8 . ? 16.437 45.463 13.596 1.00 38.22 ? 866 HOH B O 1 HETATM 5043 O O . HOH Z 8 . ? 30.524 79.065 15.981 1.00 42.25 ? 867 HOH B O 1 HETATM 5044 O O . HOH Z 8 . ? 34.731 71.357 41.403 1.00 51.04 ? 868 HOH B O 1 HETATM 5045 O O . HOH Z 8 . ? 22.053 53.497 57.355 1.00 53.28 ? 869 HOH B O 1 HETATM 5046 O O . HOH Z 8 . ? 0.048 65.036 21.667 1.00 44.85 ? 870 HOH B O 1 HETATM 5047 O O . HOH Z 8 . ? 6.633 62.937 20.259 1.00 31.59 ? 871 HOH B O 1 HETATM 5048 O O . HOH Z 8 . ? 15.928 59.918 4.001 1.00 36.79 ? 872 HOH B O 1 HETATM 5049 O O . HOH Z 8 . ? 29.207 51.027 52.361 1.00 44.30 ? 873 HOH B O 1 HETATM 5050 O O . HOH Z 8 . ? 8.285 77.379 22.371 1.00 51.90 ? 874 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 LEU 1 47 ? ? ? A . n A 1 2 PRO 2 48 ? ? ? A . n A 1 3 THR 3 49 ? ? ? A . n A 1 4 LEU 4 50 ? ? ? A . n A 1 5 GLY 5 51 ? ? ? A . n A 1 6 PRO 6 52 ? ? ? A . n A 1 7 GLY 7 53 ? ? ? A . n A 1 8 TRP 8 54 ? ? ? A . n A 1 9 GLN 9 55 ? ? ? A . n A 1 10 ARG 10 56 ? ? ? A . n A 1 11 GLN 11 57 ? ? ? A . n A 1 12 ASN 12 58 ? ? ? A . n A 1 13 PRO 13 59 ? ? ? A . n A 1 14 ASP 14 60 ? ? ? A . n A 1 15 PRO 15 61 ? ? ? A . n A 1 16 PRO 16 62 ? ? ? A . n A 1 17 VAL 17 63 63 VAL VAL A . n A 1 18 SER 18 64 64 SER SER A . n A 1 19 ARG 19 65 65 ARG ARG A . n A 1 20 THR 20 66 66 THR THR A . n A 1 21 ARG 21 67 67 ARG ARG A . n A 1 22 SER 22 68 68 SER SER A . n A 1 23 LEU 23 69 69 LEU LEU A . n A 1 24 LEU 24 70 70 LEU LEU A . n A 1 25 LEU 25 71 71 LEU LEU A . n A 1 26 ASP 26 72 72 ASP ASP A . n A 1 27 ALA 27 73 73 ALA ALA A . n A 1 28 ALA 28 74 74 ALA ALA A . n A 1 29 SER 29 75 75 SER SER A . n A 1 30 GLY 30 76 76 GLY GLY A . n A 1 31 GLN 31 77 77 GLN GLN A . n A 1 32 LEU 32 78 78 LEU LEU A . n A 1 33 ARG 33 79 79 ARG ARG A . n A 1 34 LEU 34 80 80 LEU LEU A . n A 1 35 GLU 35 81 81 GLU GLU A . n A 1 36 ASP 36 82 82 ASP ASP A . n A 1 37 GLY 37 83 83 GLY GLY A . n A 1 38 PHE 38 84 84 PHE PHE A . n A 1 39 HIS 39 85 85 HIS HIS A . n A 1 40 PRO 40 86 86 PRO PRO A . n A 1 41 ASP 41 87 87 ASP ASP A . n A 1 42 ALA 42 88 88 ALA ALA A . n A 1 43 VAL 43 89 89 VAL VAL A . n A 1 44 ALA 44 90 90 ALA ALA A . n A 1 45 TRP 45 91 91 TRP TRP A . n A 1 46 ALA 46 92 92 ALA ALA A . n A 1 47 ASN 47 93 93 ASN ASN A . n A 1 48 LEU 48 94 94 LEU LEU A . n A 1 49 THR 49 95 95 THR THR A . n A 1 50 ASN 50 96 96 ASN ASN A . n A 1 51 ALA 51 97 97 ALA ALA A . n A 1 52 ILE 52 98 98 ILE ILE A . n A 1 53 ARG 53 99 99 ARG ARG A . n A 1 54 GLU 54 100 100 GLU GLU A . n A 1 55 THR 55 101 101 THR THR A . n A 1 56 GLY 56 102 102 GLY GLY A . n A 1 57 TRP 57 103 103 TRP TRP A . n A 1 58 ALA 58 104 104 ALA ALA A . n A 1 59 TYR 59 105 105 TYR TYR A . n A 1 60 LEU 60 106 106 LEU LEU A . n A 1 61 ASP 61 107 107 ASP ASP A . n A 1 62 LEU 62 108 108 LEU LEU A . n A 1 63 SER 63 109 109 SER SER A . n A 1 64 THR 64 110 110 THR THR A . n A 1 65 ASN 65 111 111 ASN ASN A . n A 1 66 GLY 66 112 112 GLY GLY A . n A 1 67 ARG 67 113 113 ARG ARG A . n A 1 68 TYR 68 114 114 TYR TYR A . n A 1 69 ASN 69 115 115 ASN ASN A . n A 1 70 ASP 70 116 116 ASP ASP A . n A 1 71 SER 71 117 117 SER SER A . n A 1 72 LEU 72 118 118 LEU LEU A . n A 1 73 GLN 73 119 119 GLN GLN A . n A 1 74 ALA 74 120 120 ALA ALA A . n A 1 75 TYR 75 121 121 TYR TYR A . n A 1 76 ALA 76 122 122 ALA ALA A . n A 1 77 ALA 77 123 123 ALA ALA A . n A 1 78 GLY 78 124 124 GLY GLY A . n A 1 79 VAL 79 125 125 VAL VAL A . n A 1 80 VAL 80 126 126 VAL VAL A . n A 1 81 GLU 81 127 127 GLU GLU A . n A 1 82 ALA 82 128 128 ALA ALA A . n A 1 83 SER 83 129 129 SER SER A . n A 1 84 VAL 84 130 130 VAL VAL A . n A 1 85 SER 85 131 131 SER SER A . n A 1 86 GLU 86 132 132 GLU GLU A . n A 1 87 GLU 87 133 133 GLU GLU A . n A 1 88 LEU 88 134 134 LEU LEU A . n A 1 89 ILE 89 135 135 ILE ILE A . n A 1 90 TYR 90 136 136 TYR TYR A . n A 1 91 MET 91 137 137 MET MET A . n A 1 92 HIS 92 138 138 HIS HIS A . n A 1 93 TRP 93 139 139 TRP TRP A . n A 1 94 MET 94 140 140 MET MET A . n A 1 95 ASN 95 141 141 ASN ASN A . n A 1 96 THR 96 142 142 THR THR A . n A 1 97 VAL 97 143 143 VAL VAL A . n A 1 98 VAL 98 144 144 VAL VAL A . n A 1 99 ASN 99 145 145 ASN ASN A . n A 1 100 TYR 100 146 146 TYR TYR A . n A 1 101 CYS 101 147 147 CYS CYS A . n A 1 102 GLY 102 148 148 GLY GLY A . n A 1 103 PRO 103 149 149 PRO PRO A . n A 1 104 PHE 104 150 150 PHE PHE A . n A 1 105 GLU 105 151 151 GLU GLU A . n A 1 106 TYR 106 152 152 TYR TYR A . n A 1 107 GLU 107 153 153 GLU GLU A . n A 1 108 VAL 108 154 154 VAL VAL A . n A 1 109 GLY 109 155 155 GLY GLY A . n A 1 110 TYR 110 156 156 TYR TYR A . n A 1 111 CYS 111 157 157 CYS CYS A . n A 1 112 GLU 112 158 158 GLU GLU A . n A 1 113 LYS 113 159 159 LYS LYS A . n A 1 114 LEU 114 160 160 LEU LEU A . n A 1 115 LYS 115 161 161 LYS LYS A . n A 1 116 ASN 116 162 162 ASN ASN A . n A 1 117 PHE 117 163 163 PHE PHE A . n A 1 118 LEU 118 164 164 LEU LEU A . n A 1 119 GLU 119 165 165 GLU GLU A . n A 1 120 ALA 120 166 166 ALA ALA A . n A 1 121 ASN 121 167 167 ASN ASN A . n A 1 122 LEU 122 168 168 LEU LEU A . n A 1 123 GLU 123 169 169 GLU GLU A . n A 1 124 TRP 124 170 170 TRP TRP A . n A 1 125 MET 125 171 171 MET MET A . n A 1 126 GLN 126 172 172 GLN GLN A . n A 1 127 ARG 127 173 173 ARG ARG A . n A 1 128 GLU 128 174 174 GLU GLU A . n A 1 129 MET 129 175 175 MET MET A . n A 1 130 GLU 130 176 176 GLU GLU A . n A 1 131 LEU 131 177 177 LEU LEU A . n A 1 132 ASN 132 178 178 ASN ASN A . n A 1 133 PRO 133 179 179 PRO PRO A . n A 1 134 ASP 134 180 180 ASP ASP A . n A 1 135 SER 135 181 181 SER SER A . n A 1 136 PRO 136 182 182 PRO PRO A . n A 1 137 TYR 137 183 183 TYR TYR A . n A 1 138 TRP 138 184 184 TRP TRP A . n A 1 139 HIS 139 185 185 HIS HIS A . n A 1 140 GLN 140 186 186 GLN GLN A . n A 1 141 VAL 141 187 187 VAL VAL A . n A 1 142 ARG 142 188 188 ARG ARG A . n A 1 143 LEU 143 189 189 LEU LEU A . n A 1 144 THR 144 190 190 THR THR A . n A 1 145 LEU 145 191 191 LEU LEU A . n A 1 146 LEU 146 192 192 LEU LEU A . n A 1 147 GLN 147 193 193 GLN GLN A . n A 1 148 LEU 148 194 194 LEU LEU A . n A 1 149 LYS 149 195 195 LYS LYS A . n A 1 150 GLY 150 196 196 GLY GLY A . n A 1 151 LEU 151 197 197 LEU LEU A . n A 1 152 GLU 152 198 198 GLU GLU A . n A 1 153 ASP 153 199 199 ASP ASP A . n A 1 154 SER 154 200 200 SER SER A . n A 1 155 TYR 155 201 201 TYR TYR A . n A 1 156 GLU 156 202 202 GLU GLU A . n A 1 157 GLY 157 203 203 GLY GLY A . n A 1 158 ARG 158 204 204 ARG ARG A . n A 1 159 LEU 159 205 205 LEU LEU A . n A 1 160 THR 160 206 206 THR THR A . n A 1 161 PHE 161 207 207 PHE PHE A . n A 1 162 PRO 162 208 208 PRO PRO A . n A 1 163 THR 163 209 209 THR THR A . n A 1 164 GLY 164 210 210 GLY GLY A . n A 1 165 ARG 165 211 211 ARG ARG A . n A 1 166 PHE 166 212 212 PHE PHE A . n A 1 167 THR 167 213 213 THR THR A . n A 1 168 ILE 168 214 214 ILE ILE A . n A 1 169 LYS 169 215 215 LYS LYS A . n A 1 170 PRO 170 216 216 PRO PRO A . n A 1 171 LEU 171 217 217 LEU LEU A . n A 1 172 GLY 172 218 218 GLY GLY A . n A 1 173 PHE 173 219 219 PHE PHE A . n A 1 174 LEU 174 220 220 LEU LEU A . n A 1 175 LEU 175 221 221 LEU LEU A . n A 1 176 LEU 176 222 222 LEU LEU A . n A 1 177 GLN 177 223 223 GLN GLN A . n A 1 178 ILE 178 224 224 ILE ILE A . n A 1 179 SER 179 225 225 SER SER A . n A 1 180 GLY 180 226 226 GLY GLY A . n A 1 181 ASP 181 227 227 ASP ASP A . n A 1 182 LEU 182 228 228 LEU LEU A . n A 1 183 GLU 183 229 229 GLU GLU A . n A 1 184 ASP 184 230 230 ASP ASP A . n A 1 185 LEU 185 231 231 LEU LEU A . n A 1 186 GLU 186 232 232 GLU GLU A . n A 1 187 PRO 187 233 233 PRO PRO A . n A 1 188 ALA 188 234 234 ALA ALA A . n A 1 189 LEU 189 235 235 LEU LEU A . n A 1 190 ASN 190 236 236 ASN ASN A . n A 1 191 LYS 191 237 237 LYS LYS A . n A 1 192 THR 192 238 238 THR THR A . n A 1 193 ASN 193 239 ? ? ? A . n A 1 194 THR 194 240 ? ? ? A . n A 1 195 LYS 195 241 ? ? ? A . n A 1 196 PRO 196 242 ? ? ? A . n A 1 197 SER 197 243 ? ? ? A . n A 1 198 LEU 198 244 ? ? ? A . n A 1 199 GLY 199 245 245 GLY GLY A . n A 1 200 SER 200 246 246 SER SER A . n A 1 201 GLY 201 247 247 GLY GLY A . n A 1 202 SER 202 248 248 SER SER A . n B 2 1 OCS 1 249 249 OCS OCS B . n B 2 2 SER 2 250 250 SER SER B . n B 2 3 ALA 3 251 251 ALA ALA B . n B 2 4 LEU 4 252 252 LEU LEU B . n B 2 5 ILE 5 253 253 ILE ILE B . n B 2 6 LYS 6 254 254 LYS LYS B . n B 2 7 LEU 7 255 255 LEU LEU B . n B 2 8 LEU 8 256 256 LEU LEU B . n B 2 9 PRO 9 257 257 PRO PRO B . n B 2 10 GLY 10 258 258 GLY GLY B . n B 2 11 GLY 11 259 259 GLY GLY B . n B 2 12 HIS 12 260 260 HIS HIS B . n B 2 13 ASP 13 261 261 ASP ASP B . n B 2 14 LEU 14 262 262 LEU LEU B . n B 2 15 LEU 15 263 263 LEU LEU B . n B 2 16 VAL 16 264 264 VAL VAL B . n B 2 17 ALA 17 265 265 ALA ALA B . n B 2 18 HIS 18 266 266 HIS HIS B . n B 2 19 ASN 19 267 267 ASN ASN B . n B 2 20 THR 20 268 268 THR THR B . n B 2 21 TRP 21 269 269 TRP TRP B . n B 2 22 ASN 22 270 270 ASN ASN B . n B 2 23 SER 23 271 271 SER SER B . n B 2 24 TYR 24 272 272 TYR TYR B . n B 2 25 GLN 25 273 273 GLN GLN B . n B 2 26 ASN 26 274 274 ASN ASN B . n B 2 27 MET 27 275 275 MET MET B . n B 2 28 LEU 28 276 276 LEU LEU B . n B 2 29 ARG 29 277 277 ARG ARG B . n B 2 30 ILE 30 278 278 ILE ILE B . n B 2 31 ILE 31 279 279 ILE ILE B . n B 2 32 LYS 32 280 280 LYS LYS B . n B 2 33 LYS 33 281 281 LYS LYS B . n B 2 34 TYR 34 282 282 TYR TYR B . n B 2 35 ARG 35 283 283 ARG ARG B . n B 2 36 LEU 36 284 284 LEU LEU B . n B 2 37 GLN 37 285 285 GLN GLN B . n B 2 38 PHE 38 286 286 PHE PHE B . n B 2 39 ARG 39 287 287 ARG ARG B . n B 2 40 GLU 40 288 288 GLU GLU B . n B 2 41 GLY 41 289 289 GLY GLY B . n B 2 42 PRO 42 290 290 PRO PRO B . n B 2 43 GLN 43 291 291 GLN GLN B . n B 2 44 GLU 44 292 292 GLU GLU B . n B 2 45 GLU 45 293 293 GLU GLU B . n B 2 46 TYR 46 294 294 TYR TYR B . n B 2 47 PRO 47 295 295 PRO PRO B . n B 2 48 LEU 48 296 296 LEU LEU B . n B 2 49 VAL 49 297 297 VAL VAL B . n B 2 50 ALA 50 298 298 ALA ALA B . n B 2 51 GLY 51 299 299 GLY GLY B . n B 2 52 ASN 52 300 300 ASN ASN B . n B 2 53 ASN 53 301 301 ASN ASN B . n B 2 54 LEU 54 302 302 LEU LEU B . n B 2 55 VAL 55 303 303 VAL VAL B . n B 2 56 PHE 56 304 304 PHE PHE B . n B 2 57 SER 57 305 305 SER SER B . n B 2 58 SER 58 306 306 SER SER B . n B 2 59 TYR 59 307 307 TYR TYR B . n B 2 60 PRO 60 308 308 PRO PRO B . n B 2 61 GLY 61 309 309 GLY GLY B . n B 2 62 THR 62 310 310 THR THR B . n B 2 63 ILE 63 311 311 ILE ILE B . n B 2 64 PHE 64 312 312 PHE PHE B . n B 2 65 SER 65 313 313 SER SER B . n B 2 66 GLY 66 314 314 GLY GLY B . n B 2 67 ASP 67 315 315 ASP ASP B . n B 2 68 ASP 68 316 316 ASP ASP B . n B 2 69 PHE 69 317 317 PHE PHE B . n B 2 70 TYR 70 318 318 TYR TYR B . n B 2 71 ILE 71 319 319 ILE ILE B . n B 2 72 LEU 72 320 320 LEU LEU B . n B 2 73 GLY 73 321 321 GLY GLY B . n B 2 74 SER 74 322 322 SER SER B . n B 2 75 GLY 75 323 323 GLY GLY B . n B 2 76 LEU 76 324 324 LEU LEU B . n B 2 77 VAL 77 325 325 VAL VAL B . n B 2 78 THR 78 326 326 THR THR B . n B 2 79 LEU 79 327 327 LEU LEU B . n B 2 80 GLU 80 328 328 GLU GLU B . n B 2 81 THR 81 329 329 THR THR B . n B 2 82 THR 82 330 330 THR THR B . n B 2 83 ILE 83 331 331 ILE ILE B . n B 2 84 GLY 84 332 332 GLY GLY B . n B 2 85 ASN 85 333 333 ASN ASN B . n B 2 86 LYS 86 334 334 LYS LYS B . n B 2 87 ASN 87 335 335 ASN ASN B . n B 2 88 PRO 88 336 336 PRO PRO B . n B 2 89 ALA 89 337 337 ALA ALA B . n B 2 90 LEU 90 338 338 LEU LEU B . n B 2 91 TRP 91 339 339 TRP TRP B . n B 2 92 LYS 92 340 340 LYS LYS B . n B 2 93 TYR 93 341 341 TYR TYR B . n B 2 94 VAL 94 342 342 VAL VAL B . n B 2 95 GLN 95 343 343 GLN GLN B . n B 2 96 PRO 96 344 344 PRO PRO B . n B 2 97 GLN 97 345 345 GLN GLN B . n B 2 98 GLY 98 346 346 GLY GLY B . n B 2 99 CYS 99 347 347 CYS CYS B . n B 2 100 VAL 100 348 348 VAL VAL B . n B 2 101 LEU 101 349 349 LEU LEU B . n B 2 102 GLU 102 350 350 GLU GLU B . n B 2 103 TRP 103 351 351 TRP TRP B . n B 2 104 ILE 104 352 352 ILE ILE B . n B 2 105 ARG 105 353 353 ARG ARG B . n B 2 106 ASN 106 354 354 ASN ASN B . n B 2 107 VAL 107 355 355 VAL VAL B . n B 2 108 VAL 108 356 356 VAL VAL B . n B 2 109 ALA 109 357 357 ALA ALA B . n B 2 110 ASN 110 358 358 ASN ASN B . n B 2 111 ARG 111 359 359 ARG ARG B . n B 2 112 LEU 112 360 360 LEU LEU B . n B 2 113 ALA 113 361 361 ALA ALA B . n B 2 114 LEU 114 362 362 LEU LEU B . n B 2 115 ASP 115 363 363 ASP ASP B . n B 2 116 GLY 116 364 364 GLY GLY B . n B 2 117 ALA 117 365 365 ALA ALA B . n B 2 118 THR 118 366 366 THR THR B . n B 2 119 TRP 119 367 367 TRP TRP B . n B 2 120 ALA 120 368 368 ALA ALA B . n B 2 121 ASP 121 369 369 ASP ASP B . n B 2 122 VAL 122 370 370 VAL VAL B . n B 2 123 PHE 123 371 371 PHE PHE B . n B 2 124 LYS 124 372 372 LYS LYS B . n B 2 125 ARG 125 373 373 ARG ARG B . n B 2 126 PHE 126 374 374 PHE PHE B . n B 2 127 ASN 127 375 375 ASN ASN B . n B 2 128 SER 128 376 376 SER SER B . n B 2 129 GLY 129 377 377 GLY GLY B . n B 2 130 THR 130 378 378 THR THR B . n B 2 131 TYR 131 379 379 TYR TYR B . n B 2 132 ASN 132 380 380 ASN ASN B . n B 2 133 ASN 133 381 381 ASN ASN B . n B 2 134 GLN 134 382 382 GLN GLN B . n B 2 135 TRP 135 383 383 TRP TRP B . n B 2 136 MET 136 384 384 MET MET B . n B 2 137 ILE 137 385 385 ILE ILE B . n B 2 138 VAL 138 386 386 VAL VAL B . n B 2 139 ASP 139 387 387 ASP ASP B . n B 2 140 TYR 140 388 388 TYR TYR B . n B 2 141 LYS 141 389 389 LYS LYS B . n B 2 142 ALA 142 390 390 ALA ALA B . n B 2 143 PHE 143 391 391 PHE PHE B . n B 2 144 LEU 144 392 392 LEU LEU B . n B 2 145 PRO 145 393 393 PRO PRO B . n B 2 146 ASN 146 394 394 ASN ASN B . n B 2 147 GLY 147 395 395 GLY GLY B . n B 2 148 PRO 148 396 396 PRO PRO B . n B 2 149 SER 149 397 397 SER SER B . n B 2 150 PRO 150 398 398 PRO PRO B . n B 2 151 GLY 151 399 399 GLY GLY B . n B 2 152 SER 152 400 400 SER SER B . n B 2 153 ARG 153 401 401 ARG ARG B . n B 2 154 VAL 154 402 402 VAL VAL B . n B 2 155 LEU 155 403 403 LEU LEU B . n B 2 156 THR 156 404 404 THR THR B . n B 2 157 ILE 157 405 405 ILE ILE B . n B 2 158 LEU 158 406 406 LEU LEU B . n B 2 159 GLU 159 407 407 GLU GLU B . n B 2 160 GLN 160 408 408 GLN GLN B . n B 2 161 ILE 161 409 409 ILE ILE B . n B 2 162 PRO 162 410 410 PRO PRO B . n B 2 163 GLY 163 411 411 GLY GLY B . n B 2 164 MET 164 412 412 MET MET B . n B 2 165 VAL 165 413 413 VAL VAL B . n B 2 166 VAL 166 414 414 VAL VAL B . n B 2 167 VAL 167 415 415 VAL VAL B . n B 2 168 ALA 168 416 416 ALA ALA B . n B 2 169 ASP 169 417 417 ASP ASP B . n B 2 170 LYS 170 418 418 LYS LYS B . n B 2 171 THR 171 419 419 THR THR B . n B 2 172 ALA 172 420 420 ALA ALA B . n B 2 173 GLU 173 421 421 GLU GLU B . n B 2 174 LEU 174 422 422 LEU LEU B . n B 2 175 TYR 175 423 423 TYR TYR B . n B 2 176 LYS 176 424 424 LYS LYS B . n B 2 177 THR 177 425 425 THR THR B . n B 2 178 THR 178 426 426 THR THR B . n B 2 179 TYR 179 427 427 TYR TYR B . n B 2 180 TRP 180 428 428 TRP TRP B . n B 2 181 ALA 181 429 429 ALA ALA B . n B 2 182 SER 182 430 430 SER SER B . n B 2 183 TYR 183 431 431 TYR TYR B . n B 2 184 ASN 184 432 432 ASN ASN B . n B 2 185 ILE 185 433 433 ILE ILE B . n B 2 186 PRO 186 434 434 PRO PRO B . n B 2 187 TYR 187 435 435 TYR TYR B . n B 2 188 PHE 188 436 436 PHE PHE B . n B 2 189 GLU 189 437 437 GLU GLU B . n B 2 190 THR 190 438 438 THR THR B . n B 2 191 VAL 191 439 439 VAL VAL B . n B 2 192 PHE 192 440 440 PHE PHE B . n B 2 193 ASN 193 441 441 ASN ASN B . n B 2 194 ALA 194 442 442 ALA ALA B . n B 2 195 SER 195 443 443 SER SER B . n B 2 196 GLY 196 444 444 GLY GLY B . n B 2 197 LEU 197 445 445 LEU LEU B . n B 2 198 GLN 198 446 446 GLN GLN B . n B 2 199 ALA 199 447 447 ALA ALA B . n B 2 200 LEU 200 448 448 LEU LEU B . n B 2 201 VAL 201 449 449 VAL VAL B . n B 2 202 ALA 202 450 450 ALA ALA B . n B 2 203 GLN 203 451 451 GLN GLN B . n B 2 204 TYR 204 452 452 TYR TYR B . n B 2 205 GLY 205 453 453 GLY GLY B . n B 2 206 ASP 206 454 454 ASP ASP B . n B 2 207 TRP 207 455 455 TRP TRP B . n B 2 208 PHE 208 456 456 PHE PHE B . n B 2 209 SER 209 457 457 SER SER B . n B 2 210 TYR 210 458 458 TYR TYR B . n B 2 211 THR 211 459 459 THR THR B . n B 2 212 LYS 212 460 460 LYS LYS B . n B 2 213 ASN 213 461 461 ASN ASN B . n B 2 214 PRO 214 462 462 PRO PRO B . n B 2 215 ARG 215 463 463 ARG ARG B . n B 2 216 ALA 216 464 464 ALA ALA B . n B 2 217 LYS 217 465 465 LYS LYS B . n B 2 218 ILE 218 466 466 ILE ILE B . n B 2 219 PHE 219 467 467 PHE PHE B . n B 2 220 GLN 220 468 468 GLN GLN B . n B 2 221 ARG 221 469 469 ARG ARG B . n B 2 222 ASP 222 470 470 ASP ASP B . n B 2 223 GLN 223 471 471 GLN GLN B . n B 2 224 SER 224 472 472 SER SER B . n B 2 225 LEU 225 473 473 LEU LEU B . n B 2 226 VAL 226 474 474 VAL VAL B . n B 2 227 GLU 227 475 475 GLU GLU B . n B 2 228 ASP 228 476 476 ASP ASP B . n B 2 229 MET 229 477 477 MET MET B . n B 2 230 ASP 230 478 478 ASP ASP B . n B 2 231 ALA 231 479 479 ALA ALA B . n B 2 232 MET 232 480 480 MET MET B . n B 2 233 VAL 233 481 481 VAL VAL B . n B 2 234 ARG 234 482 482 ARG ARG B . n B 2 235 LEU 235 483 483 LEU LEU B . n B 2 236 MET 236 484 484 MET MET B . n B 2 237 ARG 237 485 485 ARG ARG B . n B 2 238 TYR 238 486 486 TYR TYR B . n B 2 239 ASN 239 487 487 ASN ASN B . n B 2 240 ASP 240 488 488 ASP ASP B . n B 2 241 PHE 241 489 489 PHE PHE B . n B 2 242 LEU 242 490 490 LEU LEU B . n B 2 243 HIS 243 491 491 HIS HIS B . n B 2 244 ASP 244 492 492 ASP ASP B . n B 2 245 PRO 245 493 493 PRO PRO B . n B 2 246 LEU 246 494 494 LEU LEU B . n B 2 247 SER 247 495 495 SER SER B . n B 2 248 LEU 248 496 496 LEU LEU B . n B 2 249 CYS 249 497 497 CYS CYS B . n B 2 250 GLU 250 498 498 GLU GLU B . n B 2 251 ALA 251 499 499 ALA ALA B . n B 2 252 CYS 252 500 500 CYS CYS B . n B 2 253 ASN 253 501 501 ASN ASN B . n B 2 254 PRO 254 502 502 PRO PRO B . n B 2 255 LYS 255 503 503 LYS LYS B . n B 2 256 PRO 256 504 504 PRO PRO B . n B 2 257 ASN 257 505 505 ASN ASN B . n B 2 258 ALA 258 506 506 ALA ALA B . n B 2 259 GLU 259 507 507 GLU GLU B . n B 2 260 ASN 260 508 508 ASN ASN B . n B 2 261 ALA 261 509 509 ALA ALA B . n B 2 262 ILE 262 510 510 ILE ILE B . n B 2 263 SER 263 511 511 SER SER B . n B 2 264 ALA 264 512 512 ALA ALA B . n B 2 265 ARG 265 513 513 ARG ARG B . n B 2 266 SER 266 514 514 SER SER B . n B 2 267 ASP 267 515 515 ASP ASP B . n B 2 268 LEU 268 516 516 LEU LEU B . n B 2 269 ASN 269 517 517 ASN ASN B . n B 2 270 PRO 270 518 518 PRO PRO B . n B 2 271 ALA 271 519 519 ALA ALA B . n B 2 272 ASN 272 520 520 ASN ASN B . n B 2 273 GLY 273 521 521 GLY GLY B . n B 2 274 SER 274 522 522 SER SER B . n B 2 275 TYR 275 523 523 TYR TYR B . n B 2 276 PRO 276 524 524 PRO PRO B . n B 2 277 PHE 277 525 525 PHE PHE B . n B 2 278 GLN 278 526 526 GLN GLN B . n B 2 279 ALA 279 527 527 ALA ALA B . n B 2 280 LEU 280 528 528 LEU LEU B . n B 2 281 HIS 281 529 529 HIS HIS B . n B 2 282 GLN 282 530 530 GLN GLN B . n B 2 283 ARG 283 531 531 ARG ARG B . n B 2 284 ALA 284 532 532 ALA ALA B . n B 2 285 HIS 285 533 533 HIS HIS B . n B 2 286 GLY 286 534 534 GLY GLY B . n B 2 287 GLY 287 535 535 GLY GLY B . n B 2 288 ILE 288 536 536 ILE ILE B . n B 2 289 ASP 289 537 537 ASP ASP B . n B 2 290 VAL 290 538 538 VAL VAL B . n B 2 291 LYS 291 539 539 LYS LYS B . n B 2 292 VAL 292 540 540 VAL VAL B . n B 2 293 THR 293 541 541 THR THR B . n B 2 294 SER 294 542 542 SER SER B . n B 2 295 PHE 295 543 543 PHE PHE B . n B 2 296 THR 296 544 544 THR THR B . n B 2 297 LEU 297 545 545 LEU LEU B . n B 2 298 ALA 298 546 546 ALA ALA B . n B 2 299 LYS 299 547 547 LYS LYS B . n B 2 300 TYR 300 548 548 TYR TYR B . n B 2 301 MET 301 549 549 MET MET B . n B 2 302 SER 302 550 550 SER SER B . n B 2 303 MET 303 551 551 MET MET B . n B 2 304 LEU 304 552 552 LEU LEU B . n B 2 305 ALA 305 553 553 ALA ALA B . n B 2 306 ALA 306 554 554 ALA ALA B . n B 2 307 SER 307 555 555 SER SER B . n B 2 308 GLY 308 556 556 GLY GLY B . n B 2 309 PRO 309 557 557 PRO PRO B . n B 2 310 THR 310 558 558 THR THR B . n B 2 311 TRP 311 559 559 TRP TRP B . n B 2 312 ASP 312 560 560 ASP ASP B . n B 2 313 GLN 313 561 561 GLN GLN B . n B 2 314 CYS 314 562 562 CYS CYS B . n B 2 315 PRO 315 563 563 PRO PRO B . n B 2 316 PRO 316 564 564 PRO PRO B . n B 2 317 PHE 317 565 565 PHE PHE B . n B 2 318 GLN 318 566 566 GLN GLN B . n B 2 319 TRP 319 567 567 TRP TRP B . n B 2 320 SER 320 568 568 SER SER B . n B 2 321 LYS 321 569 569 LYS LYS B . n B 2 322 SER 322 570 570 SER SER B . n B 2 323 PRO 323 571 571 PRO PRO B . n B 2 324 PHE 324 572 572 PHE PHE B . n B 2 325 HIS 325 573 573 HIS HIS B . n B 2 326 SER 326 574 574 SER SER B . n B 2 327 MET 327 575 575 MET MET B . n B 2 328 LEU 328 576 576 LEU LEU B . n B 2 329 HIS 329 577 577 HIS HIS B . n B 2 330 MET 330 578 578 MET MET B . n B 2 331 GLY 331 579 579 GLY GLY B . n B 2 332 GLN 332 580 580 GLN GLN B . n B 2 333 PRO 333 581 581 PRO PRO B . n B 2 334 ASP 334 582 582 ASP ASP B . n B 2 335 LEU 335 583 583 LEU LEU B . n B 2 336 TRP 336 584 584 TRP TRP B . n B 2 337 MET 337 585 585 MET MET B . n B 2 338 PHE 338 586 586 PHE PHE B . n B 2 339 SER 339 587 587 SER SER B . n B 2 340 PRO 340 588 588 PRO PRO B . n B 2 341 ILE 341 589 589 ILE ILE B . n B 2 342 ARG 342 590 590 ARG ARG B . n B 2 343 VAL 343 591 591 VAL VAL B . n B 2 344 PRO 344 592 592 PRO PRO B . n B 2 345 TRP 345 593 ? ? ? B . n B 2 346 ASP 346 594 ? ? ? B . n B 2 347 GLY 347 595 ? ? ? B . n B 2 348 ARG 348 596 ? ? ? B . n B 2 349 GLY 349 597 ? ? ? B . n B 2 350 SER 350 598 ? ? ? B . n B 2 351 HIS 351 599 ? ? ? B . n B 2 352 HIS 352 600 ? ? ? B . n B 2 353 HIS 353 601 ? ? ? B . n B 2 354 HIS 354 602 ? ? ? B . n B 2 355 HIS 355 603 ? ? ? B . n B 2 356 HIS 356 604 ? ? ? B . n B 2 357 GLY 357 605 ? ? ? 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 11 11 NAG NAG A . D 3 NAG 2 12 12 NAG NAG A . E 3 NAG 1 21 21 NAG NAG A . F 3 NAG 1 1 1 NAG NAG A . G 4 GOL 1 9 9 GOL GOL A . H 4 GOL 1 10 10 GOL GOL A . I 5 ACT 1 22 22 ACT ACT A . J 4 GOL 1 3 3 GOL GOL A . K 3 NAG 1 31 31 NAG NAG B . L 3 NAG 2 32 32 NAG NAG B . M 3 NAG 1 41 41 NAG NAG B . N 4 GOL 1 11 11 GOL GOL B . O 4 GOL 1 1 1 GOL GOL B . P 4 GOL 1 2 2 GOL GOL B . Q 4 GOL 1 4 4 GOL GOL B . R 4 GOL 1 5 5 GOL GOL B . S 4 GOL 1 6 6 GOL GOL B . T 4 GOL 1 7 7 GOL GOL B . U 4 GOL 1 8 8 GOL GOL B . V 5 ACT 1 21 21 ACT ACT B . W 6 XE 1 606 606 XE XE B . X 7 NA 1 607 607 NA NA B . Y 8 HOH 1 8 8 HOH HOH A . Y 8 HOH 2 13 13 HOH HOH A . Y 8 HOH 3 19 19 HOH HOH A . Y 8 HOH 4 25 25 HOH HOH A . Y 8 HOH 5 27 27 HOH HOH A . Y 8 HOH 6 28 28 HOH HOH A . Y 8 HOH 7 34 34 HOH HOH A . Y 8 HOH 8 37 37 HOH HOH A . Y 8 HOH 9 38 38 HOH HOH A . Y 8 HOH 10 39 39 HOH HOH A . Y 8 HOH 11 40 40 HOH HOH A . Y 8 HOH 12 42 42 HOH HOH A . Y 8 HOH 13 44 44 HOH HOH A . Y 8 HOH 14 45 45 HOH HOH A . Y 8 HOH 15 249 249 HOH HOH A . Y 8 HOH 16 250 250 HOH HOH A . Y 8 HOH 17 251 251 HOH HOH A . Y 8 HOH 18 252 252 HOH HOH A . Y 8 HOH 19 253 253 HOH HOH A . Y 8 HOH 20 254 254 HOH HOH A . Y 8 HOH 21 255 255 HOH HOH A . Y 8 HOH 22 256 256 HOH HOH A . Y 8 HOH 23 257 257 HOH HOH A . Y 8 HOH 24 258 258 HOH HOH A . Y 8 HOH 25 259 259 HOH HOH A . Y 8 HOH 26 260 260 HOH HOH A . Y 8 HOH 27 261 261 HOH HOH A . Y 8 HOH 28 262 262 HOH HOH A . Y 8 HOH 29 263 263 HOH HOH A . Y 8 HOH 30 264 264 HOH HOH A . Y 8 HOH 31 265 265 HOH HOH A . Y 8 HOH 32 266 266 HOH HOH A . Y 8 HOH 33 267 267 HOH HOH A . Y 8 HOH 34 268 268 HOH HOH A . Y 8 HOH 35 269 269 HOH HOH A . Y 8 HOH 36 270 270 HOH HOH A . Y 8 HOH 37 271 271 HOH HOH A . Y 8 HOH 38 272 272 HOH HOH A . Y 8 HOH 39 273 273 HOH HOH A . Y 8 HOH 40 274 274 HOH HOH A . Y 8 HOH 41 275 275 HOH HOH A . Y 8 HOH 42 276 276 HOH HOH A . Y 8 HOH 43 277 277 HOH HOH A . Y 8 HOH 44 278 278 HOH HOH A . Y 8 HOH 45 279 279 HOH HOH A . Y 8 HOH 46 280 280 HOH HOH A . Y 8 HOH 47 281 281 HOH HOH A . Y 8 HOH 48 282 282 HOH HOH A . Y 8 HOH 49 283 283 HOH HOH A . Y 8 HOH 50 284 284 HOH HOH A . Y 8 HOH 51 285 285 HOH HOH A . Y 8 HOH 52 286 286 HOH HOH A . Y 8 HOH 53 287 287 HOH HOH A . Y 8 HOH 54 288 288 HOH HOH A . Y 8 HOH 55 290 290 HOH HOH A . Y 8 HOH 56 291 291 HOH HOH A . Y 8 HOH 57 292 292 HOH HOH A . Y 8 HOH 58 293 293 HOH HOH A . Y 8 HOH 59 294 294 HOH HOH A . Y 8 HOH 60 295 295 HOH HOH A . Y 8 HOH 61 297 297 HOH HOH A . Y 8 HOH 62 298 298 HOH HOH A . Y 8 HOH 63 299 299 HOH HOH A . Y 8 HOH 64 300 300 HOH HOH A . Y 8 HOH 65 301 301 HOH HOH A . Y 8 HOH 66 303 303 HOH HOH A . Y 8 HOH 67 306 306 HOH HOH A . Y 8 HOH 68 311 311 HOH HOH A . Y 8 HOH 69 312 312 HOH HOH A . Y 8 HOH 70 313 313 HOH HOH A . Y 8 HOH 71 320 320 HOH HOH A . Y 8 HOH 72 322 322 HOH HOH A . Y 8 HOH 73 323 323 HOH HOH A . Y 8 HOH 74 324 324 HOH HOH A . Y 8 HOH 75 330 330 HOH HOH A . Y 8 HOH 76 333 333 HOH HOH A . Y 8 HOH 77 346 346 HOH HOH A . Y 8 HOH 78 352 352 HOH HOH A . Y 8 HOH 79 354 354 HOH HOH A . Y 8 HOH 80 364 364 HOH HOH A . Y 8 HOH 81 367 367 HOH HOH A . Y 8 HOH 82 368 368 HOH HOH A . Y 8 HOH 83 371 371 HOH HOH A . Y 8 HOH 84 374 374 HOH HOH A . Y 8 HOH 85 381 381 HOH HOH A . Y 8 HOH 86 383 383 HOH HOH A . Y 8 HOH 87 388 388 HOH HOH A . Y 8 HOH 88 393 393 HOH HOH A . Y 8 HOH 89 395 395 HOH HOH A . Y 8 HOH 90 407 407 HOH HOH A . Y 8 HOH 91 438 438 HOH HOH A . Y 8 HOH 92 439 439 HOH HOH A . Y 8 HOH 93 444 444 HOH HOH A . Y 8 HOH 94 458 458 HOH HOH A . Y 8 HOH 95 462 462 HOH HOH A . Y 8 HOH 96 463 463 HOH HOH A . Y 8 HOH 97 465 465 HOH HOH A . Y 8 HOH 98 469 469 HOH HOH A . Y 8 HOH 99 471 471 HOH HOH A . Y 8 HOH 100 472 472 HOH HOH A . Y 8 HOH 101 483 483 HOH HOH A . Y 8 HOH 102 484 484 HOH HOH A . Y 8 HOH 103 485 485 HOH HOH A . Y 8 HOH 104 499 499 HOH HOH A . Y 8 HOH 105 505 505 HOH HOH A . Y 8 HOH 106 506 506 HOH HOH A . Y 8 HOH 107 508 508 HOH HOH A . Y 8 HOH 108 510 510 HOH HOH A . Y 8 HOH 109 522 522 HOH HOH A . Y 8 HOH 110 534 534 HOH HOH A . Y 8 HOH 111 538 538 HOH HOH A . Y 8 HOH 112 539 539 HOH HOH A . Y 8 HOH 113 540 540 HOH HOH A . Y 8 HOH 114 542 542 HOH HOH A . Y 8 HOH 115 543 543 HOH HOH A . Y 8 HOH 116 558 558 HOH HOH A . Y 8 HOH 117 566 566 HOH HOH A . Y 8 HOH 118 582 582 HOH HOH A . Y 8 HOH 119 583 583 HOH HOH A . Y 8 HOH 120 584 584 HOH HOH A . Y 8 HOH 121 585 585 HOH HOH A . Y 8 HOH 122 587 587 HOH HOH A . Y 8 HOH 123 588 588 HOH HOH A . Y 8 HOH 124 593 593 HOH HOH A . Y 8 HOH 125 594 594 HOH HOH A . Y 8 HOH 126 595 595 HOH HOH A . Y 8 HOH 127 596 596 HOH HOH A . Y 8 HOH 128 599 599 HOH HOH A . Y 8 HOH 129 600 600 HOH HOH A . Y 8 HOH 130 601 601 HOH HOH A . Y 8 HOH 131 602 602 HOH HOH A . Y 8 HOH 132 603 603 HOH HOH A . Y 8 HOH 133 605 605 HOH HOH A . Y 8 HOH 134 606 606 HOH HOH A . Y 8 HOH 135 616 616 HOH HOH A . Y 8 HOH 136 617 617 HOH HOH A . Y 8 HOH 137 620 620 HOH HOH A . Y 8 HOH 138 649 649 HOH HOH A . Y 8 HOH 139 656 656 HOH HOH A . Y 8 HOH 140 657 657 HOH HOH A . Y 8 HOH 141 659 659 HOH HOH A . Y 8 HOH 142 660 660 HOH HOH A . Y 8 HOH 143 669 669 HOH HOH A . Y 8 HOH 144 670 670 HOH HOH A . Y 8 HOH 145 675 675 HOH HOH A . Y 8 HOH 146 690 690 HOH HOH A . Y 8 HOH 147 692 692 HOH HOH A . Y 8 HOH 148 698 698 HOH HOH A . Y 8 HOH 149 707 707 HOH HOH A . Y 8 HOH 150 710 710 HOH HOH A . Y 8 HOH 151 711 711 HOH HOH A . Y 8 HOH 152 712 712 HOH HOH A . Y 8 HOH 153 713 713 HOH HOH A . Y 8 HOH 154 715 715 HOH HOH A . Y 8 HOH 155 716 716 HOH HOH A . Y 8 HOH 156 720 720 HOH HOH A . Y 8 HOH 157 725 725 HOH HOH A . Y 8 HOH 158 728 728 HOH HOH A . Y 8 HOH 159 732 732 HOH HOH A . Y 8 HOH 160 756 756 HOH HOH A . Y 8 HOH 161 757 757 HOH HOH A . Y 8 HOH 162 758 758 HOH HOH A . Y 8 HOH 163 759 759 HOH HOH A . Z 8 HOH 1 3 3 HOH HOH B . Z 8 HOH 2 9 9 HOH HOH B . Z 8 HOH 3 10 10 HOH HOH B . Z 8 HOH 4 12 12 HOH HOH B . Z 8 HOH 5 14 14 HOH HOH B . Z 8 HOH 6 15 15 HOH HOH B . Z 8 HOH 7 16 16 HOH HOH B . Z 8 HOH 8 18 18 HOH HOH B . Z 8 HOH 9 20 20 HOH HOH B . Z 8 HOH 10 23 23 HOH HOH B . Z 8 HOH 11 26 26 HOH HOH B . Z 8 HOH 12 29 29 HOH HOH B . Z 8 HOH 13 30 30 HOH HOH B . Z 8 HOH 14 33 33 HOH HOH B . Z 8 HOH 15 35 35 HOH HOH B . Z 8 HOH 16 36 36 HOH HOH B . Z 8 HOH 17 43 43 HOH HOH B . Z 8 HOH 18 46 46 HOH HOH B . Z 8 HOH 19 47 47 HOH HOH B . Z 8 HOH 20 48 48 HOH HOH B . Z 8 HOH 21 49 49 HOH HOH B . Z 8 HOH 22 50 50 HOH HOH B . Z 8 HOH 23 53 53 HOH HOH B . Z 8 HOH 24 55 55 HOH HOH B . Z 8 HOH 25 56 56 HOH HOH B . Z 8 HOH 26 57 57 HOH HOH B . Z 8 HOH 27 58 58 HOH HOH B . Z 8 HOH 28 59 59 HOH HOH B . Z 8 HOH 29 60 60 HOH HOH B . Z 8 HOH 30 61 61 HOH HOH B . Z 8 HOH 31 62 62 HOH HOH B . Z 8 HOH 32 64 64 HOH HOH B . Z 8 HOH 33 65 65 HOH HOH B . Z 8 HOH 34 66 66 HOH HOH B . Z 8 HOH 35 67 67 HOH HOH B . Z 8 HOH 36 68 68 HOH HOH B . Z 8 HOH 37 70 70 HOH HOH B . Z 8 HOH 38 71 71 HOH HOH B . Z 8 HOH 39 72 72 HOH HOH B . Z 8 HOH 40 73 73 HOH HOH B . Z 8 HOH 41 76 76 HOH HOH B . Z 8 HOH 42 77 77 HOH HOH B . Z 8 HOH 43 79 79 HOH HOH B . Z 8 HOH 44 80 80 HOH HOH B . Z 8 HOH 45 82 82 HOH HOH B . Z 8 HOH 46 83 83 HOH HOH B . Z 8 HOH 47 84 84 HOH HOH B . Z 8 HOH 48 85 85 HOH HOH B . Z 8 HOH 49 86 86 HOH HOH B . Z 8 HOH 50 90 90 HOH HOH B . Z 8 HOH 51 91 91 HOH HOH B . Z 8 HOH 52 92 92 HOH HOH B . Z 8 HOH 53 93 93 HOH HOH B . Z 8 HOH 54 95 95 HOH HOH B . Z 8 HOH 55 96 96 HOH HOH B . Z 8 HOH 56 100 100 HOH HOH B . Z 8 HOH 57 102 102 HOH HOH B . Z 8 HOH 58 103 103 HOH HOH B . Z 8 HOH 59 104 104 HOH HOH B . Z 8 HOH 60 105 105 HOH HOH B . Z 8 HOH 61 107 107 HOH HOH B . Z 8 HOH 62 108 108 HOH HOH B . Z 8 HOH 63 109 109 HOH HOH B . Z 8 HOH 64 110 110 HOH HOH B . Z 8 HOH 65 112 112 HOH HOH B . Z 8 HOH 66 113 113 HOH HOH B . Z 8 HOH 67 114 114 HOH HOH B . Z 8 HOH 68 115 115 HOH HOH B . Z 8 HOH 69 116 116 HOH HOH B . Z 8 HOH 70 118 118 HOH HOH B . Z 8 HOH 71 119 119 HOH HOH B . Z 8 HOH 72 120 120 HOH HOH B . Z 8 HOH 73 122 122 HOH HOH B . Z 8 HOH 74 123 123 HOH HOH B . Z 8 HOH 75 124 124 HOH HOH B . Z 8 HOH 76 125 125 HOH HOH B . Z 8 HOH 77 127 127 HOH HOH B . Z 8 HOH 78 128 128 HOH HOH B . Z 8 HOH 79 130 130 HOH HOH B . Z 8 HOH 80 132 132 HOH HOH B . Z 8 HOH 81 133 133 HOH HOH B . Z 8 HOH 82 135 135 HOH HOH B . Z 8 HOH 83 136 136 HOH HOH B . Z 8 HOH 84 139 139 HOH HOH B . Z 8 HOH 85 140 140 HOH HOH B . Z 8 HOH 86 141 141 HOH HOH B . Z 8 HOH 87 142 142 HOH HOH B . Z 8 HOH 88 144 144 HOH HOH B . Z 8 HOH 89 146 146 HOH HOH B . Z 8 HOH 90 148 148 HOH HOH B . Z 8 HOH 91 149 149 HOH HOH B . Z 8 HOH 92 150 150 HOH HOH B . Z 8 HOH 93 153 153 HOH HOH B . Z 8 HOH 94 155 155 HOH HOH B . Z 8 HOH 95 156 156 HOH HOH B . Z 8 HOH 96 157 157 HOH HOH B . Z 8 HOH 97 158 158 HOH HOH B . Z 8 HOH 98 159 159 HOH HOH B . Z 8 HOH 99 163 163 HOH HOH B . Z 8 HOH 100 164 164 HOH HOH B . Z 8 HOH 101 165 165 HOH HOH B . Z 8 HOH 102 167 167 HOH HOH B . Z 8 HOH 103 168 168 HOH HOH B . Z 8 HOH 104 169 169 HOH HOH B . Z 8 HOH 105 170 170 HOH HOH B . Z 8 HOH 106 172 172 HOH HOH B . Z 8 HOH 107 174 174 HOH HOH B . Z 8 HOH 108 177 177 HOH HOH B . Z 8 HOH 109 180 180 HOH HOH B . Z 8 HOH 110 181 181 HOH HOH B . Z 8 HOH 111 184 184 HOH HOH B . Z 8 HOH 112 185 185 HOH HOH B . Z 8 HOH 113 186 186 HOH HOH B . Z 8 HOH 114 187 187 HOH HOH B . Z 8 HOH 115 189 189 HOH HOH B . Z 8 HOH 116 193 193 HOH HOH B . Z 8 HOH 117 195 195 HOH HOH B . Z 8 HOH 118 196 196 HOH HOH B . Z 8 HOH 119 199 199 HOH HOH B . Z 8 HOH 120 200 200 HOH HOH B . Z 8 HOH 121 201 201 HOH HOH B . Z 8 HOH 122 203 203 HOH HOH B . Z 8 HOH 123 204 204 HOH HOH B . Z 8 HOH 124 206 206 HOH HOH B . Z 8 HOH 125 207 207 HOH HOH B . Z 8 HOH 126 214 214 HOH HOH B . Z 8 HOH 127 216 216 HOH HOH B . Z 8 HOH 128 217 217 HOH HOH B . Z 8 HOH 129 218 218 HOH HOH B . Z 8 HOH 130 221 221 HOH HOH B . Z 8 HOH 131 222 222 HOH HOH B . Z 8 HOH 132 224 224 HOH HOH B . Z 8 HOH 133 225 225 HOH HOH B . Z 8 HOH 134 229 229 HOH HOH B . Z 8 HOH 135 230 230 HOH HOH B . Z 8 HOH 136 232 232 HOH HOH B . Z 8 HOH 137 233 233 HOH HOH B . Z 8 HOH 138 234 234 HOH HOH B . Z 8 HOH 139 235 235 HOH HOH B . Z 8 HOH 140 236 236 HOH HOH B . Z 8 HOH 141 237 237 HOH HOH B . Z 8 HOH 142 239 239 HOH HOH B . Z 8 HOH 143 241 241 HOH HOH B . Z 8 HOH 144 243 243 HOH HOH B . Z 8 HOH 145 244 244 HOH HOH B . Z 8 HOH 146 246 246 HOH HOH B . Z 8 HOH 147 608 608 HOH HOH B . Z 8 HOH 148 609 609 HOH HOH B . Z 8 HOH 149 610 610 HOH HOH B . Z 8 HOH 150 611 611 HOH HOH B . Z 8 HOH 151 612 612 HOH HOH B . Z 8 HOH 152 613 613 HOH HOH B . Z 8 HOH 153 614 614 HOH HOH B . Z 8 HOH 154 615 615 HOH HOH B . Z 8 HOH 155 616 616 HOH HOH B . Z 8 HOH 156 617 617 HOH HOH B . Z 8 HOH 157 618 618 HOH HOH B . Z 8 HOH 158 619 619 HOH HOH B . Z 8 HOH 159 620 620 HOH HOH B . Z 8 HOH 160 621 621 HOH HOH B . Z 8 HOH 161 622 622 HOH HOH B . Z 8 HOH 162 623 623 HOH HOH B . Z 8 HOH 163 624 624 HOH HOH B . Z 8 HOH 164 625 625 HOH HOH B . Z 8 HOH 165 626 626 HOH HOH B . Z 8 HOH 166 627 627 HOH HOH B . Z 8 HOH 167 628 628 HOH HOH B . Z 8 HOH 168 629 629 HOH HOH B . Z 8 HOH 169 630 630 HOH HOH B . Z 8 HOH 170 631 631 HOH HOH B . Z 8 HOH 171 632 632 HOH HOH B . Z 8 HOH 172 633 633 HOH HOH B . Z 8 HOH 173 634 634 HOH HOH B . Z 8 HOH 174 635 635 HOH HOH B . Z 8 HOH 175 636 636 HOH HOH B . Z 8 HOH 176 637 637 HOH HOH B . Z 8 HOH 177 638 638 HOH HOH B . Z 8 HOH 178 639 639 HOH HOH B . Z 8 HOH 179 640 640 HOH HOH B . Z 8 HOH 180 641 641 HOH HOH B . Z 8 HOH 181 642 642 HOH HOH B . Z 8 HOH 182 643 643 HOH HOH B . Z 8 HOH 183 644 644 HOH HOH B . Z 8 HOH 184 645 645 HOH HOH B . Z 8 HOH 185 646 646 HOH HOH B . Z 8 HOH 186 647 647 HOH HOH B . Z 8 HOH 187 648 648 HOH HOH B . Z 8 HOH 188 649 649 HOH HOH B . Z 8 HOH 189 650 650 HOH HOH B . Z 8 HOH 190 651 651 HOH HOH B . Z 8 HOH 191 652 652 HOH HOH B . Z 8 HOH 192 653 653 HOH HOH B . Z 8 HOH 193 654 654 HOH HOH B . Z 8 HOH 194 655 655 HOH HOH B . Z 8 HOH 195 656 656 HOH HOH B . Z 8 HOH 196 657 657 HOH HOH B . Z 8 HOH 197 658 658 HOH HOH B . Z 8 HOH 198 659 659 HOH HOH B . Z 8 HOH 199 660 660 HOH HOH B . Z 8 HOH 200 661 661 HOH HOH B . Z 8 HOH 201 662 662 HOH HOH B . Z 8 HOH 202 663 663 HOH HOH B . Z 8 HOH 203 664 664 HOH HOH B . Z 8 HOH 204 665 665 HOH HOH B . Z 8 HOH 205 666 666 HOH HOH B . Z 8 HOH 206 667 667 HOH HOH B . Z 8 HOH 207 668 668 HOH HOH B . Z 8 HOH 208 669 669 HOH HOH B . Z 8 HOH 209 670 670 HOH HOH B . Z 8 HOH 210 671 671 HOH HOH B . Z 8 HOH 211 672 672 HOH HOH B . Z 8 HOH 212 673 673 HOH HOH B . Z 8 HOH 213 674 674 HOH HOH B . Z 8 HOH 214 675 675 HOH HOH B . Z 8 HOH 215 676 676 HOH HOH B . Z 8 HOH 216 677 677 HOH HOH B . Z 8 HOH 217 678 678 HOH HOH B . Z 8 HOH 218 679 679 HOH HOH B . Z 8 HOH 219 680 680 HOH HOH B . Z 8 HOH 220 681 681 HOH HOH B . Z 8 HOH 221 682 682 HOH HOH B . Z 8 HOH 222 683 683 HOH HOH B . Z 8 HOH 223 684 684 HOH HOH B . Z 8 HOH 224 685 685 HOH HOH B . Z 8 HOH 225 686 686 HOH HOH B . Z 8 HOH 226 687 687 HOH HOH B . Z 8 HOH 227 688 688 HOH HOH B . Z 8 HOH 228 689 689 HOH HOH B . Z 8 HOH 229 690 690 HOH HOH B . Z 8 HOH 230 691 691 HOH HOH B . Z 8 HOH 231 692 692 HOH HOH B . Z 8 HOH 232 693 693 HOH HOH B . Z 8 HOH 233 694 694 HOH HOH B . Z 8 HOH 234 695 695 HOH HOH B . Z 8 HOH 235 696 696 HOH HOH B . Z 8 HOH 236 697 697 HOH HOH B . Z 8 HOH 237 698 698 HOH HOH B . Z 8 HOH 238 699 699 HOH HOH B . Z 8 HOH 239 700 700 HOH HOH B . Z 8 HOH 240 701 701 HOH HOH B . Z 8 HOH 241 702 702 HOH HOH B . Z 8 HOH 242 703 703 HOH HOH B . Z 8 HOH 243 704 704 HOH HOH B . Z 8 HOH 244 705 705 HOH HOH B . Z 8 HOH 245 706 706 HOH HOH B . Z 8 HOH 246 707 707 HOH HOH B . Z 8 HOH 247 708 708 HOH HOH B . Z 8 HOH 248 709 709 HOH HOH B . Z 8 HOH 249 710 710 HOH HOH B . Z 8 HOH 250 711 711 HOH HOH B . Z 8 HOH 251 712 712 HOH HOH B . Z 8 HOH 252 713 713 HOH HOH B . Z 8 HOH 253 714 714 HOH HOH B . Z 8 HOH 254 715 715 HOH HOH B . Z 8 HOH 255 716 716 HOH HOH B . Z 8 HOH 256 717 717 HOH HOH B . Z 8 HOH 257 718 718 HOH HOH B . Z 8 HOH 258 719 719 HOH HOH B . Z 8 HOH 259 720 720 HOH HOH B . Z 8 HOH 260 721 721 HOH HOH B . Z 8 HOH 261 722 722 HOH HOH B . Z 8 HOH 262 723 723 HOH HOH B . Z 8 HOH 263 724 724 HOH HOH B . Z 8 HOH 264 725 725 HOH HOH B . Z 8 HOH 265 726 726 HOH HOH B . Z 8 HOH 266 727 727 HOH HOH B . Z 8 HOH 267 728 728 HOH HOH B . Z 8 HOH 268 729 729 HOH HOH B . Z 8 HOH 269 730 730 HOH HOH B . Z 8 HOH 270 731 731 HOH HOH B . Z 8 HOH 271 732 732 HOH HOH B . Z 8 HOH 272 733 733 HOH HOH B . Z 8 HOH 273 734 734 HOH HOH B . Z 8 HOH 274 735 735 HOH HOH B . Z 8 HOH 275 736 736 HOH HOH B . Z 8 HOH 276 737 737 HOH HOH B . Z 8 HOH 277 738 738 HOH HOH B . Z 8 HOH 278 739 739 HOH HOH B . Z 8 HOH 279 740 740 HOH HOH B . Z 8 HOH 280 741 741 HOH HOH B . Z 8 HOH 281 742 742 HOH HOH B . Z 8 HOH 282 743 743 HOH HOH B . Z 8 HOH 283 744 744 HOH HOH B . Z 8 HOH 284 745 745 HOH HOH B . Z 8 HOH 285 746 746 HOH HOH B . Z 8 HOH 286 747 747 HOH HOH B . Z 8 HOH 287 748 748 HOH HOH B . Z 8 HOH 288 749 749 HOH HOH B . Z 8 HOH 289 750 750 HOH HOH B . Z 8 HOH 290 751 751 HOH HOH B . Z 8 HOH 291 752 752 HOH HOH B . Z 8 HOH 292 753 753 HOH HOH B . Z 8 HOH 293 754 754 HOH HOH B . Z 8 HOH 294 755 755 HOH HOH B . Z 8 HOH 295 756 756 HOH HOH B . Z 8 HOH 296 757 757 HOH HOH B . Z 8 HOH 297 758 758 HOH HOH B . Z 8 HOH 298 759 759 HOH HOH B . Z 8 HOH 299 760 760 HOH HOH B . Z 8 HOH 300 761 761 HOH HOH B . Z 8 HOH 301 762 762 HOH HOH B . Z 8 HOH 302 763 763 HOH HOH B . Z 8 HOH 303 764 764 HOH HOH B . Z 8 HOH 304 765 765 HOH HOH B . Z 8 HOH 305 766 766 HOH HOH B . Z 8 HOH 306 767 767 HOH HOH B . Z 8 HOH 307 768 768 HOH HOH B . Z 8 HOH 308 769 769 HOH HOH B . Z 8 HOH 309 770 770 HOH HOH B . Z 8 HOH 310 771 771 HOH HOH B . Z 8 HOH 311 772 772 HOH HOH B . Z 8 HOH 312 773 773 HOH HOH B . Z 8 HOH 313 774 774 HOH HOH B . Z 8 HOH 314 775 775 HOH HOH B . Z 8 HOH 315 776 776 HOH HOH B . Z 8 HOH 316 777 777 HOH HOH B . Z 8 HOH 317 778 778 HOH HOH B . Z 8 HOH 318 779 779 HOH HOH B . Z 8 HOH 319 780 780 HOH HOH B . Z 8 HOH 320 781 781 HOH HOH B . Z 8 HOH 321 782 782 HOH HOH B . Z 8 HOH 322 783 783 HOH HOH B . Z 8 HOH 323 784 784 HOH HOH B . Z 8 HOH 324 785 785 HOH HOH B . Z 8 HOH 325 786 786 HOH HOH B . Z 8 HOH 326 787 787 HOH HOH B . Z 8 HOH 327 788 788 HOH HOH B . Z 8 HOH 328 789 789 HOH HOH B . Z 8 HOH 329 790 790 HOH HOH B . Z 8 HOH 330 791 791 HOH HOH B . Z 8 HOH 331 792 792 HOH HOH B . Z 8 HOH 332 793 793 HOH HOH B . Z 8 HOH 333 794 794 HOH HOH B . Z 8 HOH 334 795 795 HOH HOH B . Z 8 HOH 335 796 796 HOH HOH B . Z 8 HOH 336 797 797 HOH HOH B . Z 8 HOH 337 798 798 HOH HOH B . Z 8 HOH 338 799 799 HOH HOH B . Z 8 HOH 339 800 800 HOH HOH B . Z 8 HOH 340 801 801 HOH HOH B . Z 8 HOH 341 802 802 HOH HOH B . Z 8 HOH 342 803 803 HOH HOH B . Z 8 HOH 343 804 804 HOH HOH B . Z 8 HOH 344 805 805 HOH HOH B . Z 8 HOH 345 806 806 HOH HOH B . Z 8 HOH 346 807 807 HOH HOH B . Z 8 HOH 347 808 808 HOH HOH B . Z 8 HOH 348 809 809 HOH HOH B . Z 8 HOH 349 810 810 HOH HOH B . Z 8 HOH 350 811 811 HOH HOH B . Z 8 HOH 351 812 812 HOH HOH B . Z 8 HOH 352 813 813 HOH HOH B . Z 8 HOH 353 814 814 HOH HOH B . Z 8 HOH 354 815 815 HOH HOH B . Z 8 HOH 355 816 816 HOH HOH B . Z 8 HOH 356 817 817 HOH HOH B . Z 8 HOH 357 818 818 HOH HOH B . Z 8 HOH 358 819 819 HOH HOH B . Z 8 HOH 359 820 820 HOH HOH B . Z 8 HOH 360 821 821 HOH HOH B . Z 8 HOH 361 822 822 HOH HOH B . Z 8 HOH 362 823 823 HOH HOH B . Z 8 HOH 363 824 824 HOH HOH B . Z 8 HOH 364 825 825 HOH HOH B . Z 8 HOH 365 826 826 HOH HOH B . Z 8 HOH 366 827 827 HOH HOH B . Z 8 HOH 367 828 828 HOH HOH B . Z 8 HOH 368 829 829 HOH HOH B . Z 8 HOH 369 830 830 HOH HOH B . Z 8 HOH 370 831 831 HOH HOH B . Z 8 HOH 371 832 832 HOH HOH B . Z 8 HOH 372 833 833 HOH HOH B . Z 8 HOH 373 834 834 HOH HOH B . Z 8 HOH 374 835 835 HOH HOH B . Z 8 HOH 375 836 836 HOH HOH B . Z 8 HOH 376 837 837 HOH HOH B . Z 8 HOH 377 838 838 HOH HOH B . Z 8 HOH 378 839 839 HOH HOH B . Z 8 HOH 379 840 840 HOH HOH B . Z 8 HOH 380 841 841 HOH HOH B . Z 8 HOH 381 842 842 HOH HOH B . Z 8 HOH 382 843 843 HOH HOH B . Z 8 HOH 383 844 844 HOH HOH B . Z 8 HOH 384 845 845 HOH HOH B . Z 8 HOH 385 846 846 HOH HOH B . Z 8 HOH 386 847 847 HOH HOH B . Z 8 HOH 387 848 848 HOH HOH B . Z 8 HOH 388 849 849 HOH HOH B . Z 8 HOH 389 850 850 HOH HOH B . Z 8 HOH 390 851 851 HOH HOH B . Z 8 HOH 391 852 852 HOH HOH B . Z 8 HOH 392 853 853 HOH HOH B . Z 8 HOH 393 854 854 HOH HOH B . Z 8 HOH 394 855 855 HOH HOH B . Z 8 HOH 395 856 856 HOH HOH B . Z 8 HOH 396 857 857 HOH HOH B . Z 8 HOH 397 858 858 HOH HOH B . Z 8 HOH 398 859 859 HOH HOH B . Z 8 HOH 399 860 860 HOH HOH B . Z 8 HOH 400 861 861 HOH HOH B . Z 8 HOH 401 862 862 HOH HOH B . Z 8 HOH 402 863 863 HOH HOH B . Z 8 HOH 403 864 864 HOH HOH B . Z 8 HOH 404 865 865 HOH HOH B . Z 8 HOH 405 866 866 HOH HOH B . Z 8 HOH 406 867 867 HOH HOH B . Z 8 HOH 407 868 868 HOH HOH B . Z 8 HOH 408 869 869 HOH HOH B . Z 8 HOH 409 870 870 HOH HOH B . Z 8 HOH 410 871 871 HOH HOH B . Z 8 HOH 411 872 872 HOH HOH B . Z 8 HOH 412 873 873 HOH HOH B . Z 8 HOH 413 874 874 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 47 A ASN 93 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 69 A ASN 115 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 190 A ASN 236 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 193 B ASN 441 ? ASN 'GLYCOSYLATION SITE' 5 B ASN 272 B ASN 520 ? ASN 'GLYCOSYLATION SITE' 6 B OCS 1 B OCS 249 ? CYS 'CYSTEINESULFONIC ACID' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,V,W,X,Y,Z # 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)' 11410 ? 1 MORE -34 ? 1 'SSA (A^2)' 19920 ? # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 OD1 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OD2 ? B OCS 1 ? B OCS 249 ? 1_555 49.5 ? 2 OD1 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 O ? B ASP 67 ? B ASP 315 ? 1_555 57.0 ? 3 OD2 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 O ? B ASP 67 ? B ASP 315 ? 1_555 99.7 ? 4 OD1 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OE1 ? B GLU 80 ? B GLU 328 ? 1_555 130.5 ? 5 OD2 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OE1 ? B GLU 80 ? B GLU 328 ? 1_555 137.3 ? 6 O ? B ASP 67 ? B ASP 315 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OE1 ? B GLU 80 ? B GLU 328 ? 1_555 76.3 ? 7 OD1 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OG1 ? B THR 82 ? B THR 330 ? 1_555 125.2 ? 8 OD2 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OG1 ? B THR 82 ? B THR 330 ? 1_555 78.2 ? 9 O ? B ASP 67 ? B ASP 315 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OG1 ? B THR 82 ? B THR 330 ? 1_555 168.5 ? 10 OE1 ? B GLU 80 ? B GLU 328 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OG1 ? B THR 82 ? B THR 330 ? 1_555 97.5 ? 11 OD1 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OH ? B TYR 131 ? B TYR 379 ? 1_555 127.9 ? 12 OD2 ? B OCS 1 ? B OCS 249 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OH ? B TYR 131 ? B TYR 379 ? 1_555 148.2 ? 13 O ? B ASP 67 ? B ASP 315 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OH ? B TYR 131 ? B TYR 379 ? 1_555 100.3 ? 14 OE1 ? B GLU 80 ? B GLU 328 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OH ? B TYR 131 ? B TYR 379 ? 1_555 71.9 ? 15 OG1 ? B THR 82 ? B THR 330 ? 1_555 NA ? X NA . ? B NA 607 ? 1_555 OH ? B TYR 131 ? B TYR 379 ? 1_555 86.6 ? # 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 2009-09-15 2 'Structure model' 1 1 2011-07-13 3 'Structure model' 1 2 2017-11-01 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Non-polymer description' 2 2 'Structure model' 'Version format compliance' 3 3 'Structure model' 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _phasing.method MR # loop_ _software.name _software.version _software.date _software.type _software.contact_author _software.contact_author_email _software.classification _software.location _software.language _software.citation_id _software.pdbx_ordinal DENZO . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data reduction' http://www.hkl-xray.com/ ? ? 1 SCALEPACK . ? package 'Zbyszek Otwinowski' hkl@hkl-xray.com 'data scaling' http://www.hkl-xray.com/ ? ? 2 MOLREP . ? program 'Alexei Vaguine' alexei@ysbl.york.ac.uk phasing http://www.ccp4.ac.uk/dist/html/molrep.html Fortran_77 ? 3 REFMAC . ? program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement http://www.ccp4.ac.uk/dist/html/refmac5.html Fortran_77 ? 4 PDB_EXTRACT 3.006 'June 11, 2008' package PDB help@deposit.rcsb.org 'data extraction' http://sw-tools.pdb.org/apps/PDB_EXTRACT/ C++ ? 5 MAR345 . ? ? ? ? 'data collection' ? ? ? 6 HKL-2000 . ? ? ? ? 'data reduction' ? ? ? 7 HKL-2000 . ? ? ? ? 'data scaling' ? ? ? 8 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OD1 A ASP 87 ? ? O A HOH 594 ? ? 1.84 2 1 ND2 B ASN 520 ? ? O5 B NAG 41 ? ? 1.91 3 1 OD2 A ASP 107 ? ? NH2 B ARG 283 ? ? 2.01 4 1 OG1 A THR 95 ? ? O7 A NAG 1 ? ? 2.02 5 1 O B HOH 651 ? ? O B HOH 755 ? ? 2.03 6 1 NH1 A ARG 65 ? ? O A HOH 756 ? ? 2.06 7 1 OE2 A GLU 132 ? ? O A HOH 757 ? ? 2.15 8 1 O B HOH 153 ? ? O B HOH 759 ? ? 2.17 9 1 O A HOH 271 ? ? O A HOH 712 ? ? 2.18 # 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 MET B 275 ? ? -80.21 40.10 2 1 SER B 306 ? ? -155.45 -159.50 3 1 ASN B 394 ? ? 75.78 -6.24 4 1 ARG B 401 ? ? 83.92 -27.94 5 1 ARG B 401 ? ? 80.06 -23.46 6 1 TYR B 431 ? ? -162.81 48.20 7 1 HIS B 577 ? ? -146.57 48.42 # 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 LEU 47 ? A LEU 1 2 1 Y 1 A PRO 48 ? A PRO 2 3 1 Y 1 A THR 49 ? A THR 3 4 1 Y 1 A LEU 50 ? A LEU 4 5 1 Y 1 A GLY 51 ? A GLY 5 6 1 Y 1 A PRO 52 ? A PRO 6 7 1 Y 1 A GLY 53 ? A GLY 7 8 1 Y 1 A TRP 54 ? A TRP 8 9 1 Y 1 A GLN 55 ? A GLN 9 10 1 Y 1 A ARG 56 ? A ARG 10 11 1 Y 1 A GLN 57 ? A GLN 11 12 1 Y 1 A ASN 58 ? A ASN 12 13 1 Y 1 A PRO 59 ? A PRO 13 14 1 Y 1 A ASP 60 ? A ASP 14 15 1 Y 1 A PRO 61 ? A PRO 15 16 1 Y 1 A PRO 62 ? A PRO 16 17 1 Y 1 A ASN 239 ? A ASN 193 18 1 Y 1 A THR 240 ? A THR 194 19 1 Y 1 A LYS 241 ? A LYS 195 20 1 Y 1 A PRO 242 ? A PRO 196 21 1 Y 1 A SER 243 ? A SER 197 22 1 Y 1 A LEU 244 ? A LEU 198 23 1 Y 1 B TRP 593 ? B TRP 345 24 1 Y 1 B ASP 594 ? B ASP 346 25 1 Y 1 B GLY 595 ? B GLY 347 26 1 Y 1 B ARG 596 ? B ARG 348 27 1 Y 1 B GLY 597 ? B GLY 349 28 1 Y 1 B SER 598 ? B SER 350 29 1 Y 1 B HIS 599 ? B HIS 351 30 1 Y 1 B HIS 600 ? B HIS 352 31 1 Y 1 B HIS 601 ? B HIS 353 32 1 Y 1 B HIS 602 ? B HIS 354 33 1 Y 1 B HIS 603 ? B HIS 355 34 1 Y 1 B HIS 604 ? B HIS 356 35 1 Y 1 B GLY 605 ? B GLY 357 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 N-ACETYL-D-GLUCOSAMINE NAG 4 GLYCEROL GOL 5 'ACETATE ION' ACT 6 XENON XE 7 'SODIUM ION' NA 8 water HOH #