data_1OCJ # _entry.id 1OCJ # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1OCJ PDBE EBI-12033 WWPDB D_1290012033 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 1BVW unspecified 'CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS' PDB 1GZ1 unspecified ;MUTANT D416A OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-CELLOBIOSYL-4-DEOXY-4-THIO-BETA-D- CELLOBIOSIDE ; PDB 1HGW unspecified 'CEL6A D175A MUTANT' PDB 1HGY unspecified 'CEL6A D221A MUTANT' PDB 1OC5 unspecified ;D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-CELLOBIOSYL-4-DEOXY-4-THIO-BETA-D- CELLOBIOSIDE ; PDB 1OC6 unspecified 'STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION' PDB 1OC7 unspecified ;D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-TETRATHIO-ALPHA-D-CELLOPENTOSIDE AT 1 .1 ANGSTROM RESOLUTION ; PDB 1OCB unspecified 'STRUCTURE OF THE WILD-TYPE CELLOBIOHYDROLASE CEL6A FROM HUMICOLAS INSOLENS IN COMPLEX WITH A FLUORESCENT SUBSTRATE' PDB 1OCN unspecified ;MUTANT D416A OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH A CELLOBIO-DERIVED ISOFAGOMINE AT 1.3 ANGSTROM RESOLUTION ; PDB 1QJW unspecified 'CEL6A (Y169F) WITH A NON-HYDROLYSABLE CELLOTETRAOSE' PDB 1QK0 unspecified 'CEL6A (Y169F) WITH A NON-HYDROLYSABLE CELLOTETRAOSE' PDB 1QK2 unspecified 'WILD TYPE CEL6A WITH A NON-HYDROLYSABLE CELLOTETRAOSE' PDB 2BVW unspecified 'CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS IN COMPLEX WITH GLUCOSE AND CELLOTETRAOSE' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1OCJ _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2003-02-07 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Varrot, A.' 1 'Frandsen, T.P.' 2 'Von Ossowski, I.' 3 'Boyer, V.' 4 'Driguez, H.' 5 'Schulein, M.' 6 'Davies, G.J.' 7 # _citation.id primary _citation.title 'Structural Basis for Ligand Binding and Processivity in Cellobiohydrolase Cel6A from Humicola Insolens' _citation.journal_abbrev Structure _citation.journal_volume 11 _citation.page_first 855 _citation.page_last ? _citation.year 2003 _citation.journal_id_ASTM STRUE6 _citation.country UK _citation.journal_id_ISSN 0969-2126 _citation.journal_id_CSD 2005 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 12842048 _citation.pdbx_database_id_DOI '10.1016/S0969-2126(03)00124-2' # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Varrot, A.' 1 primary 'Frandsen, T.P.' 2 primary 'Von Ossowski, I.' 3 primary 'Boyer, V.' 4 primary 'Driguez, H.' 5 primary 'Schulein, M.' 6 primary 'Davies, G.J.' 7 # _cell.entry_id 1OCJ _cell.length_a 47.440 _cell.length_b 67.552 _cell.length_c 53.663 _cell.angle_alpha 90.00 _cell.angle_beta 110.87 _cell.angle_gamma 90.00 _cell.Z_PDB 2 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1OCJ _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # 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 'CELLOBIOHYDROLASE II' 39970.504 1 3.2.1.91 ? 'CATALYTIC CORE DOMAIN RESIDUES 89-450' 'N-LINKED N-ACETYLGLUCOSAMINE ON RESIDUE ASN 141' 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 non-polymer man BETA-D-GLUCOSE 180.156 1 ? ? ? ? 4 non-polymer man 1,4-DEOXY-1,4-DITHIO-BETA-D-GLUCOPYRANOSE 212.287 2 ? ? ? ? 5 non-polymer man 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE 196.221 1 ? ? ? ? 6 non-polymer man O1-METHYL-4-DEOXY-4-THIO-ALPHA-D-GLUCOSE 210.248 1 ? ? ? ? 7 non-polymer syn 'MAGNESIUM ION' 24.305 1 ? ? ? ? 8 non-polymer syn 'ACETIC ACID' 60.052 1 ? ? ? ? 9 water nat water 18.015 402 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'CELLULASE, CEL6A' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;YNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQYA AQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAASTYR ELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPNPN YDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECDGTS DTTAARYAYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF ; _entity_poly.pdbx_seq_one_letter_code_can ;YNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQYA AQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAASTYR ELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPNPN YDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECDGTS DTTAARYAYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 TYR n 1 2 ASN n 1 3 GLY n 1 4 ASN n 1 5 PRO n 1 6 PHE n 1 7 GLU n 1 8 GLY n 1 9 VAL n 1 10 GLN n 1 11 LEU n 1 12 TRP n 1 13 ALA n 1 14 ASN n 1 15 ASN n 1 16 TYR n 1 17 TYR n 1 18 ARG n 1 19 SER n 1 20 GLU n 1 21 VAL n 1 22 HIS n 1 23 THR n 1 24 LEU n 1 25 ALA n 1 26 ILE n 1 27 PRO n 1 28 GLN n 1 29 ILE n 1 30 THR n 1 31 ASP n 1 32 PRO n 1 33 ALA n 1 34 LEU n 1 35 ARG n 1 36 ALA n 1 37 ALA n 1 38 ALA n 1 39 SER n 1 40 ALA n 1 41 VAL n 1 42 ALA n 1 43 GLU n 1 44 VAL n 1 45 PRO n 1 46 SER n 1 47 PHE n 1 48 GLN n 1 49 TRP n 1 50 LEU n 1 51 ASP n 1 52 ARG n 1 53 ASN n 1 54 VAL n 1 55 THR n 1 56 VAL n 1 57 ASP n 1 58 THR n 1 59 LEU n 1 60 LEU n 1 61 VAL n 1 62 GLN n 1 63 THR n 1 64 LEU n 1 65 SER n 1 66 GLU n 1 67 ILE n 1 68 ARG n 1 69 GLU n 1 70 ALA n 1 71 ASN n 1 72 GLN n 1 73 ALA n 1 74 GLY n 1 75 ALA n 1 76 ASN n 1 77 PRO n 1 78 GLN n 1 79 TYR n 1 80 ALA n 1 81 ALA n 1 82 GLN n 1 83 ILE n 1 84 VAL n 1 85 VAL n 1 86 TYR n 1 87 ASP n 1 88 LEU n 1 89 PRO n 1 90 ASP n 1 91 ARG n 1 92 ASP n 1 93 CYS n 1 94 ALA n 1 95 ALA n 1 96 ALA n 1 97 ALA n 1 98 SER n 1 99 ASN n 1 100 GLY n 1 101 GLU n 1 102 TRP n 1 103 ALA n 1 104 ILE n 1 105 ALA n 1 106 ASN n 1 107 ASN n 1 108 GLY n 1 109 VAL n 1 110 ASN n 1 111 ASN n 1 112 TYR n 1 113 LYS n 1 114 ALA n 1 115 TYR n 1 116 ILE n 1 117 ASN n 1 118 ARG n 1 119 ILE n 1 120 ARG n 1 121 GLU n 1 122 ILE n 1 123 LEU n 1 124 ILE n 1 125 SER n 1 126 PHE n 1 127 SER n 1 128 ASP n 1 129 VAL n 1 130 ARG n 1 131 THR n 1 132 ILE n 1 133 LEU n 1 134 VAL n 1 135 ILE n 1 136 GLU n 1 137 PRO n 1 138 ASP n 1 139 SER n 1 140 LEU n 1 141 ALA n 1 142 ASN n 1 143 MET n 1 144 VAL n 1 145 THR n 1 146 ASN n 1 147 MET n 1 148 ASN n 1 149 VAL n 1 150 PRO n 1 151 LYS n 1 152 CYS n 1 153 SER n 1 154 GLY n 1 155 ALA n 1 156 ALA n 1 157 SER n 1 158 THR n 1 159 TYR n 1 160 ARG n 1 161 GLU n 1 162 LEU n 1 163 THR n 1 164 ILE n 1 165 TYR n 1 166 ALA n 1 167 LEU n 1 168 LYS n 1 169 GLN n 1 170 LEU n 1 171 ASP n 1 172 LEU n 1 173 PRO n 1 174 HIS n 1 175 VAL n 1 176 ALA n 1 177 MET n 1 178 TYR n 1 179 MET n 1 180 ASP n 1 181 ALA n 1 182 GLY n 1 183 HIS n 1 184 ALA n 1 185 GLY n 1 186 TRP n 1 187 LEU n 1 188 GLY n 1 189 TRP n 1 190 PRO n 1 191 ALA n 1 192 ASN n 1 193 ILE n 1 194 GLN n 1 195 PRO n 1 196 ALA n 1 197 ALA n 1 198 GLU n 1 199 LEU n 1 200 PHE n 1 201 ALA n 1 202 LYS n 1 203 ILE n 1 204 TYR n 1 205 GLU n 1 206 ASP n 1 207 ALA n 1 208 GLY n 1 209 LYS n 1 210 PRO n 1 211 ARG n 1 212 ALA n 1 213 VAL n 1 214 ARG n 1 215 GLY n 1 216 LEU n 1 217 ALA n 1 218 THR n 1 219 ASN n 1 220 VAL n 1 221 ALA n 1 222 ASN n 1 223 TYR n 1 224 ASN n 1 225 ALA n 1 226 TRP n 1 227 SER n 1 228 VAL n 1 229 SER n 1 230 SER n 1 231 PRO n 1 232 PRO n 1 233 PRO n 1 234 TYR n 1 235 THR n 1 236 SER n 1 237 PRO n 1 238 ASN n 1 239 PRO n 1 240 ASN n 1 241 TYR n 1 242 ASP n 1 243 GLU n 1 244 LYS n 1 245 HIS n 1 246 TYR n 1 247 ILE n 1 248 GLU n 1 249 ALA n 1 250 PHE n 1 251 ARG n 1 252 PRO n 1 253 LEU n 1 254 LEU n 1 255 GLU n 1 256 ALA n 1 257 ARG n 1 258 GLY n 1 259 PHE n 1 260 PRO n 1 261 ALA n 1 262 GLN n 1 263 PHE n 1 264 ILE n 1 265 VAL n 1 266 ASP n 1 267 GLN n 1 268 GLY n 1 269 ARG n 1 270 SER n 1 271 GLY n 1 272 LYS n 1 273 GLN n 1 274 PRO n 1 275 THR n 1 276 GLY n 1 277 GLN n 1 278 LYS n 1 279 GLU n 1 280 TRP n 1 281 GLY n 1 282 HIS n 1 283 TRP n 1 284 CYS n 1 285 ASN n 1 286 ALA n 1 287 ILE n 1 288 GLY n 1 289 THR n 1 290 GLY n 1 291 PHE n 1 292 GLY n 1 293 MET n 1 294 ARG n 1 295 PRO n 1 296 THR n 1 297 ALA n 1 298 ASN n 1 299 THR n 1 300 GLY n 1 301 HIS n 1 302 GLN n 1 303 TYR n 1 304 VAL n 1 305 ASP n 1 306 ALA n 1 307 PHE n 1 308 VAL n 1 309 TRP n 1 310 VAL n 1 311 LYS n 1 312 PRO n 1 313 GLY n 1 314 GLY n 1 315 GLU n 1 316 CYS n 1 317 ASP n 1 318 GLY n 1 319 THR n 1 320 SER n 1 321 ASP n 1 322 THR n 1 323 THR n 1 324 ALA n 1 325 ALA n 1 326 ARG n 1 327 TYR n 1 328 ALA n 1 329 TYR n 1 330 HIS n 1 331 CYS n 1 332 GLY n 1 333 LEU n 1 334 GLU n 1 335 ASP n 1 336 ALA n 1 337 LEU n 1 338 LYS n 1 339 PRO n 1 340 ALA n 1 341 PRO n 1 342 GLU n 1 343 ALA n 1 344 GLY n 1 345 GLN n 1 346 TRP n 1 347 PHE n 1 348 ASN n 1 349 GLU n 1 350 TYR n 1 351 PHE n 1 352 ILE n 1 353 GLN n 1 354 LEU n 1 355 LEU n 1 356 ARG n 1 357 ASN n 1 358 ALA n 1 359 ASN n 1 360 PRO n 1 361 PRO n 1 362 PHE n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _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 'HUMICOLA INSOLENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 34413 _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 'ASPERGILLUS ORYZAE' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5062 _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 'UNDER CONTROL OF THE FUNGAL AMYLASE PROMOTER AND AMYLOGLUCOSIDASE TERMINATOR' _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name PDB _struct_ref.db_code 1OCJ _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession 1OCJ _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1OCJ _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 362 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 1OCJ _struct_ref_seq.db_align_beg 89 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 450 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 89 _struct_ref_seq.pdbx_auth_seq_align_end 450 # 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 ACY non-polymer . 'ACETIC ACID' ? 'C2 H4 O2' 60.052 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 BGC saccharide . BETA-D-GLUCOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MA3 D-saccharide . O1-METHYL-4-DEOXY-4-THIO-ALPHA-D-GLUCOSE ? 'C7 H14 O5 S' 210.248 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MG non-polymer . 'MAGNESIUM ION' ? 'Mg 2' 24.305 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SGC D-saccharide . 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE ? 'C6 H12 O5 S' 196.221 SSG D-saccharide . 1,4-DEOXY-1,4-DITHIO-BETA-D-GLUCOPYRANOSE ? 'C6 H12 O4 S2' 212.287 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1OCJ _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.01 _exptl_crystal.density_percent_sol 42.0 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.60 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details ;PROTEIN WAS CONCENTRATED TO 10 MG/ML IN WATER. CRYSTALLISATION IN 200MM MAGNESIUM ACETATE IN 100MM SODIUM ACETATE BUFFER AT PH 4.6. PRECIPITANT WAS 20% POLYETHYLENE GLYCOL 5K MME. ; # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date 2002-06-15 _diffrn_detector.details 'TORROIDAL MIRROR' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'DIAMOND (111), GE(220)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.934 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-1' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-1 _diffrn_source.pdbx_wavelength 0.934 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1OCJ _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 30.000 _reflns.d_resolution_high 1.300 _reflns.number_obs 79327 _reflns.number_all ? _reflns.percent_possible_obs 90.0 _reflns.pdbx_Rmerge_I_obs 0.06800 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 16.7000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.600 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.30 _reflns_shell.d_res_low 1.35 _reflns_shell.percent_possible_all 52.3 _reflns_shell.Rmerge_I_obs 0.27000 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 4.600 _reflns_shell.pdbx_redundancy 1.60 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1OCJ _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 67142 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 30.00 _refine.ls_d_res_high 1.30 _refine.ls_percent_reflns_obs 91.0 _refine.ls_R_factor_obs 0.146 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.145 _refine.ls_R_factor_R_free 0.174 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.000 _refine.ls_number_reflns_R_free 3548 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.974 _refine.correlation_coeff_Fo_to_Fc_free 0.965 _refine.B_iso_mean 12.36 _refine.aniso_B[1][1] -0.59000 _refine.aniso_B[2][2] 0.16000 _refine.aniso_B[3][3] 0.41000 _refine.aniso_B[1][2] 0.00000 _refine.aniso_B[1][3] -0.03000 _refine.aniso_B[2][3] 0.00000 _refine.solvent_model_details 'BABINET MODEL WITH MASK' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.40 _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 1GZ1' _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 0.059 _refine.pdbx_overall_ESU_R_Free 0.053 _refine.overall_SU_ML 0.032 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 0.758 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2804 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 76 _refine_hist.number_atoms_solvent 402 _refine_hist.number_atoms_total 3282 _refine_hist.d_res_high 1.30 _refine_hist.d_res_low 30.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.015 0.021 ? 3002 'X-RAY DIFFRACTION' ? r_bond_other_d 0.002 0.020 ? 2596 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.701 1.952 ? 4112 'X-RAY DIFFRACTION' ? r_angle_other_deg 0.969 3.000 ? 6045 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.037 5.000 ? 368 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_chiral_restr 0.146 0.200 ? 453 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.016 0.020 ? 3382 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.010 0.020 ? 606 'X-RAY DIFFRACTION' ? r_nbd_refined 0.231 0.200 ? 619 'X-RAY DIFFRACTION' ? r_nbd_other 0.249 0.200 ? 3166 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other 0.085 0.200 ? 1693 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.122 0.200 ? 225 '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 0.145 0.200 ? 9 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.258 0.200 ? 56 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.152 0.200 ? 33 '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 1.377 1.500 ? 1822 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 2.051 2.000 ? 2933 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.669 3.000 ? 1180 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.844 4.500 ? 1174 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.30 _refine_ls_shell.d_res_low 1.33 _refine_ls_shell.number_reflns_R_work 2974 _refine_ls_shell.R_factor_R_work 0.2100 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.2520 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 146 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 1OCJ _struct.title 'Mutant D416A of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS in complex with a THIOPENTASACCHARIDE at 1.3 angstrom resolution' _struct.pdbx_descriptor 'CELLOBIOHYDROLASE II (E.C.3.2.1.91)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1OCJ _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, CELLULOSE DEGRADATION, PROCESSIVE MECHANISM GLYCOSIDE HYDROLASE FAMILY 6' # 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 4 ? E N N 4 ? F N N 5 ? G N N 6 ? H N N 7 ? I N N 8 ? J N N 9 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 14 ? ALA A 25 ? ASN A 102 ALA A 113 1 ? 12 HELX_P HELX_P2 2 ILE A 26 ? ILE A 29 ? ILE A 114 ILE A 117 5 ? 4 HELX_P HELX_P3 3 ASP A 31 ? ALA A 42 ? ASP A 119 ALA A 130 1 ? 12 HELX_P HELX_P4 4 ARG A 52 ? VAL A 56 ? ARG A 140 VAL A 144 5 ? 5 HELX_P HELX_P5 5 THR A 58 ? ALA A 73 ? THR A 146 ALA A 161 1 ? 16 HELX_P HELX_P6 6 ALA A 103 ? ASN A 106 ? ALA A 191 ASN A 194 5 ? 4 HELX_P HELX_P7 7 ASN A 107 ? PHE A 126 ? ASN A 195 PHE A 214 1 ? 20 HELX_P HELX_P8 8 LEU A 140 ? ASN A 146 ? LEU A 228 ASN A 234 1 ? 7 HELX_P HELX_P9 9 VAL A 149 ? LEU A 170 ? VAL A 237 LEU A 258 1 ? 22 HELX_P HELX_P10 10 TRP A 189 ? ALA A 207 ? TRP A 277 ALA A 295 1 ? 19 HELX_P HELX_P11 11 PRO A 232 ? SER A 236 ? PRO A 320 SER A 324 5 ? 5 HELX_P HELX_P12 12 ASP A 242 ? ARG A 257 ? ASP A 330 ARG A 345 1 ? 16 HELX_P HELX_P13 13 ALA A 328 ? LEU A 333 ? ALA A 416 LEU A 421 5 ? 6 HELX_P HELX_P14 14 PHE A 347 ? ASN A 357 ? PHE A 435 ASN A 445 1 ? 11 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 93 SG ? ? ? 1_555 A CYS 152 SG A ? A CYS 181 A CYS 240 1_555 ? ? ? ? ? ? ? 2.314 ? disulf2 disulf ? ? A CYS 284 SG ? ? ? 1_555 A CYS 331 SG ? ? A CYS 372 A CYS 419 1_555 ? ? ? ? ? ? ? 2.070 ? covale1 covale ? ? A ASN 53 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 141 A NAG 500 1_555 ? ? ? ? ? ? ? 1.419 ? covale2 covale ? ? C BGC . C1 ? ? ? 1_555 D SSG . S4 ? ? A BGC 501 A SSG 502 1_555 ? ? ? ? ? ? ? 1.783 ? covale3 covale ? ? D SSG . C1 ? ? ? 1_555 E SSG . S4 ? ? A SSG 502 A SSG 503 1_555 ? ? ? ? ? ? ? 1.795 ? covale4 covale ? ? E SSG . C1 ? ? ? 1_555 F SGC . S4 ? ? A SSG 503 A SGC 504 1_555 ? ? ? ? ? ? ? 1.776 ? covale5 covale ? ? F SGC . C1 ? ? ? 1_555 G MA3 . S4 ? ? A SGC 504 A MA3 505 1_555 ? ? ? ? ? ? ? 1.748 ? metalc1 metalc ? ? H MG . MG ? ? ? 1_555 J HOH . O ? ? A MG 506 A HOH 2103 1_655 ? ? ? ? ? ? ? 2.172 ? metalc2 metalc ? ? H MG . MG ? ? ? 1_555 J HOH . O ? ? A MG 506 A HOH 2304 1_555 ? ? ? ? ? ? ? 2.088 ? metalc3 metalc ? ? H MG . MG ? ? ? 1_555 J HOH . O ? ? A MG 506 A HOH 2306 1_555 ? ? ? ? ? ? ? 2.001 ? metalc4 metalc ? ? H MG . MG ? ? ? 1_555 J HOH . O ? ? A MG 506 A HOH 2072 1_655 ? ? ? ? ? ? ? 1.988 ? metalc5 metalc ? ? H MG . MG ? ? ? 1_555 J HOH . O ? ? A MG 506 A HOH 2102 1_655 ? ? ? ? ? ? ? 2.160 ? metalc6 metalc ? ? H MG . MG ? ? ? 1_555 J HOH . O ? ? A MG 506 A HOH 2096 1_655 ? ? ? ? ? ? ? 2.088 ? # 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 ASN 76 A . ? ASN 164 A PRO 77 A ? PRO 165 A 1 -1.67 2 SER 236 A . ? SER 324 A PRO 237 A ? PRO 325 A 1 2.88 3 GLN 273 A . ? GLN 361 A PRO 274 A ? PRO 362 A 1 -5.37 4 LYS 338 A . ? LYS 426 A PRO 339 A ? PRO 427 A 1 0.50 5 ASN 359 A . ? ASN 447 A PRO 360 A ? PRO 448 A 1 -1.30 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 3 ? AB ? 7 ? # 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 AA 1 2 ? parallel AA 2 3 ? parallel AB 1 2 ? parallel AB 2 3 ? parallel AB 3 4 ? parallel AB 4 5 ? parallel AB 5 6 ? parallel AB 6 7 ? 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 AA 1 GLN A 10 ? LEU A 11 ? GLN A 98 LEU A 99 AA 2 TYR A 79 ? VAL A 85 ? TYR A 167 VAL A 173 AA 3 GLN A 48 ? LEU A 50 ? GLN A 136 LEU A 138 AB 1 GLN A 10 ? LEU A 11 ? GLN A 98 LEU A 99 AB 2 TYR A 79 ? VAL A 85 ? TYR A 167 VAL A 173 AB 3 THR A 131 ? ILE A 135 ? THR A 219 ILE A 223 AB 4 VAL A 175 ? ASP A 180 ? VAL A 263 ASP A 268 AB 5 VAL A 213 ? THR A 218 ? VAL A 301 THR A 306 AB 6 GLN A 262 ? ASP A 266 ? GLN A 350 ASP A 354 AB 7 VAL A 304 ? VAL A 308 ? VAL A 392 VAL A 396 # 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 AA 1 2 O GLN A 10 ? O GLN A 98 N ALA A 80 ? N ALA A 168 AA 2 3 N VAL A 84 ? N VAL A 172 O GLN A 48 ? O GLN A 136 AB 1 2 O GLN A 10 ? O GLN A 98 N ALA A 80 ? N ALA A 168 AB 2 3 N ILE A 83 ? N ILE A 171 O ILE A 132 ? O ILE A 220 AB 3 4 N LEU A 133 ? N LEU A 221 O ALA A 176 ? O ALA A 264 AB 4 5 O MET A 177 ? O MET A 265 N ARG A 214 ? N ARG A 302 AB 5 6 N LEU A 216 ? N LEU A 304 O GLN A 262 ? O GLN A 350 AB 6 7 O PHE A 263 ? O PHE A 351 N ASP A 305 ? N ASP A 393 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE MG A 506' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ACY A 507' AC3 Software ? ? ? ? 10 'BINDING SITE FOR MONO-SACCHARIDE NAG A 500 BOUND TO ASN A 141' AC4 Software ? ? ? ? 29 'BINDING SITE FOR CHAIN A OF POLYSACCHARIDE RESIDUES 501 TO 505' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 7 GLU A 69 ? GLU A 157 . ? 1_655 ? 2 AC1 7 HOH J . ? HOH A 2072 . ? 1_655 ? 3 AC1 7 HOH J . ? HOH A 2096 . ? 1_655 ? 4 AC1 7 HOH J . ? HOH A 2102 . ? 1_655 ? 5 AC1 7 HOH J . ? HOH A 2103 . ? 1_655 ? 6 AC1 7 HOH J . ? HOH A 2304 . ? 1_555 ? 7 AC1 7 HOH J . ? HOH A 2306 . ? 1_555 ? 8 AC2 4 GLN A 10 ? GLN A 98 . ? 1_555 ? 9 AC2 4 LEU A 11 ? LEU A 99 . ? 1_555 ? 10 AC2 4 PRO A 45 ? PRO A 133 . ? 1_555 ? 11 AC2 4 HOH J . ? HOH A 2349 . ? 1_555 ? 12 AC3 10 ASN A 53 ? ASN A 141 . ? 1_555 ? 13 AC3 10 ASP A 57 ? ASP A 145 . ? 1_555 ? 14 AC3 10 ASN A 111 ? ASN A 199 . ? 1_555 ? 15 AC3 10 HOH J . ? HOH A 2060 . ? 1_555 ? 16 AC3 10 HOH J . ? HOH A 2061 . ? 1_555 ? 17 AC3 10 HOH J . ? HOH A 2172 . ? 1_555 ? 18 AC3 10 HOH J . ? HOH A 2410 . ? 1_555 ? 19 AC3 10 HOH J . ? HOH A 2411 . ? 1_555 ? 20 AC3 10 HOH J . ? HOH A 2412 . ? 1_555 ? 21 AC3 10 HOH J . ? HOH A 2413 . ? 1_555 ? 22 AC4 29 TRP A 49 ? TRP A 137 . ? 1_555 ? 23 AC4 29 ASP A 51 ? ASP A 139 . ? 1_555 ? 24 AC4 29 TYR A 86 ? TYR A 174 . ? 1_555 ? 25 AC4 29 ALA A 95 ? ALA A 183 . ? 1_555 ? 26 AC4 29 ASP A 138 ? ASP A 226 . ? 1_555 ? 27 AC4 29 ASN A 142 ? ASN A 230 . ? 1_555 ? 28 AC4 29 THR A 145 ? THR A 233 . ? 1_555 ? 29 AC4 29 ASN A 146 ? ASN A 234 . ? 1_555 ? 30 AC4 29 HIS A 183 ? HIS A 271 . ? 1_555 ? 31 AC4 29 GLY A 185 ? GLY A 273 . ? 1_555 ? 32 AC4 29 TRP A 186 ? TRP A 274 . ? 1_555 ? 33 AC4 29 TRP A 189 ? TRP A 277 . ? 1_555 ? 34 AC4 29 ALA A 221 ? ALA A 309 . ? 1_555 ? 35 AC4 29 ASN A 222 ? ASN A 310 . ? 1_555 ? 36 AC4 29 TRP A 283 ? TRP A 371 . ? 1_555 ? 37 AC4 29 LYS A 311 ? LYS A 399 . ? 1_555 ? 38 AC4 29 PRO A 312 ? PRO A 400 . ? 1_555 ? 39 AC4 29 GLU A 315 ? GLU A 403 . ? 1_555 ? 40 AC4 29 ASP A 317 ? ASP A 405 . ? 1_555 ? 41 AC4 29 GLY A 344 ? GLY A 432 . ? 1_555 ? 42 AC4 29 HOH J . ? HOH A 2046 . ? 1_555 ? 43 AC4 29 HOH J . ? HOH A 2047 . ? 1_555 ? 44 AC4 29 HOH J . ? HOH A 2051 . ? 1_555 ? 45 AC4 29 HOH J . ? HOH A 2414 . ? 1_555 ? 46 AC4 29 HOH J . ? HOH A 2415 . ? 1_555 ? 47 AC4 29 HOH J . ? HOH A 2416 . ? 1_555 ? 48 AC4 29 HOH J . ? HOH A 2417 . ? 1_555 ? 49 AC4 29 HOH J . ? HOH A 2418 . ? 1_555 ? 50 AC4 29 HOH J . ? HOH A 2420 . ? 1_555 ? # _database_PDB_matrix.entry_id 1OCJ _database_PDB_matrix.origx[1][1] 1.000000 _database_PDB_matrix.origx[1][2] 0.000000 _database_PDB_matrix.origx[1][3] 0.000000 _database_PDB_matrix.origx[2][1] 0.000000 _database_PDB_matrix.origx[2][2] 1.000000 _database_PDB_matrix.origx[2][3] 0.000000 _database_PDB_matrix.origx[3][1] 0.000000 _database_PDB_matrix.origx[3][2] 0.000000 _database_PDB_matrix.origx[3][3] 1.000000 _database_PDB_matrix.origx_vector[1] 0.00000 _database_PDB_matrix.origx_vector[2] 0.00000 _database_PDB_matrix.origx_vector[3] 0.00000 # _atom_sites.entry_id 1OCJ _atom_sites.fract_transf_matrix[1][1] 0.021079 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.008037 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.014803 _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] 0.019943 _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 MG N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . GLY A 1 3 ? 10.214 21.976 9.529 1.00 21.00 ? 91 GLY A N 1 ATOM 2 C CA . GLY A 1 3 ? 9.014 21.250 9.032 1.00 20.48 ? 91 GLY A CA 1 ATOM 3 C C . GLY A 1 3 ? 8.934 19.794 9.501 1.00 19.57 ? 91 GLY A C 1 ATOM 4 O O . GLY A 1 3 ? 8.434 18.908 8.819 1.00 21.32 ? 91 GLY A O 1 ATOM 5 N N . ASN A 1 4 ? 9.423 19.558 10.695 1.00 17.64 ? 92 ASN A N 1 ATOM 6 C CA . ASN A 1 4 ? 9.394 18.231 11.298 1.00 14.41 ? 92 ASN A CA 1 ATOM 7 C C . ASN A 1 4 ? 7.950 17.836 11.581 1.00 12.78 ? 92 ASN A C 1 ATOM 8 O O . ASN A 1 4 ? 7.300 18.475 12.387 1.00 12.60 ? 92 ASN A O 1 ATOM 9 C CB . ASN A 1 4 ? 10.210 18.305 12.580 1.00 13.49 ? 92 ASN A CB 1 ATOM 10 C CG . ASN A 1 4 ? 10.301 16.989 13.285 1.00 11.96 ? 92 ASN A CG 1 ATOM 11 O OD1 . ASN A 1 4 ? 9.643 16.043 12.933 1.00 11.41 ? 92 ASN A OD1 1 ATOM 12 N ND2 . ASN A 1 4 ? 11.170 16.904 14.248 1.00 12.53 ? 92 ASN A ND2 1 ATOM 13 N N . PRO A 1 5 ? 7.455 16.757 10.980 1.00 12.51 ? 93 PRO A N 1 ATOM 14 C CA . PRO A 1 5 ? 6.060 16.385 11.236 1.00 11.76 ? 93 PRO A CA 1 ATOM 15 C C . PRO A 1 5 ? 5.752 15.923 12.639 1.00 10.99 ? 93 PRO A C 1 ATOM 16 O O . PRO A 1 5 ? 4.583 15.803 13.022 1.00 11.20 ? 93 PRO A O 1 ATOM 17 C CB . PRO A 1 5 ? 5.788 15.256 10.250 1.00 13.51 ? 93 PRO A CB 1 ATOM 18 C CG . PRO A 1 5 ? 7.124 14.725 9.964 1.00 13.17 ? 93 PRO A CG 1 ATOM 19 C CD . PRO A 1 5 ? 8.139 15.832 10.042 1.00 13.40 ? 93 PRO A CD 1 ATOM 20 N N . PHE A 1 6 ? 6.784 15.597 13.438 1.00 10.46 ? 94 PHE A N 1 ATOM 21 C CA . PHE A 1 6 ? 6.601 15.237 14.812 1.00 11.23 ? 94 PHE A CA 1 ATOM 22 C C . PHE A 1 6 ? 6.519 16.433 15.756 1.00 12.23 ? 94 PHE A C 1 ATOM 23 O O . PHE A 1 6 ? 6.173 16.261 16.923 1.00 14.04 ? 94 PHE A O 1 ATOM 24 C CB . PHE A 1 6 ? 7.718 14.287 15.239 1.00 10.68 ? 94 PHE A CB 1 ATOM 25 C CG . PHE A 1 6 ? 7.623 12.942 14.629 1.00 9.60 ? 94 PHE A CG 1 ATOM 26 C CD1 . PHE A 1 6 ? 8.143 12.706 13.363 1.00 8.42 ? 94 PHE A CD1 1 ATOM 27 C CD2 . PHE A 1 6 ? 6.979 11.893 15.303 1.00 9.81 ? 94 PHE A CD2 1 ATOM 28 C CE1 . PHE A 1 6 ? 8.054 11.465 12.802 1.00 9.16 ? 94 PHE A CE1 1 ATOM 29 C CE2 . PHE A 1 6 ? 6.896 10.652 14.736 1.00 10.51 ? 94 PHE A CE2 1 ATOM 30 C CZ . PHE A 1 6 ? 7.417 10.448 13.460 1.00 9.61 ? 94 PHE A CZ 1 ATOM 31 N N . GLU A 1 7 ? 6.877 17.612 15.270 1.00 13.57 ? 95 GLU A N 1 ATOM 32 C CA . GLU A 1 7 ? 6.838 18.840 16.084 1.00 16.71 ? 95 GLU A CA 1 ATOM 33 C C . GLU A 1 7 ? 5.429 19.409 16.030 1.00 16.40 ? 95 GLU A C 1 ATOM 34 O O . GLU A 1 7 ? 4.815 19.513 14.971 1.00 15.88 ? 95 GLU A O 1 ATOM 35 C CB . GLU A 1 7 ? 7.815 19.887 15.541 1.00 18.44 ? 95 GLU A CB 1 ATOM 36 C CG . GLU A 1 7 ? 8.036 21.115 16.433 1.00 23.31 ? 95 GLU A CG 1 ATOM 37 C CD . GLU A 1 7 ? 9.275 21.950 16.056 1.00 30.45 ? 95 GLU A CD 1 ATOM 38 O OE1 . GLU A 1 7 ? 10.232 21.390 15.470 1.00 32.74 ? 95 GLU A OE1 1 ATOM 39 O OE2 . GLU A 1 7 ? 9.305 23.185 16.364 1.00 34.89 ? 95 GLU A OE2 1 ATOM 40 N N . GLY A 1 8 ? 4.931 19.829 17.185 1.00 16.79 ? 96 GLY A N 1 ATOM 41 C CA . GLY A 1 8 ? 3.660 20.522 17.258 1.00 17.61 ? 96 GLY A CA 1 ATOM 42 C C . GLY A 1 8 ? 2.433 19.627 17.369 1.00 17.54 ? 96 GLY A C 1 ATOM 43 O O . GLY A 1 8 ? 1.296 20.112 17.202 1.00 19.64 ? 96 GLY A O 1 ATOM 44 N N . VAL A 1 9 ? 2.667 18.336 17.606 1.00 16.00 ? 97 VAL A N 1 ATOM 45 C CA . VAL A 1 9 ? 1.597 17.346 17.780 1.00 15.21 ? 97 VAL A CA 1 ATOM 46 C C . VAL A 1 9 ? 1.932 16.410 18.915 1.00 14.98 ? 97 VAL A C 1 ATOM 47 O O . VAL A 1 9 ? 3.111 16.280 19.298 1.00 17.77 ? 97 VAL A O 1 ATOM 48 C CB . VAL A 1 9 ? 1.378 16.476 16.484 1.00 14.66 ? 97 VAL A CB 1 ATOM 49 C CG1 . VAL A 1 9 ? 0.804 17.305 15.369 1.00 16.00 ? 97 VAL A CG1 1 ATOM 50 C CG2 . VAL A 1 9 ? 2.684 15.801 16.025 1.00 14.93 ? 97 VAL A CG2 1 ATOM 51 N N . GLN A 1 10 ? 0.919 15.748 19.462 1.00 14.54 ? 98 GLN A N 1 ATOM 52 C CA . GLN A 1 10 ? 1.054 14.619 20.308 1.00 16.11 ? 98 GLN A CA 1 ATOM 53 C C . GLN A 1 10 ? 0.901 13.416 19.397 1.00 15.33 ? 98 GLN A C 1 ATOM 54 O O . GLN A 1 10 ? 0.212 13.493 18.393 1.00 15.39 ? 98 GLN A O 1 ATOM 55 C CB . GLN A 1 10 ? -0.111 14.536 21.320 1.00 17.62 ? 98 GLN A CB 1 ATOM 56 C CG . GLN A 1 10 ? -0.276 15.687 22.215 1.00 20.90 ? 98 GLN A CG 1 ATOM 57 C CD . GLN A 1 10 ? -1.309 15.397 23.270 1.00 22.63 ? 98 GLN A CD 1 ATOM 58 O OE1 . GLN A 1 10 ? -1.146 14.469 24.062 1.00 22.98 ? 98 GLN A OE1 1 ATOM 59 N NE2 . GLN A 1 10 ? -2.403 16.125 23.226 1.00 23.54 ? 98 GLN A NE2 1 ATOM 60 N N . LEU A 1 11 ? 1.524 12.322 19.732 1.00 13.89 ? 99 LEU A N 1 ATOM 61 C CA . LEU A 1 11 ? 1.367 11.068 19.009 1.00 14.16 ? 99 LEU A CA 1 ATOM 62 C C . LEU A 1 11 ? 0.302 10.252 19.698 1.00 14.80 ? 99 LEU A C 1 ATOM 63 O O . LEU A 1 11 ? 0.302 10.080 20.924 1.00 15.46 ? 99 LEU A O 1 ATOM 64 C CB . LEU A 1 11 ? 2.713 10.338 18.951 1.00 14.08 ? 99 LEU A CB 1 ATOM 65 C CG . LEU A 1 11 ? 3.833 11.095 18.253 1.00 12.54 ? 99 LEU A CG 1 ATOM 66 C CD1 . LEU A 1 11 ? 5.131 10.307 18.413 1.00 12.94 ? 99 LEU A CD1 1 ATOM 67 C CD2 . LEU A 1 11 ? 3.516 11.311 16.795 1.00 13.85 ? 99 LEU A CD2 1 ATOM 68 N N . TRP A 1 12 ? -0.629 9.734 18.913 1.00 15.24 ? 100 TRP A N 1 ATOM 69 C CA . TRP A 1 12 ? -1.734 8.971 19.433 1.00 15.44 ? 100 TRP A CA 1 ATOM 70 C C . TRP A 1 12 ? -1.277 7.648 19.972 1.00 15.47 ? 100 TRP A C 1 ATOM 71 O O . TRP A 1 12 ? -0.594 6.866 19.305 1.00 15.55 ? 100 TRP A O 1 ATOM 72 C CB . TRP A 1 12 ? -2.736 8.711 18.312 1.00 15.70 ? 100 TRP A CB 1 ATOM 73 C CG . TRP A 1 12 ? -3.973 7.935 18.722 1.00 15.47 ? 100 TRP A CG 1 ATOM 74 C CD1 . TRP A 1 12 ? -4.313 6.687 18.340 1.00 15.90 ? 100 TRP A CD1 1 ATOM 75 C CD2 . TRP A 1 12 ? -5.042 8.427 19.522 1.00 16.96 ? 100 TRP A CD2 1 ATOM 76 N NE1 . TRP A 1 12 ? -5.532 6.345 18.878 1.00 16.96 ? 100 TRP A NE1 1 ATOM 77 C CE2 . TRP A 1 12 ? -6.002 7.399 19.613 1.00 17.16 ? 100 TRP A CE2 1 ATOM 78 C CE3 . TRP A 1 12 ? -5.296 9.639 20.152 1.00 17.63 ? 100 TRP A CE3 1 ATOM 79 C CZ2 . TRP A 1 12 ? -7.200 7.543 20.338 1.00 18.53 ? 100 TRP A CZ2 1 ATOM 80 C CZ3 . TRP A 1 12 ? -6.488 9.787 20.870 1.00 19.02 ? 100 TRP A CZ3 1 ATOM 81 C CH2 . TRP A 1 12 ? -7.416 8.736 20.953 1.00 19.34 ? 100 TRP A CH2 1 ATOM 82 N N . ALA A 1 13 ? -1.660 7.371 21.221 1.00 16.61 ? 101 ALA A N 1 ATOM 83 C CA . ALA A 1 13 ? -1.469 6.078 21.812 1.00 17.30 ? 101 ALA A CA 1 ATOM 84 C C . ALA A 1 13 ? -2.733 5.289 21.647 1.00 18.17 ? 101 ALA A C 1 ATOM 85 O O . ALA A 1 13 ? -3.792 5.678 22.166 1.00 19.16 ? 101 ALA A O 1 ATOM 86 C CB . ALA A 1 13 ? -1.122 6.233 23.277 1.00 18.33 ? 101 ALA A CB 1 ATOM 87 N N . ASN A 1 14 ? -2.672 4.228 20.871 1.00 18.28 ? 102 ASN A N 1 ATOM 88 C CA . ASN A 1 14 ? -3.900 3.584 20.428 1.00 19.40 ? 102 ASN A CA 1 ATOM 89 C C . ASN A 1 14 ? -4.466 2.707 21.529 1.00 20.47 ? 102 ASN A C 1 ATOM 90 O O . ASN A 1 14 ? -3.745 2.343 22.480 1.00 19.19 ? 102 ASN A O 1 ATOM 91 C CB . ASN A 1 14 ? -3.686 2.825 19.133 1.00 20.04 ? 102 ASN A CB 1 ATOM 92 C CG . ASN A 1 14 ? -2.808 1.646 19.299 1.00 18.41 ? 102 ASN A CG 1 ATOM 93 O OD1 . ASN A 1 14 ? -3.246 0.582 19.733 1.00 20.06 ? 102 ASN A OD1 1 ATOM 94 N ND2 . ASN A 1 14 ? -1.534 1.812 18.945 1.00 18.05 ? 102 ASN A ND2 1 ATOM 95 N N . ASN A 1 15 ? -5.763 2.413 21.457 1.00 22.64 ? 103 ASN A N 1 ATOM 96 C CA . ASN A 1 15 ? -6.413 1.662 22.526 1.00 23.52 ? 103 ASN A CA 1 ATOM 97 C C . ASN A 1 15 ? -6.248 0.173 22.415 1.00 22.86 ? 103 ASN A C 1 ATOM 98 O O . ASN A 1 15 ? -6.523 -0.557 23.363 1.00 22.77 ? 103 ASN A O 1 ATOM 99 C CB . ASN A 1 15 ? -7.908 1.999 22.706 1.00 24.85 ? 103 ASN A CB 1 ATOM 100 C CG . ASN A 1 15 ? -8.494 1.380 24.030 1.00 27.64 ? 103 ASN A CG 1 ATOM 101 O OD1 . ASN A 1 15 ? -7.968 1.613 25.143 1.00 28.02 ? 103 ASN A OD1 1 ATOM 102 N ND2 . ASN A 1 15 ? -9.543 0.553 23.898 1.00 30.07 ? 103 ASN A ND2 1 ATOM 103 N N . TYR A 1 16 ? -5.805 -0.319 21.271 1.00 22.58 ? 104 TYR A N 1 ATOM 104 C CA . TYR A 1 16 ? -5.538 -1.735 21.165 1.00 22.19 ? 104 TYR A CA 1 ATOM 105 C C . TYR A 1 16 ? -4.335 -2.128 22.040 1.00 22.01 ? 104 TYR A C 1 ATOM 106 O O . TYR A 1 16 ? -4.417 -3.094 22.810 1.00 21.04 ? 104 TYR A O 1 ATOM 107 C CB . TYR A 1 16 ? -5.342 -2.116 19.696 1.00 23.22 ? 104 TYR A CB 1 ATOM 108 C CG . TYR A 1 16 ? -5.099 -3.574 19.460 1.00 26.84 ? 104 TYR A CG 1 ATOM 109 C CD1 . TYR A 1 16 ? -6.160 -4.472 19.369 1.00 29.99 ? 104 TYR A CD1 1 ATOM 110 C CD2 . TYR A 1 16 ? -3.805 -4.066 19.331 1.00 27.78 ? 104 TYR A CD2 1 ATOM 111 C CE1 . TYR A 1 16 ? -5.940 -5.817 19.150 1.00 32.04 ? 104 TYR A CE1 1 ATOM 112 C CE2 . TYR A 1 16 ? -3.579 -5.403 19.106 1.00 30.30 ? 104 TYR A CE2 1 ATOM 113 C CZ . TYR A 1 16 ? -4.641 -6.277 19.024 1.00 32.32 ? 104 TYR A CZ 1 ATOM 114 O OH . TYR A 1 16 ? -4.417 -7.599 18.801 1.00 35.22 ? 104 TYR A OH 1 ATOM 115 N N . TYR A 1 17 ? -3.247 -1.361 21.937 1.00 20.93 ? 105 TYR A N 1 ATOM 116 C CA . TYR A 1 17 ? -2.056 -1.647 22.727 1.00 20.75 ? 105 TYR A CA 1 ATOM 117 C C . TYR A 1 17 ? -2.387 -1.423 24.201 1.00 21.34 ? 105 TYR A C 1 ATOM 118 O O . TYR A 1 17 ? -2.064 -2.297 25.025 1.00 21.07 ? 105 TYR A O 1 ATOM 119 C CB . TYR A 1 17 ? -0.882 -0.766 22.292 1.00 19.58 ? 105 TYR A CB 1 ATOM 120 C CG . TYR A 1 17 ? 0.420 -1.146 22.957 1.00 18.31 ? 105 TYR A CG 1 ATOM 121 C CD1 . TYR A 1 17 ? 1.134 -2.247 22.526 1.00 17.34 ? 105 TYR A CD1 1 ATOM 122 C CD2 . TYR A 1 17 ? 0.919 -0.408 24.016 1.00 17.39 ? 105 TYR A CD2 1 ATOM 123 C CE1 . TYR A 1 17 ? 2.362 -2.607 23.141 1.00 16.06 ? 105 TYR A CE1 1 ATOM 124 C CE2 . TYR A 1 17 ? 2.131 -0.754 24.628 1.00 17.26 ? 105 TYR A CE2 1 ATOM 125 C CZ . TYR A 1 17 ? 2.823 -1.858 24.185 1.00 16.14 ? 105 TYR A CZ 1 ATOM 126 O OH . TYR A 1 17 ? 4.020 -2.194 24.789 1.00 16.29 ? 105 TYR A OH 1 ATOM 127 N N . ARG A 1 18 ? -3.006 -0.271 24.496 1.00 21.67 ? 106 ARG A N 1 ATOM 128 C CA . ARG A 1 18 ? -3.419 0.073 25.866 1.00 22.92 ? 106 ARG A CA 1 ATOM 129 C C . ARG A 1 18 ? -4.190 -1.065 26.501 1.00 24.25 ? 106 ARG A C 1 ATOM 130 O O . ARG A 1 18 ? -3.940 -1.409 27.640 1.00 24.58 ? 106 ARG A O 1 ATOM 131 C CB . ARG A 1 18 ? -4.258 1.343 25.914 1.00 23.01 ? 106 ARG A CB 1 ATOM 132 C CG . ARG A 1 18 ? -4.708 1.708 27.354 1.00 24.34 ? 106 ARG A CG 1 ATOM 133 C CD . ARG A 1 18 ? -5.542 2.976 27.432 1.00 26.85 ? 106 ARG A CD 1 ATOM 134 N NE . ARG A 1 18 ? -4.811 4.133 26.976 1.00 29.46 ? 106 ARG A NE 1 ATOM 135 C CZ . ARG A 1 18 ? -4.978 4.740 25.810 1.00 31.27 ? 106 ARG A CZ 1 ATOM 136 N NH1 . ARG A 1 18 ? -5.905 4.337 24.943 1.00 31.65 ? 106 ARG A NH1 1 ATOM 137 N NH2 . ARG A 1 18 ? -4.223 5.793 25.522 1.00 32.69 ? 106 ARG A NH2 1 ATOM 138 N N . SER A 1 19 ? -5.102 -1.680 25.772 1.00 25.57 ? 107 SER A N 1 ATOM 139 C CA . SER A 1 19 ? -5.951 -2.698 26.367 1.00 26.63 ? 107 SER A CA 1 ATOM 140 C C . SER A 1 19 ? -5.268 -4.074 26.389 1.00 26.12 ? 107 SER A C 1 ATOM 141 O O . SER A 1 19 ? -5.550 -4.918 27.227 1.00 25.92 ? 107 SER A O 1 ATOM 142 C CB . SER A 1 19 ? -7.319 -2.715 25.677 1.00 27.54 ? 107 SER A CB 1 ATOM 143 O OG . SER A 1 19 ? -7.339 -3.609 24.603 1.00 30.97 ? 107 SER A OG 1 ATOM 144 N N . GLU A 1 20 ? -4.298 -4.294 25.511 1.00 25.23 ? 108 GLU A N 1 ATOM 145 C CA . GLU A 1 20 ? -3.471 -5.470 25.652 1.00 24.87 ? 108 GLU A CA 1 ATOM 146 C C . GLU A 1 20 ? -2.700 -5.352 26.980 1.00 24.63 ? 108 GLU A C 1 ATOM 147 O O . GLU A 1 20 ? -2.626 -6.311 27.726 1.00 25.52 ? 108 GLU A O 1 ATOM 148 C CB . GLU A 1 20 ? -2.471 -5.595 24.494 1.00 24.64 ? 108 GLU A CB 1 ATOM 149 C CG . GLU A 1 20 ? -3.058 -6.100 23.184 1.00 23.38 ? 108 GLU A CG 1 ATOM 150 C CD . GLU A 1 20 ? -2.015 -6.063 22.072 1.00 21.38 ? 108 GLU A CD 1 ATOM 151 O OE1 . GLU A 1 20 ? -1.432 -4.956 21.873 1.00 21.05 ? 108 GLU A OE1 1 ATOM 152 O OE2 . GLU A 1 20 ? -1.793 -7.118 21.444 1.00 24.50 ? 108 GLU A OE2 1 ATOM 153 N N . VAL A 1 21 ? -2.152 -4.182 27.269 1.00 24.17 ? 109 VAL A N 1 ATOM 154 C CA . VAL A 1 21 ? -1.347 -4.014 28.478 1.00 24.23 ? 109 VAL A CA 1 ATOM 155 C C . VAL A 1 21 ? -2.255 -4.118 29.719 1.00 25.65 ? 109 VAL A C 1 ATOM 156 O O . VAL A 1 21 ? -1.856 -4.701 30.709 1.00 25.46 ? 109 VAL A O 1 ATOM 157 C CB . VAL A 1 21 ? -0.597 -2.681 28.518 1.00 23.79 ? 109 VAL A CB 1 ATOM 158 C CG1 . VAL A 1 21 ? 0.110 -2.521 29.878 1.00 25.06 ? 109 VAL A CG1 1 ATOM 159 C CG2 . VAL A 1 21 ? 0.449 -2.594 27.401 1.00 21.83 ? 109 VAL A CG2 1 ATOM 160 N N . HIS A 1 22 ? -3.443 -3.527 29.677 1.00 26.38 ? 110 HIS A N 1 ATOM 161 C CA . HIS A 1 22 ? -4.262 -3.437 30.892 1.00 27.85 ? 110 HIS A CA 1 ATOM 162 C C . HIS A 1 22 ? -5.002 -4.704 31.175 1.00 28.80 ? 110 HIS A C 1 ATOM 163 O O . HIS A 1 22 ? -5.223 -5.031 32.349 1.00 29.95 ? 110 HIS A O 1 ATOM 164 C CB . HIS A 1 22 ? -5.199 -2.233 30.853 1.00 27.47 ? 110 HIS A CB 1 ATOM 165 C CG . HIS A 1 22 ? -4.552 -0.981 31.341 1.00 29.36 ? 110 HIS A CG 1 ATOM 166 N ND1 . HIS A 1 22 ? -4.421 -0.687 32.681 1.00 30.02 ? 110 HIS A ND1 1 ATOM 167 C CD2 . HIS A 1 22 ? -3.965 0.034 30.672 1.00 29.96 ? 110 HIS A CD2 1 ATOM 168 C CE1 . HIS A 1 22 ? -3.787 0.466 32.814 1.00 32.27 ? 110 HIS A CE1 1 ATOM 169 N NE2 . HIS A 1 22 ? -3.501 0.925 31.605 1.00 31.69 ? 110 HIS A NE2 1 ATOM 170 N N . THR A 1 23 ? -5.387 -5.440 30.142 1.00 30.13 ? 111 THR A N 1 ATOM 171 C CA . THR A 1 23 ? -6.208 -6.631 30.335 1.00 31.32 ? 111 THR A CA 1 ATOM 172 C C . THR A 1 23 ? -5.389 -7.920 30.347 1.00 31.17 ? 111 THR A C 1 ATOM 173 O O . THR A 1 23 ? -5.710 -8.842 31.080 1.00 31.55 ? 111 THR A O 1 ATOM 174 C CB . THR A 1 23 ? -7.404 -6.707 29.312 1.00 32.01 ? 111 THR A CB 1 ATOM 175 O OG1 . THR A 1 23 ? -6.937 -7.083 28.012 1.00 34.07 ? 111 THR A OG1 1 ATOM 176 C CG2 . THR A 1 23 ? -8.108 -5.335 29.126 1.00 32.34 ? 111 THR A CG2 1 ATOM 177 N N . LEU A 1 24 ? -4.298 -7.972 29.583 1.00 30.50 ? 112 LEU A N 1 ATOM 178 C CA . LEU A 1 24 ? -3.510 -9.200 29.466 1.00 29.86 ? 112 LEU A CA 1 ATOM 179 C C . LEU A 1 24 ? -2.217 -9.214 30.283 1.00 29.03 ? 112 LEU A C 1 ATOM 180 O O . LEU A 1 24 ? -1.772 -10.266 30.701 1.00 29.52 ? 112 LEU A O 1 ATOM 181 C CB . LEU A 1 24 ? -3.130 -9.448 28.000 1.00 30.35 ? 112 LEU A CB 1 ATOM 182 C CG . LEU A 1 24 ? -4.258 -9.373 26.961 1.00 31.74 ? 112 LEU A CG 1 ATOM 183 C CD1 . LEU A 1 24 ? -3.742 -9.829 25.606 1.00 32.62 ? 112 LEU A CD1 1 ATOM 184 C CD2 . LEU A 1 24 ? -5.453 -10.226 27.370 1.00 31.94 ? 112 LEU A CD2 1 ATOM 185 N N . ALA A 1 25 ? -1.595 -8.056 30.440 1.00 27.30 ? 113 ALA A N 1 ATOM 186 C CA . ALA A 1 25 ? -0.291 -7.977 31.069 1.00 26.69 ? 113 ALA A CA 1 ATOM 187 C C . ALA A 1 25 ? -0.384 -7.675 32.549 1.00 26.02 ? 113 ALA A C 1 ATOM 188 O O . ALA A 1 25 ? 0.203 -8.380 33.350 1.00 25.28 ? 113 ALA A O 1 ATOM 189 C CB . ALA A 1 25 ? 0.561 -6.919 30.388 1.00 26.73 ? 113 ALA A CB 1 ATOM 190 N N . ILE A 1 26 ? -1.062 -6.587 32.878 1.00 25.62 ? 114 ILE A N 1 ATOM 191 C CA . ILE A 1 26 ? -1.012 -6.044 34.225 1.00 25.48 ? 114 ILE A CA 1 ATOM 192 C C . ILE A 1 26 ? -1.508 -7.021 35.277 1.00 25.80 ? 114 ILE A C 1 ATOM 193 O O . ILE A 1 26 ? -0.905 -7.097 36.335 1.00 25.42 ? 114 ILE A O 1 ATOM 194 C CB . ILE A 1 26 ? -1.723 -4.676 34.305 1.00 24.99 ? 114 ILE A CB 1 ATOM 195 C CG1 . ILE A 1 26 ? -0.750 -3.575 33.865 1.00 25.30 ? 114 ILE A CG1 1 ATOM 196 C CG2 . ILE A 1 26 ? -2.209 -4.393 35.742 1.00 24.66 ? 114 ILE A CG2 1 ATOM 197 C CD1 . ILE A 1 26 ? -1.341 -2.239 33.688 1.00 26.79 ? 114 ILE A CD1 1 ATOM 198 N N . PRO A 1 27 ? -2.595 -7.748 35.036 1.00 26.86 ? 115 PRO A N 1 ATOM 199 C CA . PRO A 1 27 ? -3.086 -8.707 36.040 1.00 27.69 ? 115 PRO A CA 1 ATOM 200 C C . PRO A 1 27 ? -2.109 -9.834 36.380 1.00 28.73 ? 115 PRO A C 1 ATOM 201 O O . PRO A 1 27 ? -2.319 -10.515 37.380 1.00 28.79 ? 115 PRO A O 1 ATOM 202 C CB . PRO A 1 27 ? -4.354 -9.260 35.392 1.00 28.14 ? 115 PRO A CB 1 ATOM 203 C CG . PRO A 1 27 ? -4.800 -8.149 34.512 1.00 27.99 ? 115 PRO A CG 1 ATOM 204 C CD . PRO A 1 27 ? -3.505 -7.691 33.879 1.00 27.11 ? 115 PRO A CD 1 ATOM 205 N N . GLN A 1 28 ? -1.033 -9.972 35.598 1.00 29.21 ? 116 GLN A N 1 ATOM 206 C CA . GLN A 1 28 ? -0.047 -11.028 35.797 1.00 29.56 ? 116 GLN A CA 1 ATOM 207 C C . GLN A 1 28 ? 1.232 -10.564 36.517 1.00 28.42 ? 116 GLN A C 1 ATOM 208 O O . GLN A 1 28 ? 2.104 -11.364 36.860 1.00 28.96 ? 116 GLN A O 1 ATOM 209 C CB . GLN A 1 28 ? 0.291 -11.630 34.438 1.00 30.20 ? 116 GLN A CB 1 ATOM 210 C CG . GLN A 1 28 ? -0.964 -11.904 33.579 1.00 32.85 ? 116 GLN A CG 1 ATOM 211 C CD . GLN A 1 28 ? -0.863 -13.181 32.756 1.00 36.67 ? 116 GLN A CD 1 ATOM 212 O OE1 . GLN A 1 28 ? -1.181 -14.277 33.247 1.00 38.89 ? 116 GLN A OE1 1 ATOM 213 N NE2 . GLN A 1 28 ? -0.412 -13.053 31.508 1.00 38.57 ? 116 GLN A NE2 1 ATOM 214 N N . ILE A 1 29 ? 1.331 -9.278 36.782 1.00 26.57 ? 117 ILE A N 1 ATOM 215 C CA . ILE A 1 29 ? 2.535 -8.709 37.348 1.00 25.21 ? 117 ILE A CA 1 ATOM 216 C C . ILE A 1 29 ? 2.408 -8.664 38.858 1.00 24.62 ? 117 ILE A C 1 ATOM 217 O O . ILE A 1 29 ? 1.528 -8.002 39.392 1.00 22.99 ? 117 ILE A O 1 ATOM 218 C CB . ILE A 1 29 ? 2.789 -7.310 36.755 1.00 24.90 ? 117 ILE A CB 1 ATOM 219 C CG1 . ILE A 1 29 ? 3.135 -7.452 35.275 1.00 25.20 ? 117 ILE A CG1 1 ATOM 220 C CG2 . ILE A 1 29 ? 3.907 -6.617 37.495 1.00 24.52 ? 117 ILE A CG2 1 ATOM 221 C CD1 . ILE A 1 29 ? 3.065 -6.157 34.474 1.00 26.12 ? 117 ILE A CD1 1 ATOM 222 N N . THR A 1 30 ? 3.314 -9.345 39.536 1.00 24.56 ? 118 THR A N 1 ATOM 223 C CA . THR A 1 30 ? 3.284 -9.465 40.995 1.00 25.29 ? 118 THR A CA 1 ATOM 224 C C . THR A 1 30 ? 4.188 -8.478 41.691 1.00 26.74 ? 118 THR A C 1 ATOM 225 O O . THR A 1 30 ? 4.268 -8.425 42.924 1.00 27.33 ? 118 THR A O 1 ATOM 226 C CB . THR A 1 30 ? 3.730 -10.865 41.380 1.00 25.31 ? 118 THR A CB 1 ATOM 227 O OG1 . THR A 1 30 ? 5.070 -11.082 40.900 1.00 26.30 ? 118 THR A OG1 1 ATOM 228 C CG2 . THR A 1 30 ? 2.912 -11.897 40.668 1.00 24.83 ? 118 THR A CG2 1 ATOM 229 N N . ASP A 1 31 ? 4.924 -7.723 40.905 1.00 28.26 ? 119 ASP A N 1 ATOM 230 C CA . ASP A 1 31 ? 5.779 -6.714 41.435 1.00 29.55 ? 119 ASP A CA 1 ATOM 231 C C . ASP A 1 31 ? 5.012 -5.405 41.281 1.00 29.27 ? 119 ASP A C 1 ATOM 232 O O . ASP A 1 31 ? 4.640 -5.027 40.166 1.00 29.82 ? 119 ASP A O 1 ATOM 233 C CB . ASP A 1 31 ? 7.083 -6.719 40.645 1.00 30.40 ? 119 ASP A CB 1 ATOM 234 C CG . ASP A 1 31 ? 8.121 -5.799 41.216 1.00 34.01 ? 119 ASP A CG 1 ATOM 235 O OD1 . ASP A 1 31 ? 7.822 -5.006 42.132 1.00 36.56 ? 119 ASP A OD1 1 ATOM 236 O OD2 . ASP A 1 31 ? 9.295 -5.797 40.783 1.00 39.46 ? 119 ASP A OD2 1 ATOM 237 N N . PRO A 1 32 ? 4.740 -4.732 42.386 1.00 28.72 ? 120 PRO A N 1 ATOM 238 C CA . PRO A 1 32 ? 4.078 -3.421 42.391 1.00 28.42 ? 120 PRO A CA 1 ATOM 239 C C . PRO A 1 32 ? 4.748 -2.368 41.476 1.00 28.32 ? 120 PRO A C 1 ATOM 240 O O . PRO A 1 32 ? 4.064 -1.558 40.825 1.00 27.28 ? 120 PRO A O 1 ATOM 241 C CB . PRO A 1 32 ? 4.216 -2.978 43.852 1.00 28.89 ? 120 PRO A CB 1 ATOM 242 C CG . PRO A 1 32 ? 4.390 -4.181 44.578 1.00 28.36 ? 120 PRO A CG 1 ATOM 243 C CD . PRO A 1 32 ? 5.061 -5.181 43.751 1.00 28.68 ? 120 PRO A CD 1 ATOM 244 N N . ALA A 1 33 ? 6.074 -2.371 41.474 1.00 28.34 ? 121 ALA A N 1 ATOM 245 C CA . ALA A 1 33 ? 6.856 -1.484 40.614 1.00 28.13 ? 121 ALA A CA 1 ATOM 246 C C . ALA A 1 33 ? 6.696 -1.835 39.133 1.00 27.46 ? 121 ALA A C 1 ATOM 247 O O . ALA A 1 33 ? 6.553 -0.927 38.301 1.00 28.91 ? 121 ALA A O 1 ATOM 248 C CB . ALA A 1 33 ? 8.335 -1.521 41.015 1.00 28.18 ? 121 ALA A CB 1 ATOM 249 N N . LEU A 1 34 ? 6.743 -3.114 38.794 1.00 27.41 ? 122 LEU A N 1 ATOM 250 C CA . LEU A 1 34 ? 6.546 -3.549 37.413 1.00 26.46 ? 122 LEU A CA 1 ATOM 251 C C . LEU A 1 34 ? 5.129 -3.206 36.930 1.00 26.06 ? 122 LEU A C 1 ATOM 252 O O . LEU A 1 34 ? 4.926 -2.918 35.765 1.00 25.89 ? 122 LEU A O 1 ATOM 253 C CB . LEU A 1 34 ? 6.807 -5.046 37.204 1.00 27.53 ? 122 LEU A CB 1 ATOM 254 C CG . LEU A 1 34 ? 8.209 -5.625 36.962 1.00 28.63 ? 122 LEU A CG 1 ATOM 255 C CD1 . LEU A 1 34 ? 8.091 -7.105 36.540 1.00 29.76 ? 122 LEU A CD1 1 ATOM 256 C CD2 . LEU A 1 34 ? 9.000 -4.826 35.916 1.00 29.06 ? 122 LEU A CD2 1 ATOM 257 N N . ARG A 1 35 ? 4.150 -3.247 37.819 1.00 25.04 ? 123 ARG A N 1 ATOM 258 C CA . ARG A 1 35 ? 2.772 -2.949 37.446 1.00 24.45 ? 123 ARG A CA 1 ATOM 259 C C . ARG A 1 35 ? 2.581 -1.493 37.118 1.00 23.56 ? 123 ARG A C 1 ATOM 260 O O . ARG A 1 35 ? 1.883 -1.121 36.156 1.00 23.10 ? 123 ARG A O 1 ATOM 261 C CB . ARG A 1 35 ? 1.852 -3.305 38.601 1.00 24.40 ? 123 ARG A CB 1 ATOM 262 C CG . ARG A 1 35 ? 0.645 -3.921 38.164 1.00 24.47 ? 123 ARG A CG 1 ATOM 263 C CD . ARG A 1 35 ? -0.232 -4.314 39.303 1.00 20.52 ? 123 ARG A CD 1 ATOM 264 N NE . ARG A 1 35 ? -0.354 -5.768 39.383 1.00 18.52 ? 123 ARG A NE 1 ATOM 265 C CZ . ARG A 1 35 ? -1.506 -6.441 39.291 1.00 15.93 ? 123 ARG A CZ 1 ATOM 266 N NH1 . ARG A 1 35 ? -2.653 -5.803 39.099 1.00 13.31 ? 123 ARG A NH1 1 ATOM 267 N NH2 . ARG A 1 35 ? -1.499 -7.764 39.400 1.00 16.23 ? 123 ARG A NH2 1 ATOM 268 N N . ALA A 1 36 ? 3.221 -0.642 37.904 1.00 23.26 ? 124 ALA A N 1 ATOM 269 C CA . ALA A 1 36 ? 3.115 0.784 37.706 1.00 23.01 ? 124 ALA A CA 1 ATOM 270 C C . ALA A 1 36 ? 3.778 1.164 36.369 1.00 22.56 ? 124 ALA A C 1 ATOM 271 O O . ALA A 1 36 ? 3.272 2.009 35.601 1.00 22.73 ? 124 ALA A O 1 ATOM 272 C CB . ALA A 1 36 ? 3.780 1.541 38.848 1.00 23.49 ? 124 ALA A CB 1 ATOM 273 N N . ALA A 1 37 ? 4.923 0.556 36.112 1.00 22.85 ? 125 ALA A N 1 ATOM 274 C CA . ALA A 1 37 ? 5.654 0.818 34.882 1.00 22.30 ? 125 ALA A CA 1 ATOM 275 C C . ALA A 1 37 ? 4.811 0.365 33.681 1.00 22.62 ? 125 ALA A C 1 ATOM 276 O O . ALA A 1 37 ? 4.795 1.041 32.642 1.00 22.41 ? 125 ALA A O 1 ATOM 277 C CB . ALA A 1 37 ? 6.987 0.104 34.920 1.00 22.35 ? 125 ALA A CB 1 ATOM 278 N N . ALA A 1 38 ? 4.130 -0.765 33.795 1.00 21.78 ? 126 ALA A N 1 ATOM 279 C CA . ALA A 1 38 ? 3.270 -1.247 32.703 1.00 22.06 ? 126 ALA A CA 1 ATOM 280 C C . ALA A 1 38 ? 2.143 -0.275 32.382 1.00 22.31 ? 126 ALA A C 1 ATOM 281 O O . ALA A 1 38 ? 1.829 -0.027 31.209 1.00 21.26 ? 126 ALA A O 1 ATOM 282 C CB . ALA A 1 38 ? 2.732 -2.566 33.004 1.00 21.20 ? 126 ALA A CB 1 ATOM 283 N N . SER A 1 39 ? 1.531 0.305 33.397 1.00 22.24 ? 127 SER A N 1 ATOM 284 C CA . SER A 1 39 ? 0.511 1.311 33.156 1.00 23.27 ? 127 SER A CA 1 ATOM 285 C C . SER A 1 39 ? 1.058 2.518 32.390 1.00 22.74 ? 127 SER A C 1 ATOM 286 O O . SER A 1 39 ? 0.366 3.064 31.513 1.00 23.46 ? 127 SER A O 1 ATOM 287 C CB . SER A 1 39 ? -0.171 1.707 34.465 1.00 23.95 ? 127 SER A CB 1 ATOM 288 O OG . SER A 1 39 ? -0.781 0.561 35.034 1.00 26.99 ? 127 SER A OG 1 ATOM 289 N N . ALA A 1 40 ? 2.305 2.901 32.643 1.00 21.47 ? 128 ALA A N 1 ATOM 290 C CA . ALA A 1 40 ? 2.961 3.985 31.923 1.00 20.26 ? 128 ALA A CA 1 ATOM 291 C C . ALA A 1 40 ? 3.247 3.587 30.469 1.00 19.35 ? 128 ALA A C 1 ATOM 292 O O . ALA A 1 40 ? 3.024 4.397 29.548 1.00 18.85 ? 128 ALA A O 1 ATOM 293 C CB . ALA A 1 40 ? 4.245 4.360 32.608 1.00 20.47 ? 128 ALA A CB 1 ATOM 294 N N . VAL A 1 41 ? 3.683 2.360 30.261 1.00 18.16 ? 129 VAL A N 1 ATOM 295 C CA A VAL A 1 41 ? 4.025 1.886 28.907 0.55 17.74 ? 129 VAL A CA 1 ATOM 296 C CA B VAL A 1 41 ? 4.038 1.942 28.902 0.45 18.04 ? 129 VAL A CA 1 ATOM 297 C C . VAL A 1 41 ? 2.771 1.830 28.033 1.00 18.44 ? 129 VAL A C 1 ATOM 298 O O . VAL A 1 41 ? 2.818 2.039 26.816 1.00 17.84 ? 129 VAL A O 1 ATOM 299 C CB A VAL A 1 41 ? 4.710 0.515 28.970 0.55 17.67 ? 129 VAL A CB 1 ATOM 300 C CB B VAL A 1 41 ? 4.969 0.696 28.880 0.45 18.40 ? 129 VAL A CB 1 ATOM 301 C CG1 A VAL A 1 41 ? 4.884 -0.087 27.579 0.55 17.02 ? 129 VAL A CG1 1 ATOM 302 C CG1 B VAL A 1 41 ? 4.242 -0.610 29.077 0.45 18.32 ? 129 VAL A CG1 1 ATOM 303 C CG2 A VAL A 1 41 ? 6.064 0.681 29.627 0.55 17.32 ? 129 VAL A CG2 1 ATOM 304 C CG2 B VAL A 1 41 ? 5.750 0.683 27.581 0.45 17.68 ? 129 VAL A CG2 1 ATOM 305 N N . ALA A 1 42 ? 1.626 1.538 28.641 1.00 18.09 ? 130 ALA A N 1 ATOM 306 C CA . ALA A 1 42 ? 0.356 1.506 27.910 1.00 18.67 ? 130 ALA A CA 1 ATOM 307 C C . ALA A 1 42 ? 0.020 2.813 27.204 1.00 18.62 ? 130 ALA A C 1 ATOM 308 O O . ALA A 1 42 ? -0.745 2.784 26.243 1.00 20.12 ? 130 ALA A O 1 ATOM 309 C CB . ALA A 1 42 ? -0.794 1.155 28.862 1.00 18.64 ? 130 ALA A CB 1 ATOM 310 N N . GLU A 1 43 ? 0.578 3.936 27.644 1.00 17.84 ? 131 GLU A N 1 ATOM 311 C CA . GLU A 1 43 ? 0.335 5.268 27.092 1.00 19.15 ? 131 GLU A CA 1 ATOM 312 C C . GLU A 1 43 ? 1.402 5.726 26.121 1.00 16.76 ? 131 GLU A C 1 ATOM 313 O O . GLU A 1 43 ? 1.347 6.845 25.650 1.00 16.98 ? 131 GLU A O 1 ATOM 314 C CB . GLU A 1 43 ? 0.275 6.329 28.218 1.00 19.69 ? 131 GLU A CB 1 ATOM 315 C CG . GLU A 1 43 ? -0.782 6.100 29.281 1.00 23.77 ? 131 GLU A CG 1 ATOM 316 C CD . GLU A 1 43 ? -2.170 5.906 28.684 1.00 27.37 ? 131 GLU A CD 1 ATOM 317 O OE1 . GLU A 1 43 ? -2.573 6.775 27.862 1.00 30.42 ? 131 GLU A OE1 1 ATOM 318 O OE2 . GLU A 1 43 ? -2.832 4.883 29.019 1.00 29.08 ? 131 GLU A OE2 1 ATOM 319 N N . VAL A 1 44 ? 2.445 4.904 25.914 1.00 16.51 ? 132 VAL A N 1 ATOM 320 C CA . VAL A 1 44 ? 3.503 5.284 24.966 1.00 15.24 ? 132 VAL A CA 1 ATOM 321 C C . VAL A 1 44 ? 2.987 5.043 23.525 1.00 14.62 ? 132 VAL A C 1 ATOM 322 O O . VAL A 1 44 ? 2.509 3.966 23.224 1.00 14.73 ? 132 VAL A O 1 ATOM 323 C CB . VAL A 1 44 ? 4.771 4.479 25.202 1.00 16.03 ? 132 VAL A CB 1 ATOM 324 C CG1 . VAL A 1 44 ? 5.846 4.819 24.169 1.00 17.39 ? 132 VAL A CG1 1 ATOM 325 C CG2 . VAL A 1 44 ? 5.299 4.743 26.592 1.00 15.49 ? 132 VAL A CG2 1 ATOM 326 N N . PRO A 1 45 ? 3.020 6.087 22.703 1.00 13.80 ? 133 PRO A N 1 ATOM 327 C CA . PRO A 1 45 ? 2.415 5.994 21.344 1.00 13.72 ? 133 PRO A CA 1 ATOM 328 C C . PRO A 1 45 ? 3.294 5.215 20.337 1.00 13.39 ? 133 PRO A C 1 ATOM 329 O O . PRO A 1 45 ? 4.346 5.661 20.020 1.00 16.50 ? 133 PRO A O 1 ATOM 330 C CB . PRO A 1 45 ? 2.254 7.461 20.969 1.00 14.87 ? 133 PRO A CB 1 ATOM 331 C CG . PRO A 1 45 ? 3.297 8.160 21.664 1.00 15.50 ? 133 PRO A CG 1 ATOM 332 C CD . PRO A 1 45 ? 3.510 7.456 22.968 1.00 14.63 ? 133 PRO A CD 1 ATOM 333 N N . SER A 1 46 ? 2.826 4.083 19.871 1.00 12.18 ? 134 SER A N 1 ATOM 334 C CA . SER A 1 46 ? 3.526 3.300 18.863 1.00 12.18 ? 134 SER A CA 1 ATOM 335 C C . SER A 1 46 ? 2.775 3.241 17.555 1.00 10.90 ? 134 SER A C 1 ATOM 336 O O . SER A 1 46 ? 1.597 3.562 17.463 1.00 11.40 ? 134 SER A O 1 ATOM 337 C CB . SER A 1 46 ? 3.790 1.903 19.344 1.00 12.32 ? 134 SER A CB 1 ATOM 338 O OG . SER A 1 46 ? 2.616 1.279 19.863 1.00 15.90 ? 134 SER A OG 1 ATOM 339 N N . PHE A 1 47 ? 3.475 2.787 16.519 1.00 10.15 ? 135 PHE A N 1 ATOM 340 C CA . PHE A 1 47 ? 2.895 2.704 15.204 1.00 8.83 ? 135 PHE A CA 1 ATOM 341 C C . PHE A 1 47 ? 1.888 1.586 15.153 1.00 9.29 ? 135 PHE A C 1 ATOM 342 O O . PHE A 1 47 ? 2.015 0.538 15.840 1.00 10.95 ? 135 PHE A O 1 ATOM 343 C CB . PHE A 1 47 ? 3.963 2.440 14.126 1.00 8.49 ? 135 PHE A CB 1 ATOM 344 C CG . PHE A 1 47 ? 4.651 3.671 13.626 1.00 8.08 ? 135 PHE A CG 1 ATOM 345 C CD1 . PHE A 1 47 ? 5.502 4.410 14.433 1.00 8.03 ? 135 PHE A CD1 1 ATOM 346 C CD2 . PHE A 1 47 ? 4.471 4.095 12.301 1.00 7.91 ? 135 PHE A CD2 1 ATOM 347 C CE1 . PHE A 1 47 ? 6.098 5.560 13.954 1.00 9.17 ? 135 PHE A CE1 1 ATOM 348 C CE2 . PHE A 1 47 ? 5.059 5.215 11.829 1.00 7.63 ? 135 PHE A CE2 1 ATOM 349 C CZ . PHE A 1 47 ? 5.891 5.957 12.631 1.00 8.80 ? 135 PHE A CZ 1 ATOM 350 N N . GLN A 1 48 ? 0.936 1.722 14.254 1.00 8.59 ? 136 GLN A N 1 ATOM 351 C CA . GLN A 1 48 ? 0.042 0.665 13.871 1.00 8.76 ? 136 GLN A CA 1 ATOM 352 C C . GLN A 1 48 ? 0.320 0.161 12.469 1.00 8.25 ? 136 GLN A C 1 ATOM 353 O O . GLN A 1 48 ? 0.736 0.943 11.631 1.00 10.13 ? 136 GLN A O 1 ATOM 354 C CB . GLN A 1 48 ? -1.370 1.113 14.085 1.00 11.81 ? 136 GLN A CB 1 ATOM 355 C CG . GLN A 1 48 ? -1.614 1.351 15.589 1.00 14.16 ? 136 GLN A CG 1 ATOM 356 C CD . GLN A 1 48 ? -3.024 1.823 15.831 1.00 16.79 ? 136 GLN A CD 1 ATOM 357 O OE1 . GLN A 1 48 ? -3.324 2.995 15.598 1.00 20.02 ? 136 GLN A OE1 1 ATOM 358 N NE2 . GLN A 1 48 ? -3.887 0.922 16.245 1.00 19.73 ? 136 GLN A NE2 1 ATOM 359 N N . TRP A 1 49 ? 0.195 -1.146 12.245 1.00 8.24 ? 137 TRP A N 1 ATOM 360 C CA . TRP A 1 49 ? 0.703 -1.786 11.047 1.00 8.28 ? 137 TRP A CA 1 ATOM 361 C C . TRP A 1 49 ? -0.372 -2.237 10.065 1.00 8.25 ? 137 TRP A C 1 ATOM 362 O O . TRP A 1 49 ? -1.264 -2.993 10.393 1.00 8.95 ? 137 TRP A O 1 ATOM 363 C CB . TRP A 1 49 ? 1.533 -2.992 11.461 1.00 8.29 ? 137 TRP A CB 1 ATOM 364 C CG . TRP A 1 49 ? 2.800 -2.662 12.170 1.00 8.43 ? 137 TRP A CG 1 ATOM 365 C CD1 . TRP A 1 49 ? 2.985 -1.854 13.258 1.00 8.19 ? 137 TRP A CD1 1 ATOM 366 C CD2 . TRP A 1 49 ? 4.088 -3.134 11.806 1.00 9.96 ? 137 TRP A CD2 1 ATOM 367 N NE1 . TRP A 1 49 ? 4.318 -1.804 13.588 1.00 8.93 ? 137 TRP A NE1 1 ATOM 368 C CE2 . TRP A 1 49 ? 5.012 -2.606 12.735 1.00 9.87 ? 137 TRP A CE2 1 ATOM 369 C CE3 . TRP A 1 49 ? 4.554 -4.005 10.837 1.00 12.99 ? 137 TRP A CE3 1 ATOM 370 C CZ2 . TRP A 1 49 ? 6.367 -2.871 12.670 1.00 11.74 ? 137 TRP A CZ2 1 ATOM 371 C CZ3 . TRP A 1 49 ? 5.921 -4.275 10.794 1.00 15.36 ? 137 TRP A CZ3 1 ATOM 372 C CH2 . TRP A 1 49 ? 6.800 -3.716 11.714 1.00 14.21 ? 137 TRP A CH2 1 ATOM 373 N N . LEU A 1 50 ? -0.250 -1.803 8.826 1.00 7.34 ? 138 LEU A N 1 ATOM 374 C CA . LEU A 1 50 ? -1.147 -2.259 7.745 1.00 7.16 ? 138 LEU A CA 1 ATOM 375 C C . LEU A 1 50 ? -0.439 -3.354 6.980 1.00 7.82 ? 138 LEU A C 1 ATOM 376 O O . LEU A 1 50 ? -0.076 -3.241 5.814 1.00 8.89 ? 138 LEU A O 1 ATOM 377 C CB . LEU A 1 50 ? -1.545 -1.132 6.822 1.00 7.62 ? 138 LEU A CB 1 ATOM 378 C CG . LEU A 1 50 ? -2.111 0.103 7.494 1.00 8.32 ? 138 LEU A CG 1 ATOM 379 C CD1 . LEU A 1 50 ? -2.507 1.111 6.407 1.00 9.10 ? 138 LEU A CD1 1 ATOM 380 C CD2 . LEU A 1 50 ? -3.285 -0.225 8.360 1.00 10.10 ? 138 LEU A CD2 1 ATOM 381 N N . ASP A 1 51 ? -0.183 -4.445 7.668 1.00 7.88 ? 139 ASP A N 1 ATOM 382 C CA . ASP A 1 51 ? 0.623 -5.521 7.085 1.00 9.11 ? 139 ASP A CA 1 ATOM 383 C C . ASP A 1 51 ? -0.210 -6.623 6.457 1.00 8.42 ? 139 ASP A C 1 ATOM 384 O O . ASP A 1 51 ? 0.322 -7.626 5.998 1.00 9.04 ? 139 ASP A O 1 ATOM 385 C CB . ASP A 1 51 ? 1.601 -6.097 8.092 1.00 10.35 ? 139 ASP A CB 1 ATOM 386 C CG . ASP A 1 51 ? 0.933 -6.811 9.196 1.00 13.82 ? 139 ASP A CG 1 ATOM 387 O OD1 . ASP A 1 51 ? -0.220 -6.440 9.590 1.00 16.66 ? 139 ASP A OD1 1 ATOM 388 O OD2 . ASP A 1 51 ? 1.542 -7.779 9.732 1.00 16.77 ? 139 ASP A OD2 1 ATOM 389 N N . ARG A 1 52 ? -1.522 -6.459 6.472 1.00 9.53 ? 140 ARG A N 1 ATOM 390 C CA . ARG A 1 52 ? -2.475 -7.282 5.752 1.00 9.46 ? 140 ARG A CA 1 ATOM 391 C C . ARG A 1 52 ? -3.528 -6.373 5.139 1.00 8.92 ? 140 ARG A C 1 ATOM 392 O O . ARG A 1 52 ? -3.888 -5.368 5.737 1.00 9.36 ? 140 ARG A O 1 ATOM 393 C CB . ARG A 1 52 ? -3.201 -8.263 6.695 1.00 11.63 ? 140 ARG A CB 1 ATOM 394 C CG . ARG A 1 52 ? -2.326 -9.282 7.340 1.00 16.35 ? 140 ARG A CG 1 ATOM 395 C CD . ARG A 1 52 ? -3.068 -10.081 8.410 1.00 20.88 ? 140 ARG A CD 1 ATOM 396 N NE . ARG A 1 52 ? -3.617 -9.247 9.491 1.00 25.78 ? 140 ARG A NE 1 ATOM 397 C CZ . ARG A 1 52 ? -4.818 -9.405 10.070 1.00 29.92 ? 140 ARG A CZ 1 ATOM 398 N NH1 . ARG A 1 52 ? -5.668 -10.365 9.683 1.00 31.79 ? 140 ARG A NH1 1 ATOM 399 N NH2 . ARG A 1 52 ? -5.179 -8.584 11.062 1.00 31.55 ? 140 ARG A NH2 1 ATOM 400 N N . ASN A 1 53 ? -4.027 -6.702 3.977 1.00 7.97 ? 141 ASN A N 1 ATOM 401 C CA . ASN A 1 53 ? -4.991 -5.870 3.297 1.00 8.49 ? 141 ASN A CA 1 ATOM 402 C C . ASN A 1 53 ? -6.247 -5.593 4.104 1.00 7.88 ? 141 ASN A C 1 ATOM 403 O O . ASN A 1 53 ? -6.793 -4.497 4.019 1.00 8.08 ? 141 ASN A O 1 ATOM 404 C CB . ASN A 1 53 ? -5.298 -6.503 1.962 1.00 9.04 ? 141 ASN A CB 1 ATOM 405 C CG . ASN A 1 53 ? -6.190 -5.678 1.087 1.00 8.80 ? 141 ASN A CG 1 ATOM 406 O OD1 . ASN A 1 53 ? -5.939 -4.483 0.865 1.00 9.66 ? 141 ASN A OD1 1 ATOM 407 N ND2 . ASN A 1 53 ? -7.202 -6.342 0.514 1.00 9.13 ? 141 ASN A ND2 1 ATOM 408 N N . VAL A 1 54 ? -6.683 -6.549 4.914 1.00 8.37 ? 142 VAL A N 1 ATOM 409 C CA . VAL A 1 54 ? -7.898 -6.369 5.705 1.00 9.09 ? 142 VAL A CA 1 ATOM 410 C C . VAL A 1 54 ? -7.787 -5.219 6.698 1.00 8.76 ? 142 VAL A C 1 ATOM 411 O O . VAL A 1 54 ? -8.807 -4.724 7.146 1.00 9.59 ? 142 VAL A O 1 ATOM 412 C CB . VAL A 1 54 ? -8.301 -7.664 6.440 1.00 11.22 ? 142 VAL A CB 1 ATOM 413 C CG1 . VAL A 1 54 ? -7.252 -8.130 7.415 1.00 12.44 ? 142 VAL A CG1 1 ATOM 414 C CG2 . VAL A 1 54 ? -9.694 -7.543 7.072 1.00 14.31 ? 142 VAL A CG2 1 ATOM 415 N N . THR A 1 55 ? -6.581 -4.828 7.090 1.00 8.26 ? 143 THR A N 1 ATOM 416 C CA . THR A 1 55 ? -6.402 -3.714 8.015 1.00 8.77 ? 143 THR A CA 1 ATOM 417 C C . THR A 1 55 ? -6.812 -2.366 7.458 1.00 7.44 ? 143 THR A C 1 ATOM 418 O O . THR A 1 55 ? -7.085 -1.460 8.232 1.00 8.52 ? 143 THR A O 1 ATOM 419 C CB . THR A 1 55 ? -4.941 -3.585 8.508 1.00 8.86 ? 143 THR A CB 1 ATOM 420 O OG1 . THR A 1 55 ? -4.087 -3.267 7.392 1.00 9.53 ? 143 THR A OG1 1 ATOM 421 C CG2 . THR A 1 55 ? -4.464 -4.851 9.198 1.00 10.85 ? 143 THR A CG2 1 ATOM 422 N N . VAL A 1 56 ? -6.822 -2.212 6.143 1.00 7.37 ? 144 VAL A N 1 ATOM 423 C CA . VAL A 1 56 ? -7.083 -0.900 5.547 1.00 8.24 ? 144 VAL A CA 1 ATOM 424 C C . VAL A 1 56 ? -8.466 -0.368 5.910 1.00 8.44 ? 144 VAL A C 1 ATOM 425 O O . VAL A 1 56 ? -8.594 0.760 6.372 1.00 8.79 ? 144 VAL A O 1 ATOM 426 C CB . VAL A 1 56 ? -6.848 -0.941 4.052 1.00 8.26 ? 144 VAL A CB 1 ATOM 427 C CG1 . VAL A 1 56 ? -7.237 0.349 3.381 1.00 9.30 ? 144 VAL A CG1 1 ATOM 428 C CG2 . VAL A 1 56 ? -5.370 -1.289 3.733 1.00 7.90 ? 144 VAL A CG2 1 ATOM 429 N N . ASP A 1 57 ? -9.506 -1.184 5.701 1.00 8.36 ? 145 ASP A N 1 ATOM 430 C CA . ASP A 1 57 ? -10.898 -0.785 5.946 1.00 9.43 ? 145 ASP A CA 1 ATOM 431 C C . ASP A 1 57 ? -11.331 -1.070 7.395 1.00 9.58 ? 145 ASP A C 1 ATOM 432 O O . ASP A 1 57 ? -12.505 -0.919 7.718 1.00 10.65 ? 145 ASP A O 1 ATOM 433 C CB . ASP A 1 57 ? -11.865 -1.472 4.975 1.00 10.65 ? 145 ASP A CB 1 ATOM 434 C CG . ASP A 1 57 ? -11.894 -0.833 3.630 1.00 11.48 ? 145 ASP A CG 1 ATOM 435 O OD1 . ASP A 1 57 ? -11.577 0.354 3.523 1.00 14.32 ? 145 ASP A OD1 1 ATOM 436 O OD2 . ASP A 1 57 ? -12.253 -1.462 2.604 1.00 15.22 ? 145 ASP A OD2 1 ATOM 437 N N . THR A 1 58 ? -10.390 -1.416 8.263 1.00 8.79 ? 146 THR A N 1 ATOM 438 C CA . THR A 1 58 ? -10.673 -1.708 9.641 1.00 8.98 ? 146 THR A CA 1 ATOM 439 C C . THR A 1 58 ? -9.793 -0.850 10.492 1.00 9.36 ? 146 THR A C 1 ATOM 440 O O . THR A 1 58 ? -10.200 0.254 10.842 1.00 10.35 ? 146 THR A O 1 ATOM 441 C CB . THR A 1 58 ? -10.574 -3.231 9.942 1.00 9.24 ? 146 THR A CB 1 ATOM 442 O OG1 . THR A 1 58 ? -9.253 -3.758 9.645 1.00 9.78 ? 146 THR A OG1 1 ATOM 443 C CG2 . THR A 1 58 ? -11.553 -4.021 9.104 1.00 9.38 ? 146 THR A CG2 1 ATOM 444 N N . LEU A 1 59 ? -8.606 -1.324 10.822 1.00 9.20 ? 147 LEU A N 1 ATOM 445 C CA . LEU A 1 59 ? -7.715 -0.623 11.706 1.00 10.11 ? 147 LEU A CA 1 ATOM 446 C C . LEU A 1 59 ? -7.426 0.813 11.289 1.00 8.57 ? 147 LEU A C 1 ATOM 447 O O . LEU A 1 59 ? -7.440 1.720 12.112 1.00 8.96 ? 147 LEU A O 1 ATOM 448 C CB . LEU A 1 59 ? -6.395 -1.399 11.768 1.00 12.21 ? 147 LEU A CB 1 ATOM 449 C CG . LEU A 1 59 ? -5.319 -0.932 12.737 1.00 15.77 ? 147 LEU A CG 1 ATOM 450 C CD1 . LEU A 1 59 ? -5.817 -1.009 14.158 1.00 21.49 ? 147 LEU A CD1 1 ATOM 451 C CD2 . LEU A 1 59 ? -4.075 -1.812 12.540 1.00 17.58 ? 147 LEU A CD2 1 ATOM 452 N N . LEU A 1 60 ? -7.142 1.038 10.013 1.00 8.44 ? 148 LEU A N 1 ATOM 453 C CA . LEU A 1 60 ? -6.758 2.397 9.624 1.00 8.50 ? 148 LEU A CA 1 ATOM 454 C C . LEU A 1 60 ? -7.912 3.357 9.866 1.00 8.04 ? 148 LEU A C 1 ATOM 455 O O . LEU A 1 60 ? -7.747 4.407 10.408 1.00 9.33 ? 148 LEU A O 1 ATOM 456 C CB . LEU A 1 60 ? -6.343 2.429 8.169 1.00 8.42 ? 148 LEU A CB 1 ATOM 457 C CG . LEU A 1 60 ? -5.974 3.780 7.579 1.00 8.46 ? 148 LEU A CG 1 ATOM 458 C CD1 . LEU A 1 60 ? -4.768 4.372 8.281 1.00 8.65 ? 148 LEU A CD1 1 ATOM 459 C CD2 . LEU A 1 60 ? -5.694 3.657 6.081 1.00 8.87 ? 148 LEU A CD2 1 ATOM 460 N N . VAL A 1 61 ? -9.105 2.993 9.414 1.00 8.34 ? 149 VAL A N 1 ATOM 461 C CA . VAL A 1 61 ? -10.288 3.815 9.593 1.00 8.58 ? 149 VAL A CA 1 ATOM 462 C C . VAL A 1 61 ? -10.621 4.024 11.062 1.00 9.42 ? 149 VAL A C 1 ATOM 463 O O . VAL A 1 61 ? -10.908 5.138 11.510 1.00 9.99 ? 149 VAL A O 1 ATOM 464 C CB . VAL A 1 61 ? -11.505 3.217 8.844 1.00 8.51 ? 149 VAL A CB 1 ATOM 465 C CG1 . VAL A 1 61 ? -12.805 3.983 9.169 1.00 9.22 ? 149 VAL A CG1 1 ATOM 466 C CG2 . VAL A 1 61 ? -11.248 3.134 7.370 1.00 9.79 ? 149 VAL A CG2 1 ATOM 467 N N . GLN A 1 62 ? -10.547 2.955 11.838 1.00 10.24 ? 150 GLN A N 1 ATOM 468 C CA . GLN A 1 62 ? -10.831 3.071 13.257 1.00 11.24 ? 150 GLN A CA 1 ATOM 469 C C . GLN A 1 62 ? -9.861 4.045 13.941 1.00 11.09 ? 150 GLN A C 1 ATOM 470 O O . GLN A 1 62 ? -10.262 4.865 14.744 1.00 11.79 ? 150 GLN A O 1 ATOM 471 C CB . GLN A 1 62 ? -10.788 1.700 13.905 1.00 12.52 ? 150 GLN A CB 1 ATOM 472 C CG . GLN A 1 62 ? -11.151 1.723 15.390 1.00 17.64 ? 150 GLN A CG 1 ATOM 473 C CD . GLN A 1 62 ? -11.816 0.448 15.908 1.00 23.15 ? 150 GLN A CD 1 ATOM 474 O OE1 . GLN A 1 62 ? -12.230 -0.418 15.133 1.00 27.01 ? 150 GLN A OE1 1 ATOM 475 N NE2 . GLN A 1 62 ? -11.941 0.347 17.231 1.00 26.17 ? 150 GLN A NE2 1 ATOM 476 N N . THR A 1 63 ? -8.577 3.929 13.636 1.00 10.80 ? 151 THR A N 1 ATOM 477 C CA . THR A 1 63 ? -7.575 4.753 14.285 1.00 11.71 ? 151 THR A CA 1 ATOM 478 C C . THR A 1 63 ? -7.797 6.217 13.920 1.00 9.99 ? 151 THR A C 1 ATOM 479 O O . THR A 1 63 ? -7.803 7.084 14.778 1.00 9.93 ? 151 THR A O 1 ATOM 480 C CB . THR A 1 63 ? -6.204 4.293 13.798 1.00 12.79 ? 151 THR A CB 1 ATOM 481 O OG1 . THR A 1 63 ? -5.941 2.982 14.357 1.00 16.78 ? 151 THR A OG1 1 ATOM 482 C CG2 . THR A 1 63 ? -5.063 5.238 14.227 1.00 15.72 ? 151 THR A CG2 1 ATOM 483 N N . LEU A 1 64 ? -7.954 6.506 12.641 1.00 9.00 ? 152 LEU A N 1 ATOM 484 C CA . LEU A 1 64 ? -8.123 7.872 12.204 1.00 8.79 ? 152 LEU A CA 1 ATOM 485 C C . LEU A 1 64 ? -9.425 8.478 12.763 1.00 9.16 ? 152 LEU A C 1 ATOM 486 O O . LEU A 1 64 ? -9.436 9.647 13.172 1.00 9.39 ? 152 LEU A O 1 ATOM 487 C CB . LEU A 1 64 ? -8.077 7.959 10.694 1.00 8.52 ? 152 LEU A CB 1 ATOM 488 C CG . LEU A 1 64 ? -6.741 7.578 10.088 1.00 9.13 ? 152 LEU A CG 1 ATOM 489 C CD1 . LEU A 1 64 ? -6.877 7.450 8.569 1.00 9.59 ? 152 LEU A CD1 1 ATOM 490 C CD2 . LEU A 1 64 ? -5.622 8.552 10.434 1.00 10.86 ? 152 LEU A CD2 1 ATOM 491 N N . SER A 1 65 ? -10.483 7.693 12.862 1.00 9.84 ? 153 SER A N 1 ATOM 492 C CA A SER A 1 65 ? -11.727 8.162 13.487 0.60 11.07 ? 153 SER A CA 1 ATOM 493 C CA B SER A 1 65 ? -11.728 8.157 13.475 0.40 10.63 ? 153 SER A CA 1 ATOM 494 C C . SER A 1 65 ? -11.553 8.485 14.961 1.00 11.49 ? 153 SER A C 1 ATOM 495 O O . SER A 1 65 ? -12.054 9.506 15.449 1.00 12.36 ? 153 SER A O 1 ATOM 496 C CB A SER A 1 65 ? -12.828 7.125 13.315 0.60 11.50 ? 153 SER A CB 1 ATOM 497 C CB B SER A 1 65 ? -12.821 7.107 13.276 0.40 10.63 ? 153 SER A CB 1 ATOM 498 O OG A SER A 1 65 ? -14.016 7.544 13.979 0.60 15.25 ? 153 SER A OG 1 ATOM 499 O OG B SER A 1 65 ? -13.133 6.936 11.901 0.40 10.31 ? 153 SER A OG 1 ATOM 500 N N . GLU A 1 66 ? -10.860 7.642 15.694 1.00 11.99 ? 154 GLU A N 1 ATOM 501 C CA . GLU A 1 66 ? -10.611 7.906 17.104 1.00 12.76 ? 154 GLU A CA 1 ATOM 502 C C . GLU A 1 66 ? -9.759 9.138 17.329 1.00 11.78 ? 154 GLU A C 1 ATOM 503 O O . GLU A 1 66 ? -10.027 9.938 18.225 1.00 13.22 ? 154 GLU A O 1 ATOM 504 C CB . GLU A 1 66 ? -9.982 6.685 17.762 1.00 14.70 ? 154 GLU A CB 1 ATOM 505 C CG . GLU A 1 66 ? -10.958 5.521 17.864 1.00 18.09 ? 154 GLU A CG 1 ATOM 506 C CD . GLU A 1 66 ? -10.431 4.291 18.595 1.00 25.83 ? 154 GLU A CD 1 ATOM 507 O OE1 . GLU A 1 66 ? -9.314 4.339 19.186 1.00 30.36 ? 154 GLU A OE1 1 ATOM 508 O OE2 . GLU A 1 66 ? -11.160 3.270 18.601 1.00 29.54 ? 154 GLU A OE2 1 ATOM 509 N N . ILE A 1 67 ? -8.758 9.348 16.484 1.00 10.75 ? 155 ILE A N 1 ATOM 510 C CA . ILE A 1 67 ? -7.952 10.554 16.592 1.00 10.22 ? 155 ILE A CA 1 ATOM 511 C C . ILE A 1 67 ? -8.758 11.805 16.253 1.00 10.45 ? 155 ILE A C 1 ATOM 512 O O . ILE A 1 67 ? -8.694 12.808 16.954 1.00 11.29 ? 155 ILE A O 1 ATOM 513 C CB . ILE A 1 67 ? -6.693 10.459 15.667 1.00 9.65 ? 155 ILE A CB 1 ATOM 514 C CG1 . ILE A 1 67 ? -5.790 9.387 16.185 1.00 10.03 ? 155 ILE A CG1 1 ATOM 515 C CG2 . ILE A 1 67 ? -5.960 11.778 15.595 1.00 10.49 ? 155 ILE A CG2 1 ATOM 516 C CD1 . ILE A 1 67 ? -4.709 8.970 15.239 1.00 10.91 ? 155 ILE A CD1 1 ATOM 517 N N . ARG A 1 68 ? -9.556 11.735 15.210 1.00 10.23 ? 156 ARG A N 1 ATOM 518 C CA . ARG A 1 68 ? -10.389 12.860 14.848 1.00 10.98 ? 156 ARG A CA 1 ATOM 519 C C . ARG A 1 68 ? -11.284 13.240 16.039 1.00 12.16 ? 156 ARG A C 1 ATOM 520 O O . ARG A 1 68 ? -11.434 14.415 16.377 1.00 12.11 ? 156 ARG A O 1 ATOM 521 C CB . ARG A 1 68 ? -11.261 12.514 13.644 1.00 10.50 ? 156 ARG A CB 1 ATOM 522 C CG . ARG A 1 68 ? -12.334 13.526 13.382 1.00 12.64 ? 156 ARG A CG 1 ATOM 523 C CD . ARG A 1 68 ? -13.163 13.166 12.236 1.00 13.18 ? 156 ARG A CD 1 ATOM 524 N NE . ARG A 1 68 ? -12.472 13.440 10.986 1.00 13.10 ? 156 ARG A NE 1 ATOM 525 C CZ . ARG A 1 68 ? -12.818 12.942 9.813 1.00 12.99 ? 156 ARG A CZ 1 ATOM 526 N NH1 . ARG A 1 68 ? -13.783 12.055 9.701 1.00 13.22 ? 156 ARG A NH1 1 ATOM 527 N NH2 . ARG A 1 68 ? -12.155 13.292 8.728 1.00 11.52 ? 156 ARG A NH2 1 ATOM 528 N N . GLU A 1 69 ? -11.887 12.248 16.661 1.00 12.58 ? 157 GLU A N 1 ATOM 529 C CA . GLU A 1 69 ? -12.786 12.520 17.801 1.00 14.22 ? 157 GLU A CA 1 ATOM 530 C C . GLU A 1 69 ? -12.020 13.196 18.946 1.00 14.18 ? 157 GLU A C 1 ATOM 531 O O . GLU A 1 69 ? -12.483 14.168 19.517 1.00 15.20 ? 157 GLU A O 1 ATOM 532 C CB . GLU A 1 69 ? -13.348 11.192 18.297 1.00 15.96 ? 157 GLU A CB 1 ATOM 533 C CG . GLU A 1 69 ? -14.266 11.288 19.498 1.00 21.21 ? 157 GLU A CG 1 ATOM 534 C CD . GLU A 1 69 ? -15.713 10.948 19.204 0.50 24.68 ? 157 GLU A CD 1 ATOM 535 O OE1 . GLU A 1 69 ? -16.363 11.735 18.476 0.50 26.81 ? 157 GLU A OE1 1 ATOM 536 O OE2 . GLU A 1 69 ? -16.199 9.907 19.712 0.50 25.76 ? 157 GLU A OE2 1 ATOM 537 N N . ALA A 1 70 ? -10.837 12.689 19.272 1.00 13.67 ? 158 ALA A N 1 ATOM 538 C CA . ALA A 1 70 ? -10.022 13.295 20.334 1.00 13.82 ? 158 ALA A CA 1 ATOM 539 C C . ALA A 1 70 ? -9.651 14.735 19.991 1.00 14.50 ? 158 ALA A C 1 ATOM 540 O O . ALA A 1 70 ? -9.701 15.640 20.842 1.00 15.48 ? 158 ALA A O 1 ATOM 541 C CB . ALA A 1 70 ? -8.803 12.452 20.597 1.00 14.69 ? 158 ALA A CB 1 ATOM 542 N N . ASN A 1 71 ? -9.296 14.984 18.731 1.00 12.87 ? 159 ASN A N 1 ATOM 543 C CA . ASN A 1 71 ? -8.925 16.316 18.305 1.00 13.52 ? 159 ASN A CA 1 ATOM 544 C C . ASN A 1 71 ? -10.078 17.296 18.306 1.00 15.05 ? 159 ASN A C 1 ATOM 545 O O . ASN A 1 71 ? -9.922 18.459 18.721 1.00 16.27 ? 159 ASN A O 1 ATOM 546 C CB . ASN A 1 71 ? -8.272 16.265 16.929 1.00 12.77 ? 159 ASN A CB 1 ATOM 547 C CG . ASN A 1 71 ? -6.885 15.711 16.967 1.00 12.36 ? 159 ASN A CG 1 ATOM 548 O OD1 . ASN A 1 71 ? -6.269 15.620 18.024 1.00 13.12 ? 159 ASN A OD1 1 ATOM 549 N ND2 . ASN A 1 71 ? -6.373 15.325 15.791 1.00 12.95 ? 159 ASN A ND2 1 ATOM 550 N N . GLN A 1 72 ? -11.257 16.828 17.912 1.00 15.83 ? 160 GLN A N 1 ATOM 551 C CA . GLN A 1 72 ? -12.438 17.677 17.888 1.00 17.30 ? 160 GLN A CA 1 ATOM 552 C C . GLN A 1 72 ? -12.888 17.964 19.306 1.00 18.21 ? 160 GLN A C 1 ATOM 553 O O . GLN A 1 72 ? -13.531 18.981 19.539 1.00 20.45 ? 160 GLN A O 1 ATOM 554 C CB . GLN A 1 72 ? -13.561 17.034 17.075 1.00 16.69 ? 160 GLN A CB 1 ATOM 555 C CG . GLN A 1 72 ? -13.271 17.063 15.566 1.00 18.60 ? 160 GLN A CG 1 ATOM 556 C CD . GLN A 1 72 ? -14.282 16.322 14.729 1.00 22.87 ? 160 GLN A CD 1 ATOM 557 O OE1 . GLN A 1 72 ? -14.953 15.419 15.214 1.00 27.18 ? 160 GLN A OE1 1 ATOM 558 N NE2 . GLN A 1 72 ? -14.330 16.648 13.439 1.00 24.09 ? 160 GLN A NE2 1 ATOM 559 N N . ALA A 1 73 ? -12.565 17.089 20.247 1.00 19.90 ? 161 ALA A N 1 ATOM 560 C CA . ALA A 1 73 ? -12.908 17.308 21.655 1.00 21.72 ? 161 ALA A CA 1 ATOM 561 C C . ALA A 1 73 ? -11.955 18.310 22.336 1.00 23.17 ? 161 ALA A C 1 ATOM 562 O O . ALA A 1 73 ? -12.148 18.646 23.506 1.00 25.21 ? 161 ALA A O 1 ATOM 563 C CB . ALA A 1 73 ? -12.890 15.998 22.401 1.00 22.02 ? 161 ALA A CB 1 ATOM 564 N N . GLY A 1 74 ? -10.895 18.730 21.657 1.00 24.20 ? 162 GLY A N 1 ATOM 565 C CA . GLY A 1 74 ? -10.024 19.789 22.155 1.00 24.21 ? 162 GLY A CA 1 ATOM 566 C C . GLY A 1 74 ? -8.599 19.384 22.503 1.00 24.70 ? 162 GLY A C 1 ATOM 567 O O . GLY A 1 74 ? -7.913 20.154 23.176 1.00 25.31 ? 162 GLY A O 1 ATOM 568 N N . ALA A 1 75 ? -8.119 18.221 22.060 1.00 23.98 ? 163 ALA A N 1 ATOM 569 C CA . ALA A 1 75 ? -6.733 17.817 22.354 1.00 23.77 ? 163 ALA A CA 1 ATOM 570 C C . ALA A 1 75 ? -5.746 18.940 22.017 1.00 23.76 ? 163 ALA A C 1 ATOM 571 O O . ALA A 1 75 ? -5.844 19.606 20.971 1.00 22.84 ? 163 ALA A O 1 ATOM 572 C CB . ALA A 1 75 ? -6.364 16.550 21.615 1.00 23.73 ? 163 ALA A CB 1 ATOM 573 N N . ASN A 1 76 ? -4.811 19.163 22.939 1.00 23.94 ? 164 ASN A N 1 ATOM 574 C CA . ASN A 1 76 ? -3.831 20.231 22.793 1.00 24.74 ? 164 ASN A CA 1 ATOM 575 C C . ASN A 1 76 ? -2.482 19.764 23.297 1.00 24.49 ? 164 ASN A C 1 ATOM 576 O O . ASN A 1 76 ? -2.342 19.487 24.487 1.00 25.83 ? 164 ASN A O 1 ATOM 577 C CB . ASN A 1 76 ? -4.251 21.484 23.584 1.00 25.19 ? 164 ASN A CB 1 ATOM 578 C CG . ASN A 1 76 ? -3.293 22.631 23.377 1.00 27.52 ? 164 ASN A CG 1 ATOM 579 O OD1 . ASN A 1 76 ? -2.796 22.858 22.261 1.00 28.83 ? 164 ASN A OD1 1 ATOM 580 N ND2 . ASN A 1 76 ? -3.029 23.383 24.448 1.00 30.39 ? 164 ASN A ND2 1 ATOM 581 N N . PRO A 1 77 ? -1.497 19.600 22.405 1.00 22.62 ? 165 PRO A N 1 ATOM 582 C CA . PRO A 1 77 ? -1.647 19.810 20.958 1.00 20.79 ? 165 PRO A CA 1 ATOM 583 C C . PRO A 1 77 ? -2.467 18.697 20.265 1.00 17.21 ? 165 PRO A C 1 ATOM 584 O O . PRO A 1 77 ? -2.745 17.669 20.883 1.00 17.68 ? 165 PRO A O 1 ATOM 585 C CB . PRO A 1 77 ? -0.191 19.783 20.451 1.00 21.19 ? 165 PRO A CB 1 ATOM 586 C CG . PRO A 1 77 ? 0.499 18.955 21.362 1.00 23.31 ? 165 PRO A CG 1 ATOM 587 C CD . PRO A 1 77 ? -0.131 19.172 22.756 1.00 23.64 ? 165 PRO A CD 1 ATOM 588 N N . GLN A 1 78 ? -2.799 18.896 18.998 1.00 16.49 ? 166 GLN A N 1 ATOM 589 C CA . GLN A 1 78 ? -3.537 17.847 18.262 1.00 15.21 ? 166 GLN A CA 1 ATOM 590 C C . GLN A 1 78 ? -2.753 16.528 18.169 1.00 13.37 ? 166 GLN A C 1 ATOM 591 O O . GLN A 1 78 ? -1.531 16.504 18.194 1.00 12.70 ? 166 GLN A O 1 ATOM 592 C CB . GLN A 1 78 ? -3.930 18.313 16.863 1.00 15.86 ? 166 GLN A CB 1 ATOM 593 C CG . GLN A 1 78 ? -4.783 19.611 16.804 1.00 19.55 ? 166 GLN A CG 1 ATOM 594 C CD . GLN A 1 78 ? -6.291 19.351 16.863 1.00 20.64 ? 166 GLN A CD 1 ATOM 595 O OE1 . GLN A 1 78 ? -6.913 19.024 15.826 1.00 21.68 ? 166 GLN A OE1 1 ATOM 596 N NE2 . GLN A 1 78 ? -6.887 19.472 18.079 1.00 23.32 ? 166 GLN A NE2 1 ATOM 597 N N . TYR A 1 79 ? -3.481 15.429 18.139 1.00 11.44 ? 167 TYR A N 1 ATOM 598 C CA . TYR A 1 79 ? -2.897 14.121 17.941 1.00 11.49 ? 167 TYR A CA 1 ATOM 599 C C . TYR A 1 79 ? -2.632 13.832 16.444 1.00 10.75 ? 167 TYR A C 1 ATOM 600 O O . TYR A 1 79 ? -3.429 14.230 15.573 1.00 10.02 ? 167 TYR A O 1 ATOM 601 C CB . TYR A 1 79 ? -3.811 13.048 18.456 1.00 12.59 ? 167 TYR A CB 1 ATOM 602 C CG . TYR A 1 79 ? -3.874 12.946 19.952 1.00 16.11 ? 167 TYR A CG 1 ATOM 603 C CD1 . TYR A 1 79 ? -2.912 12.243 20.638 1.00 18.46 ? 167 TYR A CD1 1 ATOM 604 C CD2 . TYR A 1 79 ? -4.947 13.477 20.654 1.00 18.72 ? 167 TYR A CD2 1 ATOM 605 C CE1 . TYR A 1 79 ? -2.978 12.101 22.027 1.00 21.41 ? 167 TYR A CE1 1 ATOM 606 C CE2 . TYR A 1 79 ? -5.021 13.361 22.049 1.00 21.37 ? 167 TYR A CE2 1 ATOM 607 C CZ . TYR A 1 79 ? -4.038 12.655 22.704 1.00 21.72 ? 167 TYR A CZ 1 ATOM 608 O OH . TYR A 1 79 ? -4.084 12.542 24.086 1.00 24.70 ? 167 TYR A OH 1 ATOM 609 N N . ALA A 1 80 ? -1.530 13.126 16.198 1.00 10.14 ? 168 ALA A N 1 ATOM 610 C CA . ALA A 1 80 ? -1.141 12.602 14.879 1.00 9.05 ? 168 ALA A CA 1 ATOM 611 C C . ALA A 1 80 ? -1.152 11.086 14.909 1.00 8.45 ? 168 ALA A C 1 ATOM 612 O O . ALA A 1 80 ? -0.884 10.469 15.930 1.00 9.59 ? 168 ALA A O 1 ATOM 613 C CB . ALA A 1 80 ? 0.213 13.092 14.487 1.00 9.96 ? 168 ALA A CB 1 ATOM 614 N N . ALA A 1 81 ? -1.410 10.483 13.745 1.00 7.91 ? 169 ALA A N 1 ATOM 615 C CA . ALA A 1 81 ? -1.357 9.056 13.514 1.00 8.13 ? 169 ALA A CA 1 ATOM 616 C C . ALA A 1 81 ? -0.001 8.578 13.031 1.00 7.73 ? 169 ALA A C 1 ATOM 617 O O . ALA A 1 81 ? 0.703 9.306 12.321 1.00 8.00 ? 169 ALA A O 1 ATOM 618 C CB . ALA A 1 81 ? -2.407 8.667 12.486 1.00 8.73 ? 169 ALA A CB 1 ATOM 619 N N . GLN A 1 82 ? 0.343 7.334 13.372 1.00 7.34 ? 170 GLN A N 1 ATOM 620 C CA . GLN A 1 82 ? 1.592 6.693 12.979 1.00 7.00 ? 170 GLN A CA 1 ATOM 621 C C . GLN A 1 82 ? 1.250 5.324 12.394 1.00 7.07 ? 170 GLN A C 1 ATOM 622 O O . GLN A 1 82 ? 0.745 4.439 13.084 1.00 7.70 ? 170 GLN A O 1 ATOM 623 C CB . GLN A 1 82 ? 2.500 6.511 14.183 1.00 7.63 ? 170 GLN A CB 1 ATOM 624 C CG . GLN A 1 82 ? 3.030 7.779 14.808 1.00 8.93 ? 170 GLN A CG 1 ATOM 625 C CD . GLN A 1 82 ? 3.809 7.488 16.062 1.00 10.45 ? 170 GLN A CD 1 ATOM 626 O OE1 . GLN A 1 82 ? 5.034 7.641 16.084 1.00 11.13 ? 170 GLN A OE1 1 ATOM 627 N NE2 . GLN A 1 82 ? 3.123 7.050 17.078 1.00 12.23 ? 170 GLN A NE2 1 ATOM 628 N N . ILE A 1 83 ? 1.494 5.149 11.110 1.00 7.32 ? 171 ILE A N 1 ATOM 629 C CA . ILE A 1 83 ? 1.060 3.947 10.377 1.00 6.77 ? 171 ILE A CA 1 ATOM 630 C C . ILE A 1 83 ? 2.194 3.366 9.564 1.00 6.33 ? 171 ILE A C 1 ATOM 631 O O . ILE A 1 83 ? 2.952 4.083 8.934 1.00 7.40 ? 171 ILE A O 1 ATOM 632 C CB . ILE A 1 83 ? -0.128 4.324 9.450 1.00 8.21 ? 171 ILE A CB 1 ATOM 633 C CG1 . ILE A 1 83 ? -1.314 4.911 10.240 1.00 10.65 ? 171 ILE A CG1 1 ATOM 634 C CG2 . ILE A 1 83 ? -0.511 3.200 8.529 1.00 9.81 ? 171 ILE A CG2 1 ATOM 635 C CD1 . ILE A 1 83 ? -2.075 3.950 11.063 1.00 14.20 ? 171 ILE A CD1 1 ATOM 636 N N . VAL A 1 84 ? 2.307 2.034 9.549 1.00 6.15 ? 172 VAL A N 1 ATOM 637 C CA . VAL A 1 84 ? 3.233 1.320 8.697 1.00 6.52 ? 172 VAL A CA 1 ATOM 638 C C . VAL A 1 84 ? 2.492 0.713 7.516 1.00 6.10 ? 172 VAL A C 1 ATOM 639 O O . VAL A 1 84 ? 1.500 0.042 7.691 1.00 7.13 ? 172 VAL A O 1 ATOM 640 C CB . VAL A 1 84 ? 3.947 0.145 9.445 1.00 7.42 ? 172 VAL A CB 1 ATOM 641 C CG1 . VAL A 1 84 ? 5.002 -0.453 8.553 1.00 8.27 ? 172 VAL A CG1 1 ATOM 642 C CG2 . VAL A 1 84 ? 4.569 0.643 10.708 1.00 7.51 ? 172 VAL A CG2 1 ATOM 643 N N . VAL A 1 85 ? 2.980 0.970 6.300 1.00 6.06 ? 173 VAL A N 1 ATOM 644 C CA . VAL A 1 85 ? 2.445 0.382 5.058 1.00 6.50 ? 173 VAL A CA 1 ATOM 645 C C . VAL A 1 85 ? 3.369 -0.779 4.722 1.00 6.29 ? 173 VAL A C 1 ATOM 646 O O . VAL A 1 85 ? 4.564 -0.590 4.563 1.00 7.99 ? 173 VAL A O 1 ATOM 647 C CB . VAL A 1 85 ? 2.457 1.415 3.917 1.00 7.19 ? 173 VAL A CB 1 ATOM 648 C CG1 . VAL A 1 85 ? 2.013 0.807 2.623 1.00 8.52 ? 173 VAL A CG1 1 ATOM 649 C CG2 . VAL A 1 85 ? 1.578 2.610 4.311 1.00 7.95 ? 173 VAL A CG2 1 ATOM 650 N N . TYR A 1 86 ? 2.864 -2.014 4.698 1.00 6.70 ? 174 TYR A N 1 ATOM 651 C CA . TYR A 1 86 ? 3.712 -3.192 4.635 1.00 7.81 ? 174 TYR A CA 1 ATOM 652 C C . TYR A 1 86 ? 2.982 -4.336 3.963 1.00 7.88 ? 174 TYR A C 1 ATOM 653 O O . TYR A 1 86 ? 2.621 -5.336 4.593 1.00 8.11 ? 174 TYR A O 1 ATOM 654 C CB . TYR A 1 86 ? 4.149 -3.577 6.041 1.00 8.11 ? 174 TYR A CB 1 ATOM 655 C CG . TYR A 1 86 ? 5.191 -4.669 6.167 1.00 8.20 ? 174 TYR A CG 1 ATOM 656 C CD1 . TYR A 1 86 ? 6.115 -4.942 5.192 1.00 8.63 ? 174 TYR A CD1 1 ATOM 657 C CD2 . TYR A 1 86 ? 5.230 -5.451 7.290 1.00 11.28 ? 174 TYR A CD2 1 ATOM 658 C CE1 . TYR A 1 86 ? 7.076 -5.946 5.378 1.00 10.06 ? 174 TYR A CE1 1 ATOM 659 C CE2 . TYR A 1 86 ? 6.165 -6.449 7.467 1.00 13.53 ? 174 TYR A CE2 1 ATOM 660 C CZ . TYR A 1 86 ? 7.082 -6.680 6.507 1.00 11.69 ? 174 TYR A CZ 1 ATOM 661 O OH . TYR A 1 86 ? 7.986 -7.712 6.728 1.00 14.29 ? 174 TYR A OH 1 ATOM 662 N N . ASP A 1 87 ? 2.867 -4.266 2.645 1.00 7.34 ? 175 ASP A N 1 ATOM 663 C CA . ASP A 1 87 ? 2.240 -5.360 1.934 1.00 7.33 ? 175 ASP A CA 1 ATOM 664 C C . ASP A 1 87 ? 2.700 -5.534 0.487 1.00 6.60 ? 175 ASP A C 1 ATOM 665 O O . ASP A 1 87 ? 1.935 -5.998 -0.373 1.00 7.36 ? 175 ASP A O 1 ATOM 666 C CB . ASP A 1 87 ? 0.733 -5.252 2.039 1.00 7.96 ? 175 ASP A CB 1 ATOM 667 C CG . ASP A 1 87 ? 0.021 -6.588 2.033 1.00 8.27 ? 175 ASP A CG 1 ATOM 668 O OD1 . ASP A 1 87 ? 0.629 -7.687 2.027 1.00 9.39 ? 175 ASP A OD1 1 ATOM 669 O OD2 . ASP A 1 87 ? -1.256 -6.562 2.031 1.00 10.13 ? 175 ASP A OD2 1 ATOM 670 N N . LEU A 1 88 ? 3.972 -5.246 0.199 1.00 6.92 ? 176 LEU A N 1 ATOM 671 C CA . LEU A 1 88 ? 4.465 -5.475 -1.157 1.00 6.20 ? 176 LEU A CA 1 ATOM 672 C C . LEU A 1 88 ? 4.273 -6.923 -1.575 1.00 6.71 ? 176 LEU A C 1 ATOM 673 O O . LEU A 1 88 ? 4.428 -7.810 -0.745 1.00 7.53 ? 176 LEU A O 1 ATOM 674 C CB . LEU A 1 88 ? 5.954 -5.084 -1.258 1.00 6.01 ? 176 LEU A CB 1 ATOM 675 C CG . LEU A 1 88 ? 6.227 -3.608 -1.450 1.00 6.47 ? 176 LEU A CG 1 ATOM 676 C CD1 . LEU A 1 88 ? 7.690 -3.310 -1.136 1.00 8.84 ? 176 LEU A CD1 1 ATOM 677 C CD2 . LEU A 1 88 ? 5.846 -3.113 -2.835 1.00 8.55 ? 176 LEU A CD2 1 ATOM 678 N N . PRO A 1 89 ? 4.051 -7.181 -2.858 1.00 6.14 ? 177 PRO A N 1 ATOM 679 C CA . PRO A 1 89 ? 4.010 -8.546 -3.352 1.00 7.64 ? 177 PRO A CA 1 ATOM 680 C C . PRO A 1 89 ? 5.431 -9.080 -3.361 1.00 8.03 ? 177 PRO A C 1 ATOM 681 O O . PRO A 1 89 ? 6.401 -8.365 -3.466 1.00 9.34 ? 177 PRO A O 1 ATOM 682 C CB . PRO A 1 89 ? 3.432 -8.403 -4.736 1.00 7.87 ? 177 PRO A CB 1 ATOM 683 C CG . PRO A 1 89 ? 3.895 -7.052 -5.216 1.00 6.68 ? 177 PRO A CG 1 ATOM 684 C CD . PRO A 1 89 ? 3.885 -6.216 -3.933 1.00 6.99 ? 177 PRO A CD 1 ATOM 685 N N . ASP A 1 90 ? 5.554 -10.404 -3.232 1.00 8.54 ? 178 ASP A N 1 ATOM 686 C CA . ASP A 1 90 ? 6.867 -11.088 -3.007 1.00 8.95 ? 178 ASP A CA 1 ATOM 687 C C . ASP A 1 90 ? 7.596 -10.424 -1.821 1.00 9.06 ? 178 ASP A C 1 ATOM 688 O O . ASP A 1 90 ? 8.809 -10.144 -1.852 1.00 9.32 ? 178 ASP A O 1 ATOM 689 C CB . ASP A 1 90 ? 7.770 -11.108 -4.259 1.00 9.79 ? 178 ASP A CB 1 ATOM 690 C CG . ASP A 1 90 ? 7.341 -12.107 -5.301 1.00 11.33 ? 178 ASP A CG 1 ATOM 691 O OD1 . ASP A 1 90 ? 6.179 -12.568 -5.307 1.00 11.20 ? 178 ASP A OD1 1 ATOM 692 O OD2 . ASP A 1 90 ? 8.172 -12.508 -6.165 1.00 14.11 ? 178 ASP A OD2 1 ATOM 693 N N . ARG A 1 91 ? 6.846 -10.139 -0.781 1.00 8.50 ? 179 ARG A N 1 ATOM 694 C CA . ARG A 1 91 ? 7.351 -9.439 0.377 1.00 7.95 ? 179 ARG A CA 1 ATOM 695 C C . ARG A 1 91 ? 8.487 -10.204 1.010 1.00 8.49 ? 179 ARG A C 1 ATOM 696 O O . ARG A 1 91 ? 8.530 -11.444 1.023 1.00 9.29 ? 179 ARG A O 1 ATOM 697 C CB . ARG A 1 91 ? 6.234 -9.299 1.430 1.00 8.00 ? 179 ARG A CB 1 ATOM 698 C CG . ARG A 1 91 ? 6.280 -8.001 2.177 1.00 8.38 ? 179 ARG A CG 1 ATOM 699 C CD . ARG A 1 91 ? 5.134 -7.790 3.124 1.00 8.52 ? 179 ARG A CD 1 ATOM 700 N NE . ARG A 1 91 ? 5.225 -8.691 4.270 1.00 8.70 ? 179 ARG A NE 1 ATOM 701 C CZ . ARG A 1 91 ? 4.272 -8.835 5.185 1.00 8.99 ? 179 ARG A CZ 1 ATOM 702 N NH1 . ARG A 1 91 ? 3.160 -8.160 5.127 1.00 9.69 ? 179 ARG A NH1 1 ATOM 703 N NH2 . ARG A 1 91 ? 4.436 -9.701 6.165 1.00 12.07 ? 179 ARG A NH2 1 ATOM 704 N N . ASP A 1 92 ? 9.406 -9.450 1.592 1.00 8.96 ? 180 ASP A N 1 ATOM 705 C CA . ASP A 1 92 ? 10.489 -10.042 2.373 1.00 9.86 ? 180 ASP A CA 1 ATOM 706 C C . ASP A 1 92 ? 11.314 -11.022 1.537 1.00 9.94 ? 180 ASP A C 1 ATOM 707 O O . ASP A 1 92 ? 11.533 -12.171 1.912 1.00 11.34 ? 180 ASP A O 1 ATOM 708 C CB . ASP A 1 92 ? 9.913 -10.709 3.599 1.00 9.95 ? 180 ASP A CB 1 ATOM 709 C CG . ASP A 1 92 ? 9.026 -9.808 4.355 1.00 10.94 ? 180 ASP A CG 1 ATOM 710 O OD1 . ASP A 1 92 ? 9.509 -8.773 4.902 1.00 11.87 ? 180 ASP A OD1 1 ATOM 711 O OD2 . ASP A 1 92 ? 7.826 -10.114 4.487 1.00 12.45 ? 180 ASP A OD2 1 ATOM 712 N N . CYS A 1 93 ? 11.788 -10.569 0.393 1.00 10.04 ? 181 CYS A N 1 ATOM 713 C CA . CYS A 1 93 ? 12.299 -11.454 -0.657 1.00 11.07 ? 181 CYS A CA 1 ATOM 714 C C . CYS A 1 93 ? 13.482 -12.314 -0.265 1.00 12.30 ? 181 CYS A C 1 ATOM 715 O O . CYS A 1 93 ? 13.676 -13.391 -0.814 1.00 13.05 ? 181 CYS A O 1 ATOM 716 C CB . CYS A 1 93 ? 12.653 -10.641 -1.915 1.00 11.72 ? 181 CYS A CB 1 ATOM 717 S SG . CYS A 1 93 ? 13.890 -9.352 -1.635 1.00 14.71 ? 181 CYS A SG 1 ATOM 718 N N . ALA A 1 94 ? 14.260 -11.848 0.697 1.00 11.73 ? 182 ALA A N 1 ATOM 719 C CA . ALA A 1 94 ? 15.466 -12.583 1.111 1.00 13.29 ? 182 ALA A CA 1 ATOM 720 C C . ALA A 1 94 ? 15.235 -13.454 2.318 1.00 15.21 ? 182 ALA A C 1 ATOM 721 O O . ALA A 1 94 ? 16.150 -14.179 2.750 1.00 18.06 ? 182 ALA A O 1 ATOM 722 C CB . ALA A 1 94 ? 16.609 -11.603 1.406 1.00 13.59 ? 182 ALA A CB 1 ATOM 723 N N . ALA A 1 95 ? 14.040 -13.416 2.891 1.00 16.69 ? 183 ALA A N 1 ATOM 724 C CA . ALA A 1 95 ? 13.733 -14.189 4.075 1.00 17.19 ? 183 ALA A CA 1 ATOM 725 C C . ALA A 1 95 ? 13.368 -15.607 3.669 1.00 18.11 ? 183 ALA A C 1 ATOM 726 O O . ALA A 1 95 ? 12.738 -15.829 2.656 1.00 18.27 ? 183 ALA A O 1 ATOM 727 C CB . ALA A 1 95 ? 12.595 -13.537 4.843 1.00 17.35 ? 183 ALA A CB 1 ATOM 728 N N . ALA A 1 96 ? 13.780 -16.577 4.471 1.00 18.92 ? 184 ALA A N 1 ATOM 729 C CA . ALA A 1 96 ? 13.417 -17.958 4.195 1.00 19.35 ? 184 ALA A CA 1 ATOM 730 C C . ALA A 1 96 ? 11.904 -18.185 4.258 1.00 19.49 ? 184 ALA A C 1 ATOM 731 O O . ALA A 1 96 ? 11.388 -19.051 3.551 1.00 21.16 ? 184 ALA A O 1 ATOM 732 C CB . ALA A 1 96 ? 14.146 -18.875 5.133 1.00 19.90 ? 184 ALA A CB 1 ATOM 733 N N . ALA A 1 97 ? 11.223 -17.401 5.099 1.00 18.20 ? 185 ALA A N 1 ATOM 734 C CA . ALA A 1 97 ? 9.764 -17.469 5.323 1.00 16.59 ? 185 ALA A CA 1 ATOM 735 C C . ALA A 1 97 ? 9.219 -16.027 5.314 1.00 16.58 ? 185 ALA A C 1 ATOM 736 O O . ALA A 1 97 ? 9.891 -15.116 5.807 1.00 17.50 ? 185 ALA A O 1 ATOM 737 C CB . ALA A 1 97 ? 9.491 -18.119 6.669 1.00 17.18 ? 185 ALA A CB 1 ATOM 738 N N . SER A 1 98 ? 8.016 -15.814 4.810 1.00 15.91 ? 186 SER A N 1 ATOM 739 C CA . SER A 1 98 ? 7.341 -14.503 4.829 1.00 15.23 ? 186 SER A CA 1 ATOM 740 C C . SER A 1 98 ? 5.868 -14.683 5.092 1.00 14.36 ? 186 SER A C 1 ATOM 741 O O . SER A 1 98 ? 5.271 -15.644 4.611 1.00 17.57 ? 186 SER A O 1 ATOM 742 C CB . SER A 1 98 ? 7.474 -13.799 3.474 1.00 15.35 ? 186 SER A CB 1 ATOM 743 O OG . SER A 1 98 ? 6.712 -12.582 3.408 1.00 15.12 ? 186 SER A OG 1 ATOM 744 N N . ASN A 1 99 ? 5.276 -13.740 5.802 1.00 13.71 ? 187 ASN A N 1 ATOM 745 C CA . ASN A 1 99 ? 3.829 -13.657 5.979 1.00 14.83 ? 187 ASN A CA 1 ATOM 746 C C . ASN A 1 99 ? 3.122 -12.748 4.960 1.00 13.38 ? 187 ASN A C 1 ATOM 747 O O . ASN A 1 99 ? 1.923 -12.483 5.084 1.00 15.62 ? 187 ASN A O 1 ATOM 748 C CB . ASN A 1 99 ? 3.515 -13.139 7.393 1.00 15.79 ? 187 ASN A CB 1 ATOM 749 C CG . ASN A 1 99 ? 4.014 -14.057 8.488 1.00 20.78 ? 187 ASN A CG 1 ATOM 750 O OD1 . ASN A 1 99 ? 4.143 -15.253 8.288 1.00 23.59 ? 187 ASN A OD1 1 ATOM 751 N ND2 . ASN A 1 99 ? 4.349 -13.466 9.634 1.00 25.86 ? 187 ASN A ND2 1 ATOM 752 N N . GLY A 1 100 ? 3.841 -12.265 3.940 1.00 11.77 ? 188 GLY A N 1 ATOM 753 C CA . GLY A 1 100 ? 3.205 -11.471 2.916 1.00 10.96 ? 188 GLY A CA 1 ATOM 754 C C . GLY A 1 100 ? 2.130 -12.264 2.216 1.00 10.88 ? 188 GLY A C 1 ATOM 755 O O . GLY A 1 100 ? 2.262 -13.454 1.985 1.00 14.50 ? 188 GLY A O 1 ATOM 756 N N . GLU A 1 101 ? 1.049 -11.609 1.837 1.00 9.60 ? 189 GLU A N 1 ATOM 757 C CA . GLU A 1 101 ? -0.086 -12.297 1.244 1.00 9.89 ? 189 GLU A CA 1 ATOM 758 C C . GLU A 1 101 ? -0.138 -12.300 -0.259 1.00 8.05 ? 189 GLU A C 1 ATOM 759 O O . GLU A 1 101 ? -0.889 -13.108 -0.812 1.00 8.87 ? 189 GLU A O 1 ATOM 760 C CB . GLU A 1 101 ? -1.400 -11.832 1.791 1.00 11.89 ? 189 GLU A CB 1 ATOM 761 C CG . GLU A 1 101 ? -1.716 -10.415 1.453 1.00 11.62 ? 189 GLU A CG 1 ATOM 762 C CD . GLU A 1 101 ? -2.766 -9.767 2.385 1.00 13.45 ? 189 GLU A CD 1 ATOM 763 O OE1 . GLU A 1 101 ? -3.605 -10.399 3.059 1.00 16.08 ? 189 GLU A OE1 1 ATOM 764 O OE2 . GLU A 1 101 ? -2.760 -8.565 2.459 1.00 10.80 ? 189 GLU A OE2 1 ATOM 765 N N . TRP A 1 102 ? 0.664 -11.489 -0.946 1.00 6.67 ? 190 TRP A N 1 ATOM 766 C CA . TRP A 1 102 ? 0.605 -11.358 -2.376 1.00 6.68 ? 190 TRP A CA 1 ATOM 767 C C . TRP A 1 102 ? 1.883 -11.760 -3.067 1.00 6.73 ? 190 TRP A C 1 ATOM 768 O O . TRP A 1 102 ? 2.961 -11.656 -2.506 1.00 7.78 ? 190 TRP A O 1 ATOM 769 C CB . TRP A 1 102 ? 0.192 -9.927 -2.739 1.00 7.03 ? 190 TRP A CB 1 ATOM 770 C CG . TRP A 1 102 ? -1.167 -9.567 -2.309 1.00 6.84 ? 190 TRP A CG 1 ATOM 771 C CD1 . TRP A 1 102 ? -2.238 -10.404 -2.211 1.00 8.44 ? 190 TRP A CD1 1 ATOM 772 C CD2 . TRP A 1 102 ? -1.632 -8.287 -1.902 1.00 6.30 ? 190 TRP A CD2 1 ATOM 773 N NE1 . TRP A 1 102 ? -3.345 -9.732 -1.758 1.00 8.27 ? 190 TRP A NE1 1 ATOM 774 C CE2 . TRP A 1 102 ? -2.984 -8.422 -1.555 1.00 7.77 ? 190 TRP A CE2 1 ATOM 775 C CE3 . TRP A 1 102 ? -1.034 -7.033 -1.738 1.00 7.00 ? 190 TRP A CE3 1 ATOM 776 C CZ2 . TRP A 1 102 ? -3.748 -7.360 -1.120 1.00 7.85 ? 190 TRP A CZ2 1 ATOM 777 C CZ3 . TRP A 1 102 ? -1.805 -5.993 -1.306 1.00 9.55 ? 190 TRP A CZ3 1 ATOM 778 C CH2 . TRP A 1 102 ? -3.132 -6.144 -1.002 1.00 9.06 ? 190 TRP A CH2 1 ATOM 779 N N . ALA A 1 103 ? 1.759 -12.136 -4.323 1.00 7.48 ? 191 ALA A N 1 ATOM 780 C CA . ALA A 1 103 ? 2.855 -12.602 -5.176 1.00 6.91 ? 191 ALA A CA 1 ATOM 781 C C . ALA A 1 103 ? 2.809 -11.914 -6.511 1.00 7.31 ? 191 ALA A C 1 ATOM 782 O O . ALA A 1 103 ? 1.744 -11.791 -7.090 1.00 7.34 ? 191 ALA A O 1 ATOM 783 C CB . ALA A 1 103 ? 2.788 -14.103 -5.393 1.00 8.09 ? 191 ALA A CB 1 ATOM 784 N N . ILE A 1 104 ? 3.978 -11.517 -6.979 1.00 7.80 ? 192 ILE A N 1 ATOM 785 C CA . ILE A 1 104 ? 4.095 -10.900 -8.288 1.00 8.34 ? 192 ILE A CA 1 ATOM 786 C C . ILE A 1 104 ? 3.494 -11.814 -9.358 1.00 7.91 ? 192 ILE A C 1 ATOM 787 O O . ILE A 1 104 ? 2.791 -11.361 -10.235 1.00 9.45 ? 192 ILE A O 1 ATOM 788 C CB . ILE A 1 104 ? 5.560 -10.536 -8.601 1.00 9.32 ? 192 ILE A CB 1 ATOM 789 C CG1 . ILE A 1 104 ? 6.050 -9.495 -7.603 1.00 8.85 ? 192 ILE A CG1 1 ATOM 790 C CG2 . ILE A 1 104 ? 5.708 -10.007 -9.992 1.00 12.00 ? 192 ILE A CG2 1 ATOM 791 C CD1 . ILE A 1 104 ? 7.574 -9.274 -7.635 1.00 10.59 ? 192 ILE A CD1 1 ATOM 792 N N . ALA A 1 105 ? 3.759 -13.123 -9.279 1.00 8.35 ? 193 ALA A N 1 ATOM 793 C CA . ALA A 1 105 ? 3.246 -14.076 -10.264 1.00 8.67 ? 193 ALA A CA 1 ATOM 794 C C . ALA A 1 105 ? 1.744 -14.301 -10.197 1.00 8.87 ? 193 ALA A C 1 ATOM 795 O O . ALA A 1 105 ? 1.229 -14.953 -11.108 1.00 9.21 ? 193 ALA A O 1 ATOM 796 C CB . ALA A 1 105 ? 3.953 -15.367 -10.096 1.00 9.84 ? 193 ALA A CB 1 ATOM 797 N N . ASN A 1 106 ? 1.073 -13.805 -9.153 1.00 8.61 ? 194 ASN A N 1 ATOM 798 C CA . ASN A 1 106 ? -0.358 -13.978 -8.960 1.00 8.40 ? 194 ASN A CA 1 ATOM 799 C C . ASN A 1 106 ? -1.104 -12.650 -8.698 1.00 9.02 ? 194 ASN A C 1 ATOM 800 O O . ASN A 1 106 ? -1.777 -12.483 -7.701 1.00 9.19 ? 194 ASN A O 1 ATOM 801 C CB . ASN A 1 106 ? -0.584 -14.983 -7.832 1.00 9.56 ? 194 ASN A CB 1 ATOM 802 C CG . ASN A 1 106 ? -1.985 -15.500 -7.763 1.00 9.66 ? 194 ASN A CG 1 ATOM 803 O OD1 . ASN A 1 106 ? -2.707 -15.500 -8.763 1.00 10.22 ? 194 ASN A OD1 1 ATOM 804 N ND2 . ASN A 1 106 ? -2.371 -15.987 -6.575 1.00 10.50 ? 194 ASN A ND2 1 ATOM 805 N N . ASN A 1 107 ? -0.982 -11.741 -9.659 1.00 8.85 ? 195 ASN A N 1 ATOM 806 C CA . ASN A 1 107 ? -1.666 -10.446 -9.665 1.00 9.69 ? 195 ASN A CA 1 ATOM 807 C C . ASN A 1 107 ? -1.236 -9.514 -8.525 1.00 8.78 ? 195 ASN A C 1 ATOM 808 O O . ASN A 1 107 ? -1.941 -8.568 -8.180 1.00 9.04 ? 195 ASN A O 1 ATOM 809 C CB . ASN A 1 107 ? -3.191 -10.616 -9.658 1.00 13.02 ? 195 ASN A CB 1 ATOM 810 C CG . ASN A 1 107 ? -3.879 -9.516 -10.439 1.00 15.43 ? 195 ASN A CG 1 ATOM 811 O OD1 . ASN A 1 107 ? -3.308 -8.945 -11.389 1.00 18.46 ? 195 ASN A OD1 1 ATOM 812 N ND2 . ASN A 1 107 ? -5.103 -9.182 -10.037 1.00 19.78 ? 195 ASN A ND2 1 ATOM 813 N N . GLY A 1 108 ? -0.043 -9.722 -7.988 1.00 8.15 ? 196 GLY A N 1 ATOM 814 C CA . GLY A 1 108 ? 0.371 -8.917 -6.867 1.00 7.45 ? 196 GLY A CA 1 ATOM 815 C C . GLY A 1 108 ? 0.559 -7.447 -7.140 1.00 7.15 ? 196 GLY A C 1 ATOM 816 O O . GLY A 1 108 ? 0.300 -6.642 -6.246 1.00 7.79 ? 196 GLY A O 1 ATOM 817 N N . VAL A 1 109 ? 1.062 -7.090 -8.325 1.00 7.18 ? 197 VAL A N 1 ATOM 818 C CA . VAL A 1 109 ? 1.185 -5.681 -8.670 1.00 7.93 ? 197 VAL A CA 1 ATOM 819 C C . VAL A 1 109 ? -0.171 -4.971 -8.616 1.00 7.34 ? 197 VAL A C 1 ATOM 820 O O . VAL A 1 109 ? -0.307 -3.907 -7.976 1.00 8.43 ? 197 VAL A O 1 ATOM 821 C CB . VAL A 1 109 ? 1.880 -5.505 -10.015 1.00 9.04 ? 197 VAL A CB 1 ATOM 822 C CG1 . VAL A 1 109 ? 1.757 -4.071 -10.502 1.00 10.13 ? 197 VAL A CG1 1 ATOM 823 C CG2 . VAL A 1 109 ? 3.325 -5.888 -9.886 1.00 11.45 ? 197 VAL A CG2 1 ATOM 824 N N . ASN A 1 110 ? -1.153 -5.533 -9.281 1.00 7.52 ? 198 ASN A N 1 ATOM 825 C CA . ASN A 1 110 ? -2.481 -4.958 -9.251 1.00 9.00 ? 198 ASN A CA 1 ATOM 826 C C . ASN A 1 110 ? -3.094 -4.935 -7.872 1.00 7.65 ? 198 ASN A C 1 ATOM 827 O O . ASN A 1 110 ? -3.736 -3.963 -7.475 1.00 7.76 ? 198 ASN A O 1 ATOM 828 C CB . ASN A 1 110 ? -3.406 -5.606 -10.261 1.00 10.68 ? 198 ASN A CB 1 ATOM 829 C CG . ASN A 1 110 ? -3.032 -5.224 -11.720 1.00 14.88 ? 198 ASN A CG 1 ATOM 830 O OD1 . ASN A 1 110 ? -2.494 -4.158 -11.970 1.00 20.18 ? 198 ASN A OD1 1 ATOM 831 N ND2 . ASN A 1 110 ? -3.340 -6.093 -12.642 1.00 19.88 ? 198 ASN A ND2 1 ATOM 832 N N . ASN A 1 111 ? -2.873 -5.991 -7.106 1.00 7.09 ? 199 ASN A N 1 ATOM 833 C CA . ASN A 1 111 ? -3.377 -6.037 -5.763 1.00 6.18 ? 199 ASN A CA 1 ATOM 834 C C . ASN A 1 111 ? -2.780 -4.902 -4.913 1.00 5.30 ? 199 ASN A C 1 ATOM 835 O O . ASN A 1 111 ? -3.502 -4.277 -4.168 1.00 6.63 ? 199 ASN A O 1 ATOM 836 C CB . ASN A 1 111 ? -3.081 -7.381 -5.098 1.00 7.06 ? 199 ASN A CB 1 ATOM 837 C CG . ASN A 1 111 ? -3.839 -8.518 -5.699 1.00 8.74 ? 199 ASN A CG 1 ATOM 838 O OD1 . ASN A 1 111 ? -4.791 -8.354 -6.397 1.00 9.65 ? 199 ASN A OD1 1 ATOM 839 N ND2 . ASN A 1 111 ? -3.419 -9.720 -5.344 1.00 9.29 ? 199 ASN A ND2 1 ATOM 840 N N . TYR A 1 112 ? -1.482 -4.700 -5.054 1.00 6.46 ? 200 TYR A N 1 ATOM 841 C CA . TYR A 1 112 ? -0.777 -3.697 -4.276 1.00 6.03 ? 200 TYR A CA 1 ATOM 842 C C . TYR A 1 112 ? -1.232 -2.286 -4.697 1.00 6.50 ? 200 TYR A C 1 ATOM 843 O O . TYR A 1 112 ? -1.446 -1.417 -3.860 1.00 6.67 ? 200 TYR A O 1 ATOM 844 C CB . TYR A 1 112 ? 0.711 -3.828 -4.440 1.00 5.80 ? 200 TYR A CB 1 ATOM 845 C CG . TYR A 1 112 ? 1.460 -2.933 -3.495 1.00 6.46 ? 200 TYR A CG 1 ATOM 846 C CD1 . TYR A 1 112 ? 1.569 -3.292 -2.167 1.00 7.10 ? 200 TYR A CD1 1 ATOM 847 C CD2 . TYR A 1 112 ? 1.986 -1.725 -3.888 1.00 6.40 ? 200 TYR A CD2 1 ATOM 848 C CE1 . TYR A 1 112 ? 2.247 -2.534 -1.242 1.00 7.46 ? 200 TYR A CE1 1 ATOM 849 C CE2 . TYR A 1 112 ? 2.662 -0.930 -2.956 1.00 6.67 ? 200 TYR A CE2 1 ATOM 850 C CZ . TYR A 1 112 ? 2.795 -1.335 -1.640 1.00 7.45 ? 200 TYR A CZ 1 ATOM 851 O OH . TYR A 1 112 ? 3.485 -0.526 -0.766 1.00 8.54 ? 200 TYR A OH 1 ATOM 852 N N . LYS A 1 113 ? -1.348 -2.043 -5.998 1.00 6.58 ? 201 LYS A N 1 ATOM 853 C CA . LYS A 1 113 ? -1.787 -0.725 -6.441 1.00 6.99 ? 201 LYS A CA 1 ATOM 854 C C . LYS A 1 113 ? -3.169 -0.411 -5.904 1.00 7.04 ? 201 LYS A C 1 ATOM 855 O O . LYS A 1 113 ? -3.423 0.729 -5.487 1.00 7.61 ? 201 LYS A O 1 ATOM 856 C CB . LYS A 1 113 ? -1.738 -0.636 -7.963 1.00 8.57 ? 201 LYS A CB 1 ATOM 857 C CG . LYS A 1 113 ? -0.331 -0.585 -8.516 1.00 8.93 ? 201 LYS A CG 1 ATOM 858 C CD . LYS A 1 113 ? -0.318 -0.441 -10.047 1.00 14.00 ? 201 LYS A CD 1 ATOM 859 C CE . LYS A 1 113 ? 1.070 -0.169 -10.529 1.00 18.68 ? 201 LYS A CE 1 ATOM 860 N NZ . LYS A 1 113 ? 1.109 0.172 -11.999 1.00 25.19 ? 201 LYS A NZ 1 ATOM 861 N N . ALA A 1 114 ? -4.082 -1.380 -5.902 1.00 7.58 ? 202 ALA A N 1 ATOM 862 C CA . ALA A 1 114 ? -5.405 -1.189 -5.354 1.00 7.63 ? 202 ALA A CA 1 ATOM 863 C C . ALA A 1 114 ? -5.367 -0.871 -3.830 1.00 7.54 ? 202 ALA A C 1 ATOM 864 O O . ALA A 1 114 ? -6.161 -0.072 -3.333 1.00 7.79 ? 202 ALA A O 1 ATOM 865 C CB . ALA A 1 114 ? -6.326 -2.364 -5.659 1.00 8.68 ? 202 ALA A CB 1 ATOM 866 N N . TYR A 1 115 ? -4.495 -1.570 -3.092 1.00 7.37 ? 203 TYR A N 1 ATOM 867 C CA . TYR A 1 115 ? -4.253 -1.329 -1.679 1.00 6.52 ? 203 TYR A CA 1 ATOM 868 C C . TYR A 1 115 ? -3.807 0.123 -1.437 1.00 5.48 ? 203 TYR A C 1 ATOM 869 O O . TYR A 1 115 ? -4.362 0.794 -0.585 1.00 6.89 ? 203 TYR A O 1 ATOM 870 C CB . TYR A 1 115 ? -3.248 -2.417 -1.207 1.00 7.37 ? 203 TYR A CB 1 ATOM 871 C CG . TYR A 1 115 ? -2.458 -2.209 0.062 1.00 5.82 ? 203 TYR A CG 1 ATOM 872 C CD1 . TYR A 1 115 ? -2.961 -2.639 1.257 1.00 6.00 ? 203 TYR A CD1 1 ATOM 873 C CD2 . TYR A 1 115 ? -1.162 -1.735 0.032 1.00 6.20 ? 203 TYR A CD2 1 ATOM 874 C CE1 . TYR A 1 115 ? -2.207 -2.550 2.440 1.00 6.80 ? 203 TYR A CE1 1 ATOM 875 C CE2 . TYR A 1 115 ? -0.403 -1.639 1.177 1.00 6.44 ? 203 TYR A CE2 1 ATOM 876 C CZ . TYR A 1 115 ? -0.930 -2.064 2.381 1.00 6.44 ? 203 TYR A CZ 1 ATOM 877 O OH . TYR A 1 115 ? -0.133 -1.951 3.468 1.00 7.19 ? 203 TYR A OH 1 ATOM 878 N N . ILE A 1 116 ? -2.815 0.551 -2.175 1.00 5.81 ? 204 ILE A N 1 ATOM 879 C CA . ILE A 1 116 ? -2.346 1.931 -2.060 1.00 5.65 ? 204 ILE A CA 1 ATOM 880 C C . ILE A 1 116 ? -3.492 2.901 -2.421 1.00 6.23 ? 204 ILE A C 1 ATOM 881 O O . ILE A 1 116 ? -3.690 3.890 -1.725 1.00 7.25 ? 204 ILE A O 1 ATOM 882 C CB . ILE A 1 116 ? -1.156 2.125 -2.964 1.00 6.01 ? 204 ILE A CB 1 ATOM 883 C CG1 . ILE A 1 116 ? 0.066 1.333 -2.490 1.00 6.51 ? 204 ILE A CG1 1 ATOM 884 C CG2 . ILE A 1 116 ? -0.817 3.624 -3.121 1.00 7.13 ? 204 ILE A CG2 1 ATOM 885 C CD1 . ILE A 1 116 ? 0.539 1.701 -1.112 1.00 8.07 ? 204 ILE A CD1 1 ATOM 886 N N . ASN A 1 117 ? -4.256 2.579 -3.461 1.00 6.38 ? 205 ASN A N 1 ATOM 887 C CA . ASN A 1 117 ? -5.328 3.482 -3.868 1.00 7.33 ? 205 ASN A CA 1 ATOM 888 C C . ASN A 1 117 ? -6.371 3.605 -2.793 1.00 7.22 ? 205 ASN A C 1 ATOM 889 O O . ASN A 1 117 ? -6.922 4.674 -2.561 1.00 7.73 ? 205 ASN A O 1 ATOM 890 C CB . ASN A 1 117 ? -5.982 2.981 -5.136 1.00 8.09 ? 205 ASN A CB 1 ATOM 891 C CG . ASN A 1 117 ? -5.082 3.016 -6.355 1.00 10.27 ? 205 ASN A CG 1 ATOM 892 O OD1 . ASN A 1 117 ? -4.057 3.655 -6.380 1.00 11.69 ? 205 ASN A OD1 1 ATOM 893 N ND2 . ASN A 1 117 ? -5.491 2.265 -7.389 1.00 13.56 ? 205 ASN A ND2 1 ATOM 894 N N . ARG A 1 118 ? -6.677 2.508 -2.116 1.00 6.79 ? 206 ARG A N 1 ATOM 895 C CA . ARG A 1 118 ? -7.655 2.547 -1.053 1.00 6.48 ? 206 ARG A CA 1 ATOM 896 C C . ARG A 1 118 ? -7.134 3.295 0.182 1.00 6.54 ? 206 ARG A C 1 ATOM 897 O O . ARG A 1 118 ? -7.874 4.085 0.787 1.00 7.38 ? 206 ARG A O 1 ATOM 898 C CB . ARG A 1 118 ? -8.156 1.134 -0.694 1.00 7.88 ? 206 ARG A CB 1 ATOM 899 C CG . ARG A 1 118 ? -9.205 1.117 0.409 1.00 9.45 ? 206 ARG A CG 1 ATOM 900 C CD . ARG A 1 118 ? -10.481 1.927 0.047 1.00 11.90 ? 206 ARG A CD 1 ATOM 901 N NE . ARG A 1 118 ? -11.427 1.930 1.151 1.00 12.59 ? 206 ARG A NE 1 ATOM 902 C CZ . ARG A 1 118 ? -12.304 2.865 1.395 1.00 13.99 ? 206 ARG A CZ 1 ATOM 903 N NH1 . ARG A 1 118 ? -12.458 3.907 0.581 1.00 16.13 ? 206 ARG A NH1 1 ATOM 904 N NH2 . ARG A 1 118 ? -13.052 2.741 2.472 1.00 18.06 ? 206 ARG A NH2 1 ATOM 905 N N . ILE A 1 119 ? -5.897 3.050 0.551 1.00 6.38 ? 207 ILE A N 1 ATOM 906 C CA . ILE A 1 119 ? -5.276 3.847 1.610 1.00 6.12 ? 207 ILE A CA 1 ATOM 907 C C . ILE A 1 119 ? -5.351 5.339 1.270 1.00 6.99 ? 207 ILE A C 1 ATOM 908 O O . ILE A 1 119 ? -5.699 6.137 2.117 1.00 7.10 ? 207 ILE A O 1 ATOM 909 C CB . ILE A 1 119 ? -3.852 3.414 1.832 1.00 6.44 ? 207 ILE A CB 1 ATOM 910 C CG1 . ILE A 1 119 ? -3.792 2.012 2.429 1.00 7.13 ? 207 ILE A CG1 1 ATOM 911 C CG2 . ILE A 1 119 ? -3.103 4.398 2.727 1.00 7.38 ? 207 ILE A CG2 1 ATOM 912 C CD1 . ILE A 1 119 ? -2.415 1.351 2.406 1.00 7.36 ? 207 ILE A CD1 1 ATOM 913 N N . ARG A 1 120 ? -5.058 5.670 0.036 1.00 5.79 ? 208 ARG A N 1 ATOM 914 C CA . ARG A 1 120 ? -5.130 7.075 -0.357 1.00 6.16 ? 208 ARG A CA 1 ATOM 915 C C . ARG A 1 120 ? -6.526 7.645 -0.144 1.00 7.29 ? 208 ARG A C 1 ATOM 916 O O . ARG A 1 120 ? -6.674 8.743 0.366 1.00 8.06 ? 208 ARG A O 1 ATOM 917 C CB . ARG A 1 120 ? -4.684 7.254 -1.799 1.00 6.50 ? 208 ARG A CB 1 ATOM 918 C CG . ARG A 1 120 ? -4.555 8.692 -2.254 1.00 8.76 ? 208 ARG A CG 1 ATOM 919 C CD . ARG A 1 120 ? -4.273 8.871 -3.721 1.00 10.13 ? 208 ARG A CD 1 ATOM 920 N NE . ARG A 1 120 ? -3.763 10.233 -4.036 1.00 13.13 ? 208 ARG A NE 1 ATOM 921 C CZ . ARG A 1 120 ? -4.514 11.285 -4.204 1.00 14.54 ? 208 ARG A CZ 1 ATOM 922 N NH1 . ARG A 1 120 ? -5.832 11.184 -4.136 1.00 16.98 ? 208 ARG A NH1 1 ATOM 923 N NH2 . ARG A 1 120 ? -3.974 12.480 -4.438 1.00 15.42 ? 208 ARG A NH2 1 ATOM 924 N N . GLU A 1 121 ? -7.562 6.944 -0.573 1.00 7.27 ? 209 GLU A N 1 ATOM 925 C CA . GLU A 1 121 ? -8.919 7.390 -0.408 1.00 7.92 ? 209 GLU A CA 1 ATOM 926 C C . GLU A 1 121 ? -9.245 7.667 1.052 1.00 8.06 ? 209 GLU A C 1 ATOM 927 O O . GLU A 1 121 ? -9.858 8.676 1.409 1.00 9.46 ? 209 GLU A O 1 ATOM 928 C CB . GLU A 1 121 ? -9.930 6.370 -0.984 1.00 9.51 ? 209 GLU A CB 1 ATOM 929 C CG . GLU A 1 121 ? -9.948 6.204 -2.471 1.00 13.33 ? 209 GLU A CG 1 ATOM 930 C CD . GLU A 1 121 ? -10.845 5.058 -2.946 1.00 19.93 ? 209 GLU A CD 1 ATOM 931 O OE1 . GLU A 1 121 ? -11.463 4.300 -2.149 1.00 21.99 ? 209 GLU A OE1 1 ATOM 932 O OE2 . GLU A 1 121 ? -10.917 4.890 -4.179 1.00 27.54 ? 209 GLU A OE2 1 ATOM 933 N N . ILE A 1 122 ? -8.822 6.777 1.925 1.00 7.33 ? 210 ILE A N 1 ATOM 934 C CA . ILE A 1 122 ? -9.075 6.937 3.332 1.00 7.42 ? 210 ILE A CA 1 ATOM 935 C C . ILE A 1 122 ? -8.281 8.117 3.885 1.00 7.66 ? 210 ILE A C 1 ATOM 936 O O . ILE A 1 122 ? -8.842 8.911 4.612 1.00 8.02 ? 210 ILE A O 1 ATOM 937 C CB . ILE A 1 122 ? -8.764 5.614 4.077 1.00 7.85 ? 210 ILE A CB 1 ATOM 938 C CG1 . ILE A 1 122 ? -9.785 4.537 3.673 1.00 9.16 ? 210 ILE A CG1 1 ATOM 939 C CG2 . ILE A 1 122 ? -8.776 5.836 5.552 1.00 8.88 ? 210 ILE A CG2 1 ATOM 940 C CD1 . ILE A 1 122 ? -9.331 3.151 4.019 1.00 10.83 ? 210 ILE A CD1 1 ATOM 941 N N . LEU A 1 123 ? -7.008 8.246 3.535 1.00 6.80 ? 211 LEU A N 1 ATOM 942 C CA . LEU A 1 123 ? -6.212 9.382 4.019 1.00 6.71 ? 211 LEU A CA 1 ATOM 943 C C . LEU A 1 123 ? -6.800 10.701 3.534 1.00 7.63 ? 211 LEU A C 1 ATOM 944 O O . LEU A 1 123 ? -6.845 11.651 4.330 1.00 7.71 ? 211 LEU A O 1 ATOM 945 C CB . LEU A 1 123 ? -4.765 9.230 3.610 1.00 7.35 ? 211 LEU A CB 1 ATOM 946 C CG . LEU A 1 123 ? -4.028 8.035 4.185 1.00 7.24 ? 211 LEU A CG 1 ATOM 947 C CD1 . LEU A 1 123 ? -2.606 8.040 3.767 1.00 9.33 ? 211 LEU A CD1 1 ATOM 948 C CD2 . LEU A 1 123 ? -4.170 7.916 5.677 1.00 11.10 ? 211 LEU A CD2 1 ATOM 949 N N . ILE A 1 124 ? -7.287 10.780 2.304 1.00 7.70 ? 212 ILE A N 1 ATOM 950 C CA . ILE A 1 124 ? -7.931 12.007 1.813 1.00 9.41 ? 212 ILE A CA 1 ATOM 951 C C . ILE A 1 124 ? -9.155 12.332 2.626 1.00 9.51 ? 212 ILE A C 1 ATOM 952 O O . ILE A 1 124 ? -9.415 13.500 2.898 1.00 11.20 ? 212 ILE A O 1 ATOM 953 C CB . ILE A 1 124 ? -8.234 11.908 0.337 1.00 10.82 ? 212 ILE A CB 1 ATOM 954 C CG1 . ILE A 1 124 ? -6.933 11.948 -0.447 1.00 12.19 ? 212 ILE A CG1 1 ATOM 955 C CG2 . ILE A 1 124 ? -9.240 12.999 -0.127 1.00 14.62 ? 212 ILE A CG2 1 ATOM 956 C CD1 . ILE A 1 124 ? -7.099 11.579 -1.797 1.00 17.93 ? 212 ILE A CD1 1 ATOM 957 N N . SER A 1 125 ? -9.898 11.342 3.062 1.00 9.09 ? 213 SER A N 1 ATOM 958 C CA A SER A 1 125 ? -11.079 11.592 3.874 0.52 9.45 ? 213 SER A CA 1 ATOM 959 C CA B SER A 1 125 ? -11.086 11.507 3.900 0.48 9.97 ? 213 SER A CA 1 ATOM 960 C C . SER A 1 125 ? -10.752 12.010 5.293 1.00 8.67 ? 213 SER A C 1 ATOM 961 O O . SER A 1 125 ? -11.620 12.517 6.006 1.00 11.55 ? 213 SER A O 1 ATOM 962 C CB A SER A 1 125 ? -12.000 10.370 3.877 0.52 9.46 ? 213 SER A CB 1 ATOM 963 C CB B SER A 1 125 ? -11.837 10.159 3.998 0.48 10.38 ? 213 SER A CB 1 ATOM 964 O OG A SER A 1 125 ? -11.563 9.375 4.776 0.52 9.66 ? 213 SER A OG 1 ATOM 965 O OG B SER A 1 125 ? -13.023 10.240 4.769 0.48 14.13 ? 213 SER A OG 1 ATOM 966 N N . PHE A 1 126 ? -9.511 11.810 5.718 1.00 8.28 ? 214 PHE A N 1 ATOM 967 C CA . PHE A 1 126 ? -9.025 12.183 7.050 1.00 8.10 ? 214 PHE A CA 1 ATOM 968 C C . PHE A 1 126 ? -7.878 13.170 6.937 1.00 8.62 ? 214 PHE A C 1 ATOM 969 O O . PHE A 1 126 ? -6.871 13.090 7.619 1.00 8.08 ? 214 PHE A O 1 ATOM 970 C CB . PHE A 1 126 ? -8.581 10.959 7.858 1.00 8.84 ? 214 PHE A CB 1 ATOM 971 C CG . PHE A 1 126 ? -9.736 10.129 8.341 1.00 8.54 ? 214 PHE A CG 1 ATOM 972 C CD1 . PHE A 1 126 ? -10.377 10.484 9.508 1.00 9.86 ? 214 PHE A CD1 1 ATOM 973 C CD2 . PHE A 1 126 ? -10.149 8.991 7.680 1.00 9.33 ? 214 PHE A CD2 1 ATOM 974 C CE1 . PHE A 1 126 ? -11.456 9.695 9.983 1.00 10.49 ? 214 PHE A CE1 1 ATOM 975 C CE2 . PHE A 1 126 ? -11.206 8.223 8.135 1.00 11.67 ? 214 PHE A CE2 1 ATOM 976 C CZ . PHE A 1 126 ? -11.848 8.577 9.286 1.00 12.59 ? 214 PHE A CZ 1 ATOM 977 N N . SER A 1 127 ? -8.049 14.165 6.081 1.00 9.17 ? 215 SER A N 1 ATOM 978 C CA . SER A 1 127 ? -7.028 15.188 5.870 1.00 9.62 ? 215 SER A CA 1 ATOM 979 C C . SER A 1 127 ? -6.858 16.135 7.052 1.00 10.00 ? 215 SER A C 1 ATOM 980 O O . SER A 1 127 ? -5.895 16.919 7.091 1.00 9.72 ? 215 SER A O 1 ATOM 981 C CB . SER A 1 127 ? -7.339 15.980 4.599 1.00 11.44 ? 215 SER A CB 1 ATOM 982 O OG . SER A 1 127 ? -8.566 16.721 4.730 1.00 13.33 ? 215 SER A OG 1 ATOM 983 N N . ASP A 1 128 ? -7.760 16.041 8.029 1.00 9.26 ? 216 ASP A N 1 ATOM 984 C CA . ASP A 1 128 ? -7.635 16.713 9.307 1.00 9.31 ? 216 ASP A CA 1 ATOM 985 C C . ASP A 1 128 ? -6.788 15.977 10.347 1.00 8.96 ? 216 ASP A C 1 ATOM 986 O O . ASP A 1 128 ? -6.629 16.501 11.444 1.00 10.16 ? 216 ASP A O 1 ATOM 987 C CB . ASP A 1 128 ? -9.025 16.977 9.876 1.00 9.72 ? 216 ASP A CB 1 ATOM 988 C CG . ASP A 1 128 ? -9.866 15.728 10.043 1.00 13.13 ? 216 ASP A CG 1 ATOM 989 O OD1 . ASP A 1 128 ? -9.781 14.766 9.240 1.00 12.96 ? 216 ASP A OD1 1 ATOM 990 O OD2 . ASP A 1 128 ? -10.685 15.661 10.985 1.00 20.07 ? 216 ASP A OD2 1 ATOM 991 N N . VAL A 1 129 ? -6.251 14.803 10.018 1.00 8.24 ? 217 VAL A N 1 ATOM 992 C CA . VAL A 1 129 ? -5.396 14.044 10.911 1.00 7.55 ? 217 VAL A CA 1 ATOM 993 C C . VAL A 1 129 ? -3.981 13.953 10.328 1.00 7.67 ? 217 VAL A C 1 ATOM 994 O O . VAL A 1 129 ? -3.796 13.306 9.284 1.00 8.49 ? 217 VAL A O 1 ATOM 995 C CB . VAL A 1 129 ? -5.950 12.679 11.172 1.00 8.47 ? 217 VAL A CB 1 ATOM 996 C CG1 . VAL A 1 129 ? -5.049 11.907 12.142 1.00 8.87 ? 217 VAL A CG1 1 ATOM 997 C CG2 . VAL A 1 129 ? -7.368 12.768 11.743 1.00 9.47 ? 217 VAL A CG2 1 ATOM 998 N N . ARG A 1 130 ? -3.010 14.663 10.912 1.00 6.88 ? 218 ARG A N 1 ATOM 999 C CA . ARG A 1 130 ? -1.649 14.542 10.443 1.00 6.74 ? 218 ARG A CA 1 ATOM 1000 C C . ARG A 1 130 ? -1.279 13.068 10.559 1.00 6.58 ? 218 ARG A C 1 ATOM 1001 O O . ARG A 1 130 ? -1.446 12.463 11.602 1.00 6.85 ? 218 ARG A O 1 ATOM 1002 C CB . ARG A 1 130 ? -0.700 15.406 11.280 1.00 7.45 ? 218 ARG A CB 1 ATOM 1003 C CG . ARG A 1 130 ? 0.656 15.505 10.687 1.00 8.53 ? 218 ARG A CG 1 ATOM 1004 C CD . ARG A 1 130 ? 1.653 16.262 11.545 1.00 8.07 ? 218 ARG A CD 1 ATOM 1005 N NE . ARG A 1 130 ? 1.230 17.616 11.829 1.00 8.33 ? 218 ARG A NE 1 ATOM 1006 C CZ . ARG A 1 130 ? 1.984 18.543 12.409 1.00 9.61 ? 218 ARG A CZ 1 ATOM 1007 N NH1 . ARG A 1 130 ? 3.203 18.268 12.807 1.00 11.71 ? 218 ARG A NH1 1 ATOM 1008 N NH2 . ARG A 1 130 ? 1.500 19.782 12.560 1.00 10.14 ? 218 ARG A NH2 1 ATOM 1009 N N . THR A 1 131 ? -0.692 12.554 9.494 1.00 6.55 ? 219 THR A N 1 ATOM 1010 C CA . THR A 1 131 ? -0.422 11.129 9.387 1.00 6.93 ? 219 THR A CA 1 ATOM 1011 C C . THR A 1 131 ? 0.994 10.869 8.955 1.00 7.75 ? 219 THR A C 1 ATOM 1012 O O . THR A 1 131 ? 1.429 11.331 7.901 1.00 8.52 ? 219 THR A O 1 ATOM 1013 C CB . THR A 1 131 ? -1.416 10.480 8.406 1.00 7.28 ? 219 THR A CB 1 ATOM 1014 O OG1 . THR A 1 131 ? -2.763 10.666 8.894 1.00 8.96 ? 219 THR A OG1 1 ATOM 1015 C CG2 . THR A 1 131 ? -1.225 8.964 8.281 1.00 9.04 ? 219 THR A CG2 1 ATOM 1016 N N . ILE A 1 132 ? 1.709 10.123 9.784 1.00 6.69 ? 220 ILE A N 1 ATOM 1017 C CA . ILE A 1 132 ? 3.078 9.787 9.535 1.00 7.97 ? 220 ILE A CA 1 ATOM 1018 C C . ILE A 1 132 ? 3.146 8.323 9.110 1.00 6.74 ? 220 ILE A C 1 ATOM 1019 O O . ILE A 1 132 ? 2.635 7.472 9.807 1.00 7.90 ? 220 ILE A O 1 ATOM 1020 C CB . ILE A 1 132 ? 3.931 10.047 10.788 1.00 9.44 ? 220 ILE A CB 1 ATOM 1021 C CG1 . ILE A 1 132 ? 3.918 11.585 11.131 1.00 12.70 ? 220 ILE A CG1 1 ATOM 1022 C CG2 . ILE A 1 132 ? 5.329 9.525 10.542 1.00 12.57 ? 220 ILE A CG2 1 ATOM 1023 C CD1 . ILE A 1 132 ? 4.136 11.962 12.570 1.00 14.49 ? 220 ILE A CD1 1 ATOM 1024 N N . LEU A 1 133 ? 3.740 8.055 7.946 1.00 6.12 ? 221 LEU A N 1 ATOM 1025 C CA . LEU A 1 133 ? 3.849 6.723 7.389 1.00 5.94 ? 221 LEU A CA 1 ATOM 1026 C C . LEU A 1 133 ? 5.275 6.205 7.294 1.00 6.94 ? 221 LEU A C 1 ATOM 1027 O O . LEU A 1 133 ? 6.156 6.935 6.875 1.00 8.03 ? 221 LEU A O 1 ATOM 1028 C CB . LEU A 1 133 ? 3.295 6.699 5.978 1.00 7.45 ? 221 LEU A CB 1 ATOM 1029 C CG . LEU A 1 133 ? 1.904 7.222 5.755 1.00 7.36 ? 221 LEU A CG 1 ATOM 1030 C CD1 . LEU A 1 133 ? 1.542 7.136 4.300 1.00 9.60 ? 221 LEU A CD1 1 ATOM 1031 C CD2 . LEU A 1 133 ? 0.907 6.469 6.601 1.00 9.60 ? 221 LEU A CD2 1 ATOM 1032 N N . VAL A 1 134 ? 5.478 4.962 7.678 1.00 7.01 ? 222 VAL A N 1 ATOM 1033 C CA . VAL A 1 134 ? 6.696 4.217 7.340 1.00 6.58 ? 222 VAL A CA 1 ATOM 1034 C C . VAL A 1 134 ? 6.325 3.344 6.169 1.00 6.15 ? 222 VAL A C 1 ATOM 1035 O O . VAL A 1 134 ? 5.351 2.600 6.225 1.00 7.88 ? 222 VAL A O 1 ATOM 1036 C CB . VAL A 1 134 ? 7.167 3.386 8.528 1.00 7.69 ? 222 VAL A CB 1 ATOM 1037 C CG1 . VAL A 1 134 ? 8.230 2.374 8.106 1.00 9.07 ? 222 VAL A CG1 1 ATOM 1038 C CG2 . VAL A 1 134 ? 7.702 4.290 9.591 1.00 8.69 ? 222 VAL A CG2 1 ATOM 1039 N N . ILE A 1 135 ? 7.069 3.486 5.072 1.00 6.73 ? 223 ILE A N 1 ATOM 1040 C CA . ILE A 1 135 ? 6.794 2.741 3.851 1.00 7.19 ? 223 ILE A CA 1 ATOM 1041 C C . ILE A 1 135 ? 7.713 1.535 3.748 1.00 8.20 ? 223 ILE A C 1 ATOM 1042 O O . ILE A 1 135 ? 8.934 1.664 3.622 1.00 8.41 ? 223 ILE A O 1 ATOM 1043 C CB . ILE A 1 135 ? 6.983 3.642 2.632 1.00 8.44 ? 223 ILE A CB 1 ATOM 1044 C CG1 . ILE A 1 135 ? 6.126 4.918 2.795 1.00 8.98 ? 223 ILE A CG1 1 ATOM 1045 C CG2 . ILE A 1 135 ? 6.713 2.930 1.345 1.00 8.99 ? 223 ILE A CG2 1 ATOM 1046 C CD1 . ILE A 1 135 ? 4.632 4.674 2.865 1.00 10.78 ? 223 ILE A CD1 1 ATOM 1047 N N . GLU A 1 136 ? 7.069 0.358 3.853 1.00 7.68 ? 224 GLU A N 1 ATOM 1048 C CA . GLU A 1 136 ? 7.554 -0.955 3.471 1.00 8.53 ? 224 GLU A CA 1 ATOM 1049 C C . GLU A 1 136 ? 8.896 -1.316 4.105 1.00 7.58 ? 224 GLU A C 1 ATOM 1050 O O . GLU A 1 136 ? 9.938 -1.373 3.450 1.00 7.74 ? 224 GLU A O 1 ATOM 1051 C CB . GLU A 1 136 ? 7.602 -1.082 1.960 1.00 8.32 ? 224 GLU A CB 1 ATOM 1052 C CG . GLU A 1 136 ? 6.218 -1.000 1.287 1.00 8.45 ? 224 GLU A CG 1 ATOM 1053 C CD . GLU A 1 136 ? 5.271 -2.159 1.585 1.00 8.28 ? 224 GLU A CD 1 ATOM 1054 O OE1 . GLU A 1 136 ? 5.771 -3.285 1.925 1.00 8.89 ? 224 GLU A OE1 1 ATOM 1055 O OE2 . GLU A 1 136 ? 4.037 -1.981 1.386 1.00 7.78 ? 224 GLU A OE2 1 ATOM 1056 N N . PRO A 1 137 ? 8.846 -1.699 5.375 1.00 8.08 ? 225 PRO A N 1 ATOM 1057 C CA . PRO A 1 137 ? 9.973 -2.385 6.025 1.00 9.01 ? 225 PRO A CA 1 ATOM 1058 C C . PRO A 1 137 ? 10.451 -3.548 5.183 1.00 8.51 ? 225 PRO A C 1 ATOM 1059 O O . PRO A 1 137 ? 9.700 -4.230 4.506 1.00 8.85 ? 225 PRO A O 1 ATOM 1060 C CB . PRO A 1 137 ? 9.371 -2.877 7.338 1.00 10.12 ? 225 PRO A CB 1 ATOM 1061 C CG . PRO A 1 137 ? 8.240 -1.934 7.605 1.00 10.82 ? 225 PRO A CG 1 ATOM 1062 C CD . PRO A 1 137 ? 7.662 -1.616 6.259 1.00 8.66 ? 225 PRO A CD 1 ATOM 1063 N N . ASP A 1 138 ? 11.761 -3.827 5.243 1.00 9.68 ? 226 ASP A N 1 ATOM 1064 C CA . ASP A 1 138 ? 12.332 -5.045 4.663 1.00 9.67 ? 226 ASP A CA 1 ATOM 1065 C C . ASP A 1 138 ? 12.068 -5.134 3.167 1.00 9.53 ? 226 ASP A C 1 ATOM 1066 O O . ASP A 1 138 ? 11.737 -6.223 2.672 1.00 10.44 ? 226 ASP A O 1 ATOM 1067 C CB . ASP A 1 138 ? 11.799 -6.330 5.370 1.00 11.25 ? 226 ASP A CB 1 ATOM 1068 C CG . ASP A 1 138 ? 12.544 -7.587 4.973 1.00 13.22 ? 226 ASP A CG 1 ATOM 1069 O OD1 . ASP A 1 138 ? 13.734 -7.499 4.589 1.00 15.47 ? 226 ASP A OD1 1 ATOM 1070 O OD2 . ASP A 1 138 ? 12.005 -8.733 5.022 1.00 13.25 ? 226 ASP A OD2 1 ATOM 1071 N N . SER A 1 139 ? 12.182 -4.010 2.438 1.00 8.78 ? 227 SER A N 1 ATOM 1072 C CA . SER A 1 139 ? 11.947 -3.983 1.008 1.00 8.42 ? 227 SER A CA 1 ATOM 1073 C C . SER A 1 139 ? 13.196 -3.570 0.253 1.00 7.49 ? 227 SER A C 1 ATOM 1074 O O . SER A 1 139 ? 14.027 -4.431 -0.041 1.00 8.39 ? 227 SER A O 1 ATOM 1075 C CB . SER A 1 139 ? 10.716 -3.172 0.623 1.00 8.95 ? 227 SER A CB 1 ATOM 1076 O OG . SER A 1 139 ? 10.805 -1.817 0.937 1.00 8.51 ? 227 SER A OG 1 ATOM 1077 N N . LEU A 1 140 ? 13.367 -2.257 0.015 1.00 7.56 ? 228 LEU A N 1 ATOM 1078 C CA . LEU A 1 140 ? 14.491 -1.786 -0.800 1.00 8.23 ? 228 LEU A CA 1 ATOM 1079 C C . LEU A 1 140 ? 15.856 -2.039 -0.207 1.00 8.26 ? 228 LEU A C 1 ATOM 1080 O O . LEU A 1 140 ? 16.826 -2.114 -0.950 1.00 8.87 ? 228 LEU A O 1 ATOM 1081 C CB . LEU A 1 140 ? 14.319 -0.299 -1.106 1.00 9.08 ? 228 LEU A CB 1 ATOM 1082 C CG . LEU A 1 140 ? 13.133 -0.041 -2.051 1.00 10.91 ? 228 LEU A CG 1 ATOM 1083 C CD1 . LEU A 1 140 ? 12.835 1.463 -2.127 1.00 13.90 ? 228 LEU A CD1 1 ATOM 1084 C CD2 . LEU A 1 140 ? 13.386 -0.619 -3.446 1.00 12.33 ? 228 LEU A CD2 1 ATOM 1085 N N . ALA A 1 141 ? 15.969 -2.205 1.105 1.00 7.62 ? 229 ALA A N 1 ATOM 1086 C CA . ALA A 1 141 ? 17.287 -2.533 1.672 1.00 8.24 ? 229 ALA A CA 1 ATOM 1087 C C . ALA A 1 141 ? 17.828 -3.862 1.090 1.00 7.65 ? 229 ALA A C 1 ATOM 1088 O O . ALA A 1 141 ? 19.033 -4.064 0.945 1.00 8.77 ? 229 ALA A O 1 ATOM 1089 C CB . ALA A 1 141 ? 17.205 -2.580 3.175 1.00 8.26 ? 229 ALA A CB 1 ATOM 1090 N N . ASN A 1 142 ? 16.921 -4.740 0.682 1.00 7.89 ? 230 ASN A N 1 ATOM 1091 C CA . ASN A 1 142 ? 17.314 -5.989 0.049 1.00 7.85 ? 230 ASN A CA 1 ATOM 1092 C C . ASN A 1 142 ? 17.979 -5.757 -1.313 1.00 8.41 ? 230 ASN A C 1 ATOM 1093 O O . ASN A 1 142 ? 18.786 -6.599 -1.770 1.00 8.75 ? 230 ASN A O 1 ATOM 1094 C CB . ASN A 1 142 ? 16.114 -6.898 -0.146 1.00 7.92 ? 230 ASN A CB 1 ATOM 1095 C CG . ASN A 1 142 ? 15.586 -7.448 1.134 1.00 8.81 ? 230 ASN A CG 1 ATOM 1096 O OD1 . ASN A 1 142 ? 16.238 -8.259 1.793 1.00 9.86 ? 230 ASN A OD1 1 ATOM 1097 N ND2 . ASN A 1 142 ? 14.396 -6.980 1.541 1.00 11.67 ? 230 ASN A ND2 1 ATOM 1098 N N . MET A 1 143 ? 17.656 -4.661 -1.989 1.00 9.10 ? 231 MET A N 1 ATOM 1099 C CA . MET A 1 143 ? 18.271 -4.371 -3.287 1.00 9.91 ? 231 MET A CA 1 ATOM 1100 C C . MET A 1 143 ? 19.729 -4.035 -3.121 1.00 11.27 ? 231 MET A C 1 ATOM 1101 O O . MET A 1 143 ? 20.499 -4.164 -4.067 1.00 14.19 ? 231 MET A O 1 ATOM 1102 C CB . MET A 1 143 ? 17.520 -3.263 -4.040 1.00 11.93 ? 231 MET A CB 1 ATOM 1103 C CG . MET A 1 143 ? 16.374 -3.774 -4.819 1.00 12.97 ? 231 MET A CG 1 ATOM 1104 S SD . MET A 1 143 ? 14.908 -4.381 -3.921 1.00 13.30 ? 231 MET A SD 1 ATOM 1105 C CE . MET A 1 143 ? 15.171 -6.146 -3.882 1.00 11.94 ? 231 MET A CE 1 ATOM 1106 N N . VAL A 1 144 ? 20.134 -3.568 -1.943 1.00 10.54 ? 232 VAL A N 1 ATOM 1107 C CA . VAL A 1 144 ? 21.519 -3.199 -1.725 1.00 10.99 ? 232 VAL A CA 1 ATOM 1108 C C . VAL A 1 144 ? 22.399 -4.421 -1.492 1.00 11.51 ? 232 VAL A C 1 ATOM 1109 O O . VAL A 1 144 ? 23.508 -4.523 -2.053 1.00 13.82 ? 232 VAL A O 1 ATOM 1110 C CB . VAL A 1 144 ? 21.648 -2.184 -0.551 1.00 11.27 ? 232 VAL A CB 1 ATOM 1111 C CG1 . VAL A 1 144 ? 23.067 -1.776 -0.421 1.00 12.70 ? 232 VAL A CG1 1 ATOM 1112 C CG2 . VAL A 1 144 ? 20.739 -0.966 -0.781 1.00 12.34 ? 232 VAL A CG2 1 ATOM 1113 N N . THR A 1 145 ? 21.942 -5.382 -0.692 1.00 10.92 ? 233 THR A N 1 ATOM 1114 C CA . THR A 1 145 ? 22.817 -6.455 -0.221 1.00 11.60 ? 233 THR A CA 1 ATOM 1115 C C . THR A 1 145 ? 22.370 -7.856 -0.580 1.00 10.90 ? 233 THR A C 1 ATOM 1116 O O . THR A 1 145 ? 23.174 -8.761 -0.495 1.00 12.23 ? 233 THR A O 1 ATOM 1117 C CB . THR A 1 145 ? 23.011 -6.407 1.297 1.00 12.34 ? 233 THR A CB 1 ATOM 1118 O OG1 . THR A 1 145 ? 21.775 -6.670 1.929 1.00 11.97 ? 233 THR A OG1 1 ATOM 1119 C CG2 . THR A 1 145 ? 23.433 -5.040 1.787 1.00 13.20 ? 233 THR A CG2 1 ATOM 1120 N N . ASN A 1 146 ? 21.094 -8.057 -0.931 1.00 9.42 ? 234 ASN A N 1 ATOM 1121 C CA . ASN A 1 146 ? 20.501 -9.402 -1.038 1.00 9.47 ? 234 ASN A CA 1 ATOM 1122 C C . ASN A 1 146 ? 20.094 -9.799 -2.428 1.00 9.75 ? 234 ASN A C 1 ATOM 1123 O O . ASN A 1 146 ? 19.370 -10.753 -2.606 1.00 10.71 ? 234 ASN A O 1 ATOM 1124 C CB . ASN A 1 146 ? 19.328 -9.570 -0.058 1.00 9.56 ? 234 ASN A CB 1 ATOM 1125 C CG . ASN A 1 146 ? 19.764 -9.608 1.350 1.00 10.71 ? 234 ASN A CG 1 ATOM 1126 O OD1 . ASN A 1 146 ? 20.837 -10.125 1.655 1.00 14.01 ? 234 ASN A OD1 1 ATOM 1127 N ND2 . ASN A 1 146 ? 18.957 -9.052 2.234 1.00 11.42 ? 234 ASN A ND2 1 ATOM 1128 N N . MET A 1 147 ? 20.596 -9.106 -3.423 1.00 10.74 ? 235 MET A N 1 ATOM 1129 C CA . MET A 1 147 ? 20.261 -9.421 -4.814 1.00 12.57 ? 235 MET A CA 1 ATOM 1130 C C . MET A 1 147 ? 20.818 -10.751 -5.302 1.00 12.89 ? 235 MET A C 1 ATOM 1131 O O . MET A 1 147 ? 20.368 -11.253 -6.341 1.00 14.18 ? 235 MET A O 1 ATOM 1132 C CB . MET A 1 147 ? 20.768 -8.292 -5.721 1.00 14.48 ? 235 MET A CB 1 ATOM 1133 C CG . MET A 1 147 ? 20.109 -7.020 -5.412 1.00 17.41 ? 235 MET A CG 1 ATOM 1134 S SD . MET A 1 147 ? 18.491 -7.114 -5.969 1.00 22.84 ? 235 MET A SD 1 ATOM 1135 C CE . MET A 1 147 ? 18.905 -6.354 -7.388 1.00 12.35 ? 235 MET A CE 1 ATOM 1136 N N . ASN A 1 148 ? 21.775 -11.317 -4.570 1.00 12.69 ? 236 ASN A N 1 ATOM 1137 C CA . ASN A 1 148 ? 22.223 -12.683 -4.860 1.00 13.83 ? 236 ASN A CA 1 ATOM 1138 C C . ASN A 1 148 ? 21.100 -13.705 -4.631 1.00 13.55 ? 236 ASN A C 1 ATOM 1139 O O . ASN A 1 148 ? 21.164 -14.796 -5.167 1.00 15.43 ? 236 ASN A O 1 ATOM 1140 C CB . ASN A 1 148 ? 23.442 -13.024 -4.003 1.00 16.15 ? 236 ASN A CB 1 ATOM 1141 C CG . ASN A 1 148 ? 23.164 -12.817 -2.500 1.00 21.20 ? 236 ASN A CG 1 ATOM 1142 O OD1 . ASN A 1 148 ? 23.096 -11.664 -1.994 1.00 25.20 ? 236 ASN A OD1 1 ATOM 1143 N ND2 . ASN A 1 148 ? 22.910 -13.918 -1.800 1.00 26.34 ? 236 ASN A ND2 1 ATOM 1144 N N . VAL A 1 149 ? 20.106 -13.383 -3.797 1.00 11.51 ? 237 VAL A N 1 ATOM 1145 C CA . VAL A 1 149 ? 18.992 -14.281 -3.545 1.00 11.68 ? 237 VAL A CA 1 ATOM 1146 C C . VAL A 1 149 ? 18.064 -14.200 -4.756 1.00 11.61 ? 237 VAL A C 1 ATOM 1147 O O . VAL A 1 149 ? 17.602 -13.108 -5.100 1.00 10.79 ? 237 VAL A O 1 ATOM 1148 C CB . VAL A 1 149 ? 18.233 -13.873 -2.276 1.00 11.59 ? 237 VAL A CB 1 ATOM 1149 C CG1 . VAL A 1 149 ? 17.030 -14.800 -2.064 1.00 13.20 ? 237 VAL A CG1 1 ATOM 1150 C CG2 . VAL A 1 149 ? 19.150 -13.891 -1.062 1.00 12.01 ? 237 VAL A CG2 1 ATOM 1151 N N . PRO A 1 150 ? 17.821 -15.286 -5.469 1.00 12.27 ? 238 PRO A N 1 ATOM 1152 C CA . PRO A 1 150 ? 17.046 -15.212 -6.697 1.00 12.74 ? 238 PRO A CA 1 ATOM 1153 C C . PRO A 1 150 ? 15.686 -14.502 -6.551 1.00 10.99 ? 238 PRO A C 1 ATOM 1154 O O . PRO A 1 150 ? 15.341 -13.723 -7.438 1.00 11.62 ? 238 PRO A O 1 ATOM 1155 C CB . PRO A 1 150 ? 16.907 -16.690 -7.087 1.00 13.34 ? 238 PRO A CB 1 ATOM 1156 C CG . PRO A 1 150 ? 18.200 -17.257 -6.635 1.00 15.03 ? 238 PRO A CG 1 ATOM 1157 C CD . PRO A 1 150 ? 18.455 -16.616 -5.294 1.00 13.27 ? 238 PRO A CD 1 ATOM 1158 N N . LYS A 1 151 ? 14.963 -14.719 -5.473 1.00 10.29 ? 239 LYS A N 1 ATOM 1159 C CA . LYS A 1 151 ? 13.665 -14.067 -5.312 1.00 9.94 ? 239 LYS A CA 1 ATOM 1160 C C . LYS A 1 151 ? 13.859 -12.540 -5.229 1.00 9.82 ? 239 LYS A C 1 ATOM 1161 O O . LYS A 1 151 ? 13.030 -11.797 -5.711 1.00 10.04 ? 239 LYS A O 1 ATOM 1162 C CB . LYS A 1 151 ? 12.948 -14.561 -4.052 1.00 10.16 ? 239 LYS A CB 1 ATOM 1163 C CG . LYS A 1 151 ? 11.519 -14.033 -3.916 1.00 11.38 ? 239 LYS A CG 1 ATOM 1164 C CD . LYS A 1 151 ? 10.761 -14.752 -2.781 1.00 11.88 ? 239 LYS A CD 1 ATOM 1165 C CE . LYS A 1 151 ? 9.359 -14.203 -2.797 1.00 14.55 ? 239 LYS A CE 1 ATOM 1166 N NZ . LYS A 1 151 ? 8.489 -15.002 -1.904 1.00 17.79 ? 239 LYS A NZ 1 ATOM 1167 N N . CYS A 1 152 ? 14.934 -12.071 -4.611 1.00 9.42 ? 240 CYS A N 1 ATOM 1168 C CA A CYS A 1 152 ? 15.195 -10.617 -4.564 0.75 9.11 ? 240 CYS A CA 1 ATOM 1169 C CA B CYS A 1 152 ? 15.231 -10.659 -4.545 0.25 9.91 ? 240 CYS A CA 1 ATOM 1170 C C . CYS A 1 152 ? 15.560 -10.073 -5.919 1.00 9.90 ? 240 CYS A C 1 ATOM 1171 O O . CYS A 1 152 ? 15.087 -8.991 -6.296 1.00 10.20 ? 240 CYS A O 1 ATOM 1172 C CB A CYS A 1 152 ? 16.305 -10.286 -3.577 0.75 9.57 ? 240 CYS A CB 1 ATOM 1173 C CB B CYS A 1 152 ? 16.400 -10.504 -3.594 0.25 10.23 ? 240 CYS A CB 1 ATOM 1174 S SG A CYS A 1 152 ? 15.863 -10.541 -1.853 0.75 11.54 ? 240 CYS A SG 1 ATOM 1175 S SG B CYS A 1 152 ? 16.864 -8.831 -3.281 0.25 11.94 ? 240 CYS A SG 1 ATOM 1176 N N . SER A 1 153 ? 16.405 -10.748 -6.691 1.00 10.59 ? 241 SER A N 1 ATOM 1177 C CA A SER A 1 153 ? 16.714 -10.272 -8.038 0.53 11.03 ? 241 SER A CA 1 ATOM 1178 C CA B SER A 1 153 ? 16.710 -10.212 -8.017 0.47 10.94 ? 241 SER A CA 1 ATOM 1179 C C . SER A 1 153 ? 15.437 -10.190 -8.854 1.00 10.29 ? 241 SER A C 1 ATOM 1180 O O . SER A 1 153 ? 15.257 -9.275 -9.643 1.00 10.74 ? 241 SER A O 1 ATOM 1181 C CB A SER A 1 153 ? 17.712 -11.218 -8.722 0.53 11.84 ? 241 SER A CB 1 ATOM 1182 C CB B SER A 1 153 ? 17.850 -10.973 -8.719 0.47 11.77 ? 241 SER A CB 1 ATOM 1183 O OG A SER A 1 153 ? 18.256 -10.633 -9.893 0.53 15.55 ? 241 SER A OG 1 ATOM 1184 O OG B SER A 1 153 ? 17.565 -12.351 -8.833 0.47 14.41 ? 241 SER A OG 1 ATOM 1185 N N . GLY A 1 154 ? 14.547 -11.168 -8.654 1.00 9.47 ? 242 GLY A N 1 ATOM 1186 C CA . GLY A 1 154 ? 13.291 -11.207 -9.384 1.00 9.92 ? 242 GLY A CA 1 ATOM 1187 C C . GLY A 1 154 ? 12.320 -10.131 -8.955 1.00 9.38 ? 242 GLY A C 1 ATOM 1188 O O . GLY A 1 154 ? 11.524 -9.750 -9.777 1.00 11.72 ? 242 GLY A O 1 ATOM 1189 N N . ALA A 1 155 ? 12.379 -9.688 -7.694 1.00 9.44 ? 243 ALA A N 1 ATOM 1190 C CA . ALA A 1 155 ? 11.413 -8.721 -7.149 1.00 9.36 ? 243 ALA A CA 1 ATOM 1191 C C . ALA A 1 155 ? 11.871 -7.280 -7.274 1.00 9.43 ? 243 ALA A C 1 ATOM 1192 O O . ALA A 1 155 ? 11.055 -6.363 -7.179 1.00 9.01 ? 243 ALA A O 1 ATOM 1193 C CB . ALA A 1 155 ? 11.134 -9.020 -5.699 1.00 10.58 ? 243 ALA A CB 1 ATOM 1194 N N . ALA A 1 156 ? 13.147 -7.065 -7.531 1.00 8.64 ? 244 ALA A N 1 ATOM 1195 C CA . ALA A 1 156 ? 13.731 -5.742 -7.410 1.00 9.15 ? 244 ALA A CA 1 ATOM 1196 C C . ALA A 1 156 ? 13.035 -4.694 -8.254 1.00 8.59 ? 244 ALA A C 1 ATOM 1197 O O . ALA A 1 156 ? 12.741 -3.590 -7.766 1.00 8.78 ? 244 ALA A O 1 ATOM 1198 C CB . ALA A 1 156 ? 15.191 -5.793 -7.728 1.00 9.58 ? 244 ALA A CB 1 ATOM 1199 N N . SER A 1 157 ? 12.792 -4.979 -9.529 1.00 8.79 ? 245 SER A N 1 ATOM 1200 C CA . SER A 1 157 ? 12.188 -3.943 -10.390 1.00 10.25 ? 245 SER A CA 1 ATOM 1201 C C . SER A 1 157 ? 10.777 -3.598 -9.914 1.00 9.95 ? 245 SER A C 1 ATOM 1202 O O . SER A 1 157 ? 10.362 -2.440 -9.943 1.00 9.83 ? 245 SER A O 1 ATOM 1203 C CB . SER A 1 157 ? 12.238 -4.343 -11.840 1.00 11.11 ? 245 SER A CB 1 ATOM 1204 O OG . SER A 1 157 ? 13.580 -4.415 -12.316 1.00 18.22 ? 245 SER A OG 1 ATOM 1205 N N . THR A 1 158 ? 10.051 -4.585 -9.425 1.00 8.82 ? 246 THR A N 1 ATOM 1206 C CA . THR A 1 158 ? 8.716 -4.407 -8.886 1.00 9.12 ? 246 THR A CA 1 ATOM 1207 C C . THR A 1 158 ? 8.746 -3.641 -7.591 1.00 9.06 ? 246 THR A C 1 ATOM 1208 O O . THR A 1 158 ? 7.933 -2.727 -7.381 1.00 9.12 ? 246 THR A O 1 ATOM 1209 C CB . THR A 1 158 ? 8.056 -5.779 -8.679 1.00 9.93 ? 246 THR A CB 1 ATOM 1210 O OG1 . THR A 1 158 ? 7.905 -6.430 -9.942 1.00 12.11 ? 246 THR A OG1 1 ATOM 1211 C CG2 . THR A 1 158 ? 6.635 -5.637 -8.105 1.00 11.82 ? 246 THR A CG2 1 ATOM 1212 N N . TYR A 1 159 ? 9.683 -3.965 -6.700 1.00 8.41 ? 247 TYR A N 1 ATOM 1213 C CA . TYR A 1 159 ? 9.809 -3.167 -5.489 1.00 8.47 ? 247 TYR A CA 1 ATOM 1214 C C . TYR A 1 159 ? 10.037 -1.704 -5.824 1.00 8.33 ? 247 TYR A C 1 ATOM 1215 O O . TYR A 1 159 ? 9.459 -0.829 -5.219 1.00 8.82 ? 247 TYR A O 1 ATOM 1216 C CB . TYR A 1 159 ? 10.920 -3.633 -4.562 1.00 8.49 ? 247 TYR A CB 1 ATOM 1217 C CG . TYR A 1 159 ? 10.718 -4.866 -3.719 1.00 8.56 ? 247 TYR A CG 1 ATOM 1218 C CD1 . TYR A 1 159 ? 9.642 -5.754 -3.876 1.00 9.09 ? 247 TYR A CD1 1 ATOM 1219 C CD2 . TYR A 1 159 ? 11.637 -5.133 -2.734 1.00 9.16 ? 247 TYR A CD2 1 ATOM 1220 C CE1 . TYR A 1 159 ? 9.535 -6.848 -3.064 1.00 9.11 ? 247 TYR A CE1 1 ATOM 1221 C CE2 . TYR A 1 159 ? 11.543 -6.254 -1.926 1.00 9.84 ? 247 TYR A CE2 1 ATOM 1222 C CZ . TYR A 1 159 ? 10.486 -7.086 -2.088 1.00 9.96 ? 247 TYR A CZ 1 ATOM 1223 O OH . TYR A 1 159 ? 10.478 -8.220 -1.275 1.00 11.10 ? 247 TYR A OH 1 ATOM 1224 N N . ARG A 1 160 ? 10.889 -1.446 -6.781 1.00 7.58 ? 248 ARG A N 1 ATOM 1225 C CA . ARG A 1 160 ? 11.197 -0.051 -7.135 0.40 6.83 ? 248 ARG A CA 1 ATOM 1226 C C . ARG A 1 160 ? 9.958 0.645 -7.701 1.00 8.54 ? 248 ARG A C 1 ATOM 1227 O O . ARG A 1 160 ? 9.590 1.751 -7.285 1.00 10.58 ? 248 ARG A O 1 ATOM 1228 C CB A ARG A 1 160 ? 12.404 0.044 -8.088 0.60 9.50 ? 248 ARG A CB 1 ATOM 1229 C CB B ARG A 1 160 ? 12.300 -0.035 -8.207 0.40 8.88 ? 248 ARG A CB 1 ATOM 1230 C CG A ARG A 1 160 ? 12.343 1.207 -9.016 0.60 13.17 ? 248 ARG A CG 1 ATOM 1231 C CG B ARG A 1 160 ? 12.953 1.280 -8.342 0.40 10.04 ? 248 ARG A CG 1 ATOM 1232 C CD A ARG A 1 160 ? 13.538 1.302 -9.980 0.60 15.90 ? 248 ARG A CD 1 ATOM 1233 C CD B ARG A 1 160 ? 14.219 1.278 -9.158 0.40 13.09 ? 248 ARG A CD 1 ATOM 1234 N NE A ARG A 1 160 ? 13.594 2.622 -10.589 0.60 18.01 ? 248 ARG A NE 1 ATOM 1235 N NE B ARG A 1 160 ? 14.872 2.562 -9.012 0.40 12.83 ? 248 ARG A NE 1 ATOM 1236 C CZ A ARG A 1 160 ? 12.727 3.078 -11.497 0.60 19.32 ? 248 ARG A CZ 1 ATOM 1237 C CZ B ARG A 1 160 ? 14.495 3.678 -9.607 0.40 13.69 ? 248 ARG A CZ 1 ATOM 1238 N NH1 A ARG A 1 160 ? 11.745 2.296 -11.929 0.60 22.74 ? 248 ARG A NH1 1 ATOM 1239 N NH1 B ARG A 1 160 ? 13.512 3.702 -10.507 0.40 13.44 ? 248 ARG A NH1 1 ATOM 1240 N NH2 A ARG A 1 160 ? 12.831 4.320 -11.966 0.60 20.52 ? 248 ARG A NH2 1 ATOM 1241 N NH2 B ARG A 1 160 ? 15.168 4.768 -9.345 0.40 13.27 ? 248 ARG A NH2 1 ATOM 1242 N N . GLU A 1 161 ? 9.309 -0.003 -8.655 1.00 8.72 ? 249 GLU A N 1 ATOM 1243 C CA . GLU A 1 161 ? 8.157 0.607 -9.313 1.00 9.48 ? 249 GLU A CA 1 ATOM 1244 C C . GLU A 1 161 ? 6.992 0.860 -8.350 1.00 8.17 ? 249 GLU A C 1 ATOM 1245 O O . GLU A 1 161 ? 6.352 1.900 -8.404 1.00 8.23 ? 249 GLU A O 1 ATOM 1246 C CB . GLU A 1 161 ? 7.653 -0.258 -10.460 1.00 11.50 ? 249 GLU A CB 1 ATOM 1247 C CG . GLU A 1 161 ? 6.353 0.133 -11.160 1.00 18.33 ? 249 GLU A CG 1 ATOM 1248 C CD . GLU A 1 161 ? 5.827 -0.945 -12.106 0.50 22.65 ? 249 GLU A CD 1 ATOM 1249 O OE1 . GLU A 1 161 ? 6.659 -1.490 -12.879 0.50 26.67 ? 249 GLU A OE1 1 ATOM 1250 O OE2 . GLU A 1 161 ? 4.591 -1.234 -12.097 0.50 24.69 ? 249 GLU A OE2 1 ATOM 1251 N N . LEU A 1 162 ? 6.718 -0.102 -7.470 1.00 7.29 ? 250 LEU A N 1 ATOM 1252 C CA . LEU A 1 162 ? 5.619 0.004 -6.539 1.00 7.64 ? 250 LEU A CA 1 ATOM 1253 C C . LEU A 1 162 ? 5.959 0.979 -5.419 1.00 8.05 ? 250 LEU A C 1 ATOM 1254 O O . LEU A 1 162 ? 5.049 1.614 -4.872 1.00 8.45 ? 250 LEU A O 1 ATOM 1255 C CB . LEU A 1 162 ? 5.236 -1.367 -5.976 1.00 7.51 ? 250 LEU A CB 1 ATOM 1256 C CG . LEU A 1 162 ? 4.596 -2.267 -7.005 1.00 8.56 ? 250 LEU A CG 1 ATOM 1257 C CD1 . LEU A 1 162 ? 4.244 -3.548 -6.342 1.00 9.54 ? 250 LEU A CD1 1 ATOM 1258 C CD2 . LEU A 1 162 ? 3.382 -1.674 -7.685 1.00 10.96 ? 250 LEU A CD2 1 ATOM 1259 N N . THR A 1 163 ? 7.232 1.111 -5.057 1.00 7.59 ? 251 THR A N 1 ATOM 1260 C CA . THR A 1 163 ? 7.605 2.148 -4.095 1.00 7.85 ? 251 THR A CA 1 ATOM 1261 C C . THR A 1 163 ? 7.351 3.519 -4.678 1.00 8.58 ? 251 THR A C 1 ATOM 1262 O O . THR A 1 163 ? 6.733 4.366 -4.028 1.00 8.36 ? 251 THR A O 1 ATOM 1263 C CB . THR A 1 163 ? 9.052 2.000 -3.663 1.00 9.38 ? 251 THR A CB 1 ATOM 1264 O OG1 . THR A 1 163 ? 9.220 0.698 -3.075 1.00 11.46 ? 251 THR A OG1 1 ATOM 1265 C CG2 . THR A 1 163 ? 9.372 3.030 -2.559 1.00 10.54 ? 251 THR A CG2 1 ATOM 1266 N N . ILE A 1 164 ? 7.799 3.747 -5.898 1.00 7.63 ? 252 ILE A N 1 ATOM 1267 C CA . ILE A 1 164 ? 7.549 5.004 -6.585 1.00 7.94 ? 252 ILE A CA 1 ATOM 1268 C C . ILE A 1 164 ? 6.054 5.280 -6.655 1.00 8.40 ? 252 ILE A C 1 ATOM 1269 O O . ILE A 1 164 ? 5.611 6.398 -6.387 1.00 8.60 ? 252 ILE A O 1 ATOM 1270 C CB . ILE A 1 164 ? 8.258 5.061 -7.943 1.00 8.83 ? 252 ILE A CB 1 ATOM 1271 C CG1 . ILE A 1 164 ? 9.772 5.083 -7.735 1.00 9.22 ? 252 ILE A CG1 1 ATOM 1272 C CG2 . ILE A 1 164 ? 7.821 6.272 -8.704 1.00 10.21 ? 252 ILE A CG2 1 ATOM 1273 C CD1 . ILE A 1 164 ? 10.569 4.824 -8.981 1.00 12.95 ? 252 ILE A CD1 1 ATOM 1274 N N . TYR A 1 165 ? 5.252 4.278 -6.992 1.00 8.69 ? 253 TYR A N 1 ATOM 1275 C CA . TYR A 1 165 ? 3.827 4.408 -6.995 1.00 8.41 ? 253 TYR A CA 1 ATOM 1276 C C . TYR A 1 165 ? 3.285 4.881 -5.666 1.00 8.56 ? 253 TYR A C 1 ATOM 1277 O O . TYR A 1 165 ? 2.479 5.797 -5.620 1.00 9.13 ? 253 TYR A O 1 ATOM 1278 C CB . TYR A 1 165 ? 3.174 3.076 -7.414 1.00 9.12 ? 253 TYR A CB 1 ATOM 1279 C CG . TYR A 1 165 ? 1.699 3.146 -7.658 1.00 8.35 ? 253 TYR A CG 1 ATOM 1280 C CD1 . TYR A 1 165 ? 1.213 3.632 -8.856 1.00 11.61 ? 253 TYR A CD1 1 ATOM 1281 C CD2 . TYR A 1 165 ? 0.784 2.779 -6.700 1.00 8.26 ? 253 TYR A CD2 1 ATOM 1282 C CE1 . TYR A 1 165 ? -0.123 3.679 -9.103 1.00 10.82 ? 253 TYR A CE1 1 ATOM 1283 C CE2 . TYR A 1 165 ? -0.580 2.867 -6.923 1.00 9.70 ? 253 TYR A CE2 1 ATOM 1284 C CZ . TYR A 1 165 ? -1.023 3.325 -8.127 1.00 10.64 ? 253 TYR A CZ 1 ATOM 1285 O OH . TYR A 1 165 ? -2.369 3.425 -8.393 1.00 13.60 ? 253 TYR A OH 1 ATOM 1286 N N . ALA A 1 166 ? 3.677 4.230 -4.599 1.00 8.61 ? 254 ALA A N 1 ATOM 1287 C CA . ALA A 1 166 ? 3.232 4.610 -3.276 1.00 8.95 ? 254 ALA A CA 1 ATOM 1288 C C . ALA A 1 166 ? 3.635 6.027 -2.922 1.00 8.22 ? 254 ALA A C 1 ATOM 1289 O O . ALA A 1 166 ? 2.864 6.762 -2.294 1.00 9.18 ? 254 ALA A O 1 ATOM 1290 C CB . ALA A 1 166 ? 3.795 3.647 -2.264 1.00 9.12 ? 254 ALA A CB 1 ATOM 1291 N N . LEU A 1 167 ? 4.877 6.387 -3.209 1.00 7.64 ? 255 LEU A N 1 ATOM 1292 C CA . LEU A 1 167 ? 5.335 7.712 -2.864 1.00 8.03 ? 255 LEU A CA 1 ATOM 1293 C C . LEU A 1 167 ? 4.529 8.792 -3.571 1.00 8.02 ? 255 LEU A C 1 ATOM 1294 O O . LEU A 1 167 ? 4.288 9.844 -3.004 1.00 10.05 ? 255 LEU A O 1 ATOM 1295 C CB . LEU A 1 167 ? 6.812 7.888 -3.180 1.00 8.84 ? 255 LEU A CB 1 ATOM 1296 C CG . LEU A 1 167 ? 7.838 6.979 -2.480 1.00 9.77 ? 255 LEU A CG 1 ATOM 1297 C CD1 . LEU A 1 167 ? 9.217 7.345 -2.952 1.00 10.65 ? 255 LEU A CD1 1 ATOM 1298 C CD2 . LEU A 1 167 ? 7.759 6.974 -0.975 1.00 11.26 ? 255 LEU A CD2 1 ATOM 1299 N N . LYS A 1 168 ? 4.169 8.567 -4.813 1.00 7.92 ? 256 LYS A N 1 ATOM 1300 C CA . LYS A 1 168 ? 3.392 9.543 -5.560 1.00 8.26 ? 256 LYS A CA 1 ATOM 1301 C C . LYS A 1 168 ? 1.937 9.537 -5.141 1.00 8.21 ? 256 LYS A C 1 ATOM 1302 O O . LYS A 1 168 ? 1.298 10.562 -5.054 1.00 8.88 ? 256 LYS A O 1 ATOM 1303 C CB . LYS A 1 168 ? 3.475 9.279 -7.061 1.00 9.17 ? 256 LYS A CB 1 ATOM 1304 C CG . LYS A 1 168 ? 4.841 9.465 -7.677 1.00 11.62 ? 256 LYS A CG 1 ATOM 1305 C CD . LYS A 1 168 ? 4.838 9.161 -9.166 1.00 20.14 ? 256 LYS A CD 1 ATOM 1306 C CE . LYS A 1 168 ? 4.577 10.413 -9.930 1.00 24.71 ? 256 LYS A CE 1 ATOM 1307 N NZ . LYS A 1 168 ? 5.747 11.343 -9.797 1.00 29.88 ? 256 LYS A NZ 1 ATOM 1308 N N . GLN A 1 169 ? 1.361 8.390 -4.923 1.00 8.27 ? 257 GLN A N 1 ATOM 1309 C CA . GLN A 1 169 ? -0.037 8.295 -4.547 1.00 8.19 ? 257 GLN A CA 1 ATOM 1310 C C . GLN A 1 169 ? -0.330 8.766 -3.142 1.00 7.48 ? 257 GLN A C 1 ATOM 1311 O O . GLN A 1 169 ? -1.402 9.319 -2.867 1.00 9.63 ? 257 GLN A O 1 ATOM 1312 C CB . GLN A 1 169 ? -0.561 6.875 -4.747 1.00 8.89 ? 257 GLN A CB 1 ATOM 1313 C CG . GLN A 1 169 ? -0.600 6.442 -6.209 1.00 11.15 ? 257 GLN A CG 1 ATOM 1314 C CD . GLN A 1 169 ? -1.660 7.137 -7.060 1.00 14.90 ? 257 GLN A CD 1 ATOM 1315 O OE1 . GLN A 1 169 ? -2.731 7.511 -6.574 1.00 18.84 ? 257 GLN A OE1 1 ATOM 1316 N NE2 . GLN A 1 169 ? -1.394 7.226 -8.346 1.00 17.11 ? 257 GLN A NE2 1 ATOM 1317 N N . LEU A 1 170 ? 0.579 8.529 -2.227 1.00 6.79 ? 258 LEU A N 1 ATOM 1318 C CA . LEU A 1 170 ? 0.376 8.910 -0.840 1.00 6.93 ? 258 LEU A CA 1 ATOM 1319 C C . LEU A 1 170 ? 1.009 10.277 -0.497 1.00 7.46 ? 258 LEU A C 1 ATOM 1320 O O . LEU A 1 170 ? 1.009 10.679 0.657 1.00 8.42 ? 258 LEU A O 1 ATOM 1321 C CB . LEU A 1 170 ? 0.847 7.812 0.101 1.00 7.52 ? 258 LEU A CB 1 ATOM 1322 C CG . LEU A 1 170 ? 0.188 6.453 -0.141 1.00 7.30 ? 258 LEU A CG 1 ATOM 1323 C CD1 . LEU A 1 170 ? 0.706 5.466 0.874 1.00 10.02 ? 258 LEU A CD1 1 ATOM 1324 C CD2 . LEU A 1 170 ? -1.306 6.520 -0.110 1.00 9.95 ? 258 LEU A CD2 1 ATOM 1325 N N . ASP A 1 171 ? 1.440 11.006 -1.529 1.00 7.40 ? 259 ASP A N 1 ATOM 1326 C CA . ASP A 1 171 ? 1.927 12.369 -1.405 1.00 8.44 ? 259 ASP A CA 1 ATOM 1327 C C . ASP A 1 171 ? 0.756 13.344 -1.227 1.00 8.14 ? 259 ASP A C 1 ATOM 1328 O O . ASP A 1 171 ? 0.263 13.925 -2.178 1.00 10.66 ? 259 ASP A O 1 ATOM 1329 C CB . ASP A 1 171 ? 2.754 12.708 -2.621 1.00 8.31 ? 259 ASP A CB 1 ATOM 1330 C CG . ASP A 1 171 ? 3.259 14.133 -2.662 1.00 9.30 ? 259 ASP A CG 1 ATOM 1331 O OD1 . ASP A 1 171 ? 3.505 14.706 -1.593 1.00 10.62 ? 259 ASP A OD1 1 ATOM 1332 O OD2 . ASP A 1 171 ? 3.485 14.716 -3.773 1.00 11.72 ? 259 ASP A OD2 1 ATOM 1333 N N . LEU A 1 172 ? 0.318 13.464 0.008 1.00 8.12 ? 260 LEU A N 1 ATOM 1334 C CA . LEU A 1 172 ? -0.859 14.238 0.390 1.00 7.28 ? 260 LEU A CA 1 ATOM 1335 C C . LEU A 1 172 ? -0.385 15.299 1.355 1.00 7.55 ? 260 LEU A C 1 ATOM 1336 O O . LEU A 1 172 ? 0.552 15.092 2.068 1.00 7.66 ? 260 LEU A O 1 ATOM 1337 C CB . LEU A 1 172 ? -1.914 13.353 1.061 1.00 8.40 ? 260 LEU A CB 1 ATOM 1338 C CG . LEU A 1 172 ? -2.418 12.198 0.186 1.00 8.99 ? 260 LEU A CG 1 ATOM 1339 C CD1 . LEU A 1 172 ? -3.341 11.311 1.022 1.00 10.99 ? 260 LEU A CD1 1 ATOM 1340 C CD2 . LEU A 1 172 ? -3.111 12.692 -1.014 1.00 12.05 ? 260 LEU A CD2 1 ATOM 1341 N N . PRO A 1 173 ? -1.037 16.463 1.377 1.00 7.55 ? 261 PRO A N 1 ATOM 1342 C CA . PRO A 1 173 ? -0.554 17.577 2.215 1.00 6.63 ? 261 PRO A CA 1 ATOM 1343 C C . PRO A 1 173 ? -0.405 17.312 3.694 1.00 7.05 ? 261 PRO A C 1 ATOM 1344 O O . PRO A 1 173 ? 0.430 17.941 4.335 1.00 6.71 ? 261 PRO A O 1 ATOM 1345 C CB . PRO A 1 173 ? -1.575 18.687 1.937 1.00 7.50 ? 261 PRO A CB 1 ATOM 1346 C CG . PRO A 1 173 ? -2.004 18.411 0.562 1.00 8.92 ? 261 PRO A CG 1 ATOM 1347 C CD . PRO A 1 173 ? -2.057 16.903 0.415 1.00 7.72 ? 261 PRO A CD 1 ATOM 1348 N N . HIS A 1 174 ? -1.213 16.423 4.246 1.00 6.15 ? 262 HIS A N 1 ATOM 1349 C CA . HIS A 1 174 ? -1.225 16.148 5.671 1.00 6.65 ? 262 HIS A CA 1 ATOM 1350 C C . HIS A 1 174 ? -0.380 14.920 6.042 1.00 6.77 ? 262 HIS A C 1 ATOM 1351 O O . HIS A 1 174 ? -0.396 14.524 7.218 1.00 7.41 ? 262 HIS A O 1 ATOM 1352 C CB . HIS A 1 174 ? -2.662 15.978 6.185 1.00 6.71 ? 262 HIS A CB 1 ATOM 1353 C CG . HIS A 1 174 ? -3.345 14.796 5.600 1.00 7.57 ? 262 HIS A CG 1 ATOM 1354 N ND1 . HIS A 1 174 ? -3.636 14.718 4.271 1.00 8.66 ? 262 HIS A ND1 1 ATOM 1355 C CD2 . HIS A 1 174 ? -3.827 13.674 6.179 1.00 7.70 ? 262 HIS A CD2 1 ATOM 1356 C CE1 . HIS A 1 174 ? -4.247 13.576 4.048 1.00 9.21 ? 262 HIS A CE1 1 ATOM 1357 N NE2 . HIS A 1 174 ? -4.396 12.931 5.187 1.00 8.61 ? 262 HIS A NE2 1 ATOM 1358 N N . VAL A 1 175 ? 0.361 14.378 5.090 1.00 6.00 ? 263 VAL A N 1 ATOM 1359 C CA . VAL A 1 175 ? 1.150 13.171 5.283 1.00 7.31 ? 263 VAL A CA 1 ATOM 1360 C C . VAL A 1 175 ? 2.627 13.457 5.279 1.00 7.20 ? 263 VAL A C 1 ATOM 1361 O O . VAL A 1 175 ? 3.104 14.335 4.586 1.00 8.08 ? 263 VAL A O 1 ATOM 1362 C CB . VAL A 1 175 ? 0.808 12.184 4.140 1.00 7.84 ? 263 VAL A CB 1 ATOM 1363 C CG1 . VAL A 1 175 ? 1.790 11.036 4.047 1.00 8.33 ? 263 VAL A CG1 1 ATOM 1364 C CG2 . VAL A 1 175 ? -0.598 11.671 4.282 1.00 9.00 ? 263 VAL A CG2 1 ATOM 1365 N N . ALA A 1 176 ? 3.362 12.684 6.064 1.00 7.14 ? 264 ALA A N 1 ATOM 1366 C CA . ALA A 1 176 ? 4.806 12.595 5.956 1.00 6.81 ? 264 ALA A CA 1 ATOM 1367 C C . ALA A 1 176 ? 5.171 11.121 5.798 1.00 6.59 ? 264 ALA A C 1 ATOM 1368 O O . ALA A 1 176 ? 4.670 10.285 6.553 1.00 9.27 ? 264 ALA A O 1 ATOM 1369 C CB . ALA A 1 176 ? 5.483 13.145 7.206 1.00 8.19 ? 264 ALA A CB 1 ATOM 1370 N N . MET A 1 177 ? 6.020 10.826 4.827 1.00 6.81 ? 265 MET A N 1 ATOM 1371 C CA . MET A 1 177 ? 6.479 9.464 4.606 1.00 6.73 ? 265 MET A CA 1 ATOM 1372 C C . MET A 1 177 ? 7.978 9.337 4.826 1.00 7.02 ? 265 MET A C 1 ATOM 1373 O O . MET A 1 177 ? 8.787 10.189 4.443 1.00 7.18 ? 265 MET A O 1 ATOM 1374 C CB . MET A 1 177 ? 6.247 9.074 3.144 1.00 8.37 ? 265 MET A CB 1 ATOM 1375 C CG . MET A 1 177 ? 4.838 8.692 2.823 1.00 8.76 ? 265 MET A CG 1 ATOM 1376 S SD . MET A 1 177 ? 4.555 8.291 1.100 1.00 9.63 ? 265 MET A SD 1 ATOM 1377 C CE . MET A 1 177 ? 4.435 9.887 0.476 1.00 9.04 ? 265 MET A CE 1 ATOM 1378 N N . TYR A 1 178 ? 8.356 8.232 5.460 1.00 6.20 ? 266 TYR A N 1 ATOM 1379 C CA . TYR A 1 178 ? 9.728 7.784 5.642 1.00 6.77 ? 266 TYR A CA 1 ATOM 1380 C C . TYR A 1 178 ? 9.853 6.379 5.062 1.00 6.56 ? 266 TYR A C 1 ATOM 1381 O O . TYR A 1 178 ? 9.176 5.477 5.485 1.00 7.59 ? 266 TYR A O 1 ATOM 1382 C CB . TYR A 1 178 ? 10.059 7.742 7.110 1.00 6.17 ? 266 TYR A CB 1 ATOM 1383 C CG . TYR A 1 178 ? 9.952 9.087 7.797 1.00 5.75 ? 266 TYR A CG 1 ATOM 1384 C CD1 . TYR A 1 178 ? 8.744 9.536 8.284 1.00 6.71 ? 266 TYR A CD1 1 ATOM 1385 C CD2 . TYR A 1 178 ? 11.035 9.886 8.007 1.00 6.41 ? 266 TYR A CD2 1 ATOM 1386 C CE1 . TYR A 1 178 ? 8.635 10.745 8.947 1.00 6.83 ? 266 TYR A CE1 1 ATOM 1387 C CE2 . TYR A 1 178 ? 10.942 11.092 8.631 1.00 6.18 ? 266 TYR A CE2 1 ATOM 1388 C CZ . TYR A 1 178 ? 9.740 11.528 9.138 1.00 6.47 ? 266 TYR A CZ 1 ATOM 1389 O OH . TYR A 1 178 ? 9.622 12.715 9.829 1.00 8.64 ? 266 TYR A OH 1 ATOM 1390 N N . MET A 1 179 ? 10.698 6.220 4.059 1.00 6.91 ? 267 MET A N 1 ATOM 1391 C CA . MET A 1 179 ? 10.971 4.887 3.494 1.00 6.73 ? 267 MET A CA 1 ATOM 1392 C C . MET A 1 179 ? 11.863 4.093 4.415 1.00 6.53 ? 267 MET A C 1 ATOM 1393 O O . MET A 1 179 ? 12.829 4.613 4.955 1.00 7.18 ? 267 MET A O 1 ATOM 1394 C CB . MET A 1 179 ? 11.690 4.990 2.144 1.00 8.35 ? 267 MET A CB 1 ATOM 1395 C CG . MET A 1 179 ? 10.829 5.410 1.013 1.00 11.24 ? 267 MET A CG 1 ATOM 1396 S SD . MET A 1 179 ? 11.745 5.469 -0.577 1.00 10.71 ? 267 MET A SD 1 ATOM 1397 C CE . MET A 1 179 ? 12.575 6.996 -0.362 1.00 11.97 ? 267 MET A CE 1 ATOM 1398 N N . ASP A 1 180 ? 11.569 2.833 4.579 1.00 7.39 ? 268 ASP A N 1 ATOM 1399 C CA . ASP A 1 180 ? 12.443 1.992 5.358 1.00 8.14 ? 268 ASP A CA 1 ATOM 1400 C C . ASP A 1 180 ? 13.862 1.975 4.777 1.00 8.45 ? 268 ASP A C 1 ATOM 1401 O O . ASP A 1 180 ? 14.032 1.867 3.579 1.00 9.53 ? 268 ASP A O 1 ATOM 1402 C CB . ASP A 1 180 ? 11.919 0.583 5.450 1.00 8.73 ? 268 ASP A CB 1 ATOM 1403 C CG . ASP A 1 180 ? 12.799 -0.277 6.302 1.00 10.02 ? 268 ASP A CG 1 ATOM 1404 O OD1 . ASP A 1 180 ? 12.554 -0.243 7.523 1.00 14.03 ? 268 ASP A OD1 1 ATOM 1405 O OD2 . ASP A 1 180 ? 13.753 -0.991 5.840 1.00 12.68 ? 268 ASP A OD2 1 ATOM 1406 N N . ALA A 1 181 ? 14.856 2.033 5.620 1.00 6.92 ? 269 ALA A N 1 ATOM 1407 C CA . ALA A 1 181 ? 16.249 1.954 5.171 1.00 8.10 ? 269 ALA A CA 1 ATOM 1408 C C . ALA A 1 181 ? 17.056 1.042 6.093 1.00 7.66 ? 269 ALA A C 1 ATOM 1409 O O . ALA A 1 181 ? 18.204 1.315 6.469 1.00 8.81 ? 269 ALA A O 1 ATOM 1410 C CB . ALA A 1 181 ? 16.896 3.342 5.094 1.00 8.51 ? 269 ALA A CB 1 ATOM 1411 N N . GLY A 1 182 ? 16.510 -0.116 6.409 1.00 7.62 ? 270 GLY A N 1 ATOM 1412 C CA . GLY A 1 182 ? 17.293 -1.069 7.165 1.00 7.95 ? 270 GLY A CA 1 ATOM 1413 C C . GLY A 1 182 ? 17.768 -0.549 8.509 1.00 8.10 ? 270 GLY A C 1 ATOM 1414 O O . GLY A 1 182 ? 17.039 0.077 9.223 1.00 8.95 ? 270 GLY A O 1 ATOM 1415 N N . HIS A 1 183 ? 18.997 -0.894 8.844 1.00 7.66 ? 271 HIS A N 1 ATOM 1416 C CA . HIS A 1 183 ? 19.600 -0.550 10.114 1.00 7.77 ? 271 HIS A CA 1 ATOM 1417 C C . HIS A 1 183 ? 21.108 -0.599 9.983 1.00 7.39 ? 271 HIS A C 1 ATOM 1418 O O . HIS A 1 183 ? 21.625 -0.964 8.927 1.00 8.07 ? 271 HIS A O 1 ATOM 1419 C CB . HIS A 1 183 ? 19.072 -1.415 11.231 1.00 7.48 ? 271 HIS A CB 1 ATOM 1420 C CG . HIS A 1 183 ? 19.426 -2.861 11.158 1.00 7.68 ? 271 HIS A CG 1 ATOM 1421 N ND1 . HIS A 1 183 ? 20.633 -3.372 11.578 1.00 9.45 ? 271 HIS A ND1 1 ATOM 1422 C CD2 . HIS A 1 183 ? 18.705 -3.927 10.721 1.00 9.31 ? 271 HIS A CD2 1 ATOM 1423 C CE1 . HIS A 1 183 ? 20.627 -4.686 11.415 1.00 9.94 ? 271 HIS A CE1 1 ATOM 1424 N NE2 . HIS A 1 183 ? 19.475 -5.048 10.900 1.00 9.53 ? 271 HIS A NE2 1 ATOM 1425 N N . ALA A 1 184 ? 21.827 -0.166 11.011 1.00 7.04 ? 272 ALA A N 1 ATOM 1426 C CA . ALA A 1 184 ? 23.276 -0.073 10.941 1.00 7.54 ? 272 ALA A CA 1 ATOM 1427 C C . ALA A 1 184 ? 23.989 -1.373 10.558 1.00 8.29 ? 272 ALA A C 1 ATOM 1428 O O . ALA A 1 184 ? 25.006 -1.352 9.861 1.00 8.57 ? 272 ALA A O 1 ATOM 1429 C CB . ALA A 1 184 ? 23.831 0.425 12.290 1.00 9.10 ? 272 ALA A CB 1 ATOM 1430 N N . GLY A 1 185 ? 23.428 -2.503 10.955 1.00 7.84 ? 273 GLY A N 1 ATOM 1431 C CA . GLY A 1 185 ? 23.988 -3.803 10.667 1.00 7.63 ? 273 GLY A CA 1 ATOM 1432 C C . GLY A 1 185 ? 23.584 -4.373 9.328 1.00 8.09 ? 273 GLY A C 1 ATOM 1433 O O . GLY A 1 185 ? 24.009 -5.484 8.989 1.00 9.41 ? 273 GLY A O 1 ATOM 1434 N N . TRP A 1 186 ? 22.798 -3.625 8.561 1.00 8.56 ? 274 TRP A N 1 ATOM 1435 C CA . TRP A 1 186 ? 22.409 -3.978 7.228 1.00 7.95 ? 274 TRP A CA 1 ATOM 1436 C C . TRP A 1 186 ? 23.078 -3.047 6.226 1.00 8.88 ? 274 TRP A C 1 ATOM 1437 O O . TRP A 1 186 ? 24.001 -3.465 5.471 1.00 9.35 ? 274 TRP A O 1 ATOM 1438 C CB . TRP A 1 186 ? 20.863 -3.960 7.158 1.00 8.33 ? 274 TRP A CB 1 ATOM 1439 C CG . TRP A 1 186 ? 20.294 -4.553 5.940 1.00 8.21 ? 274 TRP A CG 1 ATOM 1440 C CD1 . TRP A 1 186 ? 20.968 -4.915 4.807 1.00 9.52 ? 274 TRP A CD1 1 ATOM 1441 C CD2 . TRP A 1 186 ? 18.947 -4.900 5.732 1.00 9.53 ? 274 TRP A CD2 1 ATOM 1442 N NE1 . TRP A 1 186 ? 20.112 -5.507 3.919 1.00 9.28 ? 274 TRP A NE1 1 ATOM 1443 C CE2 . TRP A 1 186 ? 18.857 -5.505 4.476 1.00 9.48 ? 274 TRP A CE2 1 ATOM 1444 C CE3 . TRP A 1 186 ? 17.792 -4.812 6.504 1.00 9.75 ? 274 TRP A CE3 1 ATOM 1445 C CZ2 . TRP A 1 186 ? 17.650 -5.961 3.958 1.00 11.39 ? 274 TRP A CZ2 1 ATOM 1446 C CZ3 . TRP A 1 186 ? 16.599 -5.298 5.983 1.00 11.14 ? 274 TRP A CZ3 1 ATOM 1447 C CH2 . TRP A 1 186 ? 16.538 -5.843 4.735 1.00 11.19 ? 274 TRP A CH2 1 ATOM 1448 N N . LEU A 1 187 ? 22.634 -1.789 6.214 1.00 8.50 ? 275 LEU A N 1 ATOM 1449 C CA . LEU A 1 187 ? 23.139 -0.800 5.284 1.00 7.78 ? 275 LEU A CA 1 ATOM 1450 C C . LEU A 1 187 ? 24.242 0.064 5.832 1.00 8.58 ? 275 LEU A C 1 ATOM 1451 O O . LEU A 1 187 ? 24.853 0.801 5.061 1.00 9.78 ? 275 LEU A O 1 ATOM 1452 C CB . LEU A 1 187 ? 21.980 0.016 4.754 1.00 7.87 ? 275 LEU A CB 1 ATOM 1453 C CG . LEU A 1 187 ? 20.816 -0.704 4.075 1.00 8.43 ? 275 LEU A CG 1 ATOM 1454 C CD1 . LEU A 1 187 ? 19.863 0.296 3.486 1.00 8.78 ? 275 LEU A CD1 1 ATOM 1455 C CD2 . LEU A 1 187 ? 21.355 -1.663 3.036 1.00 10.09 ? 275 LEU A CD2 1 ATOM 1456 N N . GLY A 1 188 ? 24.528 -0.035 7.120 1.00 8.17 ? 276 GLY A N 1 ATOM 1457 C CA . GLY A 1 188 ? 25.546 0.798 7.729 1.00 8.49 ? 276 GLY A CA 1 ATOM 1458 C C . GLY A 1 188 ? 26.969 0.368 7.566 1.00 8.75 ? 276 GLY A C 1 ATOM 1459 O O . GLY A 1 188 ? 27.863 1.171 7.773 1.00 9.73 ? 276 GLY A O 1 ATOM 1460 N N . TRP A 1 189 ? 27.174 -0.886 7.172 1.00 9.33 ? 277 TRP A N 1 ATOM 1461 C CA . TRP A 1 189 ? 28.540 -1.323 6.836 1.00 9.05 ? 277 TRP A CA 1 ATOM 1462 C C . TRP A 1 189 ? 29.098 -0.337 5.807 1.00 9.54 ? 277 TRP A C 1 ATOM 1463 O O . TRP A 1 189 ? 28.400 -0.009 4.828 1.00 10.31 ? 277 TRP A O 1 ATOM 1464 C CB . TRP A 1 189 ? 28.535 -2.733 6.282 1.00 9.21 ? 277 TRP A CB 1 ATOM 1465 C CG . TRP A 1 189 ? 28.058 -3.738 7.272 1.00 9.22 ? 277 TRP A CG 1 ATOM 1466 C CD1 . TRP A 1 189 ? 26.774 -4.150 7.506 1.00 8.96 ? 277 TRP A CD1 1 ATOM 1467 C CD2 . TRP A 1 189 ? 28.883 -4.546 8.111 1.00 8.99 ? 277 TRP A CD2 1 ATOM 1468 N NE1 . TRP A 1 189 ? 26.753 -5.098 8.494 1.00 10.34 ? 277 TRP A NE1 1 ATOM 1469 C CE2 . TRP A 1 189 ? 28.032 -5.349 8.898 1.00 9.55 ? 277 TRP A CE2 1 ATOM 1470 C CE3 . TRP A 1 189 ? 30.255 -4.617 8.334 1.00 9.44 ? 277 TRP A CE3 1 ATOM 1471 C CZ2 . TRP A 1 189 ? 28.501 -6.260 9.805 1.00 11.00 ? 277 TRP A CZ2 1 ATOM 1472 C CZ3 . TRP A 1 189 ? 30.729 -5.529 9.274 1.00 11.71 ? 277 TRP A CZ3 1 ATOM 1473 C CH2 . TRP A 1 189 ? 29.846 -6.335 9.982 1.00 10.83 ? 277 TRP A CH2 1 ATOM 1474 N N . PRO A 1 190 ? 30.327 0.146 5.993 1.00 10.73 ? 278 PRO A N 1 ATOM 1475 C CA . PRO A 1 190 ? 30.880 1.122 5.060 1.00 11.45 ? 278 PRO A CA 1 ATOM 1476 C C . PRO A 1 190 ? 30.702 0.781 3.581 1.00 12.33 ? 278 PRO A C 1 ATOM 1477 O O . PRO A 1 190 ? 30.395 1.688 2.776 1.00 13.49 ? 278 PRO A O 1 ATOM 1478 C CB . PRO A 1 190 ? 32.349 1.186 5.484 1.00 12.07 ? 278 PRO A CB 1 ATOM 1479 C CG . PRO A 1 190 ? 32.287 1.015 6.935 1.00 11.32 ? 278 PRO A CG 1 ATOM 1480 C CD . PRO A 1 190 ? 31.193 0.002 7.188 1.00 10.57 ? 278 PRO A CD 1 ATOM 1481 N N . ALA A 1 191 ? 30.864 -0.475 3.188 1.00 12.43 ? 279 ALA A N 1 ATOM 1482 C CA . ALA A 1 191 ? 30.714 -0.867 1.777 1.00 13.39 ? 279 ALA A CA 1 ATOM 1483 C C . ALA A 1 191 ? 29.302 -0.691 1.241 1.00 12.76 ? 279 ALA A C 1 ATOM 1484 O O . ALA A 1 191 ? 29.105 -0.609 0.021 1.00 13.69 ? 279 ALA A O 1 ATOM 1485 C CB . ALA A 1 191 ? 31.174 -2.276 1.537 1.00 15.22 ? 279 ALA A CB 1 ATOM 1486 N N . ASN A 1 192 ? 28.305 -0.683 2.126 1.00 11.82 ? 280 ASN A N 1 ATOM 1487 C CA . ASN A 1 192 ? 26.917 -0.591 1.678 1.00 11.59 ? 280 ASN A CA 1 ATOM 1488 C C . ASN A 1 192 ? 26.339 0.803 1.658 1.00 11.69 ? 280 ASN A C 1 ATOM 1489 O O . ASN A 1 192 ? 25.287 1.017 1.054 1.00 11.11 ? 280 ASN A O 1 ATOM 1490 C CB . ASN A 1 192 ? 26.037 -1.491 2.556 1.00 11.80 ? 280 ASN A CB 1 ATOM 1491 C CG . ASN A 1 192 ? 26.435 -2.935 2.480 1.00 11.85 ? 280 ASN A CG 1 ATOM 1492 O OD1 . ASN A 1 192 ? 27.021 -3.371 1.470 1.00 14.44 ? 280 ASN A OD1 1 ATOM 1493 N ND2 . ASN A 1 192 ? 26.099 -3.716 3.498 1.00 12.17 ? 280 ASN A ND2 1 ATOM 1494 N N . ILE A 1 193 ? 27.019 1.756 2.286 1.00 11.44 ? 281 ILE A N 1 ATOM 1495 C CA . ILE A 1 193 ? 26.464 3.094 2.423 1.00 12.88 ? 281 ILE A CA 1 ATOM 1496 C C . ILE A 1 193 ? 26.311 3.800 1.088 1.00 12.32 ? 281 ILE A C 1 ATOM 1497 O O . ILE A 1 193 ? 25.265 4.421 0.842 1.00 11.85 ? 281 ILE A O 1 ATOM 1498 C CB . ILE A 1 193 ? 27.321 3.945 3.378 1.00 15.20 ? 281 ILE A CB 1 ATOM 1499 C CG1 . ILE A 1 193 ? 27.281 3.317 4.772 1.00 20.09 ? 281 ILE A CG1 1 ATOM 1500 C CG2 . ILE A 1 193 ? 26.858 5.411 3.354 1.00 17.42 ? 281 ILE A CG2 1 ATOM 1501 C CD1 . ILE A 1 193 ? 26.587 4.140 5.828 1.00 22.86 ? 281 ILE A CD1 1 ATOM 1502 N N . GLN A 1 194 ? 27.326 3.780 0.225 1.00 12.35 ? 282 GLN A N 1 ATOM 1503 C CA . GLN A 1 194 ? 27.225 4.454 -1.046 1.00 13.15 ? 282 GLN A CA 1 ATOM 1504 C C . GLN A 1 194 ? 26.175 3.801 -1.947 1.00 11.91 ? 282 GLN A C 1 ATOM 1505 O O . GLN A 1 194 ? 25.357 4.504 -2.499 1.00 12.22 ? 282 GLN A O 1 ATOM 1506 C CB . GLN A 1 194 ? 28.578 4.586 -1.755 1.00 15.16 ? 282 GLN A CB 1 ATOM 1507 C CG . GLN A 1 194 ? 28.507 5.413 -3.045 1.00 19.14 ? 282 GLN A CG 1 ATOM 1508 C CD . GLN A 1 194 ? 29.865 5.602 -3.700 0.50 22.56 ? 282 GLN A CD 1 ATOM 1509 O OE1 . GLN A 1 194 ? 30.871 5.751 -3.014 0.50 24.99 ? 282 GLN A OE1 1 ATOM 1510 N NE2 . GLN A 1 194 ? 29.891 5.603 -5.029 0.50 24.75 ? 282 GLN A NE2 1 ATOM 1511 N N . PRO A 1 195 ? 26.165 2.481 -2.117 1.00 10.97 ? 283 PRO A N 1 ATOM 1512 C CA . PRO A 1 195 ? 25.107 1.882 -2.943 1.00 10.73 ? 283 PRO A CA 1 ATOM 1513 C C . PRO A 1 195 ? 23.715 2.157 -2.378 1.00 9.97 ? 283 PRO A C 1 ATOM 1514 O O . PRO A 1 195 ? 22.792 2.383 -3.136 1.00 10.40 ? 283 PRO A O 1 ATOM 1515 C CB . PRO A 1 195 ? 25.413 0.375 -2.962 1.00 12.82 ? 283 PRO A CB 1 ATOM 1516 C CG . PRO A 1 195 ? 26.596 0.197 -2.206 1.00 14.88 ? 283 PRO A CG 1 ATOM 1517 C CD . PRO A 1 195 ? 27.190 1.478 -1.758 1.00 11.74 ? 283 PRO A CD 1 ATOM 1518 N N . ALA A 1 196 ? 23.594 2.200 -1.063 1.00 8.59 ? 284 ALA A N 1 ATOM 1519 C CA . ALA A 1 196 ? 22.288 2.540 -0.472 1.00 8.31 ? 284 ALA A CA 1 ATOM 1520 C C . ALA A 1 196 ? 21.894 3.975 -0.799 1.00 8.69 ? 284 ALA A C 1 ATOM 1521 O O . ALA A 1 196 ? 20.767 4.277 -1.137 1.00 8.97 ? 284 ALA A O 1 ATOM 1522 C CB . ALA A 1 196 ? 22.294 2.333 1.018 1.00 9.72 ? 284 ALA A CB 1 ATOM 1523 N N . ALA A 1 197 ? 22.844 4.892 -0.698 1.00 8.37 ? 285 ALA A N 1 ATOM 1524 C CA . ALA A 1 197 ? 22.567 6.283 -1.006 1.00 8.56 ? 285 ALA A CA 1 ATOM 1525 C C . ALA A 1 197 ? 22.166 6.461 -2.454 1.00 9.42 ? 285 ALA A C 1 ATOM 1526 O O . ALA A 1 197 ? 21.231 7.206 -2.758 1.00 10.07 ? 285 ALA A O 1 ATOM 1527 C CB . ALA A 1 197 ? 23.801 7.124 -0.711 1.00 8.95 ? 285 ALA A CB 1 ATOM 1528 N N . GLU A 1 198 ? 22.857 5.778 -3.363 1.00 10.14 ? 286 GLU A N 1 ATOM 1529 C CA . GLU A 1 198 ? 22.546 5.865 -4.772 1.00 10.90 ? 286 GLU A CA 1 ATOM 1530 C C . GLU A 1 198 ? 21.114 5.363 -5.009 1.00 10.31 ? 286 GLU A C 1 ATOM 1531 O O . GLU A 1 198 ? 20.294 5.988 -5.707 1.00 11.20 ? 286 GLU A O 1 ATOM 1532 C CB . GLU A 1 198 ? 23.564 5.076 -5.608 1.00 12.50 ? 286 GLU A CB 1 ATOM 1533 C CG . GLU A 1 198 ? 24.941 5.733 -5.703 1.00 18.74 ? 286 GLU A CG 1 ATOM 1534 C CD . GLU A 1 198 ? 26.108 4.792 -5.982 1.00 26.84 ? 286 GLU A CD 1 ATOM 1535 O OE1 . GLU A 1 198 ? 25.894 3.574 -6.193 1.00 32.30 ? 286 GLU A OE1 1 ATOM 1536 O OE2 . GLU A 1 198 ? 27.277 5.278 -5.956 1.00 30.89 ? 286 GLU A OE2 1 ATOM 1537 N N . LEU A 1 199 ? 20.784 4.232 -4.399 1.00 9.62 ? 287 LEU A N 1 ATOM 1538 C CA . LEU A 1 199 ? 19.471 3.646 -4.590 1.00 9.33 ? 287 LEU A CA 1 ATOM 1539 C C . LEU A 1 199 ? 18.357 4.578 -4.101 1.00 9.04 ? 287 LEU A C 1 ATOM 1540 O O . LEU A 1 199 ? 17.411 4.891 -4.821 1.00 9.73 ? 287 LEU A O 1 ATOM 1541 C CB . LEU A 1 199 ? 19.413 2.281 -3.878 1.00 10.19 ? 287 LEU A CB 1 ATOM 1542 C CG . LEU A 1 199 ? 18.039 1.579 -3.882 1.00 13.02 ? 287 LEU A CG 1 ATOM 1543 C CD1 . LEU A 1 199 ? 17.566 1.243 -5.279 1.00 17.28 ? 287 LEU A CD1 1 ATOM 1544 C CD2 . LEU A 1 199 ? 18.026 0.375 -2.956 1.00 15.80 ? 287 LEU A CD2 1 ATOM 1545 N N . PHE A 1 200 ? 18.435 4.989 -2.842 1.00 8.92 ? 288 PHE A N 1 ATOM 1546 C CA . PHE A 1 200 ? 17.341 5.771 -2.257 1.00 8.91 ? 288 PHE A CA 1 ATOM 1547 C C . PHE A 1 200 ? 17.227 7.173 -2.866 1.00 9.06 ? 288 PHE A C 1 ATOM 1548 O O . PHE A 1 200 ? 16.108 7.679 -3.066 1.00 9.38 ? 288 PHE A O 1 ATOM 1549 C CB . PHE A 1 200 ? 17.456 5.846 -0.736 1.00 9.70 ? 288 PHE A CB 1 ATOM 1550 C CG . PHE A 1 200 ? 17.057 4.559 -0.032 1.00 8.59 ? 288 PHE A CG 1 ATOM 1551 C CD1 . PHE A 1 200 ? 15.731 4.214 0.135 1.00 9.92 ? 288 PHE A CD1 1 ATOM 1552 C CD2 . PHE A 1 200 ? 18.013 3.709 0.435 1.00 11.34 ? 288 PHE A CD2 1 ATOM 1553 C CE1 . PHE A 1 200 ? 15.371 3.046 0.749 1.00 11.33 ? 288 PHE A CE1 1 ATOM 1554 C CE2 . PHE A 1 200 ? 17.657 2.511 1.068 1.00 11.31 ? 288 PHE A CE2 1 ATOM 1555 C CZ . PHE A 1 200 ? 16.339 2.193 1.224 1.00 10.69 ? 288 PHE A CZ 1 ATOM 1556 N N . ALA A 1 201 ? 18.365 7.790 -3.189 1.00 9.18 ? 289 ALA A N 1 ATOM 1557 C CA . ALA A 1 201 ? 18.316 9.138 -3.779 1.00 8.72 ? 289 ALA A CA 1 ATOM 1558 C C . ALA A 1 201 ? 17.742 9.043 -5.168 1.00 10.03 ? 289 ALA A C 1 ATOM 1559 O O . ALA A 1 201 ? 17.005 9.926 -5.587 1.00 10.13 ? 289 ALA A O 1 ATOM 1560 C CB . ALA A 1 201 ? 19.689 9.791 -3.792 1.00 9.48 ? 289 ALA A CB 1 ATOM 1561 N N . LYS A 1 202 ? 18.006 7.967 -5.896 1.00 9.45 ? 290 LYS A N 1 ATOM 1562 C CA . LYS A 1 202 ? 17.472 7.847 -7.238 1.00 10.17 ? 290 LYS A CA 1 ATOM 1563 C C . LYS A 1 202 ? 15.967 7.567 -7.226 1.00 9.77 ? 290 LYS A C 1 ATOM 1564 O O . LYS A 1 202 ? 15.218 8.088 -8.056 1.00 11.07 ? 290 LYS A O 1 ATOM 1565 C CB . LYS A 1 202 ? 18.241 6.835 -8.111 1.00 12.05 ? 290 LYS A CB 1 ATOM 1566 C CG . LYS A 1 202 ? 17.834 6.820 -9.582 1.00 16.47 ? 290 LYS A CG 1 ATOM 1567 C CD . LYS A 1 202 ? 18.359 8.017 -10.344 0.50 18.84 ? 290 LYS A CD 1 ATOM 1568 C CE . LYS A 1 202 ? 18.970 7.544 -11.676 0.50 20.35 ? 290 LYS A CE 1 ATOM 1569 N NZ . LYS A 1 202 ? 19.059 8.584 -12.736 0.50 22.50 ? 290 LYS A NZ 1 ATOM 1570 N N . ILE A 1 203 ? 15.498 6.786 -6.270 1.00 10.08 ? 291 ILE A N 1 ATOM 1571 C CA . ILE A 1 203 ? 14.062 6.592 -6.128 1.00 10.69 ? 291 ILE A CA 1 ATOM 1572 C C . ILE A 1 203 ? 13.354 7.934 -5.807 1.00 9.93 ? 291 ILE A C 1 ATOM 1573 O O . ILE A 1 203 ? 12.311 8.235 -6.339 1.00 10.15 ? 291 ILE A O 1 ATOM 1574 C CB A ILE A 1 203 ? 13.804 5.622 -4.939 0.70 11.43 ? 291 ILE A CB 1 ATOM 1575 C CB B ILE A 1 203 ? 13.793 5.464 -5.121 0.30 10.87 ? 291 ILE A CB 1 ATOM 1576 C CG1 A ILE A 1 203 ? 14.287 4.207 -5.265 0.70 13.43 ? 291 ILE A CG1 1 ATOM 1577 C CG1 B ILE A 1 203 ? 14.051 4.131 -5.838 0.30 10.87 ? 291 ILE A CG1 1 ATOM 1578 C CG2 A ILE A 1 203 ? 12.338 5.629 -4.467 0.70 11.87 ? 291 ILE A CG2 1 ATOM 1579 C CG2 B ILE A 1 203 ? 12.372 5.518 -4.561 0.30 11.39 ? 291 ILE A CG2 1 ATOM 1580 C CD1 A ILE A 1 203 ? 13.306 3.353 -6.030 0.70 13.78 ? 291 ILE A CD1 1 ATOM 1581 C CD1 B ILE A 1 203 ? 14.220 2.938 -4.914 0.30 8.84 ? 291 ILE A CD1 1 ATOM 1582 N N . TYR A 1 204 ? 13.933 8.704 -4.905 1.00 9.76 ? 292 TYR A N 1 ATOM 1583 C CA . TYR A 1 204 ? 13.376 10.003 -4.557 1.00 9.81 ? 292 TYR A CA 1 ATOM 1584 C C . TYR A 1 204 ? 13.257 10.881 -5.799 1.00 8.89 ? 292 TYR A C 1 ATOM 1585 O O . TYR A 1 204 ? 12.203 11.462 -6.074 1.00 10.42 ? 292 TYR A O 1 ATOM 1586 C CB . TYR A 1 204 ? 14.205 10.626 -3.473 1.00 9.62 ? 292 TYR A CB 1 ATOM 1587 C CG . TYR A 1 204 ? 13.804 11.995 -3.003 1.00 9.77 ? 292 TYR A CG 1 ATOM 1588 C CD1 . TYR A 1 204 ? 12.624 12.189 -2.296 1.00 10.36 ? 292 TYR A CD1 1 ATOM 1589 C CD2 . TYR A 1 204 ? 14.628 13.090 -3.179 1.00 11.49 ? 292 TYR A CD2 1 ATOM 1590 C CE1 . TYR A 1 204 ? 12.275 13.448 -1.798 1.00 11.57 ? 292 TYR A CE1 1 ATOM 1591 C CE2 . TYR A 1 204 ? 14.268 14.343 -2.697 1.00 11.89 ? 292 TYR A CE2 1 ATOM 1592 C CZ . TYR A 1 204 ? 13.100 14.497 -1.986 1.00 11.25 ? 292 TYR A CZ 1 ATOM 1593 O OH . TYR A 1 204 ? 12.797 15.744 -1.488 1.00 13.17 ? 292 TYR A OH 1 ATOM 1594 N N . GLU A 1 205 ? 14.332 10.934 -6.585 1.00 10.13 ? 293 GLU A N 1 ATOM 1595 C CA . GLU A 1 205 ? 14.344 11.701 -7.828 1.00 11.80 ? 293 GLU A CA 1 ATOM 1596 C C . GLU A 1 205 ? 13.322 11.175 -8.820 1.00 11.50 ? 293 GLU A C 1 ATOM 1597 O O . GLU A 1 205 ? 12.552 11.937 -9.430 1.00 12.11 ? 293 GLU A O 1 ATOM 1598 C CB . GLU A 1 205 ? 15.759 11.688 -8.437 1.00 14.00 ? 293 GLU A CB 1 ATOM 1599 C CG . GLU A 1 205 ? 15.905 12.420 -9.754 1.00 18.39 ? 293 GLU A CG 1 ATOM 1600 C CD . GLU A 1 205 ? 17.303 12.304 -10.351 0.50 21.92 ? 293 GLU A CD 1 ATOM 1601 O OE1 . GLU A 1 205 ? 17.621 11.268 -10.980 0.50 24.17 ? 293 GLU A OE1 1 ATOM 1602 O OE2 . GLU A 1 205 ? 18.078 13.266 -10.191 0.50 24.66 ? 293 GLU A OE2 1 ATOM 1603 N N . ASP A 1 206 ? 13.268 9.869 -8.984 1.00 11.39 ? 294 ASP A N 1 ATOM 1604 C CA . ASP A 1 206 ? 12.385 9.294 -9.999 1.00 12.59 ? 294 ASP A CA 1 ATOM 1605 C C . ASP A 1 206 ? 10.908 9.421 -9.595 1.00 12.01 ? 294 ASP A C 1 ATOM 1606 O O . ASP A 1 206 ? 10.013 9.423 -10.476 1.00 14.37 ? 294 ASP A O 1 ATOM 1607 C CB . ASP A 1 206 ? 12.735 7.839 -10.237 1.00 13.53 ? 294 ASP A CB 1 ATOM 1608 C CG . ASP A 1 206 ? 14.027 7.658 -11.036 1.00 16.21 ? 294 ASP A CG 1 ATOM 1609 O OD1 . ASP A 1 206 ? 14.627 8.658 -11.532 1.00 20.21 ? 294 ASP A OD1 1 ATOM 1610 O OD2 . ASP A 1 206 ? 14.500 6.511 -11.172 1.00 20.15 ? 294 ASP A OD2 1 ATOM 1611 N N . ALA A 1 207 ? 10.640 9.568 -8.292 1.00 11.10 ? 295 ALA A N 1 ATOM 1612 C CA . ALA A 1 207 ? 9.300 9.842 -7.807 1.00 10.66 ? 295 ALA A CA 1 ATOM 1613 C C . ALA A 1 207 ? 8.915 11.326 -7.936 1.00 11.32 ? 295 ALA A C 1 ATOM 1614 O O . ALA A 1 207 ? 7.801 11.697 -7.572 1.00 11.82 ? 295 ALA A O 1 ATOM 1615 C CB . ALA A 1 207 ? 9.113 9.379 -6.395 1.00 9.84 ? 295 ALA A CB 1 ATOM 1616 N N . GLY A 1 208 ? 9.828 12.155 -8.425 1.00 10.93 ? 296 GLY A N 1 ATOM 1617 C CA . GLY A 1 208 ? 9.568 13.573 -8.558 1.00 11.05 ? 296 GLY A CA 1 ATOM 1618 C C . GLY A 1 208 ? 9.772 14.393 -7.288 1.00 11.10 ? 296 GLY A C 1 ATOM 1619 O O . GLY A 1 208 ? 9.246 15.496 -7.157 1.00 13.29 ? 296 GLY A O 1 ATOM 1620 N N . LYS A 1 209 ? 10.522 13.852 -6.340 1.00 10.67 ? 297 LYS A N 1 ATOM 1621 C CA . LYS A 1 209 ? 10.802 14.481 -5.073 1.00 10.57 ? 297 LYS A CA 1 ATOM 1622 C C . LYS A 1 209 ? 9.498 14.947 -4.428 1.00 10.33 ? 297 LYS A C 1 ATOM 1623 O O . LYS A 1 209 ? 9.300 16.142 -4.165 1.00 10.97 ? 297 LYS A O 1 ATOM 1624 C CB . LYS A 1 209 ? 11.787 15.615 -5.272 1.00 11.31 ? 297 LYS A CB 1 ATOM 1625 C CG . LYS A 1 209 ? 13.059 15.138 -5.962 1.00 13.97 ? 297 LYS A CG 1 ATOM 1626 C CD . LYS A 1 209 ? 14.166 16.138 -5.860 1.00 18.20 ? 297 LYS A CD 1 ATOM 1627 C CE . LYS A 1 209 ? 15.460 15.575 -6.378 1.00 20.83 ? 297 LYS A CE 1 ATOM 1628 N NZ . LYS A 1 209 ? 16.548 16.568 -6.019 1.00 23.22 ? 297 LYS A NZ 1 ATOM 1629 N N . PRO A 1 210 ? 8.604 14.022 -4.103 1.00 9.28 ? 298 PRO A N 1 ATOM 1630 C CA . PRO A 1 210 ? 7.310 14.435 -3.591 1.00 9.33 ? 298 PRO A CA 1 ATOM 1631 C C . PRO A 1 210 ? 7.461 15.128 -2.263 1.00 8.90 ? 298 PRO A C 1 ATOM 1632 O O . PRO A 1 210 ? 8.273 14.752 -1.407 1.00 9.01 ? 298 PRO A O 1 ATOM 1633 C CB . PRO A 1 210 ? 6.559 13.107 -3.395 1.00 10.11 ? 298 PRO A CB 1 ATOM 1634 C CG . PRO A 1 210 ? 7.285 12.139 -4.212 1.00 11.90 ? 298 PRO A CG 1 ATOM 1635 C CD . PRO A 1 210 ? 8.722 12.547 -4.137 1.00 10.15 ? 298 PRO A CD 1 ATOM 1636 N N . ARG A 1 211 ? 6.680 16.190 -2.074 1.00 9.38 ? 299 ARG A N 1 ATOM 1637 C CA . ARG A 1 211 ? 6.718 16.957 -0.851 1.00 9.16 ? 299 ARG A CA 1 ATOM 1638 C C . ARG A 1 211 ? 6.619 16.109 0.426 1.00 8.67 ? 299 ARG A C 1 ATOM 1639 O O . ARG A 1 211 ? 7.318 16.339 1.390 1.00 9.20 ? 299 ARG A O 1 ATOM 1640 C CB . ARG A 1 211 ? 5.621 18.042 -0.883 1.00 9.86 ? 299 ARG A CB 1 ATOM 1641 C CG . ARG A 1 211 ? 5.617 18.982 0.312 1.00 10.75 ? 299 ARG A CG 1 ATOM 1642 C CD . ARG A 1 211 ? 4.234 19.398 0.763 1.00 11.28 ? 299 ARG A CD 1 ATOM 1643 N NE . ARG A 1 211 ? 3.469 18.230 1.244 1.00 9.48 ? 299 ARG A NE 1 ATOM 1644 C CZ . ARG A 1 211 ? 3.692 17.612 2.390 1.00 8.84 ? 299 ARG A CZ 1 ATOM 1645 N NH1 . ARG A 1 211 ? 4.577 18.046 3.255 1.00 9.86 ? 299 ARG A NH1 1 ATOM 1646 N NH2 . ARG A 1 211 ? 2.975 16.549 2.651 1.00 9.20 ? 299 ARG A NH2 1 ATOM 1647 N N . ALA A 1 212 ? 5.721 15.129 0.405 1.00 8.09 ? 300 ALA A N 1 ATOM 1648 C CA . ALA A 1 212 ? 5.463 14.319 1.592 1.00 7.55 ? 300 ALA A CA 1 ATOM 1649 C C . ALA A 1 212 ? 6.595 13.395 1.957 1.00 7.57 ? 300 ALA A C 1 ATOM 1650 O O . ALA A 1 212 ? 6.576 12.885 3.064 1.00 8.81 ? 300 ALA A O 1 ATOM 1651 C CB . ALA A 1 212 ? 4.249 13.484 1.384 1.00 8.28 ? 300 ALA A CB 1 ATOM 1652 N N . VAL A 1 213 ? 7.525 13.144 1.055 1.00 7.75 ? 301 VAL A N 1 ATOM 1653 C CA . VAL A 1 213 ? 8.646 12.257 1.385 1.00 7.80 ? 301 VAL A CA 1 ATOM 1654 C C . VAL A 1 213 ? 9.680 12.985 2.217 1.00 8.86 ? 301 VAL A C 1 ATOM 1655 O O . VAL A 1 213 ? 10.436 13.821 1.719 1.00 10.44 ? 301 VAL A O 1 ATOM 1656 C CB . VAL A 1 213 ? 9.256 11.605 0.137 1.00 9.31 ? 301 VAL A CB 1 ATOM 1657 C CG1 . VAL A 1 213 ? 10.451 10.752 0.552 1.00 10.47 ? 301 VAL A CG1 1 ATOM 1658 C CG2 . VAL A 1 213 ? 8.201 10.827 -0.598 1.00 9.87 ? 301 VAL A CG2 1 ATOM 1659 N N . ARG A 1 214 ? 9.676 12.711 3.496 1.00 7.30 ? 302 ARG A N 1 ATOM 1660 C CA . ARG A 1 214 ? 10.498 13.410 4.453 1.00 8.95 ? 302 ARG A CA 1 ATOM 1661 C C . ARG A 1 214 ? 11.867 12.794 4.592 1.00 7.34 ? 302 ARG A C 1 ATOM 1662 O O . ARG A 1 214 ? 12.833 13.495 4.901 1.00 9.26 ? 302 ARG A O 1 ATOM 1663 C CB . ARG A 1 214 ? 9.744 13.434 5.773 1.00 9.46 ? 302 ARG A CB 1 ATOM 1664 C CG . ARG A 1 214 ? 10.390 14.107 6.880 1.00 9.35 ? 302 ARG A CG 1 ATOM 1665 C CD . ARG A 1 214 ? 10.594 15.617 6.661 1.00 10.70 ? 302 ARG A CD 1 ATOM 1666 N NE . ARG A 1 214 ? 11.230 16.228 7.828 1.00 11.38 ? 302 ARG A NE 1 ATOM 1667 C CZ . ARG A 1 214 ? 11.508 17.489 8.005 1.00 12.37 ? 302 ARG A CZ 1 ATOM 1668 N NH1 . ARG A 1 214 ? 11.297 18.360 7.031 1.00 14.69 ? 302 ARG A NH1 1 ATOM 1669 N NH2 . ARG A 1 214 ? 12.106 17.852 9.132 1.00 12.96 ? 302 ARG A NH2 1 ATOM 1670 N N . GLY A 1 215 ? 11.982 11.484 4.404 1.00 7.55 ? 303 GLY A N 1 ATOM 1671 C CA . GLY A 1 215 ? 13.231 10.849 4.636 1.00 7.26 ? 303 GLY A CA 1 ATOM 1672 C C . GLY A 1 215 ? 13.092 9.350 4.741 1.00 6.77 ? 303 GLY A C 1 ATOM 1673 O O . GLY A 1 215 ? 12.374 8.693 3.979 1.00 6.37 ? 303 GLY A O 1 ATOM 1674 N N . LEU A 1 216 ? 13.792 8.814 5.728 1.00 5.92 ? 304 LEU A N 1 ATOM 1675 C CA . LEU A 1 216 ? 14.019 7.382 5.869 1.00 5.58 ? 304 LEU A CA 1 ATOM 1676 C C . LEU A 1 216 ? 13.778 6.965 7.314 1.00 5.53 ? 304 LEU A C 1 ATOM 1677 O O . LEU A 1 216 ? 14.004 7.752 8.248 1.00 6.60 ? 304 LEU A O 1 ATOM 1678 C CB . LEU A 1 216 ? 15.448 7.039 5.467 1.00 6.47 ? 304 LEU A CB 1 ATOM 1679 C CG . LEU A 1 216 ? 15.844 7.359 4.013 1.00 6.41 ? 304 LEU A CG 1 ATOM 1680 C CD1 . LEU A 1 216 ? 17.291 7.003 3.773 1.00 9.54 ? 304 LEU A CD1 1 ATOM 1681 C CD2 . LEU A 1 216 ? 14.959 6.624 3.022 1.00 7.13 ? 304 LEU A CD2 1 ATOM 1682 N N . ALA A 1 217 ? 13.377 5.706 7.505 1.00 6.07 ? 305 ALA A N 1 ATOM 1683 C CA . ALA A 1 217 ? 13.150 5.107 8.818 1.00 5.61 ? 305 ALA A CA 1 ATOM 1684 C C . ALA A 1 217 ? 14.158 4.001 9.025 1.00 6.97 ? 305 ALA A C 1 ATOM 1685 O O . ALA A 1 217 ? 14.366 3.187 8.139 1.00 8.40 ? 305 ALA A O 1 ATOM 1686 C CB . ALA A 1 217 ? 11.732 4.578 8.923 1.00 7.02 ? 305 ALA A CB 1 ATOM 1687 N N . THR A 1 218 ? 14.804 3.960 10.177 1.00 7.12 ? 306 THR A N 1 ATOM 1688 C CA . THR A 1 218 ? 15.786 2.931 10.442 1.00 8.07 ? 306 THR A CA 1 ATOM 1689 C C . THR A 1 218 ? 15.470 2.171 11.724 1.00 7.29 ? 306 THR A C 1 ATOM 1690 O O . THR A 1 218 ? 14.736 2.625 12.594 1.00 6.95 ? 306 THR A O 1 ATOM 1691 C CB . THR A 1 218 ? 17.237 3.444 10.536 1.00 9.23 ? 306 THR A CB 1 ATOM 1692 O OG1 . THR A 1 218 ? 17.474 4.112 11.767 1.00 13.01 ? 306 THR A OG1 1 ATOM 1693 C CG2 . THR A 1 218 ? 17.611 4.344 9.450 1.00 10.25 ? 306 THR A CG2 1 ATOM 1694 N N . ASN A 1 219 ? 16.016 0.965 11.787 1.00 7.02 ? 307 ASN A N 1 ATOM 1695 C CA . ASN A 1 219 ? 15.913 0.067 12.914 1.00 7.25 ? 307 ASN A CA 1 ATOM 1696 C C . ASN A 1 219 ? 14.505 -0.451 13.152 1.00 7.10 ? 307 ASN A C 1 ATOM 1697 O O . ASN A 1 219 ? 14.198 -0.915 14.248 1.00 7.85 ? 307 ASN A O 1 ATOM 1698 C CB . ASN A 1 219 ? 16.483 0.702 14.191 1.00 7.72 ? 307 ASN A CB 1 ATOM 1699 C CG . ASN A 1 219 ? 16.840 -0.334 15.232 1.00 8.11 ? 307 ASN A CG 1 ATOM 1700 O OD1 . ASN A 1 219 ? 17.470 -1.354 14.929 1.00 8.50 ? 307 ASN A OD1 1 ATOM 1701 N ND2 . ASN A 1 219 ? 16.453 -0.049 16.464 1.00 9.17 ? 307 ASN A ND2 1 ATOM 1702 N N . VAL A 1 220 ? 13.643 -0.394 12.127 1.00 7.77 ? 308 VAL A N 1 ATOM 1703 C CA . VAL A 1 220 ? 12.256 -0.790 12.276 1.00 7.38 ? 308 VAL A CA 1 ATOM 1704 C C . VAL A 1 220 ? 12.173 -2.245 12.689 1.00 8.60 ? 308 VAL A C 1 ATOM 1705 O O . VAL A 1 220 ? 12.677 -3.126 12.012 1.00 9.30 ? 308 VAL A O 1 ATOM 1706 C CB . VAL A 1 220 ? 11.441 -0.557 10.975 1.00 7.02 ? 308 VAL A CB 1 ATOM 1707 C CG1 . VAL A 1 220 ? 10.035 -1.129 11.093 1.00 8.18 ? 308 VAL A CG1 1 ATOM 1708 C CG2 . VAL A 1 220 ? 11.379 0.917 10.684 1.00 7.93 ? 308 VAL A CG2 1 ATOM 1709 N N . ALA A 1 221 ? 11.553 -2.480 13.844 1.00 8.93 ? 309 ALA A N 1 ATOM 1710 C CA . ALA A 1 221 ? 11.358 -3.802 14.389 1.00 9.39 ? 309 ALA A CA 1 ATOM 1711 C C . ALA A 1 221 ? 12.678 -4.500 14.685 1.00 10.43 ? 309 ALA A C 1 ATOM 1712 O O . ALA A 1 221 ? 12.729 -5.709 14.797 1.00 11.87 ? 309 ALA A O 1 ATOM 1713 C CB . ALA A 1 221 ? 10.437 -4.643 13.490 1.00 9.98 ? 309 ALA A CB 1 ATOM 1714 N N . ASN A 1 222 ? 13.744 -3.739 14.851 1.00 8.78 ? 310 ASN A N 1 ATOM 1715 C CA . ASN A 1 222 ? 15.041 -4.289 15.237 1.00 8.66 ? 310 ASN A CA 1 ATOM 1716 C C . ASN A 1 222 ? 15.465 -3.654 16.573 1.00 8.09 ? 310 ASN A C 1 ATOM 1717 O O . ASN A 1 222 ? 14.661 -3.007 17.233 1.00 8.46 ? 310 ASN A O 1 ATOM 1718 C CB . ASN A 1 222 ? 16.060 -4.117 14.111 1.00 8.84 ? 310 ASN A CB 1 ATOM 1719 C CG . ASN A 1 222 ? 16.266 -5.390 13.295 1.00 11.67 ? 310 ASN A CG 1 ATOM 1720 O OD1 . ASN A 1 222 ? 16.872 -6.350 13.766 1.00 15.57 ? 310 ASN A OD1 1 ATOM 1721 N ND2 . ASN A 1 222 ? 15.830 -5.387 12.061 1.00 15.09 ? 310 ASN A ND2 1 ATOM 1722 N N . TYR A 1 223 ? 16.685 -3.906 17.011 1.00 7.66 ? 311 TYR A N 1 ATOM 1723 C CA . TYR A 1 223 ? 17.025 -3.721 18.419 1.00 7.66 ? 311 TYR A CA 1 ATOM 1724 C C . TYR A 1 223 ? 18.239 -2.827 18.613 1.00 8.52 ? 311 TYR A C 1 ATOM 1725 O O . TYR A 1 223 ? 18.747 -2.737 19.739 1.00 9.16 ? 311 TYR A O 1 ATOM 1726 C CB . TYR A 1 223 ? 17.267 -5.099 19.050 1.00 8.84 ? 311 TYR A CB 1 ATOM 1727 C CG . TYR A 1 223 ? 16.193 -6.110 18.827 1.00 8.96 ? 311 TYR A CG 1 ATOM 1728 C CD1 . TYR A 1 223 ? 15.078 -6.190 19.652 1.00 9.39 ? 311 TYR A CD1 1 ATOM 1729 C CD2 . TYR A 1 223 ? 16.288 -7.016 17.811 1.00 10.54 ? 311 TYR A CD2 1 ATOM 1730 C CE1 . TYR A 1 223 ? 14.091 -7.149 19.448 1.00 9.40 ? 311 TYR A CE1 1 ATOM 1731 C CE2 . TYR A 1 223 ? 15.297 -7.961 17.596 1.00 10.91 ? 311 TYR A CE2 1 ATOM 1732 C CZ . TYR A 1 223 ? 14.226 -8.051 18.434 1.00 11.09 ? 311 TYR A CZ 1 ATOM 1733 O OH . TYR A 1 223 ? 13.255 -9.011 18.208 1.00 12.01 ? 311 TYR A OH 1 ATOM 1734 N N . ASN A 1 224 ? 18.730 -2.169 17.562 1.00 7.32 ? 312 ASN A N 1 ATOM 1735 C CA . ASN A 1 224 ? 20.002 -1.476 17.657 1.00 8.14 ? 312 ASN A CA 1 ATOM 1736 C C . ASN A 1 224 ? 19.938 -0.276 18.561 1.00 8.64 ? 312 ASN A C 1 ATOM 1737 O O . ASN A 1 224 ? 18.893 0.345 18.737 1.00 8.64 ? 312 ASN A O 1 ATOM 1738 C CB . ASN A 1 224 ? 20.450 -0.973 16.272 1.00 8.33 ? 312 ASN A CB 1 ATOM 1739 C CG . ASN A 1 224 ? 20.736 -2.087 15.312 1.00 10.21 ? 312 ASN A CG 1 ATOM 1740 O OD1 . ASN A 1 224 ? 20.652 -3.289 15.642 1.00 11.89 ? 312 ASN A OD1 1 ATOM 1741 N ND2 . ASN A 1 224 ? 21.041 -1.711 14.082 1.00 11.44 ? 312 ASN A ND2 1 ATOM 1742 N N . ALA A 1 225 ? 21.068 0.063 19.146 1.00 9.54 ? 313 ALA A N 1 ATOM 1743 C CA . ALA A 1 225 ? 21.175 1.299 19.912 1.00 9.37 ? 313 ALA A CA 1 ATOM 1744 C C . ALA A 1 225 ? 21.096 2.490 18.982 1.00 8.88 ? 313 ALA A C 1 ATOM 1745 O O . ALA A 1 225 ? 21.594 2.412 17.856 1.00 9.73 ? 313 ALA A O 1 ATOM 1746 C CB . ALA A 1 225 ? 22.495 1.331 20.635 1.00 10.80 ? 313 ALA A CB 1 ATOM 1747 N N . TRP A 1 226 ? 20.530 3.611 19.442 1.00 10.70 ? 314 TRP A N 1 ATOM 1748 C CA . TRP A 1 226 ? 20.764 4.888 18.823 1.00 10.31 ? 314 TRP A CA 1 ATOM 1749 C C . TRP A 1 226 ? 22.227 5.271 19.015 1.00 10.85 ? 314 TRP A C 1 ATOM 1750 O O . TRP A 1 226 ? 22.968 5.497 18.072 1.00 10.49 ? 314 TRP A O 1 ATOM 1751 C CB . TRP A 1 226 ? 19.828 5.969 19.376 1.00 10.95 ? 314 TRP A CB 1 ATOM 1752 C CG . TRP A 1 226 ? 20.326 7.366 19.207 1.00 9.94 ? 314 TRP A CG 1 ATOM 1753 C CD1 . TRP A 1 226 ? 20.747 8.213 20.202 1.00 12.35 ? 314 TRP A CD1 1 ATOM 1754 C CD2 . TRP A 1 226 ? 20.540 8.067 17.986 1.00 10.29 ? 314 TRP A CD2 1 ATOM 1755 N NE1 . TRP A 1 226 ? 21.164 9.395 19.662 1.00 13.51 ? 314 TRP A NE1 1 ATOM 1756 C CE2 . TRP A 1 226 ? 21.047 9.341 18.300 1.00 10.80 ? 314 TRP A CE2 1 ATOM 1757 C CE3 . TRP A 1 226 ? 20.315 7.763 16.644 1.00 10.46 ? 314 TRP A CE3 1 ATOM 1758 C CZ2 . TRP A 1 226 ? 21.361 10.274 17.338 1.00 11.49 ? 314 TRP A CZ2 1 ATOM 1759 C CZ3 . TRP A 1 226 ? 20.642 8.692 15.683 1.00 11.38 ? 314 TRP A CZ3 1 ATOM 1760 C CH2 . TRP A 1 226 ? 21.154 9.936 16.021 1.00 11.03 ? 314 TRP A CH2 1 ATOM 1761 N N . SER A 1 227 ? 22.672 5.237 20.258 1.00 12.56 ? 315 SER A N 1 ATOM 1762 C CA . SER A 1 227 ? 24.043 5.611 20.579 1.00 14.18 ? 315 SER A CA 1 ATOM 1763 C C . SER A 1 227 ? 24.512 4.815 21.795 1.00 15.51 ? 315 SER A C 1 ATOM 1764 O O . SER A 1 227 ? 23.879 4.842 22.856 1.00 17.34 ? 315 SER A O 1 ATOM 1765 C CB . SER A 1 227 ? 24.161 7.131 20.773 1.00 14.99 ? 315 SER A CB 1 ATOM 1766 O OG . SER A 1 227 ? 25.530 7.514 20.960 1.00 17.14 ? 315 SER A OG 1 ATOM 1767 N N . VAL A 1 228 ? 25.546 4.013 21.600 1.00 15.54 ? 316 VAL A N 1 ATOM 1768 C CA . VAL A 1 228 ? 26.106 3.171 22.677 1.00 17.12 ? 316 VAL A CA 1 ATOM 1769 C C . VAL A 1 228 ? 27.606 3.454 22.669 1.00 18.80 ? 316 VAL A C 1 ATOM 1770 O O . VAL A 1 228 ? 28.206 3.762 21.644 1.00 18.11 ? 316 VAL A O 1 ATOM 1771 C CB . VAL A 1 228 ? 25.788 1.646 22.460 1.00 17.71 ? 316 VAL A CB 1 ATOM 1772 C CG1 . VAL A 1 228 ? 26.347 1.102 21.179 1.00 17.74 ? 316 VAL A CG1 1 ATOM 1773 C CG2 . VAL A 1 228 ? 26.167 0.803 23.682 1.00 20.36 ? 316 VAL A CG2 1 ATOM 1774 N N . SER A 1 229 ? 28.236 3.361 23.831 1.00 20.73 ? 317 SER A N 1 ATOM 1775 C CA . SER A 1 229 ? 29.627 3.816 23.916 1.00 22.52 ? 317 SER A CA 1 ATOM 1776 C C . SER A 1 229 ? 30.610 2.731 23.492 1.00 22.79 ? 317 SER A C 1 ATOM 1777 O O . SER A 1 229 ? 31.720 3.046 23.073 1.00 24.97 ? 317 SER A O 1 ATOM 1778 C CB . SER A 1 229 ? 29.958 4.273 25.337 1.00 23.67 ? 317 SER A CB 1 ATOM 1779 O OG . SER A 1 229 ? 29.749 3.210 26.236 1.00 27.14 ? 317 SER A OG 1 ATOM 1780 N N . SER A 1 230 ? 30.203 1.472 23.639 1.00 21.77 ? 318 SER A N 1 ATOM 1781 C CA . SER A 1 230 ? 30.994 0.303 23.268 1.00 22.97 ? 318 SER A CA 1 ATOM 1782 C C . SER A 1 230 ? 30.251 -0.540 22.219 1.00 21.04 ? 318 SER A C 1 ATOM 1783 O O . SER A 1 230 ? 29.072 -0.823 22.386 1.00 20.16 ? 318 SER A O 1 ATOM 1784 C CB . SER A 1 230 ? 31.251 -0.561 24.515 1.00 23.95 ? 318 SER A CB 1 ATOM 1785 O OG . SER A 1 230 ? 32.022 -1.694 24.201 1.00 29.52 ? 318 SER A OG 1 ATOM 1786 N N . PRO A 1 231 ? 30.924 -0.951 21.150 1.00 18.45 ? 319 PRO A N 1 ATOM 1787 C CA . PRO A 1 231 ? 30.286 -1.828 20.160 1.00 17.48 ? 319 PRO A CA 1 ATOM 1788 C C . PRO A 1 231 ? 29.828 -3.156 20.742 1.00 16.60 ? 319 PRO A C 1 ATOM 1789 O O . PRO A 1 231 ? 30.631 -3.871 21.318 1.00 17.68 ? 319 PRO A O 1 ATOM 1790 C CB . PRO A 1 231 ? 31.367 -2.081 19.110 1.00 17.85 ? 319 PRO A CB 1 ATOM 1791 C CG . PRO A 1 231 ? 32.649 -1.546 19.708 1.00 21.04 ? 319 PRO A CG 1 ATOM 1792 C CD . PRO A 1 231 ? 32.316 -0.608 20.797 1.00 20.35 ? 319 PRO A CD 1 ATOM 1793 N N . PRO A 1 232 ? 28.555 -3.505 20.625 1.00 14.76 ? 320 PRO A N 1 ATOM 1794 C CA . PRO A 1 232 ? 28.139 -4.859 21.022 1.00 14.79 ? 320 PRO A CA 1 ATOM 1795 C C . PRO A 1 232 ? 28.882 -5.945 20.249 1.00 15.21 ? 320 PRO A C 1 ATOM 1796 O O . PRO A 1 232 ? 29.205 -5.741 19.084 1.00 14.58 ? 320 PRO A O 1 ATOM 1797 C CB . PRO A 1 232 ? 26.643 -4.876 20.704 1.00 15.23 ? 320 PRO A CB 1 ATOM 1798 C CG . PRO A 1 232 ? 26.252 -3.450 20.751 1.00 15.29 ? 320 PRO A CG 1 ATOM 1799 C CD . PRO A 1 232 ? 27.420 -2.689 20.154 1.00 15.73 ? 320 PRO A CD 1 ATOM 1800 N N . PRO A 1 233 ? 29.217 -7.077 20.864 1.00 15.63 ? 321 PRO A N 1 ATOM 1801 C CA . PRO A 1 233 ? 30.037 -8.084 20.167 1.00 15.68 ? 321 PRO A CA 1 ATOM 1802 C C . PRO A 1 233 ? 29.527 -8.588 18.808 1.00 14.45 ? 321 PRO A C 1 ATOM 1803 O O . PRO A 1 233 ? 30.312 -8.807 17.887 1.00 16.24 ? 321 PRO A O 1 ATOM 1804 C CB . PRO A 1 233 ? 30.124 -9.226 21.193 1.00 16.22 ? 321 PRO A CB 1 ATOM 1805 C CG . PRO A 1 233 ? 30.074 -8.475 22.438 1.00 18.75 ? 321 PRO A CG 1 ATOM 1806 C CD . PRO A 1 233 ? 28.965 -7.451 22.271 1.00 17.18 ? 321 PRO A CD 1 ATOM 1807 N N . TYR A 1 234 ? 28.225 -8.734 18.654 1.00 13.69 ? 322 TYR A N 1 ATOM 1808 C CA . TYR A 1 234 ? 27.633 -9.195 17.411 1.00 13.37 ? 322 TYR A CA 1 ATOM 1809 C C . TYR A 1 234 ? 27.715 -8.142 16.281 1.00 12.20 ? 322 TYR A C 1 ATOM 1810 O O . TYR A 1 234 ? 27.375 -8.464 15.132 1.00 13.27 ? 322 TYR A O 1 ATOM 1811 C CB . TYR A 1 234 ? 26.169 -9.654 17.646 1.00 13.11 ? 322 TYR A CB 1 ATOM 1812 C CG . TYR A 1 234 ? 25.393 -8.658 18.444 1.00 12.65 ? 322 TYR A CG 1 ATOM 1813 C CD1 . TYR A 1 234 ? 24.851 -7.531 17.833 1.00 12.00 ? 322 TYR A CD1 1 ATOM 1814 C CD2 . TYR A 1 234 ? 25.185 -8.838 19.797 1.00 12.18 ? 322 TYR A CD2 1 ATOM 1815 C CE1 . TYR A 1 234 ? 24.190 -6.595 18.579 1.00 11.78 ? 322 TYR A CE1 1 ATOM 1816 C CE2 . TYR A 1 234 ? 24.547 -7.905 20.532 1.00 13.00 ? 322 TYR A CE2 1 ATOM 1817 C CZ . TYR A 1 234 ? 24.027 -6.793 19.935 1.00 12.00 ? 322 TYR A CZ 1 ATOM 1818 O OH . TYR A 1 234 ? 23.406 -5.841 20.721 1.00 12.58 ? 322 TYR A OH 1 ATOM 1819 N N . THR A 1 235 ? 28.103 -6.914 16.612 1.00 11.34 ? 323 THR A N 1 ATOM 1820 C CA . THR A 1 235 ? 28.263 -5.880 15.575 1.00 10.60 ? 323 THR A CA 1 ATOM 1821 C C . THR A 1 235 ? 29.641 -5.925 14.948 1.00 11.30 ? 323 THR A C 1 ATOM 1822 O O . THR A 1 235 ? 29.843 -5.353 13.896 1.00 11.02 ? 323 THR A O 1 ATOM 1823 C CB . THR A 1 235 ? 28.014 -4.460 16.069 1.00 10.68 ? 323 THR A CB 1 ATOM 1824 O OG1 . THR A 1 235 ? 29.024 -4.047 16.999 1.00 11.51 ? 323 THR A OG1 1 ATOM 1825 C CG2 . THR A 1 235 ? 26.684 -4.322 16.754 1.00 11.39 ? 323 THR A CG2 1 ATOM 1826 N N . SER A 1 236 ? 30.604 -6.628 15.553 1.00 12.26 ? 324 SER A N 1 ATOM 1827 C CA . SER A 1 236 ? 31.993 -6.491 15.136 1.00 13.36 ? 324 SER A CA 1 ATOM 1828 C C . SER A 1 236 ? 32.121 -7.209 13.814 1.00 12.66 ? 324 SER A C 1 ATOM 1829 O O . SER A 1 236 ? 31.507 -8.256 13.607 1.00 14.36 ? 324 SER A O 1 ATOM 1830 C CB . SER A 1 236 ? 32.903 -7.104 16.184 1.00 14.54 ? 324 SER A CB 1 ATOM 1831 O OG . SER A 1 236 ? 34.262 -7.005 15.822 1.00 19.64 ? 324 SER A OG 1 ATOM 1832 N N . PRO A 1 237 ? 32.903 -6.708 12.853 1.00 11.98 ? 325 PRO A N 1 ATOM 1833 C CA . PRO A 1 237 ? 33.735 -5.516 12.955 1.00 11.21 ? 325 PRO A CA 1 ATOM 1834 C C . PRO A 1 237 ? 33.182 -4.221 12.310 1.00 9.86 ? 325 PRO A C 1 ATOM 1835 O O . PRO A 1 237 ? 33.954 -3.373 11.869 1.00 10.73 ? 325 PRO A O 1 ATOM 1836 C CB . PRO A 1 237 ? 34.963 -5.974 12.163 1.00 10.90 ? 325 PRO A CB 1 ATOM 1837 C CG . PRO A 1 237 ? 34.383 -6.714 11.055 1.00 11.32 ? 325 PRO A CG 1 ATOM 1838 C CD . PRO A 1 237 ? 33.207 -7.454 11.611 1.00 12.01 ? 325 PRO A CD 1 ATOM 1839 N N . ASN A 1 238 ? 31.871 -4.081 12.261 1.00 9.23 ? 326 ASN A N 1 ATOM 1840 C CA . ASN A 1 238 ? 31.273 -2.915 11.610 1.00 8.67 ? 326 ASN A CA 1 ATOM 1841 C C . ASN A 1 238 ? 31.626 -1.678 12.402 1.00 9.34 ? 326 ASN A C 1 ATOM 1842 O O . ASN A 1 238 ? 31.249 -1.574 13.588 1.00 9.53 ? 326 ASN A O 1 ATOM 1843 C CB . ASN A 1 238 ? 29.769 -3.088 11.557 1.00 8.43 ? 326 ASN A CB 1 ATOM 1844 C CG . ASN A 1 238 ? 29.065 -2.011 10.726 1.00 8.83 ? 326 ASN A CG 1 ATOM 1845 O OD1 . ASN A 1 238 ? 29.659 -1.013 10.331 1.00 8.89 ? 326 ASN A OD1 1 ATOM 1846 N ND2 . ASN A 1 238 ? 27.769 -2.240 10.450 1.00 8.59 ? 326 ASN A ND2 1 ATOM 1847 N N . PRO A 1 239 ? 32.291 -0.679 11.805 1.00 9.08 ? 327 PRO A N 1 ATOM 1848 C CA . PRO A 1 239 ? 32.568 0.542 12.566 1.00 9.60 ? 327 PRO A CA 1 ATOM 1849 C C . PRO A 1 239 ? 31.305 1.362 12.870 1.00 9.75 ? 327 PRO A C 1 ATOM 1850 O O . PRO A 1 239 ? 31.286 2.168 13.805 1.00 10.78 ? 327 PRO A O 1 ATOM 1851 C CB . PRO A 1 239 ? 33.511 1.340 11.643 1.00 11.20 ? 327 PRO A CB 1 ATOM 1852 C CG . PRO A 1 239 ? 33.241 0.800 10.272 1.00 11.71 ? 327 PRO A CG 1 ATOM 1853 C CD . PRO A 1 239 ? 32.812 -0.628 10.421 1.00 9.57 ? 327 PRO A CD 1 ATOM 1854 N N . ASN A 1 240 ? 30.251 1.141 12.100 1.00 9.04 ? 328 ASN A N 1 ATOM 1855 C CA . ASN A 1 240 ? 28.973 1.868 12.288 1.00 10.11 ? 328 ASN A CA 1 ATOM 1856 C C . ASN A 1 240 ? 28.027 0.947 13.022 1.00 9.77 ? 328 ASN A C 1 ATOM 1857 O O . ASN A 1 240 ? 27.186 0.274 12.435 1.00 11.43 ? 328 ASN A O 1 ATOM 1858 C CB . ASN A 1 240 ? 28.431 2.326 10.954 1.00 9.56 ? 328 ASN A CB 1 ATOM 1859 C CG . ASN A 1 240 ? 29.364 3.306 10.273 1.00 10.49 ? 328 ASN A CG 1 ATOM 1860 O OD1 . ASN A 1 240 ? 29.964 4.129 10.936 1.00 11.50 ? 328 ASN A OD1 1 ATOM 1861 N ND2 . ASN A 1 240 ? 29.467 3.243 8.954 1.00 11.20 ? 328 ASN A ND2 1 ATOM 1862 N N . TYR A 1 241 ? 28.234 0.863 14.325 1.00 10.40 ? 329 TYR A N 1 ATOM 1863 C CA . TYR A 1 241 ? 27.669 -0.190 15.150 1.00 10.81 ? 329 TYR A CA 1 ATOM 1864 C C . TYR A 1 241 ? 26.401 0.257 15.872 1.00 11.04 ? 329 TYR A C 1 ATOM 1865 O O . TYR A 1 241 ? 25.829 -0.540 16.612 1.00 12.60 ? 329 TYR A O 1 ATOM 1866 C CB . TYR A 1 241 ? 28.707 -0.751 16.114 1.00 11.59 ? 329 TYR A CB 1 ATOM 1867 C CG . TYR A 1 241 ? 29.364 0.304 16.946 1.00 13.15 ? 329 TYR A CG 1 ATOM 1868 C CD1 . TYR A 1 241 ? 28.739 0.890 18.056 1.00 14.78 ? 329 TYR A CD1 1 ATOM 1869 C CD2 . TYR A 1 241 ? 30.647 0.728 16.625 1.00 16.31 ? 329 TYR A CD2 1 ATOM 1870 C CE1 . TYR A 1 241 ? 29.399 1.875 18.806 1.00 19.28 ? 329 TYR A CE1 1 ATOM 1871 C CE2 . TYR A 1 241 ? 31.299 1.669 17.359 1.00 21.63 ? 329 TYR A CE2 1 ATOM 1872 C CZ . TYR A 1 241 ? 30.687 2.250 18.430 1.00 22.07 ? 329 TYR A CZ 1 ATOM 1873 O OH . TYR A 1 241 ? 31.426 3.202 19.126 1.00 27.89 ? 329 TYR A OH 1 ATOM 1874 N N . ASP A 1 242 ? 26.009 1.513 15.702 1.00 9.33 ? 330 ASP A N 1 ATOM 1875 C CA . ASP A 1 242 ? 24.730 2.015 16.203 1.00 9.62 ? 330 ASP A CA 1 ATOM 1876 C C . ASP A 1 242 ? 24.096 2.925 15.152 1.00 8.02 ? 330 ASP A C 1 ATOM 1877 O O . ASP A 1 242 ? 24.708 3.238 14.121 1.00 8.30 ? 330 ASP A O 1 ATOM 1878 C CB . ASP A 1 242 ? 24.863 2.662 17.564 1.00 11.08 ? 330 ASP A CB 1 ATOM 1879 C CG . ASP A 1 242 ? 25.817 3.810 17.583 1.00 11.37 ? 330 ASP A CG 1 ATOM 1880 O OD1 . ASP A 1 242 ? 26.098 4.447 16.534 1.00 12.54 ? 330 ASP A OD1 1 ATOM 1881 O OD2 . ASP A 1 242 ? 26.347 4.176 18.670 1.00 12.90 ? 330 ASP A OD2 1 ATOM 1882 N N . GLU A 1 243 ? 22.844 3.281 15.381 1.00 8.41 ? 331 GLU A N 1 ATOM 1883 C CA . GLU A 1 243 ? 22.111 4.042 14.382 1.00 7.98 ? 331 GLU A CA 1 ATOM 1884 C C . GLU A 1 243 ? 22.679 5.430 14.167 1.00 7.95 ? 331 GLU A C 1 ATOM 1885 O O . GLU A 1 243 ? 22.669 5.933 13.055 1.00 8.56 ? 331 GLU A O 1 ATOM 1886 C CB . GLU A 1 243 ? 20.623 4.071 14.724 1.00 8.07 ? 331 GLU A CB 1 ATOM 1887 C CG . GLU A 1 243 ? 19.983 2.680 14.706 1.00 8.36 ? 331 GLU A CG 1 ATOM 1888 C CD . GLU A 1 243 ? 20.097 1.970 13.373 1.00 10.32 ? 331 GLU A CD 1 ATOM 1889 O OE1 . GLU A 1 243 ? 19.602 2.504 12.371 1.00 13.33 ? 331 GLU A OE1 1 ATOM 1890 O OE2 . GLU A 1 243 ? 20.783 0.935 13.293 1.00 12.01 ? 331 GLU A OE2 1 ATOM 1891 N N . LYS A 1 244 ? 23.205 6.064 15.210 1.00 8.51 ? 332 LYS A N 1 ATOM 1892 C CA . LYS A 1 244 ? 23.816 7.368 15.046 1.00 9.04 ? 332 LYS A CA 1 ATOM 1893 C C . LYS A 1 244 ? 25.008 7.307 14.110 1.00 8.81 ? 332 LYS A C 1 ATOM 1894 O O . LYS A 1 244 ? 25.162 8.135 13.217 1.00 8.92 ? 332 LYS A O 1 ATOM 1895 C CB . LYS A 1 244 ? 24.252 7.913 16.398 1.00 10.24 ? 332 LYS A CB 1 ATOM 1896 C CG . LYS A 1 244 ? 24.887 9.288 16.328 1.00 11.11 ? 332 LYS A CG 1 ATOM 1897 C CD . LYS A 1 244 ? 25.159 9.884 17.712 1.00 15.05 ? 332 LYS A CD 1 ATOM 1898 C CE . LYS A 1 244 ? 25.997 11.146 17.641 1.00 19.05 ? 332 LYS A CE 1 ATOM 1899 N NZ . LYS A 1 244 ? 26.141 11.704 19.010 1.00 23.13 ? 332 LYS A NZ 1 ATOM 1900 N N . HIS A 1 245 ? 25.854 6.303 14.243 1.00 8.89 ? 333 HIS A N 1 ATOM 1901 C CA . HIS A 1 245 ? 26.991 6.171 13.362 1.00 8.30 ? 333 HIS A CA 1 ATOM 1902 C C . HIS A 1 245 ? 26.530 5.984 11.908 1.00 7.96 ? 333 HIS A C 1 ATOM 1903 O O . HIS A 1 245 ? 27.060 6.566 10.954 1.00 9.09 ? 333 HIS A O 1 ATOM 1904 C CB . HIS A 1 245 ? 27.862 4.973 13.747 1.00 10.05 ? 333 HIS A CB 1 ATOM 1905 C CG . HIS A 1 245 ? 28.853 5.297 14.819 1.00 11.88 ? 333 HIS A CG 1 ATOM 1906 N ND1 . HIS A 1 245 ? 28.518 5.385 16.151 1.00 14.81 ? 333 HIS A ND1 1 ATOM 1907 C CD2 . HIS A 1 245 ? 30.173 5.605 14.741 1.00 14.88 ? 333 HIS A CD2 1 ATOM 1908 C CE1 . HIS A 1 245 ? 29.598 5.700 16.858 1.00 16.78 ? 333 HIS A CE1 1 ATOM 1909 N NE2 . HIS A 1 245 ? 30.613 5.853 16.020 1.00 17.98 ? 333 HIS A NE2 1 ATOM 1910 N N . TYR A 1 246 ? 25.551 5.113 11.730 1.00 8.19 ? 334 TYR A N 1 ATOM 1911 C CA . TYR A 1 246 ? 25.003 4.810 10.399 1.00 8.06 ? 334 TYR A CA 1 ATOM 1912 C C . TYR A 1 246 ? 24.469 6.111 9.787 1.00 7.65 ? 334 TYR A C 1 ATOM 1913 O O . TYR A 1 246 ? 24.822 6.473 8.662 1.00 8.50 ? 334 TYR A O 1 ATOM 1914 C CB . TYR A 1 246 ? 23.912 3.748 10.530 1.00 7.93 ? 334 TYR A CB 1 ATOM 1915 C CG . TYR A 1 246 ? 23.025 3.470 9.343 1.00 7.23 ? 334 TYR A CG 1 ATOM 1916 C CD1 . TYR A 1 246 ? 23.452 3.586 8.042 1.00 8.30 ? 334 TYR A CD1 1 ATOM 1917 C CD2 . TYR A 1 246 ? 21.707 3.051 9.544 1.00 8.19 ? 334 TYR A CD2 1 ATOM 1918 C CE1 . TYR A 1 246 ? 22.615 3.306 6.979 1.00 7.79 ? 334 TYR A CE1 1 ATOM 1919 C CE2 . TYR A 1 246 ? 20.884 2.774 8.509 1.00 7.13 ? 334 TYR A CE2 1 ATOM 1920 C CZ . TYR A 1 246 ? 21.309 2.910 7.235 1.00 7.46 ? 334 TYR A CZ 1 ATOM 1921 O OH . TYR A 1 246 ? 20.502 2.664 6.154 1.00 8.74 ? 334 TYR A OH 1 ATOM 1922 N N . ILE A 1 247 ? 23.595 6.776 10.519 1.00 7.61 ? 335 ILE A N 1 ATOM 1923 C CA . ILE A 1 247 ? 22.895 7.934 9.957 1.00 7.83 ? 335 ILE A CA 1 ATOM 1924 C C . ILE A 1 247 ? 23.878 9.070 9.642 1.00 9.01 ? 335 ILE A C 1 ATOM 1925 O O . ILE A 1 247 ? 23.750 9.741 8.633 1.00 8.68 ? 335 ILE A O 1 ATOM 1926 C CB . ILE A 1 247 ? 21.748 8.361 10.854 1.00 8.69 ? 335 ILE A CB 1 ATOM 1927 C CG1 . ILE A 1 247 ? 20.611 7.309 10.757 1.00 9.07 ? 335 ILE A CG1 1 ATOM 1928 C CG2 . ILE A 1 247 ? 21.229 9.747 10.497 1.00 10.68 ? 335 ILE A CG2 1 ATOM 1929 C CD1 . ILE A 1 247 ? 19.574 7.401 11.864 1.00 10.19 ? 335 ILE A CD1 1 ATOM 1930 N N . GLU A 1 248 ? 24.834 9.309 10.526 1.00 8.89 ? 336 GLU A N 1 ATOM 1931 C CA . GLU A 1 248 ? 25.820 10.362 10.268 1.00 9.25 ? 336 GLU A CA 1 ATOM 1932 C C . GLU A 1 248 ? 26.697 10.077 9.059 1.00 10.97 ? 336 GLU A C 1 ATOM 1933 O O . GLU A 1 248 ? 27.081 10.981 8.369 1.00 12.28 ? 336 GLU A O 1 ATOM 1934 C CB . GLU A 1 248 ? 26.682 10.609 11.526 1.00 11.03 ? 336 GLU A CB 1 ATOM 1935 C CG . GLU A 1 248 ? 25.862 11.291 12.623 1.00 11.41 ? 336 GLU A CG 1 ATOM 1936 C CD . GLU A 1 248 ? 26.661 11.807 13.808 1.00 15.67 ? 336 GLU A CD 1 ATOM 1937 O OE1 . GLU A 1 248 ? 27.824 11.364 14.051 1.00 17.87 ? 336 GLU A OE1 1 ATOM 1938 O OE2 . GLU A 1 248 ? 26.116 12.646 14.549 1.00 17.38 ? 336 GLU A OE2 1 ATOM 1939 N N . ALA A 1 249 ? 26.980 8.804 8.771 1.00 10.41 ? 337 ALA A N 1 ATOM 1940 C CA . ALA A 1 249 ? 27.741 8.468 7.560 1.00 11.39 ? 337 ALA A CA 1 ATOM 1941 C C . ALA A 1 249 ? 26.869 8.498 6.296 1.00 11.36 ? 337 ALA A C 1 ATOM 1942 O O . ALA A 1 249 ? 27.348 8.763 5.217 1.00 12.75 ? 337 ALA A O 1 ATOM 1943 C CB . ALA A 1 249 ? 28.353 7.129 7.701 1.00 11.76 ? 337 ALA A CB 1 ATOM 1944 N N . PHE A 1 250 ? 25.580 8.163 6.439 1.00 9.51 ? 338 PHE A N 1 ATOM 1945 C CA . PHE A 1 250 ? 24.660 7.949 5.310 1.00 8.47 ? 338 PHE A CA 1 ATOM 1946 C C . PHE A 1 250 ? 24.080 9.265 4.800 1.00 8.61 ? 338 PHE A C 1 ATOM 1947 O O . PHE A 1 250 ? 24.042 9.501 3.610 1.00 8.73 ? 338 PHE A O 1 ATOM 1948 C CB . PHE A 1 250 ? 23.575 7.026 5.834 1.00 8.93 ? 338 PHE A CB 1 ATOM 1949 C CG . PHE A 1 250 ? 22.599 6.457 4.821 1.00 7.64 ? 338 PHE A CG 1 ATOM 1950 C CD1 . PHE A 1 250 ? 22.871 6.305 3.490 1.00 8.68 ? 338 PHE A CD1 1 ATOM 1951 C CD2 . PHE A 1 250 ? 21.373 5.997 5.298 1.00 8.22 ? 338 PHE A CD2 1 ATOM 1952 C CE1 . PHE A 1 250 ? 21.935 5.694 2.651 1.00 9.56 ? 338 PHE A CE1 1 ATOM 1953 C CE2 . PHE A 1 250 ? 20.447 5.395 4.468 1.00 8.69 ? 338 PHE A CE2 1 ATOM 1954 C CZ . PHE A 1 250 ? 20.720 5.259 3.163 1.00 9.84 ? 338 PHE A CZ 1 ATOM 1955 N N . ARG A 1 251 ? 23.642 10.124 5.704 1.00 8.39 ? 339 ARG A N 1 ATOM 1956 C CA . ARG A 1 251 ? 22.980 11.359 5.295 1.00 8.92 ? 339 ARG A CA 1 ATOM 1957 C C . ARG A 1 251 ? 23.791 12.236 4.332 1.00 9.06 ? 339 ARG A C 1 ATOM 1958 O O . ARG A 1 251 ? 23.243 12.697 3.347 1.00 9.76 ? 339 ARG A O 1 ATOM 1959 C CB . ARG A 1 251 ? 22.535 12.129 6.526 1.00 9.70 ? 339 ARG A CB 1 ATOM 1960 C CG . ARG A 1 251 ? 22.063 13.566 6.242 1.00 12.32 ? 339 ARG A CG 1 ATOM 1961 C CD . ARG A 1 251 ? 20.951 13.782 5.220 1.00 11.18 ? 339 ARG A CD 1 ATOM 1962 N NE . ARG A 1 251 ? 20.735 15.220 5.166 1.00 12.44 ? 339 ARG A NE 1 ATOM 1963 C CZ . ARG A 1 251 ? 19.983 15.914 6.002 1.00 11.56 ? 339 ARG A CZ 1 ATOM 1964 N NH1 . ARG A 1 251 ? 19.168 15.348 6.848 1.00 12.07 ? 339 ARG A NH1 1 ATOM 1965 N NH2 . ARG A 1 251 ? 20.022 17.239 5.944 1.00 14.90 ? 339 ARG A NH2 1 ATOM 1966 N N . PRO A 1 252 ? 25.087 12.459 4.573 1.00 10.14 ? 340 PRO A N 1 ATOM 1967 C CA . PRO A 1 252 ? 25.791 13.306 3.606 1.00 10.45 ? 340 PRO A CA 1 ATOM 1968 C C . PRO A 1 252 ? 25.798 12.738 2.208 1.00 10.40 ? 340 PRO A C 1 ATOM 1969 O O . PRO A 1 252 ? 25.758 13.478 1.240 1.00 11.14 ? 340 PRO A O 1 ATOM 1970 C CB . PRO A 1 252 ? 27.191 13.411 4.193 1.00 11.63 ? 340 PRO A CB 1 ATOM 1971 C CG . PRO A 1 252 ? 26.983 13.201 5.656 1.00 12.84 ? 340 PRO A CG 1 ATOM 1972 C CD . PRO A 1 252 ? 25.949 12.134 5.710 1.00 10.73 ? 340 PRO A CD 1 ATOM 1973 N N . LEU A 1 253 ? 25.842 11.409 2.088 1.00 10.01 ? 341 LEU A N 1 ATOM 1974 C CA . LEU A 1 253 ? 25.867 10.788 0.768 1.00 11.11 ? 341 LEU A CA 1 ATOM 1975 C C . LEU A 1 253 ? 24.518 10.917 0.060 1.00 9.85 ? 341 LEU A C 1 ATOM 1976 O O . LEU A 1 253 ? 24.432 11.172 -1.136 1.00 11.52 ? 341 LEU A O 1 ATOM 1977 C CB A LEU A 1 253 ? 26.324 9.323 0.827 0.50 11.88 ? 341 LEU A CB 1 ATOM 1978 C CB B LEU A 1 253 ? 26.263 9.321 0.915 0.50 12.64 ? 341 LEU A CB 1 ATOM 1979 C CG A LEU A 1 253 ? 27.835 9.141 0.619 0.50 13.27 ? 341 LEU A CG 1 ATOM 1980 C CG B LEU A 1 253 ? 27.663 9.092 1.497 0.50 15.75 ? 341 LEU A CG 1 ATOM 1981 C CD1 A LEU A 1 253 ? 28.561 9.558 1.880 0.50 13.33 ? 341 LEU A CD1 1 ATOM 1982 C CD1 B LEU A 1 253 ? 27.793 7.708 1.981 0.50 17.70 ? 341 LEU A CD1 1 ATOM 1983 C CD2 A LEU A 1 253 ? 28.202 7.735 0.279 0.50 14.00 ? 341 LEU A CD2 1 ATOM 1984 C CD2 B LEU A 1 253 ? 28.693 9.341 0.424 0.50 18.83 ? 341 LEU A CD2 1 ATOM 1985 N N . LEU A 1 254 ? 23.458 10.795 0.818 1.00 9.85 ? 342 LEU A N 1 ATOM 1986 C CA . LEU A 1 254 ? 22.119 10.996 0.330 1.00 8.69 ? 342 LEU A CA 1 ATOM 1987 C C . LEU A 1 254 ? 21.929 12.447 -0.150 1.00 9.14 ? 342 LEU A C 1 ATOM 1988 O O . LEU A 1 254 ? 21.417 12.701 -1.244 1.00 9.81 ? 342 LEU A O 1 ATOM 1989 C CB . LEU A 1 254 ? 21.088 10.676 1.406 1.00 7.87 ? 342 LEU A CB 1 ATOM 1990 C CG . LEU A 1 254 ? 20.902 9.171 1.709 1.00 8.18 ? 342 LEU A CG 1 ATOM 1991 C CD1 . LEU A 1 254 ? 20.312 9.059 3.090 1.00 8.80 ? 342 LEU A CD1 1 ATOM 1992 C CD2 . LEU A 1 254 ? 20.022 8.494 0.667 1.00 8.97 ? 342 LEU A CD2 1 ATOM 1993 N N . GLU A 1 255 ? 22.341 13.388 0.686 1.00 9.88 ? 343 GLU A N 1 ATOM 1994 C CA . GLU A 1 255 ? 22.145 14.800 0.418 1.00 10.07 ? 343 GLU A CA 1 ATOM 1995 C C . GLU A 1 255 ? 22.934 15.232 -0.812 1.00 11.07 ? 343 GLU A C 1 ATOM 1996 O O . GLU A 1 255 ? 22.420 15.994 -1.609 1.00 12.32 ? 343 GLU A O 1 ATOM 1997 C CB . GLU A 1 255 ? 22.529 15.613 1.629 1.00 9.97 ? 343 GLU A CB 1 ATOM 1998 C CG . GLU A 1 255 ? 22.203 17.115 1.475 1.00 13.28 ? 343 GLU A CG 1 ATOM 1999 C CD . GLU A 1 255 ? 21.935 17.834 2.776 1.00 15.79 ? 343 GLU A CD 1 ATOM 2000 O OE1 . GLU A 1 255 ? 22.242 17.282 3.876 1.00 17.61 ? 343 GLU A OE1 1 ATOM 2001 O OE2 . GLU A 1 255 ? 21.453 18.998 2.679 1.00 19.74 ? 343 GLU A OE2 1 ATOM 2002 N N . ALA A 1 256 ? 24.133 14.703 -0.982 1.00 10.64 ? 344 ALA A N 1 ATOM 2003 C CA . ALA A 1 256 ? 24.941 15.018 -2.150 1.00 12.49 ? 344 ALA A CA 1 ATOM 2004 C C . ALA A 1 256 ? 24.304 14.549 -3.426 1.00 12.61 ? 344 ALA A C 1 ATOM 2005 O O . ALA A 1 256 ? 24.562 15.089 -4.514 1.00 14.58 ? 344 ALA A O 1 ATOM 2006 C CB . ALA A 1 256 ? 26.286 14.428 -1.986 1.00 12.27 ? 344 ALA A CB 1 ATOM 2007 N N . ARG A 1 257 ? 23.429 13.562 -3.342 1.00 11.49 ? 345 ARG A N 1 ATOM 2008 C CA . ARG A 1 257 ? 22.691 13.002 -4.460 1.00 11.49 ? 345 ARG A CA 1 ATOM 2009 C C . ARG A 1 257 ? 21.261 13.524 -4.519 1.00 11.94 ? 345 ARG A C 1 ATOM 2010 O O . ARG A 1 257 ? 20.438 12.974 -5.258 1.00 12.06 ? 345 ARG A O 1 ATOM 2011 C CB . ARG A 1 257 ? 22.715 11.496 -4.386 1.00 11.87 ? 345 ARG A CB 1 ATOM 2012 C CG . ARG A 1 257 ? 24.097 10.939 -4.595 1.00 12.89 ? 345 ARG A CG 1 ATOM 2013 C CD . ARG A 1 257 ? 24.264 9.525 -4.140 1.00 14.86 ? 345 ARG A CD 1 ATOM 2014 N NE . ARG A 1 257 ? 25.595 9.018 -4.464 1.00 17.57 ? 345 ARG A NE 1 ATOM 2015 C CZ . ARG A 1 257 ? 26.712 9.336 -3.806 1.00 19.62 ? 345 ARG A CZ 1 ATOM 2016 N NH1 . ARG A 1 257 ? 26.703 10.141 -2.754 1.00 18.77 ? 345 ARG A NH1 1 ATOM 2017 N NH2 . ARG A 1 257 ? 27.875 8.845 -4.218 1.00 22.49 ? 345 ARG A NH2 1 ATOM 2018 N N . GLY A 1 258 ? 20.971 14.602 -3.826 1.00 10.92 ? 346 GLY A N 1 ATOM 2019 C CA . GLY A 1 258 ? 19.704 15.306 -3.994 1.00 11.50 ? 346 GLY A CA 1 ATOM 2020 C C . GLY A 1 258 ? 18.577 14.956 -3.023 1.00 11.43 ? 346 GLY A C 1 ATOM 2021 O O . GLY A 1 258 ? 17.482 15.448 -3.166 1.00 11.99 ? 346 GLY A O 1 ATOM 2022 N N . PHE A 1 259 ? 18.849 14.132 -2.022 1.00 10.96 ? 347 PHE A N 1 ATOM 2023 C CA . PHE A 1 259 ? 17.836 13.671 -1.082 1.00 10.17 ? 347 PHE A CA 1 ATOM 2024 C C . PHE A 1 259 ? 18.301 14.016 0.326 1.00 10.55 ? 347 PHE A C 1 ATOM 2025 O O . PHE A 1 259 ? 19.018 13.248 0.945 1.00 10.22 ? 347 PHE A O 1 ATOM 2026 C CB . PHE A 1 259 ? 17.641 12.156 -1.236 1.00 10.36 ? 347 PHE A CB 1 ATOM 2027 C CG . PHE A 1 259 ? 16.539 11.578 -0.418 1.00 10.08 ? 347 PHE A CG 1 ATOM 2028 C CD1 . PHE A 1 259 ? 15.549 12.341 0.208 1.00 9.36 ? 347 PHE A CD1 1 ATOM 2029 C CD2 . PHE A 1 259 ? 16.459 10.183 -0.304 1.00 9.56 ? 347 PHE A CD2 1 ATOM 2030 C CE1 . PHE A 1 259 ? 14.536 11.720 0.913 1.00 8.90 ? 347 PHE A CE1 1 ATOM 2031 C CE2 . PHE A 1 259 ? 15.447 9.574 0.399 1.00 9.37 ? 347 PHE A CE2 1 ATOM 2032 C CZ . PHE A 1 259 ? 14.502 10.322 1.015 1.00 9.25 ? 347 PHE A CZ 1 ATOM 2033 N N . PRO A 1 260 ? 17.893 15.175 0.846 1.00 12.04 ? 348 PRO A N 1 ATOM 2034 C CA . PRO A 1 260 ? 18.298 15.578 2.197 1.00 11.04 ? 348 PRO A CA 1 ATOM 2035 C C . PRO A 1 260 ? 17.413 14.932 3.245 1.00 10.36 ? 348 PRO A C 1 ATOM 2036 O O . PRO A 1 260 ? 16.670 15.558 3.962 1.00 11.81 ? 348 PRO A O 1 ATOM 2037 C CB . PRO A 1 260 ? 18.142 17.109 2.161 1.00 13.34 ? 348 PRO A CB 1 ATOM 2038 C CG . PRO A 1 260 ? 17.047 17.331 1.272 1.00 13.25 ? 348 PRO A CG 1 ATOM 2039 C CD . PRO A 1 260 ? 17.083 16.223 0.197 1.00 12.85 ? 348 PRO A CD 1 ATOM 2040 N N . ALA A 1 261 ? 17.531 13.609 3.342 1.00 9.45 ? 349 ALA A N 1 ATOM 2041 C CA . ALA A 1 261 ? 16.607 12.781 4.095 1.00 8.17 ? 349 ALA A CA 1 ATOM 2042 C C . ALA A 1 261 ? 16.721 13.066 5.579 1.00 7.86 ? 349 ALA A C 1 ATOM 2043 O O . ALA A 1 261 ? 17.804 12.985 6.151 1.00 9.51 ? 349 ALA A O 1 ATOM 2044 C CB . ALA A 1 261 ? 16.896 11.299 3.809 1.00 8.81 ? 349 ALA A CB 1 ATOM 2045 N N . GLN A 1 262 ? 15.591 13.277 6.218 1.00 8.33 ? 350 GLN A N 1 ATOM 2046 C CA . GLN A 1 262 ? 15.501 13.268 7.649 1.00 7.98 ? 350 GLN A CA 1 ATOM 2047 C C . GLN A 1 262 ? 15.142 11.866 8.098 1.00 7.73 ? 350 GLN A C 1 ATOM 2048 O O . GLN A 1 262 ? 14.475 11.125 7.368 1.00 9.88 ? 350 GLN A O 1 ATOM 2049 C CB . GLN A 1 262 ? 14.486 14.264 8.129 1.00 8.45 ? 350 GLN A CB 1 ATOM 2050 C CG . GLN A 1 262 ? 14.883 15.715 7.897 1.00 9.37 ? 350 GLN A CG 1 ATOM 2051 C CD . GLN A 1 262 ? 15.987 16.205 8.779 1.00 9.46 ? 350 GLN A CD 1 ATOM 2052 O OE1 . GLN A 1 262 ? 17.036 16.540 8.276 1.00 13.12 ? 350 GLN A OE1 1 ATOM 2053 N NE2 . GLN A 1 262 ? 15.788 16.172 10.095 1.00 10.72 ? 350 GLN A NE2 1 ATOM 2054 N N . PHE A 1 263 ? 15.494 11.504 9.303 1.00 6.68 ? 351 PHE A N 1 ATOM 2055 C CA . PHE A 1 263 ? 15.353 10.142 9.778 1.00 6.82 ? 351 PHE A CA 1 ATOM 2056 C C . PHE A 1 263 ? 14.402 10.026 10.934 1.00 7.20 ? 351 PHE A C 1 ATOM 2057 O O . PHE A 1 263 ? 14.323 10.953 11.791 1.00 8.36 ? 351 PHE A O 1 ATOM 2058 C CB . PHE A 1 263 ? 16.714 9.543 10.175 1.00 7.35 ? 351 PHE A CB 1 ATOM 2059 C CG . PHE A 1 263 ? 17.621 9.276 9.004 1.00 7.82 ? 351 PHE A CG 1 ATOM 2060 C CD1 . PHE A 1 263 ? 18.290 10.298 8.352 1.00 10.33 ? 351 PHE A CD1 1 ATOM 2061 C CD2 . PHE A 1 263 ? 17.773 7.989 8.519 1.00 8.30 ? 351 PHE A CD2 1 ATOM 2062 C CE1 . PHE A 1 263 ? 19.095 10.010 7.241 1.00 10.33 ? 351 PHE A CE1 1 ATOM 2063 C CE2 . PHE A 1 263 ? 18.592 7.718 7.459 1.00 9.70 ? 351 PHE A CE2 1 ATOM 2064 C CZ . PHE A 1 263 ? 19.228 8.715 6.796 1.00 9.02 ? 351 PHE A CZ 1 ATOM 2065 N N . ILE A 1 264 ? 13.755 8.880 11.030 1.00 6.63 ? 352 ILE A N 1 ATOM 2066 C CA . ILE A 1 264 ? 13.186 8.440 12.296 1.00 7.30 ? 352 ILE A CA 1 ATOM 2067 C C . ILE A 1 264 ? 13.822 7.117 12.630 1.00 6.82 ? 352 ILE A C 1 ATOM 2068 O O . ILE A 1 264 ? 14.167 6.341 11.751 1.00 7.51 ? 352 ILE A O 1 ATOM 2069 C CB . ILE A 1 264 ? 11.648 8.386 12.285 1.00 7.01 ? 352 ILE A CB 1 ATOM 2070 C CG1 . ILE A 1 264 ? 11.116 7.422 11.229 1.00 7.01 ? 352 ILE A CG1 1 ATOM 2071 C CG2 . ILE A 1 264 ? 11.098 9.774 12.079 1.00 7.08 ? 352 ILE A CG2 1 ATOM 2072 C CD1 . ILE A 1 264 ? 9.578 7.292 11.235 1.00 7.85 ? 352 ILE A CD1 1 ATOM 2073 N N . VAL A 1 265 ? 13.967 6.832 13.916 1.00 7.52 ? 353 VAL A N 1 ATOM 2074 C CA . VAL A 1 265 ? 14.699 5.687 14.416 1.00 7.91 ? 353 VAL A CA 1 ATOM 2075 C C . VAL A 1 265 ? 13.838 4.957 15.421 1.00 6.85 ? 353 VAL A C 1 ATOM 2076 O O . VAL A 1 265 ? 13.473 5.518 16.457 1.00 8.01 ? 353 VAL A O 1 ATOM 2077 C CB . VAL A 1 265 ? 16.059 6.106 15.003 1.00 9.11 ? 353 VAL A CB 1 ATOM 2078 C CG1 . VAL A 1 265 ? 16.806 4.864 15.465 1.00 10.14 ? 353 VAL A CG1 1 ATOM 2079 C CG2 . VAL A 1 265 ? 16.906 6.903 14.022 1.00 9.80 ? 353 VAL A CG2 1 ATOM 2080 N N . ASP A 1 266 ? 13.535 3.689 15.159 1.00 6.88 ? 354 ASP A N 1 ATOM 2081 C CA . ASP A 1 266 ? 12.811 2.841 16.103 1.00 7.81 ? 354 ASP A CA 1 ATOM 2082 C C . ASP A 1 266 ? 13.753 2.612 17.293 1.00 7.56 ? 354 ASP A C 1 ATOM 2083 O O . ASP A 1 266 ? 14.900 2.229 17.122 1.00 8.44 ? 354 ASP A O 1 ATOM 2084 C CB . ASP A 1 266 ? 12.418 1.529 15.441 1.00 7.42 ? 354 ASP A CB 1 ATOM 2085 C CG . ASP A 1 266 ? 11.336 0.727 16.153 1.00 8.31 ? 354 ASP A CG 1 ATOM 2086 O OD1 . ASP A 1 266 ? 10.956 1.093 17.303 1.00 9.33 ? 354 ASP A OD1 1 ATOM 2087 O OD2 . ASP A 1 266 ? 10.801 -0.258 15.576 1.00 8.53 ? 354 ASP A OD2 1 ATOM 2088 N N . GLN A 1 267 ? 13.216 2.853 18.475 1.00 8.18 ? 355 GLN A N 1 ATOM 2089 C CA . GLN A 1 267 ? 13.921 2.539 19.727 1.00 8.89 ? 355 GLN A CA 1 ATOM 2090 C C . GLN A 1 267 ? 13.042 1.739 20.676 1.00 9.20 ? 355 GLN A C 1 ATOM 2091 O O . GLN A 1 267 ? 13.412 1.578 21.860 1.00 9.73 ? 355 GLN A O 1 ATOM 2092 C CB . GLN A 1 267 ? 14.429 3.816 20.393 1.00 8.74 ? 355 GLN A CB 1 ATOM 2093 C CG . GLN A 1 267 ? 15.569 4.480 19.631 1.00 9.61 ? 355 GLN A CG 1 ATOM 2094 C CD . GLN A 1 267 ? 16.867 3.711 19.735 1.00 9.75 ? 355 GLN A CD 1 ATOM 2095 O OE1 . GLN A 1 267 ? 17.548 3.770 20.785 1.00 12.79 ? 355 GLN A OE1 1 ATOM 2096 N NE2 . GLN A 1 267 ? 17.206 2.937 18.711 1.00 9.88 ? 355 GLN A NE2 1 ATOM 2097 N N . GLY A 1 268 ? 11.913 1.214 20.245 1.00 8.45 ? 356 GLY A N 1 ATOM 2098 C CA . GLY A 1 268 ? 10.986 0.558 21.144 1.00 8.97 ? 356 GLY A CA 1 ATOM 2099 C C . GLY A 1 268 ? 11.533 -0.671 21.830 1.00 9.14 ? 356 GLY A C 1 ATOM 2100 O O . GLY A 1 268 ? 11.033 -1.014 22.901 1.00 10.75 ? 356 GLY A O 1 ATOM 2101 N N . ARG A 1 269 ? 12.543 -1.317 21.273 1.00 8.88 ? 357 ARG A N 1 ATOM 2102 C CA . ARG A 1 269 ? 13.127 -2.518 21.863 1.00 9.06 ? 357 ARG A CA 1 ATOM 2103 C C . ARG A 1 269 ? 14.659 -2.412 21.955 1.00 8.37 ? 357 ARG A C 1 ATOM 2104 O O . ARG A 1 269 ? 15.366 -3.433 21.905 1.00 9.60 ? 357 ARG A O 1 ATOM 2105 C CB . ARG A 1 269 ? 12.674 -3.756 21.131 1.00 9.32 ? 357 ARG A CB 1 ATOM 2106 C CG . ARG A 1 269 ? 11.189 -3.933 21.141 1.00 11.05 ? 357 ARG A CG 1 ATOM 2107 C CD . ARG A 1 269 ? 10.712 -5.300 20.604 1.00 11.14 ? 357 ARG A CD 1 ATOM 2108 N NE . ARG A 1 269 ? 11.002 -5.491 19.168 1.00 9.95 ? 357 ARG A NE 1 ATOM 2109 C CZ . ARG A 1 269 ? 10.740 -6.595 18.494 1.00 9.36 ? 357 ARG A CZ 1 ATOM 2110 N NH1 . ARG A 1 269 ? 10.199 -7.636 19.109 1.00 12.86 ? 357 ARG A NH1 1 ATOM 2111 N NH2 . ARG A 1 269 ? 11.086 -6.736 17.215 1.00 11.54 ? 357 ARG A NH2 1 ATOM 2112 N N . SER A 1 270 ? 15.143 -1.187 22.123 1.00 8.87 ? 358 SER A N 1 ATOM 2113 C CA . SER A 1 270 ? 16.552 -0.855 22.055 1.00 9.95 ? 358 SER A CA 1 ATOM 2114 C C . SER A 1 270 ? 17.167 -0.428 23.379 1.00 10.54 ? 358 SER A C 1 ATOM 2115 O O . SER A 1 270 ? 18.336 -0.044 23.403 1.00 11.21 ? 358 SER A O 1 ATOM 2116 C CB . SER A 1 270 ? 16.759 0.301 21.073 1.00 10.32 ? 358 SER A CB 1 ATOM 2117 O OG . SER A 1 270 ? 16.428 -0.073 19.749 1.00 9.91 ? 358 SER A OG 1 ATOM 2118 N N . GLY A 1 271 ? 16.407 -0.494 24.471 1.00 11.75 ? 359 GLY A N 1 ATOM 2119 C CA . GLY A 1 271 ? 16.901 0.029 25.747 1.00 12.68 ? 359 GLY A CA 1 ATOM 2120 C C . GLY A 1 271 ? 18.062 -0.733 26.380 1.00 13.49 ? 359 GLY A C 1 ATOM 2121 O O . GLY A 1 271 ? 18.905 -0.106 27.024 1.00 15.88 ? 359 GLY A O 1 ATOM 2122 N N . LYS A 1 272 ? 18.116 -2.030 26.191 1.00 13.06 ? 360 LYS A N 1 ATOM 2123 C CA . LYS A 1 272 ? 19.190 -2.852 26.750 1.00 12.97 ? 360 LYS A CA 1 ATOM 2124 C C . LYS A 1 272 ? 20.244 -3.138 25.697 1.00 13.15 ? 360 LYS A C 1 ATOM 2125 O O . LYS A 1 272 ? 19.950 -3.725 24.638 1.00 12.86 ? 360 LYS A O 1 ATOM 2126 C CB . LYS A 1 272 ? 18.642 -4.150 27.291 1.00 13.92 ? 360 LYS A CB 1 ATOM 2127 C CG . LYS A 1 272 ? 19.682 -4.970 27.998 1.00 17.14 ? 360 LYS A CG 1 ATOM 2128 C CD . LYS A 1 272 ? 19.059 -6.106 28.808 1.00 21.35 ? 360 LYS A CD 1 ATOM 2129 C CE . LYS A 1 272 ? 19.458 -6.051 30.283 1.00 26.62 ? 360 LYS A CE 1 ATOM 2130 N NZ . LYS A 1 272 ? 20.916 -5.853 30.493 1.00 28.92 ? 360 LYS A NZ 1 ATOM 2131 N N . GLN A 1 273 ? 21.471 -2.752 26.001 1.00 12.84 ? 361 GLN A N 1 ATOM 2132 C CA . GLN A 1 273 ? 22.606 -2.869 25.067 1.00 13.28 ? 361 GLN A CA 1 ATOM 2133 C C . GLN A 1 273 ? 23.840 -3.339 25.849 1.00 13.93 ? 361 GLN A C 1 ATOM 2134 O O . GLN A 1 273 ? 24.126 -2.754 26.906 1.00 15.87 ? 361 GLN A O 1 ATOM 2135 C CB . GLN A 1 273 ? 22.938 -1.520 24.476 1.00 12.43 ? 361 GLN A CB 1 ATOM 2136 C CG . GLN A 1 273 ? 21.786 -0.935 23.623 1.00 11.90 ? 361 GLN A CG 1 ATOM 2137 C CD . GLN A 1 273 ? 21.469 -1.767 22.390 1.00 11.02 ? 361 GLN A CD 1 ATOM 2138 O OE1 . GLN A 1 273 ? 22.335 -2.452 21.867 1.00 11.73 ? 361 GLN A OE1 1 ATOM 2139 N NE2 . GLN A 1 273 ? 20.241 -1.669 21.901 1.00 10.74 ? 361 GLN A NE2 1 ATOM 2140 N N . PRO A 1 274 ? 24.548 -4.361 25.373 1.00 13.47 ? 362 PRO A N 1 ATOM 2141 C CA . PRO A 1 274 ? 24.182 -5.164 24.200 1.00 13.69 ? 362 PRO A CA 1 ATOM 2142 C C . PRO A 1 274 ? 22.930 -5.954 24.459 1.00 13.16 ? 362 PRO A C 1 ATOM 2143 O O . PRO A 1 274 ? 22.547 -6.188 25.615 1.00 13.61 ? 362 PRO A O 1 ATOM 2144 C CB . PRO A 1 274 ? 25.350 -6.152 24.048 1.00 14.45 ? 362 PRO A CB 1 ATOM 2145 C CG . PRO A 1 274 ? 25.848 -6.277 25.444 1.00 17.45 ? 362 PRO A CG 1 ATOM 2146 C CD . PRO A 1 274 ? 25.751 -4.915 26.038 1.00 14.76 ? 362 PRO A CD 1 ATOM 2147 N N . THR A 1 275 ? 22.264 -6.361 23.398 1.00 12.21 ? 363 THR A N 1 ATOM 2148 C CA . THR A 1 275 ? 21.103 -7.237 23.512 1.00 12.83 ? 363 THR A CA 1 ATOM 2149 C C . THR A 1 275 ? 21.594 -8.665 23.729 1.00 14.16 ? 363 THR A C 1 ATOM 2150 O O . THR A 1 275 ? 22.809 -8.917 23.786 1.00 15.02 ? 363 THR A O 1 ATOM 2151 C CB . THR A 1 275 ? 20.267 -7.231 22.218 1.00 12.12 ? 363 THR A CB 1 ATOM 2152 O OG1 . THR A 1 275 ? 21.035 -7.897 21.201 1.00 12.39 ? 363 THR A OG1 1 ATOM 2153 C CG2 . THR A 1 275 ? 19.947 -5.827 21.767 1.00 11.67 ? 363 THR A CG2 1 ATOM 2154 N N . GLY A 1 276 ? 20.663 -9.607 23.753 1.00 14.44 ? 364 GLY A N 1 ATOM 2155 C CA . GLY A 1 276 ? 20.976 -11.024 23.774 1.00 15.59 ? 364 GLY A CA 1 ATOM 2156 C C . GLY A 1 276 ? 21.095 -11.712 22.434 1.00 15.20 ? 364 GLY A C 1 ATOM 2157 O O . GLY A 1 276 ? 21.238 -12.925 22.356 1.00 16.43 ? 364 GLY A O 1 ATOM 2158 N N . GLN A 1 277 ? 21.099 -10.928 21.337 1.00 14.70 ? 365 GLN A N 1 ATOM 2159 C CA . GLN A 1 277 ? 21.271 -11.488 20.024 1.00 14.37 ? 365 GLN A CA 1 ATOM 2160 C C . GLN A 1 277 ? 22.619 -12.153 19.939 1.00 15.09 ? 365 GLN A C 1 ATOM 2161 O O . GLN A 1 277 ? 23.639 -11.596 20.391 1.00 16.11 ? 365 GLN A O 1 ATOM 2162 C CB . GLN A 1 277 ? 21.181 -10.368 18.976 1.00 13.00 ? 365 GLN A CB 1 ATOM 2163 C CG . GLN A 1 277 ? 19.791 -9.791 18.760 1.00 13.52 ? 365 GLN A CG 1 ATOM 2164 C CD . GLN A 1 277 ? 19.880 -8.471 18.030 1.00 12.07 ? 365 GLN A CD 1 ATOM 2165 O OE1 . GLN A 1 277 ? 20.294 -7.484 18.620 1.00 12.26 ? 365 GLN A OE1 1 ATOM 2166 N NE2 . GLN A 1 277 ? 19.458 -8.443 16.769 1.00 13.21 ? 365 GLN A NE2 1 ATOM 2167 N N . LYS A 1 278 ? 22.641 -13.331 19.354 1.00 15.87 ? 366 LYS A N 1 ATOM 2168 C CA . LYS A 1 278 ? 23.902 -14.004 19.097 1.00 17.25 ? 366 LYS A CA 1 ATOM 2169 C C . LYS A 1 278 ? 24.509 -13.578 17.754 1.00 16.64 ? 366 LYS A C 1 ATOM 2170 O O . LYS A 1 278 ? 25.739 -13.645 17.582 1.00 19.20 ? 366 LYS A O 1 ATOM 2171 C CB . LYS A 1 278 ? 23.741 -15.527 19.199 1.00 18.39 ? 366 LYS A CB 1 ATOM 2172 C CG . LYS A 1 278 ? 23.422 -15.989 20.637 1.00 21.46 ? 366 LYS A CG 1 ATOM 2173 C CD . LYS A 1 278 ? 24.577 -15.794 21.636 0.50 21.83 ? 366 LYS A CD 1 ATOM 2174 C CE . LYS A 1 278 ? 25.033 -17.114 22.295 0.50 22.69 ? 366 LYS A CE 1 ATOM 2175 N NZ . LYS A 1 278 ? 24.471 -17.325 23.666 0.50 23.87 ? 366 LYS A NZ 1 ATOM 2176 N N . GLU A 1 279 ? 23.654 -13.200 16.804 1.00 15.30 ? 367 GLU A N 1 ATOM 2177 C CA . GLU A 1 279 ? 24.067 -12.675 15.514 1.00 14.53 ? 367 GLU A CA 1 ATOM 2178 C C . GLU A 1 279 ? 23.170 -11.467 15.248 1.00 13.86 ? 367 GLU A C 1 ATOM 2179 O O . GLU A 1 279 ? 22.004 -11.409 15.640 1.00 12.58 ? 367 GLU A O 1 ATOM 2180 C CB . GLU A 1 279 ? 23.943 -13.693 14.395 1.00 15.50 ? 367 GLU A CB 1 ATOM 2181 C CG . GLU A 1 279 ? 24.732 -14.983 14.593 0.50 15.73 ? 367 GLU A CG 1 ATOM 2182 C CD . GLU A 1 279 ? 26.226 -14.833 14.339 0.50 19.70 ? 367 GLU A CD 1 ATOM 2183 O OE1 . GLU A 1 279 ? 26.719 -13.735 13.963 0.50 20.46 ? 367 GLU A OE1 1 ATOM 2184 O OE2 . GLU A 1 279 ? 26.920 -15.851 14.534 0.50 22.11 ? 367 GLU A OE2 1 ATOM 2185 N N . TRP A 1 280 ? 23.703 -10.484 14.539 1.00 12.80 ? 368 TRP A N 1 ATOM 2186 C CA . TRP A 1 280 ? 22.984 -9.233 14.292 1.00 12.38 ? 368 TRP A CA 1 ATOM 2187 C C . TRP A 1 280 ? 21.715 -9.402 13.481 1.00 12.53 ? 368 TRP A C 1 ATOM 2188 O O . TRP A 1 280 ? 20.749 -8.670 13.707 1.00 13.33 ? 368 TRP A O 1 ATOM 2189 C CB . TRP A 1 280 ? 23.933 -8.273 13.585 1.00 12.34 ? 368 TRP A CB 1 ATOM 2190 C CG . TRP A 1 280 ? 23.687 -6.829 13.875 1.00 10.76 ? 368 TRP A CG 1 ATOM 2191 C CD1 . TRP A 1 280 ? 22.612 -6.251 14.485 1.00 10.16 ? 368 TRP A CD1 1 ATOM 2192 C CD2 . TRP A 1 280 ? 24.607 -5.785 13.612 1.00 9.70 ? 368 TRP A CD2 1 ATOM 2193 N NE1 . TRP A 1 280 ? 22.820 -4.902 14.614 1.00 10.99 ? 368 TRP A NE1 1 ATOM 2194 C CE2 . TRP A 1 280 ? 24.037 -4.592 14.058 1.00 9.85 ? 368 TRP A CE2 1 ATOM 2195 C CE3 . TRP A 1 280 ? 25.846 -5.740 12.984 1.00 10.71 ? 368 TRP A CE3 1 ATOM 2196 C CZ2 . TRP A 1 280 ? 24.679 -3.355 13.932 1.00 10.56 ? 368 TRP A CZ2 1 ATOM 2197 C CZ3 . TRP A 1 280 ? 26.481 -4.535 12.877 1.00 10.60 ? 368 TRP A CZ3 1 ATOM 2198 C CH2 . TRP A 1 280 ? 25.896 -3.359 13.319 1.00 9.75 ? 368 TRP A CH2 1 ATOM 2199 N N . GLY A 1 281 ? 21.692 -10.374 12.572 1.00 13.21 ? 369 GLY A N 1 ATOM 2200 C CA . GLY A 1 281 ? 20.516 -10.656 11.757 1.00 14.20 ? 369 GLY A CA 1 ATOM 2201 C C . GLY A 1 281 ? 19.414 -11.466 12.429 1.00 13.60 ? 369 GLY A C 1 ATOM 2202 O O . GLY A 1 281 ? 18.426 -11.822 11.786 1.00 15.21 ? 369 GLY A O 1 ATOM 2203 N N . HIS A 1 282 ? 19.530 -11.690 13.723 1.00 14.01 ? 370 HIS A N 1 ATOM 2204 C CA . HIS A 1 282 ? 18.520 -12.449 14.485 1.00 13.69 ? 370 HIS A CA 1 ATOM 2205 C C . HIS A 1 282 ? 17.508 -11.467 14.958 1.00 12.54 ? 370 HIS A C 1 ATOM 2206 O O . HIS A 1 282 ? 17.738 -10.728 15.911 1.00 14.13 ? 370 HIS A O 1 ATOM 2207 C CB . HIS A 1 282 ? 19.173 -13.180 15.643 1.00 14.54 ? 370 HIS A CB 1 ATOM 2208 C CG . HIS A 1 282 ? 20.017 -14.319 15.195 1.00 14.85 ? 370 HIS A CG 1 ATOM 2209 N ND1 . HIS A 1 282 ? 20.738 -15.116 16.064 1.00 18.23 ? 370 HIS A ND1 1 ATOM 2210 C CD2 . HIS A 1 282 ? 20.244 -14.810 13.957 1.00 15.73 ? 370 HIS A CD2 1 ATOM 2211 C CE1 . HIS A 1 282 ? 21.387 -16.037 15.368 1.00 19.47 ? 370 HIS A CE1 1 ATOM 2212 N NE2 . HIS A 1 282 ? 21.086 -15.890 14.091 1.00 19.07 ? 370 HIS A NE2 1 ATOM 2213 N N . TRP A 1 283 ? 16.355 -11.457 14.290 1.00 11.52 ? 371 TRP A N 1 ATOM 2214 C CA . TRP A 1 283 ? 15.334 -10.447 14.469 1.00 11.87 ? 371 TRP A CA 1 ATOM 2215 C C . TRP A 1 283 ? 14.116 -10.811 15.300 1.00 11.58 ? 371 TRP A C 1 ATOM 2216 O O . TRP A 1 283 ? 13.346 -9.934 15.667 1.00 11.97 ? 371 TRP A O 1 ATOM 2217 C CB . TRP A 1 283 ? 14.822 -10.025 13.051 1.00 11.65 ? 371 TRP A CB 1 ATOM 2218 C CG . TRP A 1 283 ? 14.233 -11.166 12.238 1.00 11.96 ? 371 TRP A CG 1 ATOM 2219 C CD1 . TRP A 1 283 ? 14.906 -11.988 11.409 1.00 12.86 ? 371 TRP A CD1 1 ATOM 2220 C CD2 . TRP A 1 283 ? 12.876 -11.612 12.230 1.00 12.38 ? 371 TRP A CD2 1 ATOM 2221 N NE1 . TRP A 1 283 ? 14.066 -12.930 10.863 1.00 12.96 ? 371 TRP A NE1 1 ATOM 2222 C CE2 . TRP A 1 283 ? 12.812 -12.730 11.353 1.00 13.59 ? 371 TRP A CE2 1 ATOM 2223 C CE3 . TRP A 1 283 ? 11.698 -11.176 12.838 1.00 15.17 ? 371 TRP A CE3 1 ATOM 2224 C CZ2 . TRP A 1 283 ? 11.626 -13.402 11.067 1.00 15.74 ? 371 TRP A CZ2 1 ATOM 2225 C CZ3 . TRP A 1 283 ? 10.512 -11.865 12.563 1.00 16.60 ? 371 TRP A CZ3 1 ATOM 2226 C CH2 . TRP A 1 283 ? 10.494 -12.970 11.688 1.00 17.68 ? 371 TRP A CH2 1 ATOM 2227 N N . CYS A 1 284 ? 13.913 -12.121 15.514 1.00 12.24 ? 372 CYS A N 1 ATOM 2228 C CA . CYS A 1 284 ? 12.630 -12.585 16.019 1.00 12.03 ? 372 CYS A CA 1 ATOM 2229 C C . CYS A 1 284 ? 12.629 -12.751 17.530 1.00 12.17 ? 372 CYS A C 1 ATOM 2230 O O . CYS A 1 284 ? 13.392 -13.564 18.041 1.00 13.29 ? 372 CYS A O 1 ATOM 2231 C CB . CYS A 1 284 ? 12.248 -13.935 15.401 1.00 13.79 ? 372 CYS A CB 1 ATOM 2232 S SG . CYS A 1 284 ? 10.565 -14.392 15.823 1.00 15.33 ? 372 CYS A SG 1 ATOM 2233 N N . ASN A 1 285 ? 11.776 -12.011 18.202 1.00 12.01 ? 373 ASN A N 1 ATOM 2234 C CA . ASN A 1 285 ? 11.568 -12.169 19.642 1.00 11.91 ? 373 ASN A CA 1 ATOM 2235 C C . ASN A 1 285 ? 12.895 -12.286 20.407 1.00 12.44 ? 373 ASN A C 1 ATOM 2236 O O . ASN A 1 285 ? 13.073 -13.189 21.220 1.00 12.90 ? 373 ASN A O 1 ATOM 2237 C CB . ASN A 1 285 ? 10.699 -13.413 19.907 1.00 12.56 ? 373 ASN A CB 1 ATOM 2238 C CG . ASN A 1 285 ? 9.334 -13.353 19.217 1.00 12.98 ? 373 ASN A CG 1 ATOM 2239 O OD1 . ASN A 1 285 ? 8.719 -12.287 19.146 1.00 13.84 ? 373 ASN A OD1 1 ATOM 2240 N ND2 . ASN A 1 285 ? 8.854 -14.492 18.735 1.00 14.28 ? 373 ASN A ND2 1 ATOM 2241 N N . ALA A 1 286 ? 13.811 -11.343 20.213 1.00 12.48 ? 374 ALA A N 1 ATOM 2242 C CA . ALA A 1 286 ? 15.181 -11.494 20.694 1.00 11.92 ? 374 ALA A CA 1 ATOM 2243 C C . ALA A 1 286 ? 15.203 -11.384 22.218 1.00 12.16 ? 374 ALA A C 1 ATOM 2244 O O . ALA A 1 286 ? 14.590 -10.534 22.800 1.00 12.14 ? 374 ALA A O 1 ATOM 2245 C CB . ALA A 1 286 ? 16.134 -10.439 20.082 1.00 11.84 ? 374 ALA A CB 1 ATOM 2246 N N . ILE A 1 287 ? 15.996 -12.263 22.817 1.00 13.11 ? 375 ILE A N 1 ATOM 2247 C CA . ILE A 1 287 ? 16.205 -12.247 24.262 1.00 13.57 ? 375 ILE A CA 1 ATOM 2248 C C . ILE A 1 287 ? 17.092 -11.075 24.643 1.00 12.30 ? 375 ILE A C 1 ATOM 2249 O O . ILE A 1 287 ? 17.811 -10.536 23.793 1.00 12.66 ? 375 ILE A O 1 ATOM 2250 C CB . ILE A 1 287 ? 16.764 -13.614 24.777 1.00 14.09 ? 375 ILE A CB 1 ATOM 2251 C CG1 . ILE A 1 287 ? 18.145 -13.897 24.183 1.00 15.38 ? 375 ILE A CG1 1 ATOM 2252 C CG2 . ILE A 1 287 ? 15.774 -14.747 24.490 1.00 14.56 ? 375 ILE A CG2 1 ATOM 2253 C CD1 . ILE A 1 287 ? 18.873 -15.093 24.800 1.00 16.95 ? 375 ILE A CD1 1 ATOM 2254 N N . GLY A 1 288 ? 17.010 -10.633 25.890 1.00 13.07 ? 376 GLY A N 1 ATOM 2255 C CA . GLY A 1 288 ? 17.933 -9.676 26.412 1.00 12.26 ? 376 GLY A CA 1 ATOM 2256 C C . GLY A 1 288 ? 17.725 -8.250 25.924 1.00 11.83 ? 376 GLY A C 1 ATOM 2257 O O . GLY A 1 288 ? 18.672 -7.459 25.871 1.00 13.80 ? 376 GLY A O 1 ATOM 2258 N N . THR A 1 289 ? 16.471 -7.923 25.651 1.00 11.63 ? 377 THR A N 1 ATOM 2259 C CA . THR A 1 289 ? 16.095 -6.618 25.148 1.00 11.33 ? 377 THR A CA 1 ATOM 2260 C C . THR A 1 289 ? 15.195 -5.912 26.130 1.00 11.51 ? 377 THR A C 1 ATOM 2261 O O . THR A 1 289 ? 14.555 -6.544 26.988 1.00 12.46 ? 377 THR A O 1 ATOM 2262 C CB . THR A 1 289 ? 15.338 -6.722 23.803 1.00 12.47 ? 377 THR A CB 1 ATOM 2263 O OG1 . THR A 1 289 ? 14.133 -7.496 24.001 1.00 13.19 ? 377 THR A OG1 1 ATOM 2264 C CG2 . THR A 1 289 ? 16.211 -7.411 22.755 1.00 11.26 ? 377 THR A CG2 1 ATOM 2265 N N . GLY A 1 290 ? 15.140 -4.599 26.015 1.00 11.42 ? 378 GLY A N 1 ATOM 2266 C CA . GLY A 1 290 ? 14.310 -3.756 26.848 1.00 11.28 ? 378 GLY A CA 1 ATOM 2267 C C . GLY A 1 290 ? 13.677 -2.609 26.106 1.00 10.81 ? 378 GLY A C 1 ATOM 2268 O O . GLY A 1 290 ? 14.167 -2.223 25.031 1.00 10.93 ? 378 GLY A O 1 ATOM 2269 N N . PHE A 1 291 ? 12.579 -2.097 26.620 1.00 11.77 ? 379 PHE A N 1 ATOM 2270 C CA . PHE A 1 291 ? 12.035 -0.856 26.068 1.00 11.79 ? 379 PHE A CA 1 ATOM 2271 C C . PHE A 1 291 ? 13.087 0.236 26.062 1.00 12.71 ? 379 PHE A C 1 ATOM 2272 O O . PHE A 1 291 ? 13.822 0.427 27.060 1.00 12.37 ? 379 PHE A O 1 ATOM 2273 C CB . PHE A 1 291 ? 10.834 -0.383 26.909 1.00 12.74 ? 379 PHE A CB 1 ATOM 2274 C CG . PHE A 1 291 ? 9.617 -1.236 26.790 1.00 13.68 ? 379 PHE A CG 1 ATOM 2275 C CD1 . PHE A 1 291 ? 8.981 -1.334 25.571 1.00 13.17 ? 379 PHE A CD1 1 ATOM 2276 C CD2 . PHE A 1 291 ? 9.040 -1.858 27.890 1.00 15.70 ? 379 PHE A CD2 1 ATOM 2277 C CE1 . PHE A 1 291 ? 7.850 -2.088 25.423 1.00 14.01 ? 379 PHE A CE1 1 ATOM 2278 C CE2 . PHE A 1 291 ? 7.920 -2.624 27.756 1.00 14.82 ? 379 PHE A CE2 1 ATOM 2279 C CZ . PHE A 1 291 ? 7.289 -2.732 26.531 1.00 14.43 ? 379 PHE A CZ 1 ATOM 2280 N N . GLY A 1 292 ? 13.191 0.985 24.969 1.00 11.93 ? 380 GLY A N 1 ATOM 2281 C CA . GLY A 1 292 ? 14.162 2.057 24.846 1.00 11.43 ? 380 GLY A CA 1 ATOM 2282 C C . GLY A 1 292 ? 13.611 3.456 25.036 1.00 11.50 ? 380 GLY A C 1 ATOM 2283 O O . GLY A 1 292 ? 12.524 3.629 25.598 1.00 12.75 ? 380 GLY A O 1 ATOM 2284 N N . MET A 1 293 ? 14.330 4.449 24.539 1.00 12.10 ? 381 MET A N 1 ATOM 2285 C CA . MET A 1 293 ? 13.914 5.856 24.633 1.00 14.21 ? 381 MET A CA 1 ATOM 2286 C C . MET A 1 293 ? 12.490 6.040 24.133 1.00 14.08 ? 381 MET A C 1 ATOM 2287 O O . MET A 1 293 ? 12.109 5.512 23.084 1.00 13.40 ? 381 MET A O 1 ATOM 2288 C CB . MET A 1 293 ? 14.822 6.768 23.863 1.00 16.49 ? 381 MET A CB 1 ATOM 2289 C CG . MET A 1 293 ? 16.201 6.897 24.441 1.00 19.89 ? 381 MET A CG 1 ATOM 2290 S SD . MET A 1 293 ? 17.143 8.087 23.545 1.00 25.73 ? 381 MET A SD 1 ATOM 2291 C CE . MET A 1 293 ? 17.298 7.130 22.099 1.00 16.06 ? 381 MET A CE 1 ATOM 2292 N N . ARG A 1 294 ? 11.680 6.786 24.873 1.00 14.81 ? 382 ARG A N 1 ATOM 2293 C CA . ARG A 1 294 ? 10.304 6.994 24.464 1.00 15.15 ? 382 ARG A CA 1 ATOM 2294 C C . ARG A 1 294 ? 10.269 7.871 23.219 1.00 13.09 ? 382 ARG A C 1 ATOM 2295 O O . ARG A 1 294 ? 11.157 8.689 22.969 1.00 14.03 ? 382 ARG A O 1 ATOM 2296 C CB . ARG A 1 294 ? 9.472 7.633 25.580 1.00 15.56 ? 382 ARG A CB 1 ATOM 2297 C CG . ARG A 1 294 ? 8.976 6.621 26.630 1.00 20.26 ? 382 ARG A CG 1 ATOM 2298 C CD . ARG A 1 294 ? 9.857 6.464 27.863 1.00 23.31 ? 382 ARG A CD 1 ATOM 2299 N NE . ARG A 1 294 ? 10.786 5.352 27.699 1.00 24.56 ? 382 ARG A NE 1 ATOM 2300 C CZ . ARG A 1 294 ? 11.429 4.758 28.696 1.00 22.99 ? 382 ARG A CZ 1 ATOM 2301 N NH1 . ARG A 1 294 ? 11.251 5.171 29.959 1.00 23.50 ? 382 ARG A NH1 1 ATOM 2302 N NH2 . ARG A 1 294 ? 12.242 3.751 28.428 1.00 22.09 ? 382 ARG A NH2 1 ATOM 2303 N N . PRO A 1 295 ? 9.191 7.731 22.449 1.00 13.05 ? 383 PRO A N 1 ATOM 2304 C CA . PRO A 1 295 ? 9.000 8.596 21.286 1.00 12.20 ? 383 PRO A CA 1 ATOM 2305 C C . PRO A 1 295 ? 9.105 10.077 21.585 1.00 12.39 ? 383 PRO A C 1 ATOM 2306 O O . PRO A 1 295 ? 8.529 10.534 22.566 1.00 13.94 ? 383 PRO A O 1 ATOM 2307 C CB . PRO A 1 295 ? 7.606 8.197 20.791 1.00 12.34 ? 383 PRO A CB 1 ATOM 2308 C CG . PRO A 1 295 ? 7.463 6.804 21.191 1.00 13.12 ? 383 PRO A CG 1 ATOM 2309 C CD . PRO A 1 295 ? 8.127 6.734 22.572 1.00 12.81 ? 383 PRO A CD 1 ATOM 2310 N N . THR A 1 296 ? 9.813 10.804 20.759 1.00 12.58 ? 384 THR A N 1 ATOM 2311 C CA . THR A 1 296 ? 9.994 12.214 20.937 1.00 13.36 ? 384 THR A CA 1 ATOM 2312 C C . THR A 1 296 ? 10.499 12.867 19.664 1.00 12.47 ? 384 THR A C 1 ATOM 2313 O O . THR A 1 296 ? 11.314 12.274 18.939 1.00 10.90 ? 384 THR A O 1 ATOM 2314 C CB . THR A 1 296 ? 10.933 12.502 22.123 1.00 14.64 ? 384 THR A CB 1 ATOM 2315 O OG1 . THR A 1 296 ? 11.083 13.905 22.257 1.00 16.26 ? 384 THR A OG1 1 ATOM 2316 C CG2 . THR A 1 296 ? 12.350 11.910 21.898 1.00 15.22 ? 384 THR A CG2 1 ATOM 2317 N N . ALA A 1 297 ? 10.100 14.122 19.435 1.00 12.74 ? 385 ALA A N 1 ATOM 2318 C CA . ALA A 1 297 ? 10.705 14.945 18.431 1.00 13.71 ? 385 ALA A CA 1 ATOM 2319 C C . ALA A 1 297 ? 11.995 15.614 18.881 1.00 14.76 ? 385 ALA A C 1 ATOM 2320 O O . ALA A 1 297 ? 12.710 16.200 18.085 1.00 16.24 ? 385 ALA A O 1 ATOM 2321 C CB . ALA A 1 297 ? 9.735 15.984 17.975 1.00 14.57 ? 385 ALA A CB 1 ATOM 2322 N N . ASN A 1 298 ? 12.288 15.538 20.174 1.00 15.18 ? 386 ASN A N 1 ATOM 2323 C CA . ASN A 1 298 ? 13.416 16.286 20.733 1.00 15.54 ? 386 ASN A CA 1 ATOM 2324 C C . ASN A 1 298 ? 14.612 15.384 20.786 1.00 15.24 ? 386 ASN A C 1 ATOM 2325 O O . ASN A 1 298 ? 15.013 14.881 21.821 1.00 17.04 ? 386 ASN A O 1 ATOM 2326 C CB . ASN A 1 298 ? 13.032 16.827 22.102 1.00 17.10 ? 386 ASN A CB 1 ATOM 2327 C CG . ASN A 1 298 ? 11.971 17.859 21.999 1.00 17.25 ? 386 ASN A CG 1 ATOM 2328 O OD1 . ASN A 1 298 ? 12.186 18.939 21.416 1.00 22.22 ? 386 ASN A OD1 1 ATOM 2329 N ND2 . ASN A 1 298 ? 10.804 17.557 22.544 1.00 21.57 ? 386 ASN A ND2 1 ATOM 2330 N N . THR A 1 299 ? 15.200 15.162 19.623 1.00 13.52 ? 387 THR A N 1 ATOM 2331 C CA . THR A 1 299 ? 16.216 14.138 19.461 1.00 13.39 ? 387 THR A CA 1 ATOM 2332 C C . THR A 1 299 ? 17.595 14.678 19.753 1.00 15.21 ? 387 THR A C 1 ATOM 2333 O O . THR A 1 299 ? 18.499 13.898 19.955 1.00 17.09 ? 387 THR A O 1 ATOM 2334 C CB . THR A 1 299 ? 16.246 13.608 18.038 1.00 11.58 ? 387 THR A CB 1 ATOM 2335 O OG1 . THR A 1 299 ? 16.544 14.688 17.171 1.00 12.56 ? 387 THR A OG1 1 ATOM 2336 C CG2 . THR A 1 299 ? 14.870 13.032 17.648 1.00 13.32 ? 387 THR A CG2 1 ATOM 2337 N N . GLY A 1 300 ? 17.742 15.995 19.678 1.00 15.29 ? 388 GLY A N 1 ATOM 2338 C CA . GLY A 1 300 ? 19.050 16.611 19.789 1.00 16.61 ? 388 GLY A CA 1 ATOM 2339 C C . GLY A 1 300 ? 19.905 16.478 18.543 1.00 16.78 ? 388 GLY A C 1 ATOM 2340 O O . GLY A 1 300 ? 21.048 16.930 18.501 1.00 19.25 ? 388 GLY A O 1 ATOM 2341 N N . HIS A 1 301 ? 19.378 15.855 17.493 1.00 14.10 ? 389 HIS A N 1 ATOM 2342 C CA . HIS A 1 301 ? 20.203 15.589 16.324 1.00 12.94 ? 389 HIS A CA 1 ATOM 2343 C C . HIS A 1 301 ? 19.527 16.140 15.104 1.00 12.73 ? 389 HIS A C 1 ATOM 2344 O O . HIS A 1 301 ? 18.372 15.791 14.827 1.00 11.66 ? 389 HIS A O 1 ATOM 2345 C CB . HIS A 1 301 ? 20.471 14.109 16.185 1.00 13.31 ? 389 HIS A CB 1 ATOM 2346 C CG . HIS A 1 301 ? 21.601 13.811 15.270 1.00 12.67 ? 389 HIS A CG 1 ATOM 2347 N ND1 . HIS A 1 301 ? 21.520 13.985 13.908 1.00 13.01 ? 389 HIS A ND1 1 ATOM 2348 C CD2 . HIS A 1 301 ? 22.867 13.414 15.543 1.00 12.89 ? 389 HIS A CD2 1 ATOM 2349 C CE1 . HIS A 1 301 ? 22.688 13.661 13.375 1.00 13.27 ? 389 HIS A CE1 1 ATOM 2350 N NE2 . HIS A 1 301 ? 23.527 13.325 14.348 1.00 13.34 ? 389 HIS A NE2 1 ATOM 2351 N N . GLN A 1 302 ? 20.197 17.027 14.372 1.00 12.00 ? 390 GLN A N 1 ATOM 2352 C CA . GLN A 1 302 ? 19.551 17.691 13.272 1.00 13.09 ? 390 GLN A CA 1 ATOM 2353 C C . GLN A 1 302 ? 19.115 16.768 12.129 1.00 11.27 ? 390 GLN A C 1 ATOM 2354 O O . GLN A 1 302 ? 18.257 17.163 11.395 1.00 13.37 ? 390 GLN A O 1 ATOM 2355 C CB . GLN A 1 302 ? 20.390 18.857 12.757 1.00 14.62 ? 390 GLN A CB 1 ATOM 2356 C CG . GLN A 1 302 ? 21.503 18.536 11.823 1.00 17.90 ? 390 GLN A CG 1 ATOM 2357 C CD . GLN A 1 302 ? 21.710 19.617 10.724 1.00 21.27 ? 390 GLN A CD 1 ATOM 2358 O OE1 . GLN A 1 302 ? 21.229 19.495 9.591 1.00 20.96 ? 390 GLN A OE1 1 ATOM 2359 N NE2 . GLN A 1 302 ? 22.460 20.646 11.063 1.00 23.12 ? 390 GLN A NE2 1 ATOM 2360 N N . TYR A 1 303 ? 19.696 15.579 12.003 1.00 11.09 ? 391 TYR A N 1 ATOM 2361 C CA . TYR A 1 303 ? 19.271 14.653 10.932 1.00 9.60 ? 391 TYR A CA 1 ATOM 2362 C C . TYR A 1 303 ? 18.084 13.779 11.335 1.00 9.28 ? 391 TYR A C 1 ATOM 2363 O O . TYR A 1 303 ? 17.556 13.045 10.502 1.00 9.35 ? 391 TYR A O 1 ATOM 2364 C CB . TYR A 1 303 ? 20.390 13.717 10.507 1.00 9.71 ? 391 TYR A CB 1 ATOM 2365 C CG . TYR A 1 303 ? 21.627 14.339 9.935 1.00 10.01 ? 391 TYR A CG 1 ATOM 2366 C CD1 . TYR A 1 303 ? 21.642 15.648 9.446 1.00 11.70 ? 391 TYR A CD1 1 ATOM 2367 C CD2 . TYR A 1 303 ? 22.793 13.607 9.873 1.00 10.35 ? 391 TYR A CD2 1 ATOM 2368 C CE1 . TYR A 1 303 ? 22.825 16.189 8.881 1.00 11.97 ? 391 TYR A CE1 1 ATOM 2369 C CE2 . TYR A 1 303 ? 23.979 14.128 9.333 1.00 11.37 ? 391 TYR A CE2 1 ATOM 2370 C CZ . TYR A 1 303 ? 23.972 15.414 8.852 1.00 12.10 ? 391 TYR A CZ 1 ATOM 2371 O OH . TYR A 1 303 ? 25.156 15.905 8.314 1.00 15.16 ? 391 TYR A OH 1 ATOM 2372 N N . VAL A 1 304 ? 17.687 13.800 12.594 1.00 8.89 ? 392 VAL A N 1 ATOM 2373 C CA . VAL A 1 304 ? 16.688 12.893 13.118 1.00 8.62 ? 392 VAL A CA 1 ATOM 2374 C C . VAL A 1 304 ? 15.467 13.643 13.590 1.00 8.79 ? 392 VAL A C 1 ATOM 2375 O O . VAL A 1 304 ? 15.512 14.383 14.601 1.00 9.77 ? 392 VAL A O 1 ATOM 2376 C CB . VAL A 1 304 ? 17.272 12.004 14.257 1.00 9.18 ? 392 VAL A CB 1 ATOM 2377 C CG1 . VAL A 1 304 ? 16.283 10.937 14.729 1.00 9.92 ? 392 VAL A CG1 1 ATOM 2378 C CG2 . VAL A 1 304 ? 18.604 11.347 13.821 1.00 10.57 ? 392 VAL A CG2 1 ATOM 2379 N N . ASP A 1 305 ? 14.376 13.489 12.861 1.00 8.10 ? 393 ASP A N 1 ATOM 2380 C CA . ASP A 1 305 ? 13.131 14.100 13.256 1.00 8.62 ? 393 ASP A CA 1 ATOM 2381 C C . ASP A 1 305 ? 12.558 13.564 14.557 1.00 9.29 ? 393 ASP A C 1 ATOM 2382 O O . ASP A 1 305 ? 11.901 14.308 15.326 1.00 9.22 ? 393 ASP A O 1 ATOM 2383 C CB . ASP A 1 305 ? 12.060 13.890 12.182 1.00 8.78 ? 393 ASP A CB 1 ATOM 2384 C CG . ASP A 1 305 ? 12.218 14.765 10.987 1.00 8.54 ? 393 ASP A CG 1 ATOM 2385 O OD1 . ASP A 1 305 ? 12.916 15.811 11.027 1.00 9.61 ? 393 ASP A OD1 1 ATOM 2386 O OD2 . ASP A 1 305 ? 11.621 14.458 9.941 1.00 9.27 ? 393 ASP A OD2 1 ATOM 2387 N N . ALA A 1 306 ? 12.723 12.265 14.802 1.00 8.48 ? 394 ALA A N 1 ATOM 2388 C CA . ALA A 1 306 ? 12.145 11.604 15.962 1.00 8.43 ? 394 ALA A CA 1 ATOM 2389 C C . ALA A 1 306 ? 12.736 10.264 16.278 1.00 7.57 ? 394 ALA A C 1 ATOM 2390 O O . ALA A 1 306 ? 13.121 9.533 15.372 1.00 8.80 ? 394 ALA A O 1 ATOM 2391 C CB . ALA A 1 306 ? 10.599 11.447 15.809 1.00 8.44 ? 394 ALA A CB 1 ATOM 2392 N N . PHE A 1 307 ? 12.756 9.921 17.572 1.00 7.73 ? 395 PHE A N 1 ATOM 2393 C CA . PHE A 1 307 ? 12.779 8.559 17.999 1.00 8.14 ? 395 PHE A CA 1 ATOM 2394 C C . PHE A 1 307 ? 11.360 8.081 18.122 1.00 8.46 ? 395 PHE A C 1 ATOM 2395 O O . PHE A 1 307 ? 10.495 8.820 18.595 1.00 10.26 ? 395 PHE A O 1 ATOM 2396 C CB . PHE A 1 307 ? 13.524 8.393 19.334 1.00 8.57 ? 395 PHE A CB 1 ATOM 2397 C CG . PHE A 1 307 ? 14.906 8.899 19.281 1.00 9.67 ? 395 PHE A CG 1 ATOM 2398 C CD1 . PHE A 1 307 ? 15.819 8.332 18.414 1.00 12.29 ? 395 PHE A CD1 1 ATOM 2399 C CD2 . PHE A 1 307 ? 15.352 9.883 20.139 1.00 13.34 ? 395 PHE A CD2 1 ATOM 2400 C CE1 . PHE A 1 307 ? 17.127 8.800 18.341 1.00 14.86 ? 395 PHE A CE1 1 ATOM 2401 C CE2 . PHE A 1 307 ? 16.684 10.346 20.042 1.00 13.95 ? 395 PHE A CE2 1 ATOM 2402 C CZ . PHE A 1 307 ? 17.542 9.797 19.154 1.00 15.06 ? 395 PHE A CZ 1 ATOM 2403 N N . VAL A 1 308 ? 11.097 6.880 17.658 1.00 7.73 ? 396 VAL A N 1 ATOM 2404 C CA . VAL A 1 308 ? 9.771 6.362 17.609 1.00 7.36 ? 396 VAL A CA 1 ATOM 2405 C C . VAL A 1 308 ? 9.766 4.929 18.112 1.00 7.71 ? 396 VAL A C 1 ATOM 2406 O O . VAL A 1 308 ? 10.814 4.296 18.241 1.00 8.24 ? 396 VAL A O 1 ATOM 2407 C CB . VAL A 1 308 ? 9.211 6.404 16.120 1.00 8.09 ? 396 VAL A CB 1 ATOM 2408 C CG1 . VAL A 1 308 ? 8.943 7.836 15.729 1.00 10.18 ? 396 VAL A CG1 1 ATOM 2409 C CG2 . VAL A 1 308 ? 10.194 5.783 15.147 1.00 8.33 ? 396 VAL A CG2 1 ATOM 2410 N N . TRP A 1 309 ? 8.571 4.401 18.340 1.00 8.39 ? 397 TRP A N 1 ATOM 2411 C CA . TRP A 1 309 ? 8.364 3.008 18.605 1.00 8.50 ? 397 TRP A CA 1 ATOM 2412 C C . TRP A 1 309 ? 7.545 2.437 17.464 1.00 8.93 ? 397 TRP A C 1 ATOM 2413 O O . TRP A 1 309 ? 6.342 2.620 17.403 1.00 9.09 ? 397 TRP A O 1 ATOM 2414 C CB . TRP A 1 309 ? 7.591 2.792 19.912 1.00 9.17 ? 397 TRP A CB 1 ATOM 2415 C CG . TRP A 1 309 ? 8.406 2.997 21.174 1.00 9.69 ? 397 TRP A CG 1 ATOM 2416 C CD1 . TRP A 1 309 ? 9.588 3.620 21.282 1.00 8.62 ? 397 TRP A CD1 1 ATOM 2417 C CD2 . TRP A 1 309 ? 8.074 2.520 22.487 1.00 11.23 ? 397 TRP A CD2 1 ATOM 2418 N NE1 . TRP A 1 309 ? 10.038 3.591 22.587 1.00 10.23 ? 397 TRP A NE1 1 ATOM 2419 C CE2 . TRP A 1 309 ? 9.111 2.939 23.348 1.00 10.35 ? 397 TRP A CE2 1 ATOM 2420 C CE3 . TRP A 1 309 ? 7.002 1.816 23.033 1.00 11.62 ? 397 TRP A CE3 1 ATOM 2421 C CZ2 . TRP A 1 309 ? 9.124 2.617 24.731 1.00 11.35 ? 397 TRP A CZ2 1 ATOM 2422 C CZ3 . TRP A 1 309 ? 7.016 1.513 24.409 1.00 12.46 ? 397 TRP A CZ3 1 ATOM 2423 C CH2 . TRP A 1 309 ? 8.058 1.930 25.210 1.00 13.37 ? 397 TRP A CH2 1 ATOM 2424 N N . VAL A 1 310 ? 8.220 1.812 16.503 1.00 7.93 ? 398 VAL A N 1 ATOM 2425 C CA . VAL A 1 310 ? 7.512 1.365 15.302 1.00 8.17 ? 398 VAL A CA 1 ATOM 2426 C C . VAL A 1 310 ? 6.907 -0.006 15.574 1.00 8.29 ? 398 VAL A C 1 ATOM 2427 O O . VAL A 1 310 ? 5.684 -0.187 15.503 1.00 9.94 ? 398 VAL A O 1 ATOM 2428 C CB . VAL A 1 310 ? 8.375 1.369 14.007 1.00 7.84 ? 398 VAL A CB 1 ATOM 2429 C CG1 . VAL A 1 310 ? 7.453 1.019 12.821 1.00 8.91 ? 398 VAL A CG1 1 ATOM 2430 C CG2 . VAL A 1 310 ? 8.979 2.708 13.812 1.00 9.51 ? 398 VAL A CG2 1 ATOM 2431 N N . LYS A 1 311 ? 7.734 -0.989 15.952 1.00 9.21 ? 399 LYS A N 1 ATOM 2432 C CA . LYS A 1 311 ? 7.207 -2.265 16.462 1.00 9.93 ? 399 LYS A CA 1 ATOM 2433 C C . LYS A 1 311 ? 6.744 -2.115 17.905 1.00 11.51 ? 399 LYS A C 1 ATOM 2434 O O . LYS A 1 311 ? 7.554 -1.730 18.741 1.00 12.23 ? 399 LYS A O 1 ATOM 2435 C CB . LYS A 1 311 ? 8.285 -3.323 16.389 1.00 11.04 ? 399 LYS A CB 1 ATOM 2436 C CG . LYS A 1 311 ? 7.898 -4.682 16.973 1.00 11.14 ? 399 LYS A CG 1 ATOM 2437 C CD . LYS A 1 311 ? 6.672 -5.390 16.287 1.00 12.13 ? 399 LYS A CD 1 ATOM 2438 C CE . LYS A 1 311 ? 6.240 -6.588 17.114 1.00 12.86 ? 399 LYS A CE 1 ATOM 2439 N NZ . LYS A 1 311 ? 5.214 -7.367 16.402 1.00 13.10 ? 399 LYS A NZ 1 ATOM 2440 N N . PRO A 1 312 ? 5.457 -2.392 18.217 1.00 11.32 ? 400 PRO A N 1 ATOM 2441 C CA . PRO A 1 312 ? 5.004 -2.296 19.612 1.00 13.13 ? 400 PRO A CA 1 ATOM 2442 C C . PRO A 1 312 ? 5.472 -3.483 20.424 1.00 13.33 ? 400 PRO A C 1 ATOM 2443 O O . PRO A 1 312 ? 5.103 -4.615 20.200 1.00 14.19 ? 400 PRO A O 1 ATOM 2444 C CB . PRO A 1 312 ? 3.483 -2.273 19.497 1.00 13.66 ? 400 PRO A CB 1 ATOM 2445 C CG . PRO A 1 312 ? 3.248 -1.979 18.048 1.00 15.44 ? 400 PRO A CG 1 ATOM 2446 C CD . PRO A 1 312 ? 4.310 -2.666 17.328 1.00 12.01 ? 400 PRO A CD 1 ATOM 2447 N N . GLY A 1 313 ? 6.357 -3.194 21.364 1.00 14.14 ? 401 GLY A N 1 ATOM 2448 C CA . GLY A 1 313 ? 6.970 -4.265 22.134 1.00 14.87 ? 401 GLY A CA 1 ATOM 2449 C C . GLY A 1 313 ? 5.938 -5.017 22.989 1.00 13.47 ? 401 GLY A C 1 ATOM 2450 O O . GLY A 1 313 ? 5.159 -4.401 23.747 1.00 15.10 ? 401 GLY A O 1 ATOM 2451 N N . GLY A 1 314 ? 6.013 -6.336 22.896 1.00 13.83 ? 402 GLY A N 1 ATOM 2452 C CA . GLY A 1 314 ? 5.053 -7.235 23.532 1.00 15.05 ? 402 GLY A CA 1 ATOM 2453 C C . GLY A 1 314 ? 4.166 -7.955 22.540 1.00 15.83 ? 402 GLY A C 1 ATOM 2454 O O . GLY A 1 314 ? 3.667 -9.035 22.812 1.00 16.35 ? 402 GLY A O 1 ATOM 2455 N N . GLU A 1 315 ? 3.975 -7.358 21.355 1.00 14.61 ? 403 GLU A N 1 ATOM 2456 C CA . GLU A 1 315 ? 3.267 -8.043 20.281 1.00 14.45 ? 403 GLU A CA 1 ATOM 2457 C C . GLU A 1 315 ? 4.286 -8.942 19.582 1.00 14.52 ? 403 GLU A C 1 ATOM 2458 O O . GLU A 1 315 ? 5.394 -8.481 19.233 1.00 14.10 ? 403 GLU A O 1 ATOM 2459 C CB . GLU A 1 315 ? 2.598 -7.007 19.338 1.00 13.92 ? 403 GLU A CB 1 ATOM 2460 C CG . GLU A 1 315 ? 1.510 -6.214 20.060 1.00 16.60 ? 403 GLU A CG 1 ATOM 2461 C CD . GLU A 1 315 ? 0.754 -5.223 19.188 1.00 19.20 ? 403 GLU A CD 1 ATOM 2462 O OE1 . GLU A 1 315 ? 1.055 -5.198 17.963 1.00 19.26 ? 403 GLU A OE1 1 ATOM 2463 O OE2 . GLU A 1 315 ? -0.117 -4.466 19.723 1.00 19.37 ? 403 GLU A OE2 1 ATOM 2464 N N . CYS A 1 316 ? 3.966 -10.221 19.427 1.00 13.91 ? 404 CYS A N 1 ATOM 2465 C CA . CYS A 1 316 ? 4.900 -11.218 18.981 1.00 13.41 ? 404 CYS A CA 1 ATOM 2466 C C . CYS A 1 316 ? 5.382 -10.941 17.569 1.00 13.45 ? 404 CYS A C 1 ATOM 2467 O O . CYS A 1 316 ? 4.627 -10.366 16.790 1.00 14.09 ? 404 CYS A O 1 ATOM 2468 C CB . CYS A 1 316 ? 4.239 -12.588 18.989 1.00 14.95 ? 404 CYS A CB 1 ATOM 2469 S SG . CYS A 1 316 ? 5.440 -13.893 18.874 1.00 16.76 ? 404 CYS A SG 1 ATOM 2470 N N . ASP A 1 317 ? 6.611 -11.324 17.272 1.00 11.28 ? 405 ASP A N 1 ATOM 2471 C CA . ASP A 1 317 ? 7.160 -11.203 15.919 1.00 12.37 ? 405 ASP A CA 1 ATOM 2472 C C . ASP A 1 317 ? 6.845 -12.404 15.053 1.00 14.07 ? 405 ASP A C 1 ATOM 2473 O O . ASP A 1 317 ? 6.993 -12.370 13.848 1.00 14.82 ? 405 ASP A O 1 ATOM 2474 C CB . ASP A 1 317 ? 8.688 -11.093 15.949 1.00 12.29 ? 405 ASP A CB 1 ATOM 2475 C CG . ASP A 1 317 ? 9.194 -9.834 16.578 1.00 14.09 ? 405 ASP A CG 1 ATOM 2476 O OD1 . ASP A 1 317 ? 8.621 -8.732 16.366 1.00 15.37 ? 405 ASP A OD1 1 ATOM 2477 O OD2 . ASP A 1 317 ? 10.227 -9.843 17.320 1.00 14.82 ? 405 ASP A OD2 1 ATOM 2478 N N . GLY A 1 318 ? 6.505 -13.532 15.668 1.00 14.17 ? 406 GLY A N 1 ATOM 2479 C CA . GLY A 1 318 ? 6.364 -14.794 14.962 1.00 14.55 ? 406 GLY A CA 1 ATOM 2480 C C . GLY A 1 318 ? 6.330 -15.969 15.927 1.00 15.92 ? 406 GLY A C 1 ATOM 2481 O O . GLY A 1 318 ? 6.955 -15.917 16.992 1.00 15.18 ? 406 GLY A O 1 ATOM 2482 N N . THR A 1 319 ? 5.617 -17.018 15.545 1.00 16.05 ? 407 THR A N 1 ATOM 2483 C CA . THR A 1 319 ? 5.439 -18.183 16.417 1.00 17.32 ? 407 THR A CA 1 ATOM 2484 C C . THR A 1 319 ? 6.702 -18.998 16.483 1.00 17.79 ? 407 THR A C 1 ATOM 2485 O O . THR A 1 319 ? 7.468 -19.098 15.553 1.00 16.50 ? 407 THR A O 1 ATOM 2486 C CB . THR A 1 319 ? 4.245 -19.027 15.919 1.00 17.29 ? 407 THR A CB 1 ATOM 2487 O OG1 . THR A 1 319 ? 4.060 -20.129 16.810 1.00 19.43 ? 407 THR A OG1 1 ATOM 2488 C CG2 . THR A 1 319 ? 4.502 -19.686 14.583 1.00 18.03 ? 407 THR A CG2 1 ATOM 2489 N N . SER A 1 320 ? 6.895 -19.671 17.618 1.00 19.29 ? 408 SER A N 1 ATOM 2490 C CA . SER A 1 320 ? 7.984 -20.634 17.707 1.00 21.33 ? 408 SER A CA 1 ATOM 2491 C C . SER A 1 320 ? 7.496 -22.046 17.431 1.00 22.29 ? 408 SER A C 1 ATOM 2492 O O . SER A 1 320 ? 8.311 -22.966 17.419 1.00 23.74 ? 408 SER A O 1 ATOM 2493 C CB . SER A 1 320 ? 8.647 -20.611 19.094 1.00 21.32 ? 408 SER A CB 1 ATOM 2494 O OG . SER A 1 320 ? 7.690 -20.763 20.122 1.00 21.49 ? 408 SER A OG 1 ATOM 2495 N N . ASP A 1 321 ? 6.184 -22.189 17.214 1.00 23.32 ? 409 ASP A N 1 ATOM 2496 C CA . ASP A 1 321 ? 5.558 -23.496 16.883 1.00 24.10 ? 409 ASP A CA 1 ATOM 2497 C C . ASP A 1 321 ? 6.069 -23.931 15.506 1.00 24.67 ? 409 ASP A C 1 ATOM 2498 O O . ASP A 1 321 ? 5.634 -23.392 14.475 1.00 23.98 ? 409 ASP A O 1 ATOM 2499 C CB . ASP A 1 321 ? 4.023 -23.372 16.929 1.00 24.69 ? 409 ASP A CB 1 ATOM 2500 C CG . ASP A 1 321 ? 3.291 -24.619 16.427 1.00 27.07 ? 409 ASP A CG 1 ATOM 2501 O OD1 . ASP A 1 321 ? 3.951 -25.622 16.137 1.00 26.84 ? 409 ASP A OD1 1 ATOM 2502 O OD2 . ASP A 1 321 ? 2.049 -24.637 16.284 1.00 31.05 ? 409 ASP A OD2 1 ATOM 2503 N N . THR A 1 322 ? 7.005 -24.872 15.482 1.00 25.99 ? 410 THR A N 1 ATOM 2504 C CA . THR A 1 322 ? 7.665 -25.264 14.231 1.00 27.56 ? 410 THR A CA 1 ATOM 2505 C C . THR A 1 322 ? 6.750 -25.977 13.248 1.00 28.14 ? 410 THR A C 1 ATOM 2506 O O . THR A 1 322 ? 7.112 -26.133 12.084 1.00 29.36 ? 410 THR A O 1 ATOM 2507 C CB . THR A 1 322 ? 8.874 -26.177 14.449 1.00 28.07 ? 410 THR A CB 1 ATOM 2508 O OG1 . THR A 1 322 ? 8.444 -27.449 14.971 1.00 30.67 ? 410 THR A OG1 1 ATOM 2509 C CG2 . THR A 1 322 ? 9.848 -25.628 15.470 1.00 28.99 ? 410 THR A CG2 1 ATOM 2510 N N . THR A 1 323 ? 5.591 -26.426 13.725 1.00 28.17 ? 411 THR A N 1 ATOM 2511 C CA . THR A 1 323 ? 4.638 -27.145 12.884 1.00 27.96 ? 411 THR A CA 1 ATOM 2512 C C . THR A 1 323 ? 3.703 -26.178 12.182 1.00 27.06 ? 411 THR A C 1 ATOM 2513 O O . THR A 1 323 ? 2.916 -26.560 11.308 1.00 27.71 ? 411 THR A O 1 ATOM 2514 C CB . THR A 1 323 ? 3.820 -28.169 13.737 1.00 27.72 ? 411 THR A CB 1 ATOM 2515 O OG1 . THR A 1 323 ? 2.880 -27.488 14.582 1.00 29.92 ? 411 THR A OG1 1 ATOM 2516 C CG2 . THR A 1 323 ? 4.736 -28.959 14.689 1.00 28.76 ? 411 THR A CG2 1 ATOM 2517 N N . ALA A 1 324 ? 3.790 -24.911 12.549 1.00 25.29 ? 412 ALA A N 1 ATOM 2518 C CA . ALA A 1 324 ? 2.882 -23.921 12.039 1.00 24.37 ? 412 ALA A CA 1 ATOM 2519 C C . ALA A 1 324 ? 3.316 -23.596 10.598 1.00 23.46 ? 412 ALA A C 1 ATOM 2520 O O . ALA A 1 324 ? 4.508 -23.550 10.295 1.00 22.85 ? 412 ALA A O 1 ATOM 2521 C CB . ALA A 1 324 ? 2.917 -22.671 12.925 1.00 24.93 ? 412 ALA A CB 1 ATOM 2522 N N . ALA A 1 325 ? 2.345 -23.437 9.711 1.00 22.99 ? 413 ALA A N 1 ATOM 2523 C CA . ALA A 1 325 ? 2.628 -23.113 8.318 1.00 21.88 ? 413 ALA A CA 1 ATOM 2524 C C . ALA A 1 325 ? 3.492 -21.861 8.202 1.00 22.31 ? 413 ALA A C 1 ATOM 2525 O O . ALA A 1 325 ? 4.394 -21.806 7.367 1.00 22.82 ? 413 ALA A O 1 ATOM 2526 C CB . ALA A 1 325 ? 1.350 -22.909 7.563 1.00 22.13 ? 413 ALA A CB 1 ATOM 2527 N N . ARG A 1 326 ? 3.216 -20.879 9.056 1.00 21.75 ? 414 ARG A N 1 ATOM 2528 C CA . ARG A 1 326 ? 3.887 -19.560 9.000 1.00 21.87 ? 414 ARG A CA 1 ATOM 2529 C C . ARG A 1 326 ? 5.169 -19.483 9.814 1.00 20.63 ? 414 ARG A C 1 ATOM 2530 O O . ARG A 1 326 ? 5.756 -18.390 9.965 1.00 20.91 ? 414 ARG A O 1 ATOM 2531 C CB . ARG A 1 326 ? 2.949 -18.481 9.489 1.00 22.85 ? 414 ARG A CB 1 ATOM 2532 C CG . ARG A 1 326 ? 1.783 -18.195 8.555 1.00 24.00 ? 414 ARG A CG 1 ATOM 2533 C CD . ARG A 1 326 ? 0.655 -17.344 9.138 0.50 23.58 ? 414 ARG A CD 1 ATOM 2534 N NE . ARG A 1 326 ? 1.032 -16.475 10.252 0.50 23.24 ? 414 ARG A NE 1 ATOM 2535 C CZ . ARG A 1 326 ? 0.211 -15.607 10.843 0.50 22.89 ? 414 ARG A CZ 1 ATOM 2536 N NH1 . ARG A 1 326 ? -1.047 -15.441 10.421 0.50 23.29 ? 414 ARG A NH1 1 ATOM 2537 N NH2 . ARG A 1 326 ? 0.649 -14.877 11.850 0.50 24.09 ? 414 ARG A NH2 1 ATOM 2538 N N . TYR A 1 327 ? 5.613 -20.611 10.329 1.00 19.87 ? 415 TYR A N 1 ATOM 2539 C CA . TYR A 1 327 ? 6.795 -20.636 11.148 1.00 18.83 ? 415 TYR A CA 1 ATOM 2540 C C . TYR A 1 327 ? 8.007 -20.147 10.365 1.00 18.13 ? 415 TYR A C 1 ATOM 2541 O O . TYR A 1 327 ? 8.237 -20.546 9.230 1.00 18.43 ? 415 TYR A O 1 ATOM 2542 C CB . TYR A 1 327 ? 7.041 -22.071 11.615 1.00 18.59 ? 415 TYR A CB 1 ATOM 2543 C CG . TYR A 1 327 ? 8.346 -22.226 12.351 1.00 19.76 ? 415 TYR A CG 1 ATOM 2544 C CD1 . TYR A 1 327 ? 8.517 -21.673 13.619 1.00 22.00 ? 415 TYR A CD1 1 ATOM 2545 C CD2 . TYR A 1 327 ? 9.400 -22.921 11.790 1.00 20.51 ? 415 TYR A CD2 1 ATOM 2546 C CE1 . TYR A 1 327 ? 9.731 -21.804 14.304 1.00 21.16 ? 415 TYR A CE1 1 ATOM 2547 C CE2 . TYR A 1 327 ? 10.629 -23.058 12.473 1.00 21.06 ? 415 TYR A CE2 1 ATOM 2548 C CZ . TYR A 1 327 ? 10.765 -22.511 13.725 1.00 20.53 ? 415 TYR A CZ 1 ATOM 2549 O OH . TYR A 1 327 ? 11.968 -22.682 14.376 1.00 24.96 ? 415 TYR A OH 1 ATOM 2550 N N . ALA A 1 328 ? 8.775 -19.260 11.001 1.00 16.86 ? 416 ALA A N 1 ATOM 2551 C CA . ALA A 1 328 ? 10.030 -18.744 10.468 1.00 16.90 ? 416 ALA A CA 1 ATOM 2552 C C . ALA A 1 328 ? 11.131 -19.247 11.367 1.00 16.60 ? 416 ALA A C 1 ATOM 2553 O O . ALA A 1 328 ? 11.035 -19.083 12.580 1.00 17.18 ? 416 ALA A O 1 ATOM 2554 C CB . ALA A 1 328 ? 10.024 -17.180 10.505 1.00 16.68 ? 416 ALA A CB 1 ATOM 2555 N N . TYR A 1 329 ? 12.168 -19.824 10.786 1.00 17.22 ? 417 TYR A N 1 ATOM 2556 C CA . TYR A 1 329 ? 13.197 -20.489 11.599 1.00 16.97 ? 417 TYR A CA 1 ATOM 2557 C C . TYR A 1 329 ? 13.915 -19.545 12.550 1.00 16.83 ? 417 TYR A C 1 ATOM 2558 O O . TYR A 1 329 ? 14.384 -19.940 13.612 1.00 16.80 ? 417 TYR A O 1 ATOM 2559 C CB . TYR A 1 329 ? 14.197 -21.254 10.732 1.00 18.11 ? 417 TYR A CB 1 ATOM 2560 C CG . TYR A 1 329 ? 15.319 -20.470 10.141 1.00 19.28 ? 417 TYR A CG 1 ATOM 2561 C CD1 . TYR A 1 329 ? 16.441 -20.184 10.884 1.00 21.72 ? 417 TYR A CD1 1 ATOM 2562 C CD2 . TYR A 1 329 ? 15.290 -20.053 8.806 1.00 21.38 ? 417 TYR A CD2 1 ATOM 2563 C CE1 . TYR A 1 329 ? 17.493 -19.476 10.359 1.00 23.17 ? 417 TYR A CE1 1 ATOM 2564 C CE2 . TYR A 1 329 ? 16.345 -19.341 8.259 1.00 22.92 ? 417 TYR A CE2 1 ATOM 2565 C CZ . TYR A 1 329 ? 17.455 -19.056 9.039 1.00 24.65 ? 417 TYR A CZ 1 ATOM 2566 O OH . TYR A 1 329 ? 18.535 -18.343 8.534 1.00 27.76 ? 417 TYR A OH 1 ATOM 2567 N N . HIS A 1 330 ? 13.989 -18.266 12.208 1.00 15.45 ? 418 HIS A N 1 ATOM 2568 C CA . HIS A 1 330 ? 14.583 -17.312 13.148 1.00 14.70 ? 418 HIS A CA 1 ATOM 2569 C C . HIS A 1 330 ? 13.875 -17.294 14.501 1.00 14.45 ? 418 HIS A C 1 ATOM 2570 O O . HIS A 1 330 ? 14.481 -16.907 15.479 1.00 14.92 ? 418 HIS A O 1 ATOM 2571 C CB . HIS A 1 330 ? 14.624 -15.894 12.538 1.00 15.14 ? 418 HIS A CB 1 ATOM 2572 C CG . HIS A 1 330 ? 15.786 -15.676 11.620 1.00 15.56 ? 418 HIS A CG 1 ATOM 2573 N ND1 . HIS A 1 330 ? 15.748 -15.975 10.279 1.00 17.14 ? 418 HIS A ND1 1 ATOM 2574 C CD2 . HIS A 1 330 ? 17.041 -15.230 11.868 1.00 15.41 ? 418 HIS A CD2 1 ATOM 2575 C CE1 . HIS A 1 330 ? 16.923 -15.712 9.735 1.00 18.40 ? 418 HIS A CE1 1 ATOM 2576 N NE2 . HIS A 1 330 ? 17.723 -15.255 10.671 1.00 17.80 ? 418 HIS A NE2 1 ATOM 2577 N N . CYS A 1 331 ? 12.585 -17.641 14.550 1.00 14.56 ? 419 CYS A N 1 ATOM 2578 C CA . CYS A 1 331 ? 11.787 -17.596 15.753 1.00 14.93 ? 419 CYS A CA 1 ATOM 2579 C C . CYS A 1 331 ? 12.005 -18.850 16.629 1.00 15.49 ? 419 CYS A C 1 ATOM 2580 O O . CYS A 1 331 ? 11.534 -18.894 17.740 1.00 16.36 ? 419 CYS A O 1 ATOM 2581 C CB . CYS A 1 331 ? 10.305 -17.407 15.413 1.00 15.19 ? 419 CYS A CB 1 ATOM 2582 S SG . CYS A 1 331 ? 9.996 -15.876 14.496 1.00 16.81 ? 419 CYS A SG 1 ATOM 2583 N N . GLY A 1 332 ? 12.799 -19.779 16.133 1.00 15.68 ? 420 GLY A N 1 ATOM 2584 C CA . GLY A 1 332 ? 13.145 -20.966 16.891 1.00 16.86 ? 420 GLY A CA 1 ATOM 2585 C C . GLY A 1 332 ? 14.590 -21.022 17.312 1.00 17.79 ? 420 GLY A C 1 ATOM 2586 O O . GLY A 1 332 ? 15.052 -22.042 17.836 1.00 19.65 ? 420 GLY A O 1 ATOM 2587 N N . LEU A 1 333 ? 15.342 -19.946 17.108 1.00 18.34 ? 421 LEU A N 1 ATOM 2588 C CA . LEU A 1 333 ? 16.735 -19.915 17.497 1.00 17.52 ? 421 LEU A CA 1 ATOM 2589 C C . LEU A 1 333 ? 16.869 -19.823 19.020 1.00 19.04 ? 421 LEU A C 1 ATOM 2590 O O . LEU A 1 333 ? 15.954 -19.439 19.728 1.00 18.34 ? 421 LEU A O 1 ATOM 2591 C CB . LEU A 1 333 ? 17.459 -18.745 16.792 1.00 17.91 ? 421 LEU A CB 1 ATOM 2592 C CG . LEU A 1 333 ? 17.525 -18.829 15.263 1.00 19.41 ? 421 LEU A CG 1 ATOM 2593 C CD1 . LEU A 1 333 ? 18.095 -17.542 14.699 1.00 20.75 ? 421 LEU A CD1 1 ATOM 2594 C CD2 . LEU A 1 333 ? 18.352 -19.993 14.794 1.00 20.46 ? 421 LEU A CD2 1 ATOM 2595 N N . GLU A 1 334 ? 18.067 -20.140 19.508 1.00 19.98 ? 422 GLU A N 1 ATOM 2596 C CA . GLU A 1 334 ? 18.393 -20.108 20.930 1.00 21.69 ? 422 GLU A CA 1 ATOM 2597 C C . GLU A 1 334 ? 18.215 -18.738 21.598 1.00 21.34 ? 422 GLU A C 1 ATOM 2598 O O . GLU A 1 334 ? 17.988 -18.645 22.794 1.00 23.08 ? 422 GLU A O 1 ATOM 2599 C CB . GLU A 1 334 ? 19.856 -20.574 21.102 1.00 22.98 ? 422 GLU A CB 1 ATOM 2600 C CG . GLU A 1 334 ? 20.219 -20.989 22.501 1.00 25.07 ? 422 GLU A CG 1 ATOM 2601 C CD . GLU A 1 334 ? 21.668 -21.441 22.687 0.50 26.12 ? 422 GLU A CD 1 ATOM 2602 O OE1 . GLU A 1 334 ? 22.335 -21.854 21.709 0.50 25.01 ? 422 GLU A OE1 1 ATOM 2603 O OE2 . GLU A 1 334 ? 22.142 -21.398 23.850 0.50 27.93 ? 422 GLU A OE2 1 ATOM 2604 N N . ASP A 1 335 ? 18.340 -17.665 20.813 1.00 19.86 ? 423 ASP A N 1 ATOM 2605 C CA . ASP A 1 335 ? 18.233 -16.299 21.318 1.00 19.55 ? 423 ASP A CA 1 ATOM 2606 C C . ASP A 1 335 ? 16.872 -15.657 20.974 1.00 17.60 ? 423 ASP A C 1 ATOM 2607 O O . ASP A 1 335 ? 16.718 -14.441 21.016 1.00 17.74 ? 423 ASP A O 1 ATOM 2608 C CB . ASP A 1 335 ? 19.409 -15.443 20.804 1.00 20.47 ? 423 ASP A CB 1 ATOM 2609 C CG . ASP A 1 335 ? 19.421 -15.325 19.299 1.00 22.02 ? 423 ASP A CG 1 ATOM 2610 O OD1 . ASP A 1 335 ? 18.469 -15.848 18.651 1.00 25.95 ? 423 ASP A OD1 1 ATOM 2611 O OD2 . ASP A 1 335 ? 20.317 -14.699 18.662 1.00 21.39 ? 423 ASP A OD2 1 ATOM 2612 N N . ALA A 1 336 ? 15.879 -16.489 20.668 1.00 16.32 ? 424 ALA A N 1 ATOM 2613 C CA . ALA A 1 336 ? 14.499 -16.067 20.521 1.00 15.88 ? 424 ALA A CA 1 ATOM 2614 C C . ALA A 1 336 ? 13.733 -16.619 21.708 1.00 15.24 ? 424 ALA A C 1 ATOM 2615 O O . ALA A 1 336 ? 13.873 -17.822 22.074 1.00 17.54 ? 424 ALA A O 1 ATOM 2616 C CB . ALA A 1 336 ? 13.928 -16.624 19.271 1.00 15.67 ? 424 ALA A CB 1 ATOM 2617 N N . LEU A 1 337 ? 12.943 -15.781 22.335 1.00 14.68 ? 425 LEU A N 1 ATOM 2618 C CA . LEU A 1 337 ? 12.133 -16.196 23.479 1.00 14.90 ? 425 LEU A CA 1 ATOM 2619 C C . LEU A 1 337 ? 11.015 -17.129 23.054 1.00 16.78 ? 425 LEU A C 1 ATOM 2620 O O . LEU A 1 337 ? 10.282 -16.862 22.115 1.00 16.36 ? 425 LEU A O 1 ATOM 2621 C CB . LEU A 1 337 ? 11.568 -14.992 24.186 1.00 14.74 ? 425 LEU A CB 1 ATOM 2622 C CG . LEU A 1 337 ? 10.966 -15.219 25.575 1.00 14.13 ? 425 LEU A CG 1 ATOM 2623 C CD1 . LEU A 1 337 ? 12.044 -15.668 26.567 1.00 16.77 ? 425 LEU A CD1 1 ATOM 2624 C CD2 . LEU A 1 337 ? 10.301 -14.010 26.085 1.00 14.16 ? 425 LEU A CD2 1 ATOM 2625 N N . LYS A 1 338 ? 10.884 -18.250 23.782 1.00 19.55 ? 426 LYS A N 1 ATOM 2626 C CA . LYS A 1 338 ? 10.049 -19.385 23.395 1.00 22.06 ? 426 LYS A CA 1 ATOM 2627 C C . LYS A 1 338 ? 9.326 -19.888 24.635 1.00 23.34 ? 426 LYS A C 1 ATOM 2628 O O . LYS A 1 338 ? 9.953 -19.933 25.688 1.00 24.00 ? 426 LYS A O 1 ATOM 2629 C CB . LYS A 1 338 ? 10.967 -20.496 22.924 1.00 23.39 ? 426 LYS A CB 1 ATOM 2630 C CG . LYS A 1 338 ? 10.947 -20.790 21.474 1.00 26.67 ? 426 LYS A CG 1 ATOM 2631 C CD . LYS A 1 338 ? 12.235 -20.492 20.769 1.00 26.40 ? 426 LYS A CD 1 ATOM 2632 C CE . LYS A 1 338 ? 13.297 -21.527 20.971 1.00 28.45 ? 426 LYS A CE 1 ATOM 2633 N NZ . LYS A 1 338 ? 14.438 -20.940 21.710 1.00 30.61 ? 426 LYS A NZ 1 ATOM 2634 N N . PRO A 1 339 ? 8.081 -20.345 24.552 1.00 23.64 ? 427 PRO A N 1 ATOM 2635 C CA . PRO A 1 339 ? 7.281 -20.434 23.328 1.00 23.54 ? 427 PRO A CA 1 ATOM 2636 C C . PRO A 1 339 ? 6.622 -19.109 23.028 1.00 22.50 ? 427 PRO A C 1 ATOM 2637 O O . PRO A 1 339 ? 6.205 -18.357 23.913 1.00 24.24 ? 427 PRO A O 1 ATOM 2638 C CB . PRO A 1 339 ? 6.232 -21.501 23.700 1.00 23.75 ? 427 PRO A CB 1 ATOM 2639 C CG . PRO A 1 339 ? 6.001 -21.265 25.188 1.00 25.03 ? 427 PRO A CG 1 ATOM 2640 C CD . PRO A 1 339 ? 7.369 -20.930 25.710 1.00 24.32 ? 427 PRO A CD 1 ATOM 2641 N N . ALA A 1 340 ? 6.525 -18.820 21.730 1.00 20.39 ? 428 ALA A N 1 ATOM 2642 C CA . ALA A 1 340 ? 6.008 -17.550 21.243 1.00 18.76 ? 428 ALA A CA 1 ATOM 2643 C C . ALA A 1 340 ? 4.725 -17.797 20.441 1.00 17.92 ? 428 ALA A C 1 ATOM 2644 O O . ALA A 1 340 ? 4.710 -18.763 19.688 1.00 17.41 ? 428 ALA A O 1 ATOM 2645 C CB . ALA A 1 340 ? 7.054 -16.924 20.347 1.00 18.49 ? 428 ALA A CB 1 ATOM 2646 N N . PRO A 1 341 ? 3.705 -16.949 20.605 1.00 18.11 ? 429 PRO A N 1 ATOM 2647 C CA . PRO A 1 341 ? 2.431 -17.152 19.884 1.00 19.90 ? 429 PRO A CA 1 ATOM 2648 C C . PRO A 1 341 ? 2.519 -16.680 18.415 1.00 21.06 ? 429 PRO A C 1 ATOM 2649 O O . PRO A 1 341 ? 3.611 -16.370 17.912 1.00 21.19 ? 429 PRO A O 1 ATOM 2650 C CB . PRO A 1 341 ? 1.448 -16.315 20.705 1.00 19.80 ? 429 PRO A CB 1 ATOM 2651 C CG . PRO A 1 341 ? 2.246 -15.167 21.185 1.00 18.96 ? 429 PRO A CG 1 ATOM 2652 C CD . PRO A 1 341 ? 3.618 -15.756 21.467 1.00 19.08 ? 429 PRO A CD 1 ATOM 2653 N N . GLU A 1 342 ? 1.394 -16.638 17.716 1.00 21.16 ? 430 GLU A N 1 ATOM 2654 C CA . GLU A 1 342 ? 1.437 -16.198 16.319 1.00 20.57 ? 430 GLU A CA 1 ATOM 2655 C C . GLU A 1 342 ? 1.833 -14.721 16.236 1.00 18.69 ? 430 GLU A C 1 ATOM 2656 O O . GLU A 1 342 ? 1.622 -13.963 17.162 1.00 17.16 ? 430 GLU A O 1 ATOM 2657 C CB . GLU A 1 342 ? 0.110 -16.475 15.596 1.00 21.41 ? 430 GLU A CB 1 ATOM 2658 C CG . GLU A 1 342 ? -0.047 -17.937 15.121 1.00 25.87 ? 430 GLU A CG 1 ATOM 2659 C CD . GLU A 1 342 ? 0.639 -18.289 13.786 1.00 30.01 ? 430 GLU A CD 1 ATOM 2660 O OE1 . GLU A 1 342 ? 1.161 -17.394 13.085 1.00 30.41 ? 430 GLU A OE1 1 ATOM 2661 O OE2 . GLU A 1 342 ? 0.658 -19.488 13.405 1.00 32.53 ? 430 GLU A OE2 1 ATOM 2662 N N . ALA A 1 343 ? 2.412 -14.340 15.096 1.00 17.44 ? 431 ALA A N 1 ATOM 2663 C CA . ALA A 1 343 ? 2.785 -12.930 14.850 1.00 16.21 ? 431 ALA A CA 1 ATOM 2664 C C . ALA A 1 343 ? 1.658 -11.967 15.186 1.00 16.21 ? 431 ALA A C 1 ATOM 2665 O O . ALA A 1 343 ? 0.494 -12.186 14.785 1.00 17.17 ? 431 ALA A O 1 ATOM 2666 C CB . ALA A 1 343 ? 3.174 -12.761 13.393 1.00 16.26 ? 431 ALA A CB 1 ATOM 2667 N N . GLY A 1 344 ? 1.974 -10.916 15.912 1.00 15.91 ? 432 GLY A N 1 ATOM 2668 C CA . GLY A 1 344 ? 1.011 -9.896 16.288 1.00 16.52 ? 432 GLY A CA 1 ATOM 2669 C C . GLY A 1 344 ? 0.226 -10.185 17.550 1.00 17.73 ? 432 GLY A C 1 ATOM 2670 O O . GLY A 1 344 ? -0.282 -9.270 18.169 1.00 19.67 ? 432 GLY A O 1 ATOM 2671 N N . GLN A 1 345 ? 0.170 -11.458 17.948 1.00 17.81 ? 433 GLN A N 1 ATOM 2672 C CA . GLN A 1 345 ? -0.538 -11.832 19.168 1.00 19.32 ? 433 GLN A CA 1 ATOM 2673 C C . GLN A 1 345 ? 0.253 -11.410 20.399 1.00 17.48 ? 433 GLN A C 1 ATOM 2674 O O . GLN A 1 345 ? 1.459 -11.266 20.343 1.00 17.12 ? 433 GLN A O 1 ATOM 2675 C CB . GLN A 1 345 ? -0.800 -13.331 19.209 1.00 20.73 ? 433 GLN A CB 1 ATOM 2676 C CG . GLN A 1 345 ? -1.801 -13.843 18.148 1.00 24.38 ? 433 GLN A CG 1 ATOM 2677 C CD . GLN A 1 345 ? -3.143 -13.134 18.195 1.00 29.74 ? 433 GLN A CD 1 ATOM 2678 O OE1 . GLN A 1 345 ? -3.858 -13.205 19.197 1.00 32.77 ? 433 GLN A OE1 1 ATOM 2679 N NE2 . GLN A 1 345 ? -3.481 -12.437 17.118 1.00 31.90 ? 433 GLN A NE2 1 ATOM 2680 N N . TRP A 1 346 ? -0.421 -11.167 21.499 1.00 18.31 ? 434 TRP A N 1 ATOM 2681 C CA . TRP A 1 346 ? 0.267 -10.691 22.688 1.00 17.83 ? 434 TRP A CA 1 ATOM 2682 C C . TRP A 1 346 ? 1.163 -11.800 23.254 1.00 18.55 ? 434 TRP A C 1 ATOM 2683 O O . TRP A 1 346 ? 0.762 -12.968 23.315 1.00 18.69 ? 434 TRP A O 1 ATOM 2684 C CB . TRP A 1 346 ? -0.711 -10.218 23.749 1.00 18.03 ? 434 TRP A CB 1 ATOM 2685 C CG . TRP A 1 346 ? -0.055 -9.431 24.859 1.00 18.07 ? 434 TRP A CG 1 ATOM 2686 C CD1 . TRP A 1 346 ? 0.101 -9.839 26.194 1.00 18.05 ? 434 TRP A CD1 1 ATOM 2687 C CD2 . TRP A 1 346 ? 0.514 -8.121 24.787 1.00 18.58 ? 434 TRP A CD2 1 ATOM 2688 N NE1 . TRP A 1 346 ? 0.722 -8.851 26.902 1.00 19.19 ? 434 TRP A NE1 1 ATOM 2689 C CE2 . TRP A 1 346 ? 1.008 -7.791 26.073 1.00 17.12 ? 434 TRP A CE2 1 ATOM 2690 C CE3 . TRP A 1 346 ? 0.709 -7.197 23.753 1.00 17.86 ? 434 TRP A CE3 1 ATOM 2691 C CZ2 . TRP A 1 346 ? 1.619 -6.571 26.352 1.00 19.13 ? 434 TRP A CZ2 1 ATOM 2692 C CZ3 . TRP A 1 346 ? 1.322 -5.998 24.035 1.00 18.73 ? 434 TRP A CZ3 1 ATOM 2693 C CH2 . TRP A 1 346 ? 1.762 -5.684 25.316 1.00 18.37 ? 434 TRP A CH2 1 ATOM 2694 N N . PHE A 1 347 ? 2.400 -11.409 23.579 1.00 18.20 ? 435 PHE A N 1 ATOM 2695 C CA . PHE A 1 347 ? 3.423 -12.343 24.089 1.00 17.64 ? 435 PHE A CA 1 ATOM 2696 C C . PHE A 1 347 ? 3.834 -11.757 25.437 1.00 17.40 ? 435 PHE A C 1 ATOM 2697 O O . PHE A 1 347 ? 4.739 -10.951 25.545 1.00 16.28 ? 435 PHE A O 1 ATOM 2698 C CB . PHE A 1 347 ? 4.586 -12.387 23.084 1.00 17.65 ? 435 PHE A CB 1 ATOM 2699 C CG . PHE A 1 347 ? 5.632 -13.453 23.315 1.00 17.15 ? 435 PHE A CG 1 ATOM 2700 C CD1 . PHE A 1 347 ? 5.608 -14.350 24.393 1.00 17.54 ? 435 PHE A CD1 1 ATOM 2701 C CD2 . PHE A 1 347 ? 6.702 -13.532 22.416 1.00 17.36 ? 435 PHE A CD2 1 ATOM 2702 C CE1 . PHE A 1 347 ? 6.599 -15.289 24.511 1.00 19.81 ? 435 PHE A CE1 1 ATOM 2703 C CE2 . PHE A 1 347 ? 7.687 -14.464 22.546 1.00 18.53 ? 435 PHE A CE2 1 ATOM 2704 C CZ . PHE A 1 347 ? 7.625 -15.368 23.604 1.00 18.36 ? 435 PHE A CZ 1 ATOM 2705 N N . ASN A 1 348 ? 3.127 -12.150 26.502 1.00 17.27 ? 436 ASN A N 1 ATOM 2706 C CA . ASN A 1 348 ? 3.240 -11.453 27.754 1.00 17.39 ? 436 ASN A CA 1 ATOM 2707 C C . ASN A 1 348 ? 4.642 -11.589 28.387 1.00 14.89 ? 436 ASN A C 1 ATOM 2708 O O . ASN A 1 348 ? 5.147 -10.666 28.997 1.00 16.22 ? 436 ASN A O 1 ATOM 2709 C CB . ASN A 1 348 ? 2.181 -11.921 28.769 1.00 18.00 ? 436 ASN A CB 1 ATOM 2710 C CG . ASN A 1 348 ? 2.003 -10.939 29.827 1.00 21.19 ? 436 ASN A CG 1 ATOM 2711 O OD1 . ASN A 1 348 ? 1.728 -9.761 29.585 1.00 22.01 ? 436 ASN A OD1 1 ATOM 2712 N ND2 . ASN A 1 348 ? 2.226 -11.386 31.077 1.00 22.72 ? 436 ASN A ND2 1 ATOM 2713 N N . GLU A 1 349 ? 5.227 -12.748 28.204 1.00 16.40 ? 437 GLU A N 1 ATOM 2714 C CA . GLU A 1 349 ? 6.556 -13.010 28.738 1.00 17.20 ? 437 GLU A CA 1 ATOM 2715 C C . GLU A 1 349 ? 7.581 -12.118 28.070 1.00 15.66 ? 437 GLU A C 1 ATOM 2716 O O . GLU A 1 349 ? 8.525 -11.660 28.705 1.00 16.36 ? 437 GLU A O 1 ATOM 2717 C CB . GLU A 1 349 ? 6.899 -14.446 28.488 1.00 18.15 ? 437 GLU A CB 1 ATOM 2718 C CG . GLU A 1 349 ? 5.959 -15.442 29.201 1.00 22.29 ? 437 GLU A CG 1 ATOM 2719 C CD . GLU A 1 349 ? 4.834 -16.006 28.303 1.00 28.61 ? 437 GLU A CD 1 ATOM 2720 O OE1 . GLU A 1 349 ? 4.236 -15.272 27.454 1.00 29.32 ? 437 GLU A OE1 1 ATOM 2721 O OE2 . GLU A 1 349 ? 4.515 -17.212 28.465 1.00 30.89 ? 437 GLU A OE2 1 ATOM 2722 N N . TYR A 1 350 ? 7.347 -11.794 26.785 1.00 14.68 ? 438 TYR A N 1 ATOM 2723 C CA . TYR A 1 350 ? 8.207 -10.845 26.085 1.00 13.67 ? 438 TYR A CA 1 ATOM 2724 C C . TYR A 1 350 ? 7.994 -9.426 26.598 1.00 12.97 ? 438 TYR A C 1 ATOM 2725 O O . TYR A 1 350 ? 8.938 -8.685 26.820 1.00 13.30 ? 438 TYR A O 1 ATOM 2726 C CB . TYR A 1 350 ? 7.992 -10.959 24.565 1.00 13.71 ? 438 TYR A CB 1 ATOM 2727 C CG . TYR A 1 350 ? 9.212 -10.415 23.841 1.00 12.25 ? 438 TYR A CG 1 ATOM 2728 C CD1 . TYR A 1 350 ? 10.270 -11.220 23.542 1.00 13.17 ? 438 TYR A CD1 1 ATOM 2729 C CD2 . TYR A 1 350 ? 9.294 -9.075 23.502 1.00 13.62 ? 438 TYR A CD2 1 ATOM 2730 C CE1 . TYR A 1 350 ? 11.444 -10.704 22.945 1.00 12.55 ? 438 TYR A CE1 1 ATOM 2731 C CE2 . TYR A 1 350 ? 10.480 -8.556 22.904 1.00 13.01 ? 438 TYR A CE2 1 ATOM 2732 C CZ . TYR A 1 350 ? 11.516 -9.375 22.620 1.00 13.02 ? 438 TYR A CZ 1 ATOM 2733 O OH . TYR A 1 350 ? 12.673 -8.842 22.050 1.00 13.81 ? 438 TYR A OH 1 ATOM 2734 N N . PHE A 1 351 ? 6.731 -9.015 26.819 1.00 12.34 ? 439 PHE A N 1 ATOM 2735 C CA . PHE A 1 351 ? 6.440 -7.697 27.374 1.00 13.92 ? 439 PHE A CA 1 ATOM 2736 C C . PHE A 1 351 ? 7.160 -7.516 28.701 1.00 13.66 ? 439 PHE A C 1 ATOM 2737 O O . PHE A 1 351 ? 7.686 -6.456 29.006 1.00 13.20 ? 439 PHE A O 1 ATOM 2738 C CB . PHE A 1 351 ? 4.926 -7.508 27.590 1.00 14.30 ? 439 PHE A CB 1 ATOM 2739 C CG . PHE A 1 351 ? 4.547 -6.212 28.196 1.00 15.23 ? 439 PHE A CG 1 ATOM 2740 C CD1 . PHE A 1 351 ? 4.488 -5.066 27.416 1.00 16.17 ? 439 PHE A CD1 1 ATOM 2741 C CD2 . PHE A 1 351 ? 4.211 -6.109 29.563 1.00 17.76 ? 439 PHE A CD2 1 ATOM 2742 C CE1 . PHE A 1 351 ? 4.142 -3.879 27.946 1.00 15.69 ? 439 PHE A CE1 1 ATOM 2743 C CE2 . PHE A 1 351 ? 3.880 -4.925 30.108 1.00 19.86 ? 439 PHE A CE2 1 ATOM 2744 C CZ . PHE A 1 351 ? 3.815 -3.806 29.352 1.00 19.28 ? 439 PHE A CZ 1 ATOM 2745 N N . ILE A 1 352 ? 7.051 -8.539 29.551 1.00 15.41 ? 440 ILE A N 1 ATOM 2746 C CA . ILE A 1 352 ? 7.655 -8.453 30.888 1.00 16.27 ? 440 ILE A CA 1 ATOM 2747 C C . ILE A 1 352 ? 9.191 -8.350 30.789 1.00 14.85 ? 440 ILE A C 1 ATOM 2748 O O . ILE A 1 352 ? 9.757 -7.519 31.492 1.00 16.04 ? 440 ILE A O 1 ATOM 2749 C CB . ILE A 1 352 ? 7.168 -9.633 31.765 1.00 17.29 ? 440 ILE A CB 1 ATOM 2750 C CG1 . ILE A 1 352 ? 5.728 -9.373 32.234 1.00 20.00 ? 440 ILE A CG1 1 ATOM 2751 C CG2 . ILE A 1 352 ? 8.135 -9.954 32.945 1.00 17.56 ? 440 ILE A CG2 1 ATOM 2752 C CD1 . ILE A 1 352 ? 4.961 -10.661 32.407 1.00 24.46 ? 440 ILE A CD1 1 ATOM 2753 N N . GLN A 1 353 ? 9.799 -9.126 29.883 1.00 14.80 ? 441 GLN A N 1 ATOM 2754 C CA . GLN A 1 353 ? 11.238 -8.946 29.558 1.00 14.80 ? 441 GLN A CA 1 ATOM 2755 C C . GLN A 1 353 ? 11.566 -7.495 29.219 1.00 14.72 ? 441 GLN A C 1 ATOM 2756 O O . GLN A 1 353 ? 12.457 -6.892 29.759 1.00 14.30 ? 441 GLN A O 1 ATOM 2757 C CB . GLN A 1 353 ? 11.650 -9.852 28.410 1.00 15.14 ? 441 GLN A CB 1 ATOM 2758 C CG . GLN A 1 353 ? 13.136 -9.721 27.976 1.00 15.37 ? 441 GLN A CG 1 ATOM 2759 C CD . GLN A 1 353 ? 13.440 -10.482 26.724 1.00 15.61 ? 441 GLN A CD 1 ATOM 2760 O OE1 . GLN A 1 353 ? 13.472 -11.704 26.694 1.00 17.70 ? 441 GLN A OE1 1 ATOM 2761 N NE2 . GLN A 1 353 ? 13.644 -9.730 25.632 1.00 15.99 ? 441 GLN A NE2 1 ATOM 2762 N N . LEU A 1 354 ? 10.799 -6.912 28.290 1.00 13.64 ? 442 LEU A N 1 ATOM 2763 C CA . LEU A 1 354 ? 11.035 -5.527 27.901 1.00 13.33 ? 442 LEU A CA 1 ATOM 2764 C C . LEU A 1 354 ? 10.855 -4.515 29.037 1.00 13.90 ? 442 LEU A C 1 ATOM 2765 O O . LEU A 1 354 ? 11.578 -3.500 29.168 1.00 13.83 ? 442 LEU A O 1 ATOM 2766 C CB . LEU A 1 354 ? 10.090 -5.172 26.733 1.00 13.43 ? 442 LEU A CB 1 ATOM 2767 C CG . LEU A 1 354 ? 10.384 -5.796 25.373 1.00 12.72 ? 442 LEU A CG 1 ATOM 2768 C CD1 . LEU A 1 354 ? 9.200 -5.435 24.485 1.00 13.04 ? 442 LEU A CD1 1 ATOM 2769 C CD2 . LEU A 1 354 ? 11.662 -5.265 24.769 1.00 11.40 ? 442 LEU A CD2 1 ATOM 2770 N N . LEU A 1 355 ? 9.837 -4.780 29.873 1.00 14.43 ? 443 LEU A N 1 ATOM 2771 C CA . LEU A 1 355 ? 9.564 -3.887 31.002 1.00 17.53 ? 443 LEU A CA 1 ATOM 2772 C C . LEU A 1 355 ? 10.679 -3.927 32.062 1.00 16.30 ? 443 LEU A C 1 ATOM 2773 O O . LEU A 1 355 ? 11.179 -2.894 32.483 1.00 17.24 ? 443 LEU A O 1 ATOM 2774 C CB . LEU A 1 355 ? 8.234 -4.283 31.633 1.00 18.99 ? 443 LEU A CB 1 ATOM 2775 C CG . LEU A 1 355 ? 7.494 -3.275 32.455 1.00 23.12 ? 443 LEU A CG 1 ATOM 2776 C CD1 . LEU A 1 355 ? 6.910 -2.266 31.533 1.00 25.22 ? 443 LEU A CD1 1 ATOM 2777 C CD2 . LEU A 1 355 ? 6.360 -3.983 33.227 1.00 25.21 ? 443 LEU A CD2 1 ATOM 2778 N N . ARG A 1 356 ? 11.080 -5.142 32.390 1.00 17.07 ? 444 ARG A N 1 ATOM 2779 C CA . ARG A 1 356 ? 12.175 -5.372 33.362 1.00 17.36 ? 444 ARG A CA 1 ATOM 2780 C C . ARG A 1 356 ? 13.472 -4.748 32.887 1.00 17.06 ? 444 ARG A C 1 ATOM 2781 O O . ARG A 1 356 ? 14.196 -4.149 33.661 1.00 17.58 ? 444 ARG A O 1 ATOM 2782 C CB . ARG A 1 356 ? 12.390 -6.864 33.567 1.00 18.21 ? 444 ARG A CB 1 ATOM 2783 C CG . ARG A 1 356 ? 11.227 -7.599 34.291 1.00 21.27 ? 444 ARG A CG 1 ATOM 2784 C CD . ARG A 1 356 ? 11.519 -9.048 34.536 1.00 26.20 ? 444 ARG A CD 1 ATOM 2785 N NE . ARG A 1 356 ? 12.570 -9.121 35.545 1.00 30.44 ? 444 ARG A NE 1 ATOM 2786 C CZ . ARG A 1 356 ? 13.305 -10.186 35.810 1.00 33.55 ? 444 ARG A CZ 1 ATOM 2787 N NH1 . ARG A 1 356 ? 13.137 -11.322 35.139 1.00 35.42 ? 444 ARG A NH1 1 ATOM 2788 N NH2 . ARG A 1 356 ? 14.224 -10.112 36.765 1.00 34.39 ? 444 ARG A NH2 1 ATOM 2789 N N . ASN A 1 357 ? 13.716 -4.809 31.571 1.00 14.93 ? 445 ASN A N 1 ATOM 2790 C CA . ASN A 1 357 ? 14.962 -4.305 30.996 1.00 14.82 ? 445 ASN A CA 1 ATOM 2791 C C . ASN A 1 357 ? 14.858 -2.876 30.470 1.00 14.51 ? 445 ASN A C 1 ATOM 2792 O O . ASN A 1 357 ? 15.776 -2.361 29.866 1.00 14.03 ? 445 ASN A O 1 ATOM 2793 C CB . ASN A 1 357 ? 15.426 -5.243 29.877 1.00 14.53 ? 445 ASN A CB 1 ATOM 2794 C CG . ASN A 1 357 ? 15.864 -6.579 30.383 1.00 15.46 ? 445 ASN A CG 1 ATOM 2795 O OD1 . ASN A 1 357 ? 16.358 -6.701 31.525 1.00 18.25 ? 445 ASN A OD1 1 ATOM 2796 N ND2 . ASN A 1 357 ? 15.736 -7.598 29.567 1.00 14.70 ? 445 ASN A ND2 1 ATOM 2797 N N . ALA A 1 358 ? 13.779 -2.178 30.759 1.00 14.92 ? 446 ALA A N 1 ATOM 2798 C CA . ALA A 1 358 ? 13.622 -0.839 30.199 1.00 15.38 ? 446 ALA A CA 1 ATOM 2799 C C . ALA A 1 358 ? 14.717 0.141 30.582 1.00 15.94 ? 446 ALA A C 1 ATOM 2800 O O . ALA A 1 358 ? 15.122 0.200 31.749 1.00 17.29 ? 446 ALA A O 1 ATOM 2801 C CB . ALA A 1 358 ? 12.298 -0.265 30.614 1.00 16.07 ? 446 ALA A CB 1 ATOM 2802 N N . ASN A 1 359 ? 15.171 0.940 29.640 1.00 16.55 ? 447 ASN A N 1 ATOM 2803 C CA . ASN A 1 359 ? 16.181 1.956 29.864 1.00 17.67 ? 447 ASN A CA 1 ATOM 2804 C C . ASN A 1 359 ? 15.961 3.092 28.907 1.00 18.40 ? 447 ASN A C 1 ATOM 2805 O O . ASN A 1 359 ? 16.047 2.866 27.687 1.00 18.27 ? 447 ASN A O 1 ATOM 2806 C CB . ASN A 1 359 ? 17.572 1.384 29.646 1.00 18.55 ? 447 ASN A CB 1 ATOM 2807 C CG . ASN A 1 359 ? 18.666 2.423 29.828 1.00 22.03 ? 447 ASN A CG 1 ATOM 2808 O OD1 . ASN A 1 359 ? 18.608 3.260 30.731 1.00 25.75 ? 447 ASN A OD1 1 ATOM 2809 N ND2 . ASN A 1 359 ? 19.679 2.378 28.957 1.00 25.55 ? 447 ASN A ND2 1 ATOM 2810 N N . PRO A 1 360 ? 15.664 4.296 29.371 1.00 19.85 ? 448 PRO A N 1 ATOM 2811 C CA . PRO A 1 360 ? 15.492 4.655 30.796 1.00 20.97 ? 448 PRO A CA 1 ATOM 2812 C C . PRO A 1 360 ? 14.369 3.889 31.462 1.00 22.35 ? 448 PRO A C 1 ATOM 2813 O O . PRO A 1 360 ? 13.436 3.409 30.863 1.00 21.41 ? 448 PRO A O 1 ATOM 2814 C CB . PRO A 1 360 ? 15.116 6.130 30.752 1.00 21.80 ? 448 PRO A CB 1 ATOM 2815 C CG . PRO A 1 360 ? 15.502 6.628 29.379 1.00 22.53 ? 448 PRO A CG 1 ATOM 2816 C CD . PRO A 1 360 ? 15.516 5.453 28.478 1.00 20.72 ? 448 PRO A CD 1 ATOM 2817 N N . PRO A 1 361 ? 14.453 3.760 32.768 1.00 23.46 ? 449 PRO A N 1 ATOM 2818 C CA . PRO A 1 361 ? 13.414 3.009 33.465 1.00 24.05 ? 449 PRO A CA 1 ATOM 2819 C C . PRO A 1 361 ? 12.077 3.759 33.424 1.00 23.88 ? 449 PRO A C 1 ATOM 2820 O O . PRO A 1 361 ? 12.058 4.978 33.263 1.00 24.36 ? 449 PRO A O 1 ATOM 2821 C CB . PRO A 1 361 ? 13.977 2.867 34.881 1.00 24.47 ? 449 PRO A CB 1 ATOM 2822 C CG . PRO A 1 361 ? 15.019 3.892 35.014 1.00 25.04 ? 449 PRO A CG 1 ATOM 2823 C CD . PRO A 1 361 ? 15.520 4.254 33.657 1.00 24.32 ? 449 PRO A CD 1 ATOM 2824 N N . PHE A 1 362 ? 10.972 3.039 33.500 1.00 24.40 ? 450 PHE A N 1 ATOM 2825 C CA . PHE A 1 362 ? 9.683 3.695 33.650 1.00 25.68 ? 450 PHE A CA 1 ATOM 2826 C C . PHE A 1 362 ? 9.429 4.019 35.117 0.50 25.63 ? 450 PHE A C 1 ATOM 2827 O O . PHE A 1 362 ? 10.283 3.741 35.962 0.50 25.62 ? 450 PHE A O 1 ATOM 2828 C CB . PHE A 1 362 ? 8.583 2.832 33.042 1.00 26.16 ? 450 PHE A CB 1 ATOM 2829 C CG . PHE A 1 362 ? 8.508 2.963 31.542 1.00 27.12 ? 450 PHE A CG 1 ATOM 2830 C CD1 . PHE A 1 362 ? 7.771 4.005 30.967 1.00 28.12 ? 450 PHE A CD1 1 ATOM 2831 C CD2 . PHE A 1 362 ? 9.208 2.096 30.706 1.00 28.24 ? 450 PHE A CD2 1 ATOM 2832 C CE1 . PHE A 1 362 ? 7.710 4.168 29.587 1.00 27.00 ? 450 PHE A CE1 1 ATOM 2833 C CE2 . PHE A 1 362 ? 9.140 2.248 29.321 1.00 27.99 ? 450 PHE A CE2 1 ATOM 2834 C CZ . PHE A 1 362 ? 8.395 3.291 28.761 1.00 27.27 ? 450 PHE A CZ 1 ATOM 2835 O OXT . PHE A 1 362 ? 8.388 4.581 35.453 0.50 26.55 ? 450 PHE A OXT 1 HETATM 2836 C C1 . NAG B 2 . ? -8.165 -5.716 -0.319 1.00 9.47 ? 500 NAG A C1 1 HETATM 2837 C C2 . NAG B 2 . ? -8.802 -6.691 -1.313 1.00 10.05 ? 500 NAG A C2 1 HETATM 2838 C C3 . NAG B 2 . ? -9.921 -6.029 -2.087 1.00 11.23 ? 500 NAG A C3 1 HETATM 2839 C C4 . NAG B 2 . ? -10.896 -5.308 -1.173 1.00 12.49 ? 500 NAG A C4 1 HETATM 2840 C C5 . NAG B 2 . ? -10.111 -4.361 -0.260 1.00 11.18 ? 500 NAG A C5 1 HETATM 2841 C C6 . NAG B 2 . ? -10.980 -3.608 0.718 1.00 11.71 ? 500 NAG A C6 1 HETATM 2842 C C7 . NAG B 2 . ? -7.595 -8.463 -2.481 1.00 12.01 ? 500 NAG A C7 1 HETATM 2843 C C8 . NAG B 2 . ? -6.556 -8.785 -3.510 1.00 10.45 ? 500 NAG A C8 1 HETATM 2844 N N2 . NAG B 2 . ? -7.783 -7.169 -2.214 1.00 9.34 ? 500 NAG A N2 1 HETATM 2845 O O3 . NAG B 2 . ? -10.630 -7.004 -2.839 1.00 14.37 ? 500 NAG A O3 1 HETATM 2846 O O4 . NAG B 2 . ? -11.777 -4.557 -2.000 1.00 15.59 ? 500 NAG A O4 1 HETATM 2847 O O5 . NAG B 2 . ? -9.177 -5.123 0.482 1.00 9.94 ? 500 NAG A O5 1 HETATM 2848 O O6 . NAG B 2 . ? -10.176 -2.674 1.443 1.00 11.68 ? 500 NAG A O6 1 HETATM 2849 O O7 . NAG B 2 . ? -8.293 -9.340 -2.004 1.00 17.08 ? 500 NAG A O7 1 HETATM 2850 C C2 . BGC C 3 . ? 1.760 -8.591 13.022 1.00 13.50 ? 501 BGC A C2 1 HETATM 2851 C C3 . BGC C 3 . ? 0.690 -7.524 13.148 1.00 13.01 ? 501 BGC A C3 1 HETATM 2852 C C4 . BGC C 3 . ? 0.978 -6.503 14.232 1.00 13.52 ? 501 BGC A C4 1 HETATM 2853 C C5 . BGC C 3 . ? 2.385 -5.956 14.029 1.00 12.83 ? 501 BGC A C5 1 HETATM 2854 C C6 . BGC C 3 . ? 2.744 -4.978 15.141 1.00 12.03 ? 501 BGC A C6 1 HETATM 2855 C C1 . BGC C 3 . ? 3.127 -7.948 12.941 1.00 13.00 ? 501 BGC A C1 1 HETATM 2856 O O2 . BGC C 3 . ? 1.547 -9.325 11.839 1.00 14.34 ? 501 BGC A O2 1 HETATM 2857 O O3 . BGC C 3 . ? -0.587 -8.133 13.339 1.00 15.95 ? 501 BGC A O3 1 HETATM 2858 O O4 . BGC C 3 . ? 0.041 -5.454 14.177 1.00 15.34 ? 501 BGC A O4 1 HETATM 2859 O O5 . BGC C 3 . ? 3.331 -7.023 13.997 1.00 12.56 ? 501 BGC A O5 1 HETATM 2860 O O6 . BGC C 3 . ? 2.956 -5.745 16.340 1.00 14.44 ? 501 BGC A O6 1 HETATM 2861 C C1 . SSG D 4 . ? 8.378 -8.298 11.048 1.00 16.21 ? 502 SSG A C1 1 HETATM 2862 C C2 . SSG D 4 . ? 8.352 -8.009 12.503 1.00 16.34 ? 502 SSG A C2 1 HETATM 2863 O O2 . SSG D 4 . ? 9.546 -8.380 13.126 1.00 17.57 ? 502 SSG A O2 1 HETATM 2864 C C3 . SSG D 4 . ? 7.104 -8.474 13.161 1.00 15.78 ? 502 SSG A C3 1 HETATM 2865 O O3 . SSG D 4 . ? 7.041 -7.951 14.431 1.00 14.27 ? 502 SSG A O3 1 HETATM 2866 C C4 . SSG D 4 . ? 5.832 -8.395 12.349 1.00 13.68 ? 502 SSG A C4 1 HETATM 2867 C C5 . SSG D 4 . ? 5.988 -8.771 10.908 1.00 16.51 ? 502 SSG A C5 1 HETATM 2868 O O5 . SSG D 4 . ? 7.169 -8.307 10.308 1.00 17.81 ? 502 SSG A O5 1 HETATM 2869 C C6 . SSG D 4 . ? 4.797 -8.587 9.996 1.00 18.63 ? 502 SSG A C6 1 HETATM 2870 O O6 . SSG D 4 . ? 4.361 -7.256 10.103 1.00 22.90 ? 502 SSG A O6 1 HETATM 2871 S S4 . SSG D 4 . ? 4.430 -9.147 13.154 1.00 13.48 ? 502 SSG A S4 1 HETATM 2872 C C1 . SSG E 4 . ? 13.236 -9.512 8.632 1.00 16.02 ? 503 SSG A C1 1 HETATM 2873 C C2 . SSG E 4 . ? 11.929 -10.203 8.410 1.00 18.41 ? 503 SSG A C2 1 HETATM 2874 O O2 . SSG E 4 . ? 11.915 -10.775 7.119 1.00 20.17 ? 503 SSG A O2 1 HETATM 2875 C C3 . SSG E 4 . ? 10.709 -9.419 8.757 1.00 21.88 ? 503 SSG A C3 1 HETATM 2876 O O3 . SSG E 4 . ? 9.642 -10.340 8.837 1.00 27.65 ? 503 SSG A O3 1 HETATM 2877 C C4 . SSG E 4 . ? 10.906 -8.441 9.896 1.00 19.25 ? 503 SSG A C4 1 HETATM 2878 C C5 . SSG E 4 . ? 12.249 -7.757 9.998 1.00 17.52 ? 503 SSG A C5 1 HETATM 2879 O O5 . SSG E 4 . ? 13.308 -8.600 9.667 1.00 15.78 ? 503 SSG A O5 1 HETATM 2880 C C6 . SSG E 4 . ? 12.596 -6.926 11.226 1.00 19.78 ? 503 SSG A C6 1 HETATM 2881 O O6 . SSG E 4 . ? 12.147 -7.583 12.386 1.00 20.05 ? 503 SSG A O6 1 HETATM 2882 S S4 . SSG E 4 . ? 9.522 -7.354 10.037 1.00 19.07 ? 503 SSG A S4 1 HETATM 2883 C C1 . SGC F 5 . ? 18.806 -8.431 8.174 1.00 11.27 ? 504 SGC A C1 1 HETATM 2884 C C2 . SGC F 5 . ? 17.965 -7.906 9.263 1.00 11.21 ? 504 SGC A C2 1 HETATM 2885 O O2 . SGC F 5 . ? 18.658 -7.683 10.455 1.00 12.44 ? 504 SGC A O2 1 HETATM 2886 C C3 . SGC F 5 . ? 16.666 -8.614 9.398 1.00 12.47 ? 504 SGC A C3 1 HETATM 2887 O O3 . SGC F 5 . ? 15.825 -7.905 10.271 1.00 13.88 ? 504 SGC A O3 1 HETATM 2888 C C4 . SGC F 5 . ? 16.007 -9.051 8.083 1.00 11.19 ? 504 SGC A C4 1 HETATM 2889 C C5 . SGC F 5 . ? 16.955 -9.447 6.970 1.00 11.36 ? 504 SGC A C5 1 HETATM 2890 O O5 . SGC F 5 . ? 18.174 -8.719 6.959 1.00 12.38 ? 504 SGC A O5 1 HETATM 2891 C C6 . SGC F 5 . ? 16.332 -9.438 5.597 1.00 13.49 ? 504 SGC A C6 1 HETATM 2892 O O6 . SGC F 5 . ? 17.314 -9.957 4.688 1.00 17.11 ? 504 SGC A O6 1 HETATM 2893 S S4 . SGC F 5 . ? 14.788 -10.328 8.353 1.00 13.69 ? 504 SGC A S4 1 HETATM 2894 C C1 . MA3 G 6 . ? 23.798 -8.843 5.455 1.00 12.99 ? 505 MA3 A C1 1 HETATM 2895 C C2 . MA3 G 6 . ? 22.483 -9.173 4.825 1.00 12.01 ? 505 MA3 A C2 1 HETATM 2896 C C3 . MA3 G 6 . ? 21.290 -8.594 5.556 1.00 11.81 ? 505 MA3 A C3 1 HETATM 2897 C C4 . MA3 G 6 . ? 21.410 -8.641 7.071 1.00 12.24 ? 505 MA3 A C4 1 HETATM 2898 C C5 . MA3 G 6 . ? 22.817 -8.466 7.653 1.00 13.79 ? 505 MA3 A C5 1 HETATM 2899 C C6 . MA3 G 6 . ? 23.002 -8.796 9.137 1.00 17.13 ? 505 MA3 A C6 1 HETATM 2900 C C7 . MA3 G 6 . ? 25.084 -6.799 5.600 1.00 13.62 ? 505 MA3 A C7 1 HETATM 2901 O O1 . MA3 G 6 . ? 23.813 -7.384 5.245 1.00 14.09 ? 505 MA3 A O1 1 HETATM 2902 O O2 . MA3 G 6 . ? 22.458 -8.974 3.423 1.00 13.51 ? 505 MA3 A O2 1 HETATM 2903 O O3 . MA3 G 6 . ? 20.072 -9.161 5.074 1.00 13.61 ? 505 MA3 A O3 1 HETATM 2904 S S4 . MA3 G 6 . ? 20.303 -7.558 7.949 1.00 12.33 ? 505 MA3 A S4 1 HETATM 2905 O O5 . MA3 G 6 . ? 23.864 -8.977 6.825 1.00 13.36 ? 505 MA3 A O5 1 HETATM 2906 O O6 . MA3 G 6 . ? 24.097 -8.093 9.734 1.00 23.26 ? 505 MA3 A O6 1 HETATM 2907 MG MG . MG H 7 . ? 28.939 14.334 16.951 1.00 23.40 ? 506 MG A MG 1 HETATM 2908 C C . ACY I 8 . ? 3.547 11.985 22.524 1.00 17.33 ? 507 ACY A C 1 HETATM 2909 O O . ACY I 8 . ? 2.311 12.175 22.399 1.00 18.68 ? 507 ACY A O 1 HETATM 2910 O OXT . ACY I 8 . ? 4.081 11.278 23.469 1.00 18.47 ? 507 ACY A OXT 1 HETATM 2911 C CH3 . ACY I 8 . ? 4.421 12.670 21.527 1.00 19.71 ? 507 ACY A CH3 1 HETATM 2912 O O . HOH J 9 . ? 9.054 23.809 6.649 1.00 29.43 ? 2001 HOH A O 1 HETATM 2913 O O . HOH J 9 . ? 7.295 18.956 6.798 1.00 27.91 ? 2002 HOH A O 1 HETATM 2914 O O . HOH J 9 . ? 5.812 20.735 11.790 1.00 25.89 ? 2003 HOH A O 1 HETATM 2915 O O . HOH J 9 . ? 5.533 14.728 19.025 1.00 25.07 ? 2004 HOH A O 1 HETATM 2916 O O . HOH J 9 . ? 10.004 21.751 12.634 1.00 29.80 ? 2005 HOH A O 1 HETATM 2917 O O . HOH J 9 . ? 12.876 19.483 15.389 1.00 40.31 ? 2006 HOH A O 1 HETATM 2918 O O . HOH J 9 . ? -0.851 20.628 15.668 1.00 31.92 ? 2007 HOH A O 1 HETATM 2919 O O . HOH J 9 . ? 1.609 23.009 18.620 1.00 37.06 ? 2008 HOH A O 1 HETATM 2920 O O . HOH J 9 . ? 6.401 19.782 19.622 1.00 32.27 ? 2009 HOH A O 1 HETATM 2921 O O . HOH J 9 . ? -0.268 9.443 23.730 0.50 23.86 ? 2010 HOH A O 1 HETATM 2922 O O . HOH J 9 . ? 0.199 7.507 16.696 1.00 22.93 ? 2011 HOH A O 1 HETATM 2923 O O . HOH J 9 . ? -0.854 4.568 17.957 1.00 25.02 ? 2012 HOH A O 1 HETATM 2924 O O A HOH J 9 . ? -3.228 9.129 23.122 0.50 19.14 ? 2013 HOH A O 1 HETATM 2925 O O B HOH J 9 . ? -5.162 8.295 23.642 0.50 28.10 ? 2013 HOH A O 1 HETATM 2926 O O . HOH J 9 . ? -1.136 2.597 23.447 1.00 20.95 ? 2014 HOH A O 1 HETATM 2927 O O A HOH J 9 . ? -5.864 -5.103 34.587 0.50 21.37 ? 2016 HOH A O 1 HETATM 2928 O O B HOH J 9 . ? -5.737 -3.298 35.039 0.50 22.96 ? 2016 HOH A O 1 HETATM 2929 O O A HOH J 9 . ? -6.216 -12.491 36.640 0.50 22.12 ? 2017 HOH A O 1 HETATM 2930 O O B HOH J 9 . ? -5.027 -11.863 37.448 0.50 21.22 ? 2017 HOH A O 1 HETATM 2931 O O . HOH J 9 . ? 5.807 -9.981 37.848 1.00 27.01 ? 2018 HOH A O 1 HETATM 2932 O O . HOH J 9 . ? 5.511 -8.255 45.189 1.00 40.14 ? 2019 HOH A O 1 HETATM 2933 O O . HOH J 9 . ? 9.558 -8.784 40.510 1.00 33.41 ? 2020 HOH A O 1 HETATM 2934 O O . HOH J 9 . ? 1.595 -0.796 41.399 1.00 29.07 ? 2021 HOH A O 1 HETATM 2935 O O . HOH J 9 . ? 7.553 -2.086 44.454 1.00 33.94 ? 2022 HOH A O 1 HETATM 2936 O O . HOH J 9 . ? -3.381 -2.937 39.261 1.00 20.56 ? 2023 HOH A O 1 HETATM 2937 O O . HOH J 9 . ? -0.066 23.250 14.137 1.00 25.06 ? 2024 HOH A O 1 HETATM 2938 O O . HOH J 9 . ? 4.099 19.561 21.113 1.00 39.30 ? 2025 HOH A O 1 HETATM 2939 O O . HOH J 9 . ? 0.415 0.229 39.354 1.00 33.25 ? 2026 HOH A O 1 HETATM 2940 O O . HOH J 9 . ? -2.285 3.405 31.215 1.00 27.19 ? 2027 HOH A O 1 HETATM 2941 O O . HOH J 9 . ? 3.724 7.011 29.569 1.00 31.96 ? 2028 HOH A O 1 HETATM 2942 O O . HOH J 9 . ? -6.636 10.129 25.326 1.00 36.94 ? 2029 HOH A O 1 HETATM 2943 O O . HOH J 9 . ? 3.473 8.485 27.042 1.00 24.85 ? 2030 HOH A O 1 HETATM 2944 O O A HOH J 9 . ? 0.202 10.113 25.351 0.50 14.74 ? 2031 HOH A O 1 HETATM 2945 O O B HOH J 9 . ? 1.912 9.736 25.301 0.50 15.65 ? 2031 HOH A O 1 HETATM 2946 O O . HOH J 9 . ? 6.326 6.152 18.090 1.00 11.30 ? 2034 HOH A O 1 HETATM 2947 O O . HOH J 9 . ? 8.287 -10.372 36.416 1.00 34.28 ? 2035 HOH A O 1 HETATM 2948 O O . HOH J 9 . ? 7.113 -10.831 46.426 1.00 34.69 ? 2036 HOH A O 1 HETATM 2949 O O . HOH J 9 . ? 0.652 0.027 18.344 1.00 17.56 ? 2037 HOH A O 1 HETATM 2950 O O . HOH J 9 . ? 3.322 1.312 22.605 1.00 19.41 ? 2038 HOH A O 1 HETATM 2951 O O . HOH J 9 . ? 0.352 3.163 21.261 1.00 21.39 ? 2039 HOH A O 1 HETATM 2952 O O . HOH J 9 . ? 1.936 1.533 42.592 1.00 29.35 ? 2040 HOH A O 1 HETATM 2953 O O A HOH J 9 . ? 0.028 -2.286 43.056 0.50 25.99 ? 2041 HOH A O 1 HETATM 2954 O O B HOH J 9 . ? -1.629 -2.316 42.260 0.50 21.85 ? 2041 HOH A O 1 HETATM 2955 O O . HOH J 9 . ? 9.634 -0.875 44.844 1.00 34.51 ? 2042 HOH A O 1 HETATM 2956 O O . HOH J 9 . ? -0.008 2.732 38.843 1.00 36.81 ? 2044 HOH A O 1 HETATM 2957 O O . HOH J 9 . ? -2.786 -1.747 16.552 1.00 22.96 ? 2045 HOH A O 1 HETATM 2958 O O . HOH J 9 . ? -1.984 -4.684 12.451 1.00 13.96 ? 2046 HOH A O 1 HETATM 2959 O O . HOH J 9 . ? -0.866 -2.558 14.499 1.00 17.65 ? 2047 HOH A O 1 HETATM 2960 O O . HOH J 9 . ? 9.355 -12.524 35.334 1.00 37.67 ? 2048 HOH A O 1 HETATM 2961 O O . HOH J 9 . ? 2.195 -9.805 8.034 1.00 16.51 ? 2049 HOH A O 1 HETATM 2962 O O . HOH J 9 . ? 0.176 -9.697 4.123 1.00 18.19 ? 2050 HOH A O 1 HETATM 2963 O O . HOH J 9 . ? -2.015 -7.400 11.012 1.00 27.15 ? 2051 HOH A O 1 HETATM 2964 O O . HOH J 9 . ? -4.301 -5.687 13.411 1.00 26.91 ? 2052 HOH A O 1 HETATM 2965 O O . HOH J 9 . ? -4.631 -3.634 16.287 1.00 35.37 ? 2053 HOH A O 1 HETATM 2966 O O A HOH J 9 . ? -9.771 -9.172 1.669 0.50 20.15 ? 2054 HOH A O 1 HETATM 2967 O O B HOH J 9 . ? -7.333 -9.110 1.340 0.50 12.53 ? 2054 HOH A O 1 HETATM 2968 O O . HOH J 9 . ? -11.610 -5.232 4.583 1.00 17.29 ? 2055 HOH A O 1 HETATM 2969 O O . HOH J 9 . ? -10.850 -11.306 2.916 1.00 33.91 ? 2056 HOH A O 1 HETATM 2970 O O . HOH J 9 . ? -11.044 -7.527 2.993 1.00 39.55 ? 2057 HOH A O 1 HETATM 2971 O O . HOH J 9 . ? -11.409 -9.553 9.406 1.00 32.81 ? 2058 HOH A O 1 HETATM 2972 O O . HOH J 9 . ? -7.465 -2.202 0.428 1.00 10.40 ? 2060 HOH A O 1 HETATM 2973 O O . HOH J 9 . ? -9.376 -3.628 3.934 1.00 9.40 ? 2061 HOH A O 1 HETATM 2974 O O . HOH J 9 . ? -13.486 -5.604 6.933 1.00 20.13 ? 2062 HOH A O 1 HETATM 2975 O O . HOH J 9 . ? -14.378 -5.264 0.980 1.00 22.75 ? 2063 HOH A O 1 HETATM 2976 O O . HOH J 9 . ? -12.047 -0.682 -2.353 1.00 31.14 ? 2064 HOH A O 1 HETATM 2977 O O . HOH J 9 . ? -9.556 -8.486 10.860 1.00 35.24 ? 2065 HOH A O 1 HETATM 2978 O O . HOH J 9 . ? -14.454 -2.921 7.272 1.00 12.85 ? 2066 HOH A O 1 HETATM 2979 O O . HOH J 9 . ? -13.209 -0.757 0.087 1.00 21.82 ? 2067 HOH A O 1 HETATM 2980 O O . HOH J 9 . ? -13.564 -3.760 3.099 1.00 14.08 ? 2068 HOH A O 1 HETATM 2981 O O . HOH J 9 . ? 2.607 -5.572 -14.049 1.00 35.00 ? 2069 HOH A O 1 HETATM 2982 O O A HOH J 9 . ? 15.615 -19.590 1.603 0.50 18.64 ? 2070 HOH A O 1 HETATM 2983 O O B HOH J 9 . ? 16.030 -17.499 0.483 0.50 24.84 ? 2070 HOH A O 1 HETATM 2984 O O . HOH J 9 . ? -8.676 -6.017 11.153 1.00 25.24 ? 2071 HOH A O 1 HETATM 2985 O O . HOH J 9 . ? -18.978 15.895 18.086 1.00 33.75 ? 2072 HOH A O 1 HETATM 2986 O O . HOH J 9 . ? -12.378 20.866 15.516 0.50 23.09 ? 2073 HOH A O 1 HETATM 2987 O O . HOH J 9 . ? -9.845 -3.821 -5.785 1.00 23.69 ? 2074 HOH A O 1 HETATM 2988 O O . HOH J 9 . ? -9.396 -3.357 13.709 1.00 34.48 ? 2075 HOH A O 1 HETATM 2989 O O . HOH J 9 . ? -1.035 26.644 23.900 1.00 33.43 ? 2076 HOH A O 1 HETATM 2990 O O . HOH J 9 . ? -4.356 22.658 13.680 1.00 37.68 ? 2077 HOH A O 1 HETATM 2991 O O . HOH J 9 . ? -13.430 -2.741 16.322 1.00 29.07 ? 2078 HOH A O 1 HETATM 2992 O O . HOH J 9 . ? -14.412 10.541 14.351 1.00 22.42 ? 2079 HOH A O 1 HETATM 2993 O O . HOH J 9 . ? -16.039 9.194 15.865 1.00 32.25 ? 2080 HOH A O 1 HETATM 2994 O O . HOH J 9 . ? -14.251 6.796 16.686 1.00 31.46 ? 2081 HOH A O 1 HETATM 2995 O O . HOH J 9 . ? -11.280 9.107 20.619 1.00 21.79 ? 2082 HOH A O 1 HETATM 2996 O O . HOH J 9 . ? -6.908 3.780 18.829 1.00 26.14 ? 2083 HOH A O 1 HETATM 2997 O O . HOH J 9 . ? -13.508 3.565 17.991 1.00 31.15 ? 2084 HOH A O 1 HETATM 2998 O O . HOH J 9 . ? 18.163 -17.778 4.216 1.00 31.95 ? 2086 HOH A O 1 HETATM 2999 O O . HOH J 9 . ? 10.192 -23.672 2.887 1.00 24.55 ? 2087 HOH A O 1 HETATM 3000 O O . HOH J 9 . ? -14.845 9.987 11.819 1.00 29.31 ? 2088 HOH A O 1 HETATM 3001 O O . HOH J 9 . ? -13.986 16.473 9.768 1.00 35.38 ? 2089 HOH A O 1 HETATM 3002 O O . HOH J 9 . ? -7.381 -11.261 5.343 1.00 25.20 ? 2090 HOH A O 1 HETATM 3003 O O . HOH J 9 . ? -7.241 -13.182 3.150 1.00 24.97 ? 2091 HOH A O 1 HETATM 3004 O O . HOH J 9 . ? -3.257 -14.613 3.204 1.00 19.65 ? 2092 HOH A O 1 HETATM 3005 O O A HOH J 9 . ? 29.787 -7.417 5.828 0.50 28.64 ? 2093 HOH A O 1 HETATM 3006 O O B HOH J 9 . ? 30.002 -6.785 4.730 0.50 23.84 ? 2093 HOH A O 1 HETATM 3007 O O . HOH J 9 . ? -15.170 14.763 19.671 1.00 24.32 ? 2094 HOH A O 1 HETATM 3008 O O . HOH J 9 . ? -16.543 6.681 21.364 1.00 31.28 ? 2095 HOH A O 1 HETATM 3009 O O . HOH J 9 . ? -18.600 13.070 18.610 1.00 32.98 ? 2096 HOH A O 1 HETATM 3010 O O . HOH J 9 . ? 3.580 -8.237 -12.654 1.00 22.44 ? 2097 HOH A O 1 HETATM 3011 O O . HOH J 9 . ? -9.408 15.080 23.532 1.00 27.02 ? 2098 HOH A O 1 HETATM 3012 O O . HOH J 9 . ? 0.246 -6.148 -13.493 1.00 28.53 ? 2099 HOH A O 1 HETATM 3013 O O . HOH J 9 . ? -8.287 15.720 13.674 1.00 16.48 ? 2100 HOH A O 1 HETATM 3014 O O . HOH J 9 . ? -7.692 -5.509 -5.583 1.00 17.41 ? 2101 HOH A O 1 HETATM 3015 O O . HOH J 9 . ? -18.348 15.499 15.139 1.00 39.21 ? 2102 HOH A O 1 HETATM 3016 O O . HOH J 9 . ? -16.407 14.792 17.303 1.00 25.95 ? 2103 HOH A O 1 HETATM 3017 O O . HOH J 9 . ? -15.620 12.787 15.107 1.00 32.48 ? 2104 HOH A O 1 HETATM 3018 O O . HOH J 9 . ? -13.822 21.099 17.753 1.00 34.32 ? 2105 HOH A O 1 HETATM 3019 O O . HOH J 9 . ? -9.730 -1.977 -3.648 1.00 19.85 ? 2106 HOH A O 1 HETATM 3020 O O . HOH J 9 . ? 28.252 -9.002 7.067 1.00 37.91 ? 2107 HOH A O 1 HETATM 3021 O O . HOH J 9 . ? -9.677 -2.298 -7.858 1.00 36.36 ? 2108 HOH A O 1 HETATM 3022 O O . HOH J 9 . ? -7.636 19.539 26.327 1.00 35.66 ? 2109 HOH A O 1 HETATM 3023 O O . HOH J 9 . ? -12.721 12.193 0.786 1.00 27.41 ? 2110 HOH A O 1 HETATM 3024 O O . HOH J 9 . ? 0.206 24.701 24.708 1.00 39.04 ? 2111 HOH A O 1 HETATM 3025 O O A HOH J 9 . ? -5.968 20.733 12.332 0.50 17.18 ? 2112 HOH A O 1 HETATM 3026 O O B HOH J 9 . ? -7.129 19.170 12.132 0.50 18.43 ? 2112 HOH A O 1 HETATM 3027 O O . HOH J 9 . ? -7.435 20.298 9.694 1.00 16.47 ? 2113 HOH A O 1 HETATM 3028 O O . HOH J 9 . ? -11.773 17.442 7.223 1.00 30.38 ? 2114 HOH A O 1 HETATM 3029 O O . HOH J 9 . ? -11.884 19.463 10.773 1.00 32.40 ? 2115 HOH A O 1 HETATM 3030 O O . HOH J 9 . ? -2.260 21.498 17.613 1.00 26.26 ? 2116 HOH A O 1 HETATM 3031 O O . HOH J 9 . ? -5.536 18.207 13.630 0.40 16.04 ? 2117 HOH A O 1 HETATM 3032 O O . HOH J 9 . ? 4.648 23.704 15.227 1.00 35.99 ? 2118 HOH A O 1 HETATM 3033 O O . HOH J 9 . ? -2.262 10.411 25.280 1.00 32.51 ? 2119 HOH A O 1 HETATM 3034 O O . HOH J 9 . ? -3.498 15.948 13.438 1.00 12.50 ? 2120 HOH A O 1 HETATM 3035 O O . HOH J 9 . ? -6.689 14.719 24.936 1.00 40.12 ? 2121 HOH A O 1 HETATM 3036 O O . HOH J 9 . ? -1.262 5.208 15.027 1.00 16.48 ? 2122 HOH A O 1 HETATM 3037 O O . HOH J 9 . ? 20.512 -15.295 2.422 1.00 24.34 ? 2123 HOH A O 1 HETATM 3038 O O . HOH J 9 . ? 11.748 -17.768 -0.808 1.00 33.99 ? 2124 HOH A O 1 HETATM 3039 O O . HOH J 9 . ? 11.942 -7.752 -12.983 1.00 22.52 ? 2125 HOH A O 1 HETATM 3040 O O . HOH J 9 . ? 2.204 -9.219 0.197 1.00 9.88 ? 2126 HOH A O 1 HETATM 3041 O O . HOH J 9 . ? 10.653 -12.281 -7.189 1.00 15.57 ? 2127 HOH A O 1 HETATM 3042 O O . HOH J 9 . ? 5.853 -14.474 -3.216 1.00 17.79 ? 2128 HOH A O 1 HETATM 3043 O O . HOH J 9 . ? 7.370 3.584 -12.368 1.00 34.10 ? 2129 HOH A O 1 HETATM 3044 O O . HOH J 9 . ? 3.945 5.858 -10.449 1.00 21.12 ? 2130 HOH A O 1 HETATM 3045 O O . HOH J 9 . ? 6.636 -13.347 -0.071 1.00 21.81 ? 2131 HOH A O 1 HETATM 3046 O O . HOH J 9 . ? -6.406 5.624 -8.735 1.00 38.12 ? 2132 HOH A O 1 HETATM 3047 O O . HOH J 9 . ? 10.000 -14.556 0.963 1.00 29.65 ? 2133 HOH A O 1 HETATM 3048 O O . HOH J 9 . ? 13.964 -16.028 -0.691 1.00 26.01 ? 2134 HOH A O 1 HETATM 3049 O O . HOH J 9 . ? -5.902 15.668 0.967 1.00 22.45 ? 2135 HOH A O 1 HETATM 3050 O O . HOH J 9 . ? 7.286 16.333 6.253 1.00 25.50 ? 2136 HOH A O 1 HETATM 3051 O O . HOH J 9 . ? 17.816 -16.142 1.932 1.00 26.71 ? 2137 HOH A O 1 HETATM 3052 O O . HOH J 9 . ? 16.114 -16.165 6.261 1.00 26.44 ? 2138 HOH A O 1 HETATM 3053 O O . HOH J 9 . ? 9.628 -17.437 1.245 1.00 34.26 ? 2139 HOH A O 1 HETATM 3054 O O . HOH J 9 . ? 9.856 -21.236 4.376 1.00 28.70 ? 2140 HOH A O 1 HETATM 3055 O O A HOH J 9 . ? 12.945 -16.324 7.556 0.50 17.24 ? 2141 HOH A O 1 HETATM 3056 O O B HOH J 9 . ? 13.302 -16.930 9.426 0.50 11.90 ? 2141 HOH A O 1 HETATM 3057 O O . HOH J 9 . ? 4.822 -17.668 1.702 1.00 25.10 ? 2142 HOH A O 1 HETATM 3058 O O . HOH J 9 . ? 2.370 -17.316 5.460 1.00 32.41 ? 2143 HOH A O 1 HETATM 3059 O O . HOH J 9 . ? 7.260 -18.038 2.954 1.00 24.41 ? 2144 HOH A O 1 HETATM 3060 O O . HOH J 9 . ? 5.092 -18.218 5.714 1.00 33.55 ? 2145 HOH A O 1 HETATM 3061 O O . HOH J 9 . ? 0.273 -10.956 6.474 1.00 30.67 ? 2146 HOH A O 1 HETATM 3062 O O . HOH J 9 . ? 6.571 -16.271 8.222 1.00 28.48 ? 2147 HOH A O 1 HETATM 3063 O O . HOH J 9 . ? 6.664 -11.478 6.742 1.00 17.20 ? 2148 HOH A O 1 HETATM 3064 O O A HOH J 9 . ? 30.799 6.144 2.567 0.50 26.60 ? 2149 HOH A O 1 HETATM 3065 O O B HOH J 9 . ? 31.915 5.077 1.301 0.50 24.08 ? 2149 HOH A O 1 HETATM 3066 O O . HOH J 9 . ? 4.398 -15.153 1.991 1.00 26.70 ? 2150 HOH A O 1 HETATM 3067 O O . HOH J 9 . ? -3.187 -12.410 5.190 1.00 35.68 ? 2152 HOH A O 1 HETATM 3068 O O . HOH J 9 . ? -5.905 -9.346 4.160 1.00 13.58 ? 2153 HOH A O 1 HETATM 3069 O O . HOH J 9 . ? -4.830 -12.518 2.062 1.00 18.30 ? 2154 HOH A O 1 HETATM 3070 O O . HOH J 9 . ? 4.366 -11.754 -0.235 1.00 14.41 ? 2155 HOH A O 1 HETATM 3071 O O . HOH J 9 . ? -5.673 -10.953 -0.373 1.00 16.91 ? 2156 HOH A O 1 HETATM 3072 O O . HOH J 9 . ? 19.897 3.559 -8.487 1.00 32.87 ? 2157 HOH A O 1 HETATM 3073 O O . HOH J 9 . ? 1.857 -8.821 -10.581 1.00 10.66 ? 2158 HOH A O 1 HETATM 3074 O O . HOH J 9 . ? 2.289 -14.972 -13.818 1.00 23.29 ? 2159 HOH A O 1 HETATM 3075 O O . HOH J 9 . ? -4.914 -13.878 -8.571 1.00 26.41 ? 2160 HOH A O 1 HETATM 3076 O O . HOH J 9 . ? -0.977 -11.770 -5.187 1.00 10.43 ? 2161 HOH A O 1 HETATM 3077 O O . HOH J 9 . ? -7.225 -10.865 -12.285 1.00 35.55 ? 2162 HOH A O 1 HETATM 3078 O O . HOH J 9 . ? -0.646 -7.660 -11.277 1.00 11.22 ? 2163 HOH A O 1 HETATM 3079 O O . HOH J 9 . ? 0.622 -11.963 -12.041 1.00 11.42 ? 2164 HOH A O 1 HETATM 3080 O O . HOH J 9 . ? 9.162 19.995 -1.539 1.00 31.69 ? 2165 HOH A O 1 HETATM 3081 O O A HOH J 9 . ? 15.763 20.201 8.320 0.50 20.91 ? 2166 HOH A O 1 HETATM 3082 O O B HOH J 9 . ? 14.591 19.148 7.212 0.50 17.95 ? 2166 HOH A O 1 HETATM 3083 O O . HOH J 9 . ? 14.531 22.247 6.244 1.00 32.74 ? 2167 HOH A O 1 HETATM 3084 O O . HOH J 9 . ? 16.240 20.183 10.547 0.50 21.94 ? 2168 HOH A O 1 HETATM 3085 O O . HOH J 9 . ? -5.062 -2.236 -9.357 1.00 21.03 ? 2169 HOH A O 1 HETATM 3086 O O A HOH J 9 . ? -4.793 -12.313 -6.275 0.50 19.03 ? 2170 HOH A O 1 HETATM 3087 O O B HOH J 9 . ? -4.127 -12.658 -4.869 0.50 11.48 ? 2170 HOH A O 1 HETATM 3088 O O . HOH J 9 . ? -6.343 -10.333 -7.482 1.00 18.37 ? 2171 HOH A O 1 HETATM 3089 O O . HOH J 9 . ? -6.157 -4.990 -3.266 1.00 10.66 ? 2172 HOH A O 1 HETATM 3090 O O . HOH J 9 . ? -6.295 -6.486 -7.769 1.00 20.25 ? 2173 HOH A O 1 HETATM 3091 O O . HOH J 9 . ? 5.614 0.860 -1.581 1.00 30.69 ? 2175 HOH A O 1 HETATM 3092 O O . HOH J 9 . ? 3.617 2.052 -11.938 1.00 30.64 ? 2176 HOH A O 1 HETATM 3093 O O . HOH J 9 . ? -0.441 3.304 -12.640 1.00 36.32 ? 2177 HOH A O 1 HETATM 3094 O O . HOH J 9 . ? -8.579 0.479 -4.489 1.00 14.06 ? 2178 HOH A O 1 HETATM 3095 O O . HOH J 9 . ? -7.506 -2.742 -2.240 1.00 11.80 ? 2179 HOH A O 1 HETATM 3096 O O . HOH J 9 . ? 31.496 -9.426 8.921 1.00 34.90 ? 2180 HOH A O 1 HETATM 3097 O O . HOH J 9 . ? -4.544 1.086 -9.919 1.00 32.85 ? 2181 HOH A O 1 HETATM 3098 O O . HOH J 9 . ? -7.123 6.516 -4.660 1.00 13.50 ? 2182 HOH A O 1 HETATM 3099 O O . HOH J 9 . ? -8.107 0.725 -7.171 1.00 19.49 ? 2183 HOH A O 1 HETATM 3100 O O A HOH J 9 . ? -14.967 6.783 8.343 0.50 19.07 ? 2184 HOH A O 1 HETATM 3101 O O B HOH J 9 . ? -15.677 6.132 10.666 0.50 15.18 ? 2184 HOH A O 1 HETATM 3102 O O . HOH J 9 . ? 30.395 9.930 9.736 1.00 25.74 ? 2186 HOH A O 1 HETATM 3103 O O . HOH J 9 . ? 31.554 9.199 7.309 1.00 21.17 ? 2187 HOH A O 1 HETATM 3104 O O . HOH J 9 . ? -7.752 9.104 -3.632 1.00 20.59 ? 2188 HOH A O 1 HETATM 3105 O O . HOH J 9 . ? -7.578 13.479 -4.598 1.00 21.99 ? 2189 HOH A O 1 HETATM 3106 O O . HOH J 9 . ? 29.267 15.464 1.342 1.00 30.76 ? 2190 HOH A O 1 HETATM 3107 O O . HOH J 9 . ? -9.109 4.957 -5.921 1.00 35.41 ? 2191 HOH A O 1 HETATM 3108 O O . HOH J 9 . ? -11.761 9.907 -0.154 1.00 20.67 ? 2192 HOH A O 1 HETATM 3109 O O . HOH J 9 . ? -9.728 2.818 -3.744 1.00 27.98 ? 2193 HOH A O 1 HETATM 3110 O O . HOH J 9 . ? 22.764 12.552 -8.391 1.00 38.73 ? 2194 HOH A O 1 HETATM 3111 O O . HOH J 9 . ? 17.406 21.067 2.413 1.00 34.72 ? 2195 HOH A O 1 HETATM 3112 O O . HOH J 9 . ? -13.846 10.764 7.043 1.00 20.57 ? 2196 HOH A O 1 HETATM 3113 O O . HOH J 9 . ? -13.011 6.845 5.010 1.00 32.05 ? 2197 HOH A O 1 HETATM 3114 O O . HOH J 9 . ? -5.159 10.831 7.178 1.00 9.24 ? 2198 HOH A O 1 HETATM 3115 O O . HOH J 9 . ? -8.935 18.657 6.636 1.00 16.84 ? 2199 HOH A O 1 HETATM 3116 O O . HOH J 9 . ? -5.799 19.569 7.558 1.00 10.12 ? 2200 HOH A O 1 HETATM 3117 O O . HOH J 9 . ? -10.860 15.298 4.699 1.00 23.72 ? 2201 HOH A O 1 HETATM 3118 O O . HOH J 9 . ? -11.749 17.588 12.382 1.00 28.28 ? 2202 HOH A O 1 HETATM 3119 O O . HOH J 9 . ? 25.108 -13.052 24.766 1.00 34.24 ? 2204 HOH A O 1 HETATM 3120 O O . HOH J 9 . ? 3.445 21.778 13.335 1.00 24.46 ? 2205 HOH A O 1 HETATM 3121 O O . HOH J 9 . ? 16.418 -13.441 7.287 1.00 23.64 ? 2206 HOH A O 1 HETATM 3122 O O . HOH J 9 . ? 21.703 -10.502 27.708 1.00 31.54 ? 2207 HOH A O 1 HETATM 3123 O O . HOH J 9 . ? 10.346 1.980 1.240 1.00 14.28 ? 2208 HOH A O 1 HETATM 3124 O O . HOH J 9 . ? 15.896 9.055 26.792 1.00 32.71 ? 2209 HOH A O 1 HETATM 3125 O O . HOH J 9 . ? 5.926 8.615 26.127 1.00 26.72 ? 2210 HOH A O 1 HETATM 3126 O O . HOH J 9 . ? 8.029 -4.645 2.377 1.00 10.22 ? 2211 HOH A O 1 HETATM 3127 O O . HOH J 9 . ? 15.020 11.311 24.536 1.00 28.48 ? 2212 HOH A O 1 HETATM 3128 O O . HOH J 9 . ? 9.387 -6.645 1.279 1.00 12.36 ? 2213 HOH A O 1 HETATM 3129 O O . HOH J 9 . ? 14.084 -9.883 2.994 1.00 14.79 ? 2214 HOH A O 1 HETATM 3130 O O . HOH J 9 . ? 24.667 17.246 13.219 1.00 32.20 ? 2215 HOH A O 1 HETATM 3131 O O . HOH J 9 . ? 8.298 -14.251 9.069 1.00 25.81 ? 2216 HOH A O 1 HETATM 3132 O O . HOH J 9 . ? 22.542 -6.834 -3.612 1.00 20.94 ? 2217 HOH A O 1 HETATM 3133 O O . HOH J 9 . ? 25.812 -3.465 -3.120 1.00 26.35 ? 2218 HOH A O 1 HETATM 3134 O O . HOH J 9 . ? 22.443 -12.265 0.754 1.00 25.05 ? 2219 HOH A O 1 HETATM 3135 O O . HOH J 9 . ? -1.494 -21.727 9.568 1.00 24.42 ? 2220 HOH A O 1 HETATM 3136 O O . HOH J 9 . ? 22.228 -17.123 -4.001 1.00 25.47 ? 2221 HOH A O 1 HETATM 3137 O O . HOH J 9 . ? 22.191 -15.800 0.290 1.00 24.66 ? 2222 HOH A O 1 HETATM 3138 O O . HOH J 9 . ? 15.894 -14.297 -10.137 1.00 32.43 ? 2223 HOH A O 1 HETATM 3139 O O . HOH J 9 . ? 15.108 -17.159 -3.788 1.00 17.05 ? 2224 HOH A O 1 HETATM 3140 O O . HOH J 9 . ? 8.739 -17.738 -1.441 1.00 21.50 ? 2225 HOH A O 1 HETATM 3141 O O . HOH J 9 . ? 2.441 -19.926 22.762 1.00 36.73 ? 2226 HOH A O 1 HETATM 3142 O O . HOH J 9 . ? 18.498 -14.429 -11.377 1.00 40.17 ? 2227 HOH A O 1 HETATM 3143 O O . HOH J 9 . ? 13.894 -7.346 -10.967 1.00 12.19 ? 2228 HOH A O 1 HETATM 3144 O O . HOH J 9 . ? 19.950 -13.753 -7.867 1.00 26.88 ? 2229 HOH A O 1 HETATM 3145 O O . HOH J 9 . ? 10.394 -7.399 -10.431 1.00 12.18 ? 2230 HOH A O 1 HETATM 3146 O O . HOH J 9 . ? 14.882 -1.781 -13.378 1.00 31.27 ? 2232 HOH A O 1 HETATM 3147 O O . HOH J 9 . ? 11.445 -0.661 -11.887 1.00 26.84 ? 2233 HOH A O 1 HETATM 3148 O O A HOH J 9 . ? 6.115 -6.877 -12.114 0.50 16.39 ? 2234 HOH A O 1 HETATM 3149 O O B HOH J 9 . ? 6.629 -5.347 -11.982 0.50 21.38 ? 2234 HOH A O 1 HETATM 3150 O O . HOH J 9 . ? 18.990 5.881 26.710 1.00 32.06 ? 2236 HOH A O 1 HETATM 3151 O O . HOH J 9 . ? 10.445 5.970 -12.633 1.00 39.95 ? 2237 HOH A O 1 HETATM 3152 O O . HOH J 9 . ? 5.602 3.519 -10.499 1.00 18.79 ? 2238 HOH A O 1 HETATM 3153 O O . HOH J 9 . ? 9.473 0.260 -0.426 1.00 14.96 ? 2239 HOH A O 1 HETATM 3154 O O . HOH J 9 . ? 1.523 12.745 -6.796 1.00 25.65 ? 2240 HOH A O 1 HETATM 3155 O O . HOH J 9 . ? 1.259 7.125 -9.952 1.00 23.79 ? 2241 HOH A O 1 HETATM 3156 O O A HOH J 9 . ? -5.483 6.826 -6.629 0.50 15.32 ? 2242 HOH A O 1 HETATM 3157 O O B HOH J 9 . ? -4.316 6.202 -5.516 0.50 13.61 ? 2242 HOH A O 1 HETATM 3158 O O . HOH J 9 . ? 4.826 17.015 -3.998 1.00 14.29 ? 2244 HOH A O 1 HETATM 3159 O O . HOH J 9 . ? 3.793 13.156 -5.950 1.00 23.99 ? 2245 HOH A O 1 HETATM 3160 O O . HOH J 9 . ? -1.925 15.635 -3.047 1.00 29.38 ? 2246 HOH A O 1 HETATM 3161 O O . HOH J 9 . ? 1.765 16.667 -0.482 1.00 13.99 ? 2247 HOH A O 1 HETATM 3162 O O . HOH J 9 . ? -0.868 12.373 -4.349 1.00 15.21 ? 2248 HOH A O 1 HETATM 3163 O O . HOH J 9 . ? 1.892 20.046 3.363 1.00 9.19 ? 2249 HOH A O 1 HETATM 3164 O O . HOH J 9 . ? -4.459 17.008 2.807 1.00 14.01 ? 2250 HOH A O 1 HETATM 3165 O O . HOH J 9 . ? 4.775 16.361 5.598 1.00 14.59 ? 2251 HOH A O 1 HETATM 3166 O O . HOH J 9 . ? 14.348 -0.207 9.246 1.00 14.19 ? 2252 HOH A O 1 HETATM 3167 O O . HOH J 9 . ? 13.812 -1.657 3.157 1.00 9.47 ? 2253 HOH A O 1 HETATM 3168 O O . HOH J 9 . ? 12.671 0.519 1.712 1.00 12.81 ? 2254 HOH A O 1 HETATM 3169 O O . HOH J 9 . ? 13.788 -3.282 7.219 1.00 21.30 ? 2255 HOH A O 1 HETATM 3170 O O . HOH J 9 . ? 31.799 4.217 3.370 0.50 18.59 ? 2256 HOH A O 1 HETATM 3171 O O . HOH J 9 . ? 30.079 2.770 0.447 1.00 19.00 ? 2257 HOH A O 1 HETATM 3172 O O . HOH J 9 . ? 31.852 -2.720 4.779 1.00 14.05 ? 2258 HOH A O 1 HETATM 3173 O O . HOH J 9 . ? 30.829 0.083 -1.993 1.00 26.92 ? 2259 HOH A O 1 HETATM 3174 O O . HOH J 9 . ? 27.763 -3.222 -1.274 1.00 29.24 ? 2260 HOH A O 1 HETATM 3175 O O . HOH J 9 . ? 26.959 -6.536 2.833 1.00 32.02 ? 2261 HOH A O 1 HETATM 3176 O O . HOH J 9 . ? 22.772 1.245 -5.704 1.00 22.60 ? 2262 HOH A O 1 HETATM 3177 O O . HOH J 9 . ? 21.485 8.440 -6.846 1.00 25.02 ? 2263 HOH A O 1 HETATM 3178 O O . HOH J 9 . ? 17.174 3.699 -7.417 1.00 21.21 ? 2264 HOH A O 1 HETATM 3179 O O . HOH J 9 . ? 14.124 18.078 -1.843 1.00 31.88 ? 2265 HOH A O 1 HETATM 3180 O O . HOH J 9 . ? 10.496 15.843 -0.165 1.00 16.30 ? 2266 HOH A O 1 HETATM 3181 O O . HOH J 9 . ? 12.241 12.183 -12.720 1.00 38.20 ? 2267 HOH A O 1 HETATM 3182 O O . HOH J 9 . ? 13.069 14.608 -9.770 1.00 27.08 ? 2268 HOH A O 1 HETATM 3183 O O . HOH J 9 . ? 8.125 11.149 -11.345 1.00 34.86 ? 2269 HOH A O 1 HETATM 3184 O O . HOH J 9 . ? 5.938 13.671 -7.623 1.00 21.48 ? 2270 HOH A O 1 HETATM 3185 O O . HOH J 9 . ? 6.426 16.250 -6.746 1.00 30.78 ? 2271 HOH A O 1 HETATM 3186 O O . HOH J 9 . ? 18.759 14.975 -7.577 1.00 36.58 ? 2272 HOH A O 1 HETATM 3187 O O . HOH J 9 . ? 10.457 18.098 -2.615 1.00 39.75 ? 2273 HOH A O 1 HETATM 3188 O O . HOH J 9 . ? 9.640 17.866 1.192 1.00 33.74 ? 2274 HOH A O 1 HETATM 3189 O O . HOH J 9 . ? 8.309 16.055 3.943 1.00 20.90 ? 2275 HOH A O 1 HETATM 3190 O O . HOH J 9 . ? 6.238 20.463 3.500 1.00 19.67 ? 2276 HOH A O 1 HETATM 3191 O O . HOH J 9 . ? 13.598 16.029 4.081 1.00 25.98 ? 2277 HOH A O 1 HETATM 3192 O O . HOH J 9 . ? 10.434 18.092 4.201 1.00 26.87 ? 2278 HOH A O 1 HETATM 3193 O O . HOH J 9 . ? 13.264 20.271 10.743 1.00 24.91 ? 2279 HOH A O 1 HETATM 3194 O O . HOH J 9 . ? 15.303 -2.784 10.755 1.00 20.55 ? 2281 HOH A O 1 HETATM 3195 O O . HOH J 9 . ? 12.025 -3.928 9.342 1.00 22.62 ? 2282 HOH A O 1 HETATM 3196 O O . HOH J 9 . ? 18.868 -5.507 15.703 1.00 13.27 ? 2283 HOH A O 1 HETATM 3197 O O . HOH J 9 . ? 20.518 4.226 22.353 1.00 21.73 ? 2284 HOH A O 1 HETATM 3198 O O . HOH J 9 . ? 22.848 2.425 24.243 1.00 30.13 ? 2285 HOH A O 1 HETATM 3199 O O . HOH J 9 . ? 26.559 3.490 26.306 1.00 28.89 ? 2286 HOH A O 1 HETATM 3200 O O . HOH J 9 . ? 28.405 1.087 26.269 1.00 36.40 ? 2287 HOH A O 1 HETATM 3201 O O . HOH J 9 . ? 27.591 -2.448 23.991 1.00 26.36 ? 2288 HOH A O 1 HETATM 3202 O O . HOH J 9 . ? 26.623 -10.884 14.099 1.00 20.51 ? 2289 HOH A O 1 HETATM 3203 O O . HOH J 9 . ? 28.234 -8.568 12.543 1.00 25.82 ? 2290 HOH A O 1 HETATM 3204 O O . HOH J 9 . ? 30.616 -10.142 15.425 1.00 21.73 ? 2291 HOH A O 1 HETATM 3205 O O . HOH J 9 . ? 30.450 -9.734 11.492 1.00 27.67 ? 2292 HOH A O 1 HETATM 3206 O O . HOH J 9 . ? 35.958 -2.023 13.070 1.00 22.55 ? 2293 HOH A O 1 HETATM 3207 O O . HOH J 9 . ? 31.520 -3.222 15.786 1.00 13.01 ? 2294 HOH A O 1 HETATM 3208 O O . HOH J 9 . ? 33.308 3.571 15.031 1.00 32.25 ? 2295 HOH A O 1 HETATM 3209 O O . HOH J 9 . ? 31.329 4.783 7.093 1.00 21.09 ? 2296 HOH A O 1 HETATM 3210 O O . HOH J 9 . ? 23.426 -1.286 17.972 1.00 13.51 ? 2298 HOH A O 1 HETATM 3211 O O . HOH J 9 . ? 27.329 6.632 19.122 1.00 19.21 ? 2299 HOH A O 1 HETATM 3212 O O . HOH J 9 . ? 23.442 12.831 18.933 1.00 25.10 ? 2300 HOH A O 1 HETATM 3213 O O . HOH J 9 . ? 29.474 7.876 11.366 1.00 15.65 ? 2301 HOH A O 1 HETATM 3214 O O . HOH J 9 . ? 28.216 8.514 17.103 1.00 27.18 ? 2302 HOH A O 1 HETATM 3215 O O . HOH J 9 . ? 27.451 13.846 8.807 1.00 30.96 ? 2303 HOH A O 1 HETATM 3216 O O . HOH J 9 . ? 26.924 14.247 16.409 1.00 26.62 ? 2304 HOH A O 1 HETATM 3217 O O . HOH J 9 . ? 29.095 9.042 14.065 1.00 21.44 ? 2305 HOH A O 1 HETATM 3218 O O . HOH J 9 . ? 29.218 12.586 16.017 1.00 22.71 ? 2306 HOH A O 1 HETATM 3219 O O . HOH J 9 . ? 29.811 9.794 5.025 1.00 25.65 ? 2307 HOH A O 1 HETATM 3220 O O . HOH J 9 . ? 28.918 12.877 0.485 1.00 29.40 ? 2308 HOH A O 1 HETATM 3221 O O . HOH J 9 . ? 26.604 16.078 1.533 1.00 19.86 ? 2309 HOH A O 1 HETATM 3222 O O . HOH J 9 . ? 20.515 19.872 0.308 1.00 31.84 ? 2310 HOH A O 1 HETATM 3223 O O . HOH J 9 . ? 21.762 18.123 -4.302 1.00 42.03 ? 2311 HOH A O 1 HETATM 3224 O O . HOH J 9 . ? 20.027 17.621 -1.237 1.00 27.93 ? 2312 HOH A O 1 HETATM 3225 O O . HOH J 9 . ? 20.851 20.187 5.074 1.00 25.31 ? 2313 HOH A O 1 HETATM 3226 O O . HOH J 9 . ? 24.961 14.084 -7.726 1.00 39.89 ? 2314 HOH A O 1 HETATM 3227 O O . HOH J 9 . ? 26.485 16.970 -4.920 1.00 27.76 ? 2315 HOH A O 1 HETATM 3228 O O . HOH J 9 . ? 20.151 10.825 -7.204 1.00 29.99 ? 2316 HOH A O 1 HETATM 3229 O O . HOH J 9 . ? 24.692 8.694 -7.316 1.00 35.33 ? 2317 HOH A O 1 HETATM 3230 O O . HOH J 9 . ? 17.628 12.684 -5.230 1.00 14.87 ? 2318 HOH A O 1 HETATM 3231 O O . HOH J 9 . ? 28.908 11.729 -1.905 1.00 22.96 ? 2319 HOH A O 1 HETATM 3232 O O . HOH J 9 . ? 16.529 18.005 -3.448 1.00 32.46 ? 2320 HOH A O 1 HETATM 3233 O O . HOH J 9 . ? 16.704 3.466 23.317 1.00 13.58 ? 2321 HOH A O 1 HETATM 3234 O O . HOH J 9 . ? 8.224 -1.086 22.199 1.00 16.23 ? 2322 HOH A O 1 HETATM 3235 O O . HOH J 9 . ? 11.754 -3.294 17.569 1.00 10.04 ? 2323 HOH A O 1 HETATM 3236 O O . HOH J 9 . ? 13.978 -0.833 18.825 1.00 9.41 ? 2324 HOH A O 1 HETATM 3237 O O . HOH J 9 . ? 19.820 2.196 24.346 1.00 22.94 ? 2325 HOH A O 1 HETATM 3238 O O . HOH J 9 . ? 17.229 -3.790 23.974 1.00 10.55 ? 2326 HOH A O 1 HETATM 3239 O O . HOH J 9 . ? 22.719 -3.584 19.507 1.00 11.13 ? 2327 HOH A O 1 HETATM 3240 O O . HOH J 9 . ? 27.115 -1.244 26.290 1.00 30.56 ? 2328 HOH A O 1 HETATM 3241 O O . HOH J 9 . ? 21.853 -0.663 28.285 1.00 27.03 ? 2329 HOH A O 1 HETATM 3242 O O . HOH J 9 . ? 23.184 -5.955 28.242 1.00 25.78 ? 2330 HOH A O 1 HETATM 3243 O O . HOH J 9 . ? 24.557 -10.798 22.906 1.00 23.30 ? 2331 HOH A O 1 HETATM 3244 O O . HOH J 9 . ? 22.330 -14.661 24.068 1.00 28.83 ? 2332 HOH A O 1 HETATM 3245 O O . HOH J 9 . ? 20.902 -4.905 17.996 1.00 12.63 ? 2333 HOH A O 1 HETATM 3246 O O . HOH J 9 . ? 24.226 -17.298 27.265 1.00 36.96 ? 2334 HOH A O 1 HETATM 3247 O O . HOH J 9 . ? 28.077 -12.843 16.176 1.00 36.06 ? 2335 HOH A O 1 HETATM 3248 O O . HOH J 9 . ? 23.876 -18.310 16.431 1.00 34.90 ? 2336 HOH A O 1 HETATM 3249 O O . HOH J 9 . ? 23.891 -11.586 11.206 1.00 22.30 ? 2337 HOH A O 1 HETATM 3250 O O . HOH J 9 . ? 18.287 -12.253 9.064 1.00 19.05 ? 2338 HOH A O 1 HETATM 3251 O O . HOH J 9 . ? 21.881 -18.124 11.777 1.00 40.44 ? 2339 HOH A O 1 HETATM 3252 O O . HOH J 9 . ? 13.889 -13.812 7.920 1.00 25.90 ? 2340 HOH A O 1 HETATM 3253 O O . HOH J 9 . ? 16.229 -13.696 17.924 1.00 17.31 ? 2341 HOH A O 1 HETATM 3254 O O . HOH J 9 . ? 8.409 -10.207 20.733 1.00 21.87 ? 2342 HOH A O 1 HETATM 3255 O O . HOH J 9 . ? 20.001 -12.358 26.981 1.00 27.95 ? 2343 HOH A O 1 HETATM 3256 O O . HOH J 9 . ? 21.066 -8.045 27.049 1.00 20.12 ? 2344 HOH A O 1 HETATM 3257 O O . HOH J 9 . ? 10.123 7.630 31.058 1.00 34.46 ? 2345 HOH A O 1 HETATM 3258 O O . HOH J 9 . ? 12.658 10.113 24.776 1.00 22.47 ? 2346 HOH A O 1 HETATM 3259 O O . HOH J 9 . ? 13.305 8.385 27.031 1.00 17.69 ? 2347 HOH A O 1 HETATM 3260 O O . HOH J 9 . ? 8.584 11.869 24.968 1.00 26.66 ? 2348 HOH A O 1 HETATM 3261 O O . HOH J 9 . ? 6.295 9.490 23.831 1.00 21.77 ? 2349 HOH A O 1 HETATM 3262 O O . HOH J 9 . ? 7.795 15.166 20.954 1.00 23.92 ? 2350 HOH A O 1 HETATM 3263 O O . HOH J 9 . ? 14.003 16.658 15.729 1.00 20.74 ? 2351 HOH A O 1 HETATM 3264 O O . HOH J 9 . ? 11.201 19.296 18.210 1.00 39.66 ? 2352 HOH A O 1 HETATM 3265 O O A HOH J 9 . ? 17.571 -18.185 25.885 0.50 24.15 ? 2353 HOH A O 1 HETATM 3266 O O B HOH J 9 . ? 15.934 -18.945 24.448 0.50 22.26 ? 2353 HOH A O 1 HETATM 3267 O O A HOH J 9 . ? 11.582 21.792 21.660 0.50 20.44 ? 2354 HOH A O 1 HETATM 3268 O O B HOH J 9 . ? 11.969 23.245 20.140 0.50 20.84 ? 2354 HOH A O 1 HETATM 3269 O O . HOH J 9 . ? 15.056 14.582 24.683 1.00 22.29 ? 2355 HOH A O 1 HETATM 3270 O O . HOH J 9 . ? 19.448 12.411 21.778 1.00 38.61 ? 2356 HOH A O 1 HETATM 3271 O O . HOH J 9 . ? 16.564 18.612 19.954 1.00 34.87 ? 2357 HOH A O 1 HETATM 3272 O O . HOH J 9 . ? 16.058 17.363 14.367 1.00 27.30 ? 2358 HOH A O 1 HETATM 3273 O O . HOH J 9 . ? 23.118 21.561 13.748 1.00 29.48 ? 2359 HOH A O 1 HETATM 3274 O O . HOH J 9 . ? 23.103 17.670 15.421 1.00 23.18 ? 2360 HOH A O 1 HETATM 3275 O O . HOH J 9 . ? 22.605 19.862 7.273 1.00 21.20 ? 2361 HOH A O 1 HETATM 3276 O O . HOH J 9 . ? 19.015 18.447 8.405 1.00 16.56 ? 2362 HOH A O 1 HETATM 3277 O O . HOH J 9 . ? 25.017 18.413 7.450 1.00 22.59 ? 2363 HOH A O 1 HETATM 3278 O O . HOH J 9 . ? 13.883 17.945 12.563 1.00 19.16 ? 2364 HOH A O 1 HETATM 3279 O O . HOH J 9 . ? 10.258 -1.292 18.582 1.00 10.35 ? 2365 HOH A O 1 HETATM 3280 O O . HOH J 9 . ? 7.529 -7.528 20.847 1.00 15.01 ? 2366 HOH A O 1 HETATM 3281 O O . HOH J 9 . ? -0.971 -2.171 18.622 1.00 19.93 ? 2367 HOH A O 1 HETATM 3282 O O . HOH J 9 . ? 6.742 -13.888 11.506 1.00 22.12 ? 2368 HOH A O 1 HETATM 3283 O O . HOH J 9 . ? 7.660 -17.895 13.122 1.00 17.36 ? 2369 HOH A O 1 HETATM 3284 O O . HOH J 9 . ? 7.692 -23.199 21.287 1.00 32.95 ? 2370 HOH A O 1 HETATM 3285 O O . HOH J 9 . ? 11.123 -24.366 18.510 1.00 32.04 ? 2371 HOH A O 1 HETATM 3286 O O . HOH J 9 . ? 1.763 -29.558 15.515 1.00 39.69 ? 2372 HOH A O 1 HETATM 3287 O O . HOH J 9 . ? 0.487 -27.544 12.035 1.00 35.54 ? 2373 HOH A O 1 HETATM 3288 O O . HOH J 9 . ? 6.481 -20.139 6.988 1.00 24.97 ? 2374 HOH A O 1 HETATM 3289 O O . HOH J 9 . ? -0.499 -23.988 10.458 1.00 21.08 ? 2375 HOH A O 1 HETATM 3290 O O . HOH J 9 . ? 5.607 -16.278 11.668 1.00 25.18 ? 2376 HOH A O 1 HETATM 3291 O O . HOH J 9 . ? 20.652 -20.675 6.791 1.00 32.69 ? 2377 HOH A O 1 HETATM 3292 O O . HOH J 9 . ? 12.112 -20.722 7.801 1.00 32.18 ? 2378 HOH A O 1 HETATM 3293 O O . HOH J 9 . ? 15.527 -22.489 13.945 1.00 24.33 ? 2379 HOH A O 1 HETATM 3294 O O . HOH J 9 . ? 20.357 -14.591 10.552 1.00 33.20 ? 2380 HOH A O 1 HETATM 3295 O O . HOH J 9 . ? 15.864 -14.392 15.408 1.00 16.68 ? 2382 HOH A O 1 HETATM 3296 O O . HOH J 9 . ? 10.347 -16.916 19.279 1.00 15.81 ? 2383 HOH A O 1 HETATM 3297 O O . HOH J 9 . ? 17.035 -23.761 15.833 1.00 38.18 ? 2384 HOH A O 1 HETATM 3298 O O . HOH J 9 . ? 13.899 -24.393 18.438 1.00 23.36 ? 2385 HOH A O 1 HETATM 3299 O O . HOH J 9 . ? 25.416 -23.400 21.283 1.00 36.64 ? 2386 HOH A O 1 HETATM 3300 O O . HOH J 9 . ? 16.968 -21.631 24.266 1.00 31.49 ? 2388 HOH A O 1 HETATM 3301 O O . HOH J 9 . ? 20.298 -21.330 17.761 1.00 27.08 ? 2389 HOH A O 1 HETATM 3302 O O . HOH J 9 . ? 3.969 -21.480 20.164 1.00 32.77 ? 2390 HOH A O 1 HETATM 3303 O O . HOH J 9 . ? -1.268 -17.336 18.862 1.00 30.36 ? 2391 HOH A O 1 HETATM 3304 O O . HOH J 9 . ? 0.959 -20.848 10.902 1.00 25.99 ? 2392 HOH A O 1 HETATM 3305 O O . HOH J 9 . ? 3.538 -16.559 13.363 1.00 20.75 ? 2393 HOH A O 1 HETATM 3306 O O . HOH J 9 . ? -2.069 -12.449 14.655 1.00 36.64 ? 2394 HOH A O 1 HETATM 3307 O O . HOH J 9 . ? -2.467 -16.059 20.755 1.00 36.30 ? 2395 HOH A O 1 HETATM 3308 O O . HOH J 9 . ? -3.308 -11.678 21.408 1.00 28.44 ? 2396 HOH A O 1 HETATM 3309 O O . HOH J 9 . ? -1.385 -14.665 22.815 1.00 26.86 ? 2397 HOH A O 1 HETATM 3310 O O . HOH J 9 . ? 0.801 -13.900 26.121 1.00 22.89 ? 2398 HOH A O 1 HETATM 3311 O O . HOH J 9 . ? 3.094 -19.336 27.922 1.00 40.91 ? 2399 HOH A O 1 HETATM 3312 O O . HOH J 9 . ? 9.763 -13.119 30.661 1.00 24.41 ? 2400 HOH A O 1 HETATM 3313 O O . HOH J 9 . ? 13.517 -13.404 28.883 1.00 25.02 ? 2401 HOH A O 1 HETATM 3314 O O . HOH J 9 . ? 14.850 -10.198 32.207 1.00 34.92 ? 2402 HOH A O 1 HETATM 3315 O O . HOH J 9 . ? 13.794 -4.250 36.529 1.00 32.55 ? 2403 HOH A O 1 HETATM 3316 O O . HOH J 9 . ? 18.298 -2.640 30.929 1.00 31.11 ? 2405 HOH A O 1 HETATM 3317 O O . HOH J 9 . ? 14.648 -1.347 33.952 1.00 26.78 ? 2406 HOH A O 1 HETATM 3318 O O . HOH J 9 . ? 22.300 3.637 28.852 1.00 37.20 ? 2407 HOH A O 1 HETATM 3319 O O . HOH J 9 . ? 17.946 3.682 25.817 1.00 18.97 ? 2408 HOH A O 1 HETATM 3320 O O . HOH J 9 . ? 14.203 7.580 33.818 1.00 34.59 ? 2409 HOH A O 1 HETATM 3321 O O . HOH J 9 . ? -11.669 -9.008 -1.178 1.00 34.73 ? 2410 HOH A O 1 HETATM 3322 O O . HOH J 9 . ? -14.010 -3.464 -0.969 1.00 26.90 ? 2411 HOH A O 1 HETATM 3323 O O . HOH J 9 . ? -7.614 -11.986 -1.705 1.00 25.93 ? 2412 HOH A O 1 HETATM 3324 O O . HOH J 9 . ? -9.467 -7.537 -5.241 1.00 22.60 ? 2413 HOH A O 1 HETATM 3325 O O . HOH J 9 . ? -1.439 -5.597 16.461 1.00 31.53 ? 2414 HOH A O 1 HETATM 3326 O O . HOH J 9 . ? 7.783 -11.721 9.255 1.00 26.29 ? 2415 HOH A O 1 HETATM 3327 O O . HOH J 9 . ? 9.736 -12.383 6.614 1.00 29.35 ? 2416 HOH A O 1 HETATM 3328 O O . HOH J 9 . ? 17.544 -12.702 4.828 1.00 24.99 ? 2417 HOH A O 1 HETATM 3329 O O . HOH J 9 . ? 18.048 -8.557 12.880 1.00 13.92 ? 2418 HOH A O 1 HETATM 3330 O O . HOH J 9 . ? 24.191 -12.235 6.655 1.00 37.34 ? 2419 HOH A O 1 HETATM 3331 O O . HOH J 9 . ? 19.993 -11.916 5.056 1.00 25.59 ? 2420 HOH A O 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . GLY A 3 ? 0.2872 0.2409 0.2697 -0.0005 -0.0074 0.0075 91 GLY A N 2 C CA . GLY A 3 ? 0.2642 0.2448 0.2688 0.0049 -0.0048 0.0128 91 GLY A CA 3 C C . GLY A 3 ? 0.2563 0.2368 0.2502 0.0064 -0.0048 0.0073 91 GLY A C 4 O O . GLY A 3 ? 0.2808 0.2432 0.2859 0.0182 -0.0191 0.0103 91 GLY A O 5 N N . ASN A 4 ? 0.2222 0.2080 0.2397 0.0072 -0.0033 0.0108 92 ASN A N 6 C CA . ASN A 4 ? 0.1809 0.1723 0.1939 0.0073 0.0029 -0.0012 92 ASN A CA 7 C C . ASN A 4 ? 0.1591 0.1625 0.1638 0.0093 -0.0116 -0.0102 92 ASN A C 8 O O . ASN A 4 ? 0.1529 0.1504 0.1753 0.0111 -0.0146 -0.0105 92 ASN A O 9 C CB . ASN A 4 ? 0.1654 0.1523 0.1946 0.0124 -0.0021 -0.0059 92 ASN A CB 10 C CG . ASN A 4 ? 0.1346 0.1408 0.1790 0.0049 -0.0019 -0.0109 92 ASN A CG 11 O OD1 . ASN A 4 ? 0.1197 0.1378 0.1757 0.0042 -0.0010 -0.0195 92 ASN A OD1 12 N ND2 . ASN A 4 ? 0.1584 0.1483 0.1690 0.0128 -0.0230 -0.0109 92 ASN A ND2 13 N N . PRO A 5 ? 0.1559 0.1566 0.1628 0.0103 -0.0019 -0.0147 93 PRO A N 14 C CA . PRO A 5 ? 0.1412 0.1518 0.1536 0.0104 -0.0116 -0.0176 93 PRO A CA 15 C C . PRO A 5 ? 0.1343 0.1334 0.1496 0.0094 -0.0081 -0.0121 93 PRO A C 16 O O . PRO A 5 ? 0.1237 0.1410 0.1605 0.0035 -0.0243 -0.0255 93 PRO A O 17 C CB . PRO A 5 ? 0.1758 0.1659 0.1715 0.0030 -0.0023 -0.0229 93 PRO A CB 18 C CG . PRO A 5 ? 0.1661 0.1700 0.1642 0.0220 -0.0258 -0.0222 93 PRO A CG 19 C CD . PRO A 5 ? 0.1660 0.1731 0.1697 0.0224 0.0062 -0.0048 93 PRO A CD 20 N N . PHE A 6 ? 0.1191 0.1345 0.1435 0.0109 -0.0176 -0.0120 94 PHE A N 21 C CA . PHE A 6 ? 0.1296 0.1387 0.1580 0.0044 -0.0039 -0.0107 94 PHE A CA 22 C C . PHE A 6 ? 0.1391 0.1728 0.1527 -0.0029 -0.0130 -0.0144 94 PHE A C 23 O O . PHE A 6 ? 0.1752 0.1938 0.1644 0.0029 -0.0006 -0.0198 94 PHE A O 24 C CB . PHE A 6 ? 0.1114 0.1439 0.1501 0.0033 -0.0144 -0.0135 94 PHE A CB 25 C CG . PHE A 6 ? 0.1074 0.1349 0.1224 0.0116 -0.0112 -0.0068 94 PHE A CG 26 C CD1 . PHE A 6 ? 0.1051 0.1132 0.1015 0.0112 -0.0111 0.0121 94 PHE A CD1 27 C CD2 . PHE A 6 ? 0.1185 0.1268 0.1274 0.0101 -0.0124 -0.0154 94 PHE A CD2 28 C CE1 . PHE A 6 ? 0.1173 0.1311 0.0993 0.0124 -0.0102 0.0030 94 PHE A CE1 29 C CE2 . PHE A 6 ? 0.1329 0.1302 0.1361 0.0087 -0.0023 -0.0037 94 PHE A CE2 30 C CZ . PHE A 6 ? 0.1223 0.1244 0.1183 0.0053 -0.0189 -0.0057 94 PHE A CZ 31 N N . GLU A 7 ? 0.1731 0.1771 0.1651 0.0004 -0.0041 -0.0274 95 GLU A N 32 C CA . GLU A 7 ? 0.2108 0.2069 0.2171 0.0020 -0.0067 -0.0271 95 GLU A CA 33 C C . GLU A 7 ? 0.2109 0.1985 0.2138 0.0065 0.0008 -0.0230 95 GLU A C 34 O O . GLU A 7 ? 0.1867 0.1845 0.2319 0.0245 -0.0005 -0.0432 95 GLU A O 35 C CB . GLU A 7 ? 0.2281 0.2308 0.2416 0.0061 -0.0023 -0.0159 95 GLU A CB 36 C CG . GLU A 7 ? 0.3047 0.2911 0.2898 0.0077 -0.0011 -0.0257 95 GLU A CG 37 C CD . GLU A 7 ? 0.3779 0.3846 0.3945 -0.0164 0.0082 0.0006 95 GLU A CD 38 O OE1 . GLU A 7 ? 0.3977 0.4239 0.4221 0.0095 0.0000 -0.0097 95 GLU A OE1 39 O OE2 . GLU A 7 ? 0.4610 0.4095 0.4551 -0.0005 0.0014 -0.0071 95 GLU A OE2 40 N N . GLY A 8 ? 0.2087 0.2115 0.2178 -0.0086 0.0042 -0.0271 96 GLY A N 41 C CA . GLY A 8 ? 0.2219 0.2070 0.2401 -0.0026 0.0018 -0.0215 96 GLY A CA 42 C C . GLY A 8 ? 0.2103 0.2190 0.2370 -0.0012 0.0056 -0.0093 96 GLY A C 43 O O . GLY A 8 ? 0.2269 0.2383 0.2810 -0.0003 0.0110 -0.0242 96 GLY A O 44 N N . VAL A 9 ? 0.1961 0.2016 0.2099 -0.0030 0.0124 -0.0228 97 VAL A N 45 C CA . VAL A 9 ? 0.1817 0.1979 0.1982 0.0002 0.0084 -0.0294 97 VAL A CA 46 C C . VAL A 9 ? 0.1883 0.1923 0.1882 -0.0014 0.0017 -0.0347 97 VAL A C 47 O O . VAL A 9 ? 0.1983 0.2614 0.2153 -0.0069 -0.0042 -0.0466 97 VAL A O 48 C CB . VAL A 9 ? 0.1681 0.1905 0.1984 -0.0017 0.0081 -0.0265 97 VAL A CB 49 C CG1 . VAL A 9 ? 0.1887 0.2029 0.2160 -0.0002 0.0122 -0.0221 97 VAL A CG1 50 C CG2 . VAL A 9 ? 0.1678 0.2014 0.1980 -0.0032 0.0069 -0.0345 97 VAL A CG2 51 N N . GLN A 10 ? 0.1771 0.2016 0.1736 0.0022 0.0080 -0.0362 98 GLN A N 52 C CA . GLN A 10 ? 0.1996 0.2186 0.1938 -0.0005 -0.0047 -0.0209 98 GLN A CA 53 C C . GLN A 10 ? 0.2016 0.2028 0.1778 0.0044 -0.0083 -0.0146 98 GLN A C 54 O O . GLN A 10 ? 0.2059 0.2258 0.1531 0.0086 -0.0199 -0.0312 98 GLN A O 55 C CB . GLN A 10 ? 0.2247 0.2355 0.2093 -0.0028 0.0022 -0.0077 98 GLN A CB 56 C CG . GLN A 10 ? 0.2609 0.2765 0.2565 0.0053 0.0035 -0.0107 98 GLN A CG 57 C CD . GLN A 10 ? 0.2971 0.3096 0.2531 0.0089 0.0120 -0.0081 98 GLN A CD 58 O OE1 . GLN A 10 ? 0.2941 0.3263 0.2525 0.0131 0.0182 -0.0050 98 GLN A OE1 59 N NE2 . GLN A 10 ? 0.2955 0.3353 0.2633 0.0113 -0.0078 -0.0156 98 GLN A NE2 60 N N . LEU A 11 ? 0.1769 0.1990 0.1516 0.0106 -0.0119 -0.0181 99 LEU A N 61 C CA . LEU A 11 ? 0.1705 0.1974 0.1699 0.0110 -0.0087 -0.0093 99 LEU A CA 62 C C . LEU A 11 ? 0.1813 0.2147 0.1660 0.0087 -0.0021 -0.0040 99 LEU A C 63 O O . LEU A 11 ? 0.1892 0.2498 0.1481 0.0222 0.0137 0.0035 99 LEU A O 64 C CB . LEU A 11 ? 0.1756 0.1946 0.1645 0.0153 -0.0048 -0.0056 99 LEU A CB 65 C CG . LEU A 11 ? 0.1625 0.1664 0.1475 0.0187 -0.0083 -0.0019 99 LEU A CG 66 C CD1 . LEU A 11 ? 0.1600 0.1982 0.1333 0.0154 -0.0050 -0.0169 99 LEU A CD1 67 C CD2 . LEU A 11 ? 0.1811 0.1937 0.1514 -0.0025 0.0053 0.0035 99 LEU A CD2 68 N N . TRP A 12 ? 0.1803 0.2325 0.1659 0.0000 0.0030 -0.0051 100 TRP A N 69 C CA . TRP A 12 ? 0.1893 0.2234 0.1738 -0.0009 -0.0014 -0.0072 100 TRP A CA 70 C C . TRP A 12 ? 0.1933 0.2256 0.1686 0.0060 -0.0050 -0.0042 100 TRP A C 71 O O . TRP A 12 ? 0.1767 0.2559 0.1583 0.0176 -0.0058 -0.0061 100 TRP A O 72 C CB . TRP A 12 ? 0.1889 0.2247 0.1827 -0.0012 -0.0070 0.0041 100 TRP A CB 73 C CG . TRP A 12 ? 0.1907 0.2312 0.1656 0.0011 -0.0159 0.0149 100 TRP A CG 74 C CD1 . TRP A 12 ? 0.1952 0.2203 0.1883 0.0162 -0.0051 0.0291 100 TRP A CD1 75 C CD2 . TRP A 12 ? 0.2094 0.2320 0.2026 0.0145 -0.0093 0.0204 100 TRP A CD2 76 N NE1 . TRP A 12 ? 0.1905 0.2347 0.2190 0.0005 -0.0161 0.0217 100 TRP A NE1 77 C CE2 . TRP A 12 ? 0.2102 0.2501 0.1913 0.0065 -0.0073 0.0081 100 TRP A CE2 78 C CE3 . TRP A 12 ? 0.2056 0.2444 0.2197 0.0022 -0.0012 0.0117 100 TRP A CE3 79 C CZ2 . TRP A 12 ? 0.2094 0.2603 0.2342 -0.0052 -0.0050 0.0124 100 TRP A CZ2 80 C CZ3 . TRP A 12 ? 0.2270 0.2549 0.2407 0.0009 0.0095 -0.0011 100 TRP A CZ3 81 C CH2 . TRP A 12 ? 0.2274 0.2623 0.2451 -0.0026 0.0037 0.0069 100 TRP A CH2 82 N N . ALA A 13 ? 0.2011 0.2464 0.1834 0.0139 0.0059 -0.0020 101 ALA A N 83 C CA . ALA A 13 ? 0.2201 0.2441 0.1931 0.0052 0.0051 -0.0037 101 ALA A CA 84 C C . ALA A 13 ? 0.2256 0.2584 0.2061 0.0083 0.0015 0.0003 101 ALA A C 85 O O . ALA A 13 ? 0.2212 0.2897 0.2170 0.0142 0.0147 0.0066 101 ALA A O 86 C CB . ALA A 13 ? 0.2345 0.2597 0.2020 0.0091 -0.0067 -0.0069 101 ALA A CB 87 N N . ASN A 14 ? 0.2199 0.2540 0.2206 0.0091 -0.0003 0.0032 102 ASN A N 88 C CA . ASN A 14 ? 0.2371 0.2661 0.2338 0.0031 -0.0011 -0.0040 102 ASN A CA 89 C C . ASN A 14 ? 0.2473 0.2825 0.2479 0.0027 -0.0001 0.0066 102 ASN A C 90 O O . ASN A 14 ? 0.2159 0.3090 0.2039 0.0105 0.0159 0.0105 102 ASN A O 91 C CB . ASN A 14 ? 0.2466 0.2735 0.2411 0.0045 -0.0046 -0.0033 102 ASN A CB 92 C CG . ASN A 14 ? 0.2314 0.2641 0.2038 0.0065 -0.0109 -0.0112 102 ASN A CG 93 O OD1 . ASN A 14 ? 0.2445 0.2986 0.2190 0.0125 -0.0169 -0.0022 102 ASN A OD1 94 N ND2 . ASN A 14 ? 0.2190 0.2627 0.2040 0.0016 -0.0155 -0.0072 102 ASN A ND2 95 N N . ASN A 15 ? 0.2650 0.3184 0.2768 0.0040 -0.0036 0.0023 103 ASN A N 96 C CA . ASN A 15 ? 0.2803 0.3206 0.2925 0.0002 -0.0017 0.0063 103 ASN A CA 97 C C . ASN A 15 ? 0.2642 0.3155 0.2886 0.0037 -0.0021 0.0015 103 ASN A C 98 O O . ASN A 15 ? 0.2399 0.3399 0.2852 0.0106 0.0017 0.0102 103 ASN A O 99 C CB . ASN A 15 ? 0.2895 0.3364 0.3183 0.0041 -0.0019 -0.0045 103 ASN A CB 100 C CG . ASN A 15 ? 0.3423 0.3665 0.3412 -0.0010 0.0064 0.0017 103 ASN A CG 101 O OD1 . ASN A 15 ? 0.3181 0.3957 0.3505 0.0043 0.0050 -0.0013 103 ASN A OD1 102 N ND2 . ASN A 15 ? 0.3542 0.4109 0.3774 -0.0106 -0.0016 -0.0064 103 ASN A ND2 103 N N . TYR A 16 ? 0.2663 0.3115 0.2801 0.0026 -0.0051 0.0035 104 TYR A N 104 C CA . TYR A 16 ? 0.2689 0.3024 0.2716 -0.0015 -0.0014 0.0039 104 TYR A CA 105 C C . TYR A 16 ? 0.2639 0.3008 0.2714 -0.0016 0.0025 0.0088 104 TYR A C 106 O O . TYR A 16 ? 0.2208 0.3268 0.2515 -0.0013 0.0071 0.0210 104 TYR A O 107 C CB . TYR A 16 ? 0.2796 0.3172 0.2852 -0.0001 0.0000 -0.0008 104 TYR A CB 108 C CG . TYR A 16 ? 0.3423 0.3460 0.3315 0.0065 -0.0035 -0.0048 104 TYR A CG 109 C CD1 . TYR A 16 ? 0.3662 0.3844 0.3886 -0.0069 0.0008 0.0041 104 TYR A CD1 110 C CD2 . TYR A 16 ? 0.3387 0.3795 0.3371 0.0056 -0.0017 -0.0009 104 TYR A CD2 111 C CE1 . TYR A 16 ? 0.3981 0.4038 0.4153 0.0015 0.0045 -0.0035 104 TYR A CE1 112 C CE2 . TYR A 16 ? 0.3854 0.3838 0.3817 0.0037 -0.0033 0.0051 104 TYR A CE2 113 C CZ . TYR A 16 ? 0.3928 0.4221 0.4131 -0.0028 -0.0014 0.0029 104 TYR A CZ 114 O OH . TYR A 16 ? 0.4293 0.4491 0.4597 0.0025 0.0019 0.0014 104 TYR A OH 115 N N . TYR A 17 ? 0.2460 0.3003 0.2489 0.0051 -0.0046 0.0056 105 TYR A N 116 C CA . TYR A 17 ? 0.2492 0.2924 0.2467 -0.0001 -0.0004 0.0043 105 TYR A CA 117 C C . TYR A 17 ? 0.2574 0.2998 0.2533 0.0052 0.0018 0.0045 105 TYR A C 118 O O . TYR A 17 ? 0.2194 0.3495 0.2315 0.0085 0.0241 0.0133 105 TYR A O 119 C CB . TYR A 17 ? 0.2317 0.2807 0.2313 0.0081 -0.0028 0.0071 105 TYR A CB 120 C CG . TYR A 17 ? 0.2154 0.2625 0.2177 -0.0009 0.0030 0.0052 105 TYR A CG 121 C CD1 . TYR A 17 ? 0.2071 0.2656 0.1861 0.0132 -0.0083 0.0118 105 TYR A CD1 122 C CD2 . TYR A 17 ? 0.1969 0.2737 0.1901 0.0121 0.0105 0.0040 105 TYR A CD2 123 C CE1 . TYR A 17 ? 0.1698 0.2448 0.1954 0.0023 0.0012 0.0155 105 TYR A CE1 124 C CE2 . TYR A 17 ? 0.2050 0.2588 0.1918 0.0130 0.0051 0.0189 105 TYR A CE2 125 C CZ . TYR A 17 ? 0.1838 0.2390 0.1903 0.0048 0.0046 0.0111 105 TYR A CZ 126 O OH . TYR A 17 ? 0.1774 0.2809 0.1605 0.0170 0.0111 0.0153 105 TYR A OH 127 N N . ARG A 18 ? 0.2606 0.3142 0.2485 0.0029 0.0011 0.0031 106 ARG A N 128 C CA . ARG A 18 ? 0.2871 0.3137 0.2699 0.0053 0.0023 -0.0054 106 ARG A CA 129 C C . ARG A 18 ? 0.3010 0.3286 0.2918 0.0039 0.0028 -0.0004 106 ARG A C 130 O O . ARG A 18 ? 0.2925 0.3641 0.2773 0.0118 0.0203 0.0122 106 ARG A O 131 C CB . ARG A 18 ? 0.2850 0.3160 0.2731 0.0016 0.0045 0.0006 106 ARG A CB 132 C CG . ARG A 18 ? 0.3097 0.3331 0.2818 0.0030 -0.0005 -0.0055 106 ARG A CG 133 C CD . ARG A 18 ? 0.3382 0.3517 0.3302 0.0121 -0.0015 -0.0060 106 ARG A CD 134 N NE . ARG A 18 ? 0.3583 0.3878 0.3733 0.0091 0.0038 -0.0002 106 ARG A NE 135 C CZ . ARG A 18 ? 0.3974 0.4017 0.3890 0.0071 -0.0043 0.0039 106 ARG A CZ 136 N NH1 . ARG A 18 ? 0.3993 0.4092 0.3938 0.0011 -0.0033 -0.0057 106 ARG A NH1 137 N NH2 . ARG A 18 ? 0.4070 0.4274 0.4074 0.0043 -0.0002 0.0066 106 ARG A NH2 138 N N . SER A 19 ? 0.3074 0.3484 0.3157 0.0001 0.0017 0.0015 107 SER A N 139 C CA . SER A 19 ? 0.3302 0.3517 0.3299 -0.0016 -0.0001 0.0050 107 SER A CA 140 C C . SER A 19 ? 0.3138 0.3530 0.3257 0.0000 0.0019 0.0057 107 SER A C 141 O O . SER A 19 ? 0.2968 0.3714 0.3166 -0.0004 0.0085 0.0180 107 SER A O 142 C CB . SER A 19 ? 0.3359 0.3644 0.3460 0.0008 -0.0020 0.0044 107 SER A CB 143 O OG . SER A 19 ? 0.3810 0.4019 0.3937 0.0011 -0.0049 -0.0131 107 SER A OG 144 N N . GLU A 20 ? 0.3066 0.3474 0.3045 0.0027 0.0045 0.0062 108 GLU A N 145 C CA . GLU A 20 ? 0.3076 0.3358 0.3013 0.0017 0.0068 0.0037 108 GLU A CA 146 C C . GLU A 20 ? 0.3002 0.3362 0.2993 0.0013 0.0061 0.0041 108 GLU A C 147 O O . GLU A 20 ? 0.2915 0.3663 0.3117 0.0093 0.0040 0.0125 108 GLU A O 148 C CB . GLU A 20 ? 0.2988 0.3358 0.3013 -0.0031 0.0069 0.0049 108 GLU A CB 149 C CG . GLU A 20 ? 0.2851 0.3219 0.2812 0.0014 0.0156 0.0112 108 GLU A CG 150 C CD . GLU A 20 ? 0.2563 0.2951 0.2609 0.0045 -0.0023 0.0103 108 GLU A CD 151 O OE1 . GLU A 20 ? 0.2365 0.3088 0.2543 0.0164 -0.0100 0.0032 108 GLU A OE1 152 O OE2 . GLU A 20 ? 0.2928 0.3392 0.2989 0.0030 -0.0077 0.0074 108 GLU A OE2 153 N N . VAL A 21 ? 0.2971 0.3384 0.2827 0.0067 0.0045 0.0042 109 VAL A N 154 C CA . VAL A 21 ? 0.3012 0.3340 0.2854 0.0035 0.0039 0.0041 109 VAL A CA 155 C C . VAL A 21 ? 0.3190 0.3511 0.3045 0.0094 0.0086 0.0093 109 VAL A C 156 O O . VAL A 21 ? 0.3063 0.3646 0.2964 0.0139 0.0221 0.0250 109 VAL A O 157 C CB . VAL A 21 ? 0.2916 0.3326 0.2794 0.0067 0.0049 0.0002 109 VAL A CB 158 C CG1 . VAL A 21 ? 0.3079 0.3512 0.2930 0.0065 -0.0008 -0.0013 109 VAL A CG1 159 C CG2 . VAL A 21 ? 0.2666 0.3090 0.2537 -0.0020 -0.0036 0.0084 109 VAL A CG2 160 N N . HIS A 22 ? 0.3219 0.3660 0.3144 0.0054 0.0096 0.0105 110 HIS A N 161 C CA . HIS A 22 ? 0.3498 0.3726 0.3358 0.0023 0.0062 0.0047 110 HIS A CA 162 C C . HIS A 22 ? 0.3611 0.3779 0.3551 0.0022 0.0038 0.0048 110 HIS A C 163 O O . HIS A 22 ? 0.3738 0.4049 0.3593 0.0080 0.0093 0.0126 110 HIS A O 164 C CB . HIS A 22 ? 0.3458 0.3650 0.3329 -0.0004 0.0118 0.0056 110 HIS A CB 165 C CG . HIS A 22 ? 0.3735 0.3849 0.3569 0.0031 0.0011 -0.0019 110 HIS A CG 166 N ND1 . HIS A 22 ? 0.3796 0.4045 0.3565 -0.0008 0.0067 0.0013 110 HIS A ND1 167 C CD2 . HIS A 22 ? 0.3729 0.3927 0.3728 -0.0001 0.0111 0.0010 110 HIS A CD2 168 C CE1 . HIS A 22 ? 0.4162 0.4145 0.3954 -0.0010 0.0091 0.0017 110 HIS A CE1 169 N NE2 . HIS A 22 ? 0.4049 0.4149 0.3840 0.0008 0.0058 0.0018 110 HIS A NE2 170 N N . THR A 23 ? 0.3774 0.3970 0.3702 0.0031 0.0035 0.0020 111 THR A N 171 C CA . THR A 23 ? 0.3965 0.4031 0.3903 -0.0001 0.0025 0.0021 111 THR A CA 172 C C . THR A 23 ? 0.3900 0.4064 0.3878 0.0019 0.0053 0.0013 111 THR A C 173 O O . THR A 23 ? 0.3868 0.4180 0.3936 -0.0079 0.0086 0.0043 111 THR A O 174 C CB . THR A 23 ? 0.4054 0.4107 0.4001 0.0023 0.0001 0.0044 111 THR A CB 175 O OG1 . THR A 23 ? 0.4383 0.4437 0.4122 0.0003 0.0006 -0.0003 111 THR A OG1 176 C CG2 . THR A 23 ? 0.4059 0.4114 0.4113 -0.0008 0.0031 0.0038 111 THR A CG2 177 N N . LEU A 24 ? 0.3789 0.4029 0.3768 0.0007 0.0050 0.0046 112 LEU A N 178 C CA . LEU A 24 ? 0.3772 0.3881 0.3690 -0.0004 0.0006 0.0021 112 LEU A CA 179 C C . LEU A 24 ? 0.3664 0.3793 0.3571 -0.0017 0.0060 0.0020 112 LEU A C 180 O O . LEU A 24 ? 0.3643 0.3956 0.3617 0.0022 0.0068 0.0071 112 LEU A O 181 C CB . LEU A 24 ? 0.3786 0.3958 0.3785 -0.0017 0.0060 0.0007 112 LEU A CB 182 C CG . LEU A 24 ? 0.3958 0.4127 0.3973 0.0014 -0.0018 0.0023 112 LEU A CG 183 C CD1 . LEU A 24 ? 0.4084 0.4248 0.4060 -0.0003 0.0010 0.0018 112 LEU A CD1 184 C CD2 . LEU A 24 ? 0.4030 0.4084 0.4018 -0.0006 0.0020 0.0015 112 LEU A CD2 185 N N . ALA A 25 ? 0.3438 0.3660 0.3273 0.0032 0.0089 0.0001 113 ALA A N 186 C CA . ALA A 25 ? 0.3382 0.3525 0.3232 0.0000 0.0051 0.0002 113 ALA A CA 187 C C . ALA A 25 ? 0.3239 0.3476 0.3170 0.0043 0.0076 0.0009 113 ALA A C 188 O O . ALA A 25 ? 0.3121 0.3521 0.2962 0.0095 0.0209 0.0056 113 ALA A O 189 C CB . ALA A 25 ? 0.3335 0.3509 0.3312 -0.0010 0.0041 -0.0008 113 ALA A CB 190 N N . ILE A 26 ? 0.3218 0.3415 0.3098 0.0019 0.0034 -0.0037 114 ILE A N 191 C CA . ILE A 26 ? 0.3173 0.3394 0.3112 0.0020 0.0035 0.0007 114 ILE A CA 192 C C . ILE A 26 ? 0.3192 0.3427 0.3180 0.0039 0.0034 0.0012 114 ILE A C 193 O O . ILE A 26 ? 0.3063 0.3618 0.2976 0.0089 0.0132 0.0022 114 ILE A O 194 C CB . ILE A 26 ? 0.3125 0.3350 0.3019 0.0004 0.0015 -0.0007 114 ILE A CB 195 C CG1 . ILE A 26 ? 0.3204 0.3336 0.3069 -0.0006 0.0052 0.0025 114 ILE A CG1 196 C CG2 . ILE A 26 ? 0.3102 0.3282 0.2985 0.0080 0.0003 0.0008 114 ILE A CG2 197 C CD1 . ILE A 26 ? 0.3382 0.3464 0.3333 -0.0020 0.0053 0.0050 114 ILE A CD1 198 N N . PRO A 27 ? 0.3335 0.3534 0.3336 0.0007 0.0047 0.0002 115 PRO A N 199 C CA . PRO A 27 ? 0.3513 0.3540 0.3467 0.0004 0.0033 0.0031 115 PRO A CA 200 C C . PRO A 27 ? 0.3588 0.3676 0.3650 0.0015 0.0023 0.0030 115 PRO A C 201 O O . PRO A 27 ? 0.3642 0.3566 0.3730 -0.0045 0.0036 0.0074 115 PRO A O 202 C CB . PRO A 27 ? 0.3532 0.3605 0.3554 -0.0001 0.0061 0.0042 115 PRO A CB 203 C CG . PRO A 27 ? 0.3500 0.3686 0.3447 0.0008 0.0057 0.0034 115 PRO A CG 204 C CD . PRO A 27 ? 0.3357 0.3587 0.3357 -0.0039 0.0019 0.0043 115 PRO A CD 205 N N . GLN A 28 ? 0.3722 0.3720 0.3654 0.0021 0.0066 0.0010 116 GLN A N 206 C CA . GLN A 28 ? 0.3748 0.3733 0.3750 0.0028 -0.0004 -0.0012 116 GLN A CA 207 C C . GLN A 28 ? 0.3612 0.3560 0.3625 0.0018 0.0036 -0.0024 116 GLN A C 208 O O . GLN A 28 ? 0.3706 0.3514 0.3782 0.0047 -0.0020 -0.0032 116 GLN A O 209 C CB . GLN A 28 ? 0.3902 0.3781 0.3792 0.0024 0.0052 0.0001 116 GLN A CB 210 C CG . GLN A 28 ? 0.4096 0.4212 0.4171 0.0005 -0.0032 0.0064 116 GLN A CG 211 C CD . GLN A 28 ? 0.4714 0.4563 0.4652 -0.0007 -0.0016 -0.0083 116 GLN A CD 212 O OE1 . GLN A 28 ? 0.4939 0.4808 0.5026 -0.0044 0.0059 0.0109 116 GLN A OE1 213 N NE2 . GLN A 28 ? 0.4849 0.4949 0.4856 -0.0035 0.0012 0.0089 116 GLN A NE2 214 N N . ILE A 29 ? 0.3316 0.3384 0.3395 0.0037 0.0034 0.0012 117 ILE A N 215 C CA . ILE A 29 ? 0.3187 0.3250 0.3142 0.0061 0.0041 0.0007 117 ILE A CA 216 C C . ILE A 29 ? 0.3072 0.3207 0.3072 0.0075 0.0036 0.0006 117 ILE A C 217 O O . ILE A 29 ? 0.2797 0.3053 0.2882 0.0125 0.0069 0.0033 117 ILE A O 218 C CB . ILE A 29 ? 0.3129 0.3198 0.3133 0.0060 -0.0007 -0.0005 117 ILE A CB 219 C CG1 . ILE A 29 ? 0.3214 0.3203 0.3158 0.0105 0.0002 -0.0024 117 ILE A CG1 220 C CG2 . ILE A 29 ? 0.3064 0.3188 0.3064 0.0009 0.0039 -0.0001 117 ILE A CG2 221 C CD1 . ILE A 29 ? 0.3333 0.3270 0.3319 0.0000 0.0093 0.0080 117 ILE A CD1 222 N N . THR A 30 ? 0.3024 0.3163 0.3144 0.0154 0.0081 0.0034 118 THR A N 223 C CA . THR A 30 ? 0.3146 0.3276 0.3186 0.0094 0.0047 0.0030 118 THR A CA 224 C C . THR A 30 ? 0.3361 0.3457 0.3340 0.0039 0.0030 0.0040 118 THR A C 225 O O . THR A 30 ? 0.3370 0.3582 0.3431 0.0005 0.0014 0.0069 118 THR A O 226 C CB . THR A 30 ? 0.3165 0.3284 0.3167 0.0062 0.0060 0.0091 118 THR A CB 227 O OG1 . THR A 30 ? 0.3238 0.3337 0.3418 0.0342 0.0104 0.0086 118 THR A OG1 228 C CG2 . THR A 30 ? 0.3085 0.3139 0.3208 0.0134 0.0046 0.0010 118 THR A CG2 229 N N . ASP A 31 ? 0.3544 0.3670 0.3522 0.0011 0.0019 0.0126 119 ASP A N 230 C CA . ASP A 31 ? 0.3751 0.3795 0.3682 -0.0016 0.0002 0.0066 119 ASP A CA 231 C C . ASP A 31 ? 0.3696 0.3764 0.3659 -0.0035 0.0003 0.0063 119 ASP A C 232 O O . ASP A 31 ? 0.3740 0.3960 0.3630 -0.0103 0.0005 0.0188 119 ASP A O 233 C CB . ASP A 31 ? 0.3809 0.3914 0.3825 0.0021 0.0036 0.0077 119 ASP A CB 234 C CG . ASP A 31 ? 0.4303 0.4302 0.4315 -0.0084 -0.0072 -0.0007 119 ASP A CG 235 O OD1 . ASP A 31 ? 0.4539 0.4652 0.4698 -0.0028 0.0108 -0.0086 119 ASP A OD1 236 O OD2 . ASP A 31 ? 0.4759 0.5087 0.5144 -0.0045 0.0107 -0.0004 119 ASP A OD2 237 N N . PRO A 32 ? 0.3650 0.3745 0.3518 -0.0062 0.0030 0.0108 120 PRO A N 238 C CA . PRO A 32 ? 0.3593 0.3674 0.3531 -0.0052 0.0031 0.0078 120 PRO A CA 239 C C . PRO A 32 ? 0.3567 0.3671 0.3521 -0.0045 0.0024 0.0111 120 PRO A C 240 O O . PRO A 32 ? 0.3460 0.3632 0.3270 -0.0167 0.0068 0.0173 120 PRO A O 241 C CB . PRO A 32 ? 0.3619 0.3719 0.3636 -0.0020 0.0002 0.0081 120 PRO A CB 242 C CG . PRO A 32 ? 0.3603 0.3678 0.3491 -0.0026 0.0035 0.0079 120 PRO A CG 243 C CD . PRO A 32 ? 0.3658 0.3705 0.3531 -0.0018 0.0008 0.0131 120 PRO A CD 244 N N . ALA A 33 ? 0.3615 0.3671 0.3481 -0.0048 0.0023 0.0123 121 ALA A N 245 C CA . ALA A 33 ? 0.3552 0.3615 0.3520 -0.0052 0.0023 0.0074 121 ALA A CA 246 C C . ALA A 33 ? 0.3455 0.3543 0.3435 -0.0010 0.0004 0.0106 121 ALA A C 247 O O . ALA A 33 ? 0.3621 0.3900 0.3460 -0.0086 0.0008 0.0246 121 ALA A O 248 C CB . ALA A 33 ? 0.3588 0.3598 0.3521 -0.0024 0.0013 0.0058 121 ALA A CB 249 N N . LEU A 34 ? 0.3375 0.3637 0.3400 -0.0042 0.0026 0.0115 122 LEU A N 250 C CA . LEU A 34 ? 0.3273 0.3480 0.3298 -0.0031 0.0029 0.0066 122 LEU A CA 251 C C . LEU A 34 ? 0.3203 0.3497 0.3202 -0.0033 0.0040 0.0097 122 LEU A C 252 O O . LEU A 34 ? 0.3122 0.3606 0.3106 -0.0063 -0.0037 0.0167 122 LEU A O 253 C CB . LEU A 34 ? 0.3435 0.3588 0.3438 -0.0013 0.0036 0.0102 122 LEU A CB 254 C CG . LEU A 34 ? 0.3597 0.3629 0.3652 -0.0008 0.0084 0.0075 122 LEU A CG 255 C CD1 . LEU A 34 ? 0.3805 0.3753 0.3747 0.0021 0.0076 0.0012 122 LEU A CD1 256 C CD2 . LEU A 34 ? 0.3660 0.3765 0.3616 -0.0011 0.0092 0.0057 122 LEU A CD2 257 N N . ARG A 35 ? 0.3121 0.3373 0.3019 -0.0053 0.0009 0.0072 123 ARG A N 258 C CA . ARG A 35 ? 0.3043 0.3333 0.2913 -0.0079 0.0084 0.0053 123 ARG A CA 259 C C . ARG A 35 ? 0.2851 0.3285 0.2816 -0.0038 0.0066 0.0062 123 ARG A C 260 O O . ARG A 35 ? 0.2632 0.3741 0.2401 -0.0176 0.0193 0.0228 123 ARG A O 261 C CB . ARG A 35 ? 0.3051 0.3279 0.2938 -0.0102 0.0099 -0.0015 123 ARG A CB 262 C CG . ARG A 35 ? 0.3110 0.3164 0.3021 -0.0058 0.0116 0.0046 123 ARG A CG 263 C CD . ARG A 35 ? 0.2716 0.2472 0.2608 -0.0038 0.0032 0.0030 123 ARG A CD 264 N NE . ARG A 35 ? 0.2398 0.2271 0.2366 -0.0138 0.0059 -0.0007 123 ARG A NE 265 C CZ . ARG A 35 ? 0.1942 0.2080 0.2029 0.0021 -0.0003 0.0049 123 ARG A CZ 266 N NH1 . ARG A 35 ? 0.1808 0.1813 0.1435 -0.0010 0.0216 -0.0140 123 ARG A NH1 267 N NH2 . ARG A 35 ? 0.2050 0.2179 0.1934 0.0098 0.0226 0.0109 123 ARG A NH2 268 N N . ALA A 36 ? 0.2892 0.3254 0.2690 -0.0088 0.0061 0.0054 124 ALA A N 269 C CA . ALA A 36 ? 0.2874 0.3121 0.2747 0.0004 -0.0001 0.0027 124 ALA A CA 270 C C . ALA A 36 ? 0.2787 0.3057 0.2727 0.0022 0.0056 0.0146 124 ALA A C 271 O O . ALA A 36 ? 0.2571 0.3396 0.2669 0.0101 -0.0027 0.0250 124 ALA A O 272 C CB . ALA A 36 ? 0.2953 0.3150 0.2819 -0.0058 0.0011 0.0007 124 ALA A CB 273 N N . ALA A 37 ? 0.2863 0.3182 0.2636 0.0003 0.0046 0.0199 125 ALA A N 274 C CA . ALA A 37 ? 0.2804 0.3008 0.2660 -0.0023 0.0069 0.0098 125 ALA A CA 275 C C . ALA A 37 ? 0.2744 0.3108 0.2742 0.0021 -0.0004 0.0163 125 ALA A C 276 O O . ALA A 37 ? 0.2550 0.3430 0.2534 0.0056 0.0070 0.0398 125 ALA A O 277 C CB . ALA A 37 ? 0.2789 0.3044 0.2656 -0.0044 0.0050 0.0152 125 ALA A CB 278 N N . ALA A 38 ? 0.2680 0.3096 0.2499 -0.0006 0.0023 0.0102 126 ALA A N 279 C CA . ALA A 38 ? 0.2714 0.3049 0.2619 0.0036 0.0016 -0.0016 126 ALA A CA 280 C C . ALA A 38 ? 0.2733 0.3130 0.2612 0.0077 0.0010 0.0039 126 ALA A C 281 O O . ALA A 38 ? 0.2428 0.3330 0.2318 0.0050 0.0103 0.0074 126 ALA A O 282 C CB . ALA A 38 ? 0.2591 0.3031 0.2433 0.0086 0.0042 -0.0017 126 ALA A CB 283 N N . SER A 39 ? 0.2743 0.3112 0.2593 0.0061 0.0068 0.0056 127 SER A N 284 C CA . SER A 39 ? 0.2875 0.3160 0.2806 0.0061 0.0025 0.0000 127 SER A CA 285 C C . SER A 39 ? 0.2767 0.3143 0.2729 0.0086 0.0044 0.0025 127 SER A C 286 O O . SER A 39 ? 0.2843 0.3478 0.2591 0.0211 0.0094 0.0127 127 SER A O 287 C CB . SER A 39 ? 0.3004 0.3226 0.2868 0.0076 0.0030 -0.0024 127 SER A CB 288 O OG . SER A 39 ? 0.3508 0.3438 0.3309 0.0023 0.0020 -0.0063 127 SER A OG 289 N N . ALA A 40 ? 0.2670 0.3004 0.2481 0.0049 0.0011 0.0023 128 ALA A N 290 C CA . ALA A 40 ? 0.2547 0.2777 0.2374 0.0080 0.0038 -0.0055 128 ALA A CA 291 C C . ALA A 40 ? 0.2420 0.2712 0.2218 0.0063 0.0075 0.0002 128 ALA A C 292 O O . ALA A 40 ? 0.2216 0.2746 0.2198 0.0275 0.0217 0.0003 128 ALA A O 293 C CB . ALA A 40 ? 0.2541 0.2815 0.2421 0.0036 0.0053 0.0020 128 ALA A CB 294 N N . VAL A 41 ? 0.2288 0.2687 0.1924 0.0102 0.0066 0.0067 129 VAL A N 295 C CA A VAL A 41 ? 0.2220 0.2495 0.2025 0.0048 0.0053 -0.0004 129 VAL A CA 296 C CA B VAL A 41 ? 0.2246 0.2545 0.2062 0.0041 0.0050 -0.0008 129 VAL A CA 297 C C . VAL A 41 ? 0.2203 0.2727 0.2074 0.0038 0.0038 0.0086 129 VAL A C 298 O O . VAL A 41 ? 0.2028 0.2999 0.1749 0.0144 0.0076 0.0156 129 VAL A O 299 C CB A VAL A 41 ? 0.2261 0.2420 0.2029 -0.0022 0.0084 0.0046 129 VAL A CB 300 C CB B VAL A 41 ? 0.2324 0.2526 0.2142 0.0015 0.0063 0.0030 129 VAL A CB 301 C CG1 A VAL A 41 ? 0.2230 0.2215 0.2021 0.0038 0.0034 0.0026 129 VAL A CG1 302 C CG1 B VAL A 41 ? 0.2301 0.2490 0.2168 0.0021 0.0015 -0.0021 129 VAL A CG1 303 C CG2 A VAL A 41 ? 0.2203 0.2313 0.2065 0.0075 0.0033 0.0098 129 VAL A CG2 304 C CG2 B VAL A 41 ? 0.2200 0.2439 0.2079 0.0027 0.0080 -0.0009 129 VAL A CG2 305 N N . ALA A 42 ? 0.2114 0.2779 0.1979 0.0042 0.0078 0.0033 130 ALA A N 306 C CA . ALA A 42 ? 0.2220 0.2673 0.2198 0.0000 0.0080 0.0002 130 ALA A CA 307 C C . ALA A 42 ? 0.2153 0.2710 0.2212 0.0050 0.0142 -0.0009 130 ALA A C 308 O O . ALA A 42 ? 0.2173 0.3193 0.2277 0.0066 0.0059 -0.0047 130 ALA A O 309 C CB . ALA A 42 ? 0.2197 0.2651 0.2231 0.0003 0.0122 0.0032 130 ALA A CB 310 N N . GLU A 43 ? 0.2139 0.2625 0.2015 0.0075 0.0179 -0.0024 131 GLU A N 311 C CA . GLU A 43 ? 0.2321 0.2617 0.2337 0.0050 0.0054 -0.0021 131 GLU A CA 312 C C . GLU A 43 ? 0.2169 0.2247 0.1950 0.0174 0.0135 -0.0024 131 GLU A C 313 O O . GLU A 43 ? 0.2152 0.2546 0.1751 0.0266 0.0153 -0.0048 131 GLU A O 314 C CB . GLU A 43 ? 0.2462 0.2600 0.2419 0.0134 0.0050 -0.0022 131 GLU A CB 315 C CG . GLU A 43 ? 0.2871 0.3238 0.2921 0.0023 0.0165 0.0061 131 GLU A CG 316 C CD . GLU A 43 ? 0.3174 0.3685 0.3540 0.0103 0.0015 0.0021 131 GLU A CD 317 O OE1 . GLU A 43 ? 0.3730 0.4122 0.3706 0.0099 0.0105 0.0192 131 GLU A OE1 318 O OE2 . GLU A 43 ? 0.3535 0.3837 0.3675 0.0015 0.0027 0.0055 131 GLU A OE2 319 N N . VAL A 44 ? 0.2032 0.2403 0.1836 0.0222 0.0051 0.0038 132 VAL A N 320 C CA . VAL A 44 ? 0.1919 0.2151 0.1719 0.0078 0.0041 -0.0008 132 VAL A CA 321 C C . VAL A 44 ? 0.1794 0.2114 0.1647 0.0185 0.0107 -0.0049 132 VAL A C 322 O O . VAL A 44 ? 0.1760 0.2404 0.1431 0.0145 0.0215 -0.0055 132 VAL A O 323 C CB . VAL A 44 ? 0.1985 0.2238 0.1866 0.0131 0.0042 0.0042 132 VAL A CB 324 C CG1 . VAL A 44 ? 0.2170 0.2458 0.1976 0.0079 0.0048 0.0040 132 VAL A CG1 325 C CG2 . VAL A 44 ? 0.1787 0.2231 0.1867 0.0040 0.0077 0.0048 132 VAL A CG2 326 N N . PRO A 45 ? 0.1694 0.2116 0.1431 0.0145 0.0040 -0.0011 133 PRO A N 327 C CA . PRO A 45 ? 0.1721 0.2081 0.1408 0.0067 0.0042 -0.0117 133 PRO A CA 328 C C . PRO A 45 ? 0.1620 0.1944 0.1522 0.0043 0.0061 -0.0056 133 PRO A C 329 O O . PRO A 45 ? 0.1981 0.2446 0.1839 -0.0139 0.0312 -0.0389 133 PRO A O 330 C CB . PRO A 45 ? 0.1921 0.2164 0.1562 0.0102 0.0084 -0.0084 133 PRO A CB 331 C CG . PRO A 45 ? 0.2078 0.2103 0.1707 0.0091 0.0070 0.0071 133 PRO A CG 332 C CD . PRO A 45 ? 0.1832 0.2306 0.1422 0.0157 0.0058 -0.0001 133 PRO A CD 333 N N . SER A 46 ? 0.1545 0.1871 0.1212 0.0039 0.0099 -0.0076 134 SER A N 334 C CA . SER A 46 ? 0.1404 0.1831 0.1390 0.0076 0.0040 -0.0027 134 SER A CA 335 C C . SER A 46 ? 0.1307 0.1628 0.1203 0.0115 0.0008 -0.0086 134 SER A C 336 O O . SER A 46 ? 0.1319 0.1825 0.1186 0.0149 -0.0008 0.0034 134 SER A O 337 C CB . SER A 46 ? 0.1517 0.1782 0.1379 -0.0080 0.0051 -0.0042 134 SER A CB 338 O OG . SER A 46 ? 0.1821 0.2417 0.1801 -0.0135 0.0207 0.0251 134 SER A OG 339 N N . PHE A 47 ? 0.1146 0.1608 0.1101 0.0138 0.0009 -0.0054 135 PHE A N 340 C CA . PHE A 47 ? 0.1182 0.1209 0.0963 0.0138 -0.0085 0.0058 135 PHE A CA 341 C C . PHE A 47 ? 0.1252 0.1272 0.1006 0.0042 -0.0041 0.0105 135 PHE A C 342 O O . PHE A 47 ? 0.1402 0.1480 0.1279 0.0040 -0.0010 0.0336 135 PHE A O 343 C CB . PHE A 47 ? 0.1132 0.1162 0.0930 0.0054 -0.0052 0.0000 135 PHE A CB 344 C CG . PHE A 47 ? 0.1037 0.1113 0.0918 0.0083 0.0018 0.0017 135 PHE A CG 345 C CD1 . PHE A 47 ? 0.1056 0.1134 0.0860 0.0137 -0.0065 0.0034 135 PHE A CD1 346 C CD2 . PHE A 47 ? 0.1107 0.1027 0.0871 0.0090 -0.0107 -0.0140 135 PHE A CD2 347 C CE1 . PHE A 47 ? 0.1028 0.1321 0.1135 0.0085 -0.0127 0.0131 135 PHE A CE1 348 C CE2 . PHE A 47 ? 0.0972 0.1158 0.0766 0.0206 0.0001 -0.0017 135 PHE A CE2 349 C CZ . PHE A 47 ? 0.0810 0.1397 0.1136 -0.0018 -0.0069 0.0058 135 PHE A CZ 350 N N . GLN A 48 ? 0.1173 0.1125 0.0966 -0.0004 -0.0081 0.0046 136 GLN A N 351 C CA . GLN A 48 ? 0.1204 0.1060 0.1063 -0.0047 -0.0030 0.0080 136 GLN A CA 352 C C . GLN A 48 ? 0.1138 0.1019 0.0975 -0.0016 -0.0065 0.0085 136 GLN A C 353 O O . GLN A 48 ? 0.1512 0.1231 0.1105 -0.0075 0.0140 0.0163 136 GLN A O 354 C CB . GLN A 48 ? 0.1428 0.1442 0.1615 -0.0174 0.0043 -0.0003 136 GLN A CB 355 C CG . GLN A 48 ? 0.1709 0.1900 0.1770 0.0033 -0.0013 0.0019 136 GLN A CG 356 C CD . GLN A 48 ? 0.1912 0.2473 0.1994 0.0073 -0.0008 0.0087 136 GLN A CD 357 O OE1 . GLN A 48 ? 0.2376 0.2806 0.2423 0.0183 0.0255 -0.0081 136 GLN A OE1 358 N NE2 . GLN A 48 ? 0.2298 0.2735 0.2462 -0.0087 -0.0061 0.0122 136 GLN A NE2 359 N N . TRP A 49 ? 0.1118 0.1009 0.1004 0.0000 0.0014 0.0104 137 TRP A N 360 C CA . TRP A 49 ? 0.1106 0.1060 0.0978 0.0007 -0.0061 0.0144 137 TRP A CA 361 C C . TRP A 49 ? 0.1065 0.1070 0.0997 -0.0136 -0.0043 0.0070 137 TRP A C 362 O O . TRP A 49 ? 0.1147 0.1263 0.0989 -0.0129 -0.0075 0.0243 137 TRP A O 363 C CB . TRP A 49 ? 0.1116 0.0980 0.1051 0.0034 -0.0046 0.0086 137 TRP A CB 364 C CG . TRP A 49 ? 0.1229 0.1005 0.0968 0.0047 -0.0090 0.0109 137 TRP A CG 365 C CD1 . TRP A 49 ? 0.1093 0.1057 0.0962 0.0074 -0.0107 0.0217 137 TRP A CD1 366 C CD2 . TRP A 49 ? 0.1155 0.1402 0.1227 -0.0019 -0.0124 0.0051 137 TRP A CD2 367 N NE1 . TRP A 49 ? 0.1242 0.1108 0.1040 -0.0086 -0.0141 0.0195 137 TRP A NE1 368 C CE2 . TRP A 49 ? 0.1280 0.1255 0.1213 0.0087 -0.0205 0.0107 137 TRP A CE2 369 C CE3 . TRP A 49 ? 0.1478 0.1872 0.1586 0.0115 -0.0216 -0.0133 137 TRP A CE3 370 C CZ2 . TRP A 49 ? 0.1391 0.1614 0.1453 0.0028 -0.0214 -0.0029 137 TRP A CZ2 371 C CZ3 . TRP A 49 ? 0.1718 0.2085 0.2031 0.0220 -0.0119 -0.0438 137 TRP A CZ3 372 C CH2 . TRP A 49 ? 0.1366 0.2108 0.1925 0.0214 -0.0101 -0.0222 137 TRP A CH2 373 N N . LEU A 50 ? 0.0941 0.0941 0.0907 -0.0095 -0.0046 0.0109 138 LEU A N 374 C CA . LEU A 50 ? 0.0973 0.0914 0.0831 -0.0055 -0.0015 0.0075 138 LEU A CA 375 C C . LEU A 50 ? 0.1039 0.0959 0.0971 -0.0009 -0.0014 0.0013 138 LEU A C 376 O O . LEU A 50 ? 0.1253 0.1111 0.1013 0.0192 0.0029 0.0094 138 LEU A O 377 C CB . LEU A 50 ? 0.0831 0.0943 0.1120 -0.0073 -0.0073 0.0121 138 LEU A CB 378 C CG . LEU A 50 ? 0.1132 0.0963 0.1064 -0.0097 -0.0178 0.0046 138 LEU A CG 379 C CD1 . LEU A 50 ? 0.1252 0.0959 0.1247 -0.0081 -0.0074 0.0087 138 LEU A CD1 380 C CD2 . LEU A 50 ? 0.1374 0.1061 0.1401 0.0128 0.0017 -0.0067 138 LEU A CD2 381 N N . ASP A 51 ? 0.0978 0.1044 0.0969 -0.0017 -0.0012 0.0048 139 ASP A N 382 C CA . ASP A 51 ? 0.1097 0.1150 0.1213 0.0047 -0.0004 0.0041 139 ASP A CA 383 C C . ASP A 51 ? 0.1148 0.1035 0.1015 0.0040 0.0052 0.0036 139 ASP A C 384 O O . ASP A 51 ? 0.1106 0.1026 0.1301 0.0040 0.0082 0.0076 139 ASP A O 385 C CB . ASP A 51 ? 0.1338 0.1345 0.1248 0.0086 -0.0077 -0.0012 139 ASP A CB 386 C CG . ASP A 51 ? 0.1931 0.1556 0.1764 0.0113 0.0079 0.0116 139 ASP A CG 387 O OD1 . ASP A 51 ? 0.1912 0.2430 0.1987 -0.0020 0.0002 0.0519 139 ASP A OD1 388 O OD2 . ASP A 51 ? 0.2369 0.2126 0.1876 0.0302 0.0069 0.0318 139 ASP A OD2 389 N N . ARG A 52 ? 0.1176 0.1268 0.1175 0.0073 0.0010 -0.0056 140 ARG A N 390 C CA . ARG A 52 ? 0.1167 0.1104 0.1321 0.0078 -0.0016 -0.0015 140 ARG A CA 391 C C . ARG A 52 ? 0.1098 0.1110 0.1178 0.0085 -0.0007 -0.0051 140 ARG A C 392 O O . ARG A 52 ? 0.1239 0.1047 0.1270 0.0081 0.0048 -0.0177 140 ARG A O 393 C CB . ARG A 52 ? 0.1437 0.1286 0.1692 -0.0100 -0.0076 0.0017 140 ARG A CB 394 C CG . ARG A 52 ? 0.2056 0.1955 0.2199 0.0013 -0.0092 0.0162 140 ARG A CG 395 C CD . ARG A 52 ? 0.2626 0.2665 0.2642 -0.0122 0.0046 0.0264 140 ARG A CD 396 N NE . ARG A 52 ? 0.3479 0.3095 0.3221 0.0014 0.0001 0.0086 140 ARG A NE 397 C CZ . ARG A 52 ? 0.3737 0.3834 0.3796 0.0010 0.0046 0.0002 140 ARG A CZ 398 N NH1 . ARG A 52 ? 0.4002 0.4011 0.4064 -0.0051 -0.0024 0.0032 140 ARG A NH1 399 N NH2 . ARG A 52 ? 0.4117 0.3970 0.3897 0.0056 -0.0012 0.0001 140 ARG A NH2 400 N N . ASN A 53 ? 0.0969 0.0875 0.1183 -0.0074 0.0028 0.0019 141 ASN A N 401 C CA . ASN A 53 ? 0.1051 0.0911 0.1262 -0.0010 0.0019 -0.0004 141 ASN A CA 402 C C . ASN A 53 ? 0.0901 0.0863 0.1228 -0.0064 -0.0006 0.0103 141 ASN A C 403 O O . ASN A 53 ? 0.0846 0.0942 0.1281 0.0106 0.0079 -0.0046 141 ASN A O 404 C CB . ASN A 53 ? 0.1039 0.1144 0.1251 0.0053 0.0094 0.0002 141 ASN A CB 405 C CG . ASN A 53 ? 0.1075 0.1079 0.1190 0.0027 0.0060 0.0027 141 ASN A CG 406 O OD1 . ASN A 53 ? 0.1158 0.1027 0.1484 0.0025 0.0049 -0.0019 141 ASN A OD1 407 N ND2 . ASN A 53 ? 0.1127 0.1203 0.1136 0.0056 0.0056 0.0008 141 ASN A ND2 408 N N . VAL A 54 ? 0.0982 0.0927 0.1271 0.0017 0.0072 0.0084 142 VAL A N 409 C CA . VAL A 54 ? 0.1080 0.1041 0.1330 -0.0045 0.0069 0.0065 142 VAL A CA 410 C C . VAL A 54 ? 0.1100 0.1077 0.1151 -0.0008 0.0048 0.0040 142 VAL A C 411 O O . VAL A 54 ? 0.1094 0.1178 0.1373 -0.0009 0.0150 -0.0061 142 VAL A O 412 C CB . VAL A 54 ? 0.1397 0.1310 0.1556 -0.0104 0.0150 0.0107 142 VAL A CB 413 C CG1 . VAL A 54 ? 0.1432 0.1467 0.1824 -0.0079 0.0171 0.0207 142 VAL A CG1 414 C CG2 . VAL A 54 ? 0.1674 0.1732 0.2032 0.0036 0.0203 0.0120 142 VAL A CG2 415 N N . THR A 55 ? 0.0998 0.0989 0.1150 -0.0008 0.0085 0.0018 143 THR A N 416 C CA . THR A 55 ? 0.1085 0.1044 0.1202 -0.0053 0.0059 -0.0012 143 THR A CA 417 C C . THR A 55 ? 0.0847 0.0952 0.1028 -0.0085 0.0072 0.0027 143 THR A C 418 O O . THR A 55 ? 0.1057 0.1040 0.1139 0.0017 -0.0004 0.0021 143 THR A O 419 C CB . THR A 55 ? 0.1220 0.1022 0.1122 -0.0052 0.0071 -0.0038 143 THR A CB 420 O OG1 . THR A 55 ? 0.1012 0.1237 0.1370 -0.0086 0.0042 0.0069 143 THR A OG1 421 C CG2 . THR A 55 ? 0.1349 0.1334 0.1437 0.0033 -0.0016 0.0086 143 THR A CG2 422 N N . VAL A 56 ? 0.0947 0.0769 0.1085 0.0024 0.0029 -0.0022 144 VAL A N 423 C CA . VAL A 56 ? 0.1057 0.0912 0.1161 -0.0096 0.0012 0.0069 144 VAL A CA 424 C C . VAL A 56 ? 0.1188 0.0986 0.1031 0.0033 -0.0016 0.0009 144 VAL A C 425 O O . VAL A 56 ? 0.0960 0.1028 0.1351 -0.0049 0.0106 -0.0070 144 VAL A O 426 C CB . VAL A 56 ? 0.0990 0.0970 0.1175 -0.0018 -0.0017 0.0030 144 VAL A CB 427 C CG1 . VAL A 56 ? 0.1073 0.1188 0.1271 0.0088 0.0117 0.0126 144 VAL A CG1 428 C CG2 . VAL A 56 ? 0.0999 0.0858 0.1142 -0.0050 0.0094 0.0115 144 VAL A CG2 429 N N . ASP A 57 ? 0.1050 0.0910 0.1217 0.0076 0.0021 -0.0026 145 ASP A N 430 C CA . ASP A 57 ? 0.1172 0.1121 0.1289 0.0021 0.0041 0.0000 145 ASP A CA 431 C C . ASP A 57 ? 0.1166 0.1205 0.1266 -0.0008 0.0016 0.0003 145 ASP A C 432 O O . ASP A 57 ? 0.1180 0.1479 0.1385 -0.0044 0.0118 -0.0083 145 ASP A O 433 C CB . ASP A 57 ? 0.1263 0.1345 0.1437 0.0068 0.0073 -0.0075 145 ASP A CB 434 C CG . ASP A 57 ? 0.1293 0.1479 0.1588 0.0026 0.0018 -0.0066 145 ASP A CG 435 O OD1 . ASP A 57 ? 0.1632 0.1850 0.1958 -0.0198 0.0118 0.0219 145 ASP A OD1 436 O OD2 . ASP A 57 ? 0.1755 0.2086 0.1939 0.0135 -0.0061 -0.0331 145 ASP A OD2 437 N N . THR A 58 ? 0.1054 0.1097 0.1188 -0.0079 0.0065 0.0093 146 THR A N 438 C CA . THR A 58 ? 0.1049 0.1136 0.1226 -0.0007 0.0119 0.0044 146 THR A CA 439 C C . THR A 58 ? 0.1117 0.1218 0.1221 0.0000 0.0116 0.0034 146 THR A C 440 O O . THR A 58 ? 0.1250 0.1192 0.1488 -0.0069 0.0101 0.0003 146 THR A O 441 C CB . THR A 58 ? 0.1043 0.1177 0.1290 0.0003 0.0097 -0.0028 146 THR A CB 442 O OG1 . THR A 58 ? 0.1086 0.1130 0.1499 0.0034 0.0114 0.0072 146 THR A OG1 443 C CG2 . THR A 58 ? 0.0975 0.1177 0.1409 -0.0063 0.0104 -0.0003 146 THR A CG2 444 N N . LEU A 59 ? 0.1178 0.1035 0.1283 -0.0023 0.0083 0.0106 147 LEU A N 445 C CA . LEU A 59 ? 0.1280 0.1227 0.1333 -0.0009 0.0009 0.0063 147 LEU A CA 446 C C . LEU A 59 ? 0.1003 0.1080 0.1173 0.0058 -0.0041 -0.0022 147 LEU A C 447 O O . LEU A 59 ? 0.1042 0.1131 0.1230 -0.0054 -0.0010 -0.0071 147 LEU A O 448 C CB . LEU A 59 ? 0.1511 0.1522 0.1604 0.0054 0.0006 0.0060 147 LEU A CB 449 C CG . LEU A 59 ? 0.1920 0.1917 0.2154 0.0011 -0.0115 -0.0024 147 LEU A CG 450 C CD1 . LEU A 59 ? 0.2737 0.2832 0.2595 -0.0063 0.0009 -0.0027 147 LEU A CD1 451 C CD2 . LEU A 59 ? 0.2093 0.2246 0.2338 0.0158 -0.0036 -0.0002 147 LEU A CD2 452 N N . LEU A 60 ? 0.1049 0.0991 0.1166 -0.0037 0.0022 -0.0020 148 LEU A N 453 C CA . LEU A 60 ? 0.1030 0.0988 0.1209 -0.0085 0.0055 0.0005 148 LEU A CA 454 C C . LEU A 60 ? 0.1043 0.0976 0.1035 -0.0039 -0.0019 -0.0015 148 LEU A C 455 O O . LEU A 60 ? 0.1142 0.1083 0.1320 -0.0076 0.0022 -0.0006 148 LEU A O 456 C CB . LEU A 60 ? 0.1005 0.0986 0.1209 0.0015 -0.0018 0.0032 148 LEU A CB 457 C CG . LEU A 60 ? 0.0953 0.1043 0.1216 0.0031 0.0088 0.0045 148 LEU A CG 458 C CD1 . LEU A 60 ? 0.1025 0.1067 0.1193 0.0002 0.0101 0.0067 148 LEU A CD1 459 C CD2 . LEU A 60 ? 0.1085 0.1106 0.1178 -0.0056 0.0031 -0.0033 148 LEU A CD2 460 N N . VAL A 61 ? 0.0945 0.1030 0.1192 -0.0033 -0.0020 0.0023 149 VAL A N 461 C CA . VAL A 61 ? 0.0973 0.1011 0.1276 -0.0040 -0.0013 0.0016 149 VAL A CA 462 C C . VAL A 61 ? 0.1059 0.1157 0.1361 -0.0002 -0.0034 0.0002 149 VAL A C 463 O O . VAL A 61 ? 0.1164 0.1277 0.1353 -0.0010 -0.0033 -0.0017 149 VAL A O 464 C CB . VAL A 61 ? 0.1041 0.0910 0.1280 0.0009 -0.0038 -0.0014 149 VAL A CB 465 C CG1 . VAL A 61 ? 0.1090 0.1183 0.1227 0.0049 -0.0066 0.0023 149 VAL A CG1 466 C CG2 . VAL A 61 ? 0.1145 0.1184 0.1389 -0.0078 -0.0100 0.0056 149 VAL A CG2 467 N N . GLN A 62 ? 0.1280 0.1244 0.1368 -0.0105 0.0000 0.0034 150 GLN A N 468 C CA . GLN A 62 ? 0.1466 0.1312 0.1493 -0.0027 0.0079 -0.0017 150 GLN A CA 469 C C . GLN A 62 ? 0.1417 0.1352 0.1443 0.0013 0.0023 -0.0009 150 GLN A C 470 O O . GLN A 62 ? 0.1600 0.1457 0.1421 -0.0017 0.0037 -0.0086 150 GLN A O 471 C CB . GLN A 62 ? 0.1780 0.1381 0.1592 -0.0078 0.0012 -0.0051 150 GLN A CB 472 C CG . GLN A 62 ? 0.2472 0.2275 0.1952 -0.0056 0.0117 -0.0024 150 GLN A CG 473 C CD . GLN A 62 ? 0.3033 0.2790 0.2971 -0.0110 0.0133 0.0108 150 GLN A CD 474 O OE1 . GLN A 62 ? 0.3548 0.3369 0.3342 -0.0128 0.0050 -0.0119 150 GLN A OE1 475 N NE2 . GLN A 62 ? 0.3537 0.3294 0.3110 -0.0017 -0.0008 0.0085 150 GLN A NE2 476 N N . THR A 63 ? 0.1378 0.1252 0.1473 -0.0004 -0.0008 -0.0024 151 THR A N 477 C CA . THR A 63 ? 0.1450 0.1490 0.1507 -0.0011 -0.0070 0.0016 151 THR A CA 478 C C . THR A 63 ? 0.1231 0.1333 0.1231 0.0009 -0.0014 -0.0035 151 THR A C 479 O O . THR A 63 ? 0.1144 0.1334 0.1293 -0.0020 -0.0021 -0.0127 151 THR A O 480 C CB . THR A 63 ? 0.1424 0.1590 0.1842 0.0076 -0.0198 -0.0006 151 THR A CB 481 O OG1 . THR A 63 ? 0.1895 0.1919 0.2558 0.0109 -0.0207 0.0159 151 THR A OG1 482 C CG2 . THR A 63 ? 0.1879 0.1911 0.2181 0.0005 -0.0102 -0.0080 151 THR A CG2 483 N N . LEU A 64 ? 0.1074 0.1121 0.1223 -0.0052 -0.0014 0.0029 152 LEU A N 484 C CA . LEU A 64 ? 0.1078 0.1062 0.1200 0.0018 -0.0028 -0.0100 152 LEU A CA 485 C C . LEU A 64 ? 0.1176 0.1108 0.1195 0.0021 0.0060 -0.0072 152 LEU A C 486 O O . LEU A 64 ? 0.1215 0.1077 0.1274 -0.0072 0.0103 -0.0139 152 LEU A O 487 C CB . LEU A 64 ? 0.1092 0.0973 0.1172 0.0101 -0.0007 -0.0030 152 LEU A CB 488 C CG . LEU A 64 ? 0.1101 0.1113 0.1255 0.0001 0.0073 0.0083 152 LEU A CG 489 C CD1 . LEU A 64 ? 0.1212 0.1158 0.1272 0.0048 0.0047 -0.0077 152 LEU A CD1 490 C CD2 . LEU A 64 ? 0.1414 0.1403 0.1307 -0.0058 -0.0071 -0.0058 152 LEU A CD2 491 N N . SER A 65 ? 0.1225 0.1239 0.1274 0.0054 0.0050 -0.0087 153 SER A N 492 C CA A SER A 65 ? 0.1353 0.1406 0.1447 -0.0001 0.0073 -0.0018 153 SER A CA 493 C CA B SER A 65 ? 0.1305 0.1358 0.1376 0.0002 0.0060 -0.0007 153 SER A CA 494 C C . SER A 65 ? 0.1370 0.1479 0.1515 -0.0059 0.0064 0.0000 153 SER A C 495 O O . SER A 65 ? 0.1453 0.1614 0.1629 0.0018 0.0161 -0.0150 153 SER A O 496 C CB A SER A 65 ? 0.1395 0.1477 0.1495 0.0001 0.0045 -0.0011 153 SER A CB 497 C CB B SER A 65 ? 0.1301 0.1402 0.1336 0.0015 0.0051 -0.0011 153 SER A CB 498 O OG A SER A 65 ? 0.1647 0.2087 0.2060 -0.0077 0.0143 -0.0178 153 SER A OG 499 O OG B SER A 65 ? 0.1227 0.1502 0.1186 -0.0013 0.0041 0.0036 153 SER A OG 500 N N . GLU A 66 ? 0.1438 0.1635 0.1481 -0.0086 0.0086 -0.0023 154 GLU A N 501 C CA . GLU A 66 ? 0.1550 0.1744 0.1552 -0.0060 0.0107 -0.0091 154 GLU A CA 502 C C . GLU A 66 ? 0.1413 0.1579 0.1481 -0.0056 0.0067 -0.0074 154 GLU A C 503 O O . GLU A 66 ? 0.1600 0.1886 0.1534 -0.0042 0.0151 -0.0129 154 GLU A O 504 C CB . GLU A 66 ? 0.1920 0.2056 0.1610 -0.0058 0.0010 -0.0054 154 GLU A CB 505 C CG . GLU A 66 ? 0.2321 0.2272 0.2279 -0.0135 0.0074 0.0005 154 GLU A CG 506 C CD . GLU A 66 ? 0.3404 0.3034 0.3374 0.0070 -0.0087 0.0151 154 GLU A CD 507 O OE1 . GLU A 66 ? 0.3554 0.3793 0.4186 0.0013 -0.0151 0.0120 154 GLU A OE1 508 O OE2 . GLU A 66 ? 0.3609 0.3605 0.4010 -0.0208 0.0038 0.0083 154 GLU A OE2 509 N N . ILE A 67 ? 0.1334 0.1482 0.1268 0.0012 0.0061 -0.0092 155 ILE A N 510 C CA . ILE A 67 ? 0.1264 0.1426 0.1193 0.0003 -0.0014 -0.0110 155 ILE A CA 511 C C . ILE A 67 ? 0.1271 0.1321 0.1376 -0.0035 0.0007 -0.0111 155 ILE A C 512 O O . ILE A 67 ? 0.1379 0.1489 0.1422 -0.0016 0.0066 -0.0275 155 ILE A O 513 C CB . ILE A 67 ? 0.1218 0.1415 0.1034 -0.0053 0.0059 -0.0104 155 ILE A CB 514 C CG1 . ILE A 67 ? 0.1293 0.1379 0.1136 -0.0119 -0.0065 -0.0036 155 ILE A CG1 515 C CG2 . ILE A 67 ? 0.1448 0.1514 0.1021 -0.0129 0.0009 -0.0186 155 ILE A CG2 516 C CD1 . ILE A 67 ? 0.1349 0.1580 0.1217 -0.0041 0.0016 0.0038 155 ILE A CD1 517 N N . ARG A 68 ? 0.1343 0.1306 0.1236 0.0018 0.0015 -0.0093 156 ARG A N 518 C CA . ARG A 68 ? 0.1386 0.1421 0.1363 0.0030 -0.0009 -0.0151 156 ARG A CA 519 C C . ARG A 68 ? 0.1554 0.1630 0.1435 0.0024 0.0017 -0.0105 156 ARG A C 520 O O . ARG A 68 ? 0.1472 0.1589 0.1540 0.0023 0.0056 -0.0123 156 ARG A O 521 C CB . ARG A 68 ? 0.1376 0.1381 0.1231 0.0098 -0.0063 -0.0070 156 ARG A CB 522 C CG . ARG A 68 ? 0.1539 0.1705 0.1557 0.0080 0.0024 -0.0016 156 ARG A CG 523 C CD . ARG A 68 ? 0.1559 0.1729 0.1719 0.0028 0.0013 -0.0144 156 ARG A CD 524 N NE . ARG A 68 ? 0.1429 0.1800 0.1748 0.0161 0.0094 -0.0034 156 ARG A NE 525 C CZ . ARG A 68 ? 0.1615 0.1686 0.1634 0.0099 0.0038 -0.0032 156 ARG A CZ 526 N NH1 . ARG A 68 ? 0.1603 0.1867 0.1553 0.0024 0.0051 -0.0138 156 ARG A NH1 527 N NH2 . ARG A 68 ? 0.1286 0.1440 0.1651 0.0010 0.0020 -0.0253 156 ARG A NH2 528 N N . GLU A 69 ? 0.1554 0.1702 0.1525 0.0025 0.0143 -0.0151 157 GLU A N 529 C CA . GLU A 69 ? 0.1741 0.1949 0.1710 0.0033 0.0147 -0.0188 157 GLU A CA 530 C C . GLU A 69 ? 0.1676 0.1951 0.1758 0.0003 0.0062 -0.0094 157 GLU A C 531 O O . GLU A 69 ? 0.1801 0.2069 0.1905 0.0117 0.0154 -0.0218 157 GLU A O 532 C CB . GLU A 69 ? 0.2033 0.2041 0.1990 -0.0008 0.0066 -0.0083 157 GLU A CB 533 C CG . GLU A 69 ? 0.2735 0.2850 0.2471 0.0022 0.0206 -0.0149 157 GLU A CG 534 C CD . GLU A 69 ? 0.3040 0.3229 0.3107 -0.0048 -0.0005 -0.0018 157 GLU A CD 535 O OE1 . GLU A 69 ? 0.3364 0.3330 0.3493 0.0088 -0.0071 0.0034 157 GLU A OE1 536 O OE2 . GLU A 69 ? 0.3350 0.3164 0.3272 0.0028 0.0065 0.0021 157 GLU A OE2 537 N N . ALA A 70 ? 0.1636 0.1908 0.1649 0.0005 0.0059 -0.0121 158 ALA A N 538 C CA . ALA A 70 ? 0.1699 0.1969 0.1581 0.0009 0.0050 -0.0131 158 ALA A CA 539 C C . ALA A 70 ? 0.1818 0.2003 0.1687 -0.0058 0.0018 -0.0127 158 ALA A C 540 O O . ALA A 70 ? 0.1903 0.2132 0.1844 -0.0091 0.0232 -0.0304 158 ALA A O 541 C CB . ALA A 70 ? 0.1847 0.2029 0.1704 0.0003 -0.0035 -0.0006 158 ALA A CB 542 N N . ASN A 71 ? 0.1533 0.1872 0.1485 -0.0030 0.0131 -0.0180 159 ASN A N 543 C CA . ASN A 71 ? 0.1709 0.1828 0.1600 -0.0038 0.0030 -0.0204 159 ASN A CA 544 C C . ASN A 71 ? 0.1877 0.1922 0.1918 -0.0038 0.0028 -0.0174 159 ASN A C 545 O O . ASN A 71 ? 0.2018 0.1938 0.2224 -0.0054 0.0139 -0.0222 159 ASN A O 546 C CB . ASN A 71 ? 0.1641 0.1722 0.1486 -0.0017 0.0005 -0.0110 159 ASN A CB 547 C CG . ASN A 71 ? 0.1680 0.1529 0.1485 0.0031 0.0010 -0.0098 159 ASN A CG 548 O OD1 . ASN A 71 ? 0.1463 0.1944 0.1575 0.0015 0.0165 -0.0327 159 ASN A OD1 549 N ND2 . ASN A 71 ? 0.1650 0.1676 0.1593 0.0040 0.0148 -0.0294 159 ASN A ND2 550 N N . GLN A 72 ? 0.1983 0.2056 0.1973 -0.0035 -0.0006 -0.0208 160 GLN A N 551 C CA . GLN A 72 ? 0.2108 0.2238 0.2226 -0.0023 0.0041 -0.0084 160 GLN A CA 552 C C . GLN A 72 ? 0.2236 0.2353 0.2326 -0.0017 0.0048 -0.0118 160 GLN A C 553 O O . GLN A 72 ? 0.2567 0.2603 0.2600 0.0114 0.0153 -0.0265 160 GLN A O 554 C CB . GLN A 72 ? 0.2116 0.2124 0.2100 0.0003 0.0019 -0.0046 160 GLN A CB 555 C CG . GLN A 72 ? 0.2350 0.2485 0.2230 0.0024 0.0086 -0.0073 160 GLN A CG 556 C CD . GLN A 72 ? 0.2789 0.3106 0.2794 -0.0040 -0.0094 -0.0065 160 GLN A CD 557 O OE1 . GLN A 72 ? 0.3378 0.3603 0.3343 -0.0149 0.0040 -0.0074 160 GLN A OE1 558 N NE2 . GLN A 72 ? 0.2980 0.3191 0.2979 0.0186 -0.0078 -0.0003 160 GLN A NE2 559 N N . ALA A 73 ? 0.2396 0.2670 0.2493 0.0039 0.0081 -0.0136 161 ALA A N 560 C CA . ALA A 73 ? 0.2699 0.2908 0.2644 0.0031 0.0093 -0.0142 161 ALA A CA 561 C C . ALA A 73 ? 0.2941 0.3068 0.2794 -0.0049 0.0083 -0.0144 161 ALA A C 562 O O . ALA A 73 ? 0.3216 0.3448 0.2914 0.0067 0.0201 -0.0370 161 ALA A O 563 C CB . ALA A 73 ? 0.2799 0.2952 0.2615 0.0016 0.0142 -0.0152 161 ALA A CB 564 N N . GLY A 74 ? 0.3011 0.3174 0.3008 -0.0042 0.0081 -0.0166 162 GLY A N 565 C CA . GLY A 74 ? 0.3027 0.3141 0.3029 -0.0025 0.0039 -0.0151 162 GLY A CA 566 C C . GLY A 74 ? 0.3061 0.3184 0.3138 0.0006 0.0012 -0.0144 162 GLY A C 567 O O . GLY A 74 ? 0.3014 0.3478 0.3121 0.0000 0.0038 -0.0347 162 GLY A O 568 N N . ALA A 75 ? 0.2995 0.3153 0.2963 0.0015 0.0008 -0.0179 163 ALA A N 569 C CA . ALA A 75 ? 0.2983 0.3094 0.2952 -0.0016 0.0038 -0.0141 163 ALA A CA 570 C C . ALA A 75 ? 0.2993 0.3055 0.2978 0.0032 0.0059 -0.0172 163 ALA A C 571 O O . ALA A 75 ? 0.2873 0.3023 0.2778 -0.0017 0.0071 -0.0407 163 ALA A O 572 C CB . ALA A 75 ? 0.2940 0.3082 0.2995 -0.0038 0.0010 -0.0110 163 ALA A CB 573 N N . ASN A 76 ? 0.3010 0.3154 0.2932 0.0000 0.0080 -0.0229 164 ASN A N 574 C CA . ASN A 76 ? 0.3134 0.3165 0.3098 0.0016 0.0060 -0.0150 164 ASN A CA 575 C C . ASN A 76 ? 0.3039 0.3229 0.3035 -0.0027 0.0050 -0.0137 164 ASN A C 576 O O . ASN A 76 ? 0.3161 0.3570 0.3082 -0.0067 0.0020 -0.0180 164 ASN A O 577 C CB . ASN A 76 ? 0.3225 0.3180 0.3163 0.0023 0.0077 -0.0160 164 ASN A CB 578 C CG . ASN A 76 ? 0.3590 0.3408 0.3458 -0.0107 -0.0006 -0.0085 164 ASN A CG 579 O OD1 . ASN A 76 ? 0.3803 0.3553 0.3598 -0.0099 0.0153 -0.0216 164 ASN A OD1 580 N ND2 . ASN A 76 ? 0.4065 0.3789 0.3692 -0.0072 0.0004 -0.0226 164 ASN A ND2 581 N N . PRO A 77 ? 0.2797 0.2994 0.2803 -0.0016 0.0038 -0.0192 165 PRO A N 582 C CA . PRO A 77 ? 0.2553 0.2681 0.2665 -0.0036 0.0030 -0.0174 165 PRO A CA 583 C C . PRO A 77 ? 0.2186 0.2170 0.2181 0.0066 0.0078 -0.0233 165 PRO A C 584 O O . PRO A 77 ? 0.2327 0.2413 0.1974 -0.0119 0.0007 -0.0511 165 PRO A O 585 C CB . PRO A 77 ? 0.2609 0.2754 0.2686 -0.0045 0.0053 -0.0209 165 PRO A CB 586 C CG . PRO A 77 ? 0.2850 0.3054 0.2951 0.0045 0.0094 -0.0063 165 PRO A CG 587 C CD . PRO A 77 ? 0.2959 0.3106 0.2914 0.0013 -0.0002 -0.0168 165 PRO A CD 588 N N . GLN A 78 ? 0.2024 0.1940 0.2300 -0.0018 0.0014 -0.0279 166 GLN A N 589 C CA . GLN A 78 ? 0.1909 0.1840 0.2027 0.0000 0.0067 -0.0274 166 GLN A CA 590 C C . GLN A 78 ? 0.1641 0.1731 0.1706 0.0023 0.0088 -0.0251 166 GLN A C 591 O O . GLN A 78 ? 0.1697 0.1641 0.1485 -0.0048 0.0084 -0.0564 166 GLN A O 592 C CB . GLN A 78 ? 0.1832 0.2049 0.2142 0.0024 0.0083 -0.0160 166 GLN A CB 593 C CG . GLN A 78 ? 0.2490 0.2301 0.2636 0.0040 0.0008 -0.0009 166 GLN A CG 594 C CD . GLN A 78 ? 0.2573 0.2761 0.2506 -0.0008 -0.0051 -0.0091 166 GLN A CD 595 O OE1 . GLN A 78 ? 0.2547 0.2993 0.2697 -0.0012 -0.0044 -0.0034 166 GLN A OE1 596 N NE2 . GLN A 78 ? 0.2911 0.2952 0.2994 0.0061 0.0082 -0.0240 166 GLN A NE2 597 N N . TYR A 79 ? 0.1372 0.1572 0.1400 -0.0019 0.0070 -0.0349 167 TYR A N 598 C CA . TYR A 79 ? 0.1455 0.1609 0.1301 0.0015 -0.0041 -0.0094 167 TYR A CA 599 C C . TYR A 79 ? 0.1371 0.1493 0.1219 0.0018 -0.0075 -0.0149 167 TYR A C 601 C CB . TYR A 79 ? 0.1629 0.1750 0.1405 -0.0100 -0.0073 -0.0116 167 TYR A CB 602 C CG . TYR A 79 ? 0.2044 0.2278 0.1797 -0.0094 -0.0040 -0.0016 167 TYR A CG 603 C CD1 . TYR A 79 ? 0.2395 0.2611 0.2007 0.0020 0.0019 0.0006 167 TYR A CD1 604 C CD2 . TYR A 79 ? 0.2393 0.2662 0.2056 -0.0031 0.0018 -0.0108 167 TYR A CD2 605 C CE1 . TYR A 79 ? 0.2790 0.3078 0.2265 -0.0053 -0.0031 0.0105 167 TYR A CE1 606 C CE2 . TYR A 79 ? 0.2701 0.3153 0.2263 -0.0087 0.0116 -0.0113 167 TYR A CE2 607 C CZ . TYR A 79 ? 0.2964 0.3127 0.2159 -0.0008 0.0011 -0.0064 167 TYR A CZ 608 O OH . TYR A 79 ? 0.3455 0.3760 0.2168 -0.0093 -0.0022 0.0295 167 TYR A OH 609 N N . ALA A 80 ? 0.1350 0.1429 0.1074 0.0112 -0.0098 -0.0078 168 ALA A N 610 C CA . ALA A 80 ? 0.1269 0.1206 0.0963 0.0032 -0.0056 -0.0056 168 ALA A CA 611 C C . ALA A 80 ? 0.1188 0.1124 0.0896 0.0047 -0.0071 0.0073 168 ALA A C 612 O O . ALA A 80 ? 0.1539 0.1253 0.0852 0.0042 -0.0076 0.0057 168 ALA A O 613 C CB . ALA A 80 ? 0.1383 0.1305 0.1094 -0.0030 -0.0058 -0.0103 168 ALA A CB 614 N N . ALA A 81 ? 0.1112 0.0979 0.0913 0.0123 0.0037 -0.0057 169 ALA A N 615 C CA . ALA A 81 ? 0.1033 0.1022 0.1034 -0.0026 0.0046 0.0007 169 ALA A CA 616 C C . ALA A 81 ? 0.1057 0.0929 0.0950 0.0063 0.0029 -0.0041 169 ALA A C 617 O O . ALA A 81 ? 0.1100 0.0937 0.1002 0.0181 0.0061 0.0080 169 ALA A O 618 C CB . ALA A 81 ? 0.1066 0.1093 0.1157 0.0068 -0.0019 0.0000 169 ALA A CB 619 N N . GLN A 82 ? 0.1009 0.0893 0.0884 0.0096 0.0005 0.0016 170 GLN A N 620 C CA . GLN A 82 ? 0.0908 0.0856 0.0893 0.0056 0.0018 0.0067 170 GLN A CA 621 C C . GLN A 82 ? 0.0814 0.0912 0.0958 0.0058 -0.0036 0.0064 170 GLN A C 622 O O . GLN A 82 ? 0.1032 0.1037 0.0856 0.0032 0.0003 0.0062 170 GLN A O 623 C CB . GLN A 82 ? 0.0971 0.0977 0.0951 0.0109 -0.0026 0.0000 170 GLN A CB 624 C CG . GLN A 82 ? 0.1161 0.1216 0.1015 0.0109 0.0052 -0.0082 170 GLN A CG 625 C CD . GLN A 82 ? 0.1260 0.1555 0.1155 0.0032 -0.0014 -0.0134 170 GLN A CD 626 O OE1 . GLN A 82 ? 0.1313 0.1799 0.1115 0.0167 -0.0173 -0.0112 170 GLN A OE1 627 N NE2 . GLN A 82 ? 0.1496 0.1822 0.1327 0.0114 0.0246 -0.0141 170 GLN A NE2 628 N N . ILE A 83 ? 0.0970 0.0887 0.0922 0.0069 -0.0062 -0.0025 171 ILE A N 629 C CA . ILE A 83 ? 0.0904 0.0793 0.0873 -0.0041 -0.0012 0.0037 171 ILE A CA 630 C C . ILE A 83 ? 0.0832 0.0811 0.0760 -0.0044 -0.0028 0.0061 171 ILE A C 631 O O . ILE A 83 ? 0.1006 0.0918 0.0887 -0.0061 0.0122 0.0047 171 ILE A O 632 C CB . ILE A 83 ? 0.0969 0.1065 0.1082 0.0014 -0.0011 -0.0034 171 ILE A CB 633 C CG1 . ILE A 83 ? 0.1206 0.1504 0.1335 0.0098 -0.0097 -0.0066 171 ILE A CG1 634 C CG2 . ILE A 83 ? 0.1151 0.1144 0.1429 0.0106 -0.0100 -0.0015 171 ILE A CG2 635 C CD1 . ILE A 83 ? 0.1604 0.2035 0.1754 0.0094 -0.0066 0.0103 171 ILE A CD1 636 N N . VAL A 84 ? 0.0810 0.0818 0.0708 -0.0005 -0.0011 0.0052 172 VAL A N 637 C CA . VAL A 84 ? 0.0843 0.0781 0.0852 0.0031 0.0013 0.0101 172 VAL A CA 638 C C . VAL A 84 ? 0.0752 0.0809 0.0755 -0.0032 -0.0010 0.0108 172 VAL A C 639 O O . VAL A 84 ? 0.1032 0.0866 0.0808 -0.0123 -0.0050 0.0097 172 VAL A O 640 C CB . VAL A 84 ? 0.0872 0.0969 0.0978 0.0072 -0.0035 0.0167 172 VAL A CB 641 C CG1 . VAL A 84 ? 0.1138 0.1089 0.0913 0.0214 -0.0097 0.0117 172 VAL A CG1 642 C CG2 . VAL A 84 ? 0.1036 0.0919 0.0896 0.0118 0.0016 0.0119 172 VAL A CG2 643 N N . VAL A 85 ? 0.0824 0.0755 0.0720 -0.0142 -0.0039 0.0010 173 VAL A N 644 C CA . VAL A 85 ? 0.0884 0.0824 0.0760 -0.0032 -0.0055 -0.0012 173 VAL A CA 645 C C . VAL A 85 ? 0.0904 0.0832 0.0650 -0.0106 -0.0059 -0.0121 173 VAL A C 646 O O . VAL A 85 ? 0.1013 0.0869 0.1154 -0.0131 0.0104 -0.0055 173 VAL A O 647 C CB . VAL A 85 ? 0.0950 0.0956 0.0824 -0.0027 -0.0166 0.0000 173 VAL A CB 648 C CG1 . VAL A 85 ? 0.1330 0.1045 0.0860 -0.0044 -0.0007 0.0026 173 VAL A CG1 649 C CG2 . VAL A 85 ? 0.1128 0.1082 0.0809 0.0055 -0.0110 0.0045 173 VAL A CG2 650 N N . TYR A 86 ? 0.0873 0.0748 0.0922 -0.0094 0.0088 0.0009 174 TYR A N 651 C CA . TYR A 86 ? 0.1060 0.0969 0.0938 -0.0042 0.0026 -0.0013 174 TYR A CA 652 C C . TYR A 86 ? 0.1142 0.0912 0.0938 -0.0090 -0.0028 0.0059 174 TYR A C 653 O O . TYR A 86 ? 0.1172 0.0878 0.1030 -0.0121 0.0029 0.0011 174 TYR A O 654 C CB . TYR A 86 ? 0.1107 0.0974 0.1000 -0.0051 0.0103 0.0024 174 TYR A CB 655 C CG . TYR A 86 ? 0.1182 0.0992 0.0940 -0.0091 -0.0005 0.0125 174 TYR A CG 656 C CD1 . TYR A 86 ? 0.1063 0.1014 0.1201 0.0060 0.0050 0.0154 174 TYR A CD1 657 C CD2 . TYR A 86 ? 0.1648 0.1517 0.1118 0.0263 0.0056 0.0226 174 TYR A CD2 658 C CE1 . TYR A 86 ? 0.1226 0.1192 0.1402 0.0023 0.0068 0.0034 174 TYR A CE1 659 C CE2 . TYR A 86 ? 0.1983 0.1651 0.1506 0.0359 0.0150 0.0256 174 TYR A CE2 660 C CZ . TYR A 86 ? 0.1442 0.1501 0.1499 0.0273 -0.0038 0.0132 174 TYR A CZ 661 O OH . TYR A 86 ? 0.1873 0.1809 0.1744 0.0432 -0.0222 0.0057 174 TYR A OH 662 N N . ASP A 87 ? 0.1047 0.0879 0.0862 -0.0160 -0.0018 0.0007 175 ASP A N 663 C CA . ASP A 87 ? 0.1007 0.0820 0.0958 -0.0096 -0.0008 -0.0040 175 ASP A CA 664 C C . ASP A 87 ? 0.0904 0.0715 0.0887 0.0016 -0.0001 0.0154 175 ASP A C 665 O O . ASP A 87 ? 0.1067 0.0771 0.0955 0.0017 0.0038 0.0064 175 ASP A O 666 C CB . ASP A 87 ? 0.1089 0.0863 0.1070 -0.0017 0.0141 0.0076 175 ASP A CB 667 C CG . ASP A 87 ? 0.1084 0.0961 0.1096 -0.0001 0.0023 -0.0176 175 ASP A CG 668 O OD1 . ASP A 87 ? 0.1090 0.1130 0.1345 -0.0020 0.0151 0.0012 175 ASP A OD1 669 O OD2 . ASP A 87 ? 0.1115 0.1312 0.1419 0.0069 0.0197 -0.0116 175 ASP A OD2 670 N N . LEU A 88 ? 0.0906 0.0771 0.0952 0.0002 -0.0039 0.0032 176 LEU A N 671 C CA . LEU A 88 ? 0.0836 0.0641 0.0877 -0.0024 -0.0018 0.0028 176 LEU A CA 672 C C . LEU A 88 ? 0.0973 0.0703 0.0873 -0.0020 -0.0065 0.0077 176 LEU A C 673 O O . LEU A 88 ? 0.1085 0.0832 0.0941 0.0040 -0.0163 0.0134 176 LEU A O 674 C CB . LEU A 88 ? 0.0842 0.0581 0.0860 -0.0007 -0.0045 0.0030 176 LEU A CB 675 C CG . LEU A 88 ? 0.0885 0.0639 0.0933 -0.0124 -0.0015 -0.0013 176 LEU A CG 676 C CD1 . LEU A 88 ? 0.1076 0.1058 0.1225 -0.0122 -0.0045 0.0017 176 LEU A CD1 677 C CD2 . LEU A 88 ? 0.1025 0.0977 0.1247 -0.0022 0.0031 0.0059 176 LEU A CD2 678 N N . PRO A 89 ? 0.0882 0.0581 0.0868 0.0048 -0.0078 -0.0042 177 PRO A N 679 C CA . PRO A 89 ? 0.1042 0.0731 0.1128 -0.0099 0.0024 0.0002 177 PRO A CA 680 C C . PRO A 89 ? 0.1041 0.0783 0.1228 -0.0083 -0.0002 -0.0001 177 PRO A C 681 O O . PRO A 89 ? 0.1157 0.0959 0.1430 -0.0063 0.0087 -0.0038 177 PRO A O 682 C CB . PRO A 89 ? 0.1062 0.0733 0.1193 -0.0034 -0.0019 -0.0059 177 PRO A CB 683 C CG . PRO A 89 ? 0.0941 0.0623 0.0972 -0.0067 -0.0050 0.0005 177 PRO A CG 684 C CD . PRO A 89 ? 0.0971 0.0722 0.0961 0.0070 -0.0048 0.0032 177 PRO A CD 685 N N . ASP A 90 ? 0.1105 0.0800 0.1339 0.0043 0.0037 -0.0061 178 ASP A N 686 C CA . ASP A 90 ? 0.1146 0.0986 0.1269 0.0091 0.0007 0.0054 178 ASP A CA 687 C C . ASP A 90 ? 0.1179 0.0878 0.1385 0.0063 0.0011 -0.0019 178 ASP A C 688 O O . ASP A 90 ? 0.1122 0.1068 0.1351 -0.0002 0.0097 0.0022 178 ASP A O 689 C CB . ASP A 90 ? 0.1289 0.1083 0.1348 -0.0035 0.0042 -0.0028 178 ASP A CB 690 C CG . ASP A 90 ? 0.1385 0.1367 0.1553 -0.0052 0.0007 0.0019 178 ASP A CG 691 O OD1 . ASP A 90 ? 0.1183 0.1336 0.1736 -0.0130 -0.0035 -0.0010 178 ASP A OD1 692 O OD2 . ASP A 90 ? 0.1772 0.1581 0.2005 -0.0004 0.0244 -0.0278 178 ASP A OD2 693 N N . ARG A 91 ? 0.1070 0.0983 0.1173 -0.0083 -0.0052 0.0080 179 ARG A N 694 C CA . ARG A 91 ? 0.1025 0.0888 0.1105 0.0054 -0.0006 0.0043 179 ARG A CA 695 C C . ARG A 91 ? 0.1097 0.0973 0.1153 0.0014 -0.0058 0.0181 179 ARG A C 696 O O . ARG A 91 ? 0.1109 0.1024 0.1394 0.0034 -0.0123 0.0080 179 ARG A O 697 C CB . ARG A 91 ? 0.1076 0.0943 0.1017 -0.0045 0.0071 0.0123 179 ARG A CB 698 C CG . ARG A 91 ? 0.1057 0.0921 0.1206 -0.0003 0.0025 0.0056 179 ARG A CG 699 C CD . ARG A 91 ? 0.1151 0.0966 0.1119 -0.0095 0.0033 0.0041 179 ARG A CD 700 N NE . ARG A 91 ? 0.1151 0.0930 0.1223 0.0074 0.0030 0.0098 179 ARG A NE 701 C CZ . ARG A 91 ? 0.1269 0.1028 0.1117 0.0008 0.0100 0.0145 179 ARG A CZ 702 N NH1 . ARG A 91 ? 0.1286 0.1140 0.1255 -0.0160 0.0104 0.0160 179 ARG A NH1 703 N NH2 . ARG A 91 ? 0.1758 0.1422 0.1404 -0.0015 -0.0037 0.0183 179 ARG A NH2 704 N N . ASP A 92 ? 0.1132 0.1082 0.1189 0.0038 -0.0076 0.0115 180 ASP A N 705 C CA . ASP A 92 ? 0.1074 0.1325 0.1346 0.0097 0.0002 0.0054 180 ASP A CA 706 C C . ASP A 92 ? 0.1162 0.1217 0.1399 0.0059 0.0071 0.0059 180 ASP A C 707 O O . ASP A 92 ? 0.1361 0.1187 0.1760 0.0112 0.0105 0.0195 180 ASP A O 708 C CB . ASP A 92 ? 0.1133 0.1257 0.1389 0.0053 -0.0024 0.0019 180 ASP A CB 709 C CG . ASP A 92 ? 0.1399 0.1341 0.1416 0.0020 -0.0004 -0.0027 180 ASP A CG 710 O OD1 . ASP A 92 ? 0.1336 0.1407 0.1767 -0.0137 0.0211 -0.0023 180 ASP A OD1 711 O OD2 . ASP A 92 ? 0.1421 0.1505 0.1801 0.0096 -0.0001 0.0164 180 ASP A OD2 712 N N . CYS A 93 ? 0.1271 0.1185 0.1358 -0.0052 0.0047 0.0098 181 CYS A N 713 C CA . CYS A 93 ? 0.1364 0.1278 0.1562 -0.0052 0.0057 -0.0041 181 CYS A CA 714 C C . CYS A 93 ? 0.1471 0.1512 0.1690 -0.0029 0.0047 0.0044 181 CYS A C 715 O O . CYS A 93 ? 0.1650 0.1476 0.1831 0.0011 0.0015 -0.0157 181 CYS A O 716 C CB . CYS A 93 ? 0.1478 0.1290 0.1682 -0.0005 0.0026 -0.0022 181 CYS A CB 717 S SG . CYS A 93 ? 0.1979 0.1585 0.2025 -0.0317 0.0280 -0.0009 181 CYS A SG 718 N N . ALA A 94 ? 0.1457 0.1327 0.1672 0.0143 0.0025 -0.0097 182 ALA A N 719 C CA . ALA A 94 ? 0.1500 0.1639 0.1908 0.0105 -0.0047 -0.0020 182 ALA A CA 720 C C . ALA A 94 ? 0.1785 0.1810 0.2183 0.0077 -0.0040 0.0078 182 ALA A C 721 O O . ALA A 94 ? 0.1844 0.2201 0.2815 0.0152 -0.0122 0.0227 182 ALA A O 722 C CB . ALA A 94 ? 0.1575 0.1648 0.1941 0.0093 -0.0100 -0.0064 182 ALA A CB 723 N N . ALA A 95 ? 0.1976 0.2151 0.2213 -0.0005 0.0001 0.0073 183 ALA A N 724 C CA . ALA A 95 ? 0.2213 0.2096 0.2221 0.0044 -0.0010 0.0050 183 ALA A CA 725 C C . ALA A 95 ? 0.2358 0.2178 0.2343 -0.0057 -0.0017 0.0081 183 ALA A C 726 O O . ALA A 95 ? 0.2535 0.2019 0.2387 -0.0168 -0.0029 0.0192 183 ALA A O 727 C CB . ALA A 95 ? 0.2230 0.2179 0.2182 0.0072 0.0081 0.0162 183 ALA A CB 728 N N . ALA A 96 ? 0.2422 0.2310 0.2454 -0.0011 -0.0069 0.0060 184 ALA A N 729 C CA . ALA A 96 ? 0.2482 0.2366 0.2503 -0.0004 -0.0015 -0.0003 184 ALA A CA 730 C C . ALA A 96 ? 0.2505 0.2373 0.2524 -0.0013 -0.0012 -0.0012 184 ALA A C 731 O O . ALA A 96 ? 0.2680 0.2483 0.2874 -0.0145 -0.0040 -0.0120 184 ALA A O 732 C CB . ALA A 96 ? 0.2576 0.2398 0.2587 0.0075 -0.0029 0.0028 184 ALA A CB 733 N N . ALA A 97 ? 0.2245 0.2173 0.2496 -0.0039 0.0049 0.0053 185 ALA A N 734 C CA . ALA A 97 ? 0.2048 0.2007 0.2245 -0.0027 -0.0057 0.0061 185 ALA A CA 735 C C . ALA A 97 ? 0.2045 0.1931 0.2323 -0.0048 -0.0086 0.0012 185 ALA A C 736 O O . ALA A 97 ? 0.2037 0.2121 0.2488 -0.0107 -0.0198 -0.0075 185 ALA A O 737 C CB . ALA A 97 ? 0.2223 0.1983 0.2319 -0.0028 -0.0058 0.0052 185 ALA A CB 738 N N . SER A 98 ? 0.2003 0.1811 0.2229 -0.0058 -0.0083 0.0096 186 SER A N 739 C CA . SER A 98 ? 0.1905 0.1838 0.2041 0.0009 -0.0043 0.0105 186 SER A CA 740 C C . SER A 98 ? 0.1863 0.1772 0.1819 -0.0039 -0.0107 0.0130 186 SER A C 741 O O . SER A 98 ? 0.2216 0.2007 0.2449 -0.0173 -0.0216 0.0139 186 SER A O 742 C CB . SER A 98 ? 0.1917 0.1840 0.2073 0.0029 -0.0032 0.0121 186 SER A CB 743 O OG . SER A 98 ? 0.1716 0.1803 0.2224 0.0034 0.0134 0.0503 186 SER A OG 744 N N . ASN A 99 ? 0.1761 0.1696 0.1753 -0.0060 -0.0135 0.0134 187 ASN A N 745 C CA . ASN A 99 ? 0.1854 0.1837 0.1943 -0.0007 -0.0014 0.0074 187 ASN A CA 746 C C . ASN A 99 ? 0.1630 0.1711 0.1741 -0.0026 -0.0008 0.0057 187 ASN A C 747 O O . ASN A 99 ? 0.1773 0.2243 0.1919 -0.0090 0.0007 0.0144 187 ASN A O 748 C CB . ASN A 99 ? 0.1881 0.2163 0.1953 0.0024 0.0112 0.0209 187 ASN A CB 749 C CG . ASN A 99 ? 0.2433 0.2739 0.2723 0.0162 -0.0042 0.0153 187 ASN A CG 750 O OD1 . ASN A 99 ? 0.2870 0.2879 0.3212 -0.0137 0.0183 0.0421 187 ASN A OD1 751 N ND2 . ASN A 99 ? 0.3276 0.3737 0.2810 0.0208 -0.0064 0.0137 187 ASN A ND2 752 N N . GLY A 100 ? 0.1365 0.1554 0.1552 0.0001 -0.0070 0.0031 188 GLY A N 753 C CA . GLY A 100 ? 0.1411 0.1388 0.1362 0.0012 -0.0055 -0.0015 188 GLY A CA 754 C C . GLY A 100 ? 0.1434 0.1202 0.1497 -0.0021 -0.0054 0.0080 188 GLY A C 755 O O . GLY A 100 ? 0.1955 0.1579 0.1975 0.0137 -0.0301 -0.0173 188 GLY A O 756 N N . GLU A 101 ? 0.1192 0.1121 0.1333 -0.0025 -0.0140 -0.0051 189 GLU A N 757 C CA . GLU A 101 ? 0.1212 0.1213 0.1333 -0.0054 -0.0051 -0.0041 189 GLU A CA 758 C C . GLU A 101 ? 0.0932 0.1022 0.1104 -0.0054 -0.0014 0.0010 189 GLU A C 759 O O . GLU A 101 ? 0.1203 0.0890 0.1274 -0.0189 0.0015 -0.0072 189 GLU A O 760 C CB . GLU A 101 ? 0.1409 0.1586 0.1522 -0.0019 -0.0047 -0.0020 189 GLU A CB 761 C CG . GLU A 101 ? 0.1651 0.1336 0.1426 -0.0100 0.0087 0.0076 189 GLU A CG 762 C CD . GLU A 101 ? 0.1525 0.1442 0.2140 0.0079 0.0159 -0.0044 189 GLU A CD 763 O OE1 . GLU A 101 ? 0.1916 0.1467 0.2724 -0.0032 0.0275 -0.0088 189 GLU A OE1 764 O OE2 . GLU A 101 ? 0.1191 0.1127 0.1785 -0.0051 0.0078 -0.0184 189 GLU A OE2 765 N N . TRP A 102 ? 0.0872 0.0686 0.0974 -0.0017 0.0022 -0.0090 190 TRP A N 766 C CA . TRP A 102 ? 0.0915 0.0562 0.1059 -0.0069 0.0008 0.0086 190 TRP A CA 767 C C . TRP A 102 ? 0.0963 0.0571 0.1020 -0.0056 0.0007 0.0075 190 TRP A C 768 O O . TRP A 102 ? 0.0948 0.0818 0.1188 -0.0059 0.0017 0.0078 190 TRP A O 769 C CB . TRP A 102 ? 0.0952 0.0567 0.1150 -0.0004 -0.0019 -0.0028 190 TRP A CB 770 C CG . TRP A 102 ? 0.0846 0.0787 0.0966 -0.0030 -0.0056 -0.0020 190 TRP A CG 771 C CD1 . TRP A 102 ? 0.1057 0.0765 0.1383 -0.0026 0.0066 -0.0077 190 TRP A CD1 772 C CD2 . TRP A 102 ? 0.0869 0.0685 0.0837 0.0013 -0.0037 0.0109 190 TRP A CD2 773 N NE1 . TRP A 102 ? 0.0983 0.0886 0.1273 -0.0057 -0.0003 -0.0038 190 TRP A NE1 774 C CE2 . TRP A 102 ? 0.0965 0.0860 0.1125 -0.0016 -0.0053 -0.0019 190 TRP A CE2 775 C CE3 . TRP A 102 ? 0.1019 0.0757 0.0881 -0.0063 0.0049 0.0254 190 TRP A CE3 776 C CZ2 . TRP A 102 ? 0.0962 0.0917 0.1103 0.0027 0.0022 0.0090 190 TRP A CZ2 777 C CZ3 . TRP A 102 ? 0.1229 0.1150 0.1250 -0.0045 0.0087 0.0160 190 TRP A CZ3 778 C CH2 . TRP A 102 ? 0.1302 0.0772 0.1367 0.0079 0.0170 0.0163 190 TRP A CH2 779 N N . ALA A 103 ? 0.0929 0.0862 0.1051 -0.0050 -0.0057 0.0022 191 ALA A N 780 C CA . ALA A 103 ? 0.0945 0.0776 0.0904 -0.0123 -0.0025 -0.0085 191 ALA A CA 781 C C . ALA A 103 ? 0.0956 0.0782 0.1040 0.0015 -0.0039 -0.0023 191 ALA A C 782 O O . ALA A 103 ? 0.1067 0.0564 0.1156 -0.0010 -0.0027 -0.0068 191 ALA A O 783 C CB . ALA A 103 ? 0.1145 0.0836 0.1090 -0.0036 -0.0017 0.0041 191 ALA A CB 784 N N . ILE A 104 ? 0.1004 0.0877 0.1080 -0.0068 -0.0053 -0.0010 192 ILE A N 785 C CA . ILE A 104 ? 0.1127 0.0949 0.1091 -0.0010 0.0018 -0.0008 192 ILE A CA 786 C C . ILE A 104 ? 0.0988 0.0799 0.1216 -0.0077 0.0001 0.0018 192 ILE A C 787 O O . ILE A 104 ? 0.1365 0.0831 0.1394 -0.0061 -0.0045 -0.0025 192 ILE A O 788 C CB . ILE A 104 ? 0.1257 0.0999 0.1282 -0.0076 0.0015 -0.0062 192 ILE A CB 789 C CG1 . ILE A 104 ? 0.1231 0.0860 0.1271 -0.0137 -0.0001 0.0018 192 ILE A CG1 790 C CG2 . ILE A 104 ? 0.1548 0.1497 0.1513 -0.0197 0.0149 0.0028 192 ILE A CG2 791 C CD1 . ILE A 104 ? 0.1297 0.1110 0.1617 -0.0205 0.0068 0.0004 192 ILE A CD1 792 N N . ALA A 105 ? 0.1183 0.0904 0.1083 -0.0028 0.0034 -0.0011 193 ALA A N 793 C CA . ALA A 105 ? 0.1159 0.0970 0.1163 -0.0037 0.0008 -0.0018 193 ALA A CA 794 C C . ALA A 105 ? 0.1256 0.0895 0.1217 -0.0044 0.0046 0.0028 193 ALA A C 795 O O . ALA A 105 ? 0.1234 0.1016 0.1249 -0.0111 0.0016 -0.0055 193 ALA A O 796 C CB . ALA A 105 ? 0.1351 0.1031 0.1354 0.0020 -0.0082 -0.0040 193 ALA A CB 797 N N . ASN A 106 ? 0.1089 0.0912 0.1270 -0.0070 0.0023 0.0020 194 ASN A N 798 C CA . ASN A 106 ? 0.1083 0.0838 0.1268 -0.0109 -0.0016 -0.0078 194 ASN A CA 799 C C . ASN A 106 ? 0.1242 0.0973 0.1211 -0.0055 -0.0095 -0.0069 194 ASN A C 800 O O . ASN A 106 ? 0.1198 0.0912 0.1381 -0.0190 0.0037 -0.0089 194 ASN A O 801 C CB . ASN A 106 ? 0.1181 0.1144 0.1305 -0.0133 -0.0083 -0.0010 194 ASN A CB 802 C CG . ASN A 106 ? 0.1234 0.1179 0.1256 -0.0016 -0.0083 0.0022 194 ASN A CG 803 O OD1 . ASN A 106 ? 0.1350 0.1261 0.1271 -0.0142 -0.0163 0.0152 194 ASN A OD1 804 N ND2 . ASN A 106 ? 0.1407 0.1307 0.1273 -0.0098 0.0037 0.0023 194 ASN A ND2 805 N N . ASN A 107 ? 0.1234 0.0954 0.1172 -0.0053 -0.0068 0.0020 195 ASN A N 806 C CA . ASN A 107 ? 0.1238 0.1042 0.1401 -0.0021 -0.0051 -0.0102 195 ASN A CA 807 C C . ASN A 107 ? 0.1082 0.0984 0.1269 0.0002 -0.0015 -0.0095 195 ASN A C 808 O O . ASN A 107 ? 0.1212 0.0963 0.1258 0.0106 -0.0192 -0.0116 195 ASN A O 809 C CB . ASN A 107 ? 0.1548 0.1529 0.1869 -0.0070 -0.0118 -0.0051 195 ASN A CB 810 C CG . ASN A 107 ? 0.1933 0.1741 0.2189 0.0013 -0.0024 0.0001 195 ASN A CG 811 O OD1 . ASN A 107 ? 0.2288 0.2365 0.2358 -0.0072 -0.0104 -0.0044 195 ASN A OD1 812 N ND2 . ASN A 107 ? 0.2201 0.2524 0.2787 0.0038 0.0059 -0.0101 195 ASN A ND2 813 N N . GLY A 108 ? 0.1115 0.0858 0.1122 0.0165 -0.0100 -0.0086 196 GLY A N 814 C CA . GLY A 108 ? 0.0984 0.0844 0.1003 0.0122 -0.0094 -0.0024 196 GLY A CA 815 C C . GLY A 108 ? 0.0924 0.0850 0.0940 0.0077 -0.0064 -0.0019 196 GLY A C 816 O O . GLY A 108 ? 0.1180 0.0795 0.0984 0.0088 -0.0170 0.0026 196 GLY A O 817 N N . VAL A 109 ? 0.1061 0.0739 0.0925 0.0028 0.0000 -0.0169 197 VAL A N 818 C CA . VAL A 109 ? 0.1119 0.0925 0.0968 -0.0008 0.0007 -0.0023 197 VAL A CA 819 C C . VAL A 109 ? 0.1066 0.0821 0.0902 0.0032 -0.0004 0.0008 197 VAL A C 820 O O . VAL A 109 ? 0.1372 0.0797 0.1033 0.0021 -0.0045 0.0014 197 VAL A O 821 C CB . VAL A 109 ? 0.1277 0.1053 0.1104 -0.0066 0.0054 -0.0027 197 VAL A CB 822 C CG1 . VAL A 109 ? 0.1469 0.1153 0.1228 -0.0103 0.0185 -0.0077 197 VAL A CG1 823 C CG2 . VAL A 109 ? 0.1508 0.1523 0.1316 0.0037 0.0116 -0.0246 197 VAL A CG2 824 N N . ASN A 110 ? 0.1101 0.0840 0.0912 0.0061 -0.0053 -0.0030 198 ASN A N 825 C CA . ASN A 110 ? 0.1203 0.1071 0.1144 0.0069 -0.0053 -0.0011 198 ASN A CA 826 C C . ASN A 110 ? 0.0957 0.0935 0.1014 0.0065 -0.0089 0.0009 198 ASN A C 827 O O . ASN A 110 ? 0.1141 0.0820 0.0988 0.0131 -0.0159 -0.0030 198 ASN A O 828 C CB . ASN A 110 ? 0.1250 0.1490 0.1316 0.0133 -0.0072 0.0043 198 ASN A CB 829 C CG . ASN A 110 ? 0.1932 0.2033 0.1688 0.0114 -0.0026 0.0062 198 ASN A CG 830 O OD1 . ASN A 110 ? 0.2835 0.2702 0.2128 -0.0110 0.0050 0.0219 198 ASN A OD1 831 N ND2 . ASN A 110 ? 0.2552 0.2801 0.2197 0.0142 -0.0126 -0.0150 198 ASN A ND2 832 N N . ASN A 111 ? 0.0994 0.0798 0.0902 -0.0017 -0.0140 0.0014 199 ASN A N 833 C CA . ASN A 111 ? 0.0798 0.0686 0.0863 0.0044 -0.0046 -0.0009 199 ASN A CA 834 C C . ASN A 111 ? 0.0746 0.0601 0.0664 -0.0022 -0.0046 0.0006 199 ASN A C 835 O O . ASN A 111 ? 0.0895 0.0742 0.0881 0.0008 -0.0023 0.0040 199 ASN A O 836 C CB . ASN A 111 ? 0.0969 0.0814 0.0898 0.0049 -0.0074 0.0138 199 ASN A CB 837 C CG . ASN A 111 ? 0.1172 0.0910 0.1237 0.0053 -0.0043 0.0028 199 ASN A CG 838 O OD1 . ASN A 111 ? 0.1297 0.0933 0.1433 -0.0185 -0.0181 -0.0121 199 ASN A OD1 839 N ND2 . ASN A 111 ? 0.1217 0.0917 0.1392 0.0040 0.0132 0.0167 199 ASN A ND2 840 N N . TYR A 112 ? 0.0889 0.0780 0.0784 0.0010 -0.0045 -0.0002 200 TYR A N 841 C CA . TYR A 112 ? 0.0867 0.0602 0.0822 0.0004 -0.0039 0.0015 200 TYR A CA 842 C C . TYR A 112 ? 0.0904 0.0742 0.0822 0.0072 -0.0030 0.0030 200 TYR A C 843 O O . TYR A 112 ? 0.1096 0.0616 0.0821 0.0092 -0.0009 0.0001 200 TYR A O 844 C CB . TYR A 112 ? 0.0979 0.0552 0.0670 0.0001 0.0052 0.0012 200 TYR A CB 845 C CG . TYR A 112 ? 0.0825 0.0684 0.0944 0.0064 0.0003 -0.0055 200 TYR A CG 846 C CD1 . TYR A 112 ? 0.0996 0.0718 0.0982 0.0036 -0.0056 -0.0037 200 TYR A CD1 847 C CD2 . TYR A 112 ? 0.0745 0.0878 0.0809 0.0076 0.0086 -0.0011 200 TYR A CD2 848 C CE1 . TYR A 112 ? 0.1072 0.0762 0.0999 0.0038 -0.0113 0.0046 200 TYR A CE1 849 C CE2 . TYR A 112 ? 0.0884 0.0705 0.0944 -0.0027 0.0083 0.0023 200 TYR A CE2 850 C CZ . TYR A 112 ? 0.1141 0.0717 0.0972 -0.0032 -0.0084 -0.0076 200 TYR A CZ 851 O OH . TYR A 112 ? 0.1108 0.0976 0.1159 0.0043 -0.0163 -0.0059 200 TYR A OH 852 N N . LYS A 113 ? 0.1013 0.0610 0.0876 0.0026 -0.0072 0.0037 201 LYS A N 853 C CA . LYS A 113 ? 0.1083 0.0697 0.0873 0.0004 -0.0112 0.0000 201 LYS A CA 854 C C . LYS A 113 ? 0.1064 0.0772 0.0837 0.0036 -0.0159 0.0023 201 LYS A C 855 O O . LYS A 113 ? 0.1148 0.0768 0.0974 0.0144 -0.0104 -0.0002 201 LYS A O 856 C CB . LYS A 113 ? 0.1382 0.0871 0.1001 0.0007 -0.0066 0.0147 201 LYS A CB 857 C CG . LYS A 113 ? 0.1401 0.0800 0.1191 0.0071 0.0012 0.0000 201 LYS A CG 858 C CD . LYS A 113 ? 0.2028 0.1673 0.1617 -0.0014 -0.0060 0.0135 201 LYS A CD 859 C CE . LYS A 113 ? 0.2427 0.2336 0.2333 -0.0009 0.0116 0.0065 201 LYS A CE 860 N NZ . LYS A 113 ? 0.3515 0.3419 0.2636 -0.0086 0.0074 0.0207 201 LYS A NZ 861 N N . ALA A 114 ? 0.1061 0.0894 0.0924 0.0030 -0.0130 -0.0041 202 ALA A N 862 C CA . ALA A 114 ? 0.1045 0.0877 0.0974 0.0021 -0.0110 0.0003 202 ALA A CA 863 C C . ALA A 114 ? 0.1039 0.0869 0.0955 0.0048 -0.0035 0.0046 202 ALA A C 864 O O . ALA A 114 ? 0.0999 0.0940 0.1020 0.0115 -0.0079 -0.0088 202 ALA A O 865 C CB . ALA A 114 ? 0.1156 0.0976 0.1164 -0.0009 -0.0094 -0.0078 202 ALA A CB 866 N N . TYR A 115 ? 0.1044 0.0754 0.1002 -0.0017 -0.0131 -0.0002 203 TYR A N 867 C CA . TYR A 115 ? 0.0960 0.0592 0.0923 0.0020 -0.0017 0.0012 203 TYR A CA 868 C C . TYR A 115 ? 0.0722 0.0623 0.0734 0.0046 -0.0090 0.0057 203 TYR A C 869 O O . TYR A 115 ? 0.0960 0.0747 0.0910 0.0003 -0.0034 0.0013 203 TYR A O 870 C CB . TYR A 115 ? 0.1066 0.0671 0.1060 0.0047 -0.0130 -0.0014 203 TYR A CB 871 C CG . TYR A 115 ? 0.0901 0.0557 0.0750 0.0107 -0.0006 0.0106 203 TYR A CG 872 C CD1 . TYR A 115 ? 0.0674 0.0656 0.0948 0.0049 0.0001 0.0017 203 TYR A CD1 873 C CD2 . TYR A 115 ? 0.0812 0.0634 0.0910 0.0028 0.0055 0.0024 203 TYR A CD2 874 C CE1 . TYR A 115 ? 0.0937 0.0710 0.0935 -0.0011 0.0153 0.0116 203 TYR A CE1 875 C CE2 . TYR A 115 ? 0.0829 0.0725 0.0891 -0.0088 0.0005 -0.0002 203 TYR A CE2 876 C CZ . TYR A 115 ? 0.0808 0.0711 0.0928 0.0030 -0.0113 0.0047 203 TYR A CZ 877 O OH . TYR A 115 ? 0.0894 0.0966 0.0870 -0.0021 -0.0023 0.0094 203 TYR A OH 878 N N . ILE A 116 ? 0.0951 0.0489 0.0766 -0.0060 -0.0022 -0.0045 204 ILE A N 879 C CA . ILE A 116 ? 0.0823 0.0467 0.0857 -0.0069 -0.0039 0.0035 204 ILE A CA 880 C C . ILE A 116 ? 0.0949 0.0630 0.0789 0.0058 -0.0025 -0.0056 204 ILE A C 881 O O . ILE A 116 ? 0.1103 0.0694 0.0956 -0.0004 -0.0066 -0.0155 204 ILE A O 882 C CB . ILE A 116 ? 0.0943 0.0532 0.0807 0.0070 0.0033 -0.0039 204 ILE A CB 883 C CG1 . ILE A 116 ? 0.0890 0.0747 0.0833 0.0003 0.0058 -0.0079 204 ILE A CG1 884 C CG2 . ILE A 116 ? 0.1022 0.0650 0.1034 -0.0016 -0.0059 -0.0126 204 ILE A CG2 885 C CD1 . ILE A 116 ? 0.1019 0.0978 0.1068 0.0000 -0.0141 -0.0019 204 ILE A CD1 886 N N . ASN A 117 ? 0.0987 0.0559 0.0876 0.0169 -0.0067 0.0007 205 ASN A N 887 C CA . ASN A 117 ? 0.1005 0.0773 0.1004 0.0068 -0.0062 0.0052 205 ASN A CA 888 C C . ASN A 117 ? 0.0980 0.0713 0.1049 -0.0018 -0.0018 0.0025 205 ASN A C 889 O O . ASN A 117 ? 0.1018 0.0823 0.1092 0.0059 -0.0017 0.0008 205 ASN A O 890 C CB . ASN A 117 ? 0.1054 0.0866 0.1151 0.0208 -0.0109 0.0033 205 ASN A CB 891 C CG . ASN A 117 ? 0.1309 0.1230 0.1361 0.0121 -0.0184 0.0053 205 ASN A CG 892 O OD1 . ASN A 117 ? 0.1482 0.1401 0.1556 0.0159 0.0076 0.0311 205 ASN A OD1 893 N ND2 . ASN A 117 ? 0.1857 0.1729 0.1565 0.0134 -0.0213 -0.0111 205 ASN A ND2 894 N N . ARG A 118 ? 0.0955 0.0751 0.0873 -0.0010 -0.0059 0.0046 206 ARG A N 895 C CA . ARG A 118 ? 0.0826 0.0738 0.0896 -0.0045 -0.0124 0.0071 206 ARG A CA 896 C C . ARG A 118 ? 0.0883 0.0711 0.0889 -0.0012 0.0032 -0.0056 206 ARG A C 897 O O . ARG A 118 ? 0.1001 0.0766 0.1036 0.0078 0.0002 -0.0081 206 ARG A O 898 C CB . ARG A 118 ? 0.1157 0.0763 0.1074 -0.0002 -0.0021 -0.0001 206 ARG A CB 899 C CG . ARG A 118 ? 0.1300 0.1076 0.1215 -0.0096 -0.0037 0.0054 206 ARG A CG 900 C CD . ARG A 118 ? 0.1361 0.1713 0.1447 -0.0048 0.0077 0.0019 206 ARG A CD 901 N NE . ARG A 118 ? 0.1403 0.1695 0.1685 -0.0136 0.0180 0.0135 206 ARG A NE 902 C CZ . ARG A 118 ? 0.1730 0.1748 0.1835 -0.0070 0.0152 0.0151 206 ARG A CZ 903 N NH1 . ARG A 118 ? 0.1917 0.1862 0.2350 0.0208 0.0197 0.0210 206 ARG A NH1 904 N NH2 . ARG A 118 ? 0.2333 0.2263 0.2266 0.0168 0.0398 0.0213 206 ARG A NH2 905 N N . ILE A 119 ? 0.0962 0.0624 0.0838 -0.0002 -0.0027 0.0056 207 ILE A N 906 C CA . ILE A 119 ? 0.0861 0.0641 0.0823 -0.0020 -0.0001 0.0031 207 ILE A CA 907 C C . ILE A 119 ? 0.1000 0.0759 0.0896 0.0067 -0.0006 -0.0010 207 ILE A C 908 O O . ILE A 119 ? 0.1031 0.0728 0.0937 0.0069 -0.0067 -0.0044 207 ILE A O 909 C CB . ILE A 119 ? 0.0922 0.0595 0.0929 -0.0042 0.0003 0.0141 207 ILE A CB 910 C CG1 . ILE A 119 ? 0.1006 0.0762 0.0938 0.0094 -0.0029 0.0091 207 ILE A CG1 911 C CG2 . ILE A 119 ? 0.0873 0.0827 0.1103 0.0039 -0.0035 -0.0011 207 ILE A CG2 912 C CD1 . ILE A 119 ? 0.0912 0.0814 0.1068 -0.0037 0.0002 0.0015 207 ILE A CD1 913 N N . ARG A 120 ? 0.0909 0.0493 0.0799 0.0002 -0.0037 -0.0062 208 ARG A N 914 C CA . ARG A 120 ? 0.0973 0.0508 0.0860 -0.0004 -0.0089 -0.0001 208 ARG A CA 915 C C . ARG A 120 ? 0.1015 0.0843 0.0911 0.0015 0.0013 -0.0011 208 ARG A C 916 O O . ARG A 120 ? 0.1253 0.0704 0.1102 0.0096 -0.0060 0.0018 208 ARG A O 917 C CB . ARG A 120 ? 0.0890 0.0598 0.0980 -0.0094 0.0021 -0.0049 208 ARG A CB 918 C CG . ARG A 120 ? 0.1103 0.0963 0.1259 0.0230 0.0027 0.0110 208 ARG A CG 919 C CD . ARG A 120 ? 0.1445 0.1148 0.1255 0.0107 -0.0029 0.0155 208 ARG A CD 920 N NE . ARG A 120 ? 0.1734 0.1535 0.1717 0.0051 -0.0027 -0.0176 208 ARG A NE 921 C CZ . ARG A 120 ? 0.1950 0.1788 0.1786 -0.0073 -0.0182 0.0187 208 ARG A CZ 922 N NH1 . ARG A 120 ? 0.2107 0.2125 0.2217 0.0021 -0.0097 0.0002 208 ARG A NH1 923 N NH2 . ARG A 120 ? 0.2051 0.1848 0.1958 -0.0099 -0.0012 0.0121 208 ARG A NH2 924 N N . GLU A 121 ? 0.1109 0.0698 0.0955 0.0011 -0.0034 0.0085 209 GLU A N 925 C CA . GLU A 121 ? 0.1037 0.0979 0.0992 -0.0050 -0.0045 0.0052 209 GLU A CA 926 C C . GLU A 121 ? 0.1088 0.1001 0.0971 -0.0029 -0.0002 0.0046 209 GLU A C 927 O O . GLU A 121 ? 0.1254 0.1041 0.1299 0.0131 -0.0015 0.0051 209 GLU A O 928 C CB . GLU A 121 ? 0.1163 0.1090 0.1360 0.0073 -0.0100 0.0019 209 GLU A CB 929 C CG . GLU A 121 ? 0.1598 0.1695 0.1770 0.0121 0.0010 0.0037 209 GLU A CG 930 C CD . GLU A 121 ? 0.2461 0.2545 0.2566 -0.0194 -0.0154 0.0001 209 GLU A CD 931 O OE1 . GLU A 121 ? 0.2836 0.3033 0.2485 -0.0266 -0.0137 0.0194 209 GLU A OE1 932 O OE2 . GLU A 121 ? 0.3752 0.3788 0.2922 -0.0082 -0.0002 -0.0023 209 GLU A OE2 933 N N . ILE A 122 ? 0.0982 0.0785 0.1017 -0.0025 -0.0063 0.0022 210 ILE A N 934 C CA . ILE A 122 ? 0.0932 0.0831 0.1054 -0.0025 0.0024 0.0040 210 ILE A CA 935 C C . ILE A 122 ? 0.1089 0.0797 0.1024 -0.0002 0.0069 0.0016 210 ILE A C 936 O O . ILE A 122 ? 0.1179 0.0786 0.1079 0.0010 0.0062 -0.0035 210 ILE A O 937 C CB . ILE A 122 ? 0.1026 0.0825 0.1132 0.0076 -0.0082 0.0083 210 ILE A CB 938 C CG1 . ILE A 122 ? 0.1294 0.0970 0.1214 -0.0118 -0.0067 -0.0024 210 ILE A CG1 939 C CG2 . ILE A 122 ? 0.1238 0.0880 0.1255 -0.0010 -0.0113 -0.0036 210 ILE A CG2 940 C CD1 . ILE A 122 ? 0.1413 0.1201 0.1498 -0.0079 -0.0080 0.0004 210 ILE A CD1 941 N N . LEU A 123 ? 0.0912 0.0659 0.1011 -0.0052 -0.0014 -0.0101 211 LEU A N 942 C CA . LEU A 123 ? 0.0935 0.0682 0.0930 -0.0119 0.0035 -0.0026 211 LEU A CA 943 C C . LEU A 123 ? 0.0974 0.0935 0.0988 -0.0010 0.0014 -0.0022 211 LEU A C 944 O O . LEU A 123 ? 0.1063 0.0813 0.1054 -0.0003 -0.0003 -0.0081 211 LEU A O 945 C CB . LEU A 123 ? 0.1042 0.0684 0.1063 -0.0022 0.0029 -0.0149 211 LEU A CB 946 C CG . LEU A 123 ? 0.1026 0.0680 0.1043 -0.0012 0.0024 -0.0058 211 LEU A CG 947 C CD1 . LEU A 123 ? 0.1195 0.0996 0.1355 0.0069 -0.0016 -0.0037 211 LEU A CD1 948 C CD2 . LEU A 123 ? 0.1329 0.1492 0.1396 0.0272 -0.0008 0.0005 211 LEU A CD2 949 N N . ILE A 124 ? 0.1182 0.0716 0.1025 -0.0037 -0.0003 -0.0036 212 ILE A N 950 C CA . ILE A 124 ? 0.1248 0.1008 0.1320 0.0119 0.0005 0.0050 212 ILE A CA 951 C C . ILE A 124 ? 0.1261 0.1049 0.1301 0.0167 0.0027 -0.0005 212 ILE A C 952 O O . ILE A 124 ? 0.1490 0.1052 0.1713 0.0131 0.0086 -0.0161 212 ILE A O 953 C CB . ILE A 124 ? 0.1487 0.1250 0.1373 0.0290 0.0112 0.0065 212 ILE A CB 954 C CG1 . ILE A 124 ? 0.1609 0.1414 0.1608 0.0168 0.0053 0.0118 212 ILE A CG1 955 C CG2 . ILE A 124 ? 0.2082 0.1726 0.1745 0.0271 -0.0082 0.0142 212 ILE A CG2 956 C CD1 . ILE A 124 ? 0.2436 0.2224 0.2150 0.0088 -0.0069 0.0073 212 ILE A CD1 957 N N . SER A 125 ? 0.1050 0.1089 0.1313 0.0119 0.0043 0.0016 213 SER A N 958 C CA A SER A 125 ? 0.1148 0.1235 0.1205 0.0080 -0.0001 -0.0035 213 SER A CA 959 C CA B SER A 125 ? 0.1217 0.1309 0.1260 0.0081 0.0008 -0.0047 213 SER A CA 960 C C . SER A 125 ? 0.1063 0.1120 0.1110 0.0126 0.0002 -0.0045 213 SER A C 961 O O . SER A 125 ? 0.1285 0.1645 0.1459 0.0300 0.0006 -0.0251 213 SER A O 962 C CB A SER A 125 ? 0.1017 0.1313 0.1263 0.0071 -0.0013 0.0016 213 SER A CB 963 C CB B SER A 125 ? 0.1185 0.1394 0.1365 0.0060 -0.0020 0.0005 213 SER A CB 964 O OG A SER A 125 ? 0.1169 0.1170 0.1332 -0.0015 -0.0019 0.0032 213 SER A OG 965 O OG B SER A 125 ? 0.1615 0.1937 0.1815 -0.0071 0.0112 -0.0107 213 SER A OG 966 N N . PHE A 126 ? 0.0981 0.1059 0.1106 0.0059 -0.0039 -0.0044 214 PHE A N 967 C CA . PHE A 126 ? 0.1039 0.0970 0.1068 0.0021 0.0020 -0.0121 214 PHE A CA 968 C C . PHE A 126 ? 0.1124 0.1037 0.1115 0.0022 0.0000 -0.0035 214 PHE A C 969 O O . PHE A 126 ? 0.0966 0.0867 0.1233 0.0153 0.0008 -0.0029 214 PHE A O 970 C CB . PHE A 126 ? 0.1120 0.1042 0.1194 -0.0075 -0.0013 -0.0105 214 PHE A CB 971 C CG . PHE A 126 ? 0.1130 0.0959 0.1154 0.0062 -0.0064 0.0033 214 PHE A CG 972 C CD1 . PHE A 126 ? 0.1222 0.1158 0.1364 0.0083 0.0100 0.0059 214 PHE A CD1 973 C CD2 . PHE A 126 ? 0.1177 0.1064 0.1301 -0.0109 0.0009 0.0025 214 PHE A CD2 974 C CE1 . PHE A 126 ? 0.1192 0.1484 0.1309 0.0112 0.0290 -0.0004 214 PHE A CE1 975 C CE2 . PHE A 126 ? 0.1329 0.1493 0.1610 -0.0123 0.0064 0.0026 214 PHE A CE2 976 C CZ . PHE A 126 ? 0.1385 0.1624 0.1775 -0.0154 0.0180 0.0078 214 PHE A CZ 977 N N . SER A 127 ? 0.1114 0.1130 0.1240 0.0039 -0.0047 0.0060 215 SER A N 978 C CA . SER A 127 ? 0.1106 0.1263 0.1285 0.0020 0.0070 0.0066 215 SER A CA 979 C C . SER A 127 ? 0.1171 0.1211 0.1417 0.0073 0.0017 0.0078 215 SER A C 980 O O . SER A 127 ? 0.1244 0.1115 0.1334 0.0015 0.0062 0.0033 215 SER A O 981 C CB . SER A 127 ? 0.1416 0.1479 0.1452 0.0047 0.0109 0.0185 215 SER A CB 982 O OG . SER A 127 ? 0.1643 0.1879 0.1540 0.0195 -0.0002 0.0235 215 SER A OG 983 N N . ASP A 128 ? 0.1196 0.1091 0.1232 0.0092 -0.0014 0.0048 216 ASP A N 984 C CA . ASP A 128 ? 0.1168 0.1069 0.1298 0.0043 0.0051 0.0021 216 ASP A CA 985 C C . ASP A 128 ? 0.1181 0.1128 0.1094 0.0082 0.0026 -0.0065 216 ASP A C 986 O O . ASP A 128 ? 0.1344 0.1254 0.1261 0.0214 0.0091 -0.0172 216 ASP A O 987 C CB . ASP A 128 ? 0.1231 0.1176 0.1285 0.0174 0.0088 -0.0027 216 ASP A CB 988 C CG . ASP A 128 ? 0.1546 0.1739 0.1702 -0.0093 0.0024 -0.0165 216 ASP A CG 989 O OD1 . ASP A 128 ? 0.1500 0.1528 0.1894 -0.0003 0.0264 -0.0011 216 ASP A OD1 990 O OD2 . ASP A 128 ? 0.2265 0.2793 0.2566 -0.0290 0.0465 -0.0144 216 ASP A OD2 991 N N . VAL A 129 ? 0.1062 0.0976 0.1091 0.0075 0.0043 0.0000 217 VAL A N 992 C CA . VAL A 129 ? 0.1006 0.0927 0.0934 -0.0033 -0.0035 -0.0069 217 VAL A CA 993 C C . VAL A 129 ? 0.1049 0.0792 0.1072 -0.0047 -0.0004 -0.0049 217 VAL A C 994 O O . VAL A 129 ? 0.1046 0.1071 0.1108 0.0115 0.0081 -0.0118 217 VAL A O 995 C CB . VAL A 129 ? 0.1128 0.1012 0.1077 0.0028 0.0099 -0.0034 217 VAL A CB 996 C CG1 . VAL A 129 ? 0.1198 0.0996 0.1175 0.0020 -0.0027 0.0064 217 VAL A CG1 997 C CG2 . VAL A 129 ? 0.1103 0.1117 0.1376 -0.0117 -0.0056 0.0007 217 VAL A CG2 998 N N . ARG A 130 ? 0.0898 0.0776 0.0941 0.0012 -0.0065 -0.0023 218 ARG A N 999 C CA . ARG A 130 ? 0.0911 0.0677 0.0972 0.0010 -0.0030 0.0011 218 ARG A CA 1000 C C . ARG A 130 ? 0.0900 0.0755 0.0844 0.0027 0.0018 0.0042 218 ARG A C 1001 O O . ARG A 130 ? 0.1080 0.0796 0.0724 0.0077 -0.0082 0.0005 218 ARG A O 1002 C CB . ARG A 130 ? 0.1018 0.0755 0.1056 -0.0046 -0.0006 -0.0001 218 ARG A CB 1003 C CG . ARG A 130 ? 0.1057 0.0843 0.1341 0.0050 -0.0078 -0.0148 218 ARG A CG 1004 C CD . ARG A 130 ? 0.1003 0.0871 0.1192 0.0061 -0.0045 -0.0122 218 ARG A CD 1005 N NE . ARG A 130 ? 0.1136 0.0857 0.1171 0.0189 -0.0124 -0.0030 218 ARG A NE 1006 C CZ . ARG A 130 ? 0.1190 0.1170 0.1289 0.0107 -0.0049 -0.0186 218 ARG A CZ 1007 N NH1 . ARG A 130 ? 0.1352 0.1197 0.1900 0.0106 -0.0073 -0.0093 218 ARG A NH1 1008 N NH2 . ARG A 130 ? 0.1301 0.1209 0.1342 0.0158 -0.0042 -0.0048 218 ARG A NH2 1009 N N . THR A 131 ? 0.0973 0.0686 0.0827 0.0071 0.0000 -0.0001 219 THR A N 1010 C CA . THR A 131 ? 0.0982 0.0688 0.0961 0.0001 0.0008 0.0027 219 THR A CA 1011 C C . THR A 131 ? 0.1095 0.0866 0.0981 0.0031 -0.0016 -0.0049 219 THR A C 1012 O O . THR A 131 ? 0.1094 0.1089 0.1051 0.0143 0.0148 0.0120 219 THR A O 1013 C CB . THR A 131 ? 0.0934 0.0808 0.1023 0.0002 0.0009 -0.0172 219 THR A CB 1014 O OG1 . THR A 131 ? 0.0962 0.1112 0.1328 0.0083 0.0019 -0.0064 219 THR A OG1 1015 C CG2 . THR A 131 ? 0.1141 0.0955 0.1336 -0.0040 0.0084 -0.0112 219 THR A CG2 1016 N N . ILE A 132 ? 0.0957 0.0846 0.0738 0.0073 0.0037 0.0104 220 ILE A N 1017 C CA . ILE A 132 ? 0.1014 0.1047 0.0966 -0.0006 -0.0049 0.0024 220 ILE A CA 1018 C C . ILE A 132 ? 0.0919 0.0799 0.0841 -0.0036 0.0022 0.0047 220 ILE A C 1019 O O . ILE A 132 ? 0.1045 0.0890 0.1065 0.0005 0.0117 0.0080 220 ILE A O 1020 C CB . ILE A 132 ? 0.1139 0.1338 0.1110 -0.0038 0.0000 -0.0004 220 ILE A CB 1021 C CG1 . ILE A 132 ? 0.1663 0.1674 0.1488 0.0069 -0.0021 -0.0277 220 ILE A CG1 1022 C CG2 . ILE A 132 ? 0.1380 0.1726 0.1668 0.0007 -0.0067 -0.0007 220 ILE A CG2 1023 C CD1 . ILE A 132 ? 0.1758 0.1890 0.1855 0.0153 -0.0180 -0.0096 220 ILE A CD1 1024 N N . LEU A 133 ? 0.0893 0.0629 0.0801 -0.0031 0.0086 0.0040 221 LEU A N 1025 C CA . LEU A 133 ? 0.0803 0.0612 0.0842 -0.0015 -0.0011 0.0040 221 LEU A CA 1026 C C . LEU A 133 ? 0.0823 0.0866 0.0944 -0.0031 0.0032 0.0046 221 LEU A C 1027 O O . LEU A 133 ? 0.0996 0.0873 0.1180 -0.0011 0.0121 0.0116 221 LEU A O 1028 C CB . LEU A 133 ? 0.1024 0.0911 0.0895 0.0069 0.0070 -0.0086 221 LEU A CB 1029 C CG . LEU A 133 ? 0.1003 0.0845 0.0949 -0.0015 -0.0005 -0.0043 221 LEU A CG 1030 C CD1 . LEU A 133 ? 0.1189 0.1231 0.1227 0.0016 -0.0159 -0.0086 221 LEU A CD1 1031 C CD2 . LEU A 133 ? 0.1088 0.1328 0.1232 0.0000 0.0015 -0.0003 221 LEU A CD2 1032 N N . VAL A 134 ? 0.0929 0.0842 0.0893 0.0017 0.0095 0.0112 222 VAL A N 1033 C CA . VAL A 134 ? 0.0863 0.0782 0.0854 -0.0068 0.0080 0.0025 222 VAL A CA 1034 C C . VAL A 134 ? 0.0807 0.0653 0.0875 -0.0017 -0.0001 0.0015 222 VAL A C 1035 O O . VAL A 134 ? 0.1008 0.0915 0.1070 -0.0093 0.0021 -0.0030 222 VAL A O 1036 C CB . VAL A 134 ? 0.0927 0.0995 0.0998 -0.0065 0.0026 0.0067 222 VAL A CB 1037 C CG1 . VAL A 134 ? 0.1169 0.1169 0.1106 0.0022 -0.0149 -0.0030 222 VAL A CG1 1038 C CG2 . VAL A 134 ? 0.1050 0.1291 0.0959 0.0049 -0.0050 0.0064 222 VAL A CG2 1039 N N . ILE A 135 ? 0.0844 0.0778 0.0933 -0.0070 0.0063 -0.0012 223 ILE A N 1040 C CA . ILE A 135 ? 0.0862 0.0901 0.0966 -0.0047 -0.0045 0.0001 223 ILE A CA 1041 C C . ILE A 135 ? 0.1025 0.0954 0.1136 -0.0032 -0.0031 -0.0098 223 ILE A C 1042 O O . ILE A 135 ? 0.1036 0.1140 0.1019 -0.0085 0.0028 -0.0144 223 ILE A O 1043 C CB . ILE A 135 ? 0.1128 0.1100 0.0976 -0.0054 0.0008 -0.0053 223 ILE A CB 1044 C CG1 . ILE A 135 ? 0.1222 0.1167 0.1023 0.0020 -0.0032 -0.0041 223 ILE A CG1 1045 C CG2 . ILE A 135 ? 0.1203 0.1230 0.0980 0.0099 0.0082 -0.0007 223 ILE A CG2 1046 C CD1 . ILE A 135 ? 0.1376 0.1212 0.1505 0.0016 0.0073 -0.0085 223 ILE A CD1 1047 N N . GLU A 136 ? 0.0928 0.0965 0.1025 -0.0044 0.0073 0.0018 224 GLU A N 1048 C CA . GLU A 136 ? 0.1028 0.1092 0.1121 -0.0040 0.0039 -0.0039 224 GLU A CA 1049 C C . GLU A 136 ? 0.1002 0.0862 0.1014 -0.0007 0.0011 -0.0031 224 GLU A C 1050 O O . GLU A 136 ? 0.0939 0.0994 0.1008 -0.0111 -0.0035 -0.0072 224 GLU A O 1051 C CB . GLU A 136 ? 0.1006 0.0964 0.1191 0.0037 0.0016 0.0014 224 GLU A CB 1052 C CG . GLU A 136 ? 0.1037 0.1110 0.1061 0.0028 0.0030 0.0079 224 GLU A CG 1053 C CD . GLU A 136 ? 0.1008 0.1049 0.1088 0.0048 -0.0014 -0.0021 224 GLU A CD 1054 O OE1 . GLU A 136 ? 0.1112 0.1098 0.1166 -0.0005 -0.0014 0.0117 224 GLU A OE1 1055 O OE2 . GLU A 136 ? 0.1014 0.0884 0.1057 0.0070 -0.0049 0.0047 224 GLU A OE2 1056 N N . PRO A 137 ? 0.0940 0.1143 0.0987 0.0004 0.0016 -0.0013 225 PRO A N 1057 C CA . PRO A 137 ? 0.1140 0.1077 0.1204 0.0092 -0.0009 0.0061 225 PRO A CA 1058 C C . PRO A 137 ? 0.0999 0.1102 0.1131 -0.0041 -0.0022 0.0035 225 PRO A C 1059 O O . PRO A 137 ? 0.1155 0.1023 0.1183 -0.0056 0.0029 0.0006 225 PRO A O 1060 C CB . PRO A 137 ? 0.1302 0.1285 0.1255 0.0132 0.0029 -0.0030 225 PRO A CB 1061 C CG . PRO A 137 ? 0.1301 0.1440 0.1368 0.0149 0.0015 0.0049 225 PRO A CG 1062 C CD . PRO A 137 ? 0.1099 0.1140 0.1050 0.0134 0.0094 -0.0108 225 PRO A CD 1063 N N . ASP A 138 ? 0.1064 0.1228 0.1385 -0.0020 -0.0026 0.0004 226 ASP A N 1064 C CA . ASP A 138 ? 0.1188 0.1205 0.1282 -0.0007 0.0095 0.0035 226 ASP A CA 1065 C C . ASP A 138 ? 0.1158 0.1150 0.1311 0.0013 0.0006 0.0012 226 ASP A C 1066 O O . ASP A 138 ? 0.1223 0.1294 0.1450 -0.0076 0.0090 0.0017 226 ASP A O 1067 C CB . ASP A 138 ? 0.1404 0.1400 0.1469 0.0029 0.0142 0.0068 226 ASP A CB 1068 C CG . ASP A 138 ? 0.1547 0.1577 0.1896 0.0015 0.0082 0.0042 226 ASP A CG 1069 O OD1 . ASP A 138 ? 0.1586 0.1939 0.2352 0.0049 -0.0029 0.0043 226 ASP A OD1 1070 O OD2 . ASP A 138 ? 0.1685 0.1563 0.1783 -0.0171 -0.0040 -0.0018 226 ASP A OD2 1071 N N . SER A 139 ? 0.1064 0.1055 0.1213 0.0005 0.0072 0.0060 227 SER A N 1072 C CA . SER A 139 ? 0.0985 0.1049 0.1164 -0.0082 0.0089 -0.0051 227 SER A CA 1073 C C . SER A 139 ? 0.0893 0.0836 0.1114 -0.0068 0.0060 -0.0028 227 SER A C 1074 O O . SER A 139 ? 0.0980 0.0910 0.1297 -0.0043 0.0082 -0.0011 227 SER A O 1075 C CB . SER A 139 ? 0.1178 0.1011 0.1209 -0.0089 0.0080 0.0045 227 SER A CB 1076 O OG . SER A 139 ? 0.0992 0.1020 0.1219 0.0001 0.0112 0.0069 227 SER A OG 1077 N N . LEU A 140 ? 0.0879 0.0855 0.1137 0.0137 0.0041 0.0050 228 LEU A N 1078 C CA . LEU A 140 ? 0.1070 0.0998 0.1057 0.0000 0.0048 0.0000 228 LEU A CA 1079 C C . LEU A 140 ? 0.1136 0.0908 0.1095 0.0060 0.0056 0.0045 228 LEU A C 1080 O O . LEU A 140 ? 0.0990 0.1162 0.1216 0.0060 0.0152 0.0100 228 LEU A O 1081 C CB . LEU A 140 ? 0.1176 0.1109 0.1165 -0.0018 0.0109 0.0029 228 LEU A CB 1082 C CG . LEU A 140 ? 0.1157 0.1296 0.1692 -0.0127 0.0005 0.0201 228 LEU A CG 1083 C CD1 . LEU A 140 ? 0.1606 0.1587 0.2088 0.0079 0.0084 0.0099 228 LEU A CD1 1084 C CD2 . LEU A 140 ? 0.1288 0.1605 0.1790 -0.0031 -0.0058 0.0164 228 LEU A CD2 1085 N N . ALA A 141 ? 0.1029 0.0869 0.0997 -0.0047 0.0045 -0.0044 229 ALA A N 1086 C CA . ALA A 141 ? 0.1046 0.0961 0.1120 -0.0043 -0.0007 0.0000 229 ALA A CA 1087 C C . ALA A 141 ? 0.0950 0.0960 0.0995 0.0026 -0.0057 -0.0015 229 ALA A C 1088 O O . ALA A 141 ? 0.1048 0.1035 0.1248 -0.0034 0.0081 -0.0031 229 ALA A O 1089 C CB . ALA A 141 ? 0.1020 0.0936 0.1181 0.0000 -0.0030 0.0011 229 ALA A CB 1090 N N . ASN A 142 ? 0.0952 0.0924 0.1119 0.0050 0.0014 -0.0057 230 ASN A N 1091 C CA . ASN A 142 ? 0.0992 0.0903 0.1087 0.0003 0.0004 -0.0083 230 ASN A CA 1092 C C . ASN A 142 ? 0.1027 0.1023 0.1143 0.0092 0.0056 -0.0091 230 ASN A C 1093 O O . ASN A 142 ? 0.1069 0.0955 0.1301 0.0064 0.0092 -0.0228 230 ASN A O 1094 C CB . ASN A 142 ? 0.0956 0.0837 0.1214 0.0056 0.0044 -0.0178 230 ASN A CB 1095 C CG . ASN A 142 ? 0.0983 0.1012 0.1351 -0.0151 -0.0033 -0.0057 230 ASN A CG 1096 O OD1 . ASN A 142 ? 0.1233 0.0879 0.1635 0.0061 0.0215 0.0024 230 ASN A OD1 1097 N ND2 . ASN A 142 ? 0.1157 0.1541 0.1735 -0.0025 0.0213 -0.0159 230 ASN A ND2 1098 N N . MET A 143 ? 0.1276 0.0990 0.1191 -0.0027 0.0054 -0.0072 231 MET A N 1099 C CA . MET A 143 ? 0.1280 0.1201 0.1282 -0.0014 0.0085 -0.0096 231 MET A CA 1100 C C . MET A 143 ? 0.1439 0.1504 0.1337 -0.0067 0.0123 -0.0120 231 MET A C 1101 O O . MET A 143 ? 0.1637 0.2149 0.1604 -0.0197 0.0313 -0.0365 231 MET A O 1102 C CB . MET A 143 ? 0.1516 0.1503 0.1514 0.0032 0.0139 -0.0087 231 MET A CB 1103 C CG . MET A 143 ? 0.1524 0.1578 0.1826 -0.0050 0.0157 0.0053 231 MET A CG 1104 S SD . MET A 143 ? 0.1614 0.1658 0.1780 0.0004 0.0222 -0.0099 231 MET A SD 1105 C CE . MET A 143 ? 0.1473 0.1493 0.1571 -0.0082 -0.0094 0.0027 231 MET A CE 1106 N N . VAL A 144 ? 0.1266 0.1432 0.1307 -0.0128 0.0010 -0.0076 232 VAL A N 1107 C CA . VAL A 144 ? 0.1329 0.1454 0.1390 -0.0125 0.0107 -0.0046 232 VAL A CA 1108 C C . VAL A 144 ? 0.1476 0.1428 0.1467 -0.0123 0.0050 -0.0058 232 VAL A C 1109 O O . VAL A 144 ? 0.1682 0.1645 0.1924 -0.0212 0.0234 -0.0110 232 VAL A O 1110 C CB . VAL A 144 ? 0.1465 0.1320 0.1497 -0.0130 0.0011 -0.0083 232 VAL A CB 1111 C CG1 . VAL A 144 ? 0.1546 0.1620 0.1657 -0.0101 0.0149 -0.0027 232 VAL A CG1 1112 C CG2 . VAL A 144 ? 0.1755 0.1321 0.1612 -0.0171 0.0118 0.0009 232 VAL A CG2 1113 N N . THR A 145 ? 0.1299 0.1336 0.1511 -0.0169 0.0017 0.0014 233 THR A N 1114 C CA . THR A 145 ? 0.1388 0.1449 0.1568 -0.0055 0.0017 -0.0070 233 THR A CA 1115 C C . THR A 145 ? 0.1286 0.1296 0.1558 0.0003 -0.0039 -0.0087 233 THR A C 1116 O O . THR A 145 ? 0.1352 0.1472 0.1821 0.0049 -0.0025 -0.0098 233 THR A O 1117 C CB . THR A 145 ? 0.1526 0.1451 0.1709 -0.0090 0.0042 0.0083 233 THR A CB 1118 O OG1 . THR A 145 ? 0.1437 0.1632 0.1476 0.0018 0.0135 -0.0208 233 THR A OG1 1119 C CG2 . THR A 145 ? 0.1612 0.1710 0.1690 -0.0183 0.0002 -0.0173 233 THR A CG2 1120 N N . ASN A 146 ? 0.1145 0.1131 0.1302 -0.0051 -0.0058 -0.0001 234 ASN A N 1121 C CA . ASN A 146 ? 0.1246 0.1093 0.1258 -0.0004 0.0061 -0.0066 234 ASN A CA 1122 C C . ASN A 146 ? 0.1194 0.1186 0.1323 0.0037 0.0012 -0.0021 234 ASN A C 1123 O O . ASN A 146 ? 0.1407 0.1258 0.1403 -0.0074 -0.0009 -0.0159 234 ASN A O 1124 C CB . ASN A 146 ? 0.1168 0.1119 0.1343 -0.0020 0.0058 -0.0028 234 ASN A CB 1125 C CG . ASN A 146 ? 0.1365 0.1357 0.1344 0.0060 0.0029 0.0065 234 ASN A CG 1126 O OD1 . ASN A 146 ? 0.1481 0.2138 0.1703 0.0204 -0.0080 -0.0064 234 ASN A OD1 1127 N ND2 . ASN A 146 ? 0.1492 0.1358 0.1487 -0.0077 0.0201 0.0052 234 ASN A ND2 1128 N N . MET A 147 ? 0.1318 0.1269 0.1494 0.0050 0.0031 -0.0100 235 MET A N 1129 C CA . MET A 147 ? 0.1695 0.1560 0.1519 0.0079 0.0140 0.0022 235 MET A CA 1130 C C . MET A 147 ? 0.1687 0.1568 0.1640 0.0045 0.0030 -0.0072 235 MET A C 1131 O O . MET A 147 ? 0.1733 0.1984 0.1671 0.0183 0.0046 -0.0206 235 MET A O 1132 C CB . MET A 147 ? 0.2036 0.1796 0.1670 0.0083 0.0103 0.0047 235 MET A CB 1133 C CG . MET A 147 ? 0.2492 0.2089 0.2030 0.0160 0.0075 0.0206 235 MET A CG 1134 S SD . MET A 147 ? 0.3067 0.2856 0.2754 -0.0010 0.0086 0.0158 235 MET A SD 1135 C CE . MET A 147 ? 0.1315 0.1567 0.1810 0.0075 0.0123 0.0283 235 MET A CE 1136 N N . ASN A 148 ? 0.1605 0.1475 0.1742 0.0032 0.0052 -0.0104 236 ASN A N 1137 C CA . ASN A 148 ? 0.1785 0.1620 0.1848 0.0017 0.0115 -0.0142 236 ASN A CA 1138 C C . ASN A 148 ? 0.1703 0.1617 0.1827 0.0000 0.0174 -0.0131 236 ASN A C 1139 O O . ASN A 148 ? 0.1966 0.1741 0.2157 0.0030 0.0322 -0.0254 236 ASN A O 1140 C CB . ASN A 148 ? 0.1955 0.1894 0.2286 0.0090 0.0084 0.0000 236 ASN A CB 1141 C CG . ASN A 148 ? 0.2754 0.2742 0.2557 0.0036 -0.0057 -0.0017 236 ASN A CG 1142 O OD1 . ASN A 148 ? 0.3347 0.3201 0.3027 0.0290 -0.0107 -0.0237 236 ASN A OD1 1143 N ND2 . ASN A 148 ? 0.3408 0.3098 0.3501 0.0119 0.0050 0.0161 236 ASN A ND2 1144 N N . VAL A 149 ? 0.1432 0.1310 0.1631 0.0045 0.0067 -0.0112 237 VAL A N 1145 C CA . VAL A 149 ? 0.1507 0.1346 0.1583 0.0019 0.0024 -0.0055 237 VAL A CA 1146 C C . VAL A 149 ? 0.1490 0.1324 0.1598 0.0017 -0.0030 -0.0019 237 VAL A C 1147 O O . VAL A 149 ? 0.1293 0.1235 0.1571 0.0121 -0.0106 -0.0100 237 VAL A O 1148 C CB . VAL A 149 ? 0.1431 0.1284 0.1687 0.0087 0.0034 0.0013 237 VAL A CB 1149 C CG1 . VAL A 149 ? 0.1719 0.1494 0.1800 -0.0033 0.0197 -0.0033 237 VAL A CG1 1150 C CG2 . VAL A 149 ? 0.1584 0.1346 0.1632 0.0074 0.0069 -0.0066 237 VAL A CG2 1151 N N . PRO A 150 ? 0.1502 0.1360 0.1797 0.0090 0.0008 -0.0063 238 PRO A N 1152 C CA . PRO A 150 ? 0.1629 0.1416 0.1793 0.0044 0.0053 -0.0078 238 PRO A CA 1153 C C . PRO A 150 ? 0.1479 0.1215 0.1480 0.0011 -0.0008 -0.0187 238 PRO A C 1154 O O . PRO A 150 ? 0.1514 0.1261 0.1640 0.0074 0.0027 -0.0192 238 PRO A O 1155 C CB . PRO A 150 ? 0.1715 0.1529 0.1823 0.0098 0.0016 -0.0214 238 PRO A CB 1156 C CG . PRO A 150 ? 0.1852 0.1846 0.2012 0.0139 -0.0043 -0.0090 238 PRO A CG 1157 C CD . PRO A 150 ? 0.1630 0.1479 0.1932 0.0134 -0.0038 -0.0066 238 PRO A CD 1158 N N . LYS A 151 ? 0.1347 0.0968 0.1595 -0.0015 -0.0013 -0.0051 239 LYS A N 1159 C CA . LYS A 151 ? 0.1168 0.1162 0.1447 -0.0030 -0.0085 -0.0046 239 LYS A CA 1160 C C . LYS A 151 ? 0.1226 0.1102 0.1403 -0.0001 -0.0037 0.0016 239 LYS A C 1161 O O . LYS A 151 ? 0.1077 0.1121 0.1618 0.0003 -0.0222 0.0003 239 LYS A O 1162 C CB . LYS A 151 ? 0.1185 0.1137 0.1539 0.0074 -0.0025 -0.0059 239 LYS A CB 1163 C CG . LYS A 151 ? 0.1329 0.1334 0.1659 0.0034 -0.0056 -0.0052 239 LYS A CG 1164 C CD . LYS A 151 ? 0.1380 0.1221 0.1910 -0.0081 0.0112 0.0030 239 LYS A CD 1165 C CE . LYS A 151 ? 0.1605 0.1774 0.2148 0.0031 0.0130 0.0086 239 LYS A CE 1166 N NZ . LYS A 151 ? 0.2158 0.1972 0.2627 -0.0176 0.0328 0.0272 239 LYS A NZ 1167 N N . CYS A 152 ? 0.1247 0.0999 0.1330 0.0073 -0.0033 -0.0025 240 CYS A N 1168 C CA A CYS A 152 ? 0.1181 0.0942 0.1337 0.0119 -0.0023 -0.0055 240 CYS A CA 1169 C CA B CYS A 152 ? 0.1293 0.1119 0.1350 0.0053 -0.0010 -0.0045 240 CYS A CA 1170 C C . CYS A 152 ? 0.1240 0.1135 0.1387 0.0114 -0.0044 -0.0028 240 CYS A C 1171 O O . CYS A 152 ? 0.1374 0.0983 0.1516 0.0118 -0.0035 0.0083 240 CYS A O 1172 C CB A CYS A 152 ? 0.1167 0.1090 0.1378 0.0153 -0.0030 -0.0063 240 CYS A CB 1173 C CB B CYS A 152 ? 0.1328 0.1221 0.1338 0.0043 -0.0016 -0.0056 240 CYS A CB 1174 S SG A CYS A 152 ? 0.1450 0.1294 0.1638 -0.0199 0.0016 0.0055 240 CYS A SG 1175 S SG B CYS A 152 ? 0.1848 0.1275 0.1414 -0.0043 0.0082 -0.0319 240 CYS A SG 1176 N N . SER A 153 ? 0.1353 0.1282 0.1388 0.0084 0.0031 -0.0063 241 SER A N 1177 C CA A SER A 153 ? 0.1375 0.1372 0.1443 0.0069 0.0037 -0.0024 241 SER A CA 1178 C CA B SER A 153 ? 0.1372 0.1356 0.1428 0.0072 0.0033 -0.0015 241 SER A CA 1179 C C . SER A 153 ? 0.1325 0.1249 0.1335 0.0064 0.0089 -0.0068 241 SER A C 1180 O O . SER A 153 ? 0.1334 0.1325 0.1419 0.0116 0.0018 0.0028 241 SER A O 1181 C CB A SER A 153 ? 0.1441 0.1468 0.1586 0.0104 0.0012 -0.0090 241 SER A CB 1182 C CB B SER A 153 ? 0.1507 0.1497 0.1465 0.0115 0.0063 -0.0036 241 SER A CB 1183 O OG A SER A 153 ? 0.1958 0.1942 0.2008 0.0001 0.0134 0.0012 241 SER A OG 1184 O OG B SER A 153 ? 0.1788 0.1691 0.1997 0.0052 -0.0025 -0.0004 241 SER A OG 1185 N N . GLY A 154 ? 0.1159 0.1108 0.1330 0.0102 -0.0014 -0.0062 242 GLY A N 1186 C CA . GLY A 154 ? 0.1302 0.1139 0.1326 0.0016 -0.0004 -0.0130 242 GLY A CA 1187 C C . GLY A 154 ? 0.1198 0.1102 0.1261 0.0102 -0.0080 -0.0092 242 GLY A C 1188 O O . GLY A 154 ? 0.1529 0.1372 0.1548 0.0252 -0.0072 -0.0191 242 GLY A O 1189 N N . ALA A 155 ? 0.1182 0.1153 0.1249 0.0164 0.0080 -0.0028 243 ALA A N 1190 C CA . ALA A 155 ? 0.1137 0.1051 0.1366 0.0119 -0.0009 -0.0007 243 ALA A CA 1191 C C . ALA A 155 ? 0.1239 0.1012 0.1329 0.0049 0.0143 -0.0012 243 ALA A C 1192 O O . ALA A 155 ? 0.1081 0.0931 0.1410 0.0110 0.0103 0.0041 243 ALA A O 1193 C CB . ALA A 155 ? 0.1332 0.1150 0.1539 0.0223 0.0139 0.0054 243 ALA A CB 1194 N N . ALA A 156 ? 0.1095 0.0976 0.1212 0.0043 0.0043 -0.0117 244 ALA A N 1195 C CA . ALA A 156 ? 0.1173 0.1072 0.1229 0.0001 0.0061 -0.0016 244 ALA A CA 1196 C C . ALA A 156 ? 0.1137 0.1030 0.1095 -0.0015 0.0077 -0.0025 244 ALA A C 1197 O O . ALA A 156 ? 0.1191 0.0958 0.1184 -0.0060 0.0104 -0.0077 244 ALA A O 1198 C CB . ALA A 156 ? 0.1239 0.1166 0.1234 0.0005 0.0058 0.0023 244 ALA A CB 1199 N N . SER A 157 ? 0.1175 0.1041 0.1122 0.0031 0.0076 -0.0005 245 SER A N 1200 C CA . SER A 157 ? 0.1354 0.1267 0.1272 0.0013 0.0056 0.0092 245 SER A CA 1201 C C . SER A 157 ? 0.1250 0.1228 0.1300 0.0043 0.0002 0.0122 245 SER A C 1202 O O . SER A 157 ? 0.1253 0.1100 0.1380 0.0027 -0.0048 0.0081 245 SER A O 1203 C CB . SER A 157 ? 0.1523 0.1323 0.1374 0.0063 0.0083 0.0088 245 SER A CB 1204 O OG . SER A 157 ? 0.2082 0.2492 0.2347 0.0052 0.0185 0.0016 245 SER A OG 1205 N N . THR A 158 ? 0.1167 0.0910 0.1272 0.0101 0.0055 0.0005 246 THR A N 1206 C CA . THR A 158 ? 0.1130 0.0939 0.1395 -0.0014 -0.0012 0.0025 246 THR A CA 1207 C C . THR A 158 ? 0.1105 0.1033 0.1302 0.0014 0.0035 0.0055 246 THR A C 1208 O O . THR A 158 ? 0.1098 0.0966 0.1398 0.0048 0.0153 0.0092 246 THR A O 1209 C CB . THR A 158 ? 0.1323 0.0927 0.1521 0.0026 0.0116 0.0026 246 THR A CB 1210 O OG1 . THR A 158 ? 0.1540 0.1222 0.1836 -0.0074 -0.0073 -0.0078 246 THR A OG1 1211 C CG2 . THR A 158 ? 0.1352 0.1232 0.1906 -0.0007 0.0084 0.0039 246 THR A CG2 1212 N N . TYR A 159 ? 0.1184 0.0860 0.1151 0.0060 -0.0011 0.0120 247 TYR A N 1213 C CA . TYR A 159 ? 0.1157 0.0958 0.1103 0.0006 0.0087 0.0097 247 TYR A CA 1214 C C . TYR A 159 ? 0.1182 0.0907 0.1073 0.0063 0.0109 0.0027 247 TYR A C 1215 O O . TYR A 159 ? 0.1239 0.0858 0.1252 0.0186 0.0113 0.0037 247 TYR A O 1216 C CB . TYR A 159 ? 0.1090 0.0954 0.1179 -0.0079 0.0034 0.0003 247 TYR A CB 1217 C CG . TYR A 159 ? 0.1077 0.0870 0.1305 -0.0135 0.0042 0.0066 247 TYR A CG 1218 C CD1 . TYR A 159 ? 0.1135 0.1207 0.1109 -0.0029 0.0005 -0.0032 247 TYR A CD1 1219 C CD2 . TYR A 159 ? 0.1134 0.1099 0.1245 -0.0203 0.0108 0.0146 247 TYR A CD2 1220 C CE1 . TYR A 159 ? 0.1136 0.0978 0.1346 -0.0111 0.0111 -0.0036 247 TYR A CE1 1221 C CE2 . TYR A 159 ? 0.1332 0.1004 0.1403 0.0091 -0.0054 0.0021 247 TYR A CE2 1222 C CZ . TYR A 159 ? 0.1299 0.1230 0.1254 -0.0111 0.0124 0.0147 247 TYR A CZ 1223 O OH . TYR A 159 ? 0.1462 0.1272 0.1481 -0.0022 -0.0057 0.0297 247 TYR A OH 1224 N N . ARG A 160 ? 0.1082 0.0730 0.1068 -0.0027 0.0119 0.0000 248 ARG A N 1225 C CA . ARG A 160 ? 0.1031 0.0682 0.0879 -0.0066 0.0071 0.0004 248 ARG A CA 1226 C C . ARG A 160 ? 0.1238 0.0984 0.1022 -0.0101 0.0126 0.0074 248 ARG A C 1227 O O . ARG A 160 ? 0.1730 0.0965 0.1323 0.0002 0.0232 -0.0026 248 ARG A O 1228 C CB A ARG A 160 ? 0.1233 0.1104 0.1272 -0.0044 0.0138 0.0032 248 ARG A CB 1229 C CB B ARG A 160 ? 0.1177 0.1039 0.1158 -0.0001 0.0128 0.0080 248 ARG A CB 1230 C CG A ARG A 160 ? 0.1760 0.1465 0.1778 0.0014 -0.0060 0.0107 248 ARG A CG 1231 C CG B ARG A 160 ? 0.1493 0.1087 0.1233 0.0003 -0.0093 0.0014 248 ARG A CG 1232 C CD A ARG A 160 ? 0.1928 0.2114 0.2000 0.0054 0.0031 -0.0041 248 ARG A CD 1233 C CD B ARG A 160 ? 0.1726 0.1502 0.1746 -0.0051 0.0084 0.0025 248 ARG A CD 1234 N NE A ARG A 160 ? 0.2315 0.2274 0.2255 -0.0075 0.0066 0.0000 248 ARG A NE 1235 N NE B ARG A 160 ? 0.1519 0.1643 0.1713 -0.0044 0.0049 -0.0001 248 ARG A NE 1236 C CZ A ARG A 160 ? 0.2408 0.2475 0.2457 0.0012 0.0039 0.0012 248 ARG A CZ 1237 C CZ B ARG A 160 ? 0.1708 0.1760 0.1731 -0.0003 0.0017 -0.0006 248 ARG A CZ 1238 N NH1 A ARG A 160 ? 0.2738 0.2913 0.2987 -0.0046 -0.0154 -0.0090 248 ARG A NH1 1239 N NH1 B ARG A 160 ? 0.1677 0.1661 0.1765 0.0119 0.0055 0.0013 248 ARG A NH1 1240 N NH2 A ARG A 160 ? 0.2585 0.2632 0.2579 0.0074 0.0081 -0.0020 248 ARG A NH2 1241 N NH2 B ARG A 160 ? 0.1616 0.1675 0.1749 0.0016 -0.0107 0.0020 248 ARG A NH2 1242 N N . GLU A 161 ? 0.1207 0.0953 0.1150 -0.0043 0.0096 0.0033 249 GLU A N 1243 C CA . GLU A 161 ? 0.1331 0.1091 0.1180 0.0030 0.0092 0.0075 249 GLU A CA 1244 C C . GLU A 161 ? 0.1081 0.0930 0.1092 0.0098 0.0043 0.0048 249 GLU A C 1245 O O . GLU A 161 ? 0.1254 0.0849 0.1021 0.0205 0.0022 -0.0004 249 GLU A O 1246 C CB . GLU A 161 ? 0.1472 0.1626 0.1268 0.0000 0.0064 -0.0044 249 GLU A CB 1247 C CG . GLU A 161 ? 0.2315 0.2447 0.2200 0.0095 -0.0077 0.0089 249 GLU A CG 1248 C CD . GLU A 161 ? 0.2958 0.2854 0.2794 -0.0031 -0.0076 -0.0088 249 GLU A CD 1249 O OE1 . GLU A 161 ? 0.3402 0.3490 0.3241 0.0107 0.0064 -0.0138 249 GLU A OE1 1250 O OE2 . GLU A 161 ? 0.3171 0.3155 0.3055 -0.0078 0.0051 0.0019 249 GLU A OE2 1251 N N . LEU A 162 ? 0.1148 0.0731 0.0887 0.0007 0.0070 -0.0028 250 LEU A N 1252 C CA . LEU A 162 ? 0.1032 0.0798 0.1070 -0.0003 0.0032 0.0044 250 LEU A CA 1253 C C . LEU A 162 ? 0.1070 0.0962 0.1027 -0.0044 0.0068 -0.0003 250 LEU A C 1254 O O . LEU A 162 ? 0.1159 0.0870 0.1182 -0.0081 0.0146 -0.0033 250 LEU A O 1255 C CB . LEU A 162 ? 0.1143 0.0698 0.1011 -0.0042 0.0089 0.0031 250 LEU A CB 1256 C CG . LEU A 162 ? 0.1143 0.0928 0.1178 0.0044 0.0069 -0.0037 250 LEU A CG 1257 C CD1 . LEU A 162 ? 0.1281 0.1066 0.1277 -0.0112 0.0115 -0.0106 250 LEU A CD1 1258 C CD2 . LEU A 162 ? 0.1354 0.1383 0.1425 -0.0118 -0.0105 -0.0019 250 LEU A CD2 1259 N N . THR A 163 ? 0.1084 0.0691 0.1106 0.0076 0.0024 -0.0078 251 THR A N 1260 C CA . THR A 163 ? 0.1081 0.0852 0.1048 -0.0044 0.0023 -0.0046 251 THR A CA 1261 C C . THR A 163 ? 0.1224 0.0980 0.1055 0.0031 0.0047 -0.0044 251 THR A C 1262 O O . THR A 163 ? 0.1297 0.0842 0.1038 0.0083 0.0025 -0.0089 251 THR A O 1263 C CB . THR A 163 ? 0.1307 0.0838 0.1417 0.0050 -0.0044 -0.0034 251 THR A CB 1264 O OG1 . THR A 163 ? 0.1694 0.1209 0.1448 0.0226 -0.0098 0.0186 251 THR A OG1 1265 C CG2 . THR A 163 ? 0.1338 0.1245 0.1421 0.0094 -0.0137 0.0005 251 THR A CG2 1266 N N . ILE A 164 ? 0.1164 0.0737 0.0998 0.0032 0.0040 0.0019 252 ILE A N 1267 C CA . ILE A 164 ? 0.1120 0.0779 0.1117 0.0066 -0.0024 0.0018 252 ILE A CA 1268 C C . ILE A 164 ? 0.1124 0.0844 0.1221 0.0029 -0.0036 0.0032 252 ILE A C 1269 O O . ILE A 164 ? 0.1191 0.0754 0.1321 0.0139 -0.0090 0.0067 252 ILE A O 1270 C CB . ILE A 164 ? 0.1305 0.0771 0.1276 0.0059 0.0039 0.0081 252 ILE A CB 1271 C CG1 . ILE A 164 ? 0.1407 0.0897 0.1198 0.0037 0.0089 0.0098 252 ILE A CG1 1272 C CG2 . ILE A 164 ? 0.1400 0.1231 0.1247 0.0046 0.0052 0.0258 252 ILE A CG2 1273 C CD1 . ILE A 164 ? 0.1705 0.1721 0.1491 -0.0042 0.0201 0.0022 252 ILE A CD1 1274 N N . TYR A 165 ? 0.1124 0.0946 0.1229 -0.0018 -0.0072 -0.0024 253 TYR A N 1275 C CA . TYR A 165 ? 0.1152 0.0944 0.1100 -0.0001 -0.0017 -0.0081 253 TYR A CA 1276 C C . TYR A 165 ? 0.1134 0.1020 0.1097 0.0010 -0.0034 -0.0026 253 TYR A C 1277 O O . TYR A 165 ? 0.1141 0.1000 0.1328 0.0134 -0.0047 -0.0089 253 TYR A O 1278 C CB . TYR A 165 ? 0.1273 0.0997 0.1192 -0.0092 0.0001 -0.0059 253 TYR A CB 1279 C CG . TYR A 165 ? 0.1288 0.0853 0.1032 0.0057 0.0003 -0.0039 253 TYR A CG 1280 C CD1 . TYR A 165 ? 0.1398 0.1678 0.1335 -0.0011 0.0066 0.0074 253 TYR A CD1 1281 C CD2 . TYR A 165 ? 0.1145 0.0845 0.1147 0.0010 -0.0081 -0.0039 253 TYR A CD2 1282 C CE1 . TYR A 165 ? 0.1495 0.1515 0.1100 -0.0018 -0.0062 0.0188 253 TYR A CE1 1283 C CE2 . TYR A 165 ? 0.1416 0.0979 0.1287 -0.0039 0.0043 -0.0008 253 TYR A CE2 1284 C CZ . TYR A 165 ? 0.1286 0.1339 0.1416 -0.0029 -0.0041 -0.0008 253 TYR A CZ 1285 O OH . TYR A 165 ? 0.1509 0.1904 0.1755 -0.0111 -0.0084 0.0124 253 TYR A OH 1286 N N . ALA A 166 ? 0.1164 0.0888 0.1219 -0.0021 -0.0038 0.0051 254 ALA A N 1287 C CA . ALA A 166 ? 0.1146 0.1074 0.1179 -0.0072 0.0024 0.0095 254 ALA A CA 1288 C C . ALA A 166 ? 0.1083 0.0995 0.1045 0.0045 0.0076 0.0014 254 ALA A C 1289 O O . ALA A 166 ? 0.1268 0.1043 0.1177 0.0225 0.0082 0.0071 254 ALA A O 1290 C CB . ALA A 166 ? 0.1217 0.0983 0.1265 -0.0096 0.0078 0.0078 254 ALA A CB 1291 N N . LEU A 167 ? 0.1066 0.0772 0.1064 -0.0008 -0.0019 -0.0008 255 LEU A N 1292 C CA . LEU A 167 ? 0.1165 0.0800 0.1086 0.0004 0.0026 -0.0015 255 LEU A CA 1293 C C . LEU A 167 ? 0.1106 0.0910 0.1030 0.0107 -0.0010 -0.0029 255 LEU A C 1294 O O . LEU A 167 ? 0.1497 0.0975 0.1344 0.0234 -0.0037 0.0007 255 LEU A O 1295 C CB . LEU A 167 ? 0.1166 0.0907 0.1283 0.0048 -0.0043 -0.0069 255 LEU A CB 1296 C CG . LEU A 167 ? 0.1254 0.1066 0.1391 0.0006 -0.0091 -0.0047 255 LEU A CG 1297 C CD1 . LEU A 167 ? 0.1340 0.1316 0.1390 0.0094 0.0042 -0.0055 255 LEU A CD1 1298 C CD2 . LEU A 167 ? 0.1465 0.1250 0.1562 0.0040 0.0091 0.0167 255 LEU A CD2 1299 N N . LYS A 168 ? 0.1106 0.0756 0.1146 0.0087 0.0049 0.0018 256 LYS A N 1300 C CA . LYS A 168 ? 0.1137 0.0848 0.1152 0.0006 -0.0032 0.0161 256 LYS A CA 1301 C C . LYS A 168 ? 0.1063 0.1042 0.1014 0.0119 -0.0070 0.0059 256 LYS A C 1302 O O . LYS A 168 ? 0.1200 0.0829 0.1342 0.0114 -0.0058 0.0106 256 LYS A O 1303 C CB . LYS A 168 ? 0.1290 0.0931 0.1260 0.0056 -0.0030 0.0121 256 LYS A CB 1304 C CG . LYS A 168 ? 0.1513 0.1146 0.1755 0.0026 0.0051 0.0183 256 LYS A CG 1305 C CD . LYS A 168 ? 0.2637 0.2630 0.2382 0.0043 0.0136 -0.0104 256 LYS A CD 1306 C CE . LYS A 168 ? 0.3163 0.3140 0.3086 0.0111 0.0030 -0.0014 256 LYS A CE 1307 N NZ . LYS A 168 ? 0.3653 0.3872 0.3826 -0.0210 0.0003 0.0022 256 LYS A NZ 1308 N N . GLN A 169 ? 0.1175 0.0989 0.0976 0.0003 -0.0040 0.0006 257 GLN A N 1309 C CA . GLN A 169 ? 0.1172 0.0832 0.1106 0.0102 -0.0044 0.0066 257 GLN A CA 1310 C C . GLN A 169 ? 0.1042 0.0781 0.1019 -0.0020 -0.0015 0.0034 257 GLN A C 1311 O O . GLN A 169 ? 0.1237 0.1275 0.1144 0.0185 -0.0076 -0.0035 257 GLN A O 1312 C CB . GLN A 169 ? 0.1256 0.0959 0.1162 0.0018 -0.0052 -0.0063 257 GLN A CB 1313 C CG . GLN A 169 ? 0.1589 0.1340 0.1307 0.0008 -0.0064 -0.0033 257 GLN A CG 1314 C CD . GLN A 169 ? 0.1814 0.2005 0.1839 0.0151 -0.0106 -0.0110 257 GLN A CD 1315 O OE1 . GLN A 169 ? 0.2078 0.2703 0.2377 0.0242 -0.0093 -0.0398 257 GLN A OE1 1316 N NE2 . GLN A 169 ? 0.2227 0.2321 0.1951 0.0519 -0.0019 -0.0174 257 GLN A NE2 1317 N N . LEU A 170 ? 0.0938 0.0721 0.0918 0.0050 0.0013 -0.0014 258 LEU A N 1318 C CA . LEU A 170 ? 0.1024 0.0776 0.0831 0.0023 0.0028 -0.0062 258 LEU A CA 1319 C C . LEU A 170 ? 0.1110 0.0815 0.0908 0.0106 -0.0002 0.0007 258 LEU A C 1320 O O . LEU A 170 ? 0.1222 0.0845 0.1131 0.0019 -0.0046 -0.0107 258 LEU A O 1321 C CB . LEU A 170 ? 0.1120 0.0930 0.0808 -0.0088 0.0000 -0.0064 258 LEU A CB 1322 C CG . LEU A 170 ? 0.1053 0.0813 0.0907 0.0023 0.0035 -0.0015 258 LEU A CG 1323 C CD1 . LEU A 170 ? 0.1412 0.1207 0.1188 -0.0025 0.0056 0.0064 258 LEU A CD1 1324 C CD2 . LEU A 170 ? 0.1246 0.1149 0.1386 -0.0142 0.0042 0.0005 258 LEU A CD2 1325 N N . ASP A 171 ? 0.1031 0.0825 0.0954 0.0016 -0.0007 -0.0028 259 ASP A N 1326 C CA . ASP A 171 ? 0.1163 0.0912 0.1131 0.0016 -0.0003 -0.0069 259 ASP A CA 1327 C C . ASP A 171 ? 0.1076 0.0909 0.1106 0.0004 -0.0003 -0.0016 259 ASP A C 1328 O O . ASP A 171 ? 0.1445 0.1299 0.1306 0.0211 0.0004 0.0006 259 ASP A O 1329 C CB . ASP A 171 ? 0.1136 0.0815 0.1206 0.0130 0.0085 -0.0103 259 ASP A CB 1330 C CG . ASP A 171 ? 0.1265 0.1060 0.1208 0.0068 0.0018 0.0097 259 ASP A CG 1331 O OD1 . ASP A 171 ? 0.1570 0.1002 0.1463 -0.0062 -0.0034 0.0063 259 ASP A OD1 1332 O OD2 . ASP A 171 ? 0.1758 0.1235 0.1458 -0.0128 0.0195 0.0085 259 ASP A OD2 1333 N N . LEU A 172 ? 0.1113 0.0911 0.1059 0.0002 -0.0012 0.0008 260 LEU A N 1334 C CA . LEU A 172 ? 0.0987 0.0772 0.1006 0.0022 -0.0046 0.0041 260 LEU A CA 1335 C C . LEU A 172 ? 0.0955 0.0889 0.1025 -0.0010 0.0030 -0.0034 260 LEU A C 1336 O O . LEU A 172 ? 0.1064 0.0685 0.1160 0.0080 -0.0021 -0.0046 260 LEU A O 1337 C CB . LEU A 172 ? 0.1186 0.0895 0.1108 -0.0135 -0.0045 -0.0103 260 LEU A CB 1338 C CG . LEU A 172 ? 0.1345 0.0945 0.1126 -0.0202 0.0089 -0.0208 260 LEU A CG 1339 C CD1 . LEU A 172 ? 0.1498 0.1253 0.1425 -0.0214 0.0150 -0.0049 260 LEU A CD1 1340 C CD2 . LEU A 172 ? 0.1593 0.1504 0.1480 -0.0395 0.0003 -0.0101 260 LEU A CD2 1341 N N . PRO A 173 ? 0.0995 0.0841 0.1029 -0.0032 -0.0095 0.0017 261 PRO A N 1342 C CA . PRO A 173 ? 0.0890 0.0677 0.0953 -0.0058 -0.0044 0.0031 261 PRO A CA 1343 C C . PRO A 173 ? 0.0977 0.0721 0.0980 0.0002 -0.0072 0.0111 261 PRO A C 1344 O O . PRO A 173 ? 0.0903 0.0689 0.0956 0.0043 -0.0088 -0.0038 261 PRO A O 1345 C CB . PRO A 173 ? 0.1018 0.0730 0.1100 0.0048 0.0030 0.0072 261 PRO A CB 1346 C CG . PRO A 173 ? 0.1182 0.0942 0.1264 0.0021 -0.0047 0.0028 261 PRO A CG 1347 C CD . PRO A 173 ? 0.1006 0.0910 0.1018 0.0065 -0.0036 -0.0003 261 PRO A CD 1348 N N . HIS A 174 ? 0.0830 0.0625 0.0882 -0.0044 -0.0059 -0.0049 262 HIS A N 1349 C CA . HIS A 174 ? 0.0893 0.0711 0.0920 -0.0020 0.0036 0.0007 262 HIS A CA 1350 C C . HIS A 174 ? 0.0930 0.0771 0.0871 0.0017 0.0007 -0.0023 262 HIS A C 1351 O O . HIS A 174 ? 0.1054 0.0928 0.0831 0.0091 -0.0042 -0.0008 262 HIS A O 1352 C CB . HIS A 174 ? 0.0947 0.0658 0.0944 0.0034 0.0035 0.0025 262 HIS A CB 1353 C CG . HIS A 174 ? 0.0995 0.0915 0.0963 -0.0026 -0.0035 -0.0054 262 HIS A CG 1354 N ND1 . HIS A 174 ? 0.1171 0.0936 0.1183 0.0000 -0.0019 -0.0037 262 HIS A ND1 1355 C CD2 . HIS A 174 ? 0.1030 0.1046 0.0849 -0.0001 -0.0034 -0.0094 262 HIS A CD2 1356 C CE1 . HIS A 174 ? 0.1210 0.1093 0.1197 -0.0177 -0.0054 -0.0117 262 HIS A CE1 1357 N NE2 . HIS A 174 ? 0.1159 0.1009 0.1103 -0.0061 -0.0026 -0.0255 262 HIS A NE2 1358 N N . VAL A 175 ? 0.0855 0.0586 0.0837 0.0054 -0.0010 0.0091 263 VAL A N 1359 C CA . VAL A 175 ? 0.1006 0.0811 0.0960 0.0141 -0.0050 0.0076 263 VAL A CA 1360 C C . VAL A 175 ? 0.0999 0.0715 0.1023 0.0061 0.0003 0.0078 263 VAL A C 1361 O O . VAL A 175 ? 0.0980 0.0946 0.1144 0.0055 0.0076 0.0214 263 VAL A O 1362 C CB . VAL A 175 ? 0.1136 0.0678 0.1164 0.0066 -0.0071 0.0061 263 VAL A CB 1363 C CG1 . VAL A 175 ? 0.1124 0.1039 0.1001 0.0041 0.0009 -0.0102 263 VAL A CG1 1364 C CG2 . VAL A 175 ? 0.1189 0.0966 0.1264 0.0038 -0.0077 -0.0033 263 VAL A CG2 1365 N N . ALA A 176 ? 0.1022 0.0786 0.0902 0.0035 -0.0043 0.0042 264 ALA A N 1366 C CA . ALA A 176 ? 0.0957 0.0759 0.0870 0.0047 0.0023 0.0029 264 ALA A CA 1367 C C . ALA A 176 ? 0.0912 0.0687 0.0904 -0.0024 0.0031 0.0136 264 ALA A C 1368 O O . ALA A 176 ? 0.1374 0.0890 0.1257 0.0071 0.0317 0.0161 264 ALA A O 1369 C CB . ALA A 176 ? 0.1096 0.0877 0.1137 -0.0020 -0.0067 -0.0043 264 ALA A CB 1370 N N . MET A 177 ? 0.0889 0.0780 0.0916 0.0082 0.0010 0.0137 265 MET A N 1371 C CA . MET A 177 ? 0.0941 0.0730 0.0885 0.0000 0.0024 0.0132 265 MET A CA 1372 C C . MET A 177 ? 0.0891 0.0904 0.0872 -0.0006 0.0050 0.0139 265 MET A C 1373 O O . MET A 177 ? 0.0937 0.0680 0.1109 0.0021 0.0001 0.0146 265 MET A O 1374 C CB . MET A 177 ? 0.1090 0.1051 0.1036 0.0138 -0.0031 -0.0001 265 MET A CB 1375 C CG . MET A 177 ? 0.1111 0.1214 0.1000 0.0130 0.0043 0.0171 265 MET A CG 1376 S SD . MET A 177 ? 0.1304 0.1164 0.1192 0.0031 -0.0106 -0.0053 265 MET A SD 1377 C CE . MET A 177 ? 0.1125 0.1075 0.1234 0.0142 0.0034 -0.0073 265 MET A CE 1378 N N . TYR A 178 ? 0.0823 0.0744 0.0786 0.0033 0.0000 0.0102 266 TYR A N 1379 C CA . TYR A 178 ? 0.0869 0.0788 0.0914 -0.0014 0.0036 0.0003 266 TYR A CA 1380 C C . TYR A 178 ? 0.0798 0.0619 0.1075 -0.0088 0.0112 0.0039 266 TYR A C 1381 O O . TYR A 178 ? 0.0945 0.0780 0.1158 -0.0072 0.0144 -0.0033 266 TYR A O 1382 C CB . TYR A 178 ? 0.0808 0.0620 0.0915 -0.0053 -0.0010 0.0000 266 TYR A CB 1383 C CG . TYR A 178 ? 0.0812 0.0706 0.0666 0.0003 -0.0161 -0.0003 266 TYR A CG 1384 C CD1 . TYR A 178 ? 0.0898 0.0777 0.0875 -0.0101 0.0013 0.0093 266 TYR A CD1 1385 C CD2 . TYR A 178 ? 0.0806 0.0833 0.0794 -0.0017 -0.0102 0.0058 266 TYR A CD2 1386 C CE1 . TYR A 178 ? 0.0879 0.0895 0.0821 0.0091 -0.0038 -0.0010 266 TYR A CE1 1387 C CE2 . TYR A 178 ? 0.0677 0.0715 0.0953 -0.0147 -0.0166 0.0004 266 TYR A CE2 1388 C CZ . TYR A 178 ? 0.0953 0.0704 0.0801 0.0032 -0.0076 -0.0043 266 TYR A CZ 1389 O OH . TYR A 178 ? 0.1097 0.1044 0.1139 0.0166 -0.0048 -0.0232 266 TYR A OH 1390 N N . MET A 179 ? 0.0982 0.0718 0.0924 -0.0003 0.0100 0.0028 267 MET A N 1391 C CA . MET A 179 ? 0.0868 0.0824 0.0864 -0.0078 -0.0021 -0.0070 267 MET A CA 1392 C C . MET A 179 ? 0.0809 0.0757 0.0915 -0.0079 0.0008 -0.0038 267 MET A C 1393 O O . MET A 179 ? 0.0872 0.0888 0.0965 -0.0109 -0.0085 0.0011 267 MET A O 1394 C CB . MET A 179 ? 0.1081 0.0930 0.1160 0.0098 0.0033 -0.0029 267 MET A CB 1395 C CG . MET A 179 ? 0.1504 0.1521 0.1245 0.0113 0.0143 0.0171 267 MET A CG 1396 S SD . MET A 179 ? 0.1430 0.1395 0.1242 -0.0173 0.0089 0.0036 267 MET A SD 1397 C CE . MET A 179 ? 0.1738 0.1347 0.1460 -0.0041 -0.0111 0.0122 267 MET A CE 1398 N N . ASP A 180 ? 0.0936 0.0776 0.1096 -0.0055 -0.0057 -0.0022 268 ASP A N 1399 C CA . ASP A 180 ? 0.1007 0.0983 0.1101 -0.0054 -0.0007 0.0016 268 ASP A CA 1400 C C . ASP A 180 ? 0.1041 0.1070 0.1099 0.0029 0.0012 -0.0018 268 ASP A C 1401 O O . ASP A 180 ? 0.1134 0.1405 0.1082 0.0097 0.0042 0.0027 268 ASP A O 1402 C CB . ASP A 180 ? 0.1133 0.0972 0.1212 -0.0046 -0.0069 0.0027 268 ASP A CB 1403 C CG . ASP A 180 ? 0.1089 0.1361 0.1357 0.0071 -0.0111 -0.0018 268 ASP A CG 1404 O OD1 . ASP A 180 ? 0.1613 0.1873 0.1845 -0.0064 0.0187 -0.0003 268 ASP A OD1 1405 O OD2 . ASP A 180 ? 0.1332 0.1710 0.1774 -0.0033 0.0134 -0.0143 268 ASP A OD2 1406 N N . ALA A 181 ? 0.0906 0.0827 0.0894 0.0090 0.0036 -0.0054 269 ALA A N 1407 C CA . ALA A 181 ? 0.0904 0.1044 0.1127 0.0019 0.0006 0.0008 269 ALA A CA 1408 C C . ALA A 181 ? 0.0889 0.1032 0.0989 -0.0035 -0.0016 0.0047 269 ALA A C 1409 O O . ALA A 181 ? 0.1036 0.1139 0.1171 -0.0099 -0.0052 -0.0097 269 ALA A O 1410 C CB . ALA A 181 ? 0.0996 0.1095 0.1142 -0.0026 -0.0017 0.0103 269 ALA A CB 1411 N N . GLY A 182 ? 0.0858 0.1004 0.1032 -0.0020 -0.0126 0.0098 270 GLY A N 1412 C CA . GLY A 182 ? 0.0947 0.1006 0.1066 0.0087 -0.0044 0.0029 270 GLY A CA 1413 C C . GLY A 182 ? 0.0967 0.1165 0.0943 0.0107 -0.0036 0.0016 270 GLY A C 1414 O O . GLY A 182 ? 0.1092 0.1274 0.1033 0.0197 -0.0018 0.0103 270 GLY A O 1415 N N . HIS A 183 ? 0.0963 0.1039 0.0909 0.0084 -0.0020 -0.0028 271 HIS A N 1416 C CA . HIS A 183 ? 0.1021 0.1009 0.0922 0.0074 0.0001 -0.0022 271 HIS A CA 1417 C C . HIS A 183 ? 0.0975 0.0859 0.0971 0.0051 -0.0044 0.0010 271 HIS A C 1418 O O . HIS A 183 ? 0.1026 0.0931 0.1109 0.0180 0.0088 0.0095 271 HIS A O 1419 C CB . HIS A 183 ? 0.0940 0.1011 0.0891 0.0010 0.0023 -0.0066 271 HIS A CB 1420 C CG . HIS A 183 ? 0.1034 0.0990 0.0893 0.0038 0.0069 0.0053 271 HIS A CG 1421 N ND1 . HIS A 183 ? 0.1181 0.1235 0.1174 -0.0025 0.0004 -0.0144 271 HIS A ND1 1422 C CD2 . HIS A 183 ? 0.1114 0.1120 0.1303 -0.0036 -0.0025 -0.0051 271 HIS A CD2 1423 C CE1 . HIS A 183 ? 0.1145 0.1168 0.1461 0.0041 0.0031 0.0037 271 HIS A CE1 1424 N NE2 . HIS A 183 ? 0.1298 0.1120 0.1203 0.0015 -0.0042 -0.0069 271 HIS A NE2 1425 N N . ALA A 184 ? 0.0983 0.0820 0.0872 0.0016 0.0027 -0.0015 272 ALA A N 1426 C CA . ALA A 184 ? 0.0981 0.0888 0.0994 -0.0038 0.0032 -0.0045 272 ALA A CA 1427 C C . ALA A 184 ? 0.1106 0.0947 0.1097 0.0031 0.0030 0.0024 272 ALA A C 1428 O O . ALA A 184 ? 0.1004 0.1010 0.1242 0.0051 0.0097 -0.0025 272 ALA A O 1429 C CB . ALA A 184 ? 0.1114 0.1157 0.1185 -0.0069 -0.0039 -0.0003 272 ALA A CB 1430 N N . GLY A 185 ? 0.0888 0.0945 0.1145 -0.0031 0.0033 -0.0012 273 GLY A N 1431 C CA . GLY A 185 ? 0.0861 0.0950 0.1086 0.0123 0.0019 0.0082 273 GLY A CA 1432 C C . GLY A 185 ? 0.0906 0.0987 0.1180 0.0050 -0.0055 -0.0011 273 GLY A C 1433 O O . GLY A 185 ? 0.1158 0.0950 0.1467 0.0018 -0.0061 -0.0009 273 GLY A O 1434 N N . TRP A 186 ? 0.1055 0.0955 0.1240 0.0012 -0.0094 -0.0032 274 TRP A N 1435 C CA . TRP A 186 ? 0.0974 0.0963 0.1081 0.0013 0.0049 -0.0001 274 TRP A CA 1436 C C . TRP A 186 ? 0.1091 0.1087 0.1194 0.0076 0.0042 0.0073 274 TRP A C 1437 O O . TRP A 186 ? 0.1171 0.1043 0.1337 0.0081 0.0179 0.0047 274 TRP A O 1438 C CB . TRP A 186 ? 0.1072 0.1011 0.1082 0.0036 0.0015 -0.0011 274 TRP A CB 1439 C CG . TRP A 186 ? 0.1129 0.0792 0.1197 0.0075 0.0027 -0.0028 274 TRP A CG 1440 C CD1 . TRP A 186 ? 0.1204 0.1166 0.1247 -0.0085 0.0024 -0.0141 274 TRP A CD1 1441 C CD2 . TRP A 186 ? 0.1291 0.0989 0.1338 0.0086 -0.0038 0.0133 274 TRP A CD2 1442 N NE1 . TRP A 186 ? 0.1258 0.1095 0.1171 -0.0047 -0.0094 -0.0091 274 TRP A NE1 1443 C CE2 . TRP A 186 ? 0.1188 0.1121 0.1291 0.0053 -0.0019 0.0038 274 TRP A CE2 1444 C CE3 . TRP A 186 ? 0.1372 0.0942 0.1387 -0.0035 0.0029 0.0124 274 TRP A CE3 1445 C CZ2 . TRP A 186 ? 0.1379 0.1474 0.1475 -0.0023 -0.0110 0.0020 274 TRP A CZ2 1446 C CZ3 . TRP A 186 ? 0.1402 0.1290 0.1538 -0.0078 0.0015 0.0173 274 TRP A CZ3 1447 C CH2 . TRP A 186 ? 0.1368 0.1352 0.1532 -0.0086 -0.0032 0.0148 274 TRP A CH2 1448 N N . LEU A 187 ? 0.1092 0.1009 0.1125 0.0057 0.0139 0.0007 275 LEU A N 1449 C CA . LEU A 187 ? 0.1032 0.0891 0.1031 0.0023 0.0059 -0.0012 275 LEU A CA 1450 C C . LEU A 187 ? 0.1028 0.1114 0.1118 -0.0039 0.0028 0.0109 275 LEU A C 1451 O O . LEU A 187 ? 0.1127 0.1238 0.1351 -0.0038 0.0145 0.0145 275 LEU A O 1452 C CB . LEU A 187 ? 0.1077 0.0898 0.1014 -0.0069 0.0059 0.0069 275 LEU A CB 1453 C CG . LEU A 187 ? 0.1193 0.0969 0.1038 -0.0009 -0.0014 0.0014 275 LEU A CG 1454 C CD1 . LEU A 187 ? 0.1144 0.0976 0.1216 -0.0055 -0.0085 -0.0122 275 LEU A CD1 1455 C CD2 . LEU A 187 ? 0.1290 0.1325 0.1216 0.0055 0.0070 0.0045 275 LEU A CD2 1456 N N . GLY A 188 ? 0.1058 0.0886 0.1159 -0.0002 -0.0017 0.0063 276 GLY A N 1457 C CA . GLY A 188 ? 0.1148 0.0867 0.1209 0.0061 -0.0006 0.0131 276 GLY A CA 1458 C C . GLY A 188 ? 0.1065 0.0991 0.1268 -0.0080 -0.0016 0.0088 276 GLY A C 1459 O O . GLY A 188 ? 0.1242 0.1067 0.1385 0.0012 -0.0118 0.0023 276 GLY A O 1460 N N . TRP A 189 ? 0.1092 0.1096 0.1357 0.0046 0.0038 0.0070 277 TRP A N 1461 C CA . TRP A 189 ? 0.1110 0.1058 0.1270 0.0070 0.0006 0.0118 277 TRP A CA 1462 C C . TRP A 189 ? 0.1123 0.1218 0.1283 0.0094 -0.0027 0.0138 277 TRP A C 1463 O O . TRP A 189 ? 0.1313 0.1383 0.1219 0.0105 0.0059 0.0164 277 TRP A O 1464 C CB . TRP A 189 ? 0.1026 0.1144 0.1327 0.0138 0.0083 0.0057 277 TRP A CB 1465 C CG . TRP A 189 ? 0.1080 0.1114 0.1306 -0.0023 0.0125 -0.0005 277 TRP A CG 1466 C CD1 . TRP A 189 ? 0.1009 0.1115 0.1280 0.0068 -0.0019 0.0030 277 TRP A CD1 1467 C CD2 . TRP A 189 ? 0.1125 0.0990 0.1298 0.0056 0.0179 -0.0027 277 TRP A CD2 1468 N NE1 . TRP A 189 ? 0.1116 0.1299 0.1513 0.0043 -0.0075 0.0173 277 TRP A NE1 1469 C CE2 . TRP A 189 ? 0.1119 0.0965 0.1544 -0.0003 0.0043 0.0093 277 TRP A CE2 1470 C CE3 . TRP A 189 ? 0.1179 0.1118 0.1287 -0.0042 -0.0062 0.0137 277 TRP A CE3 1471 C CZ2 . TRP A 189 ? 0.1347 0.1250 0.1582 0.0026 0.0034 0.0123 277 TRP A CZ2 1472 C CZ3 . TRP A 189 ? 0.1376 0.1417 0.1653 0.0189 0.0061 0.0285 277 TRP A CZ3 1473 C CH2 . TRP A 189 ? 0.1224 0.1233 0.1654 0.0088 -0.0028 0.0289 277 TRP A CH2 1474 N N . PRO A 190 ? 0.1259 0.1391 0.1425 0.0074 -0.0004 0.0128 278 PRO A N 1475 C CA . PRO A 190 ? 0.1240 0.1451 0.1659 0.0049 0.0012 0.0117 278 PRO A CA 1476 C C . PRO A 190 ? 0.1318 0.1689 0.1677 0.0045 0.0063 0.0158 278 PRO A C 1477 O O . PRO A 190 ? 0.1536 0.1825 0.1764 0.0036 0.0036 0.0390 278 PRO A O 1478 C CB . PRO A 190 ? 0.1237 0.1593 0.1755 0.0024 0.0032 0.0155 278 PRO A CB 1479 C CG . PRO A 190 ? 0.1094 0.1441 0.1763 0.0040 -0.0030 0.0005 278 PRO A CG 1480 C CD . PRO A 190 ? 0.1219 0.1396 0.1398 -0.0023 -0.0041 0.0085 278 PRO A CD 1481 N N . ALA A 191 ? 0.1337 0.1743 0.1643 0.0137 0.0101 0.0148 279 ALA A N 1482 C CA . ALA A 191 ? 0.1545 0.1847 0.1693 0.0102 0.0021 0.0094 279 ALA A CA 1483 C C . ALA A 191 ? 0.1410 0.1869 0.1568 0.0062 0.0049 0.0014 279 ALA A C 1484 O O . ALA A 191 ? 0.1429 0.2196 0.1574 0.0180 0.0126 0.0030 279 ALA A O 1485 C CB . ALA A 191 ? 0.1708 0.2119 0.1955 0.0109 0.0100 -0.0041 279 ALA A CB 1486 N N . ASN A 192 ? 0.1372 0.1715 0.1402 0.0113 0.0017 0.0092 280 ASN A N 1487 C CA . ASN A 192 ? 0.1327 0.1623 0.1452 0.0057 -0.0015 0.0029 280 ASN A CA 1488 C C . ASN A 192 ? 0.1392 0.1593 0.1454 0.0017 0.0038 0.0039 280 ASN A C 1489 O O . ASN A 192 ? 0.1337 0.1544 0.1339 0.0055 0.0010 0.0069 280 ASN A O 1490 C CB . ASN A 192 ? 0.1390 0.1615 0.1478 0.0053 0.0082 -0.0012 280 ASN A CB 1491 C CG . ASN A 192 ? 0.1435 0.1571 0.1494 0.0015 0.0087 0.0089 280 ASN A CG 1492 O OD1 . ASN A 192 ? 0.2045 0.1632 0.1809 0.0158 0.0396 -0.0147 280 ASN A OD1 1493 N ND2 . ASN A 192 ? 0.1616 0.1255 0.1753 -0.0010 0.0083 0.0116 280 ASN A ND2 1494 N N . ILE A 193 ? 0.1419 0.1530 0.1396 0.0180 0.0012 -0.0045 281 ILE A N 1495 C CA . ILE A 193 ? 0.1600 0.1569 0.1724 0.0086 0.0025 -0.0059 281 ILE A CA 1496 C C . ILE A 193 ? 0.1473 0.1557 0.1651 -0.0022 0.0027 -0.0030 281 ILE A C 1497 O O . ILE A 193 ? 0.1379 0.1387 0.1734 0.0021 -0.0040 0.0000 281 ILE A O 1498 C CB . ILE A 193 ? 0.2003 0.1818 0.1953 0.0036 -0.0002 -0.0117 281 ILE A CB 1499 C CG1 . ILE A 193 ? 0.2639 0.2475 0.2518 0.0026 -0.0056 0.0129 281 ILE A CG1 1500 C CG2 . ILE A 193 ? 0.2330 0.2155 0.2132 0.0062 -0.0090 -0.0111 281 ILE A CG2 1501 C CD1 . ILE A 193 ? 0.2899 0.3013 0.2771 -0.0050 0.0166 0.0013 281 ILE A CD1 1502 N N . GLN A 194 ? 0.1351 0.1601 0.1740 0.0060 -0.0052 -0.0024 282 GLN A N 1503 C CA . GLN A 194 ? 0.1524 0.1775 0.1696 0.0007 0.0016 0.0025 282 GLN A CA 1504 C C . GLN A 194 ? 0.1355 0.1554 0.1613 -0.0059 0.0100 0.0047 282 GLN A C 1505 O O . GLN A 194 ? 0.1491 0.1517 0.1635 -0.0082 0.0121 0.0126 282 GLN A O 1506 C CB . GLN A 194 ? 0.1661 0.2093 0.2004 -0.0006 0.0038 0.0028 282 GLN A CB 1507 C CG . GLN A 194 ? 0.2380 0.2466 0.2425 -0.0010 0.0002 0.0175 282 GLN A CG 1508 C CD . GLN A 194 ? 0.2683 0.3028 0.2859 -0.0025 0.0107 0.0060 282 GLN A CD 1509 O OE1 . GLN A 194 ? 0.2983 0.3382 0.3130 -0.0065 -0.0041 0.0021 282 GLN A OE1 1510 N NE2 . GLN A 194 ? 0.3132 0.3279 0.2992 -0.0042 0.0035 0.0025 282 GLN A NE2 1511 N N . PRO A 195 ? 0.1285 0.1359 0.1522 0.0038 0.0053 -0.0007 283 PRO A N 1512 C CA . PRO A 195 ? 0.1340 0.1362 0.1374 0.0034 0.0055 0.0028 283 PRO A CA 1513 C C . PRO A 195 ? 0.1244 0.1184 0.1359 -0.0001 0.0068 -0.0029 283 PRO A C 1514 O O . PRO A 195 ? 0.1299 0.1307 0.1346 0.0028 0.0159 -0.0134 283 PRO A O 1515 C CB . PRO A 195 ? 0.1505 0.1602 0.1762 0.0054 0.0194 -0.0065 283 PRO A CB 1516 C CG . PRO A 195 ? 0.2098 0.1803 0.1751 0.0098 -0.0157 -0.0022 283 PRO A CG 1517 C CD . PRO A 195 ? 0.1360 0.1563 0.1537 0.0062 0.0058 0.0118 283 PRO A CD 1518 N N . ALA A 196 ? 0.1103 0.0922 0.1239 0.0036 0.0069 0.0011 284 ALA A N 1519 C CA . ALA A 196 ? 0.1055 0.0966 0.1133 -0.0024 0.0094 -0.0009 284 ALA A CA 1520 C C . ALA A 196 ? 0.1060 0.1026 0.1215 0.0010 0.0056 0.0046 284 ALA A C 1521 O O . ALA A 196 ? 0.1059 0.1131 0.1216 -0.0133 -0.0009 -0.0086 284 ALA A O 1522 C CB . ALA A 196 ? 0.1175 0.1239 0.1279 0.0003 0.0108 0.0067 284 ALA A CB 1523 N N . ALA A 197 ? 0.1036 0.0923 0.1220 0.0040 -0.0007 -0.0032 285 ALA A N 1524 C CA . ALA A 197 ? 0.1076 0.0919 0.1254 -0.0015 -0.0007 0.0044 285 ALA A CA 1525 C C . ALA A 197 ? 0.1176 0.1108 0.1295 -0.0032 0.0012 0.0016 285 ALA A C 1526 O O . ALA A 197 ? 0.1276 0.1121 0.1427 0.0005 0.0095 0.0297 285 ALA A O 1527 C CB . ALA A 197 ? 0.1171 0.1012 0.1215 -0.0078 -0.0017 0.0021 285 ALA A CB 1528 N N . GLU A 198 ? 0.1248 0.1196 0.1409 0.0015 0.0059 0.0001 286 GLU A N 1529 C CA . GLU A 198 ? 0.1371 0.1282 0.1488 -0.0014 0.0012 0.0105 286 GLU A CA 1530 C C . GLU A 198 ? 0.1294 0.1291 0.1332 -0.0037 -0.0010 0.0060 286 GLU A C 1531 O O . GLU A 198 ? 0.1548 0.1250 0.1457 -0.0035 0.0040 0.0292 286 GLU A O 1532 C CB . GLU A 198 ? 0.1661 0.1568 0.1518 0.0062 -0.0013 0.0054 286 GLU A CB 1533 C CG . GLU A 198 ? 0.2366 0.2418 0.2336 -0.0191 -0.0022 0.0089 286 GLU A CG 1534 C CD . GLU A 198 ? 0.3278 0.3425 0.3495 0.0142 0.0023 -0.0044 286 GLU A CD 1535 O OE1 . GLU A 198 ? 0.4201 0.3818 0.4252 -0.0063 0.0029 -0.0053 286 GLU A OE1 1536 O OE2 . GLU A 198 ? 0.3672 0.4044 0.4019 -0.0162 0.0154 0.0089 286 GLU A OE2 1537 N N . LEU A 199 ? 0.1183 0.1256 0.1217 0.0035 0.0100 0.0052 287 LEU A N 1538 C CA . LEU A 199 ? 0.1265 0.1122 0.1154 -0.0021 -0.0005 -0.0051 287 LEU A CA 1539 C C . LEU A 199 ? 0.1240 0.1016 0.1177 -0.0022 -0.0023 0.0062 287 LEU A C 1540 O O . LEU A 199 ? 0.1276 0.1133 0.1288 -0.0122 -0.0053 0.0089 287 LEU A O 1541 C CB . LEU A 199 ? 0.1307 0.1179 0.1385 0.0056 -0.0015 0.0060 287 LEU A CB 1542 C CG . LEU A 199 ? 0.1665 0.1381 0.1901 0.0028 -0.0023 0.0133 287 LEU A CG 1543 C CD1 . LEU A 199 ? 0.2115 0.2088 0.2360 -0.0113 0.0036 -0.0032 287 LEU A CD1 1544 C CD2 . LEU A 199 ? 0.1993 0.1792 0.2217 0.0014 0.0098 0.0201 287 LEU A CD2 1545 N N . PHE A 200 ? 0.1286 0.0965 0.1138 -0.0071 -0.0006 0.0068 288 PHE A N 1546 C CA . PHE A 200 ? 0.1075 0.1086 0.1223 -0.0040 -0.0044 0.0096 288 PHE A CA 1547 C C . PHE A 200 ? 0.1124 0.1071 0.1245 -0.0047 -0.0066 -0.0008 288 PHE A C 1548 O O . PHE A 200 ? 0.1183 0.0959 0.1422 -0.0023 -0.0062 0.0090 288 PHE A O 1549 C CB . PHE A 200 ? 0.1250 0.1142 0.1292 -0.0142 -0.0059 -0.0038 288 PHE A CB 1550 C CG . PHE A 200 ? 0.1097 0.1088 0.1079 -0.0016 0.0072 0.0007 288 PHE A CG 1551 C CD1 . PHE A 200 ? 0.1184 0.1124 0.1458 0.0118 0.0073 0.0107 288 PHE A CD1 1552 C CD2 . PHE A 200 ? 0.1350 0.1466 0.1492 0.0016 0.0075 0.0298 288 PHE A CD2 1553 C CE1 . PHE A 200 ? 0.1383 0.1389 0.1532 -0.0112 0.0176 0.0133 288 PHE A CE1 1554 C CE2 . PHE A 200 ? 0.1270 0.1536 0.1488 0.0164 0.0026 0.0325 288 PHE A CE2 1555 C CZ . PHE A 200 ? 0.1318 0.1421 0.1322 -0.0138 -0.0022 0.0125 288 PHE A CZ 1556 N N . ALA A 201 ? 0.1204 0.0915 0.1367 -0.0001 -0.0050 0.0119 289 ALA A N 1557 C CA . ALA A 201 ? 0.1046 0.0960 0.1307 -0.0050 0.0001 0.0155 289 ALA A CA 1558 C C . ALA A 201 ? 0.1160 0.1256 0.1392 0.0019 0.0051 0.0043 289 ALA A C 1559 O O . ALA A 201 ? 0.1233 0.1192 0.1423 0.0046 0.0053 0.0111 289 ALA A O 1560 C CB . ALA A 201 ? 0.1108 0.1009 0.1482 -0.0106 -0.0097 0.0117 289 ALA A CB 1561 N N . LYS A 202 ? 0.1247 0.1102 0.1239 0.0016 0.0042 0.0087 290 LYS A N 1562 C CA . LYS A 202 ? 0.1394 0.1203 0.1268 -0.0002 0.0084 0.0067 290 LYS A CA 1563 C C . LYS A 202 ? 0.1329 0.1153 0.1227 0.0031 -0.0001 -0.0005 290 LYS A C 1564 O O . LYS A 202 ? 0.1417 0.1434 0.1353 0.0096 -0.0097 -0.0013 290 LYS A O 1565 C CB . LYS A 202 ? 0.1611 0.1526 0.1441 0.0088 0.0058 -0.0022 290 LYS A CB 1566 C CG . LYS A 202 ? 0.2051 0.2176 0.2030 0.0071 -0.0066 -0.0146 290 LYS A CG 1567 C CD . LYS A 202 ? 0.2467 0.2402 0.2287 0.0047 0.0001 0.0038 290 LYS A CD 1568 C CE . LYS A 202 ? 0.2555 0.2706 0.2470 0.0031 0.0018 -0.0093 290 LYS A CE 1569 N NZ . LYS A 202 ? 0.2847 0.2807 0.2891 -0.0054 0.0021 -0.0011 290 LYS A NZ 1570 N N . ILE A 203 ? 0.1282 0.1222 0.1325 0.0037 -0.0063 0.0006 291 ILE A N 1571 C CA . ILE A 203 ? 0.1337 0.1251 0.1472 0.0021 -0.0044 -0.0002 291 ILE A CA 1572 C C . ILE A 203 ? 0.1321 0.1060 0.1390 -0.0031 -0.0059 0.0042 291 ILE A C 1573 O O . ILE A 203 ? 0.1349 0.1094 0.1413 -0.0048 -0.0067 0.0077 291 ILE A O 1574 C CB A ILE A 203 ? 0.1343 0.1436 0.1564 -0.0044 -0.0061 0.0053 291 ILE A CB 1575 C CB B ILE A 203 ? 0.1339 0.1357 0.1432 -0.0003 -0.0032 0.0037 291 ILE A CB 1576 C CG1 A ILE A 203 ? 0.1640 0.1557 0.1902 -0.0087 -0.0046 -0.0029 291 ILE A CG1 1577 C CG1 B ILE A 203 ? 0.1350 0.1359 0.1421 -0.0082 -0.0038 0.0047 291 ILE A CG1 1578 C CG2 A ILE A 203 ? 0.1469 0.1507 0.1532 0.0000 0.0010 0.0111 291 ILE A CG2 1579 C CG2 B ILE A 203 ? 0.1405 0.1427 0.1495 0.0011 0.0002 0.0069 291 ILE A CG2 1580 C CD1 A ILE A 203 ? 0.1860 0.1542 0.1831 -0.0009 -0.0100 -0.0039 291 ILE A CD1 1581 C CD1 B ILE A 203 ? 0.1055 0.1075 0.1229 -0.0045 -0.0037 -0.0031 291 ILE A CD1 1582 N N . TYR A 204 ? 0.1265 0.1159 0.1284 -0.0046 -0.0080 0.0055 292 TYR A N 1583 C CA . TYR A 204 ? 0.1281 0.1166 0.1279 -0.0035 0.0022 0.0058 292 TYR A CA 1584 C C . TYR A 204 ? 0.1156 0.0944 0.1276 -0.0060 -0.0009 0.0095 292 TYR A C 1585 O O . TYR A 204 ? 0.1354 0.1146 0.1458 0.0065 -0.0046 0.0089 292 TYR A O 1586 C CB . TYR A 204 ? 0.1328 0.1074 0.1251 0.0026 0.0063 0.0163 292 TYR A CB 1587 C CG . TYR A 204 ? 0.1372 0.1198 0.1139 0.0120 0.0066 0.0002 292 TYR A CG 1588 C CD1 . TYR A 204 ? 0.1234 0.1211 0.1490 -0.0047 0.0193 0.0122 292 TYR A CD1 1589 C CD2 . TYR A 204 ? 0.1361 0.1414 0.1590 0.0070 0.0069 -0.0039 292 TYR A CD2 1590 C CE1 . TYR A 204 ? 0.1518 0.1411 0.1465 -0.0147 0.0161 -0.0078 292 TYR A CE1 1591 C CE2 . TYR A 204 ? 0.1453 0.1528 0.1534 -0.0027 0.0130 0.0003 292 TYR A CE2 1592 C CZ . TYR A 204 ? 0.1501 0.1250 0.1520 0.0002 0.0167 -0.0012 292 TYR A CZ 1593 O OH . TYR A 204 ? 0.1659 0.1293 0.2051 0.0041 0.0125 -0.0200 292 TYR A OH 1594 N N . GLU A 205 ? 0.1268 0.1209 0.1370 0.0136 0.0032 0.0155 293 GLU A N 1595 C CA . GLU A 205 ? 0.1568 0.1436 0.1477 0.0033 -0.0036 0.0127 293 GLU A CA 1596 C C . GLU A 205 ? 0.1543 0.1424 0.1402 -0.0001 0.0026 0.0117 293 GLU A C 1597 O O . GLU A 205 ? 0.1627 0.1488 0.1484 0.0020 0.0010 0.0236 293 GLU A O 1598 C CB . GLU A 205 ? 0.1791 0.1719 0.1807 0.0009 0.0024 0.0118 293 GLU A CB 1599 C CG . GLU A 205 ? 0.2447 0.2316 0.2224 -0.0069 0.0048 0.0118 293 GLU A CG 1600 C CD . GLU A 205 ? 0.2640 0.2840 0.2847 -0.0020 0.0083 -0.0009 293 GLU A CD 1601 O OE1 . GLU A 205 ? 0.3042 0.3023 0.3119 0.0042 0.0024 -0.0062 293 GLU A OE1 1602 O OE2 . GLU A 205 ? 0.2932 0.3134 0.3300 -0.0142 0.0011 0.0055 293 GLU A OE2 1603 N N . ASP A 206 ? 0.1515 0.1520 0.1290 0.0015 0.0028 0.0088 294 ASP A N 1604 C CA . ASP A 206 ? 0.1654 0.1633 0.1494 -0.0008 -0.0033 0.0013 294 ASP A CA 1605 C C . ASP A 206 ? 0.1620 0.1528 0.1414 0.0017 0.0015 0.0037 294 ASP A C 1606 O O . ASP A 206 ? 0.1804 0.1909 0.1744 0.0020 -0.0065 -0.0063 294 ASP A O 1607 C CB . ASP A 206 ? 0.1750 0.1780 0.1607 -0.0033 0.0043 -0.0058 294 ASP A CB 1608 C CG . ASP A 206 ? 0.2072 0.2063 0.2023 0.0035 0.0096 -0.0180 294 ASP A CG 1609 O OD1 . ASP A 206 ? 0.2593 0.2673 0.2410 0.0017 0.0482 -0.0020 294 ASP A OD1 1610 O OD2 . ASP A 206 ? 0.2505 0.2531 0.2619 0.0310 -0.0109 -0.0158 294 ASP A OD2 1611 N N . ALA A 207 ? 0.1575 0.1229 0.1412 0.0075 0.0017 0.0092 295 ALA A N 1612 C CA . ALA A 207 ? 0.1385 0.1338 0.1326 0.0027 -0.0106 0.0042 295 ALA A CA 1613 C C . ALA A 207 ? 0.1461 0.1342 0.1497 -0.0039 0.0005 0.0100 295 ALA A C 1614 O O . ALA A 207 ? 0.1554 0.1418 0.1516 0.0014 -0.0017 0.0254 295 ALA A O 1615 C CB . ALA A 207 ? 0.1386 0.1032 0.1319 0.0020 0.0002 -0.0027 295 ALA A CB 1616 N N . GLY A 208 ? 0.1429 0.1246 0.1476 0.0038 0.0062 0.0087 296 GLY A N 1617 C CA . GLY A 208 ? 0.1484 0.1241 0.1472 0.0015 0.0075 0.0133 296 GLY A CA 1618 C C . GLY A 208 ? 0.1470 0.1335 0.1409 0.0073 0.0114 0.0137 296 GLY A C 1619 O O . GLY A 208 ? 0.1885 0.1403 0.1761 0.0091 0.0155 0.0242 296 GLY A O 1620 N N . LYS A 209 ? 0.1495 0.1272 0.1288 0.0097 0.0116 0.0052 297 LYS A N 1621 C CA . LYS A 209 ? 0.1435 0.1204 0.1376 -0.0030 0.0099 0.0088 297 LYS A CA 1622 C C . LYS A 209 ? 0.1396 0.1123 0.1405 0.0031 0.0131 0.0030 297 LYS A C 1623 O O . LYS A 209 ? 0.1613 0.1058 0.1496 0.0024 0.0338 -0.0036 297 LYS A O 1624 C CB . LYS A 209 ? 0.1507 0.1289 0.1501 -0.0041 0.0090 -0.0001 297 LYS A CB 1625 C CG . LYS A 209 ? 0.1800 0.1744 0.1764 0.0049 0.0103 -0.0047 297 LYS A CG 1626 C CD . LYS A 209 ? 0.2197 0.2273 0.2445 -0.0099 0.0054 0.0064 297 LYS A CD 1627 C CE . LYS A 209 ? 0.2549 0.2656 0.2709 0.0000 0.0119 0.0036 297 LYS A CE 1628 N NZ . LYS A 209 ? 0.2775 0.3029 0.3018 -0.0174 0.0002 0.0006 297 LYS A NZ 1629 N N . PRO A 210 ? 0.1275 0.0963 0.1286 0.0029 0.0127 0.0062 298 PRO A N 1630 C CA . PRO A 210 ? 0.1282 0.1035 0.1227 0.0031 0.0129 0.0115 298 PRO A CA 1631 C C . PRO A 210 ? 0.1199 0.0992 0.1189 0.0048 0.0133 0.0057 298 PRO A C 1632 O O . PRO A 210 ? 0.1249 0.1012 0.1158 0.0158 0.0105 0.0051 298 PRO A O 1633 C CB . PRO A 210 ? 0.1247 0.1105 0.1489 -0.0025 0.0083 0.0059 298 PRO A CB 1634 C CG . PRO A 210 ? 0.1663 0.1255 0.1602 0.0002 0.0201 0.0022 298 PRO A CG 1635 C CD . PRO A 210 ? 0.1536 0.1009 0.1311 0.0022 0.0124 0.0081 298 PRO A CD 1636 N N . ARG A 211 ? 0.1274 0.0996 0.1292 0.0125 0.0073 0.0202 299 ARG A N 1637 C CA . ARG A 211 ? 0.1246 0.1016 0.1219 0.0074 0.0052 0.0117 299 ARG A CA 1638 C C . ARG A 211 ? 0.1206 0.0983 0.1104 -0.0012 0.0052 0.0087 299 ARG A C 1639 O O . ARG A 211 ? 0.1228 0.0958 0.1310 -0.0107 0.0064 -0.0024 299 ARG A O 1640 C CB . ARG A 211 ? 0.1358 0.1042 0.1347 0.0085 0.0076 0.0151 299 ARG A CB 1641 C CG . ARG A 211 ? 0.1491 0.1136 0.1455 -0.0022 0.0119 0.0129 299 ARG A CG 1642 C CD . ARG A 211 ? 0.1548 0.1251 0.1484 -0.0107 0.0216 0.0057 299 ARG A CD 1643 N NE . ARG A 211 ? 0.1316 0.0969 0.1316 0.0068 0.0042 0.0060 299 ARG A NE 1644 C CZ . ARG A 211 ? 0.1133 0.1045 0.1179 0.0040 -0.0016 -0.0077 299 ARG A CZ 1645 N NH1 . ARG A 211 ? 0.1292 0.1101 0.1351 -0.0007 0.0066 0.0027 299 ARG A NH1 1646 N NH2 . ARG A 211 ? 0.1231 0.0970 0.1292 0.0072 0.0149 0.0089 299 ARG A NH2 1647 N N . ALA A 212 ? 0.1093 0.0890 0.1090 -0.0048 -0.0009 0.0008 300 ALA A N 1648 C CA . ALA A 212 ? 0.1066 0.0880 0.0922 0.0094 0.0022 -0.0030 300 ALA A CA 1649 C C . ALA A 212 ? 0.0974 0.0926 0.0973 0.0023 -0.0030 0.0032 300 ALA A C 1650 O O . ALA A 212 ? 0.1111 0.1102 0.1135 0.0112 0.0162 0.0349 300 ALA A O 1651 C CB . ALA A 212 ? 0.1050 0.0862 0.1234 0.0096 -0.0063 0.0038 300 ALA A CB 1652 N N . VAL A 213 ? 0.1108 0.0897 0.0938 0.0003 -0.0006 0.0064 301 VAL A N 1653 C CA . VAL A 213 ? 0.1075 0.0831 0.1056 -0.0048 -0.0032 0.0052 301 VAL A CA 1654 C C . VAL A 213 ? 0.1173 0.1052 0.1140 -0.0066 -0.0014 0.0017 301 VAL A C 1655 O O . VAL A 213 ? 0.1396 0.1235 0.1335 -0.0254 -0.0082 0.0158 301 VAL A O 1656 C CB . VAL A 213 ? 0.1208 0.1089 0.1239 0.0026 0.0021 -0.0015 301 VAL A CB 1657 C CG1 . VAL A 213 ? 0.1237 0.1299 0.1439 0.0069 0.0206 0.0056 301 VAL A CG1 1658 C CG2 . VAL A 213 ? 0.1208 0.1061 0.1481 0.0107 0.0052 -0.0001 301 VAL A CG2 1659 N N . ARG A 214 ? 0.0929 0.0759 0.1084 -0.0008 -0.0055 0.0103 302 ARG A N 1660 C CA . ARG A 214 ? 0.1157 0.1045 0.1197 0.0020 -0.0021 0.0054 302 ARG A CA 1661 C C . ARG A 214 ? 0.0984 0.0834 0.0968 0.0009 -0.0023 -0.0052 302 ARG A C 1662 O O . ARG A 214 ? 0.1087 0.1019 0.1411 -0.0029 -0.0144 0.0148 302 ARG A O 1663 C CB . ARG A 214 ? 0.1367 0.1131 0.1094 0.0030 -0.0085 0.0063 302 ARG A CB 1664 C CG . ARG A 214 ? 0.1231 0.1123 0.1199 0.0079 0.0030 -0.0016 302 ARG A CG 1665 C CD . ARG A 214 ? 0.1460 0.1221 0.1383 0.0084 -0.0121 0.0102 302 ARG A CD 1666 N NE . ARG A 214 ? 0.1629 0.1291 0.1404 0.0040 0.0048 -0.0170 302 ARG A NE 1667 C CZ . ARG A 214 ? 0.1779 0.1447 0.1470 0.0054 0.0021 -0.0061 302 ARG A CZ 1668 N NH1 . ARG A 214 ? 0.2282 0.1440 0.1856 -0.0041 -0.0286 -0.0122 302 ARG A NH1 1669 N NH2 . ARG A 214 ? 0.1891 0.1368 0.1665 0.0037 -0.0044 0.0008 302 ARG A NH2 1670 N N . GLY A 215 ? 0.1008 0.0857 0.1003 -0.0005 -0.0025 0.0010 303 GLY A N 1671 C CA . GLY A 215 ? 0.0967 0.0919 0.0872 -0.0044 -0.0009 0.0047 303 GLY A CA 1672 C C . GLY A 215 ? 0.0920 0.0776 0.0873 -0.0079 0.0000 -0.0082 303 GLY A C 1673 O O . GLY A 215 ? 0.0911 0.0687 0.0821 -0.0087 -0.0118 0.0068 303 GLY A O 1674 N N . LEU A 216 ? 0.0938 0.0565 0.0743 -0.0081 -0.0109 -0.0114 304 LEU A N 1675 C CA . LEU A 216 ? 0.0850 0.0538 0.0730 -0.0115 0.0022 -0.0049 304 LEU A CA 1676 C C . LEU A 216 ? 0.0761 0.0647 0.0691 -0.0105 0.0041 -0.0070 304 LEU A C 1677 O O . LEU A 216 ? 0.0995 0.0675 0.0835 -0.0142 -0.0081 -0.0031 304 LEU A O 1678 C CB . LEU A 216 ? 0.0965 0.0643 0.0850 0.0020 0.0061 -0.0077 304 LEU A CB 1679 C CG . LEU A 216 ? 0.0938 0.0646 0.0851 -0.0014 0.0057 0.0029 304 LEU A CG 1680 C CD1 . LEU A 216 ? 0.1070 0.1382 0.1169 -0.0117 0.0030 0.0092 304 LEU A CD1 1681 C CD2 . LEU A 216 ? 0.0849 0.0970 0.0891 0.0004 0.0216 0.0003 304 LEU A CD2 1682 N N . ALA A 217 ? 0.0982 0.0652 0.0669 -0.0019 -0.0058 0.0063 305 ALA A N 1683 C CA . ALA A 217 ? 0.0836 0.0658 0.0636 0.0037 -0.0065 0.0060 305 ALA A CA 1684 C C . ALA A 217 ? 0.0998 0.0739 0.0909 0.0059 -0.0100 -0.0029 305 ALA A C 1685 O O . ALA A 217 ? 0.1264 0.1027 0.0900 0.0215 -0.0125 -0.0052 305 ALA A O 1686 C CB . ALA A 217 ? 0.0960 0.0871 0.0836 0.0072 0.0020 0.0151 305 ALA A CB 1687 N N . THR A 218 ? 0.0980 0.0854 0.0869 0.0007 -0.0057 -0.0034 306 THR A N 1688 C CA . THR A 218 ? 0.1112 0.0952 0.1001 0.0086 -0.0053 -0.0038 306 THR A CA 1689 C C . THR A 218 ? 0.0980 0.0968 0.0819 0.0134 -0.0082 -0.0057 306 THR A C 1690 O O . THR A 218 ? 0.0947 0.0950 0.0743 0.0177 -0.0063 0.0037 306 THR A O 1691 C CB . THR A 218 ? 0.1260 0.1186 0.1062 0.0048 -0.0049 0.0011 306 THR A CB 1692 O OG1 . THR A 218 ? 0.1393 0.1712 0.1835 -0.0093 0.0245 -0.0427 306 THR A OG1 1693 C CG2 . THR A 218 ? 0.1120 0.1319 0.1454 -0.0039 0.0141 -0.0036 306 THR A CG2 1694 N N . ASN A 219 ? 0.0979 0.0901 0.0786 0.0125 0.0006 0.0068 307 ASN A N 1695 C CA . ASN A 219 ? 0.0993 0.0912 0.0849 0.0137 -0.0054 0.0124 307 ASN A CA 1696 C C . ASN A 219 ? 0.0931 0.0913 0.0853 0.0073 -0.0097 0.0176 307 ASN A C 1697 O O . ASN A 219 ? 0.1058 0.0984 0.0939 0.0011 -0.0028 0.0143 307 ASN A O 1698 C CB . ASN A 219 ? 0.0912 0.1047 0.0971 0.0067 -0.0006 0.0207 307 ASN A CB 1699 C CG . ASN A 219 ? 0.1044 0.1097 0.0937 0.0264 0.0011 0.0233 307 ASN A CG 1700 O OD1 . ASN A 219 ? 0.1249 0.1147 0.0833 0.0070 -0.0111 0.0122 307 ASN A OD1 1701 N ND2 . ASN A 219 ? 0.1181 0.1389 0.0913 0.0073 -0.0111 0.0118 307 ASN A ND2 1702 N N . VAL A 220 ? 0.0990 0.1088 0.0872 -0.0068 -0.0133 0.0087 308 VAL A N 1703 C CA . VAL A 220 ? 0.0930 0.1092 0.0779 0.0046 -0.0006 0.0099 308 VAL A CA 1704 C C . VAL A 220 ? 0.1134 0.1138 0.0993 0.0030 0.0047 0.0068 308 VAL A C 1705 O O . VAL A 220 ? 0.1447 0.1077 0.1007 0.0168 0.0003 0.0086 308 VAL A O 1706 C CB . VAL A 220 ? 0.0814 0.1003 0.0848 0.0082 -0.0034 0.0047 308 VAL A CB 1707 C CG1 . VAL A 220 ? 0.0985 0.1153 0.0970 0.0007 -0.0070 0.0123 308 VAL A CG1 1708 C CG2 . VAL A 220 ? 0.0887 0.1114 0.1010 0.0072 -0.0076 0.0069 308 VAL A CG2 1709 N N . ALA A 221 ? 0.1191 0.1197 0.1001 -0.0064 0.0008 -0.0003 309 ALA A N 1710 C CA . ALA A 221 ? 0.1117 0.1236 0.1213 -0.0061 -0.0121 0.0078 309 ALA A CA 1711 C C . ALA A 221 ? 0.1312 0.1247 0.1402 -0.0029 -0.0136 0.0120 309 ALA A C 1712 O O . ALA A 221 ? 0.1348 0.1305 0.1854 -0.0079 -0.0209 0.0257 309 ALA A O 1713 C CB . ALA A 221 ? 0.1364 0.1164 0.1261 -0.0111 -0.0119 0.0067 309 ALA A CB 1714 N N . ASN A 222 ? 0.1184 0.1162 0.0990 -0.0093 -0.0138 0.0168 310 ASN A N 1715 C CA . ASN A 222 ? 0.1203 0.1025 0.1061 -0.0019 0.0018 0.0050 310 ASN A CA 1716 C C . ASN A 222 ? 0.1047 0.0978 0.1049 0.0044 -0.0095 0.0045 310 ASN A C 1717 O O . ASN A 222 ? 0.1128 0.1115 0.0970 0.0095 -0.0090 0.0114 310 ASN A O 1718 C CB . ASN A 222 ? 0.1218 0.1157 0.0983 0.0019 -0.0062 0.0225 310 ASN A CB 1719 C CG . ASN A 222 ? 0.1487 0.1316 0.1630 0.0027 0.0045 0.0237 310 ASN A CG 1720 O OD1 . ASN A 222 ? 0.1863 0.1897 0.2155 0.0212 -0.0145 0.0042 310 ASN A OD1 1721 N ND2 . ASN A 222 ? 0.1875 0.1908 0.1949 -0.0107 0.0005 -0.0159 310 ASN A ND2 1722 N N . TYR A 223 ? 0.0982 0.1118 0.0807 -0.0098 -0.0115 0.0148 311 TYR A N 1723 C CA . TYR A 223 ? 0.1086 0.0973 0.0849 0.0027 -0.0029 0.0133 311 TYR A CA 1724 C C . TYR A 223 ? 0.1155 0.1153 0.0927 -0.0026 -0.0078 0.0171 311 TYR A C 1725 O O . TYR A 223 ? 0.1128 0.1343 0.1009 0.0039 -0.0248 0.0186 311 TYR A O 1726 C CB . TYR A 223 ? 0.1229 0.1198 0.0929 0.0093 -0.0055 0.0201 311 TYR A CB 1727 C CG . TYR A 223 ? 0.1215 0.1118 0.1069 0.0059 -0.0023 0.0207 311 TYR A CG 1728 C CD1 . TYR A 223 ? 0.1199 0.1221 0.1146 0.0050 -0.0096 0.0228 311 TYR A CD1 1729 C CD2 . TYR A 223 ? 0.1230 0.1531 0.1241 -0.0066 0.0028 0.0110 311 TYR A CD2 1730 C CE1 . TYR A 223 ? 0.1244 0.1257 0.1070 -0.0013 -0.0007 0.0294 311 TYR A CE1 1731 C CE2 . TYR A 223 ? 0.1520 0.1321 0.1304 -0.0063 -0.0044 0.0045 311 TYR A CE2 1732 C CZ . TYR A 223 ? 0.1420 0.1429 0.1363 -0.0164 -0.0106 0.0104 311 TYR A CZ 1733 O OH . TYR A 223 ? 0.1511 0.1461 0.1590 -0.0198 -0.0081 0.0255 311 TYR A OH 1734 N N . ASN A 224 ? 0.0886 0.1037 0.0857 0.0077 -0.0136 0.0198 312 ASN A N 1735 C CA . ASN A 224 ? 0.1053 0.1096 0.0940 0.0046 -0.0029 0.0124 312 ASN A CA 1736 C C . ASN A 224 ? 0.1142 0.1200 0.0938 0.0024 -0.0072 0.0074 312 ASN A C 1737 O O . ASN A 224 ? 0.1212 0.1130 0.0939 0.0093 0.0024 0.0107 312 ASN A O 1738 C CB . ASN A 224 ? 0.1022 0.1040 0.1100 -0.0100 -0.0025 0.0139 312 ASN A CB 1739 C CG . ASN A 224 ? 0.1229 0.1148 0.1501 0.0177 0.0167 0.0053 312 ASN A CG 1740 O OD1 . ASN A 224 ? 0.1508 0.1413 0.1593 0.0007 0.0190 0.0114 312 ASN A OD1 1741 N ND2 . ASN A 224 ? 0.1195 0.1718 0.1434 0.0038 0.0078 0.0113 312 ASN A ND2 1742 N N . ALA A 225 ? 0.1173 0.1329 0.1123 0.0019 -0.0074 0.0053 313 ALA A N 1743 C CA . ALA A 225 ? 0.1101 0.1296 0.1162 -0.0024 -0.0049 -0.0008 313 ALA A CA 1744 C C . ALA A 225 ? 0.1106 0.1191 0.1075 0.0038 -0.0089 -0.0033 313 ALA A C 1745 O O . ALA A 225 ? 0.1261 0.1318 0.1116 0.0079 0.0056 -0.0041 313 ALA A O 1746 C CB . ALA A 225 ? 0.1306 0.1532 0.1263 -0.0099 -0.0010 -0.0023 313 ALA A CB 1747 N N . TRP A 226 ? 0.1342 0.1451 0.1271 0.0049 0.0121 -0.0118 314 TRP A N 1748 C CA . TRP A 226 ? 0.1322 0.1385 0.1208 0.0018 0.0032 -0.0069 314 TRP A CA 1749 C C . TRP A 226 ? 0.1376 0.1438 0.1305 0.0024 0.0018 -0.0037 314 TRP A C 1750 O O . TRP A 226 ? 0.1267 0.1394 0.1325 -0.0069 -0.0067 -0.0076 314 TRP A O 1751 C CB . TRP A 226 ? 0.1268 0.1484 0.1406 0.0078 0.0109 0.0001 314 TRP A CB 1752 C CG . TRP A 226 ? 0.1087 0.1293 0.1395 0.0129 -0.0015 -0.0286 314 TRP A CG 1753 C CD1 . TRP A 226 ? 0.1403 0.1776 0.1513 0.0069 -0.0118 -0.0264 314 TRP A CD1 1754 C CD2 . TRP A 226 ? 0.1135 0.1283 0.1489 0.0040 -0.0145 -0.0135 314 TRP A CD2 1755 N NE1 . TRP A 226 ? 0.1628 0.1821 0.1683 -0.0005 -0.0152 -0.0189 314 TRP A NE1 1756 C CE2 . TRP A 226 ? 0.1260 0.1366 0.1474 0.0029 -0.0024 -0.0070 314 TRP A CE2 1757 C CE3 . TRP A 226 ? 0.1169 0.1452 0.1351 0.0166 -0.0113 -0.0037 314 TRP A CE3 1758 C CZ2 . TRP A 226 ? 0.1355 0.1433 0.1574 0.0044 -0.0129 -0.0058 314 TRP A CZ2 1759 C CZ3 . TRP A 226 ? 0.1272 0.1513 0.1537 0.0061 -0.0092 -0.0115 314 TRP A CZ3 1760 C CH2 . TRP A 226 ? 0.1341 0.1311 0.1538 0.0017 0.0028 0.0075 314 TRP A CH2 1761 N N . SER A 227 ? 0.1568 0.1667 0.1534 0.0062 -0.0086 -0.0065 315 SER A N 1762 C CA . SER A 227 ? 0.1673 0.1893 0.1819 0.0040 -0.0062 0.0000 315 SER A CA 1763 C C . SER A 227 ? 0.1946 0.2118 0.1828 0.0096 -0.0060 0.0015 315 SER A C 1764 O O . SER A 227 ? 0.2003 0.2675 0.1908 0.0313 -0.0110 0.0052 315 SER A O 1765 C CB . SER A 227 ? 0.1689 0.2031 0.1974 -0.0009 -0.0128 -0.0124 315 SER A CB 1766 O OG . SER A 227 ? 0.1767 0.2258 0.2486 -0.0090 -0.0256 -0.0407 315 SER A OG 1767 N N . VAL A 228 ? 0.1891 0.2285 0.1727 0.0097 -0.0210 0.0019 316 VAL A N 1768 C CA . VAL A 228 ? 0.2129 0.2366 0.2010 0.0145 -0.0073 0.0102 316 VAL A CA 1769 C C . VAL A 228 ? 0.2299 0.2570 0.2272 0.0020 -0.0122 0.0016 316 VAL A C 1770 O O . VAL A 228 ? 0.2064 0.2647 0.2168 0.0103 -0.0248 0.0074 316 VAL A O 1771 C CB . VAL A 228 ? 0.2086 0.2432 0.2210 0.0103 -0.0157 0.0147 316 VAL A CB 1772 C CG1 . VAL A 228 ? 0.2112 0.2233 0.2394 0.0100 -0.0191 0.0135 316 VAL A CG1 1773 C CG2 . VAL A 228 ? 0.2564 0.2670 0.2500 0.0068 -0.0154 0.0164 316 VAL A CG2 1774 N N . SER A 229 ? 0.2557 0.2839 0.2480 0.0103 -0.0113 -0.0010 317 SER A N 1775 C CA . SER A 229 ? 0.2765 0.2964 0.2826 -0.0010 -0.0096 -0.0033 317 SER A CA 1776 C C . SER A 229 ? 0.2786 0.2990 0.2881 0.0005 -0.0044 -0.0005 317 SER A C 1777 O O . SER A 229 ? 0.2911 0.3327 0.3247 0.0005 -0.0018 0.0078 317 SER A O 1778 C CB . SER A 229 ? 0.2948 0.3181 0.2862 0.0021 -0.0054 -0.0064 317 SER A CB 1779 O OG . SER A 229 ? 0.3479 0.3460 0.3371 -0.0023 -0.0170 0.0024 317 SER A OG 1780 N N . SER A 230 ? 0.2647 0.2850 0.2773 0.0021 -0.0075 -0.0023 318 SER A N 1781 C CA . SER A 230 ? 0.2852 0.2957 0.2917 0.0013 -0.0046 -0.0039 318 SER A CA 1782 C C . SER A 230 ? 0.2542 0.2783 0.2669 0.0019 -0.0013 -0.0007 318 SER A C 1783 O O . SER A 230 ? 0.2387 0.2717 0.2555 0.0110 -0.0061 -0.0047 318 SER A O 1784 C CB . SER A 230 ? 0.2968 0.3119 0.3013 -0.0016 -0.0023 -0.0005 318 SER A CB 1785 O OG . SER A 230 ? 0.3797 0.3601 0.3815 0.0132 -0.0067 -0.0061 318 SER A OG 1786 N N . PRO A 231 ? 0.2143 0.2505 0.2360 -0.0011 -0.0076 0.0053 319 PRO A N 1787 C CA . PRO A 231 ? 0.2115 0.2284 0.2241 -0.0004 -0.0034 0.0091 319 PRO A CA 1788 C C . PRO A 231 ? 0.2018 0.2153 0.2135 0.0013 -0.0107 0.0143 319 PRO A C 1789 O O . PRO A 231 ? 0.2033 0.2357 0.2327 0.0123 -0.0185 0.0250 319 PRO A O 1790 C CB . PRO A 231 ? 0.2215 0.2367 0.2199 0.0018 -0.0020 0.0086 319 PRO A CB 1791 C CG . PRO A 231 ? 0.2429 0.2816 0.2747 -0.0095 -0.0021 0.0032 319 PRO A CG 1792 C CD . PRO A 231 ? 0.2338 0.2722 0.2671 -0.0085 -0.0005 0.0061 319 PRO A CD 1793 N N . PRO A 232 ? 0.1782 0.1928 0.1897 0.0080 -0.0031 0.0156 320 PRO A N 1794 C CA . PRO A 232 ? 0.1856 0.1963 0.1797 -0.0029 -0.0022 0.0105 320 PRO A CA 1795 C C . PRO A 232 ? 0.1912 0.1996 0.1872 0.0041 -0.0066 0.0119 320 PRO A C 1796 O O . PRO A 232 ? 0.1877 0.1939 0.1722 -0.0001 0.0056 0.0100 320 PRO A O 1797 C CB . PRO A 232 ? 0.1793 0.2090 0.1903 -0.0007 0.0083 0.0066 320 PRO A CB 1798 C CG . PRO A 232 ? 0.1859 0.2084 0.1864 -0.0015 -0.0036 0.0051 320 PRO A CG 1799 C CD . PRO A 232 ? 0.1932 0.2107 0.1936 0.0095 -0.0046 0.0122 320 PRO A CD 1800 N N . PRO A 233 ? 0.2103 0.2033 0.1800 0.0009 -0.0052 0.0150 321 PRO A N 1801 C CA . PRO A 233 ? 0.2000 0.1990 0.1966 0.0030 0.0024 0.0176 321 PRO A CA 1802 C C . PRO A 233 ? 0.1868 0.1812 0.1810 0.0089 -0.0012 0.0286 321 PRO A C 1803 O O . PRO A 233 ? 0.1978 0.2107 0.2084 0.0201 0.0073 0.0214 321 PRO A O 1804 C CB . PRO A 233 ? 0.2087 0.2074 0.1998 0.0113 -0.0068 0.0200 321 PRO A CB 1805 C CG . PRO A 233 ? 0.2466 0.2432 0.2226 0.0081 0.0036 0.0081 321 PRO A CG 1806 C CD . PRO A 233 ? 0.2265 0.2278 0.1983 -0.0007 0.0020 0.0186 321 PRO A CD 1807 N N . TYR A 234 ? 0.1776 0.1684 0.1742 -0.0023 0.0118 0.0294 322 TYR A N 1808 C CA . TYR A 234 ? 0.1756 0.1618 0.1706 0.0043 0.0067 0.0225 322 TYR A CA 1809 C C . TYR A 234 ? 0.1624 0.1481 0.1530 0.0065 0.0025 0.0164 322 TYR A C 1810 O O . TYR A 234 ? 0.1743 0.1562 0.1735 0.0023 0.0063 0.0114 322 TYR A O 1811 C CB . TYR A 234 ? 0.1697 0.1549 0.1734 0.0114 0.0044 0.0178 322 TYR A CB 1812 C CG . TYR A 234 ? 0.1670 0.1620 0.1516 0.0161 0.0079 0.0256 322 TYR A CG 1813 C CD1 . TYR A 234 ? 0.1581 0.1363 0.1613 0.0085 0.0090 0.0192 322 TYR A CD1 1814 C CD2 . TYR A 234 ? 0.1463 0.1634 0.1530 0.0078 -0.0087 0.0205 322 TYR A CD2 1815 C CE1 . TYR A 234 ? 0.1511 0.1547 0.1416 0.0033 0.0066 0.0220 322 TYR A CE1 1816 C CE2 . TYR A 234 ? 0.1753 0.1686 0.1501 0.0057 0.0103 0.0357 322 TYR A CE2 1817 C CZ . TYR A 234 ? 0.1410 0.1645 0.1502 0.0024 0.0022 0.0164 322 TYR A CZ 1818 O OH . TYR A 234 ? 0.1462 0.1989 0.1327 0.0129 0.0153 0.0222 322 TYR A OH 1819 N N . THR A 235 ? 0.1418 0.1507 0.1383 0.0048 0.0047 0.0227 323 THR A N 1820 C CA . THR A 235 ? 0.1343 0.1338 0.1345 -0.0018 -0.0002 0.0249 323 THR A CA 1821 C C . THR A 235 ? 0.1384 0.1487 0.1421 0.0097 0.0044 0.0164 323 THR A C 1822 O O . THR A 235 ? 0.1282 0.1386 0.1517 -0.0004 0.0046 0.0356 323 THR A O 1823 C CB . THR A 235 ? 0.1381 0.1386 0.1291 0.0020 -0.0015 0.0239 323 THR A CB 1824 O OG1 . THR A 235 ? 0.1419 0.1404 0.1550 -0.0010 -0.0090 0.0135 323 THR A OG1 1825 C CG2 . THR A 235 ? 0.1469 0.1527 0.1330 0.0121 -0.0030 0.0260 323 THR A CG2 1826 N N . SER A 236 ? 0.1487 0.1607 0.1564 0.0095 0.0048 0.0251 324 SER A N 1827 C CA . SER A 236 ? 0.1569 0.1729 0.1777 0.0140 0.0009 0.0204 324 SER A CA 1828 C C . SER A 236 ? 0.1405 0.1568 0.1834 0.0153 0.0016 0.0126 324 SER A C 1829 O O . SER A 236 ? 0.1622 0.1546 0.2285 0.0150 0.0161 0.0100 324 SER A O 1830 C CB . SER A 236 ? 0.1696 0.1909 0.1918 0.0182 -0.0048 0.0209 324 SER A CB 1831 O OG . SER A 236 ? 0.2166 0.2662 0.2633 0.0029 0.0170 0.0345 324 SER A OG 1832 N N . PRO A 237 ? 0.1385 0.1520 0.1644 0.0108 0.0015 0.0145 325 PRO A N 1833 C CA . PRO A 237 ? 0.1285 0.1361 0.1613 0.0167 -0.0044 0.0128 325 PRO A CA 1834 C C . PRO A 237 ? 0.1235 0.1130 0.1379 0.0036 0.0017 0.0148 325 PRO A C 1835 O O . PRO A 237 ? 0.1147 0.1421 0.1507 0.0187 -0.0007 0.0262 325 PRO A O 1836 C CB . PRO A 237 ? 0.1355 0.1329 0.1455 0.0132 -0.0014 0.0173 325 PRO A CB 1837 C CG . PRO A 237 ? 0.1331 0.1264 0.1703 0.0110 0.0101 0.0004 325 PRO A CG 1838 C CD . PRO A 237 ? 0.1367 0.1541 0.1653 0.0059 0.0094 0.0137 325 PRO A CD 1839 N N . ASN A 238 ? 0.1183 0.1021 0.1300 0.0097 0.0015 0.0176 326 ASN A N 1840 C CA . ASN A 238 ? 0.1049 0.1085 0.1158 0.0052 0.0017 0.0164 326 ASN A CA 1841 C C . ASN A 238 ? 0.1063 0.1192 0.1294 0.0021 -0.0047 0.0106 326 ASN A C 1842 O O . ASN A 238 ? 0.1144 0.1186 0.1288 -0.0021 0.0037 0.0096 326 ASN A O 1843 C CB . ASN A 238 ? 0.0932 0.0997 0.1273 0.0022 0.0051 0.0241 326 ASN A CB 1844 C CG . ASN A 238 ? 0.1011 0.1033 0.1310 0.0048 -0.0068 0.0120 326 ASN A CG 1845 O OD1 . ASN A 238 ? 0.1080 0.1066 0.1230 0.0102 -0.0028 0.0123 326 ASN A OD1 1846 N ND2 . ASN A 238 ? 0.0893 0.1170 0.1199 -0.0038 0.0048 0.0028 326 ASN A ND2 1847 N N . PRO A 239 ? 0.1064 0.1147 0.1237 0.0063 -0.0030 0.0062 327 PRO A N 1848 C CA . PRO A 239 ? 0.1111 0.1217 0.1318 0.0033 -0.0025 -0.0001 327 PRO A CA 1849 C C . PRO A 239 ? 0.1123 0.1224 0.1358 0.0036 0.0000 -0.0039 327 PRO A C 1850 O O . PRO A 239 ? 0.1342 0.1433 0.1319 0.0021 0.0020 -0.0156 327 PRO A O 1851 C CB . PRO A 239 ? 0.1283 0.1507 0.1466 -0.0143 0.0018 0.0103 327 PRO A CB 1852 C CG . PRO A 239 ? 0.1472 0.1353 0.1623 -0.0083 0.0087 -0.0027 327 PRO A CG 1853 C CD . PRO A 239 ? 0.1129 0.1165 0.1339 -0.0006 0.0013 0.0065 327 PRO A CD 1854 N N . ASN A 240 ? 0.1071 0.1105 0.1259 -0.0012 -0.0020 -0.0035 328 ASN A N 1855 C CA . ASN A 240 ? 0.1272 0.1177 0.1389 0.0058 0.0011 0.0007 328 ASN A CA 1856 C C . ASN A 240 ? 0.1109 0.1269 0.1334 -0.0034 0.0010 -0.0045 328 ASN A C 1857 O O . ASN A 240 ? 0.1308 0.1534 0.1499 -0.0015 -0.0080 -0.0172 328 ASN A O 1858 C CB . ASN A 240 ? 0.1167 0.1182 0.1280 0.0019 0.0018 -0.0007 328 ASN A CB 1859 C CG . ASN A 240 ? 0.1411 0.1235 0.1337 0.0001 -0.0085 0.0095 328 ASN A CG 1860 O OD1 . ASN A 240 ? 0.1618 0.1347 0.1404 -0.0100 -0.0024 0.0031 328 ASN A OD1 1861 N ND2 . ASN A 240 ? 0.1466 0.1444 0.1345 0.0009 0.0025 -0.0009 328 ASN A ND2 1862 N N . TYR A 241 ? 0.1234 0.1306 0.1409 -0.0046 0.0010 0.0048 329 TYR A N 1863 C CA . TYR A 241 ? 0.1181 0.1351 0.1573 0.0021 0.0005 0.0060 329 TYR A CA 1864 C C . TYR A 241 ? 0.1269 0.1347 0.1579 -0.0011 0.0065 0.0043 329 TYR A C 1865 O O . TYR A 241 ? 0.1381 0.1531 0.1875 0.0123 0.0207 0.0239 329 TYR A O 1866 C CB . TYR A 241 ? 0.1332 0.1560 0.1510 0.0059 0.0090 0.0130 329 TYR A CB 1867 C CG . TYR A 241 ? 0.1471 0.1701 0.1821 0.0120 -0.0066 0.0070 329 TYR A CG 1868 C CD1 . TYR A 241 ? 0.1852 0.1948 0.1815 0.0021 -0.0030 0.0057 329 TYR A CD1 1869 C CD2 . TYR A 241 ? 0.1968 0.2388 0.1841 -0.0180 0.0084 0.0117 329 TYR A CD2 1870 C CE1 . TYR A 241 ? 0.2652 0.2547 0.2125 0.0019 -0.0121 -0.0097 329 TYR A CE1 1871 C CE2 . TYR A 241 ? 0.2787 0.2781 0.2649 -0.0237 -0.0056 -0.0026 329 TYR A CE2 1872 C CZ . TYR A 241 ? 0.2829 0.2775 0.2782 -0.0117 -0.0054 -0.0085 329 TYR A CZ 1873 O OH . TYR A 241 ? 0.3563 0.3428 0.3607 -0.0293 -0.0322 -0.0232 329 TYR A OH 1874 N N . ASP A 242 ? 0.1116 0.1224 0.1203 0.0040 -0.0012 0.0143 330 ASP A N 1875 C CA . ASP A 242 ? 0.1194 0.1252 0.1207 0.0048 -0.0056 0.0052 330 ASP A CA 1876 C C . ASP A 242 ? 0.0951 0.1039 0.1056 0.0026 -0.0024 0.0041 330 ASP A C 1877 O O . ASP A 242 ? 0.0987 0.1095 0.1070 0.0093 0.0014 -0.0004 330 ASP A O 1878 C CB . ASP A 242 ? 0.1326 0.1515 0.1368 0.0119 -0.0038 0.0046 330 ASP A CB 1879 C CG . ASP A 242 ? 0.1484 0.1518 0.1316 0.0063 -0.0175 -0.0005 330 ASP A CG 1880 O OD1 . ASP A 242 ? 0.1446 0.1751 0.1567 -0.0001 -0.0030 0.0008 330 ASP A OD1 1881 O OD2 . ASP A 242 ? 0.1422 0.1988 0.1488 0.0153 -0.0190 -0.0196 330 ASP A OD2 1882 N N . GLU A 243 ? 0.1051 0.0998 0.1145 0.0020 -0.0067 0.0008 331 GLU A N 1883 C CA . GLU A 243 ? 0.1060 0.0964 0.1004 -0.0049 -0.0066 0.0047 331 GLU A CA 1884 C C . GLU A 243 ? 0.1051 0.0981 0.0989 -0.0026 -0.0042 0.0020 331 GLU A C 1885 O O . GLU A 243 ? 0.1078 0.1107 0.1067 0.0006 -0.0061 0.0076 331 GLU A O 1886 C CB . GLU A 243 ? 0.1099 0.0884 0.1080 0.0185 -0.0047 -0.0032 331 GLU A CB 1887 C CG . GLU A 243 ? 0.0992 0.1159 0.1024 0.0062 -0.0019 0.0100 331 GLU A CG 1888 C CD . GLU A 243 ? 0.1314 0.1329 0.1277 0.0021 -0.0067 0.0029 331 GLU A CD 1889 O OE1 . GLU A 243 ? 0.1703 0.1759 0.1601 0.0256 -0.0110 0.0247 331 GLU A OE1 1890 O OE2 . GLU A 243 ? 0.1684 0.1320 0.1556 0.0067 0.0173 0.0015 331 GLU A OE2 1891 N N . LYS A 244 ? 0.1147 0.1069 0.1015 0.0040 -0.0036 0.0029 332 LYS A N 1892 C CA . LYS A 244 ? 0.1163 0.1137 0.1132 0.0029 -0.0146 0.0037 332 LYS A CA 1893 C C . LYS A 244 ? 0.1087 0.1093 0.1165 0.0003 -0.0117 0.0017 332 LYS A C 1894 O O . LYS A 244 ? 0.1165 0.1018 0.1203 -0.0087 -0.0101 0.0077 332 LYS A O 1895 C CB . LYS A 244 ? 0.1323 0.1357 0.1208 0.0058 -0.0101 -0.0100 332 LYS A CB 1896 C CG . LYS A 244 ? 0.1389 0.1545 0.1284 0.0062 -0.0176 0.0044 332 LYS A CG 1897 C CD . LYS A 244 ? 0.1952 0.1910 0.1857 0.0004 -0.0123 -0.0181 332 LYS A CD 1898 C CE . LYS A 244 ? 0.2497 0.2273 0.2467 -0.0134 0.0008 -0.0090 332 LYS A CE 1899 N NZ . LYS A 244 ? 0.3084 0.2955 0.2748 -0.0017 -0.0001 -0.0191 332 LYS A NZ 1900 N N . HIS A 245 ? 0.1096 0.1019 0.1263 -0.0025 -0.0122 0.0057 333 HIS A N 1901 C CA . HIS A 245 ? 0.1098 0.1009 0.1046 -0.0035 -0.0065 -0.0001 333 HIS A CA 1902 C C . HIS A 245 ? 0.0996 0.1078 0.0949 0.0021 -0.0067 0.0031 333 HIS A C 1903 O O . HIS A 245 ? 0.1198 0.1182 0.1074 -0.0155 -0.0114 0.0076 333 HIS A O 1904 C CB . HIS A 245 ? 0.1246 0.1180 0.1391 0.0144 -0.0070 -0.0084 333 HIS A CB 1905 C CG . HIS A 245 ? 0.1116 0.1577 0.1821 0.0211 -0.0035 -0.0124 333 HIS A CG 1906 N ND1 . HIS A 245 ? 0.1552 0.2247 0.1827 -0.0108 -0.0120 -0.0080 333 HIS A ND1 1907 C CD2 . HIS A 245 ? 0.1582 0.2229 0.1842 -0.0117 0.0132 -0.0152 333 HIS A CD2 1908 C CE1 . HIS A 245 ? 0.2035 0.2580 0.1759 -0.0085 -0.0196 -0.0024 333 HIS A CE1 1909 N NE2 . HIS A 245 ? 0.1920 0.2712 0.2197 0.0017 -0.0131 -0.0025 333 HIS A NE2 1910 N N . TYR A 246 ? 0.1072 0.0996 0.1042 -0.0056 -0.0062 0.0063 334 TYR A N 1911 C CA . TYR A 246 ? 0.1003 0.0991 0.1067 0.0021 -0.0043 0.0037 334 TYR A CA 1912 C C . TYR A 246 ? 0.1026 0.0850 0.1028 -0.0076 -0.0001 -0.0027 334 TYR A C 1913 O O . TYR A 246 ? 0.1107 0.0926 0.1195 -0.0204 -0.0017 0.0004 334 TYR A O 1914 C CB . TYR A 246 ? 0.1073 0.0861 0.1076 -0.0053 -0.0005 0.0042 334 TYR A CB 1915 C CG . TYR A 246 ? 0.0875 0.0821 0.1051 0.0026 -0.0056 0.0093 334 TYR A CG 1916 C CD1 . TYR A 246 ? 0.0967 0.0969 0.1215 0.0012 -0.0014 -0.0017 334 TYR A CD1 1917 C CD2 . TYR A 246 ? 0.1038 0.0882 0.1190 0.0049 0.0102 0.0058 334 TYR A CD2 1918 C CE1 . TYR A 246 ? 0.1064 0.0854 0.1040 -0.0077 0.0029 0.0176 334 TYR A CE1 1919 C CE2 . TYR A 246 ? 0.0834 0.0731 0.1144 0.0036 0.0111 -0.0038 334 TYR A CE2 1920 C CZ . TYR A 246 ? 0.0980 0.0847 0.1005 0.0023 -0.0016 -0.0033 334 TYR A CZ 1921 O OH . TYR A 246 ? 0.1217 0.1030 0.1071 -0.0050 -0.0034 -0.0043 334 TYR A OH 1922 N N . ILE A 247 ? 0.1019 0.0935 0.0936 -0.0013 -0.0074 0.0037 335 ILE A N 1923 C CA . ILE A 247 ? 0.0976 0.0873 0.1123 -0.0003 -0.0074 0.0017 335 ILE A CA 1924 C C . ILE A 247 ? 0.1084 0.1112 0.1224 -0.0090 -0.0002 0.0085 335 ILE A C 1925 O O . ILE A 247 ? 0.1066 0.1015 0.1217 -0.0160 -0.0064 0.0055 335 ILE A O 1926 C CB . ILE A 247 ? 0.1144 0.0924 0.1234 0.0062 -0.0041 0.0055 335 ILE A CB 1927 C CG1 . ILE A 247 ? 0.1101 0.1282 0.1063 -0.0016 -0.0123 0.0134 335 ILE A CG1 1928 C CG2 . ILE A 247 ? 0.1266 0.1160 0.1632 0.0098 0.0011 0.0120 335 ILE A CG2 1929 C CD1 . ILE A 247 ? 0.1207 0.1268 0.1394 0.0026 -0.0014 0.0082 335 ILE A CD1 1930 N N . GLU A 248 ? 0.1274 0.0913 0.1190 -0.0033 -0.0126 0.0086 336 GLU A N 1931 C CA . GLU A 248 ? 0.1263 0.1011 0.1241 -0.0082 -0.0071 -0.0009 336 GLU A CA 1932 C C . GLU A 248 ? 0.1310 0.1358 0.1497 -0.0141 -0.0028 -0.0017 336 GLU A C 1933 O O . GLU A 248 ? 0.1601 0.1483 0.1578 -0.0087 -0.0110 0.0062 336 GLU A O 1934 C CB . GLU A 248 ? 0.1357 0.1328 0.1506 -0.0137 -0.0065 -0.0001 336 GLU A CB 1935 C CG . GLU A 248 ? 0.1426 0.1312 0.1595 -0.0055 0.0000 0.0036 336 GLU A CG 1936 C CD . GLU A 248 ? 0.1723 0.2103 0.2127 -0.0043 -0.0177 -0.0171 336 GLU A CD 1937 O OE1 . GLU A 248 ? 0.1881 0.2435 0.2475 0.0173 -0.0156 -0.0205 336 GLU A OE1 1938 O OE2 . GLU A 248 ? 0.1721 0.2407 0.2475 0.0145 -0.0150 -0.0277 336 GLU A OE2 1939 N N . ALA A 249 ? 0.1215 0.1303 0.1437 -0.0230 -0.0037 -0.0143 337 ALA A N 1940 C CA . ALA A 249 ? 0.1383 0.1448 0.1496 -0.0115 0.0007 -0.0048 337 ALA A CA 1941 C C . ALA A 249 ? 0.1392 0.1467 0.1454 -0.0120 0.0000 -0.0094 337 ALA A C 1942 O O . ALA A 249 ? 0.1477 0.1784 0.1581 -0.0321 0.0032 -0.0063 337 ALA A O 1943 C CB . ALA A 249 ? 0.1377 0.1576 0.1515 -0.0012 -0.0045 -0.0071 337 ALA A CB 1944 N N . PHE A 250 ? 0.1147 0.1205 0.1261 -0.0031 -0.0078 0.0002 338 PHE A N 1945 C CA . PHE A 250 ? 0.1068 0.0982 0.1168 -0.0070 -0.0043 -0.0051 338 PHE A CA 1946 C C . PHE A 250 ? 0.1121 0.1012 0.1136 -0.0089 0.0015 -0.0004 338 PHE A C 1947 O O . PHE A 250 ? 0.1292 0.0822 0.1202 -0.0063 -0.0042 0.0057 338 PHE A O 1948 C CB . PHE A 250 ? 0.1095 0.1103 0.1194 -0.0052 0.0000 0.0012 338 PHE A CB 1949 C CG . PHE A 250 ? 0.1072 0.0868 0.0960 0.0040 -0.0011 0.0014 338 PHE A CG 1950 C CD1 . PHE A 250 ? 0.1101 0.1055 0.1140 0.0008 0.0033 0.0062 338 PHE A CD1 1951 C CD2 . PHE A 250 ? 0.1046 0.0978 0.1099 -0.0100 -0.0046 -0.0054 338 PHE A CD2 1952 C CE1 . PHE A 250 ? 0.1327 0.1119 0.1185 -0.0027 0.0050 -0.0063 338 PHE A CE1 1953 C CE2 . PHE A 250 ? 0.1007 0.1110 0.1185 -0.0049 -0.0061 0.0019 338 PHE A CE2 1954 C CZ . PHE A 250 ? 0.1227 0.1305 0.1206 -0.0020 -0.0168 -0.0059 338 PHE A CZ 1955 N N . ARG A 251 ? 0.1067 0.1010 0.1109 0.0034 -0.0045 0.0086 339 ARG A N 1956 C CA . ARG A 251 ? 0.1187 0.1008 0.1193 -0.0046 -0.0079 0.0065 339 ARG A CA 1957 C C . ARG A 251 ? 0.1264 0.1076 0.1100 -0.0054 -0.0071 -0.0027 339 ARG A C 1958 O O . ARG A 251 ? 0.1372 0.1034 0.1300 -0.0071 -0.0057 0.0032 339 ARG A O 1959 C CB . ARG A 251 ? 0.1285 0.1172 0.1226 -0.0030 0.0015 0.0140 339 ARG A CB 1960 C CG . ARG A 251 ? 0.1663 0.1464 0.1551 0.0063 0.0013 -0.0011 339 ARG A CG 1961 C CD . ARG A 251 ? 0.1548 0.1229 0.1469 0.0073 0.0081 -0.0024 339 ARG A CD 1962 N NE . ARG A 251 ? 0.1744 0.1313 0.1669 -0.0002 0.0146 0.0004 339 ARG A NE 1963 C CZ . ARG A 251 ? 0.1566 0.1208 0.1616 0.0007 0.0023 0.0053 339 ARG A CZ 1964 N NH1 . ARG A 251 ? 0.1588 0.1293 0.1705 0.0086 0.0147 -0.0119 339 ARG A NH1 1965 N NH2 . ARG A 251 ? 0.2183 0.1307 0.2170 0.0064 0.0086 0.0123 339 ARG A NH2 1966 N N . PRO A 252 ? 0.1297 0.1223 0.1331 -0.0091 0.0054 0.0113 340 PRO A N 1967 C CA . PRO A 252 ? 0.1381 0.1167 0.1419 -0.0116 0.0063 0.0094 340 PRO A CA 1968 C C . PRO A 252 ? 0.1351 0.1194 0.1404 -0.0049 0.0075 0.0084 340 PRO A C 1969 O O . PRO A 252 ? 0.1509 0.1159 0.1561 -0.0194 0.0060 0.0081 340 PRO A O 1970 C CB . PRO A 252 ? 0.1492 0.1411 0.1514 -0.0166 0.0049 0.0075 340 PRO A CB 1971 C CG . PRO A 252 ? 0.1505 0.1764 0.1609 -0.0244 -0.0067 0.0069 340 PRO A CG 1972 C CD . PRO A 252 ? 0.1438 0.1212 0.1425 -0.0122 0.0060 0.0042 340 PRO A CD 1973 N N . LEU A 253 ? 0.1328 0.1102 0.1372 -0.0145 0.0022 -0.0013 341 LEU A N 1974 C CA . LEU A 253 ? 0.1448 0.1341 0.1432 -0.0056 0.0010 0.0022 341 LEU A CA 1975 C C . LEU A 253 ? 0.1297 0.1123 0.1320 -0.0152 0.0032 -0.0009 341 LEU A C 1976 O O . LEU A 253 ? 0.1306 0.1631 0.1437 -0.0151 0.0024 -0.0027 341 LEU A O 1977 C CB A LEU A 253 ? 0.1427 0.1414 0.1671 -0.0041 -0.0056 -0.0009 341 LEU A CB 1978 C CB B LEU A 253 ? 0.1577 0.1476 0.1748 -0.0035 -0.0030 -0.0005 341 LEU A CB 1979 C CG A LEU A 253 ? 0.1589 0.1724 0.1728 -0.0007 0.0056 0.0019 341 LEU A CG 1980 C CG B LEU A 253 ? 0.1957 0.1978 0.2048 0.0069 -0.0121 -0.0033 341 LEU A CG 1981 C CD1 A LEU A 253 ? 0.1605 0.1759 0.1700 -0.0030 0.0038 -0.0053 341 LEU A CD1 1982 C CD1 B LEU A 253 ? 0.2259 0.2221 0.2245 0.0033 -0.0104 0.0056 341 LEU A CD1 1983 C CD2 A LEU A 253 ? 0.1666 0.1773 0.1879 0.0012 0.0021 -0.0116 341 LEU A CD2 1984 C CD2 B LEU A 253 ? 0.2359 0.2472 0.2323 0.0007 0.0023 0.0045 341 LEU A CD2 1985 N N . LEU A 254 ? 0.1263 0.1196 0.1280 -0.0069 0.0079 0.0043 342 LEU A N 1986 C CA . LEU A 254 ? 0.1214 0.0986 0.1101 -0.0015 0.0021 -0.0001 342 LEU A CA 1987 C C . LEU A 254 ? 0.1235 0.1108 0.1129 -0.0096 0.0028 0.0110 342 LEU A C 1988 O O . LEU A 254 ? 0.1361 0.1178 0.1187 -0.0121 0.0021 0.0087 342 LEU A O 1989 C CB . LEU A 254 ? 0.1051 0.0837 0.1102 -0.0094 0.0030 0.0055 342 LEU A CB 1990 C CG . LEU A 254 ? 0.1117 0.0835 0.1156 -0.0088 0.0062 0.0008 342 LEU A CG 1991 C CD1 . LEU A 254 ? 0.1287 0.0907 0.1148 -0.0154 0.0071 0.0061 342 LEU A CD1 1992 C CD2 . LEU A 254 ? 0.1299 0.1053 0.1055 0.0061 0.0023 -0.0082 342 LEU A CD2 1993 N N . GLU A 255 ? 0.1351 0.1085 0.1317 -0.0045 0.0078 0.0035 343 GLU A N 1994 C CA . GLU A 255 ? 0.1386 0.1119 0.1318 -0.0026 0.0002 0.0081 343 GLU A CA 1995 C C . GLU A 255 ? 0.1469 0.1287 0.1448 -0.0119 -0.0019 -0.0001 343 GLU A C 1996 O O . GLU A 255 ? 0.1753 0.1321 0.1608 -0.0216 0.0010 0.0140 343 GLU A O 1997 C CB . GLU A 255 ? 0.1533 0.0986 0.1266 -0.0113 0.0030 0.0165 343 GLU A CB 1998 C CG . GLU A 255 ? 0.2083 0.1229 0.1733 -0.0034 -0.0066 0.0191 343 GLU A CG 1999 C CD . GLU A 255 ? 0.2018 0.1764 0.2216 -0.0045 0.0018 -0.0066 343 GLU A CD 2000 O OE1 . GLU A 255 ? 0.2330 0.1989 0.2370 -0.0178 0.0203 -0.0034 343 GLU A OE1 2001 O OE2 . GLU A 255 ? 0.2638 0.2133 0.2729 0.0165 -0.0120 0.0097 343 GLU A OE2 2002 N N . ALA A 256 ? 0.1476 0.1277 0.1289 -0.0168 0.0044 0.0013 344 ALA A N 2003 C CA . ALA A 256 ? 0.1594 0.1597 0.1552 -0.0145 0.0123 0.0052 344 ALA A CA 2004 C C . ALA A 256 ? 0.1596 0.1679 0.1516 -0.0220 0.0076 0.0125 344 ALA A C 2005 O O . ALA A 256 ? 0.1977 0.2038 0.1525 -0.0418 0.0226 0.0369 344 ALA A O 2006 C CB . ALA A 256 ? 0.1449 0.1596 0.1618 -0.0191 0.0142 0.0029 344 ALA A CB 2007 N N . ARG A 257 ? 0.1452 0.1512 0.1399 -0.0254 0.0037 0.0102 345 ARG A N 2008 C CA . ARG A 257 ? 0.1496 0.1452 0.1417 -0.0171 0.0058 0.0112 345 ARG A CA 2009 C C . ARG A 257 ? 0.1616 0.1430 0.1490 -0.0080 0.0041 0.0160 345 ARG A C 2010 O O . ARG A 257 ? 0.1604 0.1436 0.1539 -0.0108 -0.0080 0.0135 345 ARG A O 2011 C CB . ARG A 257 ? 0.1483 0.1512 0.1512 -0.0102 -0.0010 0.0057 345 ARG A CB 2012 C CG . ARG A 257 ? 0.1631 0.1585 0.1681 0.0001 -0.0010 -0.0075 345 ARG A CG 2013 C CD . ARG A 257 ? 0.1972 0.1768 0.1906 -0.0033 0.0019 0.0013 345 ARG A CD 2014 N NE . ARG A 257 ? 0.2112 0.2280 0.2282 0.0099 0.0087 0.0007 345 ARG A NE 2015 C CZ . ARG A 257 ? 0.2354 0.2557 0.2543 -0.0101 0.0048 -0.0006 345 ARG A CZ 2016 N NH1 . ARG A 257 ? 0.2192 0.2593 0.2345 0.0103 0.0149 0.0034 345 ARG A NH1 2017 N NH2 . ARG A 257 ? 0.2633 0.2887 0.3025 0.0225 0.0210 0.0021 345 ARG A NH2 2018 N N . GLY A 258 ? 0.1453 0.1381 0.1313 -0.0221 0.0070 0.0119 346 GLY A N 2019 C CA . GLY A 258 ? 0.1518 0.1427 0.1425 -0.0133 0.0092 0.0124 346 GLY A CA 2020 C C . GLY A 258 ? 0.1426 0.1471 0.1443 -0.0105 0.0063 0.0137 346 GLY A C 2021 O O . GLY A 258 ? 0.1617 0.1400 0.1538 -0.0009 0.0096 0.0261 346 GLY A O 2022 N N . PHE A 259 ? 0.1371 0.1308 0.1485 -0.0103 0.0054 0.0126 347 PHE A N 2023 C CA . PHE A 259 ? 0.1241 0.1261 0.1360 -0.0051 0.0060 0.0057 347 PHE A CA 2024 C C . PHE A 259 ? 0.1353 0.1272 0.1383 -0.0043 0.0108 0.0058 347 PHE A C 2025 O O . PHE A 259 ? 0.1318 0.1212 0.1353 -0.0101 0.0101 0.0070 347 PHE A O 2026 C CB . PHE A 259 ? 0.1353 0.1257 0.1325 -0.0108 0.0051 -0.0085 347 PHE A CB 2027 C CG . PHE A 259 ? 0.1332 0.1298 0.1199 0.0004 0.0026 -0.0013 347 PHE A CG 2028 C CD1 . PHE A 259 ? 0.1341 0.0944 0.1271 -0.0175 0.0060 0.0009 347 PHE A CD1 2029 C CD2 . PHE A 259 ? 0.1252 0.1164 0.1213 -0.0040 -0.0001 -0.0067 347 PHE A CD2 2030 C CE1 . PHE A 259 ? 0.1108 0.1118 0.1155 -0.0078 0.0027 -0.0076 347 PHE A CE1 2031 C CE2 . PHE A 259 ? 0.1226 0.1057 0.1274 -0.0043 -0.0046 0.0013 347 PHE A CE2 2032 C CZ . PHE A 259 ? 0.1199 0.1122 0.1192 -0.0215 0.0026 -0.0166 347 PHE A CZ 2033 N N . PRO A 260 ? 0.1715 0.1323 0.1535 -0.0035 -0.0045 -0.0002 348 PRO A N 2034 C CA . PRO A 260 ? 0.1546 0.1216 0.1431 -0.0068 0.0132 0.0002 348 PRO A CA 2035 C C . PRO A 260 ? 0.1381 0.1134 0.1420 -0.0075 0.0106 -0.0018 348 PRO A C 2036 O O . PRO A 260 ? 0.1649 0.1186 0.1651 -0.0067 0.0251 -0.0022 348 PRO A O 2037 C CB . PRO A 260 ? 0.1861 0.1360 0.1845 -0.0041 0.0087 -0.0066 348 PRO A CB 2038 C CG . PRO A 260 ? 0.1943 0.1295 0.1793 0.0061 0.0103 0.0041 348 PRO A CG 2039 C CD . PRO A 260 ? 0.1790 0.1447 0.1643 -0.0023 -0.0003 0.0024 348 PRO A CD 2040 N N . ALA A 261 ? 0.1245 0.1052 0.1293 0.0009 0.0101 0.0002 349 ALA A N 2041 C CA . ALA A 261 ? 0.1092 0.0940 0.1070 0.0021 0.0053 -0.0022 349 ALA A CA 2042 C C . ALA A 261 ? 0.1018 0.0836 0.1130 -0.0022 0.0021 -0.0030 349 ALA A C 2043 O O . ALA A 261 ? 0.1138 0.1176 0.1299 -0.0047 -0.0018 -0.0114 349 ALA A O 2044 C CB . ALA A 261 ? 0.1067 0.0960 0.1318 -0.0031 0.0090 -0.0074 349 ALA A CB 2045 N N . GLN A 262 ? 0.1109 0.0870 0.1183 0.0066 0.0040 -0.0041 350 GLN A N 2046 C CA . GLN A 262 ? 0.1026 0.0902 0.1103 -0.0059 -0.0042 -0.0008 350 GLN A CA 2047 C C . GLN A 262 ? 0.1197 0.0749 0.0991 -0.0074 -0.0094 -0.0161 350 GLN A C 2048 O O . GLN A 262 ? 0.1581 0.1005 0.1166 -0.0194 -0.0302 -0.0089 350 GLN A O 2049 C CB . GLN A 262 ? 0.1149 0.0858 0.1203 -0.0042 0.0006 -0.0166 350 GLN A CB 2050 C CG . GLN A 262 ? 0.1425 0.0829 0.1304 0.0019 0.0033 -0.0164 350 GLN A CG 2051 C CD . GLN A 262 ? 0.1387 0.0660 0.1547 0.0041 0.0092 -0.0016 350 GLN A CD 2052 O OE1 . GLN A 262 ? 0.1655 0.1419 0.1910 -0.0141 0.0137 -0.0216 350 GLN A OE1 2053 N NE2 . GLN A 262 ? 0.1545 0.1028 0.1498 -0.0093 -0.0004 -0.0085 350 GLN A NE2 2054 N N . PHE A 263 ? 0.0998 0.0612 0.0926 -0.0060 -0.0163 -0.0135 351 PHE A N 2055 C CA . PHE A 263 ? 0.0933 0.0740 0.0918 -0.0014 -0.0051 -0.0069 351 PHE A CA 2056 C C . PHE A 263 ? 0.1033 0.0846 0.0855 -0.0054 -0.0049 -0.0054 351 PHE A C 2057 O O . PHE A 263 ? 0.1195 0.1008 0.0973 0.0051 -0.0062 -0.0162 351 PHE A O 2058 C CB . PHE A 263 ? 0.1033 0.0939 0.0821 -0.0076 -0.0150 -0.0110 351 PHE A CB 2059 C CG . PHE A 263 ? 0.1030 0.1000 0.0939 -0.0075 -0.0127 0.0015 351 PHE A CG 2060 C CD1 . PHE A 263 ? 0.1216 0.1217 0.1489 0.0002 0.0120 0.0055 351 PHE A CD1 2061 C CD2 . PHE A 263 ? 0.1123 0.0974 0.1054 0.0053 -0.0016 0.0034 351 PHE A CD2 2062 C CE1 . PHE A 263 ? 0.1425 0.1170 0.1327 0.0005 0.0127 0.0111 351 PHE A CE1 2063 C CE2 . PHE A 263 ? 0.1200 0.1342 0.1142 -0.0014 -0.0044 0.0046 351 PHE A CE2 2064 C CZ . PHE A 263 ? 0.1104 0.1200 0.1123 -0.0040 -0.0002 0.0000 351 PHE A CZ 2065 N N . ILE A 264 ? 0.0978 0.0760 0.0779 0.0004 -0.0064 -0.0039 352 ILE A N 2066 C CA . ILE A 264 ? 0.1035 0.0870 0.0866 -0.0058 0.0024 -0.0057 352 ILE A CA 2067 C C . ILE A 264 ? 0.0946 0.0889 0.0753 0.0027 -0.0033 -0.0038 352 ILE A C 2068 O O . ILE A 264 ? 0.1110 0.0901 0.0840 0.0167 -0.0051 -0.0023 352 ILE A O 2069 C CB . ILE A 264 ? 0.1063 0.0829 0.0770 -0.0032 0.0013 0.0080 352 ILE A CB 2070 C CG1 . ILE A 264 ? 0.0940 0.0769 0.0952 0.0020 -0.0013 -0.0091 352 ILE A CG1 2071 C CG2 . ILE A 264 ? 0.0946 0.0823 0.0918 -0.0052 -0.0095 -0.0123 352 ILE A CG2 2072 C CD1 . ILE A 264 ? 0.1072 0.0980 0.0930 0.0013 -0.0168 0.0004 352 ILE A CD1 2073 N N . VAL A 265 ? 0.1097 0.0953 0.0804 0.0155 -0.0026 -0.0072 353 VAL A N 2074 C CA . VAL A 265 ? 0.1142 0.0990 0.0874 0.0074 -0.0046 -0.0052 353 VAL A CA 2075 C C . VAL A 265 ? 0.0909 0.0921 0.0773 0.0130 -0.0140 0.0022 353 VAL A C 2076 O O . VAL A 265 ? 0.1086 0.1021 0.0936 0.0168 -0.0021 -0.0028 353 VAL A O 2077 C CB . VAL A 265 ? 0.1141 0.1212 0.1107 0.0077 0.0026 0.0024 353 VAL A CB 2078 C CG1 . VAL A 265 ? 0.1174 0.1491 0.1187 0.0007 -0.0080 0.0163 353 VAL A CG1 2079 C CG2 . VAL A 265 ? 0.0953 0.1513 0.1256 0.0083 -0.0144 0.0002 353 VAL A CG2 2080 N N . ASP A 266 ? 0.0874 0.0898 0.0840 0.0023 -0.0047 -0.0042 354 ASP A N 2081 C CA . ASP A 266 ? 0.1029 0.1062 0.0876 0.0101 -0.0119 0.0068 354 ASP A CA 2082 C C . ASP A 266 ? 0.0931 0.1017 0.0924 0.0165 -0.0054 0.0051 354 ASP A C 2083 O O . ASP A 266 ? 0.1056 0.1309 0.0839 0.0240 -0.0104 -0.0090 354 ASP A O 2084 C CB . ASP A 266 ? 0.0910 0.1100 0.0809 0.0003 -0.0029 0.0112 354 ASP A CB 2085 C CG . ASP A 266 ? 0.1079 0.1064 0.1015 -0.0002 -0.0062 0.0059 354 ASP A CG 2086 O OD1 . ASP A 266 ? 0.1103 0.1391 0.1050 0.0041 0.0001 -0.0059 354 ASP A OD1 2087 O OD2 . ASP A 266 ? 0.1029 0.1233 0.0977 -0.0020 -0.0057 0.0123 354 ASP A OD2 2088 N N . GLN A 267 ? 0.0963 0.1290 0.0854 0.0126 -0.0201 -0.0016 355 GLN A N 2089 C CA . GLN A 267 ? 0.1114 0.1289 0.0972 0.0001 -0.0145 0.0058 355 GLN A CA 2090 C C . GLN A 267 ? 0.1125 0.1345 0.1023 0.0010 -0.0059 0.0082 355 GLN A C 2091 O O . GLN A 267 ? 0.1247 0.1555 0.0892 0.0080 -0.0128 0.0055 355 GLN A O 2092 C CB . GLN A 267 ? 0.1161 0.1191 0.0968 0.0062 -0.0224 0.0166 355 GLN A CB 2093 C CG . GLN A 267 ? 0.1221 0.1332 0.1097 0.0004 -0.0129 0.0027 355 GLN A CG 2094 C CD . GLN A 267 ? 0.1214 0.1329 0.1161 -0.0022 -0.0048 0.0097 355 GLN A CD 2095 O OE1 . GLN A 267 ? 0.1456 0.2128 0.1275 -0.0088 -0.0378 -0.0089 355 GLN A OE1 2096 N NE2 . GLN A 267 ? 0.1279 0.1403 0.1072 -0.0083 -0.0095 0.0005 355 GLN A NE2 2097 N N . GLY A 268 ? 0.1125 0.1185 0.0901 0.0010 -0.0078 0.0152 356 GLY A N 2098 C CA . GLY A 268 ? 0.1014 0.1304 0.1087 0.0049 -0.0098 0.0137 356 GLY A CA 2099 C C . GLY A 268 ? 0.1177 0.1265 0.1029 0.0079 0.0024 0.0184 356 GLY A C 2100 O O . GLY A 268 ? 0.1228 0.1743 0.1110 0.0168 0.0110 0.0338 356 GLY A O 2101 N N . ARG A 269 ? 0.1233 0.1229 0.0910 0.0083 -0.0052 0.0190 357 ARG A N 2102 C CA . ARG A 269 ? 0.1164 0.1313 0.0964 0.0053 -0.0041 0.0206 357 ARG A CA 2103 C C . ARG A 269 ? 0.1169 0.1301 0.0708 0.0046 -0.0028 0.0118 357 ARG A C 2104 O O . ARG A 269 ? 0.1268 0.1394 0.0984 0.0052 -0.0073 0.0142 357 ARG A O 2105 C CB . ARG A 269 ? 0.1261 0.1330 0.0948 0.0168 -0.0095 0.0251 357 ARG A CB 2106 C CG . ARG A 269 ? 0.1427 0.1650 0.1122 -0.0005 -0.0053 0.0279 357 ARG A CG 2107 C CD . ARG A 269 ? 0.1371 0.1632 0.1230 0.0027 0.0054 0.0222 357 ARG A CD 2108 N NE . ARG A 269 ? 0.1373 0.1233 0.1174 -0.0123 -0.0068 0.0136 357 ARG A NE 2109 C CZ . ARG A 269 ? 0.1233 0.1112 0.1209 0.0076 -0.0055 0.0137 357 ARG A CZ 2110 N NH1 . ARG A 269 ? 0.1753 0.1655 0.1476 -0.0211 -0.0100 0.0296 357 ARG A NH1 2111 N NH2 . ARG A 269 ? 0.1592 0.1494 0.1297 0.0056 -0.0244 0.0118 357 ARG A NH2 2112 N N . SER A 270 ? 0.1220 0.1378 0.0771 0.0088 -0.0015 0.0107 358 SER A N 2113 C CA . SER A 270 ? 0.1223 0.1396 0.1159 0.0075 -0.0063 0.0123 358 SER A CA 2114 C C . SER A 270 ? 0.1295 0.1519 0.1189 0.0082 -0.0062 0.0150 358 SER A C 2115 O O . SER A 270 ? 0.1426 0.1694 0.1139 0.0051 -0.0272 0.0167 358 SER A O 2116 C CB . SER A 270 ? 0.1241 0.1513 0.1165 0.0035 -0.0088 0.0110 358 SER A CB 2117 O OG . SER A 270 ? 0.1149 0.1550 0.1065 0.0063 -0.0106 0.0115 358 SER A OG 2118 N N . GLY A 271 ? 0.1425 0.1770 0.1268 -0.0006 -0.0054 0.0030 359 GLY A N 2119 C CA . GLY A 271 ? 0.1517 0.1814 0.1484 0.0035 -0.0152 -0.0004 359 GLY A CA 2120 C C . GLY A 271 ? 0.1682 0.1842 0.1599 0.0019 -0.0117 0.0061 359 GLY A C 2121 O O . GLY A 271 ? 0.1865 0.2240 0.1926 0.0055 -0.0329 -0.0040 359 GLY A O 2122 N N . LYS A 272 ? 0.1565 0.1899 0.1496 0.0123 -0.0201 0.0068 360 LYS A N 2123 C CA . LYS A 272 ? 0.1531 0.1871 0.1524 0.0094 -0.0142 0.0053 360 LYS A CA 2124 C C . LYS A 272 ? 0.1562 0.1834 0.1598 0.0062 -0.0035 0.0051 360 LYS A C 2125 O O . LYS A 272 ? 0.1453 0.1953 0.1480 0.0051 -0.0055 0.0157 360 LYS A O 2126 C CB . LYS A 272 ? 0.1594 0.1993 0.1702 0.0124 -0.0115 0.0042 360 LYS A CB 2127 C CG . LYS A 272 ? 0.2051 0.2463 0.1996 0.0164 -0.0185 0.0130 360 LYS A CG 2128 C CD . LYS A 272 ? 0.2633 0.2713 0.2764 0.0040 -0.0031 0.0187 360 LYS A CD 2129 C CE . LYS A 272 ? 0.3461 0.3468 0.3186 -0.0002 -0.0051 -0.0008 360 LYS A CE 2130 N NZ . LYS A 272 ? 0.3540 0.3758 0.3688 -0.0031 0.0000 0.0131 360 LYS A NZ 2131 N N . GLN A 273 ? 0.1605 0.1847 0.1427 0.0048 -0.0088 0.0081 361 GLN A N 2132 C CA . GLN A 273 ? 0.1569 0.1857 0.1618 0.0064 -0.0077 0.0044 361 GLN A CA 2133 C C . GLN A 273 ? 0.1733 0.1952 0.1607 0.0043 -0.0123 0.0065 361 GLN A C 2134 O O . GLN A 273 ? 0.1831 0.2362 0.1835 0.0000 -0.0275 -0.0001 361 GLN A O 2135 C CB . GLN A 273 ? 0.1417 0.1805 0.1498 0.0055 -0.0055 -0.0011 361 GLN A CB 2136 C CG . GLN A 273 ? 0.1520 0.1693 0.1307 -0.0020 -0.0107 0.0126 361 GLN A CG 2137 C CD . GLN A 273 ? 0.1466 0.1583 0.1134 0.0121 0.0012 0.0156 361 GLN A CD 2138 O OE1 . GLN A 273 ? 0.1445 0.1884 0.1125 0.0171 -0.0091 0.0055 361 GLN A OE1 2139 N NE2 . GLN A 273 ? 0.1303 0.1576 0.1201 -0.0138 -0.0057 0.0199 361 GLN A NE2 2140 N N . PRO A 274 ? 0.1570 0.1899 0.1646 0.0058 -0.0142 0.0128 362 PRO A N 2141 C CA . PRO A 274 ? 0.1735 0.1892 0.1574 0.0005 -0.0032 0.0120 362 PRO A CA 2142 C C . PRO A 274 ? 0.1629 0.1898 0.1470 -0.0010 -0.0058 0.0093 362 PRO A C 2143 O O . PRO A 274 ? 0.1594 0.2252 0.1322 0.0059 -0.0064 0.0388 362 PRO A O 2144 C CB . PRO A 274 ? 0.1830 0.1927 0.1731 -0.0049 -0.0041 0.0067 362 PRO A CB 2145 C CG . PRO A 274 ? 0.2126 0.2438 0.2063 0.0043 -0.0085 0.0050 362 PRO A CG 2146 C CD . PRO A 274 ? 0.1596 0.2229 0.1783 0.0099 -0.0192 0.0057 362 PRO A CD 2147 N N . THR A 275 ? 0.1586 0.1700 0.1351 0.0003 -0.0125 0.0148 363 THR A N 2148 C CA . THR A 275 ? 0.1632 0.1763 0.1479 0.0025 -0.0027 0.0181 363 THR A CA 2149 C C . THR A 275 ? 0.1796 0.1856 0.1726 0.0007 0.0039 0.0225 363 THR A C 2150 O O . THR A 275 ? 0.1758 0.2000 0.1946 0.0127 -0.0046 0.0506 363 THR A O 2151 C CB . THR A 275 ? 0.1558 0.1566 0.1479 0.0043 -0.0065 0.0196 363 THR A CB 2152 O OG1 . THR A 275 ? 0.1442 0.1772 0.1491 0.0088 -0.0006 0.0303 363 THR A OG1 2153 C CG2 . THR A 275 ? 0.1381 0.1613 0.1440 0.0131 0.0005 0.0236 363 THR A CG2 2154 N N . GLY A 276 ? 0.1812 0.1936 0.1736 -0.0043 0.0004 0.0193 364 GLY A N 2155 C CA . GLY A 276 ? 0.1932 0.1977 0.2013 -0.0013 0.0052 0.0154 364 GLY A CA 2156 C C . GLY A 276 ? 0.1977 0.1869 0.1928 0.0032 0.0013 0.0214 364 GLY A C 2157 O O . GLY A 276 ? 0.2100 0.1944 0.2198 -0.0074 0.0033 0.0249 364 GLY A O 2158 N N . GLN A 277 ? 0.1943 0.1810 0.1831 -0.0014 0.0003 0.0302 365 GLN A N 2159 C CA . GLN A 277 ? 0.1858 0.1756 0.1843 0.0000 -0.0008 0.0291 365 GLN A CA 2160 C C . GLN A 277 ? 0.1981 0.1865 0.1888 0.0016 0.0032 0.0226 365 GLN A C 2161 O O . GLN A 277 ? 0.1844 0.2025 0.2250 0.0073 -0.0048 0.0383 365 GLN A O 2162 C CB . GLN A 277 ? 0.1715 0.1543 0.1679 0.0007 0.0030 0.0312 365 GLN A CB 2163 C CG . GLN A 277 ? 0.1823 0.1583 0.1729 -0.0002 0.0063 0.0236 365 GLN A CG 2164 C CD . GLN A 277 ? 0.1490 0.1519 0.1577 -0.0132 0.0025 0.0215 365 GLN A CD 2165 O OE1 . GLN A 277 ? 0.1620 0.1516 0.1518 -0.0009 0.0068 0.0125 365 GLN A OE1 2166 N NE2 . GLN A 277 ? 0.1427 0.1900 0.1690 -0.0163 0.0096 0.0179 365 GLN A NE2 2167 N N . LYS A 278 ? 0.1962 0.1955 0.2112 -0.0031 -0.0021 0.0235 366 LYS A N 2168 C CA . LYS A 278 ? 0.2093 0.2174 0.2286 0.0056 0.0065 0.0144 366 LYS A CA 2169 C C . LYS A 278 ? 0.1961 0.2154 0.2207 0.0060 0.0029 0.0194 366 LYS A C 2170 O O . LYS A 278 ? 0.2126 0.2412 0.2755 0.0140 0.0063 0.0319 366 LYS A O 2171 C CB . LYS A 278 ? 0.2282 0.2225 0.2479 0.0094 0.0017 0.0078 366 LYS A CB 2172 C CG . LYS A 278 ? 0.2710 0.2683 0.2759 0.0031 0.0085 0.0147 366 LYS A CG 2173 C CD . LYS A 278 ? 0.2800 0.2720 0.2772 -0.0027 0.0054 0.0018 366 LYS A CD 2174 C CE . LYS A 278 ? 0.2857 0.2889 0.2873 -0.0001 -0.0005 0.0054 366 LYS A CE 2175 N NZ . LYS A 278 ? 0.2992 0.3078 0.2997 0.0034 0.0066 -0.0003 366 LYS A NZ 2176 N N . GLU A 279 ? 0.1795 0.1960 0.2058 -0.0026 0.0089 0.0193 367 GLU A N 2177 C CA . GLU A 279 ? 0.1783 0.1743 0.1993 -0.0030 0.0039 0.0167 367 GLU A CA 2178 C C . GLU A 279 ? 0.1746 0.1613 0.1907 -0.0025 0.0122 0.0257 367 GLU A C 2179 O O . GLU A 279 ? 0.1703 0.1286 0.1787 -0.0140 0.0159 0.0341 367 GLU A O 2180 C CB . GLU A 279 ? 0.1953 0.1834 0.2101 0.0046 0.0022 0.0198 367 GLU A CB 2181 C CG . GLU A 279 ? 0.2020 0.1861 0.2096 0.0097 0.0015 0.0099 367 GLU A CG 2182 C CD . GLU A 279 ? 0.2326 0.2538 0.2618 0.0030 0.0063 0.0047 367 GLU A CD 2183 O OE1 . GLU A 279 ? 0.2386 0.2692 0.2693 0.0049 0.0078 0.0003 367 GLU A OE1 2184 O OE2 . GLU A 279 ? 0.2616 0.2881 0.2903 0.0189 0.0035 0.0085 367 GLU A OE2 2185 N N . TRP A 280 ? 0.1620 0.1357 0.1883 -0.0043 0.0083 0.0240 368 TRP A N 2186 C CA . TRP A 280 ? 0.1567 0.1376 0.1760 -0.0016 0.0077 0.0188 368 TRP A CA 2187 C C . TRP A 280 ? 0.1671 0.1481 0.1609 -0.0040 0.0098 0.0223 368 TRP A C 2188 O O . TRP A 280 ? 0.1746 0.1513 0.1803 -0.0057 0.0064 0.0264 368 TRP A O 2189 C CB . TRP A 280 ? 0.1598 0.1358 0.1732 -0.0056 0.0166 0.0054 368 TRP A CB 2190 C CG . TRP A 280 ? 0.1302 0.1135 0.1650 -0.0026 0.0125 0.0032 368 TRP A CG 2191 C CD1 . TRP A 280 ? 0.1273 0.1261 0.1327 -0.0006 0.0104 0.0158 368 TRP A CD1 2192 C CD2 . TRP A 280 ? 0.1169 0.1167 0.1348 -0.0018 0.0105 0.0206 368 TRP A CD2 2193 N NE1 . TRP A 280 ? 0.1375 0.1323 0.1478 0.0037 0.0116 0.0081 368 TRP A NE1 2194 C CE2 . TRP A 280 ? 0.1266 0.1157 0.1320 0.0046 -0.0010 0.0181 368 TRP A CE2 2195 C CE3 . TRP A 280 ? 0.1179 0.1354 0.1536 -0.0007 0.0167 0.0100 368 TRP A CE3 2196 C CZ2 . TRP A 280 ? 0.1428 0.1272 0.1311 -0.0043 -0.0040 0.0100 368 TRP A CZ2 2197 C CZ3 . TRP A 280 ? 0.1300 0.1320 0.1404 -0.0043 0.0036 0.0153 368 TRP A CZ3 2198 C CH2 . TRP A 280 ? 0.1296 0.1236 0.1170 0.0017 -0.0138 0.0176 368 TRP A CH2 2199 N N . GLY A 281 ? 0.1705 0.1594 0.1718 -0.0124 0.0018 0.0204 369 GLY A N 2200 C CA . GLY A 281 ? 0.1844 0.1712 0.1837 -0.0093 -0.0014 0.0049 369 GLY A CA 2201 C C . GLY A 281 ? 0.1748 0.1672 0.1748 -0.0054 0.0002 0.0043 369 GLY A C 2202 O O . GLY A 281 ? 0.1975 0.1936 0.1868 -0.0239 -0.0065 0.0089 369 GLY A O 2203 N N . HIS A 282 ? 0.1746 0.1707 0.1868 -0.0093 0.0054 0.0077 370 HIS A N 2204 C CA . HIS A 282 ? 0.1684 0.1670 0.1845 -0.0133 0.0024 0.0106 370 HIS A CA 2205 C C . HIS A 282 ? 0.1578 0.1560 0.1626 -0.0083 -0.0004 0.0062 370 HIS A C 2206 O O . HIS A 282 ? 0.1660 0.1821 0.1887 -0.0087 -0.0111 0.0007 370 HIS A O 2207 C CB . HIS A 282 ? 0.1840 0.1779 0.1904 -0.0074 -0.0015 0.0062 370 HIS A CB 2208 C CG . HIS A 282 ? 0.1863 0.1734 0.2046 -0.0088 0.0032 0.0181 370 HIS A CG 2209 N ND1 . HIS A 282 ? 0.2296 0.2144 0.2486 -0.0010 0.0007 0.0315 370 HIS A ND1 2210 C CD2 . HIS A 282 ? 0.1955 0.1758 0.2264 -0.0098 -0.0059 -0.0005 370 HIS A CD2 2211 C CE1 . HIS A 282 ? 0.2635 0.2121 0.2642 -0.0075 0.0010 0.0080 370 HIS A CE1 2212 N NE2 . HIS A 282 ? 0.2347 0.2146 0.2752 0.0087 -0.0045 0.0146 370 HIS A NE2 2213 N N . TRP A 283 ? 0.1565 0.1352 0.1458 -0.0164 -0.0033 0.0180 371 TRP A N 2214 C CA . TRP A 283 ? 0.1604 0.1490 0.1414 -0.0064 -0.0009 0.0086 371 TRP A CA 2215 C C . TRP A 283 ? 0.1623 0.1391 0.1386 0.0014 -0.0010 0.0136 371 TRP A C 2216 O O . TRP A 283 ? 0.1765 0.1460 0.1322 -0.0173 -0.0085 0.0168 371 TRP A O 2217 C CB . TRP A 283 ? 0.1615 0.1391 0.1421 -0.0046 -0.0057 0.0154 371 TRP A CB 2218 C CG . TRP A 283 ? 0.1660 0.1493 0.1391 0.0011 -0.0117 0.0201 371 TRP A CG 2219 C CD1 . TRP A 283 ? 0.1716 0.1488 0.1681 0.0001 -0.0094 0.0149 371 TRP A CD1 2220 C CD2 . TRP A 283 ? 0.1771 0.1295 0.1636 -0.0037 -0.0082 0.0223 371 TRP A CD2 2221 N NE1 . TRP A 283 ? 0.1763 0.1534 0.1625 0.0055 -0.0164 -0.0009 371 TRP A NE1 2222 C CE2 . TRP A 283 ? 0.1869 0.1622 0.1671 -0.0048 -0.0026 0.0044 371 TRP A CE2 2223 C CE3 . TRP A 283 ? 0.1892 0.2065 0.1804 -0.0068 -0.0051 0.0071 371 TRP A CE3 2224 C CZ2 . TRP A 283 ? 0.1950 0.1994 0.2036 -0.0047 -0.0109 -0.0063 371 TRP A CZ2 2225 C CZ3 . TRP A 283 ? 0.2124 0.2093 0.2087 -0.0158 0.0030 0.0076 371 TRP A CZ3 2226 C CH2 . TRP A 283 ? 0.2154 0.2326 0.2236 -0.0015 -0.0010 -0.0011 371 TRP A CH2 2227 N N . CYS A 284 ? 0.1665 0.1499 0.1484 -0.0030 -0.0044 0.0183 372 CYS A N 2228 C CA . CYS A 284 ? 0.1651 0.1485 0.1434 -0.0027 -0.0008 0.0188 372 CYS A CA 2229 C C . CYS A 284 ? 0.1714 0.1441 0.1466 -0.0066 0.0002 0.0275 372 CYS A C 2230 O O . CYS A 284 ? 0.1799 0.1520 0.1729 -0.0037 -0.0072 0.0449 372 CYS A O 2231 C CB . CYS A 284 ? 0.1768 0.1722 0.1748 -0.0126 -0.0125 0.0054 372 CYS A CB 2232 S SG . CYS A 284 ? 0.2006 0.1706 0.2111 -0.0395 -0.0182 0.0467 372 CYS A SG 2233 N N . ASN A 285 ? 0.1662 0.1461 0.1440 -0.0058 -0.0062 0.0341 373 ASN A N 2234 C CA . ASN A 285 ? 0.1570 0.1543 0.1411 -0.0079 -0.0044 0.0136 373 ASN A CA 2235 C C . ASN A 285 ? 0.1538 0.1612 0.1574 -0.0083 -0.0085 0.0354 373 ASN A C 2236 O O . ASN A 285 ? 0.1643 0.1606 0.1651 -0.0122 -0.0241 0.0587 373 ASN A O 2237 C CB . ASN A 285 ? 0.1685 0.1552 0.1534 -0.0094 -0.0106 0.0244 373 ASN A CB 2238 C CG . ASN A 285 ? 0.1728 0.1609 0.1592 -0.0107 0.0025 0.0306 373 ASN A CG 2239 O OD1 . ASN A 285 ? 0.1778 0.1654 0.1825 -0.0070 -0.0022 0.0558 373 ASN A OD1 2240 N ND2 . ASN A 285 ? 0.1997 0.1696 0.1730 -0.0160 -0.0187 0.0499 373 ASN A ND2 2241 N N . ALA A 286 ? 0.1584 0.1602 0.1554 -0.0121 -0.0113 0.0295 374 ALA A N 2242 C CA . ALA A 286 ? 0.1501 0.1543 0.1485 -0.0099 -0.0020 0.0180 374 ALA A CA 2243 C C . ALA A 286 ? 0.1498 0.1633 0.1487 -0.0102 -0.0088 0.0178 374 ALA A C 2244 O O . ALA A 286 ? 0.1493 0.1671 0.1447 -0.0074 -0.0208 0.0405 374 ALA A O 2245 C CB . ALA A 286 ? 0.1527 0.1491 0.1479 -0.0134 -0.0048 0.0199 374 ALA A CB 2246 N N . ILE A 287 ? 0.1588 0.1725 0.1667 -0.0006 -0.0044 0.0203 375 ILE A N 2247 C CA . ILE A 287 ? 0.1696 0.1766 0.1694 0.0003 -0.0048 0.0123 375 ILE A CA 2248 C C . ILE A 287 ? 0.1491 0.1664 0.1519 0.0015 -0.0036 0.0229 375 ILE A C 2249 O O . ILE A 287 ? 0.1448 0.1769 0.1593 0.0008 -0.0044 0.0443 375 ILE A O 2250 C CB . ILE A 287 ? 0.1883 0.1718 0.1751 -0.0022 -0.0081 0.0131 375 ILE A CB 2251 C CG1 . ILE A 287 ? 0.1996 0.1837 0.2012 0.0102 -0.0140 0.0190 375 ILE A CG1 2252 C CG2 . ILE A 287 ? 0.1833 0.1839 0.1859 -0.0017 -0.0138 0.0307 375 ILE A CG2 2253 C CD1 . ILE A 287 ? 0.2065 0.2024 0.2349 0.0125 -0.0110 0.0194 375 ILE A CD1 2254 N N . GLY A 288 ? 0.1676 0.1702 0.1585 -0.0058 0.0016 0.0281 376 GLY A N 2255 C CA . GLY A 288 ? 0.1628 0.1593 0.1435 0.0045 -0.0080 0.0288 376 GLY A CA 2256 C C . GLY A 288 ? 0.1529 0.1557 0.1407 -0.0026 -0.0066 0.0378 376 GLY A C 2257 O O . GLY A 288 ? 0.1751 0.1759 0.1730 0.0009 -0.0242 0.0493 376 GLY A O 2258 N N . THR A 289 ? 0.1557 0.1687 0.1175 0.0046 0.0044 0.0384 377 THR A N 2259 C CA . THR A 289 ? 0.1474 0.1570 0.1260 0.0013 -0.0097 0.0170 377 THR A CA 2260 C C . THR A 289 ? 0.1400 0.1696 0.1277 0.0025 -0.0090 0.0163 377 THR A C 2261 O O . THR A 289 ? 0.1615 0.2009 0.1108 0.0006 0.0003 0.0411 377 THR A O 2262 C CB . THR A 289 ? 0.1640 0.1744 0.1352 0.0053 -0.0138 0.0162 377 THR A CB 2263 O OG1 . THR A 289 ? 0.1611 0.2136 0.1262 0.0012 -0.0241 0.0363 377 THR A OG1 2264 C CG2 . THR A 289 ? 0.1643 0.1584 0.1051 -0.0029 -0.0099 0.0261 377 THR A CG2 2265 N N . GLY A 290 ? 0.1361 0.1688 0.1291 0.0034 -0.0149 0.0209 378 GLY A N 2266 C CA . GLY A 290 ? 0.1419 0.1676 0.1190 0.0060 -0.0162 0.0176 378 GLY A CA 2267 C C . GLY A 290 ? 0.1345 0.1583 0.1177 0.0102 -0.0073 0.0125 378 GLY A C 2268 O O . GLY A 290 ? 0.1350 0.1757 0.1044 0.0003 -0.0042 0.0280 378 GLY A O 2269 N N . PHE A 291 ? 0.1555 0.1800 0.1117 0.0073 -0.0055 0.0106 379 PHE A N 2270 C CA . PHE A 291 ? 0.1526 0.1720 0.1231 0.0128 -0.0039 0.0020 379 PHE A CA 2271 C C . PHE A 291 ? 0.1635 0.1901 0.1293 0.0065 -0.0080 0.0019 379 PHE A C 2272 O O . PHE A 291 ? 0.1564 0.2105 0.1030 0.0083 -0.0226 0.0015 379 PHE A O 2273 C CB . PHE A 291 ? 0.1567 0.2005 0.1269 0.0060 0.0012 0.0078 379 PHE A CB 2274 C CG . PHE A 291 ? 0.1520 0.2336 0.1339 0.0046 -0.0056 0.0106 379 PHE A CG 2275 C CD1 . PHE A 291 ? 0.1609 0.2235 0.1161 -0.0041 -0.0051 0.0065 379 PHE A CD1 2276 C CD2 . PHE A 291 ? 0.1883 0.2385 0.1696 0.0047 -0.0075 0.0227 379 PHE A CD2 2277 C CE1 . PHE A 291 ? 0.1750 0.2158 0.1413 -0.0071 -0.0009 0.0231 379 PHE A CE1 2278 C CE2 . PHE A 291 ? 0.1888 0.2181 0.1561 0.0086 -0.0026 0.0248 379 PHE A CE2 2279 C CZ . PHE A 291 ? 0.1601 0.2253 0.1625 -0.0022 -0.0028 0.0220 379 PHE A CZ 2280 N N . GLY A 292 ? 0.1581 0.1747 0.1203 0.0104 -0.0075 0.0071 380 GLY A N 2281 C CA . GLY A 292 ? 0.1528 0.1729 0.1085 0.0111 -0.0115 0.0024 380 GLY A CA 2282 C C . GLY A 292 ? 0.1449 0.1734 0.1185 0.0082 -0.0202 0.0004 380 GLY A C 2283 O O . GLY A 292 ? 0.1590 0.2121 0.1132 0.0128 -0.0090 -0.0044 380 GLY A O 2284 N N . MET A 293 ? 0.1672 0.1681 0.1243 0.0079 -0.0206 -0.0001 381 MET A N 2285 C CA . MET A 293 ? 0.1836 0.1876 0.1687 0.0122 -0.0183 -0.0118 381 MET A CA 2286 C C . MET A 293 ? 0.1761 0.1918 0.1670 0.0138 -0.0178 -0.0116 381 MET A C 2287 O O . MET A 293 ? 0.1750 0.1881 0.1459 0.0270 -0.0159 -0.0262 381 MET A O 2288 C CB . MET A 293 ? 0.2016 0.2199 0.2048 0.0140 -0.0089 -0.0163 381 MET A CB 2289 C CG . MET A 293 ? 0.2432 0.2642 0.2484 0.0175 -0.0186 -0.0187 381 MET A CG 2290 S SD . MET A 293 ? 0.3399 0.3276 0.3101 0.0020 0.0145 -0.0357 381 MET A SD 2291 C CE . MET A 293 ? 0.1908 0.1980 0.2212 -0.0122 0.0296 -0.0100 381 MET A CE 2292 N N . ARG A 294 ? 0.1903 0.2143 0.1578 0.0159 -0.0129 -0.0098 382 ARG A N 2293 C CA . ARG A 294 ? 0.1901 0.2069 0.1783 0.0134 0.0013 -0.0039 382 ARG A CA 2294 C C . ARG A 294 ? 0.1712 0.1788 0.1472 0.0186 0.0003 -0.0161 382 ARG A C 2295 O O . ARG A 294 ? 0.1696 0.2102 0.1531 0.0220 -0.0085 -0.0211 382 ARG A O 2296 C CB . ARG A 294 ? 0.1970 0.2162 0.1777 0.0204 -0.0080 -0.0093 382 ARG A CB 2297 C CG . ARG A 294 ? 0.2520 0.2666 0.2513 0.0061 0.0097 0.0032 382 ARG A CG 2298 C CD . ARG A 294 ? 0.2875 0.3061 0.2919 0.0076 -0.0059 -0.0038 382 ARG A CD 2299 N NE . ARG A 294 ? 0.3194 0.3147 0.2989 0.0126 -0.0108 0.0036 382 ARG A NE 2300 C CZ . ARG A 294 ? 0.3061 0.2913 0.2759 0.0090 -0.0093 0.0010 382 ARG A CZ 2301 N NH1 . ARG A 294 ? 0.3136 0.3041 0.2751 0.0080 -0.0109 0.0029 382 ARG A NH1 2302 N NH2 . ARG A 294 ? 0.2873 0.3145 0.2372 0.0127 -0.0080 -0.0071 382 ARG A NH2 2303 N N . PRO A 295 ? 0.1630 0.1898 0.1428 0.0160 0.0050 -0.0086 383 PRO A N 2304 C CA . PRO A 295 ? 0.1524 0.1661 0.1447 0.0095 0.0014 -0.0068 383 PRO A CA 2305 C C . PRO A 295 ? 0.1559 0.1661 0.1485 0.0156 0.0011 0.0048 383 PRO A C 2306 O O . PRO A 295 ? 0.1903 0.1934 0.1457 0.0310 0.0045 -0.0136 383 PRO A O 2307 C CB . PRO A 295 ? 0.1552 0.1768 0.1369 0.0092 -0.0026 -0.0197 383 PRO A CB 2308 C CG . PRO A 295 ? 0.1526 0.2011 0.1448 0.0123 0.0040 -0.0006 383 PRO A CG 2309 C CD . PRO A 295 ? 0.1755 0.1765 0.1344 0.0215 -0.0029 -0.0076 383 PRO A CD 2310 N N . THR A 296 ? 0.1640 0.1739 0.1397 0.0105 0.0096 -0.0088 384 THR A N 2311 C CA . THR A 296 ? 0.1672 0.1741 0.1660 0.0072 -0.0006 -0.0087 384 THR A CA 2312 C C . THR A 296 ? 0.1696 0.1608 0.1432 0.0126 -0.0064 -0.0157 384 THR A C 2313 O O . THR A 296 ? 0.1523 0.1455 0.1161 0.0085 -0.0105 -0.0311 384 THR A O 2314 C CB . THR A 296 ? 0.1764 0.1973 0.1825 0.0058 0.0025 -0.0028 384 THR A CB 2315 O OG1 . THR A 296 ? 0.2191 0.2198 0.1788 -0.0005 -0.0026 -0.0307 384 THR A OG1 2316 C CG2 . THR A 296 ? 0.1795 0.2158 0.1829 0.0079 -0.0077 -0.0127 384 THR A CG2 2317 N N . ALA A 297 ? 0.1686 0.1622 0.1533 0.0096 -0.0168 -0.0217 385 ALA A N 2318 C CA . ALA A 297 ? 0.1869 0.1701 0.1639 0.0051 -0.0059 -0.0223 385 ALA A CA 2319 C C . ALA A 297 ? 0.1936 0.1917 0.1754 -0.0031 -0.0040 -0.0135 385 ALA A C 2320 O O . ALA A 297 ? 0.2246 0.2207 0.1715 -0.0159 -0.0136 -0.0324 385 ALA A O 2321 C CB . ALA A 297 ? 0.1921 0.1821 0.1794 0.0043 -0.0222 -0.0207 385 ALA A CB 2322 N N . ASN A 298 ? 0.1934 0.2029 0.1803 -0.0035 -0.0043 -0.0258 386 ASN A N 2323 C CA . ASN A 298 ? 0.1968 0.2132 0.1803 0.0000 -0.0046 -0.0181 386 ASN A CA 2324 C C . ASN A 298 ? 0.1936 0.2082 0.1770 0.0007 -0.0069 -0.0146 386 ASN A C 2325 O O . ASN A 298 ? 0.2210 0.2467 0.1796 0.0032 -0.0113 -0.0076 386 ASN A O 2326 C CB . ASN A 298 ? 0.2234 0.2276 0.1988 -0.0042 -0.0055 -0.0315 386 ASN A CB 2327 C CG . ASN A 298 ? 0.2459 0.2204 0.1891 -0.0018 -0.0103 -0.0292 386 ASN A CG 2328 O OD1 . ASN A 298 ? 0.3010 0.2784 0.2647 0.0068 0.0208 -0.0183 386 ASN A OD1 2329 N ND2 . ASN A 298 ? 0.2785 0.2876 0.2534 -0.0139 0.0008 -0.0378 386 ASN A ND2 2330 N N . THR A 299 ? 0.1780 0.1878 0.1479 -0.0082 -0.0100 -0.0168 387 THR A N 2331 C CA . THR A 299 ? 0.1681 0.1886 0.1520 -0.0056 -0.0079 -0.0147 387 THR A CA 2332 C C . THR A 299 ? 0.1873 0.2052 0.1852 -0.0064 -0.0027 -0.0078 387 THR A C 2333 O O . THR A 299 ? 0.1918 0.2511 0.2061 -0.0001 -0.0096 -0.0122 387 THR A O 2334 C CB . THR A 299 ? 0.1473 0.1566 0.1360 -0.0122 -0.0158 -0.0169 387 THR A CB 2335 O OG1 . THR A 299 ? 0.1675 0.1835 0.1261 -0.0171 -0.0054 -0.0354 387 THR A OG1 2336 C CG2 . THR A 299 ? 0.1646 0.1905 0.1507 -0.0222 -0.0091 -0.0186 387 THR A CG2 2337 N N . GLY A 300 ? 0.1835 0.2102 0.1873 -0.0107 -0.0013 -0.0213 388 GLY A N 2338 C CA . GLY A 300 ? 0.1985 0.2229 0.2096 -0.0167 -0.0022 -0.0145 388 GLY A CA 2339 C C . GLY A 300 ? 0.2024 0.2259 0.2093 -0.0119 -0.0046 -0.0282 388 GLY A C 2340 O O . GLY A 300 ? 0.2284 0.2711 0.2320 -0.0315 -0.0041 -0.0316 388 GLY A O 2341 N N . HIS A 301 ? 0.1790 0.1886 0.1682 -0.0235 0.0004 -0.0331 389 HIS A N 2342 C CA . HIS A 301 ? 0.1671 0.1531 0.1713 -0.0152 0.0068 -0.0173 389 HIS A CA 2343 C C . HIS A 301 ? 0.1618 0.1522 0.1694 -0.0049 0.0091 -0.0121 389 HIS A C 2344 O O . HIS A 301 ? 0.1524 0.1312 0.1594 -0.0070 -0.0024 -0.0227 389 HIS A O 2345 C CB . HIS A 301 ? 0.1693 0.1626 0.1737 -0.0136 -0.0048 -0.0180 389 HIS A CB 2346 C CG . HIS A 301 ? 0.1638 0.1495 0.1679 -0.0213 -0.0023 -0.0107 389 HIS A CG 2347 N ND1 . HIS A 301 ? 0.1507 0.1670 0.1766 -0.0175 -0.0168 -0.0274 389 HIS A ND1 2348 C CD2 . HIS A 301 ? 0.1635 0.1538 0.1721 -0.0103 -0.0062 -0.0030 389 HIS A CD2 2349 C CE1 . HIS A 301 ? 0.1686 0.1886 0.1467 0.0116 0.0003 -0.0170 389 HIS A CE1 2350 N NE2 . HIS A 301 ? 0.1636 0.1865 0.1566 0.0054 -0.0049 -0.0172 389 HIS A NE2 2351 N N . GLN A 302 ? 0.1567 0.1392 0.1600 -0.0194 -0.0020 -0.0275 390 GLN A N 2352 C CA . GLN A 302 ? 0.1736 0.1492 0.1745 -0.0112 0.0024 -0.0212 390 GLN A CA 2353 C C . GLN A 302 ? 0.1515 0.1256 0.1508 -0.0152 -0.0112 -0.0144 390 GLN A C 2354 O O . GLN A 302 ? 0.1785 0.1264 0.2031 0.0014 -0.0159 -0.0177 390 GLN A O 2355 C CB . GLN A 302 ? 0.2040 0.1619 0.1894 -0.0203 -0.0009 -0.0166 390 GLN A CB 2356 C CG . GLN A 302 ? 0.2287 0.2198 0.2314 -0.0140 0.0100 -0.0121 390 GLN A CG 2357 C CD . GLN A 302 ? 0.2865 0.2582 0.2633 -0.0045 0.0030 0.0064 390 GLN A CD 2358 O OE1 . GLN A 302 ? 0.2683 0.2554 0.2725 -0.0182 0.0113 -0.0072 390 GLN A OE1 2359 N NE2 . GLN A 302 ? 0.2882 0.2898 0.3001 -0.0285 0.0116 -0.0124 390 GLN A NE2 2360 N N . TYR A 303 ? 0.1326 0.1361 0.1526 -0.0035 -0.0016 -0.0168 391 TYR A N 2361 C CA . TYR A 303 ? 0.1149 0.1197 0.1302 -0.0099 -0.0019 -0.0075 391 TYR A CA 2362 C C . TYR A 303 ? 0.1138 0.1151 0.1235 -0.0088 -0.0062 -0.0071 391 TYR A C 2363 O O . TYR A 303 ? 0.1234 0.1091 0.1227 -0.0188 -0.0168 -0.0135 391 TYR A O 2364 C CB . TYR A 303 ? 0.1168 0.1244 0.1277 -0.0123 0.0008 -0.0104 391 TYR A CB 2365 C CG . TYR A 303 ? 0.1282 0.1252 0.1267 -0.0159 -0.0039 -0.0125 391 TYR A CG 2366 C CD1 . TYR A 303 ? 0.1386 0.1375 0.1684 -0.0062 -0.0005 -0.0013 391 TYR A CD1 2367 C CD2 . TYR A 303 ? 0.1262 0.1161 0.1508 -0.0204 -0.0065 -0.0060 391 TYR A CD2 2368 C CE1 . TYR A 303 ? 0.1602 0.1253 0.1690 -0.0261 0.0040 -0.0042 391 TYR A CE1 2369 C CE2 . TYR A 303 ? 0.1267 0.1519 0.1534 -0.0065 -0.0026 0.0103 391 TYR A CE2 2370 C CZ . TYR A 303 ? 0.1451 0.1358 0.1788 -0.0222 0.0149 0.0029 391 TYR A CZ 2371 O OH . TYR A 303 ? 0.1733 0.1841 0.2184 -0.0394 0.0337 0.0041 391 TYR A OH 2372 N N . VAL A 304 ? 0.1024 0.1085 0.1266 -0.0064 -0.0071 -0.0147 392 VAL A N 2373 C CA . VAL A 304 ? 0.1136 0.0984 0.1154 -0.0035 -0.0038 -0.0055 392 VAL A CA 2374 C C . VAL A 304 ? 0.1068 0.1042 0.1229 -0.0025 -0.0117 -0.0133 392 VAL A C 2375 O O . VAL A 304 ? 0.1153 0.1321 0.1238 -0.0030 -0.0153 -0.0277 392 VAL A O 2376 C CB . VAL A 304 ? 0.1174 0.1099 0.1212 -0.0077 -0.0144 -0.0083 392 VAL A CB 2377 C CG1 . VAL A 304 ? 0.1398 0.1130 0.1241 -0.0040 -0.0094 0.0016 392 VAL A CG1 2378 C CG2 . VAL A 304 ? 0.1197 0.1409 0.1410 -0.0050 -0.0137 -0.0011 392 VAL A CG2 2379 N N . ASP A 305 ? 0.0919 0.1072 0.1085 -0.0030 -0.0058 -0.0147 393 ASP A N 2380 C CA . ASP A 305 ? 0.1058 0.1002 0.1212 0.0071 -0.0142 -0.0082 393 ASP A CA 2381 C C . ASP A 305 ? 0.1122 0.1194 0.1214 0.0014 -0.0077 -0.0149 393 ASP A C 2382 O O . ASP A 305 ? 0.1293 0.1020 0.1187 0.0154 -0.0072 -0.0271 393 ASP A O 2383 C CB . ASP A 305 ? 0.1118 0.1124 0.1091 -0.0035 -0.0159 -0.0099 393 ASP A CB 2384 C CG . ASP A 305 ? 0.1073 0.0947 0.1222 0.0131 -0.0010 -0.0217 393 ASP A CG 2385 O OD1 . ASP A 305 ? 0.1283 0.1042 0.1325 -0.0066 -0.0003 -0.0137 393 ASP A OD1 2386 O OD2 . ASP A 305 ? 0.1275 0.1158 0.1089 0.0056 -0.0117 -0.0049 393 ASP A OD2 2387 N N . ALA A 306 ? 0.1100 0.1029 0.1089 -0.0043 -0.0133 -0.0082 394 ALA A N 2388 C CA . ALA A 306 ? 0.1089 0.1120 0.0993 0.0047 -0.0154 -0.0151 394 ALA A CA 2389 C C . ALA A 306 ? 0.1075 0.0967 0.0832 0.0033 -0.0089 -0.0108 394 ALA A C 2390 O O . ALA A 306 ? 0.1220 0.1097 0.1024 0.0142 -0.0012 -0.0207 394 ALA A O 2391 C CB . ALA A 306 ? 0.1071 0.1233 0.0901 0.0058 -0.0153 0.0026 394 ALA A CB 2392 N N . PHE A 307 ? 0.0996 0.1162 0.0776 0.0055 -0.0112 -0.0070 395 PHE A N 2393 C CA . PHE A 307 ? 0.1103 0.1220 0.0771 0.0029 -0.0089 -0.0130 395 PHE A CA 2394 C C . PHE A 307 ? 0.1144 0.1199 0.0869 0.0083 -0.0090 -0.0059 395 PHE A C 2395 O O . PHE A 307 ? 0.1202 0.1533 0.1163 0.0116 0.0047 -0.0215 395 PHE A O 2396 C CB . PHE A 307 ? 0.1159 0.1299 0.0796 0.0161 -0.0055 -0.0115 395 PHE A CB 2397 C CG . PHE A 307 ? 0.1265 0.1510 0.0897 0.0028 -0.0248 -0.0182 395 PHE A CG 2398 C CD1 . PHE A 307 ? 0.1419 0.1952 0.1298 0.0104 -0.0108 -0.0067 395 PHE A CD1 2399 C CD2 . PHE A 307 ? 0.1646 0.1558 0.1863 0.0084 -0.0154 -0.0263 395 PHE A CD2 2400 C CE1 . PHE A 307 ? 0.1716 0.2369 0.1560 -0.0012 -0.0065 -0.0031 395 PHE A CE1 2401 C CE2 . PHE A 307 ? 0.1663 0.1870 0.1765 0.0017 -0.0276 -0.0148 395 PHE A CE2 2402 C CZ . PHE A 307 ? 0.1588 0.1983 0.2149 -0.0099 0.0004 0.0027 395 PHE A CZ 2403 N N . VAL A 308 ? 0.0994 0.1148 0.0792 0.0096 -0.0089 -0.0059 396 VAL A N 2404 C CA . VAL A 308 ? 0.0990 0.1096 0.0707 0.0015 -0.0044 0.0000 396 VAL A CA 2405 C C . VAL A 308 ? 0.1093 0.1112 0.0724 0.0058 -0.0006 -0.0022 396 VAL A C 2406 O O . VAL A 308 ? 0.1033 0.1251 0.0846 0.0049 -0.0072 -0.0022 396 VAL A O 2407 C CB . VAL A 308 ? 0.1025 0.1190 0.0858 0.0071 -0.0178 0.0085 396 VAL A CB 2408 C CG1 . VAL A 308 ? 0.1335 0.1317 0.1215 0.0104 -0.0194 0.0039 396 VAL A CG1 2409 C CG2 . VAL A 308 ? 0.1182 0.1191 0.0790 0.0058 -0.0132 0.0055 396 VAL A CG2 2410 N N . TRP A 309 ? 0.1106 0.1256 0.0825 0.0067 0.0000 -0.0091 397 TRP A N 2411 C CA . TRP A 309 ? 0.0988 0.1262 0.0977 0.0036 -0.0041 0.0015 397 TRP A CA 2412 C C . TRP A 309 ? 0.1023 0.1386 0.0984 0.0095 -0.0056 -0.0066 397 TRP A C 2413 O O . TRP A 309 ? 0.0980 0.1596 0.0877 0.0082 -0.0048 -0.0019 397 TRP A O 2414 C CB . TRP A 309 ? 0.1143 0.1355 0.0984 0.0076 -0.0083 -0.0049 397 TRP A CB 2415 C CG . TRP A 309 ? 0.1252 0.1506 0.0921 0.0051 -0.0124 0.0068 397 TRP A CG 2416 C CD1 . TRP A 309 ? 0.1221 0.1370 0.0685 0.0087 -0.0048 -0.0012 397 TRP A CD1 2417 C CD2 . TRP A 309 ? 0.1284 0.1711 0.1269 -0.0017 0.0114 0.0071 397 TRP A CD2 2418 N NE1 . TRP A 309 ? 0.1281 0.1628 0.0978 0.0102 -0.0277 -0.0036 397 TRP A NE1 2419 C CE2 . TRP A 309 ? 0.1402 0.1631 0.0897 0.0046 -0.0117 0.0122 397 TRP A CE2 2420 C CE3 . TRP A 309 ? 0.1386 0.1892 0.1134 -0.0094 -0.0072 0.0073 397 TRP A CE3 2421 C CZ2 . TRP A 309 ? 0.1512 0.1871 0.0927 0.0161 -0.0153 0.0135 397 TRP A CZ2 2422 C CZ3 . TRP A 309 ? 0.1577 0.1912 0.1244 -0.0007 0.0258 0.0191 397 TRP A CZ3 2423 C CH2 . TRP A 309 ? 0.1798 0.1946 0.1336 0.0083 0.0027 0.0108 397 TRP A CH2 2424 N N . VAL A 310 ? 0.0953 0.1241 0.0816 0.0138 -0.0125 -0.0095 398 VAL A N 2425 C CA . VAL A 310 ? 0.1054 0.1270 0.0778 0.0037 -0.0052 -0.0047 398 VAL A CA 2426 C C . VAL A 310 ? 0.1111 0.1199 0.0838 0.0100 -0.0019 0.0041 398 VAL A C 2427 O O . VAL A 310 ? 0.1242 0.1431 0.1101 0.0069 -0.0124 0.0183 398 VAL A O 2428 C CB . VAL A 310 ? 0.1020 0.1114 0.0841 0.0159 -0.0024 -0.0075 398 VAL A CB 2429 C CG1 . VAL A 310 ? 0.1151 0.1132 0.1102 0.0052 -0.0090 0.0062 398 VAL A CG1 2430 C CG2 . VAL A 310 ? 0.1141 0.1324 0.1148 0.0032 -0.0061 0.0050 398 VAL A CG2 2431 N N . LYS A 311 ? 0.1276 0.1142 0.1079 0.0035 -0.0124 0.0095 399 LYS A N 2432 C CA . LYS A 311 ? 0.1260 0.1256 0.1253 0.0000 -0.0092 0.0033 399 LYS A CA 2433 C C . LYS A 311 ? 0.1413 0.1629 0.1328 -0.0063 -0.0120 0.0131 399 LYS A C 2434 O O . LYS A 311 ? 0.1471 0.1877 0.1297 -0.0075 -0.0139 0.0120 399 LYS A O 2435 C CB . LYS A 311 ? 0.1364 0.1425 0.1404 0.0022 -0.0076 0.0029 399 LYS A CB 2436 C CG . LYS A 311 ? 0.1559 0.1351 0.1322 -0.0032 -0.0117 0.0255 399 LYS A CG 2437 C CD . LYS A 311 ? 0.1636 0.1516 0.1454 -0.0121 0.0021 0.0228 399 LYS A CD 2438 C CE . LYS A 311 ? 0.1839 0.1670 0.1374 -0.0115 0.0081 0.0266 399 LYS A CE 2439 N NZ . LYS A 311 ? 0.1697 0.1771 0.1506 -0.0057 0.0042 0.0415 399 LYS A NZ 2440 N N . PRO A 312 ? 0.1303 0.1730 0.1267 -0.0109 -0.0111 0.0151 400 PRO A N 2441 C CA . PRO A 312 ? 0.1634 0.1860 0.1494 0.0005 -0.0074 0.0151 400 PRO A CA 2442 C C . PRO A 312 ? 0.1742 0.1825 0.1496 -0.0022 -0.0122 0.0116 400 PRO A C 2443 O O . PRO A 312 ? 0.1977 0.1944 0.1468 0.0039 -0.0263 0.0364 400 PRO A O 2444 C CB . PRO A 312 ? 0.1626 0.2007 0.1554 -0.0007 0.0022 0.0207 400 PRO A CB 2445 C CG . PRO A 312 ? 0.1840 0.2300 0.1725 0.0010 -0.0036 0.0098 400 PRO A CG 2446 C CD . PRO A 312 ? 0.1475 0.1795 0.1290 -0.0026 -0.0158 0.0203 400 PRO A CD 2447 N N . GLY A 313 ? 0.1802 0.1962 0.1608 -0.0055 -0.0139 0.0182 401 GLY A N 2448 C CA . GLY A 313 ? 0.1791 0.2095 0.1764 0.0050 -0.0073 0.0189 401 GLY A CA 2449 C C . GLY A 313 ? 0.1601 0.1975 0.1540 0.0020 -0.0164 0.0063 401 GLY A C 2450 O O . GLY A 313 ? 0.1792 0.2226 0.1719 0.0146 -0.0222 0.0168 401 GLY A O 2451 N N . GLY A 314 ? 0.1562 0.2042 0.1651 -0.0022 -0.0162 0.0256 402 GLY A N 2452 C CA . GLY A 314 ? 0.1835 0.2016 0.1868 -0.0070 -0.0049 0.0215 402 GLY A CA 2453 C C . GLY A 314 ? 0.1912 0.2164 0.1938 -0.0064 -0.0080 0.0245 402 GLY A C 2454 O O . GLY A 314 ? 0.1970 0.2252 0.1989 -0.0101 -0.0204 0.0456 402 GLY A O 2455 N N . GLU A 315 ? 0.1824 0.2077 0.1648 -0.0013 -0.0074 0.0275 403 GLU A N 2456 C CA . GLU A 315 ? 0.1844 0.1898 0.1749 -0.0006 -0.0114 0.0253 403 GLU A CA 2457 C C . GLU A 315 ? 0.1825 0.2012 0.1677 -0.0035 -0.0107 0.0237 403 GLU A C 2458 O O . GLU A 315 ? 0.1759 0.2042 0.1554 -0.0183 -0.0100 0.0652 403 GLU A O 2459 C CB . GLU A 315 ? 0.1763 0.1886 0.1640 -0.0017 -0.0177 0.0258 403 GLU A CB 2460 C CG . GLU A 315 ? 0.2009 0.2276 0.2020 0.0054 -0.0060 0.0177 403 GLU A CG 2461 C CD . GLU A 315 ? 0.2337 0.2785 0.2172 0.0255 -0.0111 0.0128 403 GLU A CD 2462 O OE1 . GLU A 315 ? 0.2320 0.2880 0.2116 0.0118 0.0133 0.0423 403 GLU A OE1 2463 O OE2 . GLU A 315 ? 0.2514 0.2661 0.2182 0.0121 -0.0003 0.0209 403 GLU A OE2 2464 N N . CYS A 316 ? 0.1808 0.1956 0.1519 -0.0088 0.0053 0.0397 404 CYS A N 2465 C CA . CYS A 316 ? 0.1801 0.1741 0.1552 -0.0104 -0.0052 0.0381 404 CYS A CA 2466 C C . CYS A 316 ? 0.1766 0.1809 0.1534 -0.0050 -0.0018 0.0358 404 CYS A C 2467 O O . CYS A 316 ? 0.1763 0.1835 0.1754 -0.0031 -0.0192 0.0701 404 CYS A O 2468 C CB . CYS A 316 ? 0.2082 0.1898 0.1700 -0.0177 0.0036 0.0454 404 CYS A CB 2469 S SG . CYS A 316 ? 0.2286 0.2133 0.1949 -0.0299 0.0070 0.0935 404 CYS A SG 2470 N N . ASP A 317 ? 0.1598 0.1438 0.1246 -0.0156 -0.0036 0.0459 405 ASP A N 2471 C CA . ASP A 317 ? 0.1584 0.1704 0.1410 -0.0085 0.0015 0.0327 405 ASP A CA 2472 C C . ASP A 317 ? 0.1814 0.1877 0.1654 -0.0138 -0.0034 0.0242 405 ASP A C 2473 O O . ASP A 317 ? 0.2025 0.2030 0.1575 -0.0306 -0.0070 0.0326 405 ASP A O 2474 C CB . ASP A 317 ? 0.1561 0.1667 0.1438 -0.0019 -0.0050 0.0360 405 ASP A CB 2475 C CG . ASP A 317 ? 0.1742 0.1936 0.1675 -0.0072 0.0076 0.0200 405 ASP A CG 2476 O OD1 . ASP A 317 ? 0.1771 0.2108 0.1959 -0.0067 -0.0205 0.0429 405 ASP A OD1 2477 O OD2 . ASP A 317 ? 0.1874 0.1901 0.1856 -0.0125 -0.0167 0.0469 405 ASP A OD2 2478 N N . GLY A 318 ? 0.1878 0.1774 0.1731 -0.0117 -0.0081 0.0297 406 GLY A N 2479 C CA . GLY A 318 ? 0.1987 0.1948 0.1592 -0.0117 -0.0144 0.0242 406 GLY A CA 2480 C C . GLY A 318 ? 0.2187 0.1996 0.1863 -0.0195 -0.0189 0.0224 406 GLY A C 2481 O O . GLY A 318 ? 0.2070 0.1953 0.1744 -0.0391 -0.0331 0.0456 406 GLY A O 2482 N N . THR A 319 ? 0.2257 0.1988 0.1850 -0.0231 -0.0160 0.0392 407 THR A N 2483 C CA . THR A 319 ? 0.2362 0.2064 0.2154 -0.0197 -0.0081 0.0305 407 THR A CA 2484 C C . THR A 319 ? 0.2343 0.2117 0.2297 -0.0202 -0.0108 0.0188 407 THR A C 2485 O O . THR A 319 ? 0.2308 0.1741 0.2221 -0.0226 -0.0197 0.0378 407 THR A O 2486 C CB . THR A 319 ? 0.2379 0.2004 0.2187 -0.0224 -0.0047 0.0345 407 THR A CB 2487 O OG1 . THR A 319 ? 0.2759 0.2287 0.2333 -0.0409 -0.0123 0.0616 407 THR A OG1 2488 C CG2 . THR A 319 ? 0.2435 0.1976 0.2440 -0.0248 0.0036 0.0272 407 THR A CG2 2489 N N . SER A 320 ? 0.2555 0.2384 0.2387 -0.0202 -0.0094 0.0265 408 SER A N 2490 C CA . SER A 320 ? 0.2777 0.2610 0.2718 -0.0104 -0.0095 0.0098 408 SER A CA 2491 C C . SER A 320 ? 0.2907 0.2666 0.2896 -0.0140 -0.0081 0.0137 408 SER A C 2492 O O . SER A 320 ? 0.3080 0.2761 0.3178 -0.0197 -0.0144 0.0135 408 SER A O 2493 C CB . SER A 320 ? 0.2765 0.2653 0.2680 -0.0097 -0.0126 0.0024 408 SER A CB 2494 O OG . SER A 320 ? 0.2871 0.2649 0.2644 -0.0082 -0.0206 0.0358 408 SER A OG 2495 N N . ASP A 321 ? 0.3091 0.2802 0.2968 -0.0114 -0.0094 0.0185 409 ASP A N 2496 C CA . ASP A 321 ? 0.3197 0.2917 0.3041 -0.0101 -0.0065 0.0087 409 ASP A CA 2497 C C . ASP A 321 ? 0.3227 0.3054 0.3092 -0.0170 -0.0071 0.0060 409 ASP A C 2498 O O . ASP A 321 ? 0.3250 0.2920 0.2940 -0.0384 -0.0134 0.0179 409 ASP A O 2499 C CB . ASP A 321 ? 0.3306 0.2985 0.3087 -0.0133 -0.0007 0.0123 409 ASP A CB 2500 C CG . ASP A 321 ? 0.3552 0.3327 0.3406 -0.0143 -0.0006 0.0087 409 ASP A CG 2501 O OD1 . ASP A 321 ? 0.3888 0.2889 0.3421 -0.0339 0.0106 0.0137 409 ASP A OD1 2502 O OD2 . ASP A 321 ? 0.3787 0.4053 0.3955 -0.0267 -0.0115 0.0085 409 ASP A OD2 2503 N N . THR A 322 ? 0.3369 0.3211 0.3293 -0.0145 -0.0069 0.0048 410 THR A N 2504 C CA . THR A 322 ? 0.3568 0.3427 0.3474 -0.0121 -0.0002 0.0010 410 THR A CA 2505 C C . THR A 322 ? 0.3633 0.3518 0.3541 -0.0105 -0.0011 0.0003 410 THR A C 2506 O O . THR A 322 ? 0.3945 0.3570 0.3640 -0.0160 -0.0030 0.0020 410 THR A O 2507 C CB . THR A 322 ? 0.3627 0.3506 0.3529 -0.0099 -0.0016 0.0053 410 THR A CB 2508 O OG1 . THR A 322 ? 0.4069 0.3617 0.3965 -0.0188 -0.0071 0.0071 410 THR A OG1 2509 C CG2 . THR A 322 ? 0.3773 0.3601 0.3638 -0.0094 -0.0033 0.0022 410 THR A CG2 2510 N N . THR A 323 ? 0.3657 0.3520 0.3526 -0.0115 -0.0040 0.0018 411 THR A N 2511 C CA . THR A 323 ? 0.3601 0.3497 0.3523 -0.0104 -0.0026 0.0032 411 THR A CA 2512 C C . THR A 323 ? 0.3541 0.3390 0.3348 -0.0110 -0.0023 0.0003 411 THR A C 2513 O O . THR A 323 ? 0.3706 0.3425 0.3397 -0.0289 -0.0069 0.0030 411 THR A O 2514 C CB . THR A 323 ? 0.3609 0.3413 0.3508 -0.0141 -0.0037 0.0030 411 THR A CB 2515 O OG1 . THR A 323 ? 0.3817 0.3733 0.3817 -0.0190 0.0016 0.0068 411 THR A OG1 2516 C CG2 . THR A 323 ? 0.3619 0.3662 0.3646 -0.0089 -0.0047 -0.0022 411 THR A CG2 2517 N N . ALA A 324 ? 0.3330 0.3139 0.3138 -0.0152 -0.0012 0.0073 412 ALA A N 2518 C CA . ALA A 324 ? 0.3132 0.3093 0.3034 -0.0100 0.0015 0.0011 412 ALA A CA 2519 C C . ALA A 324 ? 0.3023 0.3037 0.2854 -0.0078 -0.0038 0.0008 412 ALA A C 2520 O O . ALA A 324 ? 0.3055 0.2913 0.2714 -0.0271 -0.0070 0.0122 412 ALA A O 2521 C CB . ALA A 324 ? 0.3250 0.3151 0.3072 -0.0057 -0.0015 0.0026 412 ALA A CB 2522 N N . ALA A 325 ? 0.2934 0.2922 0.2878 -0.0140 -0.0017 0.0066 413 ALA A N 2523 C CA . ALA A 325 ? 0.2772 0.2772 0.2769 -0.0089 0.0001 -0.0008 413 ALA A CA 2524 C C . ALA A 325 ? 0.2816 0.2829 0.2832 -0.0091 0.0011 0.0015 413 ALA A C 2525 O O . ALA A 325 ? 0.2949 0.2933 0.2788 -0.0192 0.0004 0.0015 413 ALA A O 2526 C CB . ALA A 325 ? 0.2824 0.2849 0.2734 -0.0072 -0.0024 0.0037 413 ALA A CB 2527 N N . ARG A 326 ? 0.2800 0.2705 0.2758 -0.0166 -0.0007 0.0020 414 ARG A N 2528 C CA . ARG A 326 ? 0.2774 0.2765 0.2768 -0.0156 -0.0079 0.0077 414 ARG A CA 2529 C C . ARG A 326 ? 0.2648 0.2562 0.2628 -0.0158 -0.0099 0.0072 414 ARG A C 2530 O O . ARG A 326 ? 0.2674 0.2562 0.2707 -0.0331 -0.0238 0.0252 414 ARG A O 2531 C CB . ARG A 326 ? 0.2916 0.2900 0.2866 -0.0127 -0.0051 0.0052 414 ARG A CB 2532 C CG . ARG A 326 ? 0.2940 0.3119 0.3059 -0.0024 -0.0035 0.0021 414 ARG A CG 2533 C CD . ARG A 326 ? 0.2975 0.2975 0.3008 0.0044 -0.0034 -0.0017 414 ARG A CD 2534 N NE . ARG A 326 ? 0.2881 0.2922 0.3026 -0.0050 0.0023 0.0017 414 ARG A NE 2535 C CZ . ARG A 326 ? 0.2791 0.2907 0.2999 0.0003 -0.0020 0.0027 414 ARG A CZ 2536 N NH1 . ARG A 326 ? 0.2777 0.3091 0.2979 -0.0013 0.0052 0.0021 414 ARG A NH1 2537 N NH2 . ARG A 326 ? 0.2915 0.3181 0.3056 0.0023 -0.0041 -0.0002 414 ARG A NH2 2538 N N . TYR A 327 ? 0.2503 0.2531 0.2513 -0.0203 -0.0138 0.0037 415 TYR A N 2539 C CA . TYR A 327 ? 0.2403 0.2336 0.2416 -0.0126 -0.0081 0.0087 415 TYR A CA 2540 C C . TYR A 327 ? 0.2346 0.2217 0.2325 -0.0138 -0.0071 0.0034 415 TYR A C 2541 O O . TYR A 327 ? 0.2516 0.2019 0.2468 -0.0363 -0.0035 0.0008 415 TYR A O 2542 C CB . TYR A 327 ? 0.2391 0.2279 0.2392 -0.0175 -0.0046 0.0124 415 TYR A CB 2543 C CG . TYR A 327 ? 0.2514 0.2310 0.2683 -0.0129 -0.0055 0.0183 415 TYR A CG 2544 C CD1 . TYR A 327 ? 0.2840 0.2723 0.2794 -0.0172 -0.0093 0.0210 415 TYR A CD1 2545 C CD2 . TYR A 327 ? 0.2698 0.2430 0.2663 -0.0075 -0.0012 0.0135 415 TYR A CD2 2546 C CE1 . TYR A 327 ? 0.2743 0.2500 0.2796 -0.0192 -0.0107 0.0240 415 TYR A CE1 2547 C CE2 . TYR A 327 ? 0.2760 0.2362 0.2879 -0.0106 -0.0094 0.0063 415 TYR A CE2 2548 C CZ . TYR A 327 ? 0.2760 0.2347 0.2693 -0.0257 0.0021 0.0281 415 TYR A CZ 2549 O OH . TYR A 327 ? 0.3277 0.2881 0.3326 -0.0157 -0.0310 0.0230 415 TYR A OH 2550 N N . ALA A 328 ? 0.2264 0.1946 0.2196 -0.0157 -0.0064 0.0131 416 ALA A N 2551 C CA . ALA A 328 ? 0.2156 0.2057 0.2205 -0.0072 -0.0059 0.0116 416 ALA A CA 2552 C C . ALA A 328 ? 0.2134 0.1981 0.2192 -0.0158 -0.0077 0.0108 416 ALA A C 2553 O O . ALA A 328 ? 0.2287 0.1966 0.2273 -0.0268 -0.0056 0.0239 416 ALA A O 2554 C CB . ALA A 328 ? 0.2181 0.1998 0.2159 -0.0007 -0.0095 0.0127 416 ALA A CB 2555 N N . TYR A 329 ? 0.2278 0.2009 0.2253 -0.0110 -0.0129 0.0119 417 TYR A N 2556 C CA . TYR A 329 ? 0.2178 0.2035 0.2233 -0.0040 -0.0132 0.0110 417 TYR A CA 2557 C C . TYR A 329 ? 0.2251 0.1871 0.2270 -0.0084 -0.0131 0.0086 417 TYR A C 2558 O O . TYR A 329 ? 0.2233 0.1742 0.2407 -0.0169 -0.0257 0.0188 417 TYR A O 2559 C CB . TYR A 329 ? 0.2418 0.2147 0.2314 0.0000 -0.0152 0.0005 417 TYR A CB 2560 C CG . TYR A 329 ? 0.2552 0.2332 0.2442 0.0136 -0.0006 0.0007 417 TYR A CG 2561 C CD1 . TYR A 329 ? 0.2723 0.2669 0.2861 0.0064 -0.0059 -0.0120 417 TYR A CD1 2562 C CD2 . TYR A 329 ? 0.2858 0.2687 0.2578 0.0079 -0.0071 0.0066 417 TYR A CD2 2563 C CE1 . TYR A 329 ? 0.2870 0.2896 0.3035 0.0022 0.0026 -0.0054 417 TYR A CE1 2564 C CE2 . TYR A 329 ? 0.2974 0.2820 0.2913 0.0017 0.0003 0.0029 417 TYR A CE2 2565 C CZ . TYR A 329 ? 0.3139 0.3061 0.3165 0.0003 -0.0065 -0.0003 417 TYR A CZ 2566 O OH . TYR A 329 ? 0.3533 0.3407 0.3607 0.0098 0.0238 0.0031 417 TYR A OH 2567 N N . HIS A 330 ? 0.2034 0.1786 0.2048 -0.0027 -0.0174 0.0161 418 HIS A N 2568 C CA . HIS A 330 ? 0.1984 0.1663 0.1936 -0.0043 -0.0073 0.0081 418 HIS A CA 2569 C C . HIS A 330 ? 0.1903 0.1667 0.1919 -0.0085 -0.0082 0.0135 418 HIS A C 2570 O O . HIS A 330 ? 0.2042 0.1739 0.1887 -0.0336 -0.0086 0.0202 418 HIS A O 2571 C CB . HIS A 330 ? 0.2072 0.1718 0.1962 0.0012 -0.0042 0.0123 418 HIS A CB 2572 C CG . HIS A 330 ? 0.1991 0.1769 0.2149 0.0008 -0.0063 0.0117 418 HIS A CG 2573 N ND1 . HIS A 330 ? 0.2277 0.1963 0.2271 -0.0077 0.0122 0.0101 418 HIS A ND1 2574 C CD2 . HIS A 330 ? 0.1832 0.1894 0.2128 0.0009 0.0034 0.0148 418 HIS A CD2 2575 C CE1 . HIS A 330 ? 0.2363 0.2336 0.2289 -0.0020 0.0091 -0.0028 418 HIS A CE1 2576 N NE2 . HIS A 330 ? 0.2397 0.2121 0.2245 -0.0056 0.0047 0.0179 418 HIS A NE2 2577 N N . CYS A 331 ? 0.1883 0.1713 0.1935 -0.0061 -0.0189 0.0056 419 CYS A N 2578 C CA . CYS A 331 ? 0.1949 0.1726 0.1997 -0.0070 -0.0152 0.0230 419 CYS A CA 2579 C C . CYS A 331 ? 0.2107 0.1749 0.2027 -0.0065 -0.0077 0.0157 419 CYS A C 2580 O O . CYS A 331 ? 0.2253 0.1772 0.2190 -0.0119 -0.0032 0.0283 419 CYS A O 2581 C CB . CYS A 331 ? 0.1877 0.1795 0.2099 -0.0039 -0.0012 0.0257 419 CYS A CB 2582 S SG . CYS A 331 ? 0.2224 0.1943 0.2219 -0.0282 -0.0336 0.0501 419 CYS A SG 2583 N N . GLY A 332 ? 0.2140 0.1781 0.2036 -0.0033 -0.0038 0.0230 420 GLY A N 2584 C CA . GLY A 332 ? 0.2246 0.1920 0.2241 -0.0033 -0.0036 0.0292 420 GLY A CA 2585 C C . GLY A 332 ? 0.2322 0.2078 0.2357 -0.0039 -0.0070 0.0240 420 GLY A C 2586 O O . GLY A 332 ? 0.2675 0.2113 0.2674 0.0058 -0.0161 0.0437 420 GLY A O 2587 N N . LEU A 333 ? 0.2365 0.2129 0.2473 -0.0086 -0.0097 0.0253 421 LEU A N 2588 C CA . LEU A 333 ? 0.2245 0.2000 0.2412 -0.0022 -0.0010 0.0201 421 LEU A CA 2589 C C . LEU A 333 ? 0.2439 0.2239 0.2555 -0.0011 0.0033 0.0205 421 LEU A C 2590 O O . LEU A 333 ? 0.2345 0.2124 0.2499 0.0048 -0.0033 0.0437 421 LEU A O 2591 C CB . LEU A 333 ? 0.2283 0.2114 0.2405 -0.0056 0.0010 0.0220 421 LEU A CB 2592 C CG . LEU A 333 ? 0.2461 0.2386 0.2527 -0.0100 -0.0064 0.0116 421 LEU A CG 2593 C CD1 . LEU A 333 ? 0.2622 0.2490 0.2769 -0.0038 -0.0053 0.0178 421 LEU A CD1 2594 C CD2 . LEU A 333 ? 0.2666 0.2455 0.2652 -0.0101 0.0011 0.0087 421 LEU A CD2 2595 N N . GLU A 334 ? 0.2520 0.2459 0.2609 0.0033 -0.0054 0.0181 422 GLU A N 2596 C CA . GLU A 334 ? 0.2754 0.2741 0.2744 0.0019 -0.0039 0.0095 422 GLU A CA 2597 C C . GLU A 334 ? 0.2718 0.2670 0.2719 0.0040 -0.0039 0.0133 422 GLU A C 2598 O O . GLU A 334 ? 0.2997 0.2843 0.2927 0.0101 0.0024 0.0190 422 GLU A O 2599 C CB . GLU A 334 ? 0.2836 0.2897 0.2998 0.0065 0.0005 0.0042 422 GLU A CB 2600 C CG . GLU A 334 ? 0.3157 0.3258 0.3108 -0.0024 0.0023 0.0055 422 GLU A CG 2601 C CD . GLU A 334 ? 0.3250 0.3388 0.3283 0.0040 0.0024 -0.0021 422 GLU A CD 2602 O OE1 . GLU A 334 ? 0.3161 0.3233 0.3107 -0.0003 0.0010 0.0053 422 GLU A OE1 2603 O OE2 . GLU A 334 ? 0.3627 0.3637 0.3346 0.0005 -0.0024 0.0029 422 GLU A OE2 2604 N N . ASP A 335 ? 0.2530 0.2546 0.2470 -0.0037 -0.0029 0.0153 423 ASP A N 2605 C CA . ASP A 335 ? 0.2402 0.2514 0.2511 -0.0036 -0.0016 0.0121 423 ASP A CA 2606 C C . ASP A 335 ? 0.2290 0.2128 0.2267 -0.0073 -0.0087 0.0153 423 ASP A C 2607 O O . ASP A 335 ? 0.2275 0.2012 0.2453 -0.0133 -0.0097 0.0236 423 ASP A O 2608 C CB . ASP A 335 ? 0.2522 0.2621 0.2634 -0.0061 -0.0019 0.0109 423 ASP A CB 2609 C CG . ASP A 335 ? 0.2726 0.2929 0.2712 -0.0126 0.0116 0.0109 423 ASP A CG 2610 O OD1 . ASP A 335 ? 0.3115 0.3504 0.3240 -0.0201 -0.0067 0.0073 423 ASP A OD1 2611 O OD2 . ASP A 335 ? 0.2595 0.2539 0.2993 -0.0186 0.0064 0.0429 423 ASP A OD2 2612 N N . ALA A 336 ? 0.2160 0.1961 0.2081 -0.0078 -0.0105 0.0308 424 ALA A N 2613 C CA . ALA A 336 ? 0.2101 0.1947 0.1983 -0.0048 0.0000 0.0164 424 ALA A CA 2614 C C . ALA A 336 ? 0.1997 0.1812 0.1979 -0.0071 -0.0073 0.0221 424 ALA A C 2615 O O . ALA A 336 ? 0.2578 0.1829 0.2256 0.0041 -0.0001 0.0450 424 ALA A O 2616 C CB . ALA A 336 ? 0.2141 0.1831 0.1982 0.0030 -0.0055 0.0229 424 ALA A CB 2617 N N . LEU A 337 ? 0.2013 0.1887 0.1676 -0.0053 -0.0086 0.0238 425 LEU A N 2618 C CA . LEU A 337 ? 0.1998 0.1978 0.1683 -0.0047 -0.0067 0.0248 425 LEU A CA 2619 C C . LEU A 337 ? 0.2216 0.2179 0.1980 -0.0107 -0.0147 0.0238 425 LEU A C 2620 O O . LEU A 337 ? 0.2109 0.2276 0.1831 -0.0219 -0.0152 0.0494 425 LEU A O 2621 C CB . LEU A 337 ? 0.1951 0.1930 0.1718 0.0027 -0.0078 0.0317 425 LEU A CB 2622 C CG . LEU A 337 ? 0.1827 0.1865 0.1673 -0.0125 -0.0096 0.0262 425 LEU A CG 2623 C CD1 . LEU A 337 ? 0.2090 0.2206 0.2074 0.0061 -0.0201 0.0184 425 LEU A CD1 2624 C CD2 . LEU A 337 ? 0.1827 0.1992 0.1560 0.0075 -0.0131 0.0410 425 LEU A CD2 2625 N N . LYS A 338 ? 0.2667 0.2384 0.2378 -0.0123 -0.0190 0.0296 426 LYS A N 2626 C CA . LYS A 338 ? 0.2874 0.2820 0.2686 -0.0141 -0.0119 0.0150 426 LYS A CA 2627 C C . LYS A 338 ? 0.3030 0.3012 0.2825 -0.0164 -0.0072 0.0179 426 LYS A C 2628 O O . LYS A 338 ? 0.3181 0.3103 0.2834 -0.0201 -0.0170 0.0322 426 LYS A O 2629 C CB . LYS A 338 ? 0.3049 0.2881 0.2956 -0.0171 -0.0061 0.0085 426 LYS A CB 2630 C CG . LYS A 338 ? 0.3454 0.3449 0.3230 -0.0062 -0.0019 0.0013 426 LYS A CG 2631 C CD . LYS A 338 ? 0.3351 0.3445 0.3234 -0.0116 -0.0077 0.0042 426 LYS A CD 2632 C CE . LYS A 338 ? 0.3655 0.3576 0.3578 0.0040 0.0067 -0.0020 426 LYS A CE 2633 N NZ . LYS A 338 ? 0.3783 0.4001 0.3843 -0.0034 -0.0022 -0.0023 426 LYS A NZ 2634 N N . PRO A 339 ? 0.3076 0.3093 0.2812 -0.0149 -0.0091 0.0231 427 PRO A N 2635 C CA . PRO A 339 ? 0.3029 0.3026 0.2889 -0.0133 -0.0058 0.0117 427 PRO A CA 2636 C C . PRO A 339 ? 0.2967 0.2925 0.2656 -0.0118 -0.0020 0.0109 427 PRO A C 2637 O O . PRO A 339 ? 0.3447 0.3121 0.2640 -0.0125 -0.0006 0.0183 427 PRO A O 2638 C CB . PRO A 339 ? 0.3079 0.2979 0.2963 -0.0122 -0.0052 0.0126 427 PRO A CB 2639 C CG . PRO A 339 ? 0.3232 0.3235 0.3043 -0.0105 -0.0070 0.0191 427 PRO A CG 2640 C CD . PRO A 339 ? 0.3135 0.3140 0.2963 -0.0173 0.0019 0.0199 427 PRO A CD 2641 N N . ALA A 340 ? 0.2661 0.2677 0.2408 -0.0159 -0.0074 0.0197 428 ALA A N 2642 C CA . ALA A 340 ? 0.2386 0.2436 0.2306 -0.0145 -0.0074 0.0122 428 ALA A CA 2643 C C . ALA A 340 ? 0.2346 0.2376 0.2087 -0.0186 0.0009 0.0311 428 ALA A C 2644 O O . ALA A 340 ? 0.2386 0.2306 0.1921 -0.0252 -0.0124 0.0591 428 ALA A O 2645 C CB . ALA A 340 ? 0.2281 0.2410 0.2332 -0.0140 -0.0109 0.0172 428 ALA A CB 2646 N N . PRO A 341 ? 0.2336 0.2378 0.2163 -0.0229 0.0024 0.0353 429 PRO A N 2647 C CA . PRO A 341 ? 0.2503 0.2634 0.2424 -0.0132 -0.0059 0.0249 429 PRO A CA 2648 C C . PRO A 341 ? 0.2596 0.2855 0.2548 -0.0120 -0.0053 0.0233 429 PRO A C 2649 O O . PRO A 341 ? 0.2614 0.2899 0.2538 -0.0240 -0.0124 0.0394 429 PRO A O 2650 C CB . PRO A 341 ? 0.2582 0.2550 0.2391 -0.0141 -0.0064 0.0281 429 PRO A CB 2651 C CG . PRO A 341 ? 0.2454 0.2472 0.2277 -0.0137 0.0018 0.0272 429 PRO A CG 2652 C CD . PRO A 341 ? 0.2431 0.2558 0.2258 -0.0102 0.0080 0.0304 429 PRO A CD 2653 N N . GLU A 342 ? 0.2643 0.2809 0.2586 -0.0165 -0.0084 0.0254 430 GLU A N 2654 C CA . GLU A 342 ? 0.2622 0.2672 0.2519 -0.0077 -0.0041 0.0142 430 GLU A CA 2655 C C . GLU A 342 ? 0.2373 0.2472 0.2253 -0.0064 -0.0048 0.0145 430 GLU A C 2656 O O . GLU A 342 ? 0.2238 0.2196 0.2082 -0.0203 -0.0153 0.0445 430 GLU A O 2657 C CB . GLU A 342 ? 0.2711 0.2834 0.2588 -0.0096 -0.0057 0.0154 430 GLU A CB 2658 C CG . GLU A 342 ? 0.3313 0.3112 0.3402 -0.0106 -0.0073 0.0091 430 GLU A CG 2659 C CD . GLU A 342 ? 0.3879 0.3759 0.3763 -0.0061 0.0025 0.0022 430 GLU A CD 2660 O OE1 . GLU A 342 ? 0.3790 0.3973 0.3789 -0.0176 0.0136 0.0195 430 GLU A OE1 2661 O OE2 . GLU A 342 ? 0.4242 0.3971 0.4146 -0.0033 0.0040 -0.0064 430 GLU A OE2 2662 N N . ALA A 343 ? 0.2262 0.2215 0.2149 -0.0155 -0.0081 0.0236 431 ALA A N 2663 C CA . ALA A 343 ? 0.2155 0.2097 0.1908 -0.0106 -0.0053 0.0149 431 ALA A CA 2664 C C . ALA A 343 ? 0.2077 0.2110 0.1972 -0.0118 -0.0079 0.0292 431 ALA A C 2665 O O . ALA A 343 ? 0.2022 0.2452 0.2049 -0.0157 -0.0195 0.0631 431 ALA A O 2666 C CB . ALA A 343 ? 0.2130 0.2112 0.1934 -0.0067 0.0019 0.0196 431 ALA A CB 2667 N N . GLY A 344 ? 0.2047 0.2145 0.1851 -0.0021 -0.0095 0.0252 432 GLY A N 2668 C CA . GLY A 344 ? 0.2127 0.2141 0.2007 -0.0006 -0.0038 0.0148 432 GLY A CA 2669 C C . GLY A 344 ? 0.2266 0.2289 0.2180 0.0050 0.0000 0.0137 432 GLY A C 2670 O O . GLY A 344 ? 0.2624 0.2439 0.2407 0.0063 0.0079 0.0289 432 GLY A O 2671 N N . GLN A 345 ? 0.2216 0.2338 0.2210 0.0048 -0.0067 0.0176 433 GLN A N 2672 C CA . GLN A 345 ? 0.2373 0.2634 0.2333 -0.0035 -0.0057 0.0114 433 GLN A CA 2673 C C . GLN A 345 ? 0.2132 0.2372 0.2135 0.0022 -0.0087 0.0196 433 GLN A C 2674 O O . GLN A 345 ? 0.2017 0.2408 0.2079 -0.0060 -0.0045 0.0490 433 GLN A O 2675 C CB . GLN A 345 ? 0.2605 0.2739 0.2530 0.0000 -0.0019 0.0133 433 GLN A CB 2676 C CG . GLN A 345 ? 0.3021 0.3222 0.3018 -0.0107 -0.0079 0.0101 433 GLN A CG 2677 C CD . GLN A 345 ? 0.3562 0.3876 0.3859 0.0079 0.0005 0.0039 433 GLN A CD 2678 O OE1 . GLN A 345 ? 0.4008 0.4411 0.4030 -0.0085 0.0076 0.0071 433 GLN A OE1 2679 N NE2 . GLN A 345 ? 0.3905 0.4336 0.3877 0.0009 -0.0060 0.0154 433 GLN A NE2 2680 N N . TRP A 346 ? 0.2117 0.2589 0.2251 -0.0046 -0.0069 0.0224 434 TRP A N 2681 C CA . TRP A 346 ? 0.2193 0.2432 0.2149 -0.0028 -0.0043 0.0242 434 TRP A CA 2682 C C . TRP A 346 ? 0.2224 0.2501 0.2320 -0.0010 -0.0133 0.0266 434 TRP A C 2683 O O . TRP A 346 ? 0.2202 0.2666 0.2233 -0.0020 -0.0312 0.0545 434 TRP A O 2684 C CB . TRP A 346 ? 0.2180 0.2482 0.2187 0.0029 -0.0058 0.0230 434 TRP A CB 2685 C CG . TRP A 346 ? 0.2393 0.2504 0.1968 0.0018 -0.0064 0.0257 434 TRP A CG 2686 C CD1 . TRP A 346 ? 0.2333 0.2636 0.1888 -0.0045 0.0191 0.0423 434 TRP A CD1 2687 C CD2 . TRP A 346 ? 0.2164 0.2674 0.2219 -0.0111 -0.0002 0.0214 434 TRP A CD2 2688 N NE1 . TRP A 346 ? 0.2236 0.2762 0.2293 -0.0021 0.0110 0.0400 434 TRP A NE1 2689 C CE2 . TRP A 346 ? 0.1983 0.2478 0.2043 -0.0037 0.0052 0.0208 434 TRP A CE2 2690 C CE3 . TRP A 346 ? 0.2299 0.2533 0.1953 0.0030 -0.0073 0.0202 434 TRP A CE3 2691 C CZ2 . TRP A 346 ? 0.2209 0.2697 0.2360 0.0027 0.0149 0.0179 434 TRP A CZ2 2692 C CZ3 . TRP A 346 ? 0.2263 0.2760 0.2092 -0.0030 0.0028 0.0070 434 TRP A CZ3 2693 C CH2 . TRP A 346 ? 0.2261 0.2520 0.2196 -0.0010 -0.0046 0.0007 434 TRP A CH2 2694 N N . PHE A 347 ? 0.2228 0.2421 0.2266 -0.0085 -0.0065 0.0416 435 PHE A N 2695 C CA . PHE A 347 ? 0.2104 0.2358 0.2237 -0.0025 -0.0055 0.0260 435 PHE A CA 2696 C C . PHE A 347 ? 0.2167 0.2372 0.2070 -0.0071 -0.0076 0.0387 435 PHE A C 2697 O O . PHE A 347 ? 0.2099 0.2400 0.1683 -0.0068 -0.0177 0.0686 435 PHE A O 2698 C CB . PHE A 347 ? 0.2244 0.2387 0.2074 -0.0041 -0.0019 0.0207 435 PHE A CB 2699 C CG . PHE A 347 ? 0.1958 0.2350 0.2208 -0.0182 -0.0040 0.0326 435 PHE A CG 2700 C CD1 . PHE A 347 ? 0.2144 0.2468 0.2052 -0.0176 0.0037 0.0221 435 PHE A CD1 2701 C CD2 . PHE A 347 ? 0.2303 0.2311 0.1981 0.0020 -0.0013 0.0050 435 PHE A CD2 2702 C CE1 . PHE A 347 ? 0.2457 0.2558 0.2510 -0.0068 -0.0017 0.0249 435 PHE A CE1 2703 C CE2 . PHE A 347 ? 0.2221 0.2461 0.2356 -0.0182 -0.0014 0.0230 435 PHE A CE2 2704 C CZ . PHE A 347 ? 0.2290 0.2409 0.2277 0.0060 -0.0186 0.0284 435 PHE A CZ 2705 N N . ASN A 348 ? 0.2025 0.2354 0.2183 -0.0007 0.0061 0.0328 436 ASN A N 2706 C CA . ASN A 348 ? 0.2071 0.2424 0.2109 -0.0028 0.0060 0.0343 436 ASN A CA 2707 C C . ASN A 348 ? 0.1888 0.2069 0.1698 -0.0090 0.0116 0.0356 436 ASN A C 2708 O O . ASN A 348 ? 0.2024 0.2459 0.1680 -0.0088 0.0127 0.0638 436 ASN A O 2709 C CB . ASN A 348 ? 0.2072 0.2530 0.2235 -0.0048 0.0019 0.0361 436 ASN A CB 2710 C CG . ASN A 348 ? 0.2674 0.2935 0.2442 -0.0054 0.0208 0.0283 436 ASN A CG 2711 O OD1 . ASN A 348 ? 0.3037 0.3278 0.2046 0.0164 0.0247 0.0478 436 ASN A OD1 2712 N ND2 . ASN A 348 ? 0.2900 0.3499 0.2232 -0.0097 0.0015 0.0487 436 ASN A ND2 2713 N N . GLU A 349 ? 0.1985 0.2364 0.1880 -0.0116 0.0173 0.0427 437 GLU A N 2714 C CA . GLU A 349 ? 0.2073 0.2355 0.2107 -0.0100 -0.0005 0.0290 437 GLU A CA 2715 C C . GLU A 349 ? 0.1959 0.2270 0.1720 -0.0094 0.0010 0.0355 437 GLU A C 2716 O O . GLU A 349 ? 0.2029 0.2534 0.1652 -0.0119 -0.0040 0.0585 437 GLU A O 2717 C CB . GLU A 349 ? 0.2212 0.2423 0.2260 -0.0066 -0.0016 0.0325 437 GLU A CB 2718 C CG . GLU A 349 ? 0.2663 0.2862 0.2944 -0.0132 0.0096 0.0353 437 GLU A CG 2719 C CD . GLU A 349 ? 0.3572 0.3657 0.3641 -0.0117 -0.0166 0.0075 437 GLU A CD 2720 O OE1 . GLU A 349 ? 0.3671 0.3753 0.3715 -0.0091 -0.0088 0.0374 437 GLU A OE1 2721 O OE2 . GLU A 349 ? 0.3930 0.3736 0.4069 -0.0151 -0.0123 0.0177 437 GLU A OE2 2722 N N . TYR A 350 ? 0.1733 0.2085 0.1760 -0.0034 -0.0162 0.0438 438 TYR A N 2723 C CA . TYR A 350 ? 0.1525 0.2030 0.1639 -0.0005 -0.0054 0.0314 438 TYR A CA 2724 C C . TYR A 350 ? 0.1683 0.1956 0.1288 -0.0054 -0.0082 0.0470 438 TYR A C 2725 O O . TYR A 350 ? 0.1516 0.2133 0.1403 0.0000 -0.0099 0.0550 438 TYR A O 2726 C CB . TYR A 350 ? 0.1538 0.2040 0.1631 -0.0099 -0.0092 0.0241 438 TYR A CB 2727 C CG . TYR A 350 ? 0.1470 0.1787 0.1397 -0.0027 -0.0096 0.0341 438 TYR A CG 2728 C CD1 . TYR A 350 ? 0.1689 0.2001 0.1311 -0.0008 -0.0061 0.0346 438 TYR A CD1 2729 C CD2 . TYR A 350 ? 0.1657 0.1862 0.1654 -0.0093 0.0005 0.0226 438 TYR A CD2 2730 C CE1 . TYR A 350 ? 0.1386 0.1839 0.1543 -0.0016 -0.0168 0.0250 438 TYR A CE1 2731 C CE2 . TYR A 350 ? 0.1744 0.1902 0.1297 -0.0046 0.0045 0.0429 438 TYR A CE2 2732 C CZ . TYR A 350 ? 0.1788 0.1930 0.1228 -0.0083 -0.0037 0.0173 438 TYR A CZ 2733 O OH . TYR A 350 ? 0.1817 0.2062 0.1366 -0.0210 -0.0010 0.0409 438 TYR A OH 2734 N N . PHE A 351 ? 0.1468 0.1930 0.1291 -0.0066 -0.0041 0.0447 439 PHE A N 2735 C CA . PHE A 351 ? 0.1569 0.2101 0.1620 -0.0007 -0.0001 0.0299 439 PHE A CA 2736 C C . PHE A 351 ? 0.1689 0.1927 0.1572 0.0018 0.0012 0.0267 439 PHE A C 2737 O O . PHE A 351 ? 0.1434 0.2194 0.1386 0.0069 -0.0063 0.0434 439 PHE A O 2738 C CB . PHE A 351 ? 0.1663 0.2128 0.1640 -0.0026 -0.0044 0.0424 439 PHE A CB 2739 C CG . PHE A 351 ? 0.1616 0.2332 0.1838 0.0011 -0.0009 0.0266 439 PHE A CG 2740 C CD1 . PHE A 351 ? 0.1935 0.2252 0.1956 -0.0030 -0.0093 0.0308 439 PHE A CD1 2741 C CD2 . PHE A 351 ? 0.2144 0.2589 0.2015 0.0005 0.0046 0.0173 439 PHE A CD2 2742 C CE1 . PHE A 351 ? 0.1742 0.2502 0.1717 -0.0099 -0.0006 0.0100 439 PHE A CE1 2743 C CE2 . PHE A 351 ? 0.2421 0.2742 0.2382 -0.0051 0.0201 0.0150 439 PHE A CE2 2744 C CZ . PHE A 351 ? 0.2462 0.2746 0.2114 0.0067 0.0192 0.0070 439 PHE A CZ 2745 N N . ILE A 352 ? 0.1827 0.2244 0.1784 -0.0023 0.0067 0.0346 440 ILE A N 2746 C CA . ILE A 352 ? 0.1946 0.2282 0.1952 -0.0010 -0.0033 0.0244 440 ILE A CA 2747 C C . ILE A 352 ? 0.1856 0.2039 0.1747 -0.0028 -0.0028 0.0281 440 ILE A C 2748 O O . ILE A 352 ? 0.2046 0.2430 0.1616 -0.0054 0.0050 0.0411 440 ILE A O 2749 C CB . ILE A 352 ? 0.2119 0.2373 0.2074 -0.0110 -0.0022 0.0229 440 ILE A CB 2750 C CG1 . ILE A 352 ? 0.2500 0.2756 0.2340 0.0006 0.0002 0.0226 440 ILE A CG1 2751 C CG2 . ILE A 352 ? 0.2183 0.2462 0.2024 -0.0108 0.0052 0.0254 440 ILE A CG2 2752 C CD1 . ILE A 352 ? 0.3153 0.3039 0.3101 -0.0115 -0.0081 0.0004 440 ILE A CD1 2753 N N . GLN A 353 ? 0.1722 0.2195 0.1704 0.0016 -0.0061 0.0382 441 GLN A N 2754 C CA . GLN A 353 ? 0.1697 0.2096 0.1830 -0.0002 -0.0073 0.0250 441 GLN A CA 2755 C C . GLN A 353 ? 0.1749 0.2124 0.1719 0.0016 -0.0098 0.0276 441 GLN A C 2756 O O . GLN A 353 ? 0.1718 0.2331 0.1382 -0.0039 -0.0058 0.0425 441 GLN A O 2757 C CB . GLN A 353 ? 0.1730 0.2144 0.1877 0.0006 -0.0113 0.0325 441 GLN A CB 2758 C CG . GLN A 353 ? 0.1764 0.2165 0.1910 0.0003 0.0021 0.0133 441 GLN A CG 2759 C CD . GLN A 353 ? 0.1877 0.2239 0.1813 -0.0053 0.0091 0.0196 441 GLN A CD 2760 O OE1 . GLN A 353 ? 0.2264 0.2611 0.1849 -0.0064 0.0062 0.0377 441 GLN A OE1 2761 N NE2 . GLN A 353 ? 0.1892 0.2456 0.1727 -0.0086 0.0102 0.0438 441 GLN A NE2 2762 N N . LEU A 354 ? 0.1670 0.2100 0.1410 0.0000 -0.0181 0.0282 442 LEU A N 2763 C CA . LEU A 354 ? 0.1534 0.1968 0.1562 -0.0011 -0.0133 0.0155 442 LEU A CA 2764 C C . LEU A 354 ? 0.1752 0.2065 0.1465 -0.0018 -0.0137 0.0214 442 LEU A C 2765 O O . LEU A 354 ? 0.1860 0.2189 0.1203 0.0055 -0.0096 0.0369 442 LEU A O 2766 C CB . LEU A 354 ? 0.1541 0.2037 0.1523 0.0038 -0.0144 0.0250 442 LEU A CB 2767 C CG . LEU A 354 ? 0.1455 0.1909 0.1466 0.0031 -0.0066 0.0238 442 LEU A CG 2768 C CD1 . LEU A 354 ? 0.1521 0.2021 0.1410 0.0045 -0.0186 0.0187 442 LEU A CD1 2769 C CD2 . LEU A 354 ? 0.1271 0.1997 0.1064 0.0106 0.0031 -0.0096 442 LEU A CD2 2770 N N . LEU A 355 ? 0.1645 0.2141 0.1694 0.0071 -0.0091 0.0361 443 LEU A N 2771 C CA . LEU A 355 ? 0.2123 0.2456 0.2079 0.0021 -0.0047 0.0146 443 LEU A CA 2772 C C . LEU A 355 ? 0.2069 0.2386 0.1737 0.0016 0.0114 0.0070 443 LEU A C 2773 O O . LEU A 355 ? 0.2302 0.2814 0.1432 0.0054 0.0034 0.0146 443 LEU A O 2774 C CB . LEU A 355 ? 0.2290 0.2635 0.2291 -0.0005 -0.0017 0.0251 443 LEU A CB 2775 C CG . LEU A 355 ? 0.2915 0.2965 0.2902 -0.0016 0.0072 0.0043 443 LEU A CG 2776 C CD1 . LEU A 355 ? 0.3191 0.3246 0.3145 0.0065 0.0003 0.0074 443 LEU A CD1 2777 C CD2 . LEU A 355 ? 0.3117 0.3331 0.3127 -0.0074 0.0077 0.0181 443 LEU A CD2 2778 N N . ARG A 356 ? 0.2104 0.2579 0.1801 0.0012 -0.0010 0.0129 444 ARG A N 2779 C CA . ARG A 356 ? 0.2157 0.2531 0.1907 0.0020 -0.0050 0.0055 444 ARG A CA 2780 C C . ARG A 356 ? 0.2163 0.2500 0.1818 0.0000 -0.0006 0.0060 444 ARG A C 2781 O O . ARG A 356 ? 0.2165 0.2874 0.1639 -0.0008 -0.0008 0.0116 444 ARG A O 2782 C CB . ARG A 356 ? 0.2241 0.2613 0.2061 0.0006 -0.0033 0.0119 444 ARG A CB 2783 C CG . ARG A 356 ? 0.2565 0.2983 0.2533 -0.0104 0.0025 0.0013 444 ARG A CG 2784 C CD . ARG A 356 ? 0.3342 0.3307 0.3305 0.0007 0.0054 0.0069 444 ARG A CD 2785 N NE . ARG A 356 ? 0.3820 0.4072 0.3673 -0.0024 -0.0068 0.0068 444 ARG A NE 2786 C CZ . ARG A 356 ? 0.4232 0.4236 0.4278 0.0048 0.0017 0.0045 444 ARG A CZ 2787 N NH1 . ARG A 356 ? 0.4556 0.4451 0.4451 -0.0037 -0.0018 -0.0046 444 ARG A NH1 2788 N NH2 . ARG A 356 ? 0.4274 0.4486 0.4305 -0.0007 -0.0049 0.0063 444 ARG A NH2 2789 N N . ASN A 357 ? 0.1948 0.2285 0.1438 0.0038 -0.0193 0.0231 445 ASN A N 2790 C CA . ASN A 357 ? 0.1829 0.2116 0.1684 0.0077 -0.0110 0.0015 445 ASN A CA 2791 C C . ASN A 357 ? 0.1861 0.2167 0.1484 0.0033 -0.0157 0.0084 445 ASN A C 2792 O O . ASN A 357 ? 0.1749 0.2226 0.1355 -0.0024 -0.0184 0.0134 445 ASN A O 2793 C CB . ASN A 357 ? 0.1767 0.2114 0.1639 0.0044 -0.0051 -0.0011 445 ASN A CB 2794 C CG . ASN A 357 ? 0.1908 0.2227 0.1738 0.0057 -0.0036 0.0110 445 ASN A CG 2795 O OD1 . ASN A 357 ? 0.2440 0.2907 0.1586 0.0106 -0.0280 0.0138 445 ASN A OD1 2796 N ND2 . ASN A 357 ? 0.1634 0.2257 0.1695 0.0085 -0.0123 0.0264 445 ASN A ND2 2797 N N . ALA A 358 ? 0.1972 0.2269 0.1428 0.0091 -0.0081 0.0022 446 ALA A N 2798 C CA . ALA A 358 ? 0.2011 0.2175 0.1658 0.0045 0.0057 0.0020 446 ALA A CA 2799 C C . ALA A 358 ? 0.1997 0.2311 0.1746 0.0118 -0.0068 -0.0020 446 ALA A C 2800 O O . ALA A 358 ? 0.2316 0.2800 0.1452 0.0109 -0.0247 -0.0017 446 ALA A O 2801 C CB . ALA A 358 ? 0.2065 0.2279 0.1761 0.0169 -0.0055 -0.0058 446 ALA A CB 2802 N N . ASN A 359 ? 0.2201 0.2345 0.1741 0.0102 -0.0079 -0.0029 447 ASN A N 2803 C CA . ASN A 359 ? 0.2319 0.2439 0.1956 0.0048 -0.0024 0.0008 447 ASN A CA 2804 C C . ASN A 359 ? 0.2437 0.2543 0.2010 0.0049 -0.0094 0.0016 447 ASN A C 2805 O O . ASN A 359 ? 0.2369 0.2794 0.1776 0.0075 -0.0201 -0.0085 447 ASN A O 2806 C CB . ASN A 359 ? 0.2476 0.2555 0.2014 0.0109 -0.0054 0.0026 447 ASN A CB 2807 C CG . ASN A 359 ? 0.2668 0.2957 0.2743 0.0065 -0.0125 -0.0043 447 ASN A CG 2808 O OD1 . ASN A 359 ? 0.3359 0.3322 0.3101 -0.0044 -0.0175 -0.0269 447 ASN A OD1 2809 N ND2 . ASN A 359 ? 0.3102 0.3492 0.3113 0.0001 0.0039 -0.0030 447 ASN A ND2 2810 N N . PRO A 360 ? 0.2676 0.2673 0.2193 0.0106 -0.0041 0.0024 448 PRO A N 2811 C CA . PRO A 360 ? 0.2791 0.2733 0.2443 0.0076 -0.0034 -0.0055 448 PRO A CA 2812 C C . PRO A 360 ? 0.2898 0.2930 0.2663 0.0072 0.0006 -0.0009 448 PRO A C 2813 O O . PRO A 360 ? 0.2832 0.2875 0.2426 0.0154 0.0079 -0.0038 448 PRO A O 2814 C CB . PRO A 360 ? 0.2881 0.2785 0.2617 0.0090 -0.0023 -0.0036 448 PRO A CB 2815 C CG . PRO A 360 ? 0.3006 0.2851 0.2703 0.0085 -0.0046 -0.0035 448 PRO A CG 2816 C CD . PRO A 360 ? 0.2783 0.2661 0.2428 0.0136 -0.0087 0.0050 448 PRO A CD 2817 N N . PRO A 361 ? 0.2991 0.3140 0.2783 0.0057 -0.0021 0.0000 449 PRO A N 2818 C CA . PRO A 361 ? 0.3103 0.3172 0.2863 0.0041 -0.0021 0.0020 449 PRO A CA 2819 C C . PRO A 361 ? 0.3130 0.3155 0.2787 0.0033 0.0047 -0.0021 449 PRO A C 2820 O O . PRO A 361 ? 0.3129 0.3276 0.2851 0.0131 0.0149 -0.0007 449 PRO A O 2821 C CB . PRO A 361 ? 0.3191 0.3243 0.2862 0.0038 -0.0041 0.0048 449 PRO A CB 2822 C CG . PRO A 361 ? 0.3250 0.3297 0.2964 0.0002 -0.0012 0.0061 449 PRO A CG 2823 C CD . PRO A 361 ? 0.3109 0.3198 0.2930 0.0031 -0.0002 -0.0016 449 PRO A CD 2824 N N . PHE A 362 ? 0.3150 0.3237 0.2881 0.0043 0.0044 -0.0011 450 PHE A N 2825 C CA . PHE A 362 ? 0.3288 0.3299 0.3169 0.0036 -0.0002 0.0011 450 PHE A CA 2826 C C . PHE A 362 ? 0.3260 0.3303 0.3175 0.0032 0.0011 0.0010 450 PHE A C 2827 O O . PHE A 362 ? 0.3174 0.3300 0.3259 -0.0012 -0.0009 -0.0012 450 PHE A O 2828 C CB . PHE A 362 ? 0.3278 0.3356 0.3304 0.0020 -0.0003 0.0053 450 PHE A CB 2829 C CG . PHE A 362 ? 0.3507 0.3496 0.3299 0.0028 0.0000 -0.0021 450 PHE A CG 2830 C CD1 . PHE A 362 ? 0.3565 0.3635 0.3483 0.0051 -0.0033 0.0003 450 PHE A CD1 2831 C CD2 . PHE A 362 ? 0.3602 0.3622 0.3506 0.0086 -0.0019 0.0032 450 PHE A CD2 2832 C CE1 . PHE A 362 ? 0.3280 0.3518 0.3459 0.0070 0.0003 -0.0011 450 PHE A CE1 2833 C CE2 . PHE A 362 ? 0.3613 0.3527 0.3495 0.0074 0.0019 -0.0073 450 PHE A CE2 2834 C CZ . PHE A 362 ? 0.3555 0.3532 0.3273 0.0014 -0.0041 -0.0068 450 PHE A CZ 2835 O OXT . PHE A 362 ? 0.3400 0.3342 0.3346 0.0105 0.0007 0.0005 450 PHE A OXT 2836 C C1 . NAG B . ? 0.1348 0.1036 0.1212 -0.0044 -0.0069 -0.0043 500 NAG A C1 2837 C C2 . NAG B . ? 0.1256 0.1234 0.1328 -0.0093 -0.0040 -0.0122 500 NAG A C2 2838 C C3 . NAG B . ? 0.1506 0.1211 0.1546 -0.0032 -0.0071 -0.0116 500 NAG A C3 2839 C C4 . NAG B . ? 0.1421 0.1608 0.1716 0.0019 -0.0027 0.0001 500 NAG A C4 2840 C C5 . NAG B . ? 0.1551 0.1378 0.1318 0.0121 -0.0042 0.0048 500 NAG A C5 2841 C C6 . NAG B . ? 0.1440 0.1435 0.1573 0.0155 0.0000 0.0050 500 NAG A C6 2842 C C7 . NAG B . ? 0.1341 0.1435 0.1786 0.0141 0.0052 0.0027 500 NAG A C7 2843 C C8 . NAG B . ? 0.1263 0.1156 0.1549 -0.0042 -0.0152 -0.0202 500 NAG A C8 2844 N N2 . NAG B . ? 0.1222 0.1175 0.1149 -0.0069 0.0005 -0.0037 500 NAG A N2 2845 O O3 . NAG B . ? 0.1604 0.1718 0.2138 -0.0013 -0.0190 -0.0254 500 NAG A O3 2846 O O4 . NAG B . ? 0.1866 0.2082 0.1975 0.0199 -0.0244 -0.0066 500 NAG A O4 2847 O O5 . NAG B . ? 0.1102 0.1292 0.1380 0.0060 -0.0011 0.0083 500 NAG A O5 2848 O O6 . NAG B . ? 0.1544 0.1376 0.1518 0.0148 -0.0034 -0.0029 500 NAG A O6 2849 O O7 . NAG B . ? 0.2145 0.1797 0.2545 -0.0059 0.0269 -0.0115 500 NAG A O7 2850 C C2 . BGC C . ? 0.1662 0.1668 0.1796 -0.0088 0.0008 0.0232 501 BGC A C2 2851 C C3 . BGC C . ? 0.1572 0.1719 0.1652 -0.0098 0.0056 0.0243 501 BGC A C3 2852 C C4 . BGC C . ? 0.1685 0.1681 0.1770 -0.0075 0.0150 0.0191 501 BGC A C4 2853 C C5 . BGC C . ? 0.1640 0.1665 0.1568 -0.0002 -0.0025 0.0295 501 BGC A C5 2854 C C6 . BGC C . ? 0.1689 0.1461 0.1418 0.0012 -0.0085 0.0389 501 BGC A C6 2855 C C1 . BGC C . ? 0.1603 0.1658 0.1678 -0.0014 -0.0023 0.0236 501 BGC A C1 2856 O O2 . BGC C . ? 0.1658 0.1893 0.1894 -0.0159 -0.0044 0.0075 501 BGC A O2 2857 O O3 . BGC C . ? 0.1579 0.2252 0.2229 -0.0285 0.0018 0.0139 501 BGC A O3 2858 O O4 . BGC C . ? 0.1879 0.2042 0.1905 -0.0008 0.0024 0.0409 501 BGC A O4 2859 O O5 . BGC C . ? 0.1703 0.1581 0.1485 0.0045 0.0115 0.0228 501 BGC A O5 2860 O O6 . BGC C . ? 0.1936 0.2092 0.1455 -0.0008 -0.0182 0.0583 501 BGC A O6 2861 C C1 . SSG D . ? 0.1851 0.2354 0.1954 -0.0006 0.0032 0.0220 502 SSG A C1 2862 C C2 . SSG D . ? 0.1970 0.2188 0.2048 -0.0035 0.0139 0.0208 502 SSG A C2 2863 O O2 . SSG D . ? 0.2171 0.2604 0.1898 0.0056 -0.0027 0.0323 502 SSG A O2 2864 C C3 . SSG D . ? 0.1737 0.2156 0.2101 -0.0062 -0.0011 0.0174 502 SSG A C3 2865 O O3 . SSG D . ? 0.1841 0.1837 0.1744 0.0048 0.0100 0.0314 502 SSG A O3 2866 C C4 . SSG D . ? 0.1572 0.1936 0.1689 -0.0297 0.0141 0.0357 502 SSG A C4 2867 C C5 . SSG D . ? 0.1949 0.2250 0.2074 -0.0088 0.0083 -0.0005 502 SSG A C5 2868 O O5 . SSG D . ? 0.1837 0.2762 0.2165 -0.0114 0.0052 0.0131 502 SSG A O5 2869 C C6 . SSG D . ? 0.2192 0.2685 0.2200 -0.0143 -0.0041 0.0009 502 SSG A C6 2870 O O6 . SSG D . ? 0.2768 0.2932 0.2999 0.0085 -0.0049 0.0108 502 SSG A O6 2871 S S4 . SSG D . ? 0.1562 0.1772 0.1786 -0.0104 0.0043 0.0571 502 SSG A S4 2872 C C1 . SSG E . ? 0.1947 0.1997 0.2140 -0.0129 0.0021 0.0035 503 SSG A C1 2873 C C2 . SSG E . ? 0.2186 0.2442 0.2368 -0.0293 0.0034 -0.0048 503 SSG A C2 2874 O O2 . SSG E . ? 0.2537 0.2965 0.2161 -0.0314 0.0072 -0.0345 503 SSG A O2 2875 C C3 . SSG E . ? 0.2813 0.2748 0.2750 -0.0060 0.0135 -0.0133 503 SSG A C3 2876 O O3 . SSG E . ? 0.3077 0.3885 0.3540 -0.0434 0.0013 -0.0217 503 SSG A O3 2877 C C4 . SSG E . ? 0.2246 0.2585 0.2482 -0.0025 0.0004 0.0046 503 SSG A C4 2878 C C5 . SSG E . ? 0.2079 0.2367 0.2210 0.0000 0.0100 0.0078 503 SSG A C5 2879 O O5 . SSG E . ? 0.1934 0.1918 0.2141 -0.0062 0.0146 0.0082 503 SSG A O5 2880 C C6 . SSG E . ? 0.2583 0.2507 0.2425 0.0165 0.0051 -0.0043 503 SSG A C6 2881 O O6 . SSG E . ? 0.2360 0.2418 0.2837 -0.0101 0.0074 0.0134 503 SSG A O6 2882 S S4 . SSG E . ? 0.1996 0.3157 0.2091 0.0017 0.0218 0.0527 503 SSG A S4 2883 C C1 . SGC F . ? 0.1340 0.1542 0.1400 -0.0035 -0.0018 0.0121 504 SGC A C1 2884 C C2 . SGC F . ? 0.1507 0.1284 0.1465 0.0054 -0.0031 0.0045 504 SGC A C2 2885 O O2 . SGC F . ? 0.1732 0.1620 0.1373 -0.0122 -0.0122 0.0016 504 SGC A O2 2886 C C3 . SGC F . ? 0.1619 0.1423 0.1694 0.0023 0.0007 0.0070 504 SGC A C3 2887 O O3 . SGC F . ? 0.1912 0.1739 0.1621 0.0031 0.0038 -0.0154 504 SGC A O3 2888 C C4 . SGC F . ? 0.1341 0.1306 0.1604 0.0018 0.0002 0.0029 504 SGC A C4 2889 C C5 . SGC F . ? 0.1497 0.1274 0.1542 -0.0141 -0.0005 0.0038 504 SGC A C5 2890 O O5 . SGC F . ? 0.1581 0.1678 0.1444 -0.0196 -0.0046 0.0083 504 SGC A O5 2891 C C6 . SGC F . ? 0.1740 0.1745 0.1639 -0.0036 -0.0049 -0.0030 504 SGC A C6 2892 O O6 . SGC F . ? 0.2183 0.2219 0.2096 -0.0144 0.0255 -0.0110 504 SGC A O6 2893 S S4 . SGC F . ? 0.1838 0.1599 0.1765 -0.0212 0.0053 0.0156 504 SGC A S4 2894 C C1 . MA3 G . ? 0.1556 0.1555 0.1825 0.0037 -0.0015 -0.0132 505 MA3 A C1 2895 C C2 . MA3 G . ? 0.1383 0.1491 0.1689 0.0077 -0.0045 0.0024 505 MA3 A C2 2896 C C3 . MA3 G . ? 0.1506 0.1455 0.1523 -0.0032 0.0105 0.0005 505 MA3 A C3 2897 C C4 . MA3 G . ? 0.1488 0.1617 0.1545 -0.0051 0.0047 0.0063 505 MA3 A C4 2898 C C5 . MA3 G . ? 0.1586 0.1782 0.1872 -0.0152 0.0018 -0.0011 505 MA3 A C5 2899 C C6 . MA3 G . ? 0.2175 0.2219 0.2113 -0.0083 -0.0073 0.0050 505 MA3 A C6 2900 C C7 . MA3 G . ? 0.1550 0.1672 0.1949 -0.0020 0.0047 -0.0163 505 MA3 A C7 2901 O O1 . MA3 G . ? 0.1467 0.1883 0.2004 0.0011 -0.0014 -0.0130 505 MA3 A O1 2902 O O2 . MA3 G . ? 0.1623 0.1721 0.1788 -0.0007 -0.0052 -0.0095 505 MA3 A O2 2903 O O3 . MA3 G . ? 0.1687 0.1697 0.1787 -0.0191 -0.0075 -0.0095 505 MA3 A O3 2904 S S4 . MA3 G . ? 0.1681 0.1330 0.1671 -0.0161 0.0020 0.0094 505 MA3 A S4 2905 O O5 . MA3 G . ? 0.1710 0.1612 0.1753 0.0094 -0.0042 -0.0018 505 MA3 A O5 2906 O O6 . MA3 G . ? 0.2859 0.2951 0.3026 -0.0142 -0.0257 0.0166 505 MA3 A O6 2907 MG MG . MG H . ? 0.2702 0.3143 0.3045 -0.0375 -0.0264 -0.0445 506 MG A MG 2908 C C . ACY I . ? 0.2198 0.2308 0.2079 0.0066 -0.0139 0.0010 507 ACY A C 2909 O O . ACY I . ? 0.2278 0.2518 0.2300 0.0117 -0.0055 -0.0069 507 ACY A O 2910 O OXT . ACY I . ? 0.2296 0.2425 0.2293 0.0237 -0.0043 -0.0033 507 ACY A OXT 2911 C CH3 . ACY I . ? 0.2509 0.2493 0.2486 -0.0024 -0.0010 -0.0060 507 ACY A CH3 2912 O O . HOH J . ? 0.3622 0.3685 0.3874 -0.0141 -0.0035 -0.0023 2001 HOH A O 2913 O O . HOH J . ? 0.3403 0.3434 0.3764 -0.0016 -0.0144 0.0006 2002 HOH A O 2914 O O . HOH J . ? 0.3020 0.2968 0.3846 0.0115 0.0059 -0.0109 2003 HOH A O 2915 O O . HOH J . ? 0.3010 0.3390 0.3123 0.0123 0.0232 -0.0008 2004 HOH A O 2916 O O . HOH J . ? 0.4170 0.3253 0.3898 -0.0101 -0.0005 -0.0056 2005 HOH A O 2917 O O . HOH J . ? 0.5168 0.5027 0.5120 -0.0029 -0.0034 0.0054 2006 HOH A O 2918 O O . HOH J . ? 0.4158 0.4021 0.3948 0.0155 0.0055 0.0112 2007 HOH A O 2919 O O . HOH J . ? 0.4668 0.4545 0.4867 0.0087 0.0044 -0.0071 2008 HOH A O 2920 O O . HOH J . ? 0.4208 0.4181 0.3871 -0.0094 -0.0018 -0.0223 2009 HOH A O 2921 O O . HOH J . ? 0.3161 0.3038 0.2865 0.0011 -0.0051 -0.0142 2010 HOH A O 2922 O O . HOH J . ? 0.2567 0.3806 0.2337 0.0271 0.0317 -0.0132 2011 HOH A O 2923 O O . HOH J . ? 0.2857 0.3329 0.3320 0.0209 0.0289 -0.0230 2012 HOH A O 2924 O O A HOH J . ? 0.2450 0.2799 0.2022 0.0064 0.0323 -0.0066 2013 HOH A O 2925 O O B HOH J . ? 0.3524 0.3664 0.3488 -0.0008 0.0022 0.0036 2013 HOH A O 2926 O O . HOH J . ? 0.2600 0.3066 0.2293 0.0223 0.0047 0.0131 2014 HOH A O 2927 O O A HOH J . ? 0.2655 0.2979 0.2483 -0.0087 0.0005 0.0149 2016 HOH A O 2928 O O B HOH J . ? 0.2845 0.3252 0.2625 0.0062 0.0037 -0.0105 2016 HOH A O 2929 O O A HOH J . ? 0.2790 0.2740 0.2874 -0.0094 -0.0040 0.0136 2017 HOH A O 2930 O O B HOH J . ? 0.2896 0.2722 0.2443 0.0055 0.0029 -0.0033 2017 HOH A O 2931 O O . HOH J . ? 0.3394 0.3631 0.3236 0.0270 0.0293 0.0016 2018 HOH A O 2932 O O . HOH J . ? 0.5061 0.5171 0.5017 -0.0011 -0.0038 0.0042 2019 HOH A O 2933 O O . HOH J . ? 0.4320 0.3879 0.4495 0.0029 -0.0100 0.0064 2020 HOH A O 2934 O O . HOH J . ? 0.3631 0.3917 0.3495 -0.0032 -0.0010 -0.0038 2021 HOH A O 2935 O O . HOH J . ? 0.4197 0.4332 0.4366 0.0089 -0.0034 0.0028 2022 HOH A O 2936 O O . HOH J . ? 0.2536 0.2298 0.2974 -0.0027 0.0176 0.0111 2023 HOH A O 2937 O O . HOH J . ? 0.3416 0.3373 0.2729 -0.0199 -0.0008 -0.0259 2024 HOH A O 2938 O O . HOH J . ? 0.4933 0.5021 0.4977 0.0009 -0.0037 0.0074 2025 HOH A O 2939 O O . HOH J . ? 0.4171 0.4412 0.4047 0.0141 0.0023 0.0014 2026 HOH A O 2940 O O . HOH J . ? 0.3396 0.3825 0.3108 0.0030 0.0040 0.0091 2027 HOH A O 2941 O O . HOH J . ? 0.3982 0.4247 0.3914 0.0032 0.0101 -0.0049 2028 HOH A O 2942 O O . HOH J . ? 0.4694 0.4548 0.4792 -0.0057 -0.0004 0.0033 2029 HOH A O 2943 O O . HOH J . ? 0.3010 0.3564 0.2867 0.0223 0.0072 -0.0099 2030 HOH A O 2944 O O A HOH J . ? 0.2059 0.2170 0.1372 0.0140 0.0032 -0.0077 2031 HOH A O 2945 O O B HOH J . ? 0.2129 0.2217 0.1598 0.0073 -0.0145 0.0163 2031 HOH A O 2946 O O . HOH J . ? 0.1355 0.1603 0.1336 0.0283 -0.0149 0.0083 2034 HOH A O 2947 O O . HOH J . ? 0.4411 0.4413 0.4200 -0.0163 0.0025 -0.0102 2035 HOH A O 2948 O O . HOH J . ? 0.4403 0.4234 0.4543 0.0013 -0.0007 0.0038 2036 HOH A O 2949 O O . HOH J . ? 0.2012 0.2297 0.2361 0.0019 -0.0089 0.0441 2037 HOH A O 2950 O O . HOH J . ? 0.2357 0.2878 0.2140 0.0213 0.0002 0.0150 2038 HOH A O 2951 O O . HOH J . ? 0.2535 0.2942 0.2648 0.0075 0.0474 -0.0221 2039 HOH A O 2952 O O . HOH J . ? 0.4094 0.3866 0.3190 0.0051 -0.0076 -0.0142 2040 HOH A O 2953 O O A HOH J . ? 0.3281 0.3488 0.3103 -0.0070 0.0055 -0.0012 2041 HOH A O 2954 O O B HOH J . ? 0.2813 0.2751 0.2737 -0.0079 0.0097 0.0031 2041 HOH A O 2955 O O . HOH J . ? 0.4318 0.4488 0.4304 -0.0011 0.0137 -0.0016 2042 HOH A O 2956 O O . HOH J . ? 0.4721 0.4701 0.4564 0.0014 0.0026 -0.0106 2044 HOH A O 2957 O O . HOH J . ? 0.2682 0.3443 0.2596 0.0017 -0.0171 0.0385 2045 HOH A O 2958 O O . HOH J . ? 0.1669 0.1959 0.1676 -0.0210 -0.0028 0.0367 2046 HOH A O 2959 O O . HOH J . ? 0.2796 0.1995 0.1912 -0.0355 0.0344 0.0528 2047 HOH A O 2960 O O . HOH J . ? 0.4861 0.4701 0.4751 -0.0043 -0.0013 0.0067 2048 HOH A O 2961 O O . HOH J . ? 0.2335 0.1944 0.1993 -0.0082 0.0166 0.0046 2049 HOH A O 2962 O O . HOH J . ? 0.2279 0.1797 0.2833 -0.0049 0.0029 -0.0275 2050 HOH A O 2963 O O . HOH J . ? 0.3549 0.3623 0.3141 -0.0017 0.0238 0.0089 2051 HOH A O 2964 O O . HOH J . ? 0.2866 0.3518 0.3840 -0.0101 0.0055 0.0131 2052 HOH A O 2965 O O . HOH J . ? 0.4519 0.4552 0.4369 -0.0097 0.0069 0.0078 2053 HOH A O 2966 O O A HOH J . ? 0.2528 0.2727 0.2401 0.0071 0.0104 -0.0028 2054 HOH A O 2967 O O B HOH J . ? 0.2061 0.0755 0.1943 0.0079 -0.0065 0.0207 2054 HOH A O 2968 O O . HOH J . ? 0.1822 0.1841 0.2904 0.0009 -0.0139 0.0163 2055 HOH A O 2969 O O . HOH J . ? 0.4503 0.3925 0.4453 0.0098 0.0045 0.0122 2056 HOH A O 2970 O O . HOH J . ? 0.5036 0.4929 0.5058 0.0113 -0.0055 -0.0023 2057 HOH A O 2971 O O . HOH J . ? 0.4320 0.4022 0.4122 -0.0021 0.0061 0.0105 2058 HOH A O 2972 O O . HOH J . ? 0.1405 0.1173 0.1372 0.0034 -0.0136 -0.0099 2060 HOH A O 2973 O O . HOH J . ? 0.1034 0.1066 0.1471 0.0039 -0.0011 -0.0144 2061 HOH A O 2974 O O . HOH J . ? 0.2303 0.2519 0.2825 -0.0064 0.0033 -0.0062 2062 HOH A O 2975 O O . HOH J . ? 0.2755 0.2857 0.3032 -0.0073 -0.0079 -0.0169 2063 HOH A O 2976 O O . HOH J . ? 0.4057 0.4057 0.3714 0.0022 0.0083 0.0030 2064 HOH A O 2977 O O . HOH J . ? 0.4388 0.4372 0.4626 0.0074 0.0033 -0.0006 2065 HOH A O 2978 O O . HOH J . ? 0.1173 0.1858 0.1852 -0.0076 0.0000 0.0183 2066 HOH A O 2979 O O . HOH J . ? 0.2716 0.2762 0.2809 -0.0155 -0.0002 0.0238 2067 HOH A O 2980 O O . HOH J . ? 0.1586 0.1789 0.1973 0.0276 0.0056 0.0095 2068 HOH A O 2981 O O . HOH J . ? 0.4342 0.4666 0.4288 0.0004 0.0023 -0.0010 2069 HOH A O 2982 O O A HOH J . ? 0.2305 0.2370 0.2406 0.0023 0.0154 0.0062 2070 HOH A O 2983 O O B HOH J . ? 0.3362 0.3160 0.2914 0.0108 0.0026 0.0028 2070 HOH A O 2984 O O . HOH J . ? 0.2983 0.3202 0.3402 0.0003 -0.0155 0.0320 2071 HOH A O 2985 O O . HOH J . ? 0.4185 0.4317 0.4318 0.0090 0.0074 -0.0218 2072 HOH A O 2986 O O . HOH J . ? 0.3185 0.2657 0.2929 0.0013 0.0040 0.0067 2073 HOH A O 2987 O O . HOH J . ? 0.2956 0.2856 0.3187 -0.0027 -0.0051 -0.0010 2074 HOH A O 2988 O O . HOH J . ? 0.4289 0.4604 0.4207 -0.0034 -0.0127 0.0000 2075 HOH A O 2989 O O . HOH J . ? 0.4113 0.4313 0.4273 0.0065 -0.0054 0.0070 2076 HOH A O 2990 O O . HOH J . ? 0.4842 0.4816 0.4657 -0.0004 -0.0009 0.0145 2077 HOH A O 2991 O O . HOH J . ? 0.3323 0.4012 0.3710 -0.0075 0.0030 -0.0024 2078 HOH A O 2992 O O . HOH J . ? 0.2399 0.3009 0.3108 0.0201 -0.0070 -0.0062 2079 HOH A O 2993 O O . HOH J . ? 0.4186 0.4130 0.3936 -0.0077 0.0007 0.0032 2080 HOH A O 2994 O O . HOH J . ? 0.3655 0.4250 0.4047 -0.0091 0.0089 0.0065 2081 HOH A O 2995 O O . HOH J . ? 0.2711 0.3192 0.2375 -0.0023 0.0291 0.0130 2082 HOH A O 2996 O O . HOH J . ? 0.3002 0.3587 0.3342 0.0032 -0.0127 -0.0166 2083 HOH A O 2997 O O . HOH J . ? 0.3626 0.4206 0.4002 -0.0172 0.0014 -0.0029 2084 HOH A O 2998 O O . HOH J . ? 0.4027 0.4080 0.4030 0.0111 0.0045 0.0074 2086 HOH A O 2999 O O . HOH J . ? 0.3230 0.2776 0.3321 0.0008 -0.0046 -0.0048 2087 HOH A O 3000 O O . HOH J . ? 0.3514 0.3839 0.3781 -0.0366 0.0015 0.0078 2088 HOH A O 3001 O O . HOH J . ? 0.4486 0.4277 0.4679 0.0004 -0.0057 0.0077 2089 HOH A O 3002 O O . HOH J . ? 0.3529 0.2859 0.3185 -0.0308 0.0209 0.0083 2090 HOH A O 3003 O O . HOH J . ? 0.3134 0.2908 0.3444 -0.0216 0.0175 -0.0077 2091 HOH A O 3004 O O . HOH J . ? 0.2439 0.2082 0.2943 -0.0256 -0.0029 0.0159 2092 HOH A O 3005 O O A HOH J . ? 0.3824 0.3421 0.3637 -0.0028 0.0054 -0.0023 2093 HOH A O 3006 O O B HOH J . ? 0.3008 0.3093 0.2955 0.0071 -0.0015 0.0021 2093 HOH A O 3007 O O . HOH J . ? 0.2461 0.3511 0.3269 0.0072 0.0202 -0.0236 2094 HOH A O 3008 O O . HOH J . ? 0.3963 0.4002 0.3918 0.0011 -0.0005 -0.0039 2095 HOH A O 3009 O O . HOH J . ? 0.3924 0.4463 0.4142 -0.0107 -0.0085 -0.0015 2096 HOH A O 3010 O O . HOH J . ? 0.2763 0.3404 0.2357 -0.0103 0.0464 0.0147 2097 HOH A O 3011 O O . HOH J . ? 0.3344 0.3819 0.3103 -0.0009 -0.0084 -0.0136 2098 HOH A O 3012 O O . HOH J . ? 0.3661 0.3698 0.3478 -0.0114 0.0008 0.0171 2099 HOH A O 3013 O O . HOH J . ? 0.2228 0.2405 0.1625 -0.0045 0.0083 -0.0316 2100 HOH A O 3014 O O . HOH J . ? 0.2371 0.2085 0.2156 -0.0083 -0.0210 0.0050 2101 HOH A O 3015 O O . HOH J . ? 0.4914 0.4893 0.5092 -0.0001 0.0059 0.0018 2102 HOH A O 3016 O O . HOH J . ? 0.3140 0.3402 0.3316 -0.0101 -0.0054 -0.0183 2103 HOH A O 3017 O O . HOH J . ? 0.3859 0.4133 0.4348 -0.0007 0.0149 -0.0118 2104 HOH A O 3018 O O . HOH J . ? 0.4252 0.4428 0.4358 0.0036 -0.0034 0.0090 2105 HOH A O 3019 O O . HOH J . ? 0.2217 0.2613 0.2710 0.0327 -0.0270 0.0263 2106 HOH A O 3020 O O . HOH J . ? 0.4880 0.4807 0.4715 0.0012 -0.0043 -0.0065 2107 HOH A O 3021 O O . HOH J . ? 0.4658 0.4556 0.4600 0.0045 -0.0035 -0.0042 2108 HOH A O 3022 O O . HOH J . ? 0.4535 0.4553 0.4459 0.0000 -0.0013 0.0050 2109 HOH A O 3023 O O . HOH J . ? 0.3284 0.3539 0.3588 0.0252 0.0028 -0.0032 2110 HOH A O 3024 O O . HOH J . ? 0.5065 0.4895 0.4870 -0.0017 0.0046 0.0028 2111 HOH A O 3025 O O A HOH J . ? 0.2386 0.1876 0.2264 0.0300 0.0052 0.0062 2112 HOH A O 3026 O O B HOH J . ? 0.2296 0.2420 0.2285 0.0074 0.0084 -0.0107 2112 HOH A O 3027 O O . HOH J . ? 0.2225 0.1574 0.2455 -0.0052 0.0213 -0.0097 2113 HOH A O 3028 O O . HOH J . ? 0.3875 0.3869 0.3797 0.0242 -0.0186 0.0072 2114 HOH A O 3029 O O . HOH J . ? 0.3879 0.4259 0.4171 0.0024 0.0060 -0.0120 2115 HOH A O 3030 O O . HOH J . ? 0.3489 0.3134 0.3352 -0.0169 0.0103 -0.0086 2116 HOH A O 3031 O O . HOH J . ? 0.2148 0.1767 0.2178 0.0112 0.0059 -0.0082 2117 HOH A O 3032 O O . HOH J . ? 0.4495 0.4654 0.4523 -0.0026 -0.0005 0.0078 2118 HOH A O 3033 O O . HOH J . ? 0.4241 0.4223 0.3885 0.0115 0.0053 0.0066 2119 HOH A O 3034 O O . HOH J . ? 0.1629 0.1926 0.1191 0.0165 0.0050 -0.0050 2120 HOH A O 3035 O O . HOH J . ? 0.5213 0.5085 0.4943 -0.0056 0.0022 -0.0060 2121 HOH A O 3036 O O . HOH J . ? 0.1858 0.2680 0.1723 -0.0108 0.0134 0.0221 2122 HOH A O 3037 O O . HOH J . ? 0.3086 0.3100 0.3062 0.0306 -0.0003 -0.0059 2123 HOH A O 3038 O O . HOH J . ? 0.4322 0.4101 0.4490 0.0033 -0.0026 -0.0052 2124 HOH A O 3039 O O . HOH J . ? 0.2876 0.3018 0.2660 0.0010 -0.0125 -0.0231 2125 HOH A O 3040 O O . HOH J . ? 0.1393 0.0865 0.1494 -0.0261 -0.0064 -0.0146 2126 HOH A O 3041 O O . HOH J . ? 0.1653 0.2085 0.2176 -0.0274 -0.0190 0.0034 2127 HOH A O 3042 O O . HOH J . ? 0.1905 0.2299 0.2553 -0.0232 -0.0074 0.0185 2128 HOH A O 3043 O O . HOH J . ? 0.4412 0.4406 0.4135 0.0024 0.0088 -0.0001 2129 HOH A O 3044 O O . HOH J . ? 0.2700 0.2434 0.2889 0.0159 -0.0006 0.0224 2130 HOH A O 3045 O O . HOH J . ? 0.2739 0.2767 0.2779 0.0228 0.0038 0.0160 2131 HOH A O 3046 O O . HOH J . ? 0.4905 0.4867 0.4710 0.0069 0.0006 0.0073 2132 HOH A O 3047 O O . HOH J . ? 0.3676 0.3769 0.3818 -0.0221 0.0164 -0.0117 2133 HOH A O 3048 O O . HOH J . ? 0.2994 0.3061 0.3827 0.0025 -0.0097 0.0082 2134 HOH A O 3049 O O . HOH J . ? 0.2956 0.2932 0.2640 -0.0210 -0.0075 -0.0045 2135 HOH A O 3050 O O . HOH J . ? 0.2880 0.3392 0.3416 -0.0074 -0.0046 0.0119 2136 HOH A O 3051 O O . HOH J . ? 0.3214 0.3397 0.3535 0.0141 -0.0058 -0.0049 2137 HOH A O 3052 O O . HOH J . ? 0.3220 0.3222 0.3604 -0.0169 -0.0112 0.0106 2138 HOH A O 3053 O O . HOH J . ? 0.4285 0.4302 0.4428 -0.0127 -0.0067 -0.0168 2139 HOH A O 3054 O O . HOH J . ? 0.3996 0.3231 0.3675 -0.0078 -0.0003 -0.0118 2140 HOH A O 3055 O O A HOH J . ? 0.1744 0.2341 0.2464 -0.0288 -0.0091 -0.0086 2141 HOH A O 3056 O O B HOH J . ? 0.1348 0.1296 0.1875 0.0159 0.0151 0.0392 2141 HOH A O 3057 O O . HOH J . ? 0.3308 0.3110 0.3119 0.0160 -0.0073 -0.0162 2142 HOH A O 3058 O O . HOH J . ? 0.4194 0.4070 0.4049 -0.0011 0.0093 -0.0003 2143 HOH A O 3059 O O . HOH J . ? 0.3372 0.2531 0.3370 0.0014 -0.0117 -0.0155 2144 HOH A O 3060 O O . HOH J . ? 0.4252 0.4009 0.4484 -0.0035 0.0105 0.0167 2145 HOH A O 3061 O O . HOH J . ? 0.3586 0.4024 0.4043 0.0172 -0.0034 -0.0089 2146 HOH A O 3062 O O . HOH J . ? 0.3693 0.3735 0.3391 -0.0041 0.0042 0.0238 2147 HOH A O 3063 O O . HOH J . ? 0.2263 0.1951 0.2320 -0.0073 0.0236 0.0121 2148 HOH A O 3064 O O A HOH J . ? 0.3387 0.3277 0.3440 0.0012 -0.0050 0.0020 2149 HOH A O 3065 O O B HOH J . ? 0.2979 0.2995 0.3173 -0.0037 -0.0006 -0.0062 2149 HOH A O 3066 O O . HOH J . ? 0.3680 0.3019 0.3443 0.0242 -0.0047 -0.0195 2150 HOH A O 3067 O O . HOH J . ? 0.4634 0.4335 0.4586 -0.0032 0.0015 0.0069 2152 HOH A O 3068 O O . HOH J . ? 0.1568 0.1212 0.2378 -0.0001 0.0125 -0.0129 2153 HOH A O 3069 O O . HOH J . ? 0.2124 0.2117 0.2710 -0.0231 0.0288 -0.0383 2154 HOH A O 3070 O O . HOH J . ? 0.1654 0.2206 0.1613 -0.0334 -0.0269 0.0225 2155 HOH A O 3071 O O . HOH J . ? 0.1883 0.1483 0.3060 -0.0074 0.0405 0.0280 2156 HOH A O 3072 O O . HOH J . ? 0.4124 0.4276 0.4089 0.0186 0.0072 0.0067 2157 HOH A O 3073 O O . HOH J . ? 0.1636 0.1084 0.1330 0.0026 -0.0037 -0.0136 2158 HOH A O 3074 O O . HOH J . ? 0.2916 0.3142 0.2790 0.0307 -0.0214 0.0242 2159 HOH A O 3075 O O . HOH J . ? 0.3045 0.3054 0.3933 0.0184 -0.0114 0.0096 2160 HOH A O 3076 O O . HOH J . ? 0.1232 0.1190 0.1538 -0.0091 -0.0016 0.0104 2161 HOH A O 3077 O O . HOH J . ? 0.4581 0.4353 0.4574 -0.0043 -0.0098 0.0114 2162 HOH A O 3078 O O . HOH J . ? 0.1562 0.1317 0.1381 -0.0047 -0.0024 -0.0148 2163 HOH A O 3079 O O . HOH J . ? 0.1631 0.1215 0.1492 -0.0074 -0.0073 -0.0024 2164 HOH A O 3080 O O . HOH J . ? 0.3857 0.3910 0.4274 0.0098 -0.0091 -0.0114 2165 HOH A O 3081 O O A HOH J . ? 0.2672 0.2419 0.2853 0.0110 0.0067 -0.0034 2166 HOH A O 3082 O O B HOH J . ? 0.2814 0.2059 0.1946 0.0333 -0.0043 -0.0034 2166 HOH A O 3083 O O . HOH J . ? 0.4132 0.4117 0.4189 0.0086 0.0043 0.0008 2167 HOH A O 3084 O O . HOH J . ? 0.2842 0.2771 0.2722 -0.0030 0.0042 -0.0007 2168 HOH A O 3085 O O . HOH J . ? 0.2783 0.2835 0.2370 0.0174 -0.0186 0.0165 2169 HOH A O 3086 O O A HOH J . ? 0.2348 0.2136 0.2746 -0.0007 0.0151 0.0138 2170 HOH A O 3087 O O B HOH J . ? 0.1344 0.1212 0.1803 -0.0188 0.0038 -0.0140 2170 HOH A O 3088 O O . HOH J . ? 0.2211 0.2270 0.2496 -0.0269 -0.0160 -0.0106 2171 HOH A O 3089 O O . HOH J . ? 0.1258 0.1324 0.1465 0.0006 -0.0073 0.0255 2172 HOH A O 3090 O O . HOH J . ? 0.2616 0.2291 0.2786 -0.0016 -0.0318 -0.0112 2173 HOH A O 3091 O O . HOH J . ? 0.3733 0.3918 0.4008 0.0075 0.0079 0.0106 2175 HOH A O 3092 O O . HOH J . ? 0.3797 0.3848 0.3996 -0.0017 -0.0212 0.0016 2176 HOH A O 3093 O O . HOH J . ? 0.4840 0.4728 0.4231 -0.0107 0.0018 0.0004 2177 HOH A O 3094 O O . HOH J . ? 0.1576 0.1640 0.2126 -0.0007 -0.0344 -0.0221 2178 HOH A O 3095 O O . HOH J . ? 0.1572 0.1204 0.1705 -0.0195 0.0109 0.0028 2179 HOH A O 3096 O O . HOH J . ? 0.4518 0.4249 0.4492 -0.0020 0.0054 -0.0112 2180 HOH A O 3097 O O . HOH J . ? 0.4105 0.4382 0.3993 0.0084 0.0005 -0.0173 2181 HOH A O 3098 O O . HOH J . ? 0.1956 0.1552 0.1618 -0.0030 -0.0179 0.0124 2182 HOH A O 3099 O O . HOH J . ? 0.2409 0.2979 0.2014 0.0015 -0.0175 -0.0106 2183 HOH A O 3100 O O A HOH J . ? 0.1928 0.2263 0.3053 -0.0019 -0.0128 -0.0058 2184 HOH A O 3101 O O B HOH J . ? 0.1870 0.1600 0.2298 0.0126 -0.0192 -0.0040 2184 HOH A O 3102 O O . HOH J . ? 0.3071 0.3547 0.3159 -0.0145 0.0025 -0.0066 2186 HOH A O 3103 O O . HOH J . ? 0.2323 0.2782 0.2936 -0.0287 0.0007 0.0053 2187 HOH A O 3104 O O . HOH J . ? 0.2670 0.1993 0.3158 -0.0036 0.0052 0.0171 2188 HOH A O 3105 O O . HOH J . ? 0.2833 0.2343 0.3176 0.0332 0.0028 0.0148 2189 HOH A O 3106 O O . HOH J . ? 0.3877 0.3541 0.4269 -0.0193 0.0076 -0.0045 2190 HOH A O 3107 O O . HOH J . ? 0.4370 0.4588 0.4496 -0.0022 0.0010 -0.0027 2191 HOH A O 3108 O O . HOH J . ? 0.2555 0.2588 0.2709 0.0303 -0.0535 0.0097 2192 HOH A O 3109 O O . HOH J . ? 0.3343 0.3647 0.3640 0.0224 -0.0284 -0.0002 2193 HOH A O 3110 O O . HOH J . ? 0.4990 0.4876 0.4849 0.0098 0.0048 -0.0002 2194 HOH A O 3111 O O . HOH J . ? 0.4396 0.4355 0.4439 -0.0013 -0.0059 -0.0049 2195 HOH A O 3112 O O . HOH J . ? 0.2544 0.2921 0.2350 -0.0342 0.0062 -0.0109 2196 HOH A O 3113 O O . HOH J . ? 0.3840 0.3811 0.4526 -0.0190 -0.0039 -0.0205 2197 HOH A O 3114 O O . HOH J . ? 0.1196 0.1001 0.1311 -0.0101 0.0140 0.0042 2198 HOH A O 3115 O O . HOH J . ? 0.1972 0.1998 0.2425 0.0123 -0.0121 0.0041 2199 HOH A O 3116 O O . HOH J . ? 0.1222 0.0948 0.1674 0.0046 -0.0094 0.0148 2200 HOH A O 3117 O O . HOH J . ? 0.2929 0.2693 0.3390 -0.0379 -0.0023 0.0026 2201 HOH A O 3118 O O . HOH J . ? 0.3568 0.3743 0.3432 0.0192 0.0111 -0.0132 2202 HOH A O 3119 O O . HOH J . ? 0.4285 0.4281 0.4443 0.0073 0.0013 0.0047 2204 HOH A O 3120 O O . HOH J . ? 0.2963 0.2969 0.3361 -0.0377 -0.0249 -0.0278 2205 HOH A O 3121 O O . HOH J . ? 0.3208 0.2567 0.3204 -0.0207 -0.0017 -0.0031 2206 HOH A O 3122 O O . HOH J . ? 0.3906 0.3953 0.4123 0.0197 -0.0220 0.0177 2207 HOH A O 3123 O O . HOH J . ? 0.1528 0.1750 0.2147 -0.0074 0.0294 0.0019 2208 HOH A O 3124 O O . HOH J . ? 0.4154 0.4225 0.4048 0.0025 0.0010 -0.0161 2209 HOH A O 3125 O O . HOH J . ? 0.3234 0.3496 0.3420 0.0240 0.0037 -0.0092 2210 HOH A O 3126 O O . HOH J . ? 0.1221 0.1210 0.1450 0.0074 0.0042 0.0109 2211 HOH A O 3127 O O . HOH J . ? 0.3640 0.3712 0.3467 0.0052 -0.0097 -0.0170 2212 HOH A O 3128 O O . HOH J . ? 0.1503 0.1168 0.2023 -0.0123 0.0112 0.0139 2213 HOH A O 3129 O O . HOH J . ? 0.1818 0.1770 0.2030 -0.0093 0.0119 -0.0023 2214 HOH A O 3130 O O . HOH J . ? 0.4007 0.4157 0.4068 -0.0100 -0.0185 0.0087 2215 HOH A O 3131 O O . HOH J . ? 0.3664 0.2984 0.3159 0.0001 -0.0127 0.0278 2216 HOH A O 3132 O O . HOH J . ? 0.3003 0.2496 0.2458 -0.0406 0.0500 -0.0169 2217 HOH A O 3133 O O . HOH J . ? 0.3233 0.3684 0.3093 -0.0197 0.0117 0.0094 2218 HOH A O 3134 O O . HOH J . ? 0.3353 0.2952 0.3210 0.0375 0.0056 -0.0126 2219 HOH A O 3135 O O . HOH J . ? 0.3153 0.3244 0.2881 -0.0349 -0.0180 -0.0018 2220 HOH A O 3136 O O . HOH J . ? 0.3632 0.2757 0.3287 0.0116 -0.0121 0.0279 2221 HOH A O 3137 O O . HOH J . ? 0.2814 0.3227 0.3326 0.0222 -0.0098 0.0215 2222 HOH A O 3138 O O . HOH J . ? 0.4398 0.3914 0.4007 0.0032 -0.0032 -0.0221 2223 HOH A O 3139 O O . HOH J . ? 0.2209 0.1629 0.2639 -0.0047 0.0096 0.0218 2224 HOH A O 3140 O O . HOH J . ? 0.3045 0.2291 0.2831 -0.0078 -0.0038 -0.0004 2225 HOH A O 3141 O O . HOH J . ? 0.4722 0.4642 0.4591 -0.0013 0.0001 0.0078 2226 HOH A O 3142 O O . HOH J . ? 0.5127 0.5032 0.5104 0.0088 0.0029 0.0013 2227 HOH A O 3143 O O . HOH J . ? 0.1545 0.1464 0.1621 0.0272 0.0250 -0.0215 2228 HOH A O 3144 O O . HOH J . ? 0.3077 0.3541 0.3595 -0.0003 0.0235 -0.0093 2229 HOH A O 3145 O O . HOH J . ? 0.1608 0.1352 0.1668 0.0124 0.0151 -0.0250 2230 HOH A O 3146 O O . HOH J . ? 0.4221 0.3830 0.3830 0.0122 -0.0112 0.0080 2232 HOH A O 3147 O O . HOH J . ? 0.3739 0.3080 0.3377 0.0023 0.0116 0.0031 2233 HOH A O 3148 O O A HOH J . ? 0.1823 0.2415 0.1988 -0.0113 -0.0082 -0.0070 2234 HOH A O 3149 O O B HOH J . ? 0.2556 0.2822 0.2744 0.0045 0.0061 0.0011 2234 HOH A O 3150 O O . HOH J . ? 0.3963 0.4220 0.3995 -0.0050 0.0085 -0.0106 2236 HOH A O 3151 O O . HOH J . ? 0.5031 0.5007 0.5140 -0.0007 -0.0064 0.0001 2237 HOH A O 3152 O O . HOH J . ? 0.3062 0.2138 0.1937 0.0023 -0.0151 0.0297 2238 HOH A O 3153 O O . HOH J . ? 0.2078 0.1744 0.1861 0.0105 0.0334 0.0070 2239 HOH A O 3154 O O . HOH J . ? 0.3572 0.2810 0.3362 0.0088 0.0033 -0.0138 2240 HOH A O 3155 O O . HOH J . ? 0.3206 0.2825 0.3005 0.0168 0.0053 0.0020 2241 HOH A O 3156 O O A HOH J . ? 0.1692 0.2111 0.2015 0.0038 -0.0016 -0.0023 2242 HOH A O 3157 O O B HOH J . ? 0.2009 0.1666 0.1495 -0.0045 0.0004 -0.0170 2242 HOH A O 3158 O O . HOH J . ? 0.2141 0.1264 0.2024 0.0034 0.0267 0.0196 2244 HOH A O 3159 O O . HOH J . ? 0.3464 0.2875 0.2773 0.0169 -0.0102 -0.0109 2245 HOH A O 3160 O O . HOH J . ? 0.3940 0.3532 0.3691 -0.0239 0.0055 0.0142 2246 HOH A O 3161 O O . HOH J . ? 0.1934 0.1842 0.1536 -0.0168 -0.0031 -0.0254 2247 HOH A O 3162 O O . HOH J . ? 0.2006 0.2018 0.1753 0.0057 -0.0123 -0.0056 2248 HOH A O 3163 O O . HOH J . ? 0.1329 0.0773 0.1390 0.0171 0.0105 -0.0015 2249 HOH A O 3164 O O . HOH J . ? 0.1484 0.1611 0.2225 0.0164 0.0031 0.0063 2250 HOH A O 3165 O O . HOH J . ? 0.1934 0.1689 0.1920 0.0182 0.0093 0.0178 2251 HOH A O 3166 O O . HOH J . ? 0.1483 0.2676 0.1230 -0.0022 0.0187 -0.0335 2252 HOH A O 3167 O O . HOH J . ? 0.1340 0.0973 0.1282 0.0152 0.0101 0.0076 2253 HOH A O 3168 O O . HOH J . ? 0.1557 0.1554 0.1755 0.0064 0.0207 -0.0103 2254 HOH A O 3169 O O . HOH J . ? 0.2034 0.2988 0.3071 -0.0141 -0.0048 -0.0031 2255 HOH A O 3170 O O . HOH J . ? 0.2489 0.2210 0.2363 0.0010 -0.0062 0.0073 2256 HOH A O 3171 O O . HOH J . ? 0.2309 0.2647 0.2260 0.0373 0.0082 0.0460 2257 HOH A O 3172 O O . HOH J . ? 0.1429 0.2006 0.1900 0.0148 -0.0111 0.0074 2258 HOH A O 3173 O O . HOH J . ? 0.3050 0.3685 0.3493 0.0072 0.0169 0.0111 2259 HOH A O 3174 O O . HOH J . ? 0.3958 0.3740 0.3411 0.0097 0.0015 -0.0034 2260 HOH A O 3175 O O . HOH J . ? 0.4268 0.3746 0.4152 0.0152 0.0020 -0.0015 2261 HOH A O 3176 O O . HOH J . ? 0.3116 0.3029 0.2442 0.0081 -0.0007 -0.0517 2262 HOH A O 3177 O O . HOH J . ? 0.3146 0.3135 0.3225 -0.0044 0.0101 0.0190 2263 HOH A O 3178 O O . HOH J . ? 0.2916 0.2508 0.2633 -0.0006 -0.0177 -0.0217 2264 HOH A O 3179 O O . HOH J . ? 0.4011 0.3880 0.4221 0.0000 0.0045 -0.0062 2265 HOH A O 3180 O O . HOH J . ? 0.1788 0.2003 0.2402 0.0048 0.0146 -0.0057 2266 HOH A O 3181 O O . HOH J . ? 0.4875 0.4686 0.4951 0.0013 -0.0055 0.0143 2267 HOH A O 3182 O O . HOH J . ? 0.3601 0.2961 0.3724 -0.0041 0.0123 0.0206 2268 HOH A O 3183 O O . HOH J . ? 0.4379 0.4454 0.4413 0.0148 0.0012 0.0018 2269 HOH A O 3184 O O . HOH J . ? 0.2706 0.2643 0.2813 0.0414 0.0122 0.0113 2270 HOH A O 3185 O O . HOH J . ? 0.3975 0.3751 0.3967 0.0101 -0.0031 0.0072 2271 HOH A O 3186 O O . HOH J . ? 0.4698 0.4652 0.4548 0.0100 0.0067 0.0068 2272 HOH A O 3187 O O . HOH J . ? 0.5015 0.4899 0.5186 0.0030 -0.0063 -0.0080 2273 HOH A O 3188 O O . HOH J . ? 0.4133 0.4217 0.4467 0.0013 -0.0015 -0.0055 2274 HOH A O 3189 O O . HOH J . ? 0.3129 0.2410 0.2400 0.0217 -0.0268 -0.0174 2275 HOH A O 3190 O O . HOH J . ? 0.2363 0.2071 0.3037 -0.0460 -0.0098 -0.0350 2276 HOH A O 3191 O O . HOH J . ? 0.3319 0.2926 0.3625 -0.0121 0.0193 -0.0020 2277 HOH A O 3192 O O . HOH J . ? 0.3681 0.3263 0.3263 -0.0061 -0.0088 0.0322 2278 HOH A O 3193 O O . HOH J . ? 0.3269 0.2621 0.3574 -0.0083 -0.0063 -0.0188 2279 HOH A O 3194 O O . HOH J . ? 0.2634 0.2575 0.2599 0.0432 0.0292 0.0134 2281 HOH A O 3195 O O . HOH J . ? 0.2577 0.3261 0.2754 -0.0108 0.0040 -0.0035 2282 HOH A O 3196 O O . HOH J . ? 0.1496 0.1914 0.1632 0.0113 0.0210 0.0235 2283 HOH A O 3197 O O . HOH J . ? 0.2610 0.3420 0.2223 0.0118 0.0164 0.0191 2284 HOH A O 3198 O O . HOH J . ? 0.4044 0.3662 0.3741 0.0003 -0.0005 0.0052 2285 HOH A O 3199 O O . HOH J . ? 0.3644 0.3971 0.3362 0.0115 -0.0078 0.0004 2286 HOH A O 3200 O O . HOH J . ? 0.4626 0.4767 0.4435 -0.0069 -0.0047 0.0061 2287 HOH A O 3201 O O . HOH J . ? 0.3539 0.3402 0.3072 -0.0116 0.0071 -0.0015 2288 HOH A O 3202 O O . HOH J . ? 0.2380 0.2225 0.3187 0.0125 0.0329 -0.0057 2289 HOH A O 3203 O O . HOH J . ? 0.3582 0.3046 0.3180 0.0345 0.0168 0.0271 2290 HOH A O 3204 O O . HOH J . ? 0.2767 0.2753 0.2737 0.0106 0.0425 0.0234 2291 HOH A O 3205 O O . HOH J . ? 0.3441 0.3471 0.3600 -0.0227 0.0009 0.0076 2292 HOH A O 3206 O O . HOH J . ? 0.2808 0.3112 0.2646 -0.0347 -0.0296 -0.0053 2293 HOH A O 3207 O O . HOH J . ? 0.1467 0.1865 0.1610 0.0093 -0.0075 0.0368 2294 HOH A O 3208 O O . HOH J . ? 0.3875 0.4165 0.4212 -0.0048 -0.0012 -0.0278 2295 HOH A O 3209 O O . HOH J . ? 0.2205 0.2606 0.3200 0.0272 0.0079 0.0369 2296 HOH A O 3210 O O . HOH J . ? 0.1378 0.1906 0.1846 0.0052 0.0095 0.0259 2298 HOH A O 3211 O O . HOH J . ? 0.2073 0.2777 0.2446 -0.0218 0.0154 -0.0194 2299 HOH A O 3212 O O . HOH J . ? 0.3100 0.3235 0.3201 -0.0105 0.0074 -0.0348 2300 HOH A O 3213 O O . HOH J . ? 0.1680 0.2219 0.2048 -0.0451 -0.0322 -0.0183 2301 HOH A O 3214 O O . HOH J . ? 0.3372 0.3379 0.3575 -0.0099 0.0049 0.0074 2302 HOH A O 3215 O O . HOH J . ? 0.3964 0.4033 0.3766 -0.0043 -0.0064 0.0126 2303 HOH A O 3216 O O . HOH J . ? 0.3255 0.3388 0.3470 -0.0070 0.0016 -0.0281 2304 HOH A O 3217 O O . HOH J . ? 0.2492 0.2716 0.2938 0.0016 -0.0226 -0.0242 2305 HOH A O 3218 O O . HOH J . ? 0.2520 0.3029 0.3077 0.0039 -0.0133 -0.0315 2306 HOH A O 3219 O O . HOH J . ? 0.3016 0.3628 0.3101 -0.0181 0.0080 -0.0011 2307 HOH A O 3220 O O . HOH J . ? 0.3488 0.3492 0.4189 -0.0071 0.0000 -0.0076 2308 HOH A O 3221 O O . HOH J . ? 0.2950 0.2011 0.2584 -0.0455 0.0012 0.0206 2309 HOH A O 3222 O O . HOH J . ? 0.4237 0.3699 0.4161 0.0073 0.0014 0.0054 2310 HOH A O 3223 O O . HOH J . ? 0.5315 0.5384 0.5269 -0.0042 0.0042 0.0058 2311 HOH A O 3224 O O . HOH J . ? 0.3468 0.3471 0.3671 0.0091 0.0008 0.0100 2312 HOH A O 3225 O O . HOH J . ? 0.2927 0.3441 0.3246 -0.0074 0.0184 -0.0009 2313 HOH A O 3226 O O . HOH J . ? 0.5169 0.5033 0.4952 -0.0030 0.0034 0.0019 2314 HOH A O 3227 O O . HOH J . ? 0.3438 0.3795 0.3313 -0.0225 0.0063 0.0100 2315 HOH A O 3228 O O . HOH J . ? 0.4034 0.3628 0.3732 -0.0048 0.0101 0.0031 2316 HOH A O 3229 O O . HOH J . ? 0.4478 0.4350 0.4594 0.0014 0.0116 0.0029 2317 HOH A O 3230 O O . HOH J . ? 0.1926 0.1580 0.2144 -0.0129 -0.0165 -0.0210 2318 HOH A O 3231 O O . HOH J . ? 0.2623 0.3054 0.3045 -0.0191 0.0256 0.0147 2319 HOH A O 3232 O O . HOH J . ? 0.4000 0.3875 0.4456 -0.0057 -0.0019 -0.0007 2320 HOH A O 3233 O O . HOH J . ? 0.1638 0.2112 0.1409 0.0023 -0.0054 -0.0237 2321 HOH A O 3234 O O . HOH J . ? 0.1654 0.2641 0.1871 -0.0068 0.0130 0.0220 2322 HOH A O 3235 O O . HOH J . ? 0.1467 0.1551 0.0798 -0.0058 -0.0095 0.0296 2323 HOH A O 3236 O O . HOH J . ? 0.1119 0.1558 0.0897 0.0012 0.0186 0.0085 2324 HOH A O 3237 O O . HOH J . ? 0.2672 0.2811 0.3232 0.0097 -0.0360 -0.0130 2325 HOH A O 3238 O O . HOH J . ? 0.1259 0.1826 0.0923 0.0097 -0.0223 0.0309 2326 HOH A O 3239 O O . HOH J . ? 0.1284 0.1656 0.1288 -0.0041 -0.0118 0.0198 2327 HOH A O 3240 O O . HOH J . ? 0.3928 0.4003 0.3678 -0.0012 0.0034 -0.0055 2328 HOH A O 3241 O O . HOH J . ? 0.3413 0.3588 0.3269 -0.0003 -0.0107 -0.0248 2329 HOH A O 3242 O O . HOH J . ? 0.3294 0.3717 0.2784 0.0008 -0.0103 0.0171 2330 HOH A O 3243 O O . HOH J . ? 0.2847 0.2930 0.3074 0.0195 0.0237 0.0301 2331 HOH A O 3244 O O . HOH J . ? 0.3625 0.3631 0.3696 0.0108 -0.0088 0.0317 2332 HOH A O 3245 O O . HOH J . ? 0.1421 0.1667 0.1711 0.0058 -0.0146 0.0210 2333 HOH A O 3246 O O . HOH J . ? 0.4356 0.4924 0.4760 -0.0056 -0.0035 -0.0005 2334 HOH A O 3247 O O . HOH J . ? 0.4668 0.4354 0.4678 0.0084 0.0008 0.0018 2335 HOH A O 3248 O O . HOH J . ? 0.4470 0.4316 0.4474 -0.0043 -0.0114 0.0000 2336 HOH A O 3249 O O . HOH J . ? 0.2785 0.2856 0.2831 0.0124 0.0126 0.0036 2337 HOH A O 3250 O O . HOH J . ? 0.2497 0.2157 0.2581 -0.0069 0.0047 0.0112 2338 HOH A O 3251 O O . HOH J . ? 0.5083 0.5154 0.5127 0.0029 0.0026 0.0038 2339 HOH A O 3252 O O . HOH J . ? 0.3204 0.3333 0.3304 -0.0152 -0.0042 -0.0052 2340 HOH A O 3253 O O . HOH J . ? 0.2310 0.1858 0.2406 -0.0339 0.0109 0.0238 2341 HOH A O 3254 O O . HOH J . ? 0.2964 0.2806 0.2538 0.0158 -0.0280 0.0108 2342 HOH A O 3255 O O . HOH J . ? 0.3770 0.3609 0.3238 0.0076 -0.0082 0.0191 2343 HOH A O 3256 O O . HOH J . ? 0.2227 0.2654 0.2763 0.0142 -0.0074 0.0328 2344 HOH A O 3257 O O . HOH J . ? 0.4583 0.4333 0.4175 0.0074 -0.0024 -0.0027 2345 HOH A O 3258 O O . HOH J . ? 0.3009 0.2917 0.2609 0.0067 -0.0165 -0.0187 2346 HOH A O 3259 O O . HOH J . ? 0.2235 0.2380 0.2106 0.0220 -0.0377 -0.0431 2347 HOH A O 3260 O O . HOH J . ? 0.3529 0.3561 0.3039 0.0086 0.0193 -0.0278 2348 HOH A O 3261 O O . HOH J . ? 0.2542 0.3134 0.2593 0.0370 0.0373 -0.0081 2349 HOH A O 3262 O O . HOH J . ? 0.2915 0.3232 0.2940 0.0424 0.0028 -0.0443 2350 HOH A O 3263 O O . HOH J . ? 0.2500 0.2575 0.2804 -0.0058 0.0028 -0.0273 2351 HOH A O 3264 O O . HOH J . ? 0.5083 0.4826 0.5158 0.0000 -0.0037 -0.0001 2352 HOH A O 3265 O O A HOH J . ? 0.3225 0.2992 0.2958 -0.0012 0.0107 0.0072 2353 HOH A O 3266 O O B HOH J . ? 0.2943 0.2715 0.2799 -0.0066 0.0187 0.0200 2353 HOH A O 3267 O O A HOH J . ? 0.2907 0.2440 0.2418 0.0229 0.0122 -0.0333 2354 HOH A O 3268 O O B HOH J . ? 0.2660 0.2466 0.2792 -0.0236 -0.0138 -0.0244 2354 HOH A O 3269 O O . HOH J . ? 0.3222 0.2684 0.2561 -0.0130 -0.0382 -0.0285 2355 HOH A O 3270 O O . HOH J . ? 0.4986 0.4863 0.4819 0.0013 -0.0046 0.0027 2356 HOH A O 3271 O O . HOH J . ? 0.4384 0.4457 0.4408 0.0154 0.0143 0.0037 2357 HOH A O 3272 O O . HOH J . ? 0.3159 0.3438 0.3772 0.0173 -0.0061 -0.0011 2358 HOH A O 3273 O O . HOH J . ? 0.3721 0.3698 0.3781 -0.0013 -0.0048 -0.0108 2359 HOH A O 3274 O O . HOH J . ? 0.2890 0.2913 0.3003 -0.0340 -0.0049 0.0164 2360 HOH A O 3275 O O . HOH J . ? 0.2721 0.2427 0.2905 -0.0170 0.0174 -0.0059 2361 HOH A O 3276 O O . HOH J . ? 0.2275 0.1730 0.2287 -0.0227 0.0074 -0.0080 2362 HOH A O 3277 O O . HOH J . ? 0.2853 0.2830 0.2896 0.0091 0.0289 0.0077 2363 HOH A O 3278 O O . HOH J . ? 0.2727 0.2116 0.2435 -0.0274 0.0056 -0.0256 2364 HOH A O 3279 O O . HOH J . ? 0.1465 0.1357 0.1109 0.0022 -0.0020 0.0160 2365 HOH A O 3280 O O . HOH J . ? 0.1696 0.2421 0.1584 -0.0167 -0.0048 0.0474 2366 HOH A O 3281 O O . HOH J . ? 0.2392 0.2918 0.2263 -0.0120 -0.0081 0.0207 2367 HOH A O 3282 O O . HOH J . ? 0.3027 0.2997 0.2380 -0.0343 -0.0077 0.0187 2368 HOH A O 3283 O O . HOH J . ? 0.2418 0.1764 0.2411 -0.0265 -0.0130 0.0258 2369 HOH A O 3284 O O . HOH J . ? 0.4330 0.3925 0.4263 -0.0081 0.0058 0.0119 2370 HOH A O 3285 O O . HOH J . ? 0.4060 0.4240 0.3872 -0.0147 0.0041 0.0092 2371 HOH A O 3286 O O . HOH J . ? 0.5092 0.4929 0.5058 -0.0049 0.0053 0.0135 2372 HOH A O 3287 O O . HOH J . ? 0.4703 0.4487 0.4312 -0.0075 0.0010 0.0157 2373 HOH A O 3288 O O . HOH J . ? 0.3296 0.3147 0.3041 -0.0203 -0.0054 -0.0022 2374 HOH A O 3289 O O . HOH J . ? 0.3184 0.2323 0.2501 -0.0426 0.0022 0.0129 2375 HOH A O 3290 O O . HOH J . ? 0.3303 0.3071 0.3193 -0.0299 0.0020 0.0123 2376 HOH A O 3291 O O . HOH J . ? 0.4155 0.3931 0.4332 0.0207 0.0151 -0.0286 2377 HOH A O 3292 O O . HOH J . ? 0.4232 0.4194 0.3801 -0.0005 -0.0178 -0.0076 2378 HOH A O 3293 O O . HOH J . ? 0.3280 0.2910 0.3051 -0.0005 0.0056 0.0268 2379 HOH A O 3294 O O . HOH J . ? 0.3941 0.4343 0.4329 0.0085 -0.0058 0.0089 2380 HOH A O 3295 O O . HOH J . ? 0.2142 0.1470 0.2724 -0.0244 -0.0041 0.0330 2382 HOH A O 3296 O O . HOH J . ? 0.2226 0.2130 0.1650 -0.0150 -0.0345 0.0455 2383 HOH A O 3297 O O . HOH J . ? 0.4747 0.4834 0.4925 0.0081 -0.0017 0.0102 2384 HOH A O 3298 O O . HOH J . ? 0.3013 0.2776 0.3086 0.0007 0.0205 0.0245 2385 HOH A O 3299 O O . HOH J . ? 0.4701 0.4827 0.4392 -0.0042 -0.0137 0.0066 2386 HOH A O 3300 O O . HOH J . ? 0.4215 0.3882 0.3865 -0.0064 0.0067 -0.0063 2388 HOH A O 3301 O O . HOH J . ? 0.3195 0.3374 0.3721 0.0147 -0.0038 0.0060 2389 HOH A O 3302 O O . HOH J . ? 0.4373 0.4073 0.4004 -0.0186 -0.0056 0.0221 2390 HOH A O 3303 O O . HOH J . ? 0.3834 0.4049 0.3650 -0.0286 -0.0010 0.0212 2391 HOH A O 3304 O O . HOH J . ? 0.3376 0.3258 0.3241 -0.0313 -0.0025 0.0161 2392 HOH A O 3305 O O . HOH J . ? 0.3228 0.2404 0.2250 -0.0056 -0.0194 0.0376 2393 HOH A O 3306 O O . HOH J . ? 0.4523 0.4746 0.4651 0.0055 -0.0047 0.0024 2394 HOH A O 3307 O O . HOH J . ? 0.4563 0.4611 0.4619 -0.0142 0.0000 0.0021 2395 HOH A O 3308 O O . HOH J . ? 0.3128 0.4057 0.3619 -0.0017 -0.0083 0.0120 2396 HOH A O 3309 O O . HOH J . ? 0.3018 0.3808 0.3379 -0.0204 -0.0041 0.0167 2397 HOH A O 3310 O O . HOH J . ? 0.2538 0.3274 0.2883 -0.0234 0.0062 0.0332 2398 HOH A O 3311 O O . HOH J . ? 0.5131 0.5119 0.5293 -0.0055 -0.0070 0.0003 2399 HOH A O 3312 O O . HOH J . ? 0.3377 0.3245 0.2653 0.0156 -0.0325 0.0260 2400 HOH A O 3313 O O . HOH J . ? 0.3395 0.3224 0.2886 -0.0052 -0.0074 0.0286 2401 HOH A O 3314 O O . HOH J . ? 0.4591 0.4203 0.4474 0.0000 0.0026 0.0048 2402 HOH A O 3315 O O . HOH J . ? 0.4240 0.4234 0.3892 0.0014 -0.0136 0.0075 2403 HOH A O 3316 O O . HOH J . ? 0.3631 0.4191 0.3997 0.0034 -0.0072 0.0156 2405 HOH A O 3317 O O . HOH J . ? 0.3967 0.3737 0.2468 -0.0010 -0.0107 0.0057 2406 HOH A O 3318 O O . HOH J . ? 0.4732 0.4723 0.4677 -0.0024 -0.0004 -0.0067 2407 HOH A O 3319 O O . HOH J . ? 0.2479 0.2918 0.1811 0.0142 -0.0160 0.0076 2408 HOH A O 3320 O O . HOH J . ? 0.4661 0.4417 0.4063 0.0089 0.0083 0.0030 2409 HOH A O 3321 O O . HOH J . ? 0.4263 0.4364 0.4567 -0.0149 0.0023 -0.0051 2410 HOH A O 3322 O O . HOH J . ? 0.3084 0.3648 0.3488 -0.0046 0.0167 -0.0166 2411 HOH A O 3323 O O . HOH J . ? 0.3095 0.2958 0.3798 0.0040 -0.0082 -0.0053 2412 HOH A O 3324 O O . HOH J . ? 0.2884 0.2831 0.2872 -0.0179 -0.0036 -0.0051 2413 HOH A O 3325 O O . HOH J . ? 0.3994 0.4162 0.3822 0.0107 0.0028 0.0032 2414 HOH A O 3326 O O . HOH J . ? 0.3424 0.3562 0.3001 -0.0149 -0.0029 0.0046 2415 HOH A O 3327 O O . HOH J . ? 0.3547 0.3707 0.3895 -0.0162 0.0067 -0.0147 2416 HOH A O 3328 O O . HOH J . ? 0.3305 0.2984 0.3203 0.0070 0.0019 -0.0017 2417 HOH A O 3329 O O . HOH J . ? 0.1783 0.1739 0.1763 -0.0065 0.0224 0.0216 2418 HOH A O 3330 O O . HOH J . ? 0.4764 0.4534 0.4888 0.0129 0.0025 0.0021 2419 HOH A O 3331 O O . HOH J . ? 0.3375 0.2882 0.3464 -0.0021 -0.0034 0.0101 2420 HOH A O # 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 TYR 1 89 ? ? ? A . n A 1 2 ASN 2 90 ? ? ? A . n A 1 3 GLY 3 91 91 GLY GLY A . n A 1 4 ASN 4 92 92 ASN ASN A . n A 1 5 PRO 5 93 93 PRO PRO A . n A 1 6 PHE 6 94 94 PHE PHE A . n A 1 7 GLU 7 95 95 GLU GLU A . n A 1 8 GLY 8 96 96 GLY GLY A . n A 1 9 VAL 9 97 97 VAL VAL A . n A 1 10 GLN 10 98 98 GLN GLN A . n A 1 11 LEU 11 99 99 LEU LEU A . n A 1 12 TRP 12 100 100 TRP TRP A . n A 1 13 ALA 13 101 101 ALA ALA A . n A 1 14 ASN 14 102 102 ASN ASN A . n A 1 15 ASN 15 103 103 ASN ASN A . n A 1 16 TYR 16 104 104 TYR TYR A . n A 1 17 TYR 17 105 105 TYR TYR A . n A 1 18 ARG 18 106 106 ARG ARG A . n A 1 19 SER 19 107 107 SER SER A . n A 1 20 GLU 20 108 108 GLU GLU A . n A 1 21 VAL 21 109 109 VAL VAL A . n A 1 22 HIS 22 110 110 HIS HIS A . n A 1 23 THR 23 111 111 THR THR A . n A 1 24 LEU 24 112 112 LEU LEU A . n A 1 25 ALA 25 113 113 ALA ALA A . n A 1 26 ILE 26 114 114 ILE ILE A . n A 1 27 PRO 27 115 115 PRO PRO A . n A 1 28 GLN 28 116 116 GLN GLN A . n A 1 29 ILE 29 117 117 ILE ILE A . n A 1 30 THR 30 118 118 THR THR A . n A 1 31 ASP 31 119 119 ASP ASP A . n A 1 32 PRO 32 120 120 PRO PRO A . n A 1 33 ALA 33 121 121 ALA ALA A . n A 1 34 LEU 34 122 122 LEU LEU A . n A 1 35 ARG 35 123 123 ARG ARG A . n A 1 36 ALA 36 124 124 ALA ALA A . n A 1 37 ALA 37 125 125 ALA ALA A . n A 1 38 ALA 38 126 126 ALA ALA A . n A 1 39 SER 39 127 127 SER SER A . n A 1 40 ALA 40 128 128 ALA ALA A . n A 1 41 VAL 41 129 129 VAL VAL A . n A 1 42 ALA 42 130 130 ALA ALA A . n A 1 43 GLU 43 131 131 GLU GLU A . n A 1 44 VAL 44 132 132 VAL VAL A . n A 1 45 PRO 45 133 133 PRO PRO A . n A 1 46 SER 46 134 134 SER SER A . n A 1 47 PHE 47 135 135 PHE PHE A . n A 1 48 GLN 48 136 136 GLN GLN A . n A 1 49 TRP 49 137 137 TRP TRP A . n A 1 50 LEU 50 138 138 LEU LEU A . n A 1 51 ASP 51 139 139 ASP ASP A . n A 1 52 ARG 52 140 140 ARG ARG A . n A 1 53 ASN 53 141 141 ASN ASN A . n A 1 54 VAL 54 142 142 VAL VAL A . n A 1 55 THR 55 143 143 THR THR A . n A 1 56 VAL 56 144 144 VAL VAL A . n A 1 57 ASP 57 145 145 ASP ASP A . n A 1 58 THR 58 146 146 THR THR A . n A 1 59 LEU 59 147 147 LEU LEU A . n A 1 60 LEU 60 148 148 LEU LEU A . n A 1 61 VAL 61 149 149 VAL VAL A . n A 1 62 GLN 62 150 150 GLN GLN A . n A 1 63 THR 63 151 151 THR THR A . n A 1 64 LEU 64 152 152 LEU LEU A . n A 1 65 SER 65 153 153 SER SER A . n A 1 66 GLU 66 154 154 GLU GLU A . n A 1 67 ILE 67 155 155 ILE ILE A . n A 1 68 ARG 68 156 156 ARG ARG A . n A 1 69 GLU 69 157 157 GLU GLU A . n A 1 70 ALA 70 158 158 ALA ALA A . n A 1 71 ASN 71 159 159 ASN ASN A . n A 1 72 GLN 72 160 160 GLN GLN A . n A 1 73 ALA 73 161 161 ALA ALA A . n A 1 74 GLY 74 162 162 GLY GLY A . n A 1 75 ALA 75 163 163 ALA ALA A . n A 1 76 ASN 76 164 164 ASN ASN A . n A 1 77 PRO 77 165 165 PRO PRO A . n A 1 78 GLN 78 166 166 GLN GLN A . n A 1 79 TYR 79 167 167 TYR TYR A . n A 1 80 ALA 80 168 168 ALA ALA A . n A 1 81 ALA 81 169 169 ALA ALA A . n A 1 82 GLN 82 170 170 GLN GLN A . n A 1 83 ILE 83 171 171 ILE ILE A . n A 1 84 VAL 84 172 172 VAL VAL A . n A 1 85 VAL 85 173 173 VAL VAL A . n A 1 86 TYR 86 174 174 TYR TYR A . n A 1 87 ASP 87 175 175 ASP ASP A . n A 1 88 LEU 88 176 176 LEU LEU A . n A 1 89 PRO 89 177 177 PRO PRO A . n A 1 90 ASP 90 178 178 ASP ASP A . n A 1 91 ARG 91 179 179 ARG ARG A . n A 1 92 ASP 92 180 180 ASP ASP A . n A 1 93 CYS 93 181 181 CYS CYS A . n A 1 94 ALA 94 182 182 ALA ALA A . n A 1 95 ALA 95 183 183 ALA ALA A . n A 1 96 ALA 96 184 184 ALA ALA A . n A 1 97 ALA 97 185 185 ALA ALA A . n A 1 98 SER 98 186 186 SER SER A . n A 1 99 ASN 99 187 187 ASN ASN A . n A 1 100 GLY 100 188 188 GLY GLY A . n A 1 101 GLU 101 189 189 GLU GLU A . n A 1 102 TRP 102 190 190 TRP TRP A . n A 1 103 ALA 103 191 191 ALA ALA A . n A 1 104 ILE 104 192 192 ILE ILE A . n A 1 105 ALA 105 193 193 ALA ALA A . n A 1 106 ASN 106 194 194 ASN ASN A . n A 1 107 ASN 107 195 195 ASN ASN A . n A 1 108 GLY 108 196 196 GLY GLY A . n A 1 109 VAL 109 197 197 VAL VAL A . n A 1 110 ASN 110 198 198 ASN ASN A . n A 1 111 ASN 111 199 199 ASN ASN A . n A 1 112 TYR 112 200 200 TYR TYR A . n A 1 113 LYS 113 201 201 LYS LYS A . n A 1 114 ALA 114 202 202 ALA ALA A . n A 1 115 TYR 115 203 203 TYR TYR A . n A 1 116 ILE 116 204 204 ILE ILE A . n A 1 117 ASN 117 205 205 ASN ASN A . n A 1 118 ARG 118 206 206 ARG ARG A . n A 1 119 ILE 119 207 207 ILE ILE A . n A 1 120 ARG 120 208 208 ARG ARG A . n A 1 121 GLU 121 209 209 GLU GLU A . n A 1 122 ILE 122 210 210 ILE ILE A . n A 1 123 LEU 123 211 211 LEU LEU A . n A 1 124 ILE 124 212 212 ILE ILE A . n A 1 125 SER 125 213 213 SER SER A . n A 1 126 PHE 126 214 214 PHE PHE A . n A 1 127 SER 127 215 215 SER SER A . n A 1 128 ASP 128 216 216 ASP ASP A . n A 1 129 VAL 129 217 217 VAL VAL A . n A 1 130 ARG 130 218 218 ARG ARG A . n A 1 131 THR 131 219 219 THR THR A . n A 1 132 ILE 132 220 220 ILE ILE A . n A 1 133 LEU 133 221 221 LEU LEU A . n A 1 134 VAL 134 222 222 VAL VAL A . n A 1 135 ILE 135 223 223 ILE ILE A . n A 1 136 GLU 136 224 224 GLU GLU A . n A 1 137 PRO 137 225 225 PRO PRO A . n A 1 138 ASP 138 226 226 ASP ASP A . n A 1 139 SER 139 227 227 SER SER A . n A 1 140 LEU 140 228 228 LEU LEU A . n A 1 141 ALA 141 229 229 ALA ALA A . n A 1 142 ASN 142 230 230 ASN ASN A . n A 1 143 MET 143 231 231 MET MET A . n A 1 144 VAL 144 232 232 VAL VAL A . n A 1 145 THR 145 233 233 THR THR A . n A 1 146 ASN 146 234 234 ASN ASN A . n A 1 147 MET 147 235 235 MET MET A . n A 1 148 ASN 148 236 236 ASN ASN A . n A 1 149 VAL 149 237 237 VAL VAL A . n A 1 150 PRO 150 238 238 PRO PRO A . n A 1 151 LYS 151 239 239 LYS LYS A . n A 1 152 CYS 152 240 240 CYS CYS A . n A 1 153 SER 153 241 241 SER SER A . n A 1 154 GLY 154 242 242 GLY GLY A . n A 1 155 ALA 155 243 243 ALA ALA A . n A 1 156 ALA 156 244 244 ALA ALA A . n A 1 157 SER 157 245 245 SER SER A . n A 1 158 THR 158 246 246 THR THR A . n A 1 159 TYR 159 247 247 TYR TYR A . n A 1 160 ARG 160 248 248 ARG ARG A . n A 1 161 GLU 161 249 249 GLU GLU A . n A 1 162 LEU 162 250 250 LEU LEU A . n A 1 163 THR 163 251 251 THR THR A . n A 1 164 ILE 164 252 252 ILE ILE A . n A 1 165 TYR 165 253 253 TYR TYR A . n A 1 166 ALA 166 254 254 ALA ALA A . n A 1 167 LEU 167 255 255 LEU LEU A . n A 1 168 LYS 168 256 256 LYS LYS A . n A 1 169 GLN 169 257 257 GLN GLN A . n A 1 170 LEU 170 258 258 LEU LEU A . n A 1 171 ASP 171 259 259 ASP ASP A . n A 1 172 LEU 172 260 260 LEU LEU A . n A 1 173 PRO 173 261 261 PRO PRO A . n A 1 174 HIS 174 262 262 HIS HIS A . n A 1 175 VAL 175 263 263 VAL VAL A . n A 1 176 ALA 176 264 264 ALA ALA A . n A 1 177 MET 177 265 265 MET MET A . n A 1 178 TYR 178 266 266 TYR TYR A . n A 1 179 MET 179 267 267 MET MET A . n A 1 180 ASP 180 268 268 ASP ASP A . n A 1 181 ALA 181 269 269 ALA ALA A . n A 1 182 GLY 182 270 270 GLY GLY A . n A 1 183 HIS 183 271 271 HIS HIS A . n A 1 184 ALA 184 272 272 ALA ALA A . n A 1 185 GLY 185 273 273 GLY GLY A . n A 1 186 TRP 186 274 274 TRP TRP A . n A 1 187 LEU 187 275 275 LEU LEU A . n A 1 188 GLY 188 276 276 GLY GLY A . n A 1 189 TRP 189 277 277 TRP TRP A . n A 1 190 PRO 190 278 278 PRO PRO A . n A 1 191 ALA 191 279 279 ALA ALA A . n A 1 192 ASN 192 280 280 ASN ASN A . n A 1 193 ILE 193 281 281 ILE ILE A . n A 1 194 GLN 194 282 282 GLN GLN A . n A 1 195 PRO 195 283 283 PRO PRO A . n A 1 196 ALA 196 284 284 ALA ALA A . n A 1 197 ALA 197 285 285 ALA ALA A . n A 1 198 GLU 198 286 286 GLU GLU A . n A 1 199 LEU 199 287 287 LEU LEU A . n A 1 200 PHE 200 288 288 PHE PHE A . n A 1 201 ALA 201 289 289 ALA ALA A . n A 1 202 LYS 202 290 290 LYS LYS A . n A 1 203 ILE 203 291 291 ILE ILE A . n A 1 204 TYR 204 292 292 TYR TYR A . n A 1 205 GLU 205 293 293 GLU GLU A . n A 1 206 ASP 206 294 294 ASP ASP A . n A 1 207 ALA 207 295 295 ALA ALA A . n A 1 208 GLY 208 296 296 GLY GLY A . n A 1 209 LYS 209 297 297 LYS LYS A . n A 1 210 PRO 210 298 298 PRO PRO A . n A 1 211 ARG 211 299 299 ARG ARG A . n A 1 212 ALA 212 300 300 ALA ALA A . n A 1 213 VAL 213 301 301 VAL VAL A . n A 1 214 ARG 214 302 302 ARG ARG A . n A 1 215 GLY 215 303 303 GLY GLY A . n A 1 216 LEU 216 304 304 LEU LEU A . n A 1 217 ALA 217 305 305 ALA ALA A . n A 1 218 THR 218 306 306 THR THR A . n A 1 219 ASN 219 307 307 ASN ASN A . n A 1 220 VAL 220 308 308 VAL VAL A . n A 1 221 ALA 221 309 309 ALA ALA A . n A 1 222 ASN 222 310 310 ASN ASN A . n A 1 223 TYR 223 311 311 TYR TYR A . n A 1 224 ASN 224 312 312 ASN ASN A . n A 1 225 ALA 225 313 313 ALA ALA A . n A 1 226 TRP 226 314 314 TRP TRP A . n A 1 227 SER 227 315 315 SER SER A . n A 1 228 VAL 228 316 316 VAL VAL A . n A 1 229 SER 229 317 317 SER SER A . n A 1 230 SER 230 318 318 SER SER A . n A 1 231 PRO 231 319 319 PRO PRO A . n A 1 232 PRO 232 320 320 PRO PRO A . n A 1 233 PRO 233 321 321 PRO PRO A . n A 1 234 TYR 234 322 322 TYR TYR A . n A 1 235 THR 235 323 323 THR THR A . n A 1 236 SER 236 324 324 SER SER A . n A 1 237 PRO 237 325 325 PRO PRO A . n A 1 238 ASN 238 326 326 ASN ASN A . n A 1 239 PRO 239 327 327 PRO PRO A . n A 1 240 ASN 240 328 328 ASN ASN A . n A 1 241 TYR 241 329 329 TYR TYR A . n A 1 242 ASP 242 330 330 ASP ASP A . n A 1 243 GLU 243 331 331 GLU GLU A . n A 1 244 LYS 244 332 332 LYS LYS A . n A 1 245 HIS 245 333 333 HIS HIS A . n A 1 246 TYR 246 334 334 TYR TYR A . n A 1 247 ILE 247 335 335 ILE ILE A . n A 1 248 GLU 248 336 336 GLU GLU A . n A 1 249 ALA 249 337 337 ALA ALA A . n A 1 250 PHE 250 338 338 PHE PHE A . n A 1 251 ARG 251 339 339 ARG ARG A . n A 1 252 PRO 252 340 340 PRO PRO A . n A 1 253 LEU 253 341 341 LEU LEU A . n A 1 254 LEU 254 342 342 LEU LEU A . n A 1 255 GLU 255 343 343 GLU GLU A . n A 1 256 ALA 256 344 344 ALA ALA A . n A 1 257 ARG 257 345 345 ARG ARG A . n A 1 258 GLY 258 346 346 GLY GLY A . n A 1 259 PHE 259 347 347 PHE PHE A . n A 1 260 PRO 260 348 348 PRO PRO A . n A 1 261 ALA 261 349 349 ALA ALA A . n A 1 262 GLN 262 350 350 GLN GLN A . n A 1 263 PHE 263 351 351 PHE PHE A . n A 1 264 ILE 264 352 352 ILE ILE A . n A 1 265 VAL 265 353 353 VAL VAL A . n A 1 266 ASP 266 354 354 ASP ASP A . n A 1 267 GLN 267 355 355 GLN GLN A . n A 1 268 GLY 268 356 356 GLY GLY A . n A 1 269 ARG 269 357 357 ARG ARG A . n A 1 270 SER 270 358 358 SER SER A . n A 1 271 GLY 271 359 359 GLY GLY A . n A 1 272 LYS 272 360 360 LYS LYS A . n A 1 273 GLN 273 361 361 GLN GLN A . n A 1 274 PRO 274 362 362 PRO PRO A . n A 1 275 THR 275 363 363 THR THR A . n A 1 276 GLY 276 364 364 GLY GLY A . n A 1 277 GLN 277 365 365 GLN GLN A . n A 1 278 LYS 278 366 366 LYS LYS A . n A 1 279 GLU 279 367 367 GLU GLU A . n A 1 280 TRP 280 368 368 TRP TRP A . n A 1 281 GLY 281 369 369 GLY GLY A . n A 1 282 HIS 282 370 370 HIS HIS A . n A 1 283 TRP 283 371 371 TRP TRP A . n A 1 284 CYS 284 372 372 CYS CYS A . n A 1 285 ASN 285 373 373 ASN ASN A . n A 1 286 ALA 286 374 374 ALA ALA A . n A 1 287 ILE 287 375 375 ILE ILE A . n A 1 288 GLY 288 376 376 GLY GLY A . n A 1 289 THR 289 377 377 THR THR A . n A 1 290 GLY 290 378 378 GLY GLY A . n A 1 291 PHE 291 379 379 PHE PHE A . n A 1 292 GLY 292 380 380 GLY GLY A . n A 1 293 MET 293 381 381 MET MET A . n A 1 294 ARG 294 382 382 ARG ARG A . n A 1 295 PRO 295 383 383 PRO PRO A . n A 1 296 THR 296 384 384 THR THR A . n A 1 297 ALA 297 385 385 ALA ALA A . n A 1 298 ASN 298 386 386 ASN ASN A . n A 1 299 THR 299 387 387 THR THR A . n A 1 300 GLY 300 388 388 GLY GLY A . n A 1 301 HIS 301 389 389 HIS HIS A . n A 1 302 GLN 302 390 390 GLN GLN A . n A 1 303 TYR 303 391 391 TYR TYR A . n A 1 304 VAL 304 392 392 VAL VAL A . n A 1 305 ASP 305 393 393 ASP ASP A . n A 1 306 ALA 306 394 394 ALA ALA A . n A 1 307 PHE 307 395 395 PHE PHE A . n A 1 308 VAL 308 396 396 VAL VAL A . n A 1 309 TRP 309 397 397 TRP TRP A . n A 1 310 VAL 310 398 398 VAL VAL A . n A 1 311 LYS 311 399 399 LYS LYS A . n A 1 312 PRO 312 400 400 PRO PRO A . n A 1 313 GLY 313 401 401 GLY GLY A . n A 1 314 GLY 314 402 402 GLY GLY A . n A 1 315 GLU 315 403 403 GLU GLU A . n A 1 316 CYS 316 404 404 CYS CYS A . n A 1 317 ASP 317 405 405 ASP ASP A . n A 1 318 GLY 318 406 406 GLY GLY A . n A 1 319 THR 319 407 407 THR THR A . n A 1 320 SER 320 408 408 SER SER A . n A 1 321 ASP 321 409 409 ASP ASP A . n A 1 322 THR 322 410 410 THR THR A . n A 1 323 THR 323 411 411 THR THR A . n A 1 324 ALA 324 412 412 ALA ALA A . n A 1 325 ALA 325 413 413 ALA ALA A . n A 1 326 ARG 326 414 414 ARG ARG A . n A 1 327 TYR 327 415 415 TYR TYR A . n A 1 328 ALA 328 416 416 ALA ALA A . n A 1 329 TYR 329 417 417 TYR TYR A . n A 1 330 HIS 330 418 418 HIS HIS A . n A 1 331 CYS 331 419 419 CYS CYS A . n A 1 332 GLY 332 420 420 GLY GLY A . n A 1 333 LEU 333 421 421 LEU LEU A . n A 1 334 GLU 334 422 422 GLU GLU A . n A 1 335 ASP 335 423 423 ASP ASP A . n A 1 336 ALA 336 424 424 ALA ALA A . n A 1 337 LEU 337 425 425 LEU LEU A . n A 1 338 LYS 338 426 426 LYS LYS A . n A 1 339 PRO 339 427 427 PRO PRO A . n A 1 340 ALA 340 428 428 ALA ALA A . n A 1 341 PRO 341 429 429 PRO PRO A . n A 1 342 GLU 342 430 430 GLU GLU A . n A 1 343 ALA 343 431 431 ALA ALA A . n A 1 344 GLY 344 432 432 GLY GLY A . n A 1 345 GLN 345 433 433 GLN GLN A . n A 1 346 TRP 346 434 434 TRP TRP A . n A 1 347 PHE 347 435 435 PHE PHE A . n A 1 348 ASN 348 436 436 ASN ASN A . n A 1 349 GLU 349 437 437 GLU GLU A . n A 1 350 TYR 350 438 438 TYR TYR A . n A 1 351 PHE 351 439 439 PHE PHE A . n A 1 352 ILE 352 440 440 ILE ILE A . n A 1 353 GLN 353 441 441 GLN GLN A . n A 1 354 LEU 354 442 442 LEU LEU A . n A 1 355 LEU 355 443 443 LEU LEU A . n A 1 356 ARG 356 444 444 ARG ARG A . n A 1 357 ASN 357 445 445 ASN ASN A . n A 1 358 ALA 358 446 446 ALA ALA A . n A 1 359 ASN 359 447 447 ASN ASN A . n A 1 360 PRO 360 448 448 PRO PRO A . n A 1 361 PRO 361 449 449 PRO PRO A . n A 1 362 PHE 362 450 450 PHE PHE A . 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 B 2 NAG 1 500 500 NAG NAG A . C 3 BGC 1 501 501 BGC BGC A . D 4 SSG 2 502 502 SSG SSG A . E 4 SSG 3 503 503 SSG SSG A . F 5 SGC 4 504 504 SGC SGC A . G 6 MA3 5 505 505 MA3 MA3 A . H 7 MG 1 506 506 MG MG A . I 8 ACY 1 507 507 ACY ACY A . J 9 HOH 1 2001 2001 HOH HOH A . J 9 HOH 2 2002 2002 HOH HOH A . J 9 HOH 3 2003 2003 HOH HOH A . J 9 HOH 4 2004 2004 HOH HOH A . J 9 HOH 5 2005 2005 HOH HOH A . J 9 HOH 6 2006 2006 HOH HOH A . J 9 HOH 7 2007 2007 HOH HOH A . J 9 HOH 8 2008 2008 HOH HOH A . J 9 HOH 9 2009 2009 HOH HOH A . J 9 HOH 10 2010 2010 HOH HOH A . J 9 HOH 11 2011 2011 HOH HOH A . J 9 HOH 12 2012 2012 HOH HOH A . J 9 HOH 13 2013 2013 HOH HOH A . J 9 HOH 14 2014 2014 HOH HOH A . J 9 HOH 15 2016 2016 HOH HOH A . J 9 HOH 16 2017 2017 HOH HOH A . J 9 HOH 17 2018 2018 HOH HOH A . J 9 HOH 18 2019 2019 HOH HOH A . J 9 HOH 19 2020 2020 HOH HOH A . J 9 HOH 20 2021 2021 HOH HOH A . J 9 HOH 21 2022 2022 HOH HOH A . J 9 HOH 22 2023 2023 HOH HOH A . J 9 HOH 23 2024 2024 HOH HOH A . J 9 HOH 24 2025 2025 HOH HOH A . J 9 HOH 25 2026 2026 HOH HOH A . J 9 HOH 26 2027 2027 HOH HOH A . J 9 HOH 27 2028 2028 HOH HOH A . J 9 HOH 28 2029 2029 HOH HOH A . J 9 HOH 29 2030 2030 HOH HOH A . J 9 HOH 30 2031 2031 HOH HOH A . J 9 HOH 31 2034 2034 HOH HOH A . J 9 HOH 32 2035 2035 HOH HOH A . J 9 HOH 33 2036 2036 HOH HOH A . J 9 HOH 34 2037 2037 HOH HOH A . J 9 HOH 35 2038 2038 HOH HOH A . J 9 HOH 36 2039 2039 HOH HOH A . J 9 HOH 37 2040 2040 HOH HOH A . J 9 HOH 38 2041 2041 HOH HOH A . J 9 HOH 39 2042 2042 HOH HOH A . J 9 HOH 40 2044 2044 HOH HOH A . J 9 HOH 41 2045 2045 HOH HOH A . J 9 HOH 42 2046 2046 HOH HOH A . J 9 HOH 43 2047 2047 HOH HOH A . J 9 HOH 44 2048 2048 HOH HOH A . J 9 HOH 45 2049 2049 HOH HOH A . J 9 HOH 46 2050 2050 HOH HOH A . J 9 HOH 47 2051 2051 HOH HOH A . J 9 HOH 48 2052 2052 HOH HOH A . J 9 HOH 49 2053 2053 HOH HOH A . J 9 HOH 50 2054 2054 HOH HOH A . J 9 HOH 51 2055 2055 HOH HOH A . J 9 HOH 52 2056 2056 HOH HOH A . J 9 HOH 53 2057 2057 HOH HOH A . J 9 HOH 54 2058 2058 HOH HOH A . J 9 HOH 55 2060 2060 HOH HOH A . J 9 HOH 56 2061 2061 HOH HOH A . J 9 HOH 57 2062 2062 HOH HOH A . J 9 HOH 58 2063 2063 HOH HOH A . J 9 HOH 59 2064 2064 HOH HOH A . J 9 HOH 60 2065 2065 HOH HOH A . J 9 HOH 61 2066 2066 HOH HOH A . J 9 HOH 62 2067 2067 HOH HOH A . J 9 HOH 63 2068 2068 HOH HOH A . J 9 HOH 64 2069 2069 HOH HOH A . J 9 HOH 65 2070 2070 HOH HOH A . J 9 HOH 66 2071 2071 HOH HOH A . J 9 HOH 67 2072 2072 HOH HOH A . J 9 HOH 68 2073 2073 HOH HOH A . J 9 HOH 69 2074 2074 HOH HOH A . J 9 HOH 70 2075 2075 HOH HOH A . J 9 HOH 71 2076 2076 HOH HOH A . J 9 HOH 72 2077 2077 HOH HOH A . J 9 HOH 73 2078 2078 HOH HOH A . J 9 HOH 74 2079 2079 HOH HOH A . J 9 HOH 75 2080 2080 HOH HOH A . J 9 HOH 76 2081 2081 HOH HOH A . J 9 HOH 77 2082 2082 HOH HOH A . J 9 HOH 78 2083 2083 HOH HOH A . J 9 HOH 79 2084 2084 HOH HOH A . J 9 HOH 80 2086 2086 HOH HOH A . J 9 HOH 81 2087 2087 HOH HOH A . J 9 HOH 82 2088 2088 HOH HOH A . J 9 HOH 83 2089 2089 HOH HOH A . J 9 HOH 84 2090 2090 HOH HOH A . J 9 HOH 85 2091 2091 HOH HOH A . J 9 HOH 86 2092 2092 HOH HOH A . J 9 HOH 87 2093 2093 HOH HOH A . J 9 HOH 88 2094 2094 HOH HOH A . J 9 HOH 89 2095 2095 HOH HOH A . J 9 HOH 90 2096 2096 HOH HOH A . J 9 HOH 91 2097 2097 HOH HOH A . J 9 HOH 92 2098 2098 HOH HOH A . J 9 HOH 93 2099 2099 HOH HOH A . J 9 HOH 94 2100 2100 HOH HOH A . J 9 HOH 95 2101 2101 HOH HOH A . J 9 HOH 96 2102 2102 HOH HOH A . J 9 HOH 97 2103 2103 HOH HOH A . J 9 HOH 98 2104 2104 HOH HOH A . J 9 HOH 99 2105 2105 HOH HOH A . J 9 HOH 100 2106 2106 HOH HOH A . J 9 HOH 101 2107 2107 HOH HOH A . J 9 HOH 102 2108 2108 HOH HOH A . J 9 HOH 103 2109 2109 HOH HOH A . J 9 HOH 104 2110 2110 HOH HOH A . J 9 HOH 105 2111 2111 HOH HOH A . J 9 HOH 106 2112 2112 HOH HOH A . J 9 HOH 107 2113 2113 HOH HOH A . J 9 HOH 108 2114 2114 HOH HOH A . J 9 HOH 109 2115 2115 HOH HOH A . J 9 HOH 110 2116 2116 HOH HOH A . J 9 HOH 111 2117 2117 HOH HOH A . J 9 HOH 112 2118 2118 HOH HOH A . J 9 HOH 113 2119 2119 HOH HOH A . J 9 HOH 114 2120 2120 HOH HOH A . J 9 HOH 115 2121 2121 HOH HOH A . J 9 HOH 116 2122 2122 HOH HOH A . J 9 HOH 117 2123 2123 HOH HOH A . J 9 HOH 118 2124 2124 HOH HOH A . J 9 HOH 119 2125 2125 HOH HOH A . J 9 HOH 120 2126 2126 HOH HOH A . J 9 HOH 121 2127 2127 HOH HOH A . J 9 HOH 122 2128 2128 HOH HOH A . J 9 HOH 123 2129 2129 HOH HOH A . J 9 HOH 124 2130 2130 HOH HOH A . J 9 HOH 125 2131 2131 HOH HOH A . J 9 HOH 126 2132 2132 HOH HOH A . J 9 HOH 127 2133 2133 HOH HOH A . J 9 HOH 128 2134 2134 HOH HOH A . J 9 HOH 129 2135 2135 HOH HOH A . J 9 HOH 130 2136 2136 HOH HOH A . J 9 HOH 131 2137 2137 HOH HOH A . J 9 HOH 132 2138 2138 HOH HOH A . J 9 HOH 133 2139 2139 HOH HOH A . J 9 HOH 134 2140 2140 HOH HOH A . J 9 HOH 135 2141 2141 HOH HOH A . J 9 HOH 136 2142 2142 HOH HOH A . J 9 HOH 137 2143 2143 HOH HOH A . J 9 HOH 138 2144 2144 HOH HOH A . J 9 HOH 139 2145 2145 HOH HOH A . J 9 HOH 140 2146 2146 HOH HOH A . J 9 HOH 141 2147 2147 HOH HOH A . J 9 HOH 142 2148 2148 HOH HOH A . J 9 HOH 143 2149 2149 HOH HOH A . J 9 HOH 144 2150 2150 HOH HOH A . J 9 HOH 145 2152 2152 HOH HOH A . J 9 HOH 146 2153 2153 HOH HOH A . J 9 HOH 147 2154 2154 HOH HOH A . J 9 HOH 148 2155 2155 HOH HOH A . J 9 HOH 149 2156 2156 HOH HOH A . J 9 HOH 150 2157 2157 HOH HOH A . J 9 HOH 151 2158 2158 HOH HOH A . J 9 HOH 152 2159 2159 HOH HOH A . J 9 HOH 153 2160 2160 HOH HOH A . J 9 HOH 154 2161 2161 HOH HOH A . J 9 HOH 155 2162 2162 HOH HOH A . J 9 HOH 156 2163 2163 HOH HOH A . J 9 HOH 157 2164 2164 HOH HOH A . J 9 HOH 158 2165 2165 HOH HOH A . J 9 HOH 159 2166 2166 HOH HOH A . J 9 HOH 160 2167 2167 HOH HOH A . J 9 HOH 161 2168 2168 HOH HOH A . J 9 HOH 162 2169 2169 HOH HOH A . J 9 HOH 163 2170 2170 HOH HOH A . J 9 HOH 164 2171 2171 HOH HOH A . J 9 HOH 165 2172 2172 HOH HOH A . J 9 HOH 166 2173 2173 HOH HOH A . J 9 HOH 167 2175 2175 HOH HOH A . J 9 HOH 168 2176 2176 HOH HOH A . J 9 HOH 169 2177 2177 HOH HOH A . J 9 HOH 170 2178 2178 HOH HOH A . J 9 HOH 171 2179 2179 HOH HOH A . J 9 HOH 172 2180 2180 HOH HOH A . J 9 HOH 173 2181 2181 HOH HOH A . J 9 HOH 174 2182 2182 HOH HOH A . J 9 HOH 175 2183 2183 HOH HOH A . J 9 HOH 176 2184 2184 HOH HOH A . J 9 HOH 177 2186 2186 HOH HOH A . J 9 HOH 178 2187 2187 HOH HOH A . J 9 HOH 179 2188 2188 HOH HOH A . J 9 HOH 180 2189 2189 HOH HOH A . J 9 HOH 181 2190 2190 HOH HOH A . J 9 HOH 182 2191 2191 HOH HOH A . J 9 HOH 183 2192 2192 HOH HOH A . J 9 HOH 184 2193 2193 HOH HOH A . J 9 HOH 185 2194 2194 HOH HOH A . J 9 HOH 186 2195 2195 HOH HOH A . J 9 HOH 187 2196 2196 HOH HOH A . J 9 HOH 188 2197 2197 HOH HOH A . J 9 HOH 189 2198 2198 HOH HOH A . J 9 HOH 190 2199 2199 HOH HOH A . J 9 HOH 191 2200 2200 HOH HOH A . J 9 HOH 192 2201 2201 HOH HOH A . J 9 HOH 193 2202 2202 HOH HOH A . J 9 HOH 194 2204 2204 HOH HOH A . J 9 HOH 195 2205 2205 HOH HOH A . J 9 HOH 196 2206 2206 HOH HOH A . J 9 HOH 197 2207 2207 HOH HOH A . J 9 HOH 198 2208 2208 HOH HOH A . J 9 HOH 199 2209 2209 HOH HOH A . J 9 HOH 200 2210 2210 HOH HOH A . J 9 HOH 201 2211 2211 HOH HOH A . J 9 HOH 202 2212 2212 HOH HOH A . J 9 HOH 203 2213 2213 HOH HOH A . J 9 HOH 204 2214 2214 HOH HOH A . J 9 HOH 205 2215 2215 HOH HOH A . J 9 HOH 206 2216 2216 HOH HOH A . J 9 HOH 207 2217 2217 HOH HOH A . J 9 HOH 208 2218 2218 HOH HOH A . J 9 HOH 209 2219 2219 HOH HOH A . J 9 HOH 210 2220 2220 HOH HOH A . J 9 HOH 211 2221 2221 HOH HOH A . J 9 HOH 212 2222 2222 HOH HOH A . J 9 HOH 213 2223 2223 HOH HOH A . J 9 HOH 214 2224 2224 HOH HOH A . J 9 HOH 215 2225 2225 HOH HOH A . J 9 HOH 216 2226 2226 HOH HOH A . J 9 HOH 217 2227 2227 HOH HOH A . J 9 HOH 218 2228 2228 HOH HOH A . J 9 HOH 219 2229 2229 HOH HOH A . J 9 HOH 220 2230 2230 HOH HOH A . J 9 HOH 221 2232 2232 HOH HOH A . J 9 HOH 222 2233 2233 HOH HOH A . J 9 HOH 223 2234 2234 HOH HOH A . J 9 HOH 224 2236 2236 HOH HOH A . J 9 HOH 225 2237 2237 HOH HOH A . J 9 HOH 226 2238 2238 HOH HOH A . J 9 HOH 227 2239 2239 HOH HOH A . J 9 HOH 228 2240 2240 HOH HOH A . J 9 HOH 229 2241 2241 HOH HOH A . J 9 HOH 230 2242 2242 HOH HOH A . J 9 HOH 231 2244 2244 HOH HOH A . J 9 HOH 232 2245 2245 HOH HOH A . J 9 HOH 233 2246 2246 HOH HOH A . J 9 HOH 234 2247 2247 HOH HOH A . J 9 HOH 235 2248 2248 HOH HOH A . J 9 HOH 236 2249 2249 HOH HOH A . J 9 HOH 237 2250 2250 HOH HOH A . J 9 HOH 238 2251 2251 HOH HOH A . J 9 HOH 239 2252 2252 HOH HOH A . J 9 HOH 240 2253 2253 HOH HOH A . J 9 HOH 241 2254 2254 HOH HOH A . J 9 HOH 242 2255 2255 HOH HOH A . J 9 HOH 243 2256 2256 HOH HOH A . J 9 HOH 244 2257 2257 HOH HOH A . J 9 HOH 245 2258 2258 HOH HOH A . J 9 HOH 246 2259 2259 HOH HOH A . J 9 HOH 247 2260 2260 HOH HOH A . J 9 HOH 248 2261 2261 HOH HOH A . J 9 HOH 249 2262 2262 HOH HOH A . J 9 HOH 250 2263 2263 HOH HOH A . J 9 HOH 251 2264 2264 HOH HOH A . J 9 HOH 252 2265 2265 HOH HOH A . J 9 HOH 253 2266 2266 HOH HOH A . J 9 HOH 254 2267 2267 HOH HOH A . J 9 HOH 255 2268 2268 HOH HOH A . J 9 HOH 256 2269 2269 HOH HOH A . J 9 HOH 257 2270 2270 HOH HOH A . J 9 HOH 258 2271 2271 HOH HOH A . J 9 HOH 259 2272 2272 HOH HOH A . J 9 HOH 260 2273 2273 HOH HOH A . J 9 HOH 261 2274 2274 HOH HOH A . J 9 HOH 262 2275 2275 HOH HOH A . J 9 HOH 263 2276 2276 HOH HOH A . J 9 HOH 264 2277 2277 HOH HOH A . J 9 HOH 265 2278 2278 HOH HOH A . J 9 HOH 266 2279 2279 HOH HOH A . J 9 HOH 267 2281 2281 HOH HOH A . J 9 HOH 268 2282 2282 HOH HOH A . J 9 HOH 269 2283 2283 HOH HOH A . J 9 HOH 270 2284 2284 HOH HOH A . J 9 HOH 271 2285 2285 HOH HOH A . J 9 HOH 272 2286 2286 HOH HOH A . J 9 HOH 273 2287 2287 HOH HOH A . J 9 HOH 274 2288 2288 HOH HOH A . J 9 HOH 275 2289 2289 HOH HOH A . J 9 HOH 276 2290 2290 HOH HOH A . J 9 HOH 277 2291 2291 HOH HOH A . J 9 HOH 278 2292 2292 HOH HOH A . J 9 HOH 279 2293 2293 HOH HOH A . J 9 HOH 280 2294 2294 HOH HOH A . J 9 HOH 281 2295 2295 HOH HOH A . J 9 HOH 282 2296 2296 HOH HOH A . J 9 HOH 283 2298 2298 HOH HOH A . J 9 HOH 284 2299 2299 HOH HOH A . J 9 HOH 285 2300 2300 HOH HOH A . J 9 HOH 286 2301 2301 HOH HOH A . J 9 HOH 287 2302 2302 HOH HOH A . J 9 HOH 288 2303 2303 HOH HOH A . J 9 HOH 289 2304 2304 HOH HOH A . J 9 HOH 290 2305 2305 HOH HOH A . J 9 HOH 291 2306 2306 HOH HOH A . J 9 HOH 292 2307 2307 HOH HOH A . J 9 HOH 293 2308 2308 HOH HOH A . J 9 HOH 294 2309 2309 HOH HOH A . J 9 HOH 295 2310 2310 HOH HOH A . J 9 HOH 296 2311 2311 HOH HOH A . J 9 HOH 297 2312 2312 HOH HOH A . J 9 HOH 298 2313 2313 HOH HOH A . J 9 HOH 299 2314 2314 HOH HOH A . J 9 HOH 300 2315 2315 HOH HOH A . J 9 HOH 301 2316 2316 HOH HOH A . J 9 HOH 302 2317 2317 HOH HOH A . J 9 HOH 303 2318 2318 HOH HOH A . J 9 HOH 304 2319 2319 HOH HOH A . J 9 HOH 305 2320 2320 HOH HOH A . J 9 HOH 306 2321 2321 HOH HOH A . J 9 HOH 307 2322 2322 HOH HOH A . J 9 HOH 308 2323 2323 HOH HOH A . J 9 HOH 309 2324 2324 HOH HOH A . J 9 HOH 310 2325 2325 HOH HOH A . J 9 HOH 311 2326 2326 HOH HOH A . J 9 HOH 312 2327 2327 HOH HOH A . J 9 HOH 313 2328 2328 HOH HOH A . J 9 HOH 314 2329 2329 HOH HOH A . J 9 HOH 315 2330 2330 HOH HOH A . J 9 HOH 316 2331 2331 HOH HOH A . J 9 HOH 317 2332 2332 HOH HOH A . J 9 HOH 318 2333 2333 HOH HOH A . J 9 HOH 319 2334 2334 HOH HOH A . J 9 HOH 320 2335 2335 HOH HOH A . J 9 HOH 321 2336 2336 HOH HOH A . J 9 HOH 322 2337 2337 HOH HOH A . J 9 HOH 323 2338 2338 HOH HOH A . J 9 HOH 324 2339 2339 HOH HOH A . J 9 HOH 325 2340 2340 HOH HOH A . J 9 HOH 326 2341 2341 HOH HOH A . J 9 HOH 327 2342 2342 HOH HOH A . J 9 HOH 328 2343 2343 HOH HOH A . J 9 HOH 329 2344 2344 HOH HOH A . J 9 HOH 330 2345 2345 HOH HOH A . J 9 HOH 331 2346 2346 HOH HOH A . J 9 HOH 332 2347 2347 HOH HOH A . J 9 HOH 333 2348 2348 HOH HOH A . J 9 HOH 334 2349 2349 HOH HOH A . J 9 HOH 335 2350 2350 HOH HOH A . J 9 HOH 336 2351 2351 HOH HOH A . J 9 HOH 337 2352 2352 HOH HOH A . J 9 HOH 338 2353 2353 HOH HOH A . J 9 HOH 339 2354 2354 HOH HOH A . J 9 HOH 340 2355 2355 HOH HOH A . J 9 HOH 341 2356 2356 HOH HOH A . J 9 HOH 342 2357 2357 HOH HOH A . J 9 HOH 343 2358 2358 HOH HOH A . J 9 HOH 344 2359 2359 HOH HOH A . J 9 HOH 345 2360 2360 HOH HOH A . J 9 HOH 346 2361 2361 HOH HOH A . J 9 HOH 347 2362 2362 HOH HOH A . J 9 HOH 348 2363 2363 HOH HOH A . J 9 HOH 349 2364 2364 HOH HOH A . J 9 HOH 350 2365 2365 HOH HOH A . J 9 HOH 351 2366 2366 HOH HOH A . J 9 HOH 352 2367 2367 HOH HOH A . J 9 HOH 353 2368 2368 HOH HOH A . J 9 HOH 354 2369 2369 HOH HOH A . J 9 HOH 355 2370 2370 HOH HOH A . J 9 HOH 356 2371 2371 HOH HOH A . J 9 HOH 357 2372 2372 HOH HOH A . J 9 HOH 358 2373 2373 HOH HOH A . J 9 HOH 359 2374 2374 HOH HOH A . J 9 HOH 360 2375 2375 HOH HOH A . J 9 HOH 361 2376 2376 HOH HOH A . J 9 HOH 362 2377 2377 HOH HOH A . J 9 HOH 363 2378 2378 HOH HOH A . J 9 HOH 364 2379 2379 HOH HOH A . J 9 HOH 365 2380 2380 HOH HOH A . J 9 HOH 366 2382 2382 HOH HOH A . J 9 HOH 367 2383 2383 HOH HOH A . J 9 HOH 368 2384 2384 HOH HOH A . J 9 HOH 369 2385 2385 HOH HOH A . J 9 HOH 370 2386 2386 HOH HOH A . J 9 HOH 371 2388 2388 HOH HOH A . J 9 HOH 372 2389 2389 HOH HOH A . J 9 HOH 373 2390 2390 HOH HOH A . J 9 HOH 374 2391 2391 HOH HOH A . J 9 HOH 375 2392 2392 HOH HOH A . J 9 HOH 376 2393 2393 HOH HOH A . J 9 HOH 377 2394 2394 HOH HOH A . J 9 HOH 378 2395 2395 HOH HOH A . J 9 HOH 379 2396 2396 HOH HOH A . J 9 HOH 380 2397 2397 HOH HOH A . J 9 HOH 381 2398 2398 HOH HOH A . J 9 HOH 382 2399 2399 HOH HOH A . J 9 HOH 383 2400 2400 HOH HOH A . J 9 HOH 384 2401 2401 HOH HOH A . J 9 HOH 385 2402 2402 HOH HOH A . J 9 HOH 386 2403 2403 HOH HOH A . J 9 HOH 387 2405 2405 HOH HOH A . J 9 HOH 388 2406 2406 HOH HOH A . J 9 HOH 389 2407 2407 HOH HOH A . J 9 HOH 390 2408 2408 HOH HOH A . J 9 HOH 391 2409 2409 HOH HOH A . J 9 HOH 392 2410 2410 HOH HOH A . J 9 HOH 393 2411 2411 HOH HOH A . J 9 HOH 394 2412 2412 HOH HOH A . J 9 HOH 395 2413 2413 HOH HOH A . J 9 HOH 396 2414 2414 HOH HOH A . J 9 HOH 397 2415 2415 HOH HOH A . J 9 HOH 398 2416 2416 HOH HOH A . J 9 HOH 399 2417 2417 HOH HOH A . J 9 HOH 400 2418 2418 HOH HOH A . J 9 HOH 401 2419 2419 HOH HOH A . J 9 HOH 402 2420 2420 HOH HOH A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 53 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 141 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _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 # _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 O ? J HOH . ? A HOH 2103 ? 1_655 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2304 ? 1_555 168.8 ? 2 O ? J HOH . ? A HOH 2103 ? 1_655 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2306 ? 1_555 97.2 ? 3 O ? J HOH . ? A HOH 2304 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2306 ? 1_555 88.7 ? 4 O ? J HOH . ? A HOH 2103 ? 1_655 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2072 ? 1_655 88.5 ? 5 O ? J HOH . ? A HOH 2304 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2072 ? 1_655 87.1 ? 6 O ? J HOH . ? A HOH 2306 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2072 ? 1_655 170.3 ? 7 O ? J HOH . ? A HOH 2103 ? 1_655 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2102 ? 1_655 87.4 ? 8 O ? J HOH . ? A HOH 2304 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2102 ? 1_655 82.7 ? 9 O ? J HOH . ? A HOH 2306 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2102 ? 1_655 94.0 ? 10 O ? J HOH . ? A HOH 2072 ? 1_655 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2102 ? 1_655 94.2 ? 11 O ? J HOH . ? A HOH 2103 ? 1_655 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2096 ? 1_655 92.6 ? 12 O ? J HOH . ? A HOH 2304 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2096 ? 1_655 97.8 ? 13 O ? J HOH . ? A HOH 2306 ? 1_555 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2096 ? 1_655 81.3 ? 14 O ? J HOH . ? A HOH 2072 ? 1_655 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2096 ? 1_655 90.6 ? 15 O ? J HOH . ? A HOH 2102 ? 1_655 MG ? H MG . ? A MG 506 ? 1_555 O ? J HOH . ? A HOH 2096 ? 1_655 175.2 ? # 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 2003-07-10 2 'Structure model' 1 1 2012-01-25 # _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' 'Atomic model' 2 2 'Structure model' 'Derived calculations' 3 2 'Structure model' 'Non-polymer description' 4 2 'Structure model' Other 5 2 'Structure model' 'Structure summary' 6 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.1.24 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 AMoRE phasing . ? 4 # _pdbx_database_remark.id 700 _pdbx_database_remark.text ; SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. ; # _pdbx_entry_details.entry_id 1OCJ _pdbx_entry_details.compound_details 'ENGINEERED MUTATION ASP 416 ALA CHAIN A' _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THIS MUTANT HAS BEEN PRODUCED BY SITE-DIRECTED MUTAGENESIS. THE CLONING WAS PERFORMED SUCH HAS ONLY THE PRO-SEQUENCE AND THE CATALYTIC DOMAIN WERE EXPRESSED. THE CELLULOSE BINDING DOMAIN HAS BEEN REMOVED.THE CONSTRUCT IS POST-TRANSLATIONALLY CLEAVED TO YIELD TO A MATURE PROTEIN OF 450 RESIDUES WHICH COMMENCES AT RESIDUE TYR 89. THIS PROTEIN IS CLOSELY RELATED TO AVICELASE 2 (SWISS-PROT ACCESSION ID:Q9C1S9) WITH WHICH IT HAS 96% SEQUENCE IDENTITY. ; # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 THR A 146 ? ? -126.14 -89.30 2 1 TYR A 174 ? ? -152.40 75.81 3 1 ASP A 175 ? ? -152.82 33.95 4 1 GLU A 224 ? ? 54.21 77.75 5 1 SER A 227 ? ? -118.29 -90.40 6 1 TRP A 274 ? ? -110.50 -70.45 7 1 ASN A 328 ? ? -101.22 78.80 # loop_ _pdbx_distant_solvent_atoms.id _pdbx_distant_solvent_atoms.PDB_model_num _pdbx_distant_solvent_atoms.auth_atom_id _pdbx_distant_solvent_atoms.label_alt_id _pdbx_distant_solvent_atoms.auth_asym_id _pdbx_distant_solvent_atoms.auth_comp_id _pdbx_distant_solvent_atoms.auth_seq_id _pdbx_distant_solvent_atoms.PDB_ins_code _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance _pdbx_distant_solvent_atoms.neighbor_ligand_distance 1 1 O ? A HOH 2056 ? . 5.88 2 1 O ? A HOH 2108 ? 6.00 . # 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 TYR 89 ? A TYR 1 2 1 Y 1 A ASN 90 ? A ASN 2 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 BETA-D-GLUCOSE BGC 4 1,4-DEOXY-1,4-DITHIO-BETA-D-GLUCOPYRANOSE SSG 5 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE SGC 6 O1-METHYL-4-DEOXY-4-THIO-ALPHA-D-GLUCOSE MA3 7 'MAGNESIUM ION' MG 8 'ACETIC ACID' ACY 9 water HOH #