data_1OC7 # _entry.id 1OC7 # _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 1OC7 PDBE EBI-9308 WWPDB D_1290009308 # 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 1OCB unspecified 'STRUCTURE OF THE WILD-TYPE CELLOBIOHYDROLASE CEL6A FROM HUMICOLAS INSOLENS IN COMPLEX WITH A FLUORESCENT SUBSTRATE' PDB 1OCJ unspecified 'MUTANT D416A OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH A THIOPENTASACCHARIDE AT 1.3 ANGSTROM RESOLUTION' 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 1OC7 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2003-02-06 _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 1OC7 _cell.length_a 57.504 _cell.length_b 60.148 _cell.length_c 97.207 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1OC7 _symmetry.space_group_name_H-M 'P 21 21 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 19 # 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' 40181.723 1 3.2.1.91 YES 'CATALYTIC CORE DOMAIN RESIDUES 87-450' 'N-LINKED N-ACETYLGLUCOSAMINE ON RESIDUE ASN 141' 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 non-polymer syn 'MAGNESIUM ION' 24.305 1 ? ? ? ? 4 non-polymer syn 'ACETATE ION' 59.044 1 ? ? ? ? 5 non-polymer syn DIMETHYLFORMAMIDE 73.094 2 ? ? ? ? 6 non-polymer syn GLYCEROL 92.094 2 ? ? ? ? 7 non-polymer man BETA-D-GLUCOSE 180.156 1 ? ? ? ? 8 non-polymer man 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE 196.221 3 ? ? ? ? 9 non-polymer man O1-METHYL-4-DEOXY-4-THIO-ALPHA-D-GLUCOSE 210.248 1 ? ? ? ? 10 water nat water 18.015 603 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'CLLULASE, 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 ;APYNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQ YAAQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAAST YRELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPN PNYDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECNG TSDTTAARYDYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF ; _entity_poly.pdbx_seq_one_letter_code_can ;APYNGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQ YAAQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAAST YRELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPN PNYDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECNG TSDTTAARYDYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF ; _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 ALA n 1 2 PRO n 1 3 TYR n 1 4 ASN n 1 5 GLY n 1 6 ASN n 1 7 PRO n 1 8 PHE n 1 9 GLU n 1 10 GLY n 1 11 VAL n 1 12 GLN n 1 13 LEU n 1 14 TRP n 1 15 ALA n 1 16 ASN n 1 17 ASN n 1 18 TYR n 1 19 TYR n 1 20 ARG n 1 21 SER n 1 22 GLU n 1 23 VAL n 1 24 HIS n 1 25 THR n 1 26 LEU n 1 27 ALA n 1 28 ILE n 1 29 PRO n 1 30 GLN n 1 31 ILE n 1 32 THR n 1 33 ASP n 1 34 PRO n 1 35 ALA n 1 36 LEU n 1 37 ARG n 1 38 ALA n 1 39 ALA n 1 40 ALA n 1 41 SER n 1 42 ALA n 1 43 VAL n 1 44 ALA n 1 45 GLU n 1 46 VAL n 1 47 PRO n 1 48 SER n 1 49 PHE n 1 50 GLN n 1 51 TRP n 1 52 LEU n 1 53 ASP n 1 54 ARG n 1 55 ASN n 1 56 VAL n 1 57 THR n 1 58 VAL n 1 59 ASP n 1 60 THR n 1 61 LEU n 1 62 LEU n 1 63 VAL n 1 64 GLN n 1 65 THR n 1 66 LEU n 1 67 SER n 1 68 GLU n 1 69 ILE n 1 70 ARG n 1 71 GLU n 1 72 ALA n 1 73 ASN n 1 74 GLN n 1 75 ALA n 1 76 GLY n 1 77 ALA n 1 78 ASN n 1 79 PRO n 1 80 GLN n 1 81 TYR n 1 82 ALA n 1 83 ALA n 1 84 GLN n 1 85 ILE n 1 86 VAL n 1 87 VAL n 1 88 TYR n 1 89 ASP n 1 90 LEU n 1 91 PRO n 1 92 ASP n 1 93 ARG n 1 94 ASP n 1 95 CYS n 1 96 ALA n 1 97 ALA n 1 98 ALA n 1 99 ALA n 1 100 SER n 1 101 ASN n 1 102 GLY n 1 103 GLU n 1 104 TRP n 1 105 ALA n 1 106 ILE n 1 107 ALA n 1 108 ASN n 1 109 ASN n 1 110 GLY n 1 111 VAL n 1 112 ASN n 1 113 ASN n 1 114 TYR n 1 115 LYS n 1 116 ALA n 1 117 TYR n 1 118 ILE n 1 119 ASN n 1 120 ARG n 1 121 ILE n 1 122 ARG n 1 123 GLU n 1 124 ILE n 1 125 LEU n 1 126 ILE n 1 127 SER n 1 128 PHE n 1 129 SER n 1 130 ASP n 1 131 VAL n 1 132 ARG n 1 133 THR n 1 134 ILE n 1 135 LEU n 1 136 VAL n 1 137 ILE n 1 138 GLU n 1 139 PRO n 1 140 ASP n 1 141 SER n 1 142 LEU n 1 143 ALA n 1 144 ASN n 1 145 MET n 1 146 VAL n 1 147 THR n 1 148 ASN n 1 149 MET n 1 150 ASN n 1 151 VAL n 1 152 PRO n 1 153 LYS n 1 154 CYS n 1 155 SER n 1 156 GLY n 1 157 ALA n 1 158 ALA n 1 159 SER n 1 160 THR n 1 161 TYR n 1 162 ARG n 1 163 GLU n 1 164 LEU n 1 165 THR n 1 166 ILE n 1 167 TYR n 1 168 ALA n 1 169 LEU n 1 170 LYS n 1 171 GLN n 1 172 LEU n 1 173 ASP n 1 174 LEU n 1 175 PRO n 1 176 HIS n 1 177 VAL n 1 178 ALA n 1 179 MET n 1 180 TYR n 1 181 MET n 1 182 ASP n 1 183 ALA n 1 184 GLY n 1 185 HIS n 1 186 ALA n 1 187 GLY n 1 188 TRP n 1 189 LEU n 1 190 GLY n 1 191 TRP n 1 192 PRO n 1 193 ALA n 1 194 ASN n 1 195 ILE n 1 196 GLN n 1 197 PRO n 1 198 ALA n 1 199 ALA n 1 200 GLU n 1 201 LEU n 1 202 PHE n 1 203 ALA n 1 204 LYS n 1 205 ILE n 1 206 TYR n 1 207 GLU n 1 208 ASP n 1 209 ALA n 1 210 GLY n 1 211 LYS n 1 212 PRO n 1 213 ARG n 1 214 ALA n 1 215 VAL n 1 216 ARG n 1 217 GLY n 1 218 LEU n 1 219 ALA n 1 220 THR n 1 221 ASN n 1 222 VAL n 1 223 ALA n 1 224 ASN n 1 225 TYR n 1 226 ASN n 1 227 ALA n 1 228 TRP n 1 229 SER n 1 230 VAL n 1 231 SER n 1 232 SER n 1 233 PRO n 1 234 PRO n 1 235 PRO n 1 236 TYR n 1 237 THR n 1 238 SER n 1 239 PRO n 1 240 ASN n 1 241 PRO n 1 242 ASN n 1 243 TYR n 1 244 ASP n 1 245 GLU n 1 246 LYS n 1 247 HIS n 1 248 TYR n 1 249 ILE n 1 250 GLU n 1 251 ALA n 1 252 PHE n 1 253 ARG n 1 254 PRO n 1 255 LEU n 1 256 LEU n 1 257 GLU n 1 258 ALA n 1 259 ARG n 1 260 GLY n 1 261 PHE n 1 262 PRO n 1 263 ALA n 1 264 GLN n 1 265 PHE n 1 266 ILE n 1 267 VAL n 1 268 ASP n 1 269 GLN n 1 270 GLY n 1 271 ARG n 1 272 SER n 1 273 GLY n 1 274 LYS n 1 275 GLN n 1 276 PRO n 1 277 THR n 1 278 GLY n 1 279 GLN n 1 280 LYS n 1 281 GLU n 1 282 TRP n 1 283 GLY n 1 284 HIS n 1 285 TRP n 1 286 CYS n 1 287 ASN n 1 288 ALA n 1 289 ILE n 1 290 GLY n 1 291 THR n 1 292 GLY n 1 293 PHE n 1 294 GLY n 1 295 MET n 1 296 ARG n 1 297 PRO n 1 298 THR n 1 299 ALA n 1 300 ASN n 1 301 THR n 1 302 GLY n 1 303 HIS n 1 304 GLN n 1 305 TYR n 1 306 VAL n 1 307 ASP n 1 308 ALA n 1 309 PHE n 1 310 VAL n 1 311 TRP n 1 312 VAL n 1 313 LYS n 1 314 PRO n 1 315 GLY n 1 316 GLY n 1 317 GLU n 1 318 CYS n 1 319 ASN n 1 320 GLY n 1 321 THR n 1 322 SER n 1 323 ASP n 1 324 THR n 1 325 THR n 1 326 ALA n 1 327 ALA n 1 328 ARG n 1 329 TYR n 1 330 ASP n 1 331 TYR n 1 332 HIS n 1 333 CYS n 1 334 GLY n 1 335 LEU n 1 336 GLU n 1 337 ASP n 1 338 ALA n 1 339 LEU n 1 340 LYS n 1 341 PRO n 1 342 ALA n 1 343 PRO n 1 344 GLU n 1 345 ALA n 1 346 GLY n 1 347 GLN n 1 348 TRP n 1 349 PHE n 1 350 ASN n 1 351 GLU n 1 352 TYR n 1 353 PHE n 1 354 ILE n 1 355 GLN n 1 356 LEU n 1 357 LEU n 1 358 ARG n 1 359 ASN n 1 360 ALA n 1 361 ASN n 1 362 PRO n 1 363 PRO n 1 364 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 1OC7 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession 1OC7 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1OC7 _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 364 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 1OC7 _struct_ref_seq.db_align_beg 87 _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 87 _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 ACT non-polymer . 'ACETATE ION' ? 'C2 H3 O2 -1' 59.044 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BGC saccharide . BETA-D-GLUCOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 DMF non-polymer . DIMETHYLFORMAMIDE ? 'C3 H7 N O' 73.094 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 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 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 1OC7 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 4.05 _exptl_crystal.density_percent_sol 38.8 _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 20 MG/ML IN WATER. CRYSTALLISATION IN 100MM MAGNESIUM ACETATE, 100MM ACETATE BUFFER AT PH 4.6. PRECIPITANT WAS 21% POLYETHYLENE GLYCOL 5000MME AND 5% DIMETHYLFORMAMIDE AS ADDITIVE.THE PROTEIN WAS INCUBATED WITH 1MM OF THE INHIBITOR PRIOR CRYSTALLISATION FOR AT LEAST 1 HOUR. ; # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 1999-10-15 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.8445 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'EMBL/DESY, HAMBURG BEAMLINE BW7B' _diffrn_source.pdbx_synchrotron_site 'EMBL/DESY, Hamburg' _diffrn_source.pdbx_synchrotron_beamline BW7B _diffrn_source.pdbx_wavelength 0.8445 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1OC7 _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 20.000 _reflns.d_resolution_high 1.100 _reflns.number_obs 120133 _reflns.number_all ? _reflns.percent_possible_obs 96.0 _reflns.pdbx_Rmerge_I_obs 0.05300 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 23.7000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 4.300 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.10 _reflns_shell.d_res_low 1.13 _reflns_shell.percent_possible_all 91.5 _reflns_shell.Rmerge_I_obs 0.24200 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 5.600 _reflns_shell.pdbx_redundancy 4.30 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1OC7 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 120318 _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 20.00 _refine.ls_d_res_high 1.11 _refine.ls_percent_reflns_obs 94.5 _refine.ls_R_factor_obs 0.106 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.105 _refine.ls_R_factor_R_free 0.124 _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 6359 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.984 _refine.correlation_coeff_Fo_to_Fc_free 0.980 _refine.B_iso_mean 8.57 _refine.aniso_B[1][1] -0.31000 _refine.aniso_B[2][2] 0.28000 _refine.aniso_B[3][3] 0.03000 _refine.aniso_B[1][2] 0.00000 _refine.aniso_B[1][3] 0.00000 _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 1OC5' _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 0.024 _refine.pdbx_overall_ESU_R_Free 0.025 _refine.overall_SU_ML 0.014 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 0.286 _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 2839 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 98 _refine_hist.number_atoms_solvent 603 _refine_hist.number_atoms_total 3540 _refine_hist.d_res_high 1.11 _refine_hist.d_res_low 20.00 # 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 0.017 0.021 ? 3106 'X-RAY DIFFRACTION' ? r_bond_other_d 0.002 0.020 ? 2701 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.907 1.957 ? 4247 'X-RAY DIFFRACTION' ? r_angle_other_deg 1.861 3.000 ? 6304 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.232 5.000 ? 371 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 40.071 24.211 ? 152 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 10.940 15.000 ? 450 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 19.962 15.000 ? 20 'X-RAY DIFFRACTION' ? r_chiral_restr 0.122 0.200 ? 466 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.011 0.020 ? 3434 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.004 0.020 ? 620 'X-RAY DIFFRACTION' ? r_nbd_refined 0.234 0.200 ? 589 'X-RAY DIFFRACTION' ? r_nbd_other 0.274 0.200 ? 3063 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other 0.085 0.200 ? 1572 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.129 0.200 ? 335 '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 0.163 0.200 ? 11 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.253 0.200 ? 59 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.139 0.200 ? 45 '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 1.269 1.500 ? 1859 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.822 2.000 ? 3002 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.494 3.000 ? 1247 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.434 4.500 ? 1241 '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 1.11 _refine_ls_shell.d_res_low 1.14 _refine_ls_shell.number_reflns_R_work 7886 _refine_ls_shell.R_factor_R_work 0.1160 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.1400 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 400 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 1OC7 _struct.title ;D405N mutant of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS in complex with methyl-tetrathio-alpha-d-cellopentoside at 1.1 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 1OC7 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, CELLULOSE DEGRADATION, CELLOBIOHYDROLASE, CELLULASE, GLYCOSIDE HYDROLASE FAMILY 6, PROCESSIVE MECHANISM' # 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 5 ? F N N 5 ? G N N 6 ? H N N 6 ? I N N 7 ? J N N 8 ? K N N 8 ? L N N 8 ? M N N 9 ? N N N 10 ? # _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 16 ? LEU A 26 ? ASN A 102 LEU A 112 1 ? 11 HELX_P HELX_P2 2 ALA A 27 ? ILE A 31 ? ALA A 113 ILE A 117 5 ? 5 HELX_P HELX_P3 3 ASP A 33 ? ALA A 44 ? ASP A 119 ALA A 130 1 ? 12 HELX_P HELX_P4 4 ARG A 54 ? VAL A 58 ? ARG A 140 VAL A 144 5 ? 5 HELX_P HELX_P5 5 THR A 60 ? ALA A 75 ? THR A 146 ALA A 161 1 ? 16 HELX_P HELX_P6 6 ALA A 105 ? ASN A 108 ? ALA A 191 ASN A 194 5 ? 4 HELX_P HELX_P7 7 ASN A 109 ? PHE A 128 ? ASN A 195 PHE A 214 1 ? 20 HELX_P HELX_P8 8 LEU A 142 ? ASN A 148 ? LEU A 228 ASN A 234 1 ? 7 HELX_P HELX_P9 9 VAL A 151 ? LEU A 172 ? VAL A 237 LEU A 258 1 ? 22 HELX_P HELX_P10 10 TRP A 191 ? ALA A 209 ? TRP A 277 ALA A 295 1 ? 19 HELX_P HELX_P11 11 PRO A 234 ? SER A 238 ? PRO A 320 SER A 324 5 ? 5 HELX_P HELX_P12 12 ASP A 244 ? ARG A 259 ? ASP A 330 ARG A 345 1 ? 16 HELX_P HELX_P13 13 ASP A 330 ? LEU A 335 ? ASP A 416 LEU A 421 5 ? 6 HELX_P HELX_P14 14 PHE A 349 ? ASN A 359 ? 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 95 SG ? ? ? 1_555 A CYS 154 SG ? ? A CYS 181 A CYS 240 1_555 ? ? ? ? ? ? ? 2.128 ? disulf2 disulf ? ? A CYS 286 SG ? ? ? 1_555 A CYS 333 SG ? ? A CYS 372 A CYS 419 1_555 ? ? ? ? ? ? ? 2.047 ? covale1 covale ? ? A ASN 55 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 141 A NAG 500 1_555 ? ? ? ? ? ? ? 1.441 ? metalc1 metalc ? ? C MG . MG ? ? ? 1_555 N HOH . O ? ? A MG 501 A HOH 2073 1_555 ? ? ? ? ? ? ? 2.071 ? metalc2 metalc ? ? C MG . MG ? ? ? 1_555 N HOH . O ? ? A MG 501 A HOH 2581 1_555 ? ? ? ? ? ? ? 2.088 ? metalc3 metalc ? ? C MG . MG ? ? ? 1_555 N HOH . O ? ? A MG 501 A HOH 2168 1_555 ? ? ? ? ? ? ? 2.059 ? metalc4 metalc ? ? C MG . MG ? ? ? 1_555 N HOH . O ? ? A MG 501 A HOH 2048 1_555 ? ? ? ? ? ? ? 2.085 ? metalc5 metalc ? ? C MG . MG ? ? ? 1_555 N HOH . O ? ? A MG 501 A HOH 2578 1_555 ? ? ? ? ? ? ? 2.026 ? metalc6 metalc ? ? C MG . MG ? ? ? 1_555 N HOH . O ? ? A MG 501 A HOH 2019 1_555 ? ? ? ? ? ? ? 2.057 ? covale2 covale ? ? I BGC . C1 ? ? ? 1_555 J SGC . S4 ? ? A BGC 601 A SGC 602 1_555 ? ? ? ? ? ? ? 1.805 ? covale3 covale ? ? J SGC . C1 ? ? ? 1_555 K SGC . S4 ? ? A SGC 602 A SGC 603 1_555 ? ? ? ? ? ? ? 1.829 ? covale4 covale ? ? K SGC . C1 ? ? ? 1_555 L SGC . S4 ? ? A SGC 603 A SGC 604 1_555 ? ? ? ? ? ? ? 1.810 ? covale5 covale ? ? L SGC . C1 ? ? ? 1_555 M MA3 . S4 ? ? A SGC 604 A MA3 605 1_555 ? ? ? ? ? ? ? 1.797 ? # 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 78 A . ? ASN 164 A PRO 79 A ? PRO 165 A 1 -4.07 2 SER 238 A . ? SER 324 A PRO 239 A ? PRO 325 A 1 1.72 3 GLN 275 A . ? GLN 361 A PRO 276 A ? PRO 362 A 1 -15.07 4 LYS 340 A . ? LYS 426 A PRO 341 A ? PRO 427 A 1 -6.40 5 ASN 361 A . ? ASN 447 A PRO 362 A ? PRO 448 A 1 3.54 # 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 12 ? LEU A 13 ? GLN A 98 LEU A 99 AA 2 TYR A 81 ? VAL A 87 ? TYR A 167 VAL A 173 AA 3 GLN A 50 ? LEU A 52 ? GLN A 136 LEU A 138 AB 1 GLN A 12 ? LEU A 13 ? GLN A 98 LEU A 99 AB 2 TYR A 81 ? VAL A 87 ? TYR A 167 VAL A 173 AB 3 THR A 133 ? ILE A 137 ? THR A 219 ILE A 223 AB 4 VAL A 177 ? ASP A 182 ? VAL A 263 ASP A 268 AB 5 VAL A 215 ? THR A 220 ? VAL A 301 THR A 306 AB 6 GLN A 264 ? ASP A 268 ? GLN A 350 ASP A 354 AB 7 VAL A 306 ? VAL A 310 ? 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 12 ? O GLN A 98 N ALA A 82 ? N ALA A 168 AA 2 3 N VAL A 86 ? N VAL A 172 O GLN A 50 ? O GLN A 136 AB 1 2 O GLN A 12 ? O GLN A 98 N ALA A 82 ? N ALA A 168 AB 2 3 N ILE A 85 ? N ILE A 171 O ILE A 134 ? O ILE A 220 AB 3 4 N LEU A 135 ? N LEU A 221 O ALA A 178 ? O ALA A 264 AB 4 5 O MET A 179 ? O MET A 265 N ARG A 216 ? N ARG A 302 AB 5 6 N LEU A 218 ? N LEU A 304 O GLN A 264 ? O GLN A 350 AB 6 7 O PHE A 265 ? O PHE A 351 N ASP A 307 ? 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 ? ? ? ? 15 'BINDING SITE FOR RESIDUE NAG A 500' AC2 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE BGC A 601' AC3 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE SGC A 602' AC4 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE SGC A 603' AC5 Software ? ? ? ? 13 'BINDING SITE FOR RESIDUE SGC A 604' AC6 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE MA3 A 605' AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MG A 501' AC8 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE ACT A 502' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE DMF A 503' BC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE DMF A 504' BC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE GOL A 505' BC3 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL A 506' # 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 15 ASN A 55 ? ASN A 141 . ? 1_555 ? 2 AC1 15 ASP A 59 ? ASP A 145 . ? 1_555 ? 3 AC1 15 ASN A 113 ? ASN A 199 . ? 1_555 ? 4 AC1 15 GLU A 281 ? GLU A 367 . ? 1_555 ? 5 AC1 15 HIS A 284 ? HIS A 370 . ? 1_555 ? 6 AC1 15 LEU A 335 ? LEU A 421 . ? 1_555 ? 7 AC1 15 HOH N . ? HOH A 2105 . ? 1_555 ? 8 AC1 15 HOH N . ? HOH A 2106 . ? 1_555 ? 9 AC1 15 HOH N . ? HOH A 2238 . ? 1_555 ? 10 AC1 15 HOH N . ? HOH A 2460 . ? 1_555 ? 11 AC1 15 HOH N . ? HOH A 2527 . ? 1_555 ? 12 AC1 15 HOH N . ? HOH A 2573 . ? 1_555 ? 13 AC1 15 HOH N . ? HOH A 2574 . ? 1_555 ? 14 AC1 15 HOH N . ? HOH A 2575 . ? 1_555 ? 15 AC1 15 HOH N . ? HOH A 2577 . ? 1_555 ? 16 AC2 11 TRP A 51 ? TRP A 137 . ? 1_555 ? 17 AC2 11 TYR A 88 ? TYR A 174 . ? 1_555 ? 18 AC2 11 ASN A 101 ? ASN A 187 . ? 1_555 ? 19 AC2 11 ALA A 223 ? ALA A 309 . ? 1_555 ? 20 AC2 11 SGC J . ? SGC A 602 . ? 1_555 ? 21 AC2 11 HOH N . ? HOH A 2205 . ? 1_555 ? 22 AC2 11 HOH N . ? HOH A 2586 . ? 1_555 ? 23 AC2 11 HOH N . ? HOH A 2587 . ? 1_555 ? 24 AC2 11 HOH N . ? HOH A 2588 . ? 1_555 ? 25 AC2 11 HOH N . ? HOH A 2589 . ? 1_555 ? 26 AC2 11 HOH N . ? HOH A 2590 . ? 1_555 ? 27 AC3 11 ALA A 97 ? ALA A 183 . ? 1_555 ? 28 AC3 11 ASN A 224 ? ASN A 310 . ? 1_555 ? 29 AC3 11 TRP A 285 ? TRP A 371 . ? 1_555 ? 30 AC3 11 BGC I . ? BGC A 601 . ? 1_555 ? 31 AC3 11 SGC K . ? SGC A 603 . ? 1_555 ? 32 AC3 11 HOH N . ? HOH A 2396 . ? 1_555 ? 33 AC3 11 HOH N . ? HOH A 2465 . ? 1_555 ? 34 AC3 11 HOH N . ? HOH A 2525 . ? 1_555 ? 35 AC3 11 HOH N . ? HOH A 2591 . ? 1_555 ? 36 AC3 11 HOH N . ? HOH A 2592 . ? 1_555 ? 37 AC3 11 HOH N . ? HOH A 2593 . ? 1_555 ? 38 AC4 13 ASN A 148 ? ASN A 234 . ? 1_555 ? 39 AC4 13 HIS A 185 ? HIS A 271 . ? 1_555 ? 40 AC4 13 TRP A 188 ? TRP A 274 . ? 1_555 ? 41 AC4 13 SGC J . ? SGC A 602 . ? 1_555 ? 42 AC4 13 SGC L . ? SGC A 604 . ? 1_555 ? 43 AC4 13 HOH N . ? HOH A 2308 . ? 1_555 ? 44 AC4 13 HOH N . ? HOH A 2463 . ? 1_555 ? 45 AC4 13 HOH N . ? HOH A 2592 . ? 1_555 ? 46 AC4 13 HOH N . ? HOH A 2593 . ? 1_555 ? 47 AC4 13 HOH N . ? HOH A 2594 . ? 1_555 ? 48 AC4 13 HOH N . ? HOH A 2595 . ? 1_555 ? 49 AC4 13 HOH N . ? HOH A 2596 . ? 1_555 ? 50 AC4 13 HOH N . ? HOH A 2597 . ? 1_555 ? 51 AC5 13 TRP A 188 ? TRP A 274 . ? 1_555 ? 52 AC5 13 ASN A 194 ? ASN A 280 . ? 1_555 ? 53 AC5 13 GLY A 283 ? GLY A 369 . ? 1_555 ? 54 AC5 13 SGC K . ? SGC A 603 . ? 1_555 ? 55 AC5 13 MA3 M . ? MA3 A 605 . ? 1_555 ? 56 AC5 13 HOH N . ? HOH A 2462 . ? 1_555 ? 57 AC5 13 HOH N . ? HOH A 2595 . ? 1_555 ? 58 AC5 13 HOH N . ? HOH A 2597 . ? 1_555 ? 59 AC5 13 HOH N . ? HOH A 2598 . ? 1_555 ? 60 AC5 13 HOH N . ? HOH A 2599 . ? 1_555 ? 61 AC5 13 HOH N . ? HOH A 2600 . ? 1_555 ? 62 AC5 13 HOH N . ? HOH A 2601 . ? 1_555 ? 63 AC5 13 HOH N . ? HOH A 2603 . ? 1_555 ? 64 AC6 9 GLU A 103 ? GLU A 189 . ? 1_555 ? 65 AC6 9 TRP A 191 ? TRP A 277 . ? 1_555 ? 66 AC6 9 ALA A 193 ? ALA A 279 . ? 1_555 ? 67 AC6 9 SGC L . ? SGC A 604 . ? 1_555 ? 68 AC6 9 HOH N . ? HOH A 2370 . ? 1_555 ? 69 AC6 9 HOH N . ? HOH A 2598 . ? 1_555 ? 70 AC6 9 HOH N . ? HOH A 2599 . ? 1_555 ? 71 AC6 9 HOH N . ? HOH A 2602 . ? 1_555 ? 72 AC6 9 HOH N . ? HOH A 2603 . ? 1_555 ? 73 AC7 6 HOH N . ? HOH A 2019 . ? 1_555 ? 74 AC7 6 HOH N . ? HOH A 2048 . ? 1_555 ? 75 AC7 6 HOH N . ? HOH A 2073 . ? 1_555 ? 76 AC7 6 HOH N . ? HOH A 2168 . ? 1_555 ? 77 AC7 6 HOH N . ? HOH A 2578 . ? 1_555 ? 78 AC7 6 HOH N . ? HOH A 2581 . ? 1_555 ? 79 AC8 7 GLN A 12 ? GLN A 98 . ? 1_555 ? 80 AC8 7 LEU A 13 ? LEU A 99 . ? 1_555 ? 81 AC8 7 PRO A 47 ? PRO A 133 . ? 1_555 ? 82 AC8 7 HOH N . ? HOH A 2019 . ? 1_555 ? 83 AC8 7 HOH N . ? HOH A 2578 . ? 1_555 ? 84 AC8 7 HOH N . ? HOH A 2579 . ? 1_555 ? 85 AC8 7 HOH N . ? HOH A 2580 . ? 1_555 ? 86 AC9 6 TRP A 14 ? TRP A 100 . ? 1_555 ? 87 AC9 6 ALA A 15 ? ALA A 101 . ? 1_555 ? 88 AC9 6 ARG A 20 ? ARG A 106 . ? 1_555 ? 89 AC9 6 GLU A 45 ? GLU A 131 . ? 1_555 ? 90 AC9 6 TYR A 81 ? TYR A 167 . ? 1_555 ? 91 AC9 6 HOH N . ? HOH A 2581 . ? 1_555 ? 92 BC1 6 GLU A 250 ? GLU A 336 . ? 1_555 ? 93 BC1 6 HIS A 303 ? HIS A 389 . ? 1_555 ? 94 BC1 6 TYR A 305 ? TYR A 391 . ? 1_555 ? 95 BC1 6 ARG A 358 ? ARG A 444 . ? 1_555 ? 96 BC1 6 ASN A 359 ? ASN A 445 . ? 1_555 ? 97 BC1 6 HOH N . ? HOH A 2582 . ? 1_555 ? 98 BC2 6 TYR A 206 ? TYR A 292 . ? 1_555 ? 99 BC2 6 VAL A 215 ? VAL A 301 . ? 1_555 ? 100 BC2 6 ARG A 216 ? ARG A 302 . ? 1_555 ? 101 BC2 6 PHE A 261 ? PHE A 347 . ? 1_555 ? 102 BC2 6 PRO A 262 ? PRO A 348 . ? 1_555 ? 103 BC2 6 HOH N . ? HOH A 2583 . ? 1_555 ? 104 BC3 9 ALA A 227 ? ALA A 313 . ? 1_555 ? 105 BC3 9 TRP A 228 ? TRP A 314 . ? 1_555 ? 106 BC3 9 SER A 229 ? SER A 315 . ? 1_555 ? 107 BC3 9 GLN A 269 ? GLN A 355 . ? 1_555 ? 108 BC3 9 SER A 272 ? SER A 358 . ? 1_555 ? 109 BC3 9 GLY A 273 ? GLY A 359 . ? 1_555 ? 110 BC3 9 ASN A 361 ? ASN A 447 . ? 1_555 ? 111 BC3 9 HOH N . ? HOH A 2584 . ? 1_555 ? 112 BC3 9 HOH N . ? HOH A 2585 . ? 1_555 ? # _database_PDB_matrix.entry_id 1OC7 _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 1OC7 _atom_sites.fract_transf_matrix[1][1] 0.017390 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.016626 _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] 0.010287 _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 . ALA A 1 1 ? -1.641 36.328 18.845 1.00 11.10 ? 87 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? -2.906 35.741 18.301 1.00 10.98 ? 87 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? -2.801 34.229 18.273 1.00 9.31 ? 87 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? -1.695 33.678 18.152 1.00 10.39 ? 87 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? -3.158 36.254 16.897 1.00 12.91 ? 87 ALA A CB 1 ATOM 6 N N . PRO A 1 2 ? -3.895 33.528 18.351 1.00 10.58 ? 88 PRO A N 1 ATOM 7 C CA . PRO A 1 2 ? -3.870 32.078 18.279 1.00 11.13 ? 88 PRO A CA 1 ATOM 8 C C . PRO A 1 2 ? -3.675 31.606 16.847 1.00 10.13 ? 88 PRO A C 1 ATOM 9 O O . PRO A 1 2 ? -3.801 32.381 15.887 1.00 11.67 ? 88 PRO A O 1 ATOM 10 C CB . PRO A 1 2 ? -5.242 31.692 18.781 1.00 13.72 ? 88 PRO A CB 1 ATOM 11 C CG . PRO A 1 2 ? -6.101 32.841 18.300 1.00 14.75 ? 88 PRO A CG 1 ATOM 12 C CD . PRO A 1 2 ? -5.278 34.067 18.458 1.00 11.79 ? 88 PRO A CD 1 ATOM 13 N N . TYR A 1 3 ? -3.416 30.331 16.702 1.00 10.93 ? 89 TYR A N 1 ATOM 14 C CA . TYR A 1 3 ? -3.362 29.692 15.408 1.00 10.83 ? 89 TYR A CA 1 ATOM 15 C C . TYR A 1 3 ? -3.925 28.267 15.592 1.00 10.02 ? 89 TYR A C 1 ATOM 16 O O . TYR A 1 3 ? -3.866 27.712 16.656 1.00 12.01 ? 89 TYR A O 1 ATOM 17 C CB . TYR A 1 3 ? -1.944 29.723 14.791 1.00 10.35 ? 89 TYR A CB 1 ATOM 18 C CG . TYR A 1 3 ? -0.946 28.842 15.590 1.00 9.25 ? 89 TYR A CG 1 ATOM 19 C CD1 . TYR A 1 3 ? -0.299 29.342 16.710 1.00 8.80 ? 89 TYR A CD1 1 ATOM 20 C CD2 . TYR A 1 3 ? -0.707 27.507 15.252 1.00 9.18 ? 89 TYR A CD2 1 ATOM 21 C CE1 . TYR A 1 3 ? 0.510 28.566 17.479 1.00 8.33 ? 89 TYR A CE1 1 ATOM 22 C CE2 . TYR A 1 3 ? 0.085 26.706 16.033 1.00 8.70 ? 89 TYR A CE2 1 ATOM 23 C CZ . TYR A 1 3 ? 0.704 27.230 17.161 1.00 8.30 ? 89 TYR A CZ 1 ATOM 24 O OH . TYR A 1 3 ? 1.435 26.398 17.963 1.00 8.70 ? 89 TYR A OH 1 ATOM 25 N N . ASN A 1 4 ? -4.347 27.706 14.472 1.00 11.83 ? 90 ASN A N 1 ATOM 26 C CA . ASN A 1 4 ? -4.765 26.302 14.413 1.00 11.87 ? 90 ASN A CA 1 ATOM 27 C C . ASN A 1 4 ? -3.801 25.513 13.516 1.00 10.86 ? 90 ASN A C 1 ATOM 28 O O . ASN A 1 4 ? -3.327 26.041 12.535 1.00 13.31 ? 90 ASN A O 1 ATOM 29 C CB . ASN A 1 4 ? -6.216 26.176 13.898 1.00 14.13 ? 90 ASN A CB 1 ATOM 30 C CG . ASN A 1 4 ? -7.229 26.882 14.797 1.00 17.37 ? 90 ASN A CG 1 ATOM 31 O OD1 . ASN A 1 4 ? -7.170 26.815 16.049 1.00 22.87 ? 90 ASN A OD1 1 ATOM 32 N ND2 . ASN A 1 4 ? -8.133 27.555 14.165 1.00 27.66 ? 90 ASN A ND2 1 ATOM 33 N N . GLY A 1 5 ? -3.534 24.297 13.855 1.00 10.47 ? 91 GLY A N 1 ATOM 34 C CA . GLY A 1 5 ? -2.789 23.453 12.979 1.00 9.60 ? 91 GLY A CA 1 ATOM 35 C C . GLY A 1 5 ? -1.303 23.791 12.861 1.00 8.83 ? 91 GLY A C 1 ATOM 36 O O . GLY A 1 5 ? -0.646 24.151 13.847 1.00 10.02 ? 91 GLY A O 1 ATOM 37 N N . ASN A 1 6 ? -0.780 23.615 11.648 1.00 8.47 ? 92 ASN A N 1 ATOM 38 C CA . ASN A 1 6 ? 0.658 23.751 11.378 1.00 7.95 ? 92 ASN A CA 1 ATOM 39 C C . ASN A 1 6 ? 1.065 25.214 11.524 1.00 7.11 ? 92 ASN A C 1 ATOM 40 O O . ASN A 1 6 ? 0.542 26.063 10.768 1.00 7.89 ? 92 ASN A O 1 ATOM 41 C CB . ASN A 1 6 ? 0.892 23.253 9.974 1.00 7.76 ? 92 ASN A CB 1 ATOM 42 C CG . ASN A 1 6 ? 2.342 23.348 9.541 1.00 7.14 ? 92 ASN A CG 1 ATOM 43 O OD1 . ASN A 1 6 ? 3.192 23.839 10.289 1.00 7.95 ? 92 ASN A OD1 1 ATOM 44 N ND2 . ASN A 1 6 ? 2.620 22.891 8.334 1.00 8.58 ? 92 ASN A ND2 1 ATOM 45 N N . PRO A 1 7 ? 1.953 25.565 12.451 1.00 7.21 ? 93 PRO A N 1 ATOM 46 C CA . PRO A 1 7 ? 2.325 26.970 12.647 1.00 7.46 ? 93 PRO A CA 1 ATOM 47 C C . PRO A 1 7 ? 3.062 27.570 11.473 1.00 7.76 ? 93 PRO A C 1 ATOM 48 O O . PRO A 1 7 ? 3.189 28.790 11.411 1.00 8.17 ? 93 PRO A O 1 ATOM 49 C CB . PRO A 1 7 ? 3.157 26.942 13.913 1.00 7.56 ? 93 PRO A CB 1 ATOM 50 C CG . PRO A 1 7 ? 3.817 25.559 13.864 1.00 7.24 ? 93 PRO A CG 1 ATOM 51 C CD . PRO A 1 7 ? 2.715 24.675 13.354 1.00 7.54 ? 93 PRO A CD 1 ATOM 52 N N . PHE A 1 8 ? 3.596 26.752 10.565 1.00 7.18 ? 94 PHE A N 1 ATOM 53 C CA . PHE A 1 8 ? 4.283 27.243 9.387 1.00 7.58 ? 94 PHE A CA 1 ATOM 54 C C . PHE A 1 8 ? 3.307 27.627 8.274 1.00 8.43 ? 94 PHE A C 1 ATOM 55 O O . PHE A 1 8 ? 3.723 28.247 7.300 1.00 8.54 ? 94 PHE A O 1 ATOM 56 C CB . PHE A 1 8 ? 5.303 26.245 8.864 1.00 7.65 ? 94 PHE A CB 1 ATOM 57 C CG . PHE A 1 8 ? 6.475 25.993 9.770 1.00 6.99 ? 94 PHE A CG 1 ATOM 58 C CD1 . PHE A 1 8 ? 6.398 25.123 10.844 1.00 7.11 ? 94 PHE A CD1 1 ATOM 59 C CD2 . PHE A 1 8 ? 7.644 26.667 9.559 1.00 7.35 ? 94 PHE A CD2 1 ATOM 60 C CE1 . PHE A 1 8 ? 7.498 24.927 11.666 1.00 7.53 ? 94 PHE A CE1 1 ATOM 61 C CE2 . PHE A 1 8 ? 8.758 26.469 10.339 1.00 7.13 ? 94 PHE A CE2 1 ATOM 62 C CZ . PHE A 1 8 ? 8.675 25.615 11.401 1.00 7.15 ? 94 PHE A CZ 1 ATOM 63 N N . GLU A 1 9 ? 2.058 27.218 8.393 1.00 8.71 ? 95 GLU A N 1 ATOM 64 C CA . GLU A 1 9 ? 1.064 27.548 7.359 1.00 10.07 ? 95 GLU A CA 1 ATOM 65 C C . GLU A 1 9 ? 0.537 28.957 7.579 1.00 10.30 ? 95 GLU A C 1 ATOM 66 O O . GLU A 1 9 ? 0.253 29.362 8.693 1.00 12.00 ? 95 GLU A O 1 ATOM 67 C CB A GLU A 1 9 ? -0.114 26.593 7.387 0.55 10.93 ? 95 GLU A CB 1 ATOM 68 C CB B GLU A 1 9 ? -0.079 26.533 7.446 0.45 11.15 ? 95 GLU A CB 1 ATOM 69 C CG A GLU A 1 9 ? 0.281 25.322 6.724 0.55 14.26 ? 95 GLU A CG 1 ATOM 70 C CG B GLU A 1 9 ? -0.982 26.448 6.250 0.45 12.67 ? 95 GLU A CG 1 ATOM 71 C CD A GLU A 1 9 ? -0.663 24.150 6.798 0.55 20.17 ? 95 GLU A CD 1 ATOM 72 C CD B GLU A 1 9 ? -0.264 25.828 5.043 0.45 18.08 ? 95 GLU A CD 1 ATOM 73 O OE1 A GLU A 1 9 ? -1.882 24.323 7.042 0.55 20.86 ? 95 GLU A OE1 1 ATOM 74 O OE1 B GLU A 1 9 ? 0.317 24.707 5.106 0.45 22.63 ? 95 GLU A OE1 1 ATOM 75 O OE2 A GLU A 1 9 ? -0.092 23.035 6.622 0.55 21.06 ? 95 GLU A OE2 1 ATOM 76 O OE2 B GLU A 1 9 ? -0.258 26.484 4.021 0.45 24.84 ? 95 GLU A OE2 1 ATOM 77 N N . GLY A 1 10 ? 0.439 29.689 6.470 1.00 12.26 ? 96 GLY A N 1 ATOM 78 C CA . GLY A 1 10 ? -0.186 30.971 6.520 1.00 13.37 ? 96 GLY A CA 1 ATOM 79 C C . GLY A 1 10 ? 0.687 32.126 6.952 1.00 12.16 ? 96 GLY A C 1 ATOM 80 O O . GLY A 1 10 ? 0.189 33.267 7.139 1.00 14.91 ? 96 GLY A O 1 ATOM 81 N N . VAL A 1 11 ? 1.981 31.900 7.122 1.00 10.53 ? 97 VAL A N 1 ATOM 82 C CA . VAL A 1 11 ? 2.972 32.894 7.445 1.00 9.40 ? 97 VAL A CA 1 ATOM 83 C C . VAL A 1 11 ? 4.161 32.795 6.507 1.00 9.05 ? 97 VAL A C 1 ATOM 84 O O . VAL A 1 11 ? 4.409 31.742 5.908 1.00 11.89 ? 97 VAL A O 1 ATOM 85 C CB . VAL A 1 11 ? 3.464 32.738 8.898 1.00 8.69 ? 97 VAL A CB 1 ATOM 86 C CG1 . VAL A 1 11 ? 2.349 33.071 9.884 1.00 12.36 ? 97 VAL A CG1 1 ATOM 87 C CG2 . VAL A 1 11 ? 4.005 31.348 9.181 1.00 9.87 ? 97 VAL A CG2 1 ATOM 88 N N . GLN A 1 12 ? 4.915 33.863 6.399 1.00 8.80 ? 98 GLN A N 1 ATOM 89 C CA . GLN A 1 12 ? 6.279 33.852 5.873 1.00 9.69 ? 98 GLN A CA 1 ATOM 90 C C . GLN A 1 12 ? 7.241 33.582 6.999 1.00 7.82 ? 98 GLN A C 1 ATOM 91 O O . GLN A 1 12 ? 6.942 33.856 8.145 1.00 8.96 ? 98 GLN A O 1 ATOM 92 C CB . GLN A 1 12 ? 6.588 35.296 5.285 1.00 11.91 ? 98 GLN A CB 1 ATOM 93 C CG . GLN A 1 12 ? 5.921 35.622 3.995 1.00 12.64 ? 98 GLN A CG 1 ATOM 94 C CD . GLN A 1 12 ? 6.487 36.890 3.475 1.00 14.11 ? 98 GLN A CD 1 ATOM 95 O OE1 . GLN A 1 12 ? 7.538 36.866 2.851 1.00 13.80 ? 98 GLN A OE1 1 ATOM 96 N NE2 . GLN A 1 12 ? 5.768 38.008 3.698 1.00 12.82 ? 98 GLN A NE2 1 ATOM 97 N N . LEU A 1 13 ? 8.450 33.199 6.690 1.00 7.83 ? 99 LEU A N 1 ATOM 98 C CA . LEU A 1 13 ? 9.486 33.007 7.713 1.00 7.34 ? 99 LEU A CA 1 ATOM 99 C C . LEU A 1 13 ? 10.484 34.141 7.611 1.00 7.15 ? 99 LEU A C 1 ATOM 100 O O . LEU A 1 13 ? 11.043 34.370 6.537 1.00 7.90 ? 99 LEU A O 1 ATOM 101 C CB . LEU A 1 13 ? 10.139 31.623 7.552 1.00 7.40 ? 99 LEU A CB 1 ATOM 102 C CG . LEU A 1 13 ? 9.178 30.439 7.730 1.00 7.75 ? 99 LEU A CG 1 ATOM 103 C CD1 . LEU A 1 13 ? 9.937 29.162 7.380 1.00 8.97 ? 99 LEU A CD1 1 ATOM 104 C CD2 . LEU A 1 13 ? 8.569 30.407 9.139 1.00 8.71 ? 99 LEU A CD2 1 ATOM 105 N N . TRP A 1 14 ? 10.695 34.842 8.709 1.00 7.15 ? 100 TRP A N 1 ATOM 106 C CA . TRP A 1 14 ? 11.657 35.951 8.771 1.00 7.30 ? 100 TRP A CA 1 ATOM 107 C C . TRP A 1 14 ? 13.073 35.450 8.645 1.00 7.11 ? 100 TRP A C 1 ATOM 108 O O . TRP A 1 14 ? 13.474 34.538 9.393 1.00 7.73 ? 100 TRP A O 1 ATOM 109 C CB . TRP A 1 14 ? 11.501 36.667 10.099 1.00 8.02 ? 100 TRP A CB 1 ATOM 110 C CG . TRP A 1 14 ? 12.404 37.813 10.336 1.00 8.20 ? 100 TRP A CG 1 ATOM 111 C CD1 . TRP A 1 14 ? 13.438 37.899 11.209 1.00 8.40 ? 100 TRP A CD1 1 ATOM 112 C CD2 . TRP A 1 14 ? 12.286 39.122 9.749 1.00 8.27 ? 100 TRP A CD2 1 ATOM 113 N NE1 . TRP A 1 14 ? 13.996 39.153 11.215 1.00 8.75 ? 100 TRP A NE1 1 ATOM 114 C CE2 . TRP A 1 14 ? 13.288 39.917 10.336 1.00 9.00 ? 100 TRP A CE2 1 ATOM 115 C CE3 . TRP A 1 14 ? 11.413 39.709 8.840 1.00 9.55 ? 100 TRP A CE3 1 ATOM 116 C CZ2 . TRP A 1 14 ? 13.458 41.265 10.012 1.00 9.90 ? 100 TRP A CZ2 1 ATOM 117 C CZ3 . TRP A 1 14 ? 11.578 41.078 8.546 1.00 10.55 ? 100 TRP A CZ3 1 ATOM 118 C CH2 . TRP A 1 14 ? 12.591 41.807 9.128 1.00 10.54 ? 100 TRP A CH2 1 ATOM 119 N N . ALA A 1 15 ? 13.862 36.085 7.793 1.00 7.29 ? 101 ALA A N 1 ATOM 120 C CA . ALA A 1 15 ? 15.288 35.833 7.655 1.00 7.91 ? 101 ALA A CA 1 ATOM 121 C C . ALA A 1 15 ? 15.965 36.910 8.486 1.00 8.34 ? 101 ALA A C 1 ATOM 122 O O . ALA A 1 15 ? 15.878 38.124 8.145 1.00 9.11 ? 101 ALA A O 1 ATOM 123 C CB . ALA A 1 15 ? 15.713 35.828 6.190 1.00 7.91 ? 101 ALA A CB 1 ATOM 124 N N . ASN A 1 16 ? 16.612 36.531 9.570 1.00 7.80 ? 102 ASN A N 1 ATOM 125 C CA . ASN A 1 16 ? 17.021 37.480 10.574 1.00 8.28 ? 102 ASN A CA 1 ATOM 126 C C . ASN A 1 16 ? 18.264 38.261 10.200 1.00 7.74 ? 102 ASN A C 1 ATOM 127 O O . ASN A 1 16 ? 19.091 37.876 9.366 1.00 8.37 ? 102 ASN A O 1 ATOM 128 C CB . ASN A 1 16 ? 17.163 36.778 11.964 1.00 8.41 ? 102 ASN A CB 1 ATOM 129 C CG . ASN A 1 16 ? 18.372 35.841 12.011 1.00 7.77 ? 102 ASN A CG 1 ATOM 130 O OD1 . ASN A 1 16 ? 19.512 36.322 12.061 1.00 8.49 ? 102 ASN A OD1 1 ATOM 131 N ND2 . ASN A 1 16 ? 18.127 34.541 11.967 1.00 8.32 ? 102 ASN A ND2 1 ATOM 132 N N . ASN A 1 17 ? 18.429 39.410 10.859 1.00 8.72 ? 103 ASN A N 1 ATOM 133 C CA . ASN A 1 17 ? 19.539 40.322 10.610 1.00 9.18 ? 103 ASN A CA 1 ATOM 134 C C . ASN A 1 17 ? 20.844 39.903 11.167 1.00 9.32 ? 103 ASN A C 1 ATOM 135 O O . ASN A 1 17 ? 21.874 40.432 10.715 1.00 9.60 ? 103 ASN A O 1 ATOM 136 C CB . ASN A 1 17 ? 19.154 41.747 11.001 1.00 10.02 ? 103 ASN A CB 1 ATOM 137 C CG . ASN A 1 17 ? 18.340 42.407 9.926 1.00 12.30 ? 103 ASN A CG 1 ATOM 138 O OD1 . ASN A 1 17 ? 18.773 42.430 8.754 1.00 13.51 ? 103 ASN A OD1 1 ATOM 139 N ND2 . ASN A 1 17 ? 17.148 42.916 10.271 1.00 13.31 ? 103 ASN A ND2 1 ATOM 140 N N . TYR A 1 18 ? 20.892 39.012 12.144 1.00 8.93 ? 104 TYR A N 1 ATOM 141 C CA . TYR A 1 18 ? 22.140 38.477 12.649 1.00 9.31 ? 104 TYR A CA 1 ATOM 142 C C . TYR A 1 18 ? 22.860 37.712 11.527 1.00 8.17 ? 104 TYR A C 1 ATOM 143 O O . TYR A 1 18 ? 23.985 38.004 11.171 1.00 8.55 ? 104 TYR A O 1 ATOM 144 C CB . TYR A 1 18 ? 21.897 37.658 13.897 1.00 9.48 ? 104 TYR A CB 1 ATOM 145 C CG . TYR A 1 18 ? 23.111 37.078 14.523 1.00 8.96 ? 104 TYR A CG 1 ATOM 146 C CD1 . TYR A 1 18 ? 23.663 35.879 14.080 1.00 10.40 ? 104 TYR A CD1 1 ATOM 147 C CD2 . TYR A 1 18 ? 23.714 37.676 15.624 1.00 9.66 ? 104 TYR A CD2 1 ATOM 148 C CE1 . TYR A 1 18 ? 24.727 35.311 14.695 1.00 11.51 ? 104 TYR A CE1 1 ATOM 149 C CE2 . TYR A 1 18 ? 24.791 37.063 16.250 1.00 10.95 ? 104 TYR A CE2 1 ATOM 150 C CZ . TYR A 1 18 ? 25.292 35.901 15.797 1.00 10.01 ? 104 TYR A CZ 1 ATOM 151 O OH . TYR A 1 18 ? 26.371 35.356 16.464 1.00 13.59 ? 104 TYR A OH 1 ATOM 152 N N . TYR A 1 19 ? 22.156 36.722 10.968 1.00 7.95 ? 105 TYR A N 1 ATOM 153 C CA . TYR A 1 19 ? 22.753 35.942 9.868 1.00 7.50 ? 105 TYR A CA 1 ATOM 154 C C . TYR A 1 19 ? 23.016 36.826 8.645 1.00 7.70 ? 105 TYR A C 1 ATOM 155 O O . TYR A 1 19 ? 24.062 36.731 8.001 1.00 7.73 ? 105 TYR A O 1 ATOM 156 C CB . TYR A 1 19 ? 21.843 34.773 9.512 1.00 7.87 ? 105 TYR A CB 1 ATOM 157 C CG . TYR A 1 19 ? 22.470 33.790 8.540 1.00 7.30 ? 105 TYR A CG 1 ATOM 158 C CD1 . TYR A 1 19 ? 23.377 32.859 8.982 1.00 7.39 ? 105 TYR A CD1 1 ATOM 159 C CD2 . TYR A 1 19 ? 22.191 33.857 7.179 1.00 7.65 ? 105 TYR A CD2 1 ATOM 160 C CE1 . TYR A 1 19 ? 23.981 31.960 8.118 1.00 7.87 ? 105 TYR A CE1 1 ATOM 161 C CE2 . TYR A 1 19 ? 22.796 32.980 6.289 1.00 7.47 ? 105 TYR A CE2 1 ATOM 162 C CZ . TYR A 1 19 ? 23.697 32.030 6.747 1.00 7.54 ? 105 TYR A CZ 1 ATOM 163 O OH . TYR A 1 19 ? 24.260 31.173 5.841 1.00 8.34 ? 105 TYR A OH 1 ATOM 164 N N . ARG A 1 20 ? 22.067 37.713 8.311 1.00 8.01 ? 106 ARG A N 1 ATOM 165 C CA . ARG A 1 20 ? 22.290 38.606 7.163 1.00 7.84 ? 106 ARG A CA 1 ATOM 166 C C . ARG A 1 20 ? 23.537 39.439 7.383 1.00 9.00 ? 106 ARG A C 1 ATOM 167 O O . ARG A 1 20 ? 24.321 39.623 6.436 1.00 8.86 ? 106 ARG A O 1 ATOM 168 C CB . ARG A 1 20 ? 21.054 39.463 6.961 1.00 9.06 ? 106 ARG A CB 1 ATOM 169 C CG . ARG A 1 20 ? 21.144 40.417 5.773 1.00 9.13 ? 106 ARG A CG 1 ATOM 170 C CD . ARG A 1 20 ? 19.889 41.276 5.563 1.00 9.75 ? 106 ARG A CD 1 ATOM 171 N NE . ARG A 1 20 ? 18.722 40.469 5.152 1.00 9.51 ? 106 ARG A NE 1 ATOM 172 C CZ . ARG A 1 20 ? 17.778 39.947 5.932 1.00 9.62 ? 106 ARG A CZ 1 ATOM 173 N NH1 . ARG A 1 20 ? 17.689 40.204 7.228 1.00 9.96 ? 106 ARG A NH1 1 ATOM 174 N NH2 . ARG A 1 20 ? 16.895 39.146 5.421 1.00 10.34 ? 106 ARG A NH2 1 ATOM 175 N N . SER A 1 21 ? 23.764 39.949 8.602 1.00 8.68 ? 107 SER A N 1 ATOM 176 C CA . SER A 1 21 ? 24.951 40.733 8.898 1.00 9.14 ? 107 SER A CA 1 ATOM 177 C C . SER A 1 21 ? 26.191 39.865 8.811 1.00 8.30 ? 107 SER A C 1 ATOM 178 O O . SER A 1 21 ? 27.244 40.321 8.367 1.00 9.55 ? 107 SER A O 1 ATOM 179 C CB A SER A 1 21 ? 24.812 41.432 10.243 0.52 10.21 ? 107 SER A CB 1 ATOM 180 C CB B SER A 1 21 ? 24.902 41.342 10.288 0.48 10.07 ? 107 SER A CB 1 ATOM 181 O OG A SER A 1 21 ? 25.046 40.566 11.343 0.52 10.94 ? 107 SER A OG 1 ATOM 182 O OG B SER A 1 21 ? 23.980 42.405 10.346 0.48 12.99 ? 107 SER A OG 1 ATOM 183 N N . GLU A 1 22 ? 26.163 38.613 9.259 1.00 8.48 ? 108 GLU A N 1 ATOM 184 C CA . GLU A 1 22 ? 27.319 37.751 9.083 1.00 8.24 ? 108 GLU A CA 1 ATOM 185 C C . GLU A 1 22 ? 27.681 37.659 7.612 1.00 8.28 ? 108 GLU A C 1 ATOM 186 O O . GLU A 1 22 ? 28.843 37.778 7.220 1.00 8.70 ? 108 GLU A O 1 ATOM 187 C CB . GLU A 1 22 ? 27.074 36.344 9.669 1.00 8.17 ? 108 GLU A CB 1 ATOM 188 C CG . GLU A 1 22 ? 26.997 36.338 11.181 1.00 8.39 ? 108 GLU A CG 1 ATOM 189 C CD . GLU A 1 22 ? 26.748 34.990 11.738 1.00 8.27 ? 108 GLU A CD 1 ATOM 190 O OE1 . GLU A 1 22 ? 25.686 34.419 11.304 1.00 8.53 ? 108 GLU A OE1 1 ATOM 191 O OE2 . GLU A 1 22 ? 27.518 34.452 12.568 1.00 9.11 ? 108 GLU A OE2 1 ATOM 192 N N . VAL A 1 23 ? 26.679 37.397 6.760 1.00 8.23 ? 109 VAL A N 1 ATOM 193 C CA . VAL A 1 23 ? 26.976 37.229 5.347 1.00 7.99 ? 109 VAL A CA 1 ATOM 194 C C . VAL A 1 23 ? 27.519 38.565 4.771 1.00 8.36 ? 109 VAL A C 1 ATOM 195 O O . VAL A 1 23 ? 28.500 38.551 4.021 1.00 9.40 ? 109 VAL A O 1 ATOM 196 C CB . VAL A 1 23 ? 25.750 36.698 4.560 1.00 8.23 ? 109 VAL A CB 1 ATOM 197 C CG1 . VAL A 1 23 ? 26.064 36.672 3.092 1.00 9.19 ? 109 VAL A CG1 1 ATOM 198 C CG2 . VAL A 1 23 ? 25.380 35.317 5.074 1.00 8.28 ? 109 VAL A CG2 1 ATOM 199 N N . HIS A 1 24 ? 26.834 39.655 5.008 1.00 8.93 ? 110 HIS A N 1 ATOM 200 C CA . HIS A 1 24 ? 27.229 40.908 4.374 1.00 9.48 ? 110 HIS A CA 1 ATOM 201 C C . HIS A 1 24 ? 28.488 41.540 4.928 1.00 10.00 ? 110 HIS A C 1 ATOM 202 O O . HIS A 1 24 ? 29.276 42.121 4.157 1.00 12.01 ? 110 HIS A O 1 ATOM 203 C CB . HIS A 1 24 ? 26.077 41.887 4.364 1.00 10.08 ? 110 HIS A CB 1 ATOM 204 C CG . HIS A 1 24 ? 25.079 41.539 3.312 1.00 9.80 ? 110 HIS A CG 1 ATOM 205 N ND1 . HIS A 1 24 ? 25.189 41.959 2.001 1.00 13.42 ? 110 HIS A ND1 1 ATOM 206 C CD2 . HIS A 1 24 ? 23.974 40.752 3.388 1.00 11.44 ? 110 HIS A CD2 1 ATOM 207 C CE1 . HIS A 1 24 ? 24.155 41.447 1.327 1.00 13.51 ? 110 HIS A CE1 1 ATOM 208 N NE2 . HIS A 1 24 ? 23.388 40.734 2.150 1.00 11.46 ? 110 HIS A NE2 1 ATOM 209 N N . THR A 1 25 ? 28.726 41.440 6.231 1.00 10.34 ? 111 THR A N 1 ATOM 210 C CA . THR A 1 25 ? 29.889 42.093 6.826 1.00 10.77 ? 111 THR A CA 1 ATOM 211 C C . THR A 1 25 ? 31.097 41.168 6.973 1.00 10.03 ? 111 THR A C 1 ATOM 212 O O . THR A 1 25 ? 32.237 41.642 7.012 1.00 11.59 ? 111 THR A O 1 ATOM 213 C CB . THR A 1 25 ? 29.552 42.750 8.135 1.00 13.72 ? 111 THR A CB 1 ATOM 214 O OG1 . THR A 1 25 ? 29.336 41.797 9.119 1.00 16.91 ? 111 THR A OG1 1 ATOM 215 C CG2 . THR A 1 25 ? 28.364 43.639 8.061 1.00 14.73 ? 111 THR A CG2 1 ATOM 216 N N . LEU A 1 26 ? 30.878 39.849 7.091 1.00 9.75 ? 112 LEU A N 1 ATOM 217 C CA . LEU A 1 26 ? 31.973 38.930 7.298 1.00 9.48 ? 112 LEU A CA 1 ATOM 218 C C . LEU A 1 26 ? 32.286 38.109 6.045 1.00 9.77 ? 112 LEU A C 1 ATOM 219 O O . LEU A 1 26 ? 33.459 37.938 5.700 1.00 12.74 ? 112 LEU A O 1 ATOM 220 C CB . LEU A 1 26 ? 31.725 37.985 8.492 1.00 9.07 ? 112 LEU A CB 1 ATOM 221 C CG . LEU A 1 26 ? 31.273 38.698 9.765 1.00 9.58 ? 112 LEU A CG 1 ATOM 222 C CD1 . LEU A 1 26 ? 31.021 37.689 10.866 1.00 9.45 ? 112 LEU A CD1 1 ATOM 223 C CD2 . LEU A 1 26 ? 32.281 39.728 10.277 1.00 11.12 ? 112 LEU A CD2 1 ATOM 224 N N . ALA A 1 27 ? 31.297 37.574 5.352 1.00 8.88 ? 113 ALA A N 1 ATOM 225 C CA . ALA A 1 27 ? 31.518 36.633 4.235 1.00 8.68 ? 113 ALA A CA 1 ATOM 226 C C . ALA A 1 27 ? 31.834 37.382 2.931 1.00 9.10 ? 113 ALA A C 1 ATOM 227 O O . ALA A 1 27 ? 32.878 37.141 2.320 1.00 10.52 ? 113 ALA A O 1 ATOM 228 C CB . ALA A 1 27 ? 30.335 35.723 4.045 1.00 8.62 ? 113 ALA A CB 1 ATOM 229 N N . ILE A 1 28 ? 30.891 38.215 2.485 1.00 9.39 ? 114 ILE A N 1 ATOM 230 C CA . ILE A 1 28 ? 30.959 38.861 1.160 1.00 9.53 ? 114 ILE A CA 1 ATOM 231 C C . ILE A 1 28 ? 32.250 39.638 1.004 1.00 10.31 ? 114 ILE A C 1 ATOM 232 O O . ILE A 1 28 ? 32.817 39.557 -0.100 1.00 11.51 ? 114 ILE A O 1 ATOM 233 C CB . ILE A 1 28 ? 29.654 39.598 0.860 1.00 10.23 ? 114 ILE A CB 1 ATOM 234 C CG1 . ILE A 1 28 ? 28.548 38.553 0.570 1.00 9.96 ? 114 ILE A CG1 1 ATOM 235 C CG2 . ILE A 1 28 ? 29.798 40.486 -0.382 1.00 12.35 ? 114 ILE A CG2 1 ATOM 236 C CD1 . ILE A 1 28 ? 27.165 39.123 0.409 1.00 11.01 ? 114 ILE A CD1 1 ATOM 237 N N . PRO A 1 29 ? 32.733 40.379 1.993 1.00 10.91 ? 115 PRO A N 1 ATOM 238 C CA . PRO A 1 29 ? 34.003 41.108 1.792 1.00 13.08 ? 115 PRO A CA 1 ATOM 239 C C . PRO A 1 29 ? 35.142 40.215 1.448 1.00 14.02 ? 115 PRO A C 1 ATOM 240 O O . PRO A 1 29 ? 36.195 40.741 0.982 1.00 17.75 ? 115 PRO A O 1 ATOM 241 C CB . PRO A 1 29 ? 34.150 41.910 3.095 1.00 14.23 ? 115 PRO A CB 1 ATOM 242 C CG . PRO A 1 29 ? 32.764 42.119 3.524 1.00 13.45 ? 115 PRO A CG 1 ATOM 243 C CD . PRO A 1 29 ? 32.094 40.765 3.265 1.00 11.57 ? 115 PRO A CD 1 ATOM 244 N N . GLN A 1 30 ? 35.073 38.922 1.773 1.00 13.98 ? 116 GLN A N 1 ATOM 245 C CA . GLN A 1 30 ? 36.138 37.936 1.516 1.00 14.64 ? 116 GLN A CA 1 ATOM 246 C C . GLN A 1 30 ? 35.947 37.230 0.187 1.00 15.32 ? 116 GLN A C 1 ATOM 247 O O . GLN A 1 30 ? 36.738 36.316 -0.108 1.00 18.49 ? 116 GLN A O 1 ATOM 248 C CB . GLN A 1 30 ? 36.227 36.931 2.677 1.00 15.34 ? 116 GLN A CB 1 ATOM 249 C CG . GLN A 1 30 ? 36.536 37.528 4.031 1.00 18.27 ? 116 GLN A CG 1 ATOM 250 C CD . GLN A 1 30 ? 36.704 36.401 5.100 1.00 22.79 ? 116 GLN A CD 1 ATOM 251 O OE1 . GLN A 1 30 ? 37.664 35.620 5.034 1.00 26.41 ? 116 GLN A OE1 1 ATOM 252 N NE2 . GLN A 1 30 ? 35.760 36.286 6.050 1.00 21.39 ? 116 GLN A NE2 1 ATOM 253 N N . ILE A 1 31 ? 34.881 37.539 -0.557 1.00 13.06 ? 117 ILE A N 1 ATOM 254 C CA . ILE A 1 31 ? 34.539 36.831 -1.759 1.00 13.22 ? 117 ILE A CA 1 ATOM 255 C C . ILE A 1 31 ? 34.711 37.776 -2.925 1.00 13.29 ? 117 ILE A C 1 ATOM 256 O O . ILE A 1 31 ? 34.069 38.848 -2.952 1.00 14.35 ? 117 ILE A O 1 ATOM 257 C CB . ILE A 1 31 ? 33.120 36.280 -1.703 1.00 12.71 ? 117 ILE A CB 1 ATOM 258 C CG1 . ILE A 1 31 ? 32.966 35.331 -0.484 1.00 13.58 ? 117 ILE A CG1 1 ATOM 259 C CG2 . ILE A 1 31 ? 32.779 35.559 -2.986 1.00 13.39 ? 117 ILE A CG2 1 ATOM 260 C CD1 . ILE A 1 31 ? 31.568 34.820 -0.232 1.00 14.38 ? 117 ILE A CD1 1 ATOM 261 N N . THR A 1 32 ? 35.576 37.449 -3.890 1.00 15.11 ? 118 THR A N 1 ATOM 262 C CA . THR A 1 32 ? 35.795 38.338 -5.073 1.00 15.13 ? 118 THR A CA 1 ATOM 263 C C . THR A 1 32 ? 35.054 37.873 -6.322 1.00 14.45 ? 118 THR A C 1 ATOM 264 O O . THR A 1 32 ? 34.782 38.665 -7.215 1.00 16.14 ? 118 THR A O 1 ATOM 265 C CB . THR A 1 32 ? 37.264 38.470 -5.420 1.00 16.64 ? 118 THR A CB 1 ATOM 266 O OG1 . THR A 1 32 ? 37.800 37.162 -5.669 1.00 19.66 ? 118 THR A OG1 1 ATOM 267 C CG2 . THR A 1 32 ? 38.056 39.071 -4.268 1.00 19.94 ? 118 THR A CG2 1 ATOM 268 N N . ASP A 1 33 ? 34.629 36.632 -6.383 1.00 14.12 ? 119 ASP A N 1 ATOM 269 C CA . ASP A 1 33 ? 33.976 36.151 -7.590 1.00 14.51 ? 119 ASP A CA 1 ATOM 270 C C . ASP A 1 33 ? 32.545 36.710 -7.719 1.00 14.16 ? 119 ASP A C 1 ATOM 271 O O . ASP A 1 33 ? 31.736 36.532 -6.763 1.00 14.08 ? 119 ASP A O 1 ATOM 272 C CB . ASP A 1 33 ? 33.893 34.647 -7.548 1.00 16.01 ? 119 ASP A CB 1 ATOM 273 C CG . ASP A 1 33 ? 33.140 34.120 -8.727 1.00 18.08 ? 119 ASP A CG 1 ATOM 274 O OD1 . ASP A 1 33 ? 33.648 34.223 -9.868 1.00 22.31 ? 119 ASP A OD1 1 ATOM 275 O OD2 . ASP A 1 33 ? 31.978 33.665 -8.658 1.00 19.78 ? 119 ASP A OD2 1 ATOM 276 N N . PRO A 1 34 ? 32.169 37.379 -8.791 1.00 14.03 ? 120 PRO A N 1 ATOM 277 C CA . PRO A 1 34 ? 30.840 37.990 -8.856 1.00 14.71 ? 120 PRO A CA 1 ATOM 278 C C . PRO A 1 34 ? 29.697 37.006 -8.598 1.00 14.56 ? 120 PRO A C 1 ATOM 279 O O . PRO A 1 34 ? 28.741 37.293 -7.890 1.00 14.40 ? 120 PRO A O 1 ATOM 280 C CB . PRO A 1 34 ? 30.791 38.596 -10.275 1.00 15.96 ? 120 PRO A CB 1 ATOM 281 C CG . PRO A 1 34 ? 32.257 38.992 -10.505 1.00 15.83 ? 120 PRO A CG 1 ATOM 282 C CD . PRO A 1 34 ? 33.044 37.816 -9.936 1.00 14.63 ? 120 PRO A CD 1 ATOM 283 N N . ALA A 1 35 ? 29.758 35.834 -9.217 1.00 15.47 ? 121 ALA A N 1 ATOM 284 C CA . ALA A 1 35 ? 28.619 34.910 -9.089 1.00 15.46 ? 121 ALA A CA 1 ATOM 285 C C . ALA A 1 35 ? 28.521 34.372 -7.651 1.00 14.65 ? 121 ALA A C 1 ATOM 286 O O . ALA A 1 35 ? 27.424 34.276 -7.088 1.00 14.88 ? 121 ALA A O 1 ATOM 287 C CB . ALA A 1 35 ? 28.676 33.806 -10.123 1.00 16.47 ? 121 ALA A CB 1 ATOM 288 N N . LEU A 1 36 ? 29.630 34.108 -7.013 1.00 14.03 ? 122 LEU A N 1 ATOM 289 C CA . LEU A 1 36 ? 29.600 33.639 -5.616 1.00 13.42 ? 122 LEU A CA 1 ATOM 290 C C . LEU A 1 36 ? 29.133 34.759 -4.683 1.00 12.54 ? 122 LEU A C 1 ATOM 291 O O . LEU A 1 36 ? 28.440 34.493 -3.689 1.00 12.29 ? 122 LEU A O 1 ATOM 292 C CB . LEU A 1 36 ? 30.935 33.071 -5.161 1.00 14.81 ? 122 LEU A CB 1 ATOM 293 C CG . LEU A 1 36 ? 31.342 31.606 -5.415 1.00 17.05 ? 122 LEU A CG 1 ATOM 294 C CD1 . LEU A 1 36 ? 32.686 31.415 -4.809 1.00 22.26 ? 122 LEU A CD1 1 ATOM 295 C CD2 . LEU A 1 36 ? 30.294 30.679 -4.790 1.00 20.75 ? 122 LEU A CD2 1 ATOM 296 N N . ARG A 1 37 ? 29.492 36.020 -4.971 1.00 11.51 ? 123 ARG A N 1 ATOM 297 C CA . ARG A 1 37 ? 28.980 37.106 -4.149 1.00 10.22 ? 123 ARG A CA 1 ATOM 298 C C . ARG A 1 37 ? 27.466 37.172 -4.241 1.00 11.02 ? 123 ARG A C 1 ATOM 299 O O . ARG A 1 37 ? 26.775 37.417 -3.249 1.00 11.23 ? 123 ARG A O 1 ATOM 300 C CB . ARG A 1 37 ? 29.579 38.426 -4.629 1.00 11.29 ? 123 ARG A CB 1 ATOM 301 C CG . ARG A 1 37 ? 31.049 38.635 -4.296 1.00 12.11 ? 123 ARG A CG 1 ATOM 302 C CD . ARG A 1 37 ? 31.632 39.927 -4.839 1.00 11.98 ? 123 ARG A CD 1 ATOM 303 N NE . ARG A 1 37 ? 30.922 41.078 -4.300 1.00 12.72 ? 123 ARG A NE 1 ATOM 304 C CZ . ARG A 1 37 ? 31.311 41.659 -3.174 1.00 12.41 ? 123 ARG A CZ 1 ATOM 305 N NH1 . ARG A 1 37 ? 32.376 41.216 -2.522 1.00 13.59 ? 123 ARG A NH1 1 ATOM 306 N NH2 . ARG A 1 37 ? 30.692 42.757 -2.769 1.00 13.76 ? 123 ARG A NH2 1 ATOM 307 N N . ALA A 1 38 ? 26.949 37.085 -5.455 1.00 11.41 ? 124 ALA A N 1 ATOM 308 C CA . ALA A 1 38 ? 25.496 37.112 -5.663 1.00 11.74 ? 124 ALA A CA 1 ATOM 309 C C . ALA A 1 38 ? 24.787 35.933 -4.958 1.00 11.22 ? 124 ALA A C 1 ATOM 310 O O . ALA A 1 38 ? 23.726 36.117 -4.356 1.00 11.79 ? 124 ALA A O 1 ATOM 311 C CB . ALA A 1 38 ? 25.113 37.168 -7.115 1.00 13.12 ? 124 ALA A CB 1 ATOM 312 N N . ALA A 1 39 ? 25.377 34.757 -5.061 1.00 10.98 ? 125 ALA A N 1 ATOM 313 C CA . ALA A 1 39 ? 24.854 33.579 -4.373 1.00 10.93 ? 125 ALA A CA 1 ATOM 314 C C . ALA A 1 39 ? 24.851 33.782 -2.873 1.00 9.79 ? 125 ALA A C 1 ATOM 315 O O . ALA A 1 39 ? 23.898 33.448 -2.156 1.00 10.64 ? 125 ALA A O 1 ATOM 316 C CB . ALA A 1 39 ? 25.681 32.379 -4.763 1.00 12.77 ? 125 ALA A CB 1 ATOM 317 N N . ALA A 1 40 ? 25.958 34.366 -2.336 1.00 10.01 ? 126 ALA A N 1 ATOM 318 C CA . ALA A 1 40 ? 26.046 34.667 -0.922 1.00 10.41 ? 126 ALA A CA 1 ATOM 319 C C . ALA A 1 40 ? 24.937 35.609 -0.493 1.00 9.07 ? 126 ALA A C 1 ATOM 320 O O . ALA A 1 40 ? 24.283 35.416 0.548 1.00 9.68 ? 126 ALA A O 1 ATOM 321 C CB . ALA A 1 40 ? 27.435 35.219 -0.594 1.00 10.23 ? 126 ALA A CB 1 ATOM 322 N N . SER A 1 41 ? 24.745 36.687 -1.278 1.00 9.74 ? 127 SER A N 1 ATOM 323 C CA . SER A 1 41 ? 23.705 37.607 -0.956 1.00 10.14 ? 127 SER A CA 1 ATOM 324 C C . SER A 1 41 ? 22.346 36.922 -0.902 1.00 9.28 ? 127 SER A C 1 ATOM 325 O O . SER A 1 41 ? 21.493 37.232 -0.070 1.00 10.46 ? 127 SER A O 1 ATOM 326 C CB A SER A 1 41 ? 23.759 38.808 -1.894 0.70 11.82 ? 127 SER A CB 1 ATOM 327 C CB B SER A 1 41 ? 23.633 38.732 -1.996 0.30 11.34 ? 127 SER A CB 1 ATOM 328 O OG A SER A 1 41 ? 22.814 39.764 -1.444 0.70 12.97 ? 127 SER A OG 1 ATOM 329 O OG B SER A 1 41 ? 24.759 39.573 -1.896 0.30 13.89 ? 127 SER A OG 1 ATOM 330 N N . ALA A 1 42 ? 22.105 35.992 -1.817 1.00 8.99 ? 128 ALA A N 1 ATOM 331 C CA . ALA A 1 42 ? 20.835 35.270 -1.838 1.00 8.18 ? 128 ALA A CA 1 ATOM 332 C C . ALA A 1 42 ? 20.675 34.382 -0.610 1.00 7.54 ? 128 ALA A C 1 ATOM 333 O O . ALA A 1 42 ? 19.592 34.293 -0.061 1.00 8.96 ? 128 ALA A O 1 ATOM 334 C CB . ALA A 1 42 ? 20.720 34.481 -3.112 1.00 9.21 ? 128 ALA A CB 1 ATOM 335 N N . VAL A 1 43 ? 21.735 33.697 -0.169 1.00 7.96 ? 129 VAL A N 1 ATOM 336 C CA A VAL A 1 43 ? 21.558 32.810 0.970 0.60 7.87 ? 129 VAL A CA 1 ATOM 337 C CA B VAL A 1 43 ? 21.649 32.810 1.000 0.40 8.10 ? 129 VAL A CA 1 ATOM 338 C C . VAL A 1 43 ? 21.300 33.602 2.251 1.00 7.48 ? 129 VAL A C 1 ATOM 339 O O . VAL A 1 43 ? 20.628 33.110 3.161 1.00 7.83 ? 129 VAL A O 1 ATOM 340 C CB A VAL A 1 43 ? 22.620 31.754 1.064 0.60 8.66 ? 129 VAL A CB 1 ATOM 341 C CB B VAL A 1 43 ? 22.931 31.993 1.280 0.40 8.40 ? 129 VAL A CB 1 ATOM 342 C CG1 A VAL A 1 43 ? 23.879 32.353 1.500 0.60 7.83 ? 129 VAL A CG1 1 ATOM 343 C CG1 B VAL A 1 43 ? 22.634 30.910 2.311 0.40 11.11 ? 129 VAL A CG1 1 ATOM 344 C CG2 A VAL A 1 43 ? 22.131 30.589 1.961 0.60 8.49 ? 129 VAL A CG2 1 ATOM 345 C CG2 B VAL A 1 43 ? 23.441 31.300 0.037 0.40 11.13 ? 129 VAL A CG2 1 ATOM 346 N N . ALA A 1 44 ? 21.781 34.841 2.343 1.00 7.73 ? 130 ALA A N 1 ATOM 347 C CA . ALA A 1 44 ? 21.470 35.708 3.468 1.00 8.20 ? 130 ALA A CA 1 ATOM 348 C C . ALA A 1 44 ? 19.992 35.959 3.635 1.00 8.34 ? 130 ALA A C 1 ATOM 349 O O . ALA A 1 44 ? 19.554 36.357 4.731 1.00 9.25 ? 130 ALA A O 1 ATOM 350 C CB . ALA A 1 44 ? 22.191 37.040 3.328 1.00 9.33 ? 130 ALA A CB 1 ATOM 351 N N . GLU A 1 45 ? 19.216 35.751 2.577 1.00 8.05 ? 131 GLU A N 1 ATOM 352 C CA . GLU A 1 45 ? 17.762 35.947 2.592 1.00 8.22 ? 131 GLU A CA 1 ATOM 353 C C . GLU A 1 45 ? 16.989 34.689 2.877 1.00 7.85 ? 131 GLU A C 1 ATOM 354 O O . GLU A 1 45 ? 15.754 34.715 2.903 1.00 8.56 ? 131 GLU A O 1 ATOM 355 C CB . GLU A 1 45 ? 17.306 36.550 1.260 1.00 8.72 ? 131 GLU A CB 1 ATOM 356 C CG . GLU A 1 45 ? 17.988 37.885 0.915 1.00 8.93 ? 131 GLU A CG 1 ATOM 357 C CD . GLU A 1 45 ? 17.830 38.878 2.030 1.00 9.44 ? 131 GLU A CD 1 ATOM 358 O OE1 . GLU A 1 45 ? 16.678 39.107 2.490 1.00 10.80 ? 131 GLU A OE1 1 ATOM 359 O OE2 . GLU A 1 45 ? 18.842 39.449 2.491 1.00 11.10 ? 131 GLU A OE2 1 ATOM 360 N N . VAL A 1 46 ? 17.678 33.564 3.110 1.00 7.06 ? 132 VAL A N 1 ATOM 361 C CA . VAL A 1 46 ? 16.999 32.300 3.442 1.00 6.84 ? 132 VAL A CA 1 ATOM 362 C C . VAL A 1 46 ? 16.730 32.278 4.958 1.00 6.96 ? 132 VAL A C 1 ATOM 363 O O . VAL A 1 46 ? 17.657 32.513 5.739 1.00 8.28 ? 132 VAL A O 1 ATOM 364 C CB . VAL A 1 46 ? 17.847 31.101 3.003 1.00 7.93 ? 132 VAL A CB 1 ATOM 365 C CG1 . VAL A 1 46 ? 17.132 29.800 3.426 1.00 7.99 ? 132 VAL A CG1 1 ATOM 366 C CG2 . VAL A 1 46 ? 18.044 31.115 1.507 1.00 8.75 ? 132 VAL A CG2 1 ATOM 367 N N . PRO A 1 47 ? 15.517 32.021 5.382 1.00 6.72 ? 133 PRO A N 1 ATOM 368 C CA . PRO A 1 47 ? 15.184 32.182 6.806 1.00 7.17 ? 133 PRO A CA 1 ATOM 369 C C . PRO A 1 47 ? 15.550 30.953 7.658 1.00 6.62 ? 133 PRO A C 1 ATOM 370 O O . PRO A 1 47 ? 14.803 29.989 7.697 1.00 8.25 ? 133 PRO A O 1 ATOM 371 C CB . PRO A 1 47 ? 13.680 32.452 6.767 1.00 7.54 ? 133 PRO A CB 1 ATOM 372 C CG . PRO A 1 47 ? 13.212 31.666 5.568 1.00 8.01 ? 133 PRO A CG 1 ATOM 373 C CD . PRO A 1 47 ? 14.313 31.867 4.534 1.00 7.32 ? 133 PRO A CD 1 ATOM 374 N N . SER A 1 48 ? 16.645 31.091 8.404 1.00 6.94 ? 134 SER A N 1 ATOM 375 C CA . SER A 1 48 ? 17.134 30.080 9.308 1.00 6.22 ? 134 SER A CA 1 ATOM 376 C C . SER A 1 48 ? 16.804 30.465 10.761 1.00 6.42 ? 134 SER A C 1 ATOM 377 O O . SER A 1 48 ? 16.561 31.628 11.115 1.00 6.98 ? 134 SER A O 1 ATOM 378 C CB . SER A 1 48 ? 18.638 29.869 9.149 1.00 7.07 ? 134 SER A CB 1 ATOM 379 O OG . SER A 1 48 ? 19.348 31.099 9.248 1.00 7.34 ? 134 SER A OG 1 ATOM 380 N N . PHE A 1 49 ? 16.803 29.464 11.643 1.00 6.35 ? 135 PHE A N 1 ATOM 381 C CA . PHE A 1 49 ? 16.576 29.700 13.066 1.00 6.20 ? 135 PHE A CA 1 ATOM 382 C C . PHE A 1 49 ? 17.654 30.556 13.674 1.00 6.26 ? 135 PHE A C 1 ATOM 383 O O . PHE A 1 49 ? 18.837 30.467 13.336 1.00 6.81 ? 135 PHE A O 1 ATOM 384 C CB . PHE A 1 49 ? 16.520 28.354 13.834 1.00 6.31 ? 135 PHE A CB 1 ATOM 385 C CG . PHE A 1 49 ? 15.187 27.654 13.804 1.00 6.11 ? 135 PHE A CG 1 ATOM 386 C CD1 . PHE A 1 49 ? 14.654 27.076 12.652 1.00 5.66 ? 135 PHE A CD1 1 ATOM 387 C CD2 . PHE A 1 49 ? 14.425 27.593 14.944 1.00 6.02 ? 135 PHE A CD2 1 ATOM 388 C CE1 . PHE A 1 49 ? 13.400 26.497 12.640 1.00 6.30 ? 135 PHE A CE1 1 ATOM 389 C CE2 . PHE A 1 49 ? 13.171 27.024 14.968 1.00 6.48 ? 135 PHE A CE2 1 ATOM 390 C CZ . PHE A 1 49 ? 12.664 26.468 13.797 1.00 6.70 ? 135 PHE A CZ 1 ATOM 391 N N . GLN A 1 50 ? 17.247 31.344 14.672 1.00 6.61 ? 136 GLN A N 1 ATOM 392 C CA . GLN A 1 50 ? 18.129 32.107 15.532 1.00 7.29 ? 136 GLN A CA 1 ATOM 393 C C . GLN A 1 50 ? 18.272 31.405 16.880 1.00 6.63 ? 136 GLN A C 1 ATOM 394 O O . GLN A 1 50 ? 17.266 31.035 17.478 1.00 7.56 ? 136 GLN A O 1 ATOM 395 C CB A GLN A 1 50 ? 17.583 33.519 15.708 0.70 8.63 ? 136 GLN A CB 1 ATOM 396 C CB B GLN A 1 50 ? 17.517 33.490 15.728 0.30 8.14 ? 136 GLN A CB 1 ATOM 397 C CG A GLN A 1 50 ? 18.346 34.359 16.717 0.70 10.23 ? 136 GLN A CG 1 ATOM 398 C CG B GLN A 1 50 ? 18.504 34.508 16.210 0.30 10.75 ? 136 GLN A CG 1 ATOM 399 C CD A GLN A 1 50 ? 18.183 35.805 16.456 0.70 10.73 ? 136 GLN A CD 1 ATOM 400 C CD B GLN A 1 50 ? 17.840 35.844 16.394 0.30 12.89 ? 136 GLN A CD 1 ATOM 401 O OE1 A GLN A 1 50 ? 17.154 36.377 16.868 0.70 14.18 ? 136 GLN A OE1 1 ATOM 402 O OE1 B GLN A 1 50 ? 17.602 36.284 17.511 0.30 12.89 ? 136 GLN A OE1 1 ATOM 403 N NE2 A GLN A 1 50 ? 19.088 36.411 15.766 0.70 11.37 ? 136 GLN A NE2 1 ATOM 404 N NE2 B GLN A 1 50 ? 17.461 36.452 15.307 0.30 9.40 ? 136 GLN A NE2 1 ATOM 405 N N . TRP A 1 51 ? 19.491 31.197 17.328 1.00 7.26 ? 137 TRP A N 1 ATOM 406 C CA . TRP A 1 51 ? 19.764 30.396 18.525 1.00 7.19 ? 137 TRP A CA 1 ATOM 407 C C . TRP A 1 51 ? 19.987 31.223 19.767 1.00 6.78 ? 137 TRP A C 1 ATOM 408 O O . TRP A 1 51 ? 20.863 32.096 19.792 1.00 8.38 ? 137 TRP A O 1 ATOM 409 C CB . TRP A 1 51 ? 20.996 29.513 18.302 1.00 7.92 ? 137 TRP A CB 1 ATOM 410 C CG . TRP A 1 51 ? 20.802 28.426 17.264 1.00 7.77 ? 137 TRP A CG 1 ATOM 411 C CD1 . TRP A 1 51 ? 20.395 28.559 15.955 1.00 7.37 ? 137 TRP A CD1 1 ATOM 412 C CD2 . TRP A 1 51 ? 21.068 27.042 17.451 1.00 7.25 ? 137 TRP A CD2 1 ATOM 413 N NE1 . TRP A 1 51 ? 20.382 27.345 15.332 1.00 7.68 ? 137 TRP A NE1 1 ATOM 414 C CE2 . TRP A 1 51 ? 20.784 26.383 16.212 1.00 7.32 ? 137 TRP A CE2 1 ATOM 415 C CE3 . TRP A 1 51 ? 21.506 26.277 18.537 1.00 8.21 ? 137 TRP A CE3 1 ATOM 416 C CZ2 . TRP A 1 51 ? 20.952 25.021 16.056 1.00 8.03 ? 137 TRP A CZ2 1 ATOM 417 C CZ3 . TRP A 1 51 ? 21.676 24.922 18.370 1.00 9.17 ? 137 TRP A CZ3 1 ATOM 418 C CH2 . TRP A 1 51 ? 21.388 24.290 17.138 1.00 8.20 ? 137 TRP A CH2 1 ATOM 419 N N . LEU A 1 52 ? 19.263 30.882 20.835 1.00 6.73 ? 138 LEU A N 1 ATOM 420 C CA . LEU A 1 52 ? 19.502 31.485 22.163 1.00 6.65 ? 138 LEU A CA 1 ATOM 421 C C . LEU A 1 52 ? 20.416 30.538 22.900 1.00 6.43 ? 138 LEU A C 1 ATOM 422 O O . LEU A 1 52 ? 20.057 29.908 23.910 1.00 8.17 ? 138 LEU A O 1 ATOM 423 C CB . LEU A 1 52 ? 18.169 31.728 22.886 1.00 6.89 ? 138 LEU A CB 1 ATOM 424 C CG . LEU A 1 52 ? 17.133 32.485 22.102 1.00 7.74 ? 138 LEU A CG 1 ATOM 425 C CD1 . LEU A 1 52 ? 15.884 32.696 22.959 1.00 8.34 ? 138 LEU A CD1 1 ATOM 426 C CD2 . LEU A 1 52 ? 17.639 33.804 21.538 1.00 8.90 ? 138 LEU A CD2 1 ATOM 427 N N . ASP A 1 53 ? 21.645 30.425 22.439 1.00 6.91 ? 139 ASP A N 1 ATOM 428 C CA . ASP A 1 53 ? 22.594 29.455 22.943 1.00 7.07 ? 139 ASP A CA 1 ATOM 429 C C . ASP A 1 53 ? 23.472 29.975 24.085 1.00 7.06 ? 139 ASP A C 1 ATOM 430 O O . ASP A 1 53 ? 24.257 29.228 24.648 1.00 8.93 ? 139 ASP A O 1 ATOM 431 C CB . ASP A 1 53 ? 23.469 28.942 21.829 1.00 8.42 ? 139 ASP A CB 1 ATOM 432 C CG . ASP A 1 53 ? 24.337 29.988 21.253 1.00 10.80 ? 139 ASP A CG 1 ATOM 433 O OD1 . ASP A 1 53 ? 24.011 31.149 21.082 1.00 12.79 ? 139 ASP A OD1 1 ATOM 434 O OD2 . ASP A 1 53 ? 25.508 29.674 20.955 1.00 21.87 ? 139 ASP A OD2 1 ATOM 435 N N . ARG A 1 54 ? 23.280 31.232 24.440 1.00 7.80 ? 140 ARG A N 1 ATOM 436 C CA . ARG A 1 54 ? 23.904 31.890 25.578 1.00 9.36 ? 140 ARG A CA 1 ATOM 437 C C . ARG A 1 54 ? 22.863 32.831 26.160 1.00 7.75 ? 140 ARG A C 1 ATOM 438 O O . ARG A 1 54 ? 22.088 33.429 25.405 1.00 8.70 ? 140 ARG A O 1 ATOM 439 C CB . ARG A 1 54 ? 25.142 32.717 25.161 1.00 11.47 ? 140 ARG A CB 1 ATOM 440 C CG . ARG A 1 54 ? 26.256 31.900 24.628 1.00 16.83 ? 140 ARG A CG 1 ATOM 441 C CD . ARG A 1 54 ? 27.223 32.740 23.831 1.00 23.81 ? 140 ARG A CD 1 ATOM 442 N NE . ARG A 1 54 ? 26.558 33.281 22.640 1.00 27.91 ? 140 ARG A NE 1 ATOM 443 C CZ . ARG A 1 54 ? 26.551 34.588 22.273 1.00 32.43 ? 140 ARG A CZ 1 ATOM 444 N NH1 . ARG A 1 54 ? 27.243 35.517 22.904 1.00 35.30 ? 140 ARG A NH1 1 ATOM 445 N NH2 . ARG A 1 54 ? 25.886 34.969 21.190 1.00 37.61 ? 140 ARG A NH2 1 ATOM 446 N N . ASN A 1 55 ? 22.855 33.000 27.470 1.00 7.83 ? 141 ASN A N 1 ATOM 447 C CA . ASN A 1 55 ? 21.878 33.849 28.110 1.00 7.90 ? 141 ASN A CA 1 ATOM 448 C C . ASN A 1 55 ? 21.845 35.266 27.615 1.00 7.35 ? 141 ASN A C 1 ATOM 449 O O . ASN A 1 55 ? 20.762 35.881 27.548 1.00 7.55 ? 141 ASN A O 1 ATOM 450 C CB . ASN A 1 55 ? 22.096 33.742 29.612 1.00 8.23 ? 141 ASN A CB 1 ATOM 451 C CG . ASN A 1 55 ? 21.063 34.490 30.426 1.00 7.69 ? 141 ASN A CG 1 ATOM 452 O OD1 . ASN A 1 55 ? 19.855 34.250 30.285 1.00 8.10 ? 141 ASN A OD1 1 ATOM 453 N ND2 . ASN A 1 55 ? 21.536 35.361 31.322 1.00 7.51 ? 141 ASN A ND2 1 ATOM 454 N N . VAL A 1 56 ? 22.994 35.829 27.241 1.00 8.07 ? 142 VAL A N 1 ATOM 455 C CA . VAL A 1 56 ? 23.056 37.205 26.773 1.00 8.27 ? 142 VAL A CA 1 ATOM 456 C C . VAL A 1 56 ? 22.207 37.432 25.520 1.00 8.41 ? 142 VAL A C 1 ATOM 457 O O . VAL A 1 56 ? 21.875 38.573 25.202 1.00 9.17 ? 142 VAL A O 1 ATOM 458 C CB A VAL A 1 56 ? 24.442 37.776 26.505 0.53 9.71 ? 142 VAL A CB 1 ATOM 459 C CB B VAL A 1 56 ? 24.542 37.509 26.484 0.47 9.62 ? 142 VAL A CB 1 ATOM 460 C CG1 A VAL A 1 56 ? 25.199 38.023 27.825 0.53 9.05 ? 142 VAL A CG1 1 ATOM 461 C CG1 B VAL A 1 56 ? 25.128 36.662 25.318 0.47 9.68 ? 142 VAL A CG1 1 ATOM 462 C CG2 A VAL A 1 56 ? 25.233 36.850 25.610 0.53 10.15 ? 142 VAL A CG2 1 ATOM 463 C CG2 B VAL A 1 56 ? 24.688 38.927 26.135 0.47 11.63 ? 142 VAL A CG2 1 ATOM 464 N N . THR A 1 57 ? 21.856 36.373 24.767 1.00 7.57 ? 143 THR A N 1 ATOM 465 C CA . THR A 1 57 ? 21.054 36.525 23.561 1.00 7.65 ? 143 THR A CA 1 ATOM 466 C C . THR A 1 57 ? 19.589 36.884 23.861 1.00 7.67 ? 143 THR A C 1 ATOM 467 O O . THR A 1 57 ? 18.897 37.326 22.955 1.00 8.65 ? 143 THR A O 1 ATOM 468 C CB . THR A 1 57 ? 21.075 35.256 22.691 1.00 8.21 ? 143 THR A CB 1 ATOM 469 O OG1 . THR A 1 57 ? 20.426 34.184 23.387 1.00 8.61 ? 143 THR A OG1 1 ATOM 470 C CG2 . THR A 1 57 ? 22.471 34.858 22.258 1.00 10.06 ? 143 THR A CG2 1 ATOM 471 N N . VAL A 1 58 ? 19.110 36.624 25.091 1.00 7.16 ? 144 VAL A N 1 ATOM 472 C CA . VAL A 1 58 ? 17.673 36.809 25.375 1.00 6.92 ? 144 VAL A CA 1 ATOM 473 C C . VAL A 1 58 ? 17.269 38.247 25.324 1.00 7.21 ? 144 VAL A C 1 ATOM 474 O O . VAL A 1 58 ? 16.317 38.617 24.621 1.00 8.28 ? 144 VAL A O 1 ATOM 475 C CB . VAL A 1 58 ? 17.352 36.164 26.727 1.00 7.17 ? 144 VAL A CB 1 ATOM 476 C CG1 . VAL A 1 58 ? 15.931 36.453 27.155 1.00 7.41 ? 144 VAL A CG1 1 ATOM 477 C CG2 . VAL A 1 58 ? 17.597 34.639 26.668 1.00 7.91 ? 144 VAL A CG2 1 ATOM 478 N N . ASP A 1 59 ? 17.975 39.140 26.052 1.00 7.23 ? 145 ASP A N 1 ATOM 479 C CA . ASP A 1 59 ? 17.654 40.541 26.058 1.00 7.70 ? 145 ASP A CA 1 ATOM 480 C C . ASP A 1 59 ? 18.325 41.339 24.949 1.00 9.09 ? 145 ASP A C 1 ATOM 481 O O . ASP A 1 59 ? 18.187 42.556 24.912 1.00 11.67 ? 145 ASP A O 1 ATOM 482 C CB . ASP A 1 59 ? 17.889 41.157 27.432 1.00 7.81 ? 145 ASP A CB 1 ATOM 483 C CG . ASP A 1 59 ? 16.644 41.129 28.293 1.00 7.98 ? 145 ASP A CG 1 ATOM 484 O OD1 . ASP A 1 59 ? 15.670 41.834 27.919 1.00 10.88 ? 145 ASP A OD1 1 ATOM 485 O OD2 . ASP A 1 59 ? 16.549 40.447 29.336 1.00 8.89 ? 145 ASP A OD2 1 ATOM 486 N N . THR A 1 60 ? 19.016 40.682 24.049 1.00 8.58 ? 146 THR A N 1 ATOM 487 C CA . THR A 1 60 ? 19.595 41.284 22.853 1.00 8.56 ? 146 THR A CA 1 ATOM 488 C C . THR A 1 60 ? 18.892 40.729 21.593 1.00 8.97 ? 146 THR A C 1 ATOM 489 O O . THR A 1 60 ? 17.935 41.361 21.141 1.00 10.23 ? 146 THR A O 1 ATOM 490 C CB . THR A 1 60 ? 21.114 41.175 22.824 1.00 9.87 ? 146 THR A CB 1 ATOM 491 O OG1 . THR A 1 60 ? 21.532 39.786 22.837 1.00 9.95 ? 146 THR A OG1 1 ATOM 492 C CG2 . THR A 1 60 ? 21.764 41.866 24.016 1.00 11.21 ? 146 THR A CG2 1 ATOM 493 N N . LEU A 1 61 ? 19.381 39.618 21.095 1.00 8.66 ? 147 LEU A N 1 ATOM 494 C CA . LEU A 1 61 ? 18.925 39.064 19.841 1.00 9.16 ? 147 LEU A CA 1 ATOM 495 C C . LEU A 1 61 ? 17.427 38.784 19.831 1.00 8.41 ? 147 LEU A C 1 ATOM 496 O O . LEU A 1 61 ? 16.767 39.067 18.834 1.00 8.78 ? 147 LEU A O 1 ATOM 497 C CB . LEU A 1 61 ? 19.699 37.787 19.507 1.00 10.45 ? 147 LEU A CB 1 ATOM 498 C CG . LEU A 1 61 ? 21.188 37.911 19.395 1.00 12.19 ? 147 LEU A CG 1 ATOM 499 C CD1 . LEU A 1 61 ? 21.796 36.552 18.897 1.00 14.46 ? 147 LEU A CD1 1 ATOM 500 C CD2 . LEU A 1 61 ? 21.602 39.122 18.574 1.00 15.12 ? 147 LEU A CD2 1 ATOM 501 N N . LEU A 1 62 ? 16.886 38.138 20.871 1.00 7.96 ? 148 LEU A N 1 ATOM 502 C CA . LEU A 1 62 ? 15.486 37.765 20.820 1.00 7.75 ? 148 LEU A CA 1 ATOM 503 C C . LEU A 1 62 ? 14.618 38.994 20.697 1.00 7.88 ? 148 LEU A C 1 ATOM 504 O O . LEU A 1 62 ? 13.718 39.089 19.872 1.00 7.92 ? 148 LEU A O 1 ATOM 505 C CB . LEU A 1 62 ? 15.119 36.917 22.041 1.00 7.20 ? 148 LEU A CB 1 ATOM 506 C CG . LEU A 1 62 ? 13.637 36.498 22.068 1.00 7.53 ? 148 LEU A CG 1 ATOM 507 C CD1 . LEU A 1 62 ? 13.274 35.566 20.955 1.00 7.68 ? 148 LEU A CD1 1 ATOM 508 C CD2 . LEU A 1 62 ? 13.332 35.837 23.431 1.00 8.27 ? 148 LEU A CD2 1 ATOM 509 N N . VAL A 1 63 ? 14.873 39.977 21.566 1.00 8.18 ? 149 VAL A N 1 ATOM 510 C CA . VAL A 1 63 ? 14.131 41.229 21.553 1.00 8.18 ? 149 VAL A CA 1 ATOM 511 C C . VAL A 1 63 ? 14.283 41.931 20.202 1.00 8.56 ? 149 VAL A C 1 ATOM 512 O O . VAL A 1 63 ? 13.314 42.449 19.651 1.00 8.84 ? 149 VAL A O 1 ATOM 513 C CB . VAL A 1 63 ? 14.562 42.135 22.703 1.00 9.15 ? 149 VAL A CB 1 ATOM 514 C CG1 . VAL A 1 63 ? 13.902 43.517 22.603 1.00 10.71 ? 149 VAL A CG1 1 ATOM 515 C CG2 . VAL A 1 63 ? 14.179 41.503 24.034 1.00 9.87 ? 149 VAL A CG2 1 ATOM 516 N N . GLN A 1 64 ? 15.496 42.008 19.680 1.00 8.78 ? 150 GLN A N 1 ATOM 517 C CA . GLN A 1 64 ? 15.726 42.686 18.409 1.00 9.56 ? 150 GLN A CA 1 ATOM 518 C C . GLN A 1 64 ? 14.978 41.995 17.287 1.00 8.67 ? 150 GLN A C 1 ATOM 519 O O . GLN A 1 64 ? 14.330 42.671 16.480 1.00 10.13 ? 150 GLN A O 1 ATOM 520 C CB A GLN A 1 64 ? 17.219 42.680 18.112 0.70 12.06 ? 150 GLN A CB 1 ATOM 521 C CB B GLN A 1 64 ? 17.199 42.771 18.114 0.30 10.20 ? 150 GLN A CB 1 ATOM 522 C CG A GLN A 1 64 ? 18.006 43.616 18.974 0.70 15.83 ? 150 GLN A CG 1 ATOM 523 C CG B GLN A 1 64 ? 17.477 43.655 16.915 0.30 9.78 ? 150 GLN A CG 1 ATOM 524 C CD A GLN A 1 64 ? 19.496 43.298 19.165 0.70 18.62 ? 150 GLN A CD 1 ATOM 525 C CD B GLN A 1 64 ? 17.139 45.117 17.189 0.30 15.97 ? 150 GLN A CD 1 ATOM 526 O OE1 A GLN A 1 64 ? 20.118 43.901 20.072 0.70 22.39 ? 150 GLN A OE1 1 ATOM 527 O OE1 B GLN A 1 64 ? 17.315 45.612 18.306 0.30 19.40 ? 150 GLN A OE1 1 ATOM 528 N NE2 A GLN A 1 64 ? 20.064 42.363 18.401 0.70 18.51 ? 150 GLN A NE2 1 ATOM 529 N NE2 B GLN A 1 64 ? 16.647 45.812 16.179 0.30 17.04 ? 150 GLN A NE2 1 ATOM 530 N N . THR A 1 65 ? 15.088 40.689 17.169 1.00 8.32 ? 151 THR A N 1 ATOM 531 C CA . THR A 1 65 ? 14.396 39.964 16.103 1.00 8.48 ? 151 THR A CA 1 ATOM 532 C C . THR A 1 65 ? 12.894 40.153 16.175 1.00 7.67 ? 151 THR A C 1 ATOM 533 O O . THR A 1 65 ? 12.246 40.428 15.154 1.00 8.36 ? 151 THR A O 1 ATOM 534 C CB . THR A 1 65 ? 14.816 38.531 16.098 1.00 9.31 ? 151 THR A CB 1 ATOM 535 O OG1 . THR A 1 65 ? 16.185 38.536 15.617 1.00 12.80 ? 151 THR A OG1 1 ATOM 536 C CG2 . THR A 1 65 ? 13.970 37.691 15.129 1.00 10.47 ? 151 THR A CG2 1 ATOM 537 N N . LEU A 1 66 ? 12.317 39.963 17.348 1.00 7.54 ? 152 LEU A N 1 ATOM 538 C CA . LEU A 1 66 ? 10.865 40.083 17.472 1.00 7.52 ? 152 LEU A CA 1 ATOM 539 C C . LEU A 1 66 ? 10.446 41.532 17.156 1.00 7.80 ? 152 LEU A C 1 ATOM 540 O O . LEU A 1 66 ? 9.429 41.764 16.532 1.00 8.52 ? 152 LEU A O 1 ATOM 541 C CB . LEU A 1 66 ? 10.394 39.642 18.845 1.00 7.60 ? 152 LEU A CB 1 ATOM 542 C CG . LEU A 1 66 ? 10.614 38.153 19.128 1.00 7.08 ? 152 LEU A CG 1 ATOM 543 C CD1 . LEU A 1 66 ? 10.302 37.834 20.555 1.00 8.18 ? 152 LEU A CD1 1 ATOM 544 C CD2 . LEU A 1 66 ? 9.770 37.271 18.177 1.00 10.11 ? 152 LEU A CD2 1 ATOM 545 N N . SER A 1 67 ? 11.222 42.509 17.614 1.00 8.26 ? 153 SER A N 1 ATOM 546 C CA . SER A 1 67 ? 10.926 43.920 17.320 1.00 9.19 ? 153 SER A CA 1 ATOM 547 C C . SER A 1 67 ? 10.967 44.184 15.818 1.00 9.21 ? 153 SER A C 1 ATOM 548 O O . SER A 1 67 ? 10.085 44.880 15.267 1.00 9.34 ? 153 SER A O 1 ATOM 549 C CB . SER A 1 67 ? 11.945 44.816 18.000 1.00 10.83 ? 153 SER A CB 1 ATOM 550 O OG . SER A 1 67 ? 11.905 44.786 19.403 1.00 13.13 ? 153 SER A OG 1 ATOM 551 N N . GLU A 1 68 ? 11.938 43.634 15.128 1.00 8.74 ? 154 GLU A N 1 ATOM 552 C CA . GLU A 1 68 ? 12.087 43.837 13.677 1.00 9.26 ? 154 GLU A CA 1 ATOM 553 C C . GLU A 1 68 ? 10.962 43.123 12.932 1.00 9.51 ? 154 GLU A C 1 ATOM 554 O O . GLU A 1 68 ? 10.476 43.669 11.923 1.00 9.54 ? 154 GLU A O 1 ATOM 555 C CB . GLU A 1 68 ? 13.444 43.335 13.219 1.00 9.19 ? 154 GLU A CB 1 ATOM 556 C CG . GLU A 1 68 ? 14.533 44.288 13.711 1.00 9.96 ? 154 GLU A CG 1 ATOM 557 C CD . GLU A 1 68 ? 15.939 43.801 13.428 1.00 12.09 ? 154 GLU A CD 1 ATOM 558 O OE1 . GLU A 1 68 ? 16.137 42.705 12.885 1.00 13.28 ? 154 GLU A OE1 1 ATOM 559 O OE2 . GLU A 1 68 ? 16.909 44.576 13.681 1.00 16.06 ? 154 GLU A OE2 1 ATOM 560 N N . ILE A 1 69 ? 10.526 41.955 13.384 1.00 8.11 ? 155 ILE A N 1 ATOM 561 C CA . ILE A 1 69 ? 9.408 41.269 12.729 1.00 8.34 ? 155 ILE A CA 1 ATOM 562 C C . ILE A 1 69 ? 8.105 42.070 12.947 1.00 8.20 ? 155 ILE A C 1 ATOM 563 O O . ILE A 1 69 ? 7.335 42.254 12.011 1.00 8.78 ? 155 ILE A O 1 ATOM 564 C CB . ILE A 1 69 ? 9.261 39.827 13.243 1.00 7.84 ? 155 ILE A CB 1 ATOM 565 C CG1 . ILE A 1 69 ? 10.442 38.995 12.812 1.00 8.21 ? 155 ILE A CG1 1 ATOM 566 C CG2 . ILE A 1 69 ? 7.968 39.257 12.736 1.00 8.56 ? 155 ILE A CG2 1 ATOM 567 C CD1 . ILE A 1 69 ? 10.539 37.671 13.538 1.00 8.36 ? 155 ILE A CD1 1 ATOM 568 N N . ARG A 1 70 ? 7.869 42.530 14.162 1.00 8.45 ? 156 ARG A N 1 ATOM 569 C CA . ARG A 1 70 ? 6.706 43.366 14.429 1.00 8.38 ? 156 ARG A CA 1 ATOM 570 C C . ARG A 1 70 ? 6.737 44.558 13.467 1.00 9.36 ? 156 ARG A C 1 ATOM 571 O O . ARG A 1 70 ? 5.690 44.909 12.854 1.00 9.78 ? 156 ARG A O 1 ATOM 572 C CB . ARG A 1 70 ? 6.686 43.839 15.855 1.00 9.72 ? 156 ARG A CB 1 ATOM 573 C CG . ARG A 1 70 ? 5.626 44.924 16.135 1.00 8.90 ? 156 ARG A CG 1 ATOM 574 C CD . ARG A 1 70 ? 5.642 45.438 17.558 1.00 9.99 ? 156 ARG A CD 1 ATOM 575 N NE . ARG A 1 70 ? 5.100 44.444 18.451 1.00 9.35 ? 156 ARG A NE 1 ATOM 576 C CZ . ARG A 1 70 ? 5.193 44.510 19.775 1.00 9.43 ? 156 ARG A CZ 1 ATOM 577 N NH1 . ARG A 1 70 ? 5.947 45.416 20.346 1.00 11.90 ? 156 ARG A NH1 1 ATOM 578 N NH2 . ARG A 1 70 ? 4.566 43.634 20.522 1.00 9.36 ? 156 ARG A NH2 1 ATOM 579 N N . GLU A 1 71 ? 7.858 45.237 13.356 1.00 9.02 ? 157 GLU A N 1 ATOM 580 C CA . GLU A 1 71 ? 7.977 46.388 12.431 1.00 10.21 ? 157 GLU A CA 1 ATOM 581 C C . GLU A 1 71 ? 7.601 45.968 11.023 1.00 9.84 ? 157 GLU A C 1 ATOM 582 O O . GLU A 1 71 ? 6.836 46.666 10.327 1.00 10.67 ? 157 GLU A O 1 ATOM 583 C CB . GLU A 1 71 ? 9.371 46.980 12.520 1.00 11.01 ? 157 GLU A CB 1 ATOM 584 C CG . GLU A 1 71 ? 9.640 48.131 11.586 1.00 14.03 ? 157 GLU A CG 1 ATOM 585 C CD . GLU A 1 71 ? 11.073 48.598 11.650 1.00 16.64 ? 157 GLU A CD 1 ATOM 586 O OE1 . GLU A 1 71 ? 12.043 47.812 11.593 1.00 19.87 ? 157 GLU A OE1 1 ATOM 587 O OE2 . GLU A 1 71 ? 11.262 49.853 11.784 1.00 23.04 ? 157 GLU A OE2 1 ATOM 588 N N . ALA A 1 72 ? 8.144 44.873 10.512 1.00 9.84 ? 158 ALA A N 1 ATOM 589 C CA . ALA A 1 72 ? 7.860 44.424 9.138 1.00 9.90 ? 158 ALA A CA 1 ATOM 590 C C . ALA A 1 72 ? 6.428 44.084 8.947 1.00 9.88 ? 158 ALA A C 1 ATOM 591 O O . ALA A 1 72 ? 5.831 44.398 7.869 1.00 10.28 ? 158 ALA A O 1 ATOM 592 C CB . ALA A 1 72 ? 8.775 43.244 8.815 1.00 10.66 ? 158 ALA A CB 1 ATOM 593 N N . ASN A 1 73 ? 5.794 43.482 9.947 1.00 9.43 ? 159 ASN A N 1 ATOM 594 C CA . ASN A 1 73 ? 4.424 43.087 9.845 1.00 9.00 ? 159 ASN A CA 1 ATOM 595 C C . ASN A 1 73 ? 3.508 44.301 9.898 1.00 10.08 ? 159 ASN A C 1 ATOM 596 O O . ASN A 1 73 ? 2.532 44.409 9.135 1.00 10.88 ? 159 ASN A O 1 ATOM 597 C CB . ASN A 1 73 ? 4.066 42.090 10.962 1.00 8.99 ? 159 ASN A CB 1 ATOM 598 C CG . ASN A 1 73 ? 4.645 40.711 10.667 1.00 8.61 ? 159 ASN A CG 1 ATOM 599 O OD1 . ASN A 1 73 ? 5.101 40.433 9.543 1.00 9.65 ? 159 ASN A OD1 1 ATOM 600 N ND2 . ASN A 1 73 ? 4.624 39.841 11.687 1.00 9.21 ? 159 ASN A ND2 1 ATOM 601 N N . GLN A 1 74 ? 3.812 45.233 10.791 1.00 10.03 ? 160 GLN A N 1 ATOM 602 C CA . GLN A 1 74 ? 3.033 46.489 10.833 1.00 10.64 ? 160 GLN A CA 1 ATOM 603 C C . GLN A 1 74 ? 3.197 47.296 9.559 1.00 12.19 ? 160 GLN A C 1 ATOM 604 O O . GLN A 1 74 ? 2.304 48.099 9.230 1.00 13.88 ? 160 GLN A O 1 ATOM 605 C CB . GLN A 1 74 ? 3.407 47.276 12.088 1.00 11.39 ? 160 GLN A CB 1 ATOM 606 C CG . GLN A 1 74 ? 2.877 46.600 13.367 1.00 11.59 ? 160 GLN A CG 1 ATOM 607 C CD . GLN A 1 74 ? 3.265 47.323 14.631 1.00 11.39 ? 160 GLN A CD 1 ATOM 608 O OE1 . GLN A 1 74 ? 4.180 48.138 14.639 1.00 15.41 ? 160 GLN A OE1 1 ATOM 609 N NE2 . GLN A 1 74 ? 2.646 46.950 15.754 1.00 12.87 ? 160 GLN A NE2 1 ATOM 610 N N . ALA A 1 75 ? 4.321 47.125 8.861 1.00 11.48 ? 161 ALA A N 1 ATOM 611 C CA . ALA A 1 75 ? 4.605 47.786 7.561 1.00 12.29 ? 161 ALA A CA 1 ATOM 612 C C . ALA A 1 75 ? 4.070 46.975 6.400 1.00 11.88 ? 161 ALA A C 1 ATOM 613 O O . ALA A 1 75 ? 4.397 47.311 5.242 1.00 14.14 ? 161 ALA A O 1 ATOM 614 C CB . ALA A 1 75 ? 6.075 48.080 7.425 1.00 13.14 ? 161 ALA A CB 1 ATOM 615 N N . GLY A 1 76 ? 3.239 45.987 6.642 1.00 12.61 ? 162 GLY A N 1 ATOM 616 C CA . GLY A 1 76 ? 2.444 45.351 5.616 1.00 12.17 ? 162 GLY A CA 1 ATOM 617 C C . GLY A 1 76 ? 2.933 44.044 5.044 1.00 12.46 ? 162 GLY A C 1 ATOM 618 O O . GLY A 1 76 ? 2.440 43.599 4.000 1.00 13.34 ? 162 GLY A O 1 ATOM 619 N N . ALA A 1 77 ? 3.878 43.362 5.701 1.00 11.56 ? 163 ALA A N 1 ATOM 620 C CA . ALA A 1 77 ? 4.300 42.057 5.184 1.00 11.65 ? 163 ALA A CA 1 ATOM 621 C C . ALA A 1 77 ? 3.091 41.165 4.989 1.00 10.99 ? 163 ALA A C 1 ATOM 622 O O . ALA A 1 77 ? 2.252 41.036 5.850 1.00 13.09 ? 163 ALA A O 1 ATOM 623 C CB . ALA A 1 77 ? 5.286 41.433 6.133 1.00 11.72 ? 163 ALA A CB 1 ATOM 624 N N . ASN A 1 78 ? 3.009 40.492 3.839 1.00 12.64 ? 164 ASN A N 1 ATOM 625 C CA . ASN A 1 78 ? 1.868 39.691 3.511 1.00 13.72 ? 164 ASN A CA 1 ATOM 626 C C . ASN A 1 78 ? 2.299 38.404 2.807 1.00 14.25 ? 164 ASN A C 1 ATOM 627 O O . ASN A 1 78 ? 2.834 38.476 1.696 1.00 16.89 ? 164 ASN A O 1 ATOM 628 C CB . ASN A 1 78 ? 0.966 40.507 2.560 1.00 15.60 ? 164 ASN A CB 1 ATOM 629 C CG . ASN A 1 78 ? -0.361 39.819 2.286 1.00 21.34 ? 164 ASN A CG 1 ATOM 630 O OD1 . ASN A 1 78 ? -1.129 40.287 1.406 1.00 30.61 ? 164 ASN A OD1 1 ATOM 631 N ND2 . ASN A 1 78 ? -0.704 38.816 3.030 1.00 21.31 ? 164 ASN A ND2 1 ATOM 632 N N . PRO A 1 79 ? 2.091 37.243 3.405 1.00 13.16 ? 165 PRO A N 1 ATOM 633 C CA . PRO A 1 79 ? 1.545 37.088 4.752 1.00 12.68 ? 165 PRO A CA 1 ATOM 634 C C . PRO A 1 79 ? 2.529 37.552 5.838 1.00 10.94 ? 165 PRO A C 1 ATOM 635 O O . PRO A 1 79 ? 3.667 37.869 5.554 1.00 10.96 ? 165 PRO A O 1 ATOM 636 C CB . PRO A 1 79 ? 1.257 35.578 4.923 1.00 15.80 ? 165 PRO A CB 1 ATOM 637 C CG . PRO A 1 79 ? 2.033 34.909 3.965 1.00 18.83 ? 165 PRO A CG 1 ATOM 638 C CD . PRO A 1 79 ? 2.349 35.923 2.817 1.00 14.91 ? 165 PRO A CD 1 ATOM 639 N N . GLN A 1 80 ? 2.017 37.639 7.061 1.00 10.49 ? 166 GLN A N 1 ATOM 640 C CA . GLN A 1 80 ? 2.819 38.007 8.203 1.00 10.31 ? 166 GLN A CA 1 ATOM 641 C C . GLN A 1 80 ? 4.082 37.138 8.334 1.00 8.67 ? 166 GLN A C 1 ATOM 642 O O . GLN A 1 80 ? 4.005 35.933 8.077 1.00 9.21 ? 166 GLN A O 1 ATOM 643 C CB . GLN A 1 80 ? 2.005 37.838 9.510 1.00 13.76 ? 166 GLN A CB 1 ATOM 644 C CG . GLN A 1 80 ? 1.197 39.025 9.950 1.00 19.55 ? 166 GLN A CG 1 ATOM 645 C CD . GLN A 1 80 ? 0.803 38.917 11.421 1.00 20.86 ? 166 GLN A CD 1 ATOM 646 O OE1 . GLN A 1 80 ? 1.061 37.848 12.133 1.00 20.86 ? 166 GLN A OE1 1 ATOM 647 N NE2 . GLN A 1 80 ? 0.227 39.999 11.933 1.00 21.00 ? 166 GLN A NE2 1 ATOM 648 N N . TYR A 1 81 ? 5.174 37.737 8.762 1.00 8.40 ? 167 TYR A N 1 ATOM 649 C CA . TYR A 1 81 ? 6.367 36.957 9.150 1.00 8.24 ? 167 TYR A CA 1 ATOM 650 C C . TYR A 1 81 ? 6.177 36.288 10.508 1.00 7.39 ? 167 TYR A C 1 ATOM 651 O O . TYR A 1 81 ? 5.592 36.862 11.437 1.00 8.51 ? 167 TYR A O 1 ATOM 652 C CB . TYR A 1 81 ? 7.554 37.887 9.232 1.00 8.25 ? 167 TYR A CB 1 ATOM 653 C CG . TYR A 1 81 ? 8.126 38.290 7.905 1.00 8.60 ? 167 TYR A CG 1 ATOM 654 C CD1 . TYR A 1 81 ? 8.786 37.362 7.129 1.00 8.96 ? 167 TYR A CD1 1 ATOM 655 C CD2 . TYR A 1 81 ? 8.006 39.588 7.451 1.00 9.79 ? 167 TYR A CD2 1 ATOM 656 C CE1 . TYR A 1 81 ? 9.341 37.719 5.929 1.00 10.76 ? 167 TYR A CE1 1 ATOM 657 C CE2 . TYR A 1 81 ? 8.589 39.971 6.256 1.00 10.73 ? 167 TYR A CE2 1 ATOM 658 C CZ . TYR A 1 81 ? 9.228 39.032 5.490 1.00 10.83 ? 167 TYR A CZ 1 ATOM 659 O OH . TYR A 1 81 ? 9.818 39.396 4.276 1.00 13.15 ? 167 TYR A OH 1 ATOM 660 N N . ALA A 1 82 ? 6.786 35.095 10.658 1.00 7.41 ? 168 ALA A N 1 ATOM 661 C CA . ALA A 1 82 ? 6.940 34.410 11.943 1.00 6.99 ? 168 ALA A CA 1 ATOM 662 C C . ALA A 1 82 ? 8.415 34.250 12.293 1.00 6.43 ? 168 ALA A C 1 ATOM 663 O O . ALA A 1 82 ? 9.263 34.183 11.404 1.00 7.42 ? 168 ALA A O 1 ATOM 664 C CB . ALA A 1 82 ? 6.284 33.032 11.842 1.00 7.65 ? 168 ALA A CB 1 ATOM 665 N N . ALA A 1 83 ? 8.685 34.142 13.583 1.00 6.39 ? 169 ALA A N 1 ATOM 666 C CA . ALA A 1 83 ? 10.007 33.921 14.128 1.00 6.57 ? 169 ALA A CA 1 ATOM 667 C C . ALA A 1 83 ? 10.302 32.427 14.318 1.00 6.44 ? 169 ALA A C 1 ATOM 668 O O . ALA A 1 83 ? 9.405 31.652 14.576 1.00 6.79 ? 169 ALA A O 1 ATOM 669 C CB . ALA A 1 83 ? 10.147 34.628 15.468 1.00 6.98 ? 169 ALA A CB 1 ATOM 670 N N . GLN A 1 84 ? 11.590 32.091 14.179 1.00 6.12 ? 170 GLN A N 1 ATOM 671 C CA . GLN A 1 84 ? 12.108 30.744 14.387 1.00 6.18 ? 170 GLN A CA 1 ATOM 672 C C . GLN A 1 84 ? 13.293 30.841 15.373 1.00 6.15 ? 170 GLN A C 1 ATOM 673 O O . GLN A 1 84 ? 14.293 31.487 15.034 1.00 6.55 ? 170 GLN A O 1 ATOM 674 C CB . GLN A 1 84 ? 12.602 30.137 13.083 1.00 6.76 ? 170 GLN A CB 1 ATOM 675 C CG . GLN A 1 84 ? 11.472 29.798 12.083 1.00 7.20 ? 170 GLN A CG 1 ATOM 676 C CD . GLN A 1 84 ? 12.053 29.381 10.744 1.00 6.77 ? 170 GLN A CD 1 ATOM 677 O OE1 . GLN A 1 84 ? 12.033 28.200 10.360 1.00 7.40 ? 170 GLN A OE1 1 ATOM 678 N NE2 . GLN A 1 84 ? 12.659 30.346 10.035 1.00 7.46 ? 170 GLN A NE2 1 ATOM 679 N N . ILE A 1 85 ? 13.149 30.257 16.554 1.00 5.75 ? 171 ILE A N 1 ATOM 680 C CA . ILE A 1 85 ? 14.102 30.459 17.670 1.00 6.01 ? 171 ILE A CA 1 ATOM 681 C C . ILE A 1 85 ? 14.438 29.091 18.283 1.00 5.24 ? 171 ILE A C 1 ATOM 682 O O . ILE A 1 85 ? 13.576 28.248 18.430 1.00 6.07 ? 171 ILE A O 1 ATOM 683 C CB . ILE A 1 85 ? 13.444 31.350 18.734 1.00 5.98 ? 171 ILE A CB 1 ATOM 684 C CG1 . ILE A 1 85 ? 13.057 32.746 18.206 1.00 8.33 ? 171 ILE A CG1 1 ATOM 685 C CG2 . ILE A 1 85 ? 14.356 31.479 19.959 1.00 8.49 ? 171 ILE A CG2 1 ATOM 686 C CD1 . ILE A 1 85 ? 14.143 33.651 17.759 1.00 10.42 ? 171 ILE A CD1 1 ATOM 687 N N . VAL A 1 86 ? 15.711 28.906 18.585 1.00 5.78 ? 172 VAL A N 1 ATOM 688 C CA . VAL A 1 86 ? 16.178 27.732 19.333 1.00 5.88 ? 172 VAL A CA 1 ATOM 689 C C . VAL A 1 86 ? 16.443 28.085 20.803 1.00 5.72 ? 172 VAL A C 1 ATOM 690 O O . VAL A 1 86 ? 17.194 29.044 21.076 1.00 6.50 ? 172 VAL A O 1 ATOM 691 C CB . VAL A 1 86 ? 17.455 27.098 18.716 1.00 5.81 ? 172 VAL A CB 1 ATOM 692 C CG1 . VAL A 1 86 ? 17.775 25.777 19.410 1.00 6.80 ? 172 VAL A CG1 1 ATOM 693 C CG2 . VAL A 1 86 ? 17.304 26.927 17.220 1.00 6.74 ? 172 VAL A CG2 1 ATOM 694 N N . VAL A 1 87 ? 15.887 27.327 21.712 1.00 5.65 ? 173 VAL A N 1 ATOM 695 C CA . VAL A 1 87 ? 16.166 27.415 23.153 1.00 6.03 ? 173 VAL A CA 1 ATOM 696 C C . VAL A 1 87 ? 17.269 26.408 23.451 1.00 6.11 ? 173 VAL A C 1 ATOM 697 O O . VAL A 1 87 ? 17.065 25.213 23.216 1.00 6.58 ? 173 VAL A O 1 ATOM 698 C CB . VAL A 1 87 ? 14.891 27.155 23.939 1.00 5.82 ? 173 VAL A CB 1 ATOM 699 C CG1 . VAL A 1 87 ? 15.159 27.205 25.447 1.00 7.39 ? 173 VAL A CG1 1 ATOM 700 C CG2 . VAL A 1 87 ? 13.794 28.139 23.591 1.00 7.40 ? 173 VAL A CG2 1 ATOM 701 N N . TYR A 1 88 ? 18.449 26.848 23.884 1.00 6.13 ? 174 TYR A N 1 ATOM 702 C CA . TYR A 1 88 ? 19.600 25.960 23.979 1.00 6.10 ? 174 TYR A CA 1 ATOM 703 C C . TYR A 1 88 ? 20.555 26.404 25.082 1.00 5.86 ? 174 TYR A C 1 ATOM 704 O O . TYR A 1 88 ? 21.659 26.873 24.813 1.00 7.06 ? 174 TYR A O 1 ATOM 705 C CB . TYR A 1 88 ? 20.315 25.884 22.617 1.00 6.51 ? 174 TYR A CB 1 ATOM 706 C CG . TYR A 1 88 ? 21.470 24.889 22.521 1.00 6.35 ? 174 TYR A CG 1 ATOM 707 C CD1 . TYR A 1 88 ? 21.403 23.614 23.029 1.00 7.52 ? 174 TYR A CD1 1 ATOM 708 C CD2 . TYR A 1 88 ? 22.608 25.257 21.833 1.00 8.06 ? 174 TYR A CD2 1 ATOM 709 C CE1 . TYR A 1 88 ? 22.443 22.718 22.887 1.00 7.85 ? 174 TYR A CE1 1 ATOM 710 C CE2 . TYR A 1 88 ? 23.682 24.364 21.672 1.00 8.18 ? 174 TYR A CE2 1 ATOM 711 C CZ . TYR A 1 88 ? 23.565 23.081 22.184 1.00 7.76 ? 174 TYR A CZ 1 ATOM 712 O OH . TYR A 1 88 ? 24.643 22.235 22.013 1.00 9.49 ? 174 TYR A OH 1 ATOM 713 N N . ASP A 1 89 ? 20.138 26.210 26.337 1.00 6.20 ? 175 ASP A N 1 ATOM 714 C CA . ASP A 1 89 ? 21.008 26.604 27.445 1.00 6.65 ? 175 ASP A CA 1 ATOM 715 C C . ASP A 1 89 ? 20.820 25.784 28.701 1.00 6.51 ? 175 ASP A C 1 ATOM 716 O O . ASP A 1 89 ? 21.065 26.277 29.801 1.00 7.02 ? 175 ASP A O 1 ATOM 717 C CB . ASP A 1 89 ? 20.909 28.091 27.736 1.00 7.23 ? 175 ASP A CB 1 ATOM 718 C CG . ASP A 1 89 ? 22.202 28.682 28.275 1.00 6.97 ? 175 ASP A CG 1 ATOM 719 O OD1 . ASP A 1 89 ? 23.277 28.057 28.311 1.00 7.77 ? 175 ASP A OD1 1 ATOM 720 O OD2 . ASP A 1 89 ? 22.105 29.913 28.673 1.00 8.26 ? 175 ASP A OD2 1 ATOM 721 N N . LEU A 1 90 ? 20.453 24.506 28.573 1.00 6.56 ? 176 LEU A N 1 ATOM 722 C CA . LEU A 1 90 ? 20.358 23.653 29.768 1.00 6.05 ? 176 LEU A CA 1 ATOM 723 C C . LEU A 1 90 ? 21.663 23.664 30.532 1.00 6.30 ? 176 LEU A C 1 ATOM 724 O O . LEU A 1 90 ? 22.755 23.695 29.948 1.00 7.11 ? 176 LEU A O 1 ATOM 725 C CB . LEU A 1 90 ? 19.960 22.238 29.420 1.00 6.63 ? 176 LEU A CB 1 ATOM 726 C CG . LEU A 1 90 ? 18.496 21.994 29.140 1.00 7.10 ? 176 LEU A CG 1 ATOM 727 C CD1 . LEU A 1 90 ? 18.288 20.679 28.432 1.00 7.44 ? 176 LEU A CD1 1 ATOM 728 C CD2 . LEU A 1 90 ? 17.638 22.075 30.415 1.00 7.24 ? 176 LEU A CD2 1 ATOM 729 N N . PRO A 1 91 ? 21.599 23.579 31.863 1.00 6.53 ? 177 PRO A N 1 ATOM 730 C CA . PRO A 1 91 ? 22.818 23.391 32.646 1.00 6.58 ? 177 PRO A CA 1 ATOM 731 C C . PRO A 1 91 ? 23.350 22.003 32.455 1.00 6.87 ? 177 PRO A C 1 ATOM 732 O O . PRO A 1 91 ? 22.630 21.064 32.161 1.00 7.56 ? 177 PRO A O 1 ATOM 733 C CB . PRO A 1 91 ? 22.341 23.668 34.076 1.00 7.62 ? 177 PRO A CB 1 ATOM 734 C CG . PRO A 1 91 ? 20.923 23.146 34.088 1.00 7.42 ? 177 PRO A CG 1 ATOM 735 C CD . PRO A 1 91 ? 20.367 23.488 32.702 1.00 6.83 ? 177 PRO A CD 1 ATOM 736 N N . ASP A 1 92 ? 24.681 21.870 32.603 1.00 7.21 ? 178 ASP A N 1 ATOM 737 C CA . ASP A 1 92 ? 25.359 20.648 32.248 1.00 7.41 ? 178 ASP A CA 1 ATOM 738 C C . ASP A 1 92 ? 24.988 20.228 30.815 1.00 7.23 ? 178 ASP A C 1 ATOM 739 O O . ASP A 1 92 ? 24.759 19.050 30.515 1.00 8.25 ? 178 ASP A O 1 ATOM 740 C CB . ASP A 1 92 ? 25.116 19.510 33.238 1.00 7.87 ? 178 ASP A CB 1 ATOM 741 C CG . ASP A 1 92 ? 25.936 19.623 34.510 1.00 8.82 ? 178 ASP A CG 1 ATOM 742 O OD1 . ASP A 1 92 ? 26.384 20.714 34.879 1.00 9.71 ? 178 ASP A OD1 1 ATOM 743 O OD2 . ASP A 1 92 ? 26.108 18.583 35.197 1.00 12.15 ? 178 ASP A OD2 1 ATOM 744 N N . ARG A 1 93 ? 24.975 21.195 29.927 1.00 7.83 ? 179 ARG A N 1 ATOM 745 C CA . ARG A 1 93 ? 24.546 21.042 28.527 1.00 7.53 ? 179 ARG A CA 1 ATOM 746 C C . ARG A 1 93 ? 25.431 20.050 27.837 1.00 7.53 ? 179 ARG A C 1 ATOM 747 O O . ARG A 1 93 ? 26.648 19.957 28.096 1.00 8.21 ? 179 ARG A O 1 ATOM 748 C CB . ARG A 1 93 ? 24.638 22.381 27.796 1.00 7.60 ? 179 ARG A CB 1 ATOM 749 C CG . ARG A 1 93 ? 23.555 22.573 26.740 1.00 7.96 ? 179 ARG A CG 1 ATOM 750 C CD . ARG A 1 93 ? 23.609 23.917 26.027 1.00 7.48 ? 179 ARG A CD 1 ATOM 751 N NE . ARG A 1 93 ? 24.796 24.015 25.184 1.00 7.40 ? 179 ARG A NE 1 ATOM 752 C CZ . ARG A 1 93 ? 25.197 25.138 24.600 1.00 7.74 ? 179 ARG A CZ 1 ATOM 753 N NH1 . ARG A 1 93 ? 24.517 26.247 24.774 1.00 7.81 ? 179 ARG A NH1 1 ATOM 754 N NH2 . ARG A 1 93 ? 26.298 25.129 23.861 1.00 9.03 ? 179 ARG A NH2 1 ATOM 755 N N . ASP A 1 94 ? 24.854 19.309 26.901 1.00 7.14 ? 180 ASP A N 1 ATOM 756 C CA . ASP A 1 94 ? 25.629 18.392 26.032 1.00 6.89 ? 180 ASP A CA 1 ATOM 757 C C . ASP A 1 94 ? 26.388 17.395 26.876 1.00 7.79 ? 180 ASP A C 1 ATOM 758 O O . ASP A 1 94 ? 27.613 17.231 26.739 1.00 8.49 ? 180 ASP A O 1 ATOM 759 C CB . ASP A 1 94 ? 26.562 19.158 25.073 1.00 7.54 ? 180 ASP A CB 1 ATOM 760 C CG . ASP A 1 94 ? 25.838 20.281 24.378 1.00 8.66 ? 180 ASP A CG 1 ATOM 761 O OD1 . ASP A 1 94 ? 25.007 20.020 23.464 1.00 8.80 ? 180 ASP A OD1 1 ATOM 762 O OD2 . ASP A 1 94 ? 26.104 21.469 24.740 1.00 10.14 ? 180 ASP A OD2 1 ATOM 763 N N . CYS A 1 95 ? 25.659 16.658 27.726 1.00 7.74 ? 181 CYS A N 1 ATOM 764 C CA . CYS A 1 95 ? 26.304 15.865 28.768 1.00 7.90 ? 181 CYS A CA 1 ATOM 765 C C . CYS A 1 95 ? 27.259 14.788 28.270 1.00 8.21 ? 181 CYS A C 1 ATOM 766 O O . CYS A 1 95 ? 28.136 14.381 29.032 1.00 8.85 ? 181 CYS A O 1 ATOM 767 C CB . CYS A 1 95 ? 25.250 15.208 29.672 1.00 8.06 ? 181 CYS A CB 1 ATOM 768 S SG . CYS A 1 95 ? 24.060 14.150 28.811 1.00 8.96 ? 181 CYS A SG 1 ATOM 769 N N . ALA A 1 96 ? 27.058 14.268 27.049 1.00 7.72 ? 182 ALA A N 1 ATOM 770 C CA . ALA A 1 96 ? 27.897 13.222 26.511 1.00 9.32 ? 182 ALA A CA 1 ATOM 771 C C . ALA A 1 96 ? 28.992 13.750 25.582 1.00 9.64 ? 182 ALA A C 1 ATOM 772 O O . ALA A 1 96 ? 29.781 12.926 25.040 1.00 11.75 ? 182 ALA A O 1 ATOM 773 C CB . ALA A 1 96 ? 27.060 12.157 25.781 1.00 9.63 ? 182 ALA A CB 1 ATOM 774 N N . ALA A 1 97 ? 29.073 15.036 25.396 1.00 8.94 ? 183 ALA A N 1 ATOM 775 C CA . ALA A 1 97 ? 30.054 15.621 24.462 1.00 9.49 ? 183 ALA A CA 1 ATOM 776 C C . ALA A 1 97 ? 31.474 15.530 25.021 1.00 8.97 ? 183 ALA A C 1 ATOM 777 O O . ALA A 1 97 ? 31.685 15.596 26.248 1.00 11.10 ? 183 ALA A O 1 ATOM 778 C CB . ALA A 1 97 ? 29.718 17.059 24.127 1.00 10.10 ? 183 ALA A CB 1 ATOM 779 N N . ALA A 1 98 ? 32.424 15.476 24.129 1.00 8.71 ? 184 ALA A N 1 ATOM 780 C CA . ALA A 1 98 ? 33.822 15.522 24.518 1.00 9.18 ? 184 ALA A CA 1 ATOM 781 C C . ALA A 1 98 ? 34.159 16.823 25.149 1.00 9.41 ? 184 ALA A C 1 ATOM 782 O O . ALA A 1 98 ? 35.004 16.918 26.060 1.00 12.04 ? 184 ALA A O 1 ATOM 783 C CB . ALA A 1 98 ? 34.697 15.291 23.289 1.00 9.92 ? 184 ALA A CB 1 ATOM 784 N N . ALA A 1 99 ? 33.526 17.909 24.709 1.00 9.85 ? 185 ALA A N 1 ATOM 785 C CA . ALA A 1 99 ? 33.693 19.259 25.264 1.00 10.23 ? 185 ALA A CA 1 ATOM 786 C C . ALA A 1 99 ? 32.336 19.934 25.083 1.00 10.50 ? 185 ALA A C 1 ATOM 787 O O . ALA A 1 99 ? 31.662 19.750 24.060 1.00 15.62 ? 185 ALA A O 1 ATOM 788 C CB . ALA A 1 99 ? 34.769 20.025 24.521 1.00 11.60 ? 185 ALA A CB 1 ATOM 789 N N . SER A 1 100 ? 31.890 20.688 26.035 1.00 11.02 ? 186 SER A N 1 ATOM 790 C CA . SER A 1 100 ? 30.660 21.461 25.892 1.00 11.27 ? 186 SER A CA 1 ATOM 791 C C . SER A 1 100 ? 30.963 22.919 25.961 1.00 10.59 ? 186 SER A C 1 ATOM 792 O O . SER A 1 100 ? 31.819 23.350 26.756 1.00 12.28 ? 186 SER A O 1 ATOM 793 C CB . SER A 1 100 ? 29.683 21.115 26.984 1.00 12.24 ? 186 SER A CB 1 ATOM 794 O OG . SER A 1 100 ? 28.494 21.936 26.882 1.00 12.06 ? 186 SER A OG 1 ATOM 795 N N . ASN A 1 101 ? 30.254 23.706 25.168 1.00 10.70 ? 187 ASN A N 1 ATOM 796 C CA . ASN A 1 101 ? 30.266 25.151 25.218 1.00 11.09 ? 187 ASN A CA 1 ATOM 797 C C . ASN A 1 101 ? 29.166 25.732 26.082 1.00 10.64 ? 187 ASN A C 1 ATOM 798 O O . ASN A 1 101 ? 29.037 26.935 26.187 1.00 13.01 ? 187 ASN A O 1 ATOM 799 C CB . ASN A 1 101 ? 30.140 25.674 23.780 1.00 12.56 ? 187 ASN A CB 1 ATOM 800 C CG . ASN A 1 101 ? 31.306 25.162 22.919 1.00 14.50 ? 187 ASN A CG 1 ATOM 801 O OD1 . ASN A 1 101 ? 31.111 24.486 21.887 1.00 18.60 ? 187 ASN A OD1 1 ATOM 802 N ND2 . ASN A 1 101 ? 32.489 25.395 23.399 1.00 16.00 ? 187 ASN A ND2 1 ATOM 803 N N . GLY A 1 102 ? 28.361 24.910 26.743 1.00 9.48 ? 188 GLY A N 1 ATOM 804 C CA . GLY A 1 102 ? 27.294 25.419 27.594 1.00 9.20 ? 188 GLY A CA 1 ATOM 805 C C . GLY A 1 102 ? 27.872 26.211 28.777 1.00 8.89 ? 188 GLY A C 1 ATOM 806 O O . GLY A 1 102 ? 28.871 25.814 29.408 1.00 10.86 ? 188 GLY A O 1 ATOM 807 N N . GLU A 1 103 ? 27.281 27.352 29.089 1.00 8.87 ? 189 GLU A N 1 ATOM 808 C CA . GLU A 1 103 ? 27.828 28.246 30.102 1.00 8.48 ? 189 GLU A CA 1 ATOM 809 C C . GLU A 1 103 ? 27.468 27.862 31.535 1.00 8.68 ? 189 GLU A C 1 ATOM 810 O O . GLU A 1 103 ? 28.118 28.373 32.459 1.00 9.53 ? 189 GLU A O 1 ATOM 811 C CB . GLU A 1 103 ? 27.417 29.666 29.809 1.00 9.23 ? 189 GLU A CB 1 ATOM 812 C CG . GLU A 1 103 ? 25.915 29.923 29.969 1.00 8.25 ? 189 GLU A CG 1 ATOM 813 C CD . GLU A 1 103 ? 25.428 31.168 29.349 1.00 8.73 ? 189 GLU A CD 1 ATOM 814 O OE1 . GLU A 1 103 ? 26.241 32.121 29.120 1.00 12.87 ? 189 GLU A OE1 1 ATOM 815 O OE2 . GLU A 1 103 ? 24.216 31.308 29.120 1.00 8.58 ? 189 GLU A OE2 1 ATOM 816 N N . TRP A 1 104 ? 26.424 27.064 31.773 1.00 8.17 ? 190 TRP A N 1 ATOM 817 C CA . TRP A 1 104 ? 25.945 26.832 33.129 1.00 8.77 ? 190 TRP A CA 1 ATOM 818 C C . TRP A 1 104 ? 26.175 25.410 33.594 1.00 8.51 ? 190 TRP A C 1 ATOM 819 O O . TRP A 1 104 ? 26.027 24.457 32.821 1.00 9.05 ? 190 TRP A O 1 ATOM 820 C CB . TRP A 1 104 ? 24.481 27.204 33.260 1.00 8.80 ? 190 TRP A CB 1 ATOM 821 C CG . TRP A 1 104 ? 24.216 28.673 33.166 1.00 8.06 ? 190 TRP A CG 1 ATOM 822 C CD1 . TRP A 1 104 ? 25.071 29.683 33.538 1.00 8.04 ? 190 TRP A CD1 1 ATOM 823 C CD2 . TRP A 1 104 ? 23.038 29.319 32.673 1.00 7.73 ? 190 TRP A CD2 1 ATOM 824 N NE1 . TRP A 1 104 ? 24.481 30.897 33.290 1.00 8.27 ? 190 TRP A NE1 1 ATOM 825 C CE2 . TRP A 1 104 ? 23.219 30.695 32.772 1.00 7.85 ? 190 TRP A CE2 1 ATOM 826 C CE3 . TRP A 1 104 ? 21.831 28.841 32.152 1.00 7.90 ? 190 TRP A CE3 1 ATOM 827 C CZ2 . TRP A 1 104 ? 22.244 31.597 32.410 1.00 8.02 ? 190 TRP A CZ2 1 ATOM 828 C CZ3 . TRP A 1 104 ? 20.889 29.722 31.775 1.00 8.57 ? 190 TRP A CZ3 1 ATOM 829 C CH2 . TRP A 1 104 ? 21.087 31.093 31.906 1.00 8.62 ? 190 TRP A CH2 1 ATOM 830 N N . ALA A 1 105 ? 26.443 25.262 34.890 1.00 9.56 ? 191 ALA A N 1 ATOM 831 C CA . ALA A 1 105 ? 26.635 23.974 35.515 1.00 9.39 ? 191 ALA A CA 1 ATOM 832 C C . ALA A 1 105 ? 25.576 23.762 36.575 1.00 9.00 ? 191 ALA A C 1 ATOM 833 O O . ALA A 1 105 ? 25.251 24.683 37.362 1.00 9.60 ? 191 ALA A O 1 ATOM 834 C CB . ALA A 1 105 ? 28.000 23.879 36.163 1.00 10.23 ? 191 ALA A CB 1 ATOM 835 N N . ILE A 1 106 ? 25.050 22.551 36.665 1.00 8.87 ? 192 ILE A N 1 ATOM 836 C CA . ILE A 1 106 ? 24.135 22.210 37.738 1.00 9.21 ? 192 ILE A CA 1 ATOM 837 C C . ILE A 1 106 ? 24.753 22.583 39.109 1.00 10.52 ? 192 ILE A C 1 ATOM 838 O O . ILE A 1 106 ? 24.069 23.109 40.006 1.00 11.65 ? 192 ILE A O 1 ATOM 839 C CB . ILE A 1 106 ? 23.703 20.752 37.647 1.00 10.05 ? 192 ILE A CB 1 ATOM 840 C CG1 . ILE A 1 106 ? 22.891 20.539 36.343 1.00 9.49 ? 192 ILE A CG1 1 ATOM 841 C CG2 . ILE A 1 106 ? 22.891 20.366 38.885 1.00 12.79 ? 192 ILE A CG2 1 ATOM 842 C CD1 . ILE A 1 106 ? 22.537 19.075 36.101 1.00 11.01 ? 192 ILE A CD1 1 ATOM 843 N N . ALA A 1 107 ? 26.049 22.318 39.282 1.00 11.20 ? 193 ALA A N 1 ATOM 844 C CA . ALA A 1 107 ? 26.764 22.577 40.560 1.00 12.08 ? 193 ALA A CA 1 ATOM 845 C C . ALA A 1 107 ? 26.876 24.048 40.876 1.00 12.07 ? 193 ALA A C 1 ATOM 846 O O . ALA A 1 107 ? 27.194 24.386 42.037 1.00 14.42 ? 193 ALA A O 1 ATOM 847 C CB . ALA A 1 107 ? 28.120 21.960 40.556 1.00 14.02 ? 193 ALA A CB 1 ATOM 848 N N . ASN A 1 108 ? 26.714 24.967 39.909 1.00 12.16 ? 194 ASN A N 1 ATOM 849 C CA . ASN A 1 108 ? 26.898 26.381 40.120 1.00 11.82 ? 194 ASN A CA 1 ATOM 850 C C . ASN A 1 108 ? 25.549 27.120 39.817 1.00 10.22 ? 194 ASN A C 1 ATOM 851 O O . ASN A 1 108 ? 25.508 27.966 38.964 1.00 10.47 ? 194 ASN A O 1 ATOM 852 C CB . ASN A 1 108 ? 28.036 26.950 39.236 1.00 13.87 ? 194 ASN A CB 1 ATOM 853 C CG . ASN A 1 108 ? 29.389 26.278 39.406 1.00 16.19 ? 194 ASN A CG 1 ATOM 854 O OD1 . ASN A 1 108 ? 29.974 25.837 38.413 1.00 20.76 ? 194 ASN A OD1 1 ATOM 855 N ND2 . ASN A 1 108 ? 29.907 26.198 40.619 1.00 20.38 ? 194 ASN A ND2 1 ATOM 856 N N . ASN A 1 109 ? 24.506 26.720 40.512 1.00 10.00 ? 195 ASN A N 1 ATOM 857 C CA . ASN A 1 109 ? 23.211 27.372 40.427 1.00 9.48 ? 195 ASN A CA 1 ATOM 858 C C . ASN A 1 109 ? 22.552 27.230 39.049 1.00 8.50 ? 195 ASN A C 1 ATOM 859 O O . ASN A 1 109 ? 21.670 28.030 38.721 1.00 8.81 ? 195 ASN A O 1 ATOM 860 C CB . ASN A 1 109 ? 23.283 28.848 40.845 1.00 10.64 ? 195 ASN A CB 1 ATOM 861 C CG . ASN A 1 109 ? 22.007 29.329 41.450 1.00 12.20 ? 195 ASN A CG 1 ATOM 862 O OD1 . ASN A 1 109 ? 21.272 28.532 42.054 1.00 13.83 ? 195 ASN A OD1 1 ATOM 863 N ND2 . ASN A 1 109 ? 21.738 30.636 41.354 1.00 13.57 ? 195 ASN A ND2 1 ATOM 864 N N . GLY A 1 110 ? 22.887 26.166 38.315 1.00 8.53 ? 196 GLY A N 1 ATOM 865 C CA . GLY A 1 110 ? 22.395 26.073 36.944 1.00 7.99 ? 196 GLY A CA 1 ATOM 866 C C . GLY A 1 110 ? 20.905 25.923 36.815 1.00 8.11 ? 196 GLY A C 1 ATOM 867 O O . GLY A 1 110 ? 20.318 26.418 35.839 1.00 7.94 ? 196 GLY A O 1 ATOM 868 N N . VAL A 1 111 ? 20.276 25.155 37.701 1.00 8.21 ? 197 VAL A N 1 ATOM 869 C CA . VAL A 1 111 ? 18.823 24.993 37.666 1.00 8.58 ? 197 VAL A CA 1 ATOM 870 C C . VAL A 1 111 ? 18.123 26.332 37.804 1.00 7.79 ? 197 VAL A C 1 ATOM 871 O O . VAL A 1 111 ? 17.241 26.694 36.985 1.00 8.25 ? 197 VAL A O 1 ATOM 872 C CB . VAL A 1 111 ? 18.352 24.003 38.701 1.00 9.47 ? 197 VAL A CB 1 ATOM 873 C CG1 . VAL A 1 111 ? 16.849 23.999 38.867 1.00 11.64 ? 197 VAL A CG1 1 ATOM 874 C CG2 . VAL A 1 111 ? 18.841 22.617 38.306 1.00 12.36 ? 197 VAL A CG2 1 ATOM 875 N N . ASN A 1 112 ? 18.491 27.125 38.822 1.00 8.10 ? 198 ASN A N 1 ATOM 876 C CA . ASN A 1 112 ? 17.891 28.424 38.990 1.00 8.01 ? 198 ASN A CA 1 ATOM 877 C C . ASN A 1 112 ? 18.177 29.334 37.816 1.00 7.47 ? 198 ASN A C 1 ATOM 878 O O . ASN A 1 112 ? 17.308 30.092 37.367 1.00 7.82 ? 198 ASN A O 1 ATOM 879 C CB . ASN A 1 112 ? 18.317 29.062 40.308 1.00 10.11 ? 198 ASN A CB 1 ATOM 880 C CG . ASN A 1 112 ? 17.672 28.387 41.500 1.00 13.04 ? 198 ASN A CG 1 ATOM 881 O OD1 . ASN A 1 112 ? 16.570 27.868 41.394 1.00 15.73 ? 198 ASN A OD1 1 ATOM 882 N ND2 . ASN A 1 112 ? 18.372 28.395 42.645 1.00 17.02 ? 198 ASN A ND2 1 ATOM 883 N N . ASN A 1 113 ? 19.397 29.265 37.297 1.00 7.32 ? 199 ASN A N 1 ATOM 884 C CA . ASN A 1 113 ? 19.745 30.103 36.152 1.00 7.11 ? 199 ASN A CA 1 ATOM 885 C C . ASN A 1 113 ? 18.823 29.795 34.965 1.00 6.78 ? 199 ASN A C 1 ATOM 886 O O . ASN A 1 113 ? 18.372 30.704 34.271 1.00 6.83 ? 199 ASN A O 1 ATOM 887 C CB . ASN A 1 113 ? 21.200 29.860 35.732 1.00 7.62 ? 199 ASN A CB 1 ATOM 888 C CG . ASN A 1 113 ? 22.211 30.396 36.734 1.00 7.98 ? 199 ASN A CG 1 ATOM 889 O OD1 . ASN A 1 113 ? 21.862 31.102 37.677 1.00 8.46 ? 199 ASN A OD1 1 ATOM 890 N ND2 . ASN A 1 113 ? 23.461 30.038 36.501 1.00 9.21 ? 199 ASN A ND2 1 ATOM 891 N N . TYR A 1 114 ? 18.610 28.503 34.723 1.00 6.56 ? 200 TYR A N 1 ATOM 892 C CA . TYR A 1 114 ? 17.804 28.084 33.588 1.00 6.63 ? 200 TYR A CA 1 ATOM 893 C C . TYR A 1 114 ? 16.345 28.450 33.745 1.00 6.30 ? 200 TYR A C 1 ATOM 894 O O . TYR A 1 114 ? 15.698 28.930 32.812 1.00 6.72 ? 200 TYR A O 1 ATOM 895 C CB . TYR A 1 114 ? 17.934 26.598 33.367 1.00 6.36 ? 200 TYR A CB 1 ATOM 896 C CG . TYR A 1 114 ? 17.315 26.156 32.042 1.00 6.16 ? 200 TYR A CG 1 ATOM 897 C CD1 . TYR A 1 114 ? 17.987 26.317 30.861 1.00 6.57 ? 200 TYR A CD1 1 ATOM 898 C CD2 . TYR A 1 114 ? 16.032 25.630 31.987 1.00 6.55 ? 200 TYR A CD2 1 ATOM 899 C CE1 . TYR A 1 114 ? 17.441 25.963 29.631 1.00 6.53 ? 200 TYR A CE1 1 ATOM 900 C CE2 . TYR A 1 114 ? 15.457 25.228 30.769 1.00 6.57 ? 200 TYR A CE2 1 ATOM 901 C CZ . TYR A 1 114 ? 16.175 25.390 29.607 1.00 6.16 ? 200 TYR A CZ 1 ATOM 902 O OH . TYR A 1 114 ? 15.617 24.978 28.408 1.00 7.14 ? 200 TYR A OH 1 ATOM 903 N N . LYS A 1 115 ? 15.797 28.272 34.958 1.00 6.76 ? 201 LYS A N 1 ATOM 904 C CA . LYS A 1 115 ? 14.410 28.650 35.166 1.00 6.51 ? 201 LYS A CA 1 ATOM 905 C C . LYS A 1 115 ? 14.204 30.142 34.927 1.00 6.51 ? 201 LYS A C 1 ATOM 906 O O . LYS A 1 115 ? 13.218 30.556 34.348 1.00 7.04 ? 201 LYS A O 1 ATOM 907 C CB . LYS A 1 115 ? 13.906 28.251 36.564 1.00 7.60 ? 201 LYS A CB 1 ATOM 908 C CG . LYS A 1 115 ? 13.794 26.747 36.723 1.00 8.50 ? 201 LYS A CG 1 ATOM 909 C CD A LYS A 1 115 ? 13.215 26.386 38.080 0.60 12.12 ? 201 LYS A CD 1 ATOM 910 C CD B LYS A 1 115 ? 13.333 26.331 38.112 0.40 13.19 ? 201 LYS A CD 1 ATOM 911 C CE A LYS A 1 115 ? 12.877 24.893 38.134 0.60 14.52 ? 201 LYS A CE 1 ATOM 912 C CE B LYS A 1 115 ? 12.019 26.900 38.535 0.40 16.03 ? 201 LYS A CE 1 ATOM 913 N NZ A LYS A 1 115 ? 12.162 24.535 39.402 0.60 19.96 ? 201 LYS A NZ 1 ATOM 914 N NZ B LYS A 1 115 ? 11.620 26.352 39.876 0.40 19.89 ? 201 LYS A NZ 1 ATOM 915 N N . ALA A 1 116 ? 15.174 30.958 35.392 1.00 6.86 ? 202 ALA A N 1 ATOM 916 C CA . ALA A 1 116 ? 15.086 32.394 35.167 1.00 6.95 ? 202 ALA A CA 1 ATOM 917 C C . ALA A 1 116 ? 15.153 32.742 33.672 1.00 6.15 ? 202 ALA A C 1 ATOM 918 O O . ALA A 1 116 ? 14.469 33.656 33.225 1.00 6.90 ? 202 ALA A O 1 ATOM 919 C CB . ALA A 1 116 ? 16.147 33.140 35.962 1.00 7.67 ? 202 ALA A CB 1 ATOM 920 N N . TYR A 1 117 ? 16.021 32.056 32.928 1.00 6.39 ? 203 TYR A N 1 ATOM 921 C CA . TYR A 1 117 ? 16.161 32.214 31.468 1.00 6.48 ? 203 TYR A CA 1 ATOM 922 C C . TYR A 1 117 ? 14.818 31.904 30.793 1.00 5.86 ? 203 TYR A C 1 ATOM 923 O O . TYR A 1 117 ? 14.337 32.690 29.982 1.00 6.55 ? 203 TYR A O 1 ATOM 924 C CB . TYR A 1 117 ? 17.328 31.316 31.041 1.00 6.69 ? 203 TYR A CB 1 ATOM 925 C CG . TYR A 1 117 ? 17.474 30.887 29.602 1.00 6.06 ? 203 TYR A CG 1 ATOM 926 C CD1 . TYR A 1 117 ? 18.203 31.617 28.690 1.00 6.34 ? 203 TYR A CD1 1 ATOM 927 C CD2 . TYR A 1 117 ? 16.961 29.671 29.191 1.00 6.28 ? 203 TYR A CD2 1 ATOM 928 C CE1 . TYR A 1 117 ? 18.409 31.148 27.380 1.00 6.63 ? 203 TYR A CE1 1 ATOM 929 C CE2 . TYR A 1 117 ? 17.166 29.209 27.894 1.00 6.13 ? 203 TYR A CE2 1 ATOM 930 C CZ . TYR A 1 117 ? 17.887 29.941 26.995 1.00 6.19 ? 203 TYR A CZ 1 ATOM 931 O OH . TYR A 1 117 ? 18.091 29.439 25.726 1.00 7.19 ? 203 TYR A OH 1 ATOM 932 N N . ILE A 1 118 ? 14.205 30.773 31.120 1.00 6.16 ? 204 ILE A N 1 ATOM 933 C CA . ILE A 1 118 ? 12.870 30.440 30.591 1.00 6.24 ? 204 ILE A CA 1 ATOM 934 C C . ILE A 1 118 ? 11.851 31.511 30.974 1.00 6.19 ? 204 ILE A C 1 ATOM 935 O O . ILE A 1 118 ? 11.040 31.918 30.152 1.00 6.79 ? 204 ILE A O 1 ATOM 936 C CB . ILE A 1 118 ? 12.438 29.043 31.062 1.00 6.36 ? 204 ILE A CB 1 ATOM 937 C CG1 . ILE A 1 118 ? 13.325 27.962 30.488 1.00 6.41 ? 204 ILE A CG1 1 ATOM 938 C CG2 . ILE A 1 118 ? 10.965 28.798 30.745 1.00 6.82 ? 204 ILE A CG2 1 ATOM 939 C CD1 . ILE A 1 118 ? 13.397 27.868 28.961 1.00 7.42 ? 204 ILE A CD1 1 ATOM 940 N N . ASN A 1 119 ? 11.868 31.952 32.228 1.00 6.27 ? 205 ASN A N 1 ATOM 941 C CA . ASN A 1 119 ? 10.898 32.936 32.691 1.00 7.10 ? 205 ASN A CA 1 ATOM 942 C C . ASN A 1 119 ? 11.056 34.227 31.907 1.00 6.43 ? 205 ASN A C 1 ATOM 943 O O . ASN A 1 119 ? 10.064 34.906 31.599 1.00 6.94 ? 205 ASN A O 1 ATOM 944 C CB . ASN A 1 119 ? 11.075 33.229 34.199 1.00 8.20 ? 205 ASN A CB 1 ATOM 945 C CG . ASN A 1 119 ? 10.771 32.112 35.102 1.00 8.99 ? 205 ASN A CG 1 ATOM 946 O OD1 . ASN A 1 119 ? 10.074 31.184 34.731 1.00 9.84 ? 205 ASN A OD1 1 ATOM 947 N ND2 . ASN A 1 119 ? 11.240 32.202 36.390 1.00 10.85 ? 205 ASN A ND2 1 ATOM 948 N N . ARG A 1 120 ? 12.297 34.641 31.635 1.00 6.78 ? 206 ARG A N 1 ATOM 949 C CA . ARG A 1 120 ? 12.528 35.881 30.878 1.00 6.54 ? 206 ARG A CA 1 ATOM 950 C C . ARG A 1 120 ? 12.096 35.715 29.425 1.00 6.14 ? 206 ARG A C 1 ATOM 951 O O . ARG A 1 120 ? 11.478 36.619 28.862 1.00 6.93 ? 206 ARG A O 1 ATOM 952 C CB . ARG A 1 120 ? 13.986 36.321 30.988 1.00 7.04 ? 206 ARG A CB 1 ATOM 953 C CG . ARG A 1 120 ? 14.290 37.629 30.311 1.00 7.12 ? 206 ARG A CG 1 ATOM 954 C CD . ARG A 1 120 ? 13.516 38.799 30.921 1.00 9.24 ? 206 ARG A CD 1 ATOM 955 N NE . ARG A 1 120 ? 13.759 39.995 30.153 1.00 8.37 ? 206 ARG A NE 1 ATOM 956 C CZ . ARG A 1 120 ? 12.829 40.854 29.811 1.00 9.19 ? 206 ARG A CZ 1 ATOM 957 N NH1 . ARG A 1 120 ? 11.579 40.750 30.270 1.00 11.75 ? 206 ARG A NH1 1 ATOM 958 N NH2 . ARG A 1 120 ? 13.161 41.861 29.025 1.00 11.32 ? 206 ARG A NH2 1 ATOM 959 N N . ILE A 1 121 ? 12.397 34.574 28.822 1.00 6.35 ? 207 ILE A N 1 ATOM 960 C CA . ILE A 1 121 ? 11.913 34.284 27.477 1.00 6.42 ? 207 ILE A CA 1 ATOM 961 C C . ILE A 1 121 ? 10.385 34.381 27.465 1.00 6.29 ? 207 ILE A C 1 ATOM 962 O O . ILE A 1 121 ? 9.819 35.004 26.556 1.00 6.81 ? 207 ILE A O 1 ATOM 963 C CB . ILE A 1 121 ? 12.433 32.941 26.972 1.00 5.98 ? 207 ILE A CB 1 ATOM 964 C CG1 . ILE A 1 121 ? 13.943 32.985 26.736 1.00 6.57 ? 207 ILE A CG1 1 ATOM 965 C CG2 . ILE A 1 121 ? 11.714 32.514 25.695 1.00 6.74 ? 207 ILE A CG2 1 ATOM 966 C CD1 . ILE A 1 121 ? 14.586 31.638 26.569 1.00 7.24 ? 207 ILE A CD1 1 ATOM 967 N N . ARG A 1 122 ? 9.703 33.782 28.445 1.00 6.49 ? 208 ARG A N 1 ATOM 968 C CA . ARG A 1 122 ? 8.239 33.865 28.495 1.00 6.46 ? 208 ARG A CA 1 ATOM 969 C C . ARG A 1 122 ? 7.775 35.311 28.502 1.00 6.75 ? 208 ARG A C 1 ATOM 970 O O . ARG A 1 122 ? 6.841 35.693 27.779 1.00 6.92 ? 208 ARG A O 1 ATOM 971 C CB . ARG A 1 122 ? 7.704 33.122 29.718 1.00 6.57 ? 208 ARG A CB 1 ATOM 972 C CG . ARG A 1 122 ? 6.196 33.161 29.808 1.00 7.84 ? 208 ARG A CG 1 ATOM 973 C CD A ARG A 1 122 ? 5.686 32.540 31.118 0.75 8.40 ? 208 ARG A CD 1 ATOM 974 C CD B ARG A 1 122 ? 5.663 32.537 31.026 0.25 7.62 ? 208 ARG A CD 1 ATOM 975 N NE A ARG A 1 122 ? 4.291 32.922 31.420 0.75 9.20 ? 208 ARG A NE 1 ATOM 976 N NE B ARG A 1 122 ? 4.300 32.027 30.839 0.25 7.61 ? 208 ARG A NE 1 ATOM 977 C CZ A ARG A 1 122 ? 3.248 32.162 31.088 0.75 8.66 ? 208 ARG A CZ 1 ATOM 978 C CZ B ARG A 1 122 ? 3.205 32.671 31.260 0.25 9.50 ? 208 ARG A CZ 1 ATOM 979 N NH1 A ARG A 1 122 ? 3.407 30.985 30.546 0.75 8.92 ? 208 ARG A NH1 1 ATOM 980 N NH1 B ARG A 1 122 ? 3.282 33.877 31.826 0.25 8.64 ? 208 ARG A NH1 1 ATOM 981 N NH2 A ARG A 1 122 ? 1.989 32.584 31.320 0.75 11.61 ? 208 ARG A NH2 1 ATOM 982 N NH2 B ARG A 1 122 ? 1.997 32.116 31.092 0.25 9.80 ? 208 ARG A NH2 1 ATOM 983 N N . GLU A 1 123 ? 8.387 36.168 29.330 1.00 6.52 ? 209 GLU A N 1 ATOM 984 C CA . GLU A 1 123 ? 7.987 37.558 29.407 1.00 6.82 ? 209 GLU A CA 1 ATOM 985 C C . GLU A 1 123 ? 8.129 38.222 28.030 1.00 6.53 ? 209 GLU A C 1 ATOM 986 O O . GLU A 1 123 ? 7.252 39.020 27.627 1.00 6.88 ? 209 GLU A O 1 ATOM 987 C CB . GLU A 1 123 ? 8.856 38.310 30.405 1.00 7.26 ? 209 GLU A CB 1 ATOM 988 C CG . GLU A 1 123 ? 8.581 37.969 31.845 1.00 8.13 ? 209 GLU A CG 1 ATOM 989 C CD . GLU A 1 123 ? 9.478 38.668 32.831 1.00 10.59 ? 209 GLU A CD 1 ATOM 990 O OE1 . GLU A 1 123 ? 10.564 39.162 32.501 1.00 11.51 ? 209 GLU A OE1 1 ATOM 991 O OE2 . GLU A 1 123 ? 9.128 38.612 34.057 1.00 16.53 ? 209 GLU A OE2 1 ATOM 992 N N . ILE A 1 124 ? 9.224 37.970 27.334 1.00 6.61 ? 210 ILE A N 1 ATOM 993 C CA . ILE A 1 124 ? 9.462 38.582 26.025 1.00 6.64 ? 210 ILE A CA 1 ATOM 994 C C . ILE A 1 124 ? 8.479 38.064 24.994 1.00 6.73 ? 210 ILE A C 1 ATOM 995 O O . ILE A 1 124 ? 7.930 38.847 24.208 1.00 6.78 ? 210 ILE A O 1 ATOM 996 C CB . ILE A 1 124 ? 10.920 38.418 25.624 1.00 6.33 ? 210 ILE A CB 1 ATOM 997 C CG1 . ILE A 1 124 ? 11.842 39.216 26.571 1.00 7.35 ? 210 ILE A CG1 1 ATOM 998 C CG2 . ILE A 1 124 ? 11.143 38.793 24.169 1.00 7.21 ? 210 ILE A CG2 1 ATOM 999 C CD1 . ILE A 1 124 ? 13.278 38.778 26.548 1.00 7.66 ? 210 ILE A CD1 1 ATOM 1000 N N . LEU A 1 125 ? 8.237 36.752 24.971 1.00 6.26 ? 211 LEU A N 1 ATOM 1001 C CA . LEU A 1 125 ? 7.274 36.211 24.028 1.00 6.54 ? 211 LEU A CA 1 ATOM 1002 C C . LEU A 1 125 ? 5.872 36.804 24.260 1.00 6.57 ? 211 LEU A C 1 ATOM 1003 O O . LEU A 1 125 ? 5.175 37.129 23.314 1.00 7.09 ? 211 LEU A O 1 ATOM 1004 C CB . LEU A 1 125 ? 7.246 34.689 24.092 1.00 6.61 ? 211 LEU A CB 1 ATOM 1005 C CG . LEU A 1 125 ? 8.554 33.999 23.734 1.00 7.06 ? 211 LEU A CG 1 ATOM 1006 C CD1 . LEU A 1 125 ? 8.341 32.505 23.812 1.00 9.65 ? 211 LEU A CD1 1 ATOM 1007 C CD2 . LEU A 1 125 ? 9.069 34.410 22.374 1.00 9.98 ? 211 LEU A CD2 1 ATOM 1008 N N . ILE A 1 126 ? 5.458 36.924 25.528 1.00 6.50 ? 212 ILE A N 1 ATOM 1009 C CA . ILE A 1 126 ? 4.175 37.596 25.820 1.00 7.38 ? 212 ILE A CA 1 ATOM 1010 C C . ILE A 1 126 ? 4.154 39.005 25.290 1.00 6.55 ? 212 ILE A C 1 ATOM 1011 O O . ILE A 1 126 ? 3.160 39.427 24.645 1.00 7.35 ? 212 ILE A O 1 ATOM 1012 C CB . ILE A 1 126 ? 3.927 37.539 27.362 1.00 8.55 ? 212 ILE A CB 1 ATOM 1013 C CG1 . ILE A 1 126 ? 3.477 36.159 27.768 1.00 8.85 ? 212 ILE A CG1 1 ATOM 1014 C CG2 . ILE A 1 126 ? 2.982 38.648 27.858 1.00 9.22 ? 212 ILE A CG2 1 ATOM 1015 C CD1 . ILE A 1 126 ? 3.416 35.940 29.270 1.00 10.45 ? 212 ILE A CD1 1 ATOM 1016 N N . SER A 1 127 ? 5.216 39.758 25.494 1.00 6.94 ? 213 SER A N 1 ATOM 1017 C CA A SER A 1 127 ? 5.300 41.122 24.969 0.50 6.95 ? 213 SER A CA 1 ATOM 1018 C CA B SER A 1 127 ? 5.226 41.123 24.986 0.20 7.07 ? 213 SER A CA 1 ATOM 1019 C CA C SER A 1 127 ? 5.308 41.118 24.953 0.30 7.17 ? 213 SER A CA 1 ATOM 1020 C C . SER A 1 127 ? 5.055 41.138 23.465 1.00 6.88 ? 213 SER A C 1 ATOM 1021 O O . SER A 1 127 ? 4.376 42.026 22.953 1.00 7.29 ? 213 SER A O 1 ATOM 1022 C CB A SER A 1 127 ? 6.623 41.725 25.375 0.50 8.07 ? 213 SER A CB 1 ATOM 1023 C CB B SER A 1 127 ? 6.450 41.880 25.453 0.20 7.54 ? 213 SER A CB 1 ATOM 1024 C CB C SER A 1 127 ? 6.671 41.709 25.246 0.30 7.92 ? 213 SER A CB 1 ATOM 1025 O OG A SER A 1 127 ? 6.740 43.088 24.976 0.50 8.42 ? 213 SER A OG 1 ATOM 1026 O OG B SER A 1 127 ? 7.597 41.476 24.759 0.20 6.85 ? 213 SER A OG 1 ATOM 1027 O OG C SER A 1 127 ? 6.740 42.121 26.596 0.30 10.64 ? 213 SER A OG 1 ATOM 1028 N N . PHE A 1 128 ? 5.614 40.152 22.777 1.00 6.80 ? 214 PHE A N 1 ATOM 1029 C CA . PHE A 1 128 ? 5.512 39.971 21.331 1.00 6.95 ? 214 PHE A CA 1 ATOM 1030 C C . PHE A 1 128 ? 4.520 38.907 20.928 1.00 6.65 ? 214 PHE A C 1 ATOM 1031 O O . PHE A 1 128 ? 4.740 38.184 19.921 1.00 7.39 ? 214 PHE A O 1 ATOM 1032 C CB . PHE A 1 128 ? 6.905 39.764 20.710 1.00 7.61 ? 214 PHE A CB 1 ATOM 1033 C CG . PHE A 1 128 ? 7.789 40.968 20.838 1.00 7.81 ? 214 PHE A CG 1 ATOM 1034 C CD1 . PHE A 1 128 ? 7.678 41.995 19.916 1.00 9.21 ? 214 PHE A CD1 1 ATOM 1035 C CD2 . PHE A 1 128 ? 8.691 41.070 21.842 1.00 8.56 ? 214 PHE A CD2 1 ATOM 1036 C CE1 . PHE A 1 128 ? 8.508 43.118 20.029 1.00 11.37 ? 214 PHE A CE1 1 ATOM 1037 C CE2 . PHE A 1 128 ? 9.505 42.192 21.955 1.00 10.19 ? 214 PHE A CE2 1 ATOM 1038 C CZ . PHE A 1 128 ? 9.403 43.218 21.058 1.00 13.54 ? 214 PHE A CZ 1 ATOM 1039 N N . SER A 1 129 ? 3.373 38.847 21.603 1.00 6.57 ? 215 SER A N 1 ATOM 1040 C CA . SER A 1 129 ? 2.331 37.895 21.257 1.00 6.82 ? 215 SER A CA 1 ATOM 1041 C C . SER A 1 129 ? 1.797 38.046 19.842 1.00 7.18 ? 215 SER A C 1 ATOM 1042 O O . SER A 1 129 ? 1.216 37.102 19.293 1.00 7.75 ? 215 SER A O 1 ATOM 1043 C CB . SER A 1 129 ? 1.185 38.052 22.235 1.00 7.22 ? 215 SER A CB 1 ATOM 1044 O OG . SER A 1 129 ? 0.621 39.354 22.189 1.00 7.50 ? 215 SER A OG 1 ATOM 1045 N N . ASP A 1 130 ? 1.971 39.223 19.258 1.00 6.94 ? 216 ASP A N 1 ATOM 1046 C CA . ASP A 1 130 ? 1.593 39.492 17.882 1.00 7.57 ? 216 ASP A CA 1 ATOM 1047 C C . ASP A 1 130 ? 2.505 38.841 16.861 1.00 7.13 ? 216 ASP A C 1 ATOM 1048 O O . ASP A 1 130 ? 2.160 38.873 15.659 1.00 9.60 ? 216 ASP A O 1 ATOM 1049 C CB . ASP A 1 130 ? 1.480 40.989 17.651 1.00 7.89 ? 216 ASP A CB 1 ATOM 1050 C CG . ASP A 1 130 ? 2.647 41.806 18.119 1.00 8.55 ? 216 ASP A CG 1 ATOM 1051 O OD1 . ASP A 1 130 ? 3.322 41.506 19.137 1.00 10.12 ? 216 ASP A OD1 1 ATOM 1052 O OD2 . ASP A 1 130 ? 2.908 42.873 17.490 1.00 10.96 ? 216 ASP A OD2 1 ATOM 1053 N N . VAL A 1 131 ? 3.623 38.264 17.236 1.00 7.17 ? 217 VAL A N 1 ATOM 1054 C CA . VAL A 1 131 ? 4.580 37.629 16.328 1.00 7.16 ? 217 VAL A CA 1 ATOM 1055 C C . VAL A 1 131 ? 4.544 36.116 16.555 1.00 6.67 ? 217 VAL A C 1 ATOM 1056 O O . VAL A 1 131 ? 5.034 35.660 17.585 1.00 7.10 ? 217 VAL A O 1 ATOM 1057 C CB . VAL A 1 131 ? 5.995 38.171 16.503 1.00 7.53 ? 217 VAL A CB 1 ATOM 1058 C CG1 . VAL A 1 131 ? 6.915 37.427 15.605 1.00 8.25 ? 217 VAL A CG1 1 ATOM 1059 C CG2 . VAL A 1 131 ? 6.055 39.686 16.292 1.00 8.43 ? 217 VAL A CG2 1 ATOM 1060 N N . ARG A 1 132 ? 3.932 35.390 15.653 1.00 7.20 ? 218 ARG A N 1 ATOM 1061 C CA . ARG A 1 132 ? 3.901 33.938 15.805 1.00 6.92 ? 218 ARG A CA 1 ATOM 1062 C C . ARG A 1 132 ? 5.348 33.428 15.914 1.00 6.53 ? 218 ARG A C 1 ATOM 1063 O O . ARG A 1 132 ? 6.190 33.836 15.116 1.00 7.29 ? 218 ARG A O 1 ATOM 1064 C CB . ARG A 1 132 ? 3.215 33.292 14.610 1.00 7.72 ? 218 ARG A CB 1 ATOM 1065 C CG . ARG A 1 132 ? 2.906 31.785 14.888 1.00 8.30 ? 218 ARG A CG 1 ATOM 1066 C CD . ARG A 1 132 ? 2.281 31.068 13.730 1.00 8.62 ? 218 ARG A CD 1 ATOM 1067 N NE . ARG A 1 132 ? 0.996 31.661 13.384 1.00 9.19 ? 218 ARG A NE 1 ATOM 1068 C CZ . ARG A 1 132 ? 0.315 31.242 12.325 1.00 9.50 ? 218 ARG A CZ 1 ATOM 1069 N NH1 . ARG A 1 132 ? 0.778 30.302 11.523 1.00 10.07 ? 218 ARG A NH1 1 ATOM 1070 N NH2 . ARG A 1 132 ? -0.876 31.783 12.051 1.00 11.26 ? 218 ARG A NH2 1 ATOM 1071 N N . THR A 1 133 ? 5.630 32.590 16.896 1.00 6.57 ? 219 THR A N 1 ATOM 1072 C CA . THR A 1 133 ? 6.998 32.201 17.241 1.00 6.24 ? 219 THR A CA 1 ATOM 1073 C C . THR A 1 133 ? 7.101 30.692 17.350 1.00 5.86 ? 219 THR A C 1 ATOM 1074 O O . THR A 1 133 ? 6.392 30.064 18.128 1.00 7.16 ? 219 THR A O 1 ATOM 1075 C CB . THR A 1 133 ? 7.417 32.898 18.507 1.00 7.00 ? 219 THR A CB 1 ATOM 1076 O OG1 . THR A 1 133 ? 7.393 34.318 18.344 1.00 7.05 ? 219 THR A OG1 1 ATOM 1077 C CG2 . THR A 1 133 ? 8.821 32.490 18.914 1.00 8.07 ? 219 THR A CG2 1 ATOM 1078 N N . ILE A 1 134 ? 7.999 30.133 16.562 1.00 5.90 ? 220 ILE A N 1 ATOM 1079 C CA . ILE A 1 134 ? 8.235 28.699 16.491 1.00 5.82 ? 220 ILE A CA 1 ATOM 1080 C C . ILE A 1 134 ? 9.551 28.378 17.161 1.00 5.44 ? 220 ILE A C 1 ATOM 1081 O O . ILE A 1 134 ? 10.587 28.967 16.771 1.00 6.31 ? 220 ILE A O 1 ATOM 1082 C CB . ILE A 1 134 ? 8.212 28.248 15.014 1.00 6.59 ? 220 ILE A CB 1 ATOM 1083 C CG1 . ILE A 1 134 ? 6.830 28.554 14.373 1.00 8.04 ? 220 ILE A CG1 1 ATOM 1084 C CG2 . ILE A 1 134 ? 8.536 26.775 14.940 1.00 7.65 ? 220 ILE A CG2 1 ATOM 1085 C CD1 . ILE A 1 134 ? 6.822 28.636 12.857 1.00 8.38 ? 220 ILE A CD1 1 ATOM 1086 N N . LEU A 1 135 ? 9.532 27.490 18.130 1.00 5.85 ? 221 LEU A N 1 ATOM 1087 C CA . LEU A 1 135 ? 10.695 27.145 18.932 1.00 6.10 ? 221 LEU A CA 1 ATOM 1088 C C . LEU A 1 135 ? 11.143 25.704 18.713 1.00 5.56 ? 221 LEU A C 1 ATOM 1089 O O . LEU A 1 135 ? 10.312 24.792 18.672 1.00 6.24 ? 221 LEU A O 1 ATOM 1090 C CB . LEU A 1 135 ? 10.369 27.260 20.440 1.00 6.31 ? 221 LEU A CB 1 ATOM 1091 C CG . LEU A 1 135 ? 9.794 28.595 20.915 1.00 6.48 ? 221 LEU A CG 1 ATOM 1092 C CD1 . LEU A 1 135 ? 9.528 28.561 22.405 1.00 6.93 ? 221 LEU A CD1 1 ATOM 1093 C CD2 . LEU A 1 135 ? 10.720 29.715 20.549 1.00 7.61 ? 221 LEU A CD2 1 ATOM 1094 N N . VAL A 1 136 ? 12.458 25.513 18.617 1.00 5.38 ? 222 VAL A N 1 ATOM 1095 C CA . VAL A 1 136 ? 13.092 24.222 18.825 1.00 5.22 ? 222 VAL A CA 1 ATOM 1096 C C . VAL A 1 136 ? 13.602 24.211 20.250 1.00 5.45 ? 222 VAL A C 1 ATOM 1097 O O . VAL A 1 136 ? 14.351 25.114 20.650 1.00 6.46 ? 222 VAL A O 1 ATOM 1098 C CB . VAL A 1 136 ? 14.232 23.956 17.824 1.00 6.19 ? 222 VAL A CB 1 ATOM 1099 C CG1 . VAL A 1 136 ? 15.057 22.737 18.241 1.00 6.57 ? 222 VAL A CG1 1 ATOM 1100 C CG2 . VAL A 1 136 ? 13.637 23.764 16.419 1.00 6.37 ? 222 VAL A CG2 1 ATOM 1101 N N . ILE A 1 137 ? 13.221 23.200 21.039 1.00 5.38 ? 223 ILE A N 1 ATOM 1102 C CA . ILE A 1 137 ? 13.630 23.083 22.419 1.00 5.86 ? 223 ILE A CA 1 ATOM 1103 C C . ILE A 1 137 ? 14.813 22.132 22.561 1.00 5.68 ? 223 ILE A C 1 ATOM 1104 O O . ILE A 1 137 ? 14.710 20.924 22.335 1.00 5.98 ? 223 ILE A O 1 ATOM 1105 C CB . ILE A 1 137 ? 12.461 22.637 23.338 1.00 5.96 ? 223 ILE A CB 1 ATOM 1106 C CG1 . ILE A 1 137 ? 11.240 23.547 23.155 1.00 6.93 ? 223 ILE A CG1 1 ATOM 1107 C CG2 . ILE A 1 137 ? 12.892 22.514 24.778 1.00 6.72 ? 223 ILE A CG2 1 ATOM 1108 C CD1 . ILE A 1 137 ? 11.469 25.013 23.567 1.00 7.59 ? 223 ILE A CD1 1 ATOM 1109 N N . GLU A 1 138 ? 15.955 22.734 22.932 1.00 5.42 ? 224 GLU A N 1 ATOM 1110 C CA . GLU A 1 138 ? 17.151 22.050 23.482 1.00 5.56 ? 224 GLU A CA 1 ATOM 1111 C C . GLU A 1 138 ? 17.699 20.908 22.648 1.00 5.44 ? 224 GLU A C 1 ATOM 1112 O O . GLU A 1 138 ? 17.624 19.719 23.003 1.00 5.82 ? 224 GLU A O 1 ATOM 1113 C CB . GLU A 1 138 ? 16.904 21.661 24.936 1.00 6.23 ? 224 GLU A CB 1 ATOM 1114 C CG . GLU A 1 138 ? 16.654 22.838 25.873 1.00 6.18 ? 224 GLU A CG 1 ATOM 1115 C CD . GLU A 1 138 ? 17.867 23.723 26.140 1.00 6.19 ? 224 GLU A CD 1 ATOM 1116 O OE1 . GLU A 1 138 ? 19.018 23.288 25.916 1.00 6.64 ? 224 GLU A OE1 1 ATOM 1117 O OE2 . GLU A 1 138 ? 17.617 24.865 26.631 1.00 6.40 ? 224 GLU A OE2 1 ATOM 1118 N N . PRO A 1 139 ? 18.366 21.229 21.533 1.00 5.97 ? 225 PRO A N 1 ATOM 1119 C CA . PRO A 1 139 ? 19.180 20.229 20.819 1.00 6.09 ? 225 PRO A CA 1 ATOM 1120 C C . PRO A 1 139 ? 20.098 19.483 21.789 1.00 6.13 ? 225 PRO A C 1 ATOM 1121 O O . PRO A 1 139 ? 20.604 20.038 22.762 1.00 6.41 ? 225 PRO A O 1 ATOM 1122 C CB . PRO A 1 139 ? 19.950 21.113 19.798 1.00 7.16 ? 225 PRO A CB 1 ATOM 1123 C CG . PRO A 1 139 ? 19.023 22.255 19.555 1.00 7.05 ? 225 PRO A CG 1 ATOM 1124 C CD . PRO A 1 139 ? 18.488 22.566 20.916 1.00 6.48 ? 225 PRO A CD 1 ATOM 1125 N N . ASP A 1 140 ? 20.368 18.238 21.444 1.00 6.34 ? 226 ASP A N 1 ATOM 1126 C CA . ASP A 1 140 ? 21.398 17.454 22.144 1.00 6.35 ? 226 ASP A CA 1 ATOM 1127 C C . ASP A 1 140 ? 21.117 17.371 23.651 1.00 6.26 ? 226 ASP A C 1 ATOM 1128 O O . ASP A 1 140 ? 22.071 17.472 24.446 1.00 6.65 ? 226 ASP A O 1 ATOM 1129 C CB . ASP A 1 140 ? 22.794 18.017 21.905 1.00 7.31 ? 226 ASP A CB 1 ATOM 1130 C CG . ASP A 1 140 ? 23.861 17.071 22.388 1.00 7.55 ? 226 ASP A CG 1 ATOM 1131 O OD1 . ASP A 1 140 ? 23.695 15.842 22.340 1.00 9.76 ? 226 ASP A OD1 1 ATOM 1132 O OD2 . ASP A 1 140 ? 24.969 17.570 22.825 1.00 8.01 ? 226 ASP A OD2 1 ATOM 1133 N N . SER A 1 141 ? 19.869 17.154 24.039 1.00 6.08 ? 227 SER A N 1 ATOM 1134 C CA . SER A 1 141 ? 19.482 17.066 25.453 1.00 6.17 ? 227 SER A CA 1 ATOM 1135 C C . SER A 1 141 ? 18.909 15.695 25.749 1.00 6.32 ? 227 SER A C 1 ATOM 1136 O O . SER A 1 141 ? 19.665 14.775 26.032 1.00 6.58 ? 227 SER A O 1 ATOM 1137 C CB . SER A 1 141 ? 18.583 18.254 25.871 1.00 6.61 ? 227 SER A CB 1 ATOM 1138 O OG . SER A 1 141 ? 17.329 18.239 25.226 1.00 6.18 ? 227 SER A OG 1 ATOM 1139 N N . LEU A 1 142 ? 17.584 15.548 25.656 1.00 6.35 ? 228 LEU A N 1 ATOM 1140 C CA . LEU A 1 142 ? 16.932 14.301 26.037 1.00 6.55 ? 228 LEU A CA 1 ATOM 1141 C C . LEU A 1 142 ? 17.321 13.137 25.170 1.00 6.12 ? 228 LEU A C 1 ATOM 1142 O O . LEU A 1 142 ? 17.231 11.986 25.642 1.00 6.72 ? 228 LEU A O 1 ATOM 1143 C CB . LEU A 1 142 ? 15.432 14.496 26.026 1.00 6.90 ? 228 LEU A CB 1 ATOM 1144 C CG . LEU A 1 142 ? 14.884 15.387 27.133 1.00 8.33 ? 228 LEU A CG 1 ATOM 1145 C CD1 . LEU A 1 142 ? 13.393 15.677 26.845 1.00 10.29 ? 228 LEU A CD1 1 ATOM 1146 C CD2 . LEU A 1 142 ? 15.067 14.771 28.491 1.00 10.48 ? 228 LEU A CD2 1 ATOM 1147 N N . ALA A 1 143 ? 17.796 13.332 23.940 1.00 6.61 ? 229 ALA A N 1 ATOM 1148 C CA . ALA A 1 143 ? 18.284 12.191 23.176 1.00 6.59 ? 229 ALA A CA 1 ATOM 1149 C C . ALA A 1 143 ? 19.375 11.440 23.941 1.00 6.55 ? 229 ALA A C 1 ATOM 1150 O O . ALA A 1 143 ? 19.538 10.232 23.821 1.00 7.32 ? 229 ALA A O 1 ATOM 1151 C CB . ALA A 1 143 ? 18.788 12.658 21.836 1.00 7.60 ? 229 ALA A CB 1 ATOM 1152 N N . ASN A 1 144 ? 20.155 12.161 24.767 1.00 6.51 ? 230 ASN A N 1 ATOM 1153 C CA . ASN A 1 144 ? 21.176 11.522 25.587 1.00 7.13 ? 230 ASN A CA 1 ATOM 1154 C C . ASN A 1 144 ? 20.595 10.575 26.640 1.00 6.74 ? 230 ASN A C 1 ATOM 1155 O O . ASN A 1 144 ? 21.293 9.640 27.066 1.00 8.04 ? 230 ASN A O 1 ATOM 1156 C CB . ASN A 1 144 ? 22.026 12.582 26.309 1.00 7.05 ? 230 ASN A CB 1 ATOM 1157 C CG . ASN A 1 144 ? 22.852 13.382 25.349 1.00 7.12 ? 230 ASN A CG 1 ATOM 1158 O OD1 . ASN A 1 144 ? 23.824 12.858 24.796 1.00 8.06 ? 230 ASN A OD1 1 ATOM 1159 N ND2 . ASN A 1 144 ? 22.479 14.619 25.096 1.00 7.90 ? 230 ASN A ND2 1 ATOM 1160 N N . MET A 1 145 ? 19.376 10.777 27.090 1.00 7.20 ? 231 MET A N 1 ATOM 1161 C CA . MET A 1 145 ? 18.761 9.874 28.052 1.00 7.44 ? 231 MET A CA 1 ATOM 1162 C C . MET A 1 145 ? 18.406 8.587 27.380 1.00 7.86 ? 231 MET A C 1 ATOM 1163 O O . MET A 1 145 ? 18.199 7.569 28.063 1.00 10.75 ? 231 MET A O 1 ATOM 1164 C CB . MET A 1 145 ? 17.547 10.488 28.732 1.00 8.68 ? 231 MET A CB 1 ATOM 1165 C CG . MET A 1 145 ? 17.816 11.389 29.925 1.00 9.12 ? 231 MET A CG 1 ATOM 1166 S SD . MET A 1 145 ? 18.612 12.971 29.593 1.00 8.58 ? 231 MET A SD 1 ATOM 1167 C CE . MET A 1 145 ? 20.343 12.582 29.855 1.00 8.39 ? 231 MET A CE 1 ATOM 1168 N N . VAL A 1 146 ? 18.329 8.539 26.064 1.00 8.24 ? 232 VAL A N 1 ATOM 1169 C CA . VAL A 1 146 ? 18.026 7.297 25.357 1.00 8.78 ? 232 VAL A CA 1 ATOM 1170 C C . VAL A 1 146 ? 19.239 6.390 25.260 1.00 9.68 ? 232 VAL A C 1 ATOM 1171 O O . VAL A 1 146 ? 19.131 5.180 25.540 1.00 12.17 ? 232 VAL A O 1 ATOM 1172 C CB . VAL A 1 146 ? 17.446 7.545 23.949 1.00 9.24 ? 232 VAL A CB 1 ATOM 1173 C CG1 . VAL A 1 146 ? 17.073 6.210 23.282 1.00 10.16 ? 232 VAL A CG1 1 ATOM 1174 C CG2 . VAL A 1 146 ? 16.242 8.457 24.028 1.00 10.06 ? 232 VAL A CG2 1 ATOM 1175 N N . THR A 1 147 ? 20.399 6.907 24.917 1.00 8.69 ? 233 THR A N 1 ATOM 1176 C CA . THR A 1 147 ? 21.535 6.082 24.612 1.00 9.06 ? 233 THR A CA 1 ATOM 1177 C C . THR A 1 147 ? 22.761 6.333 25.465 1.00 9.05 ? 233 THR A C 1 ATOM 1178 O O . THR A 1 147 ? 23.663 5.500 25.420 1.00 10.52 ? 233 THR A O 1 ATOM 1179 C CB . THR A 1 147 ? 21.977 6.234 23.139 1.00 9.81 ? 233 THR A CB 1 ATOM 1180 O OG1 . THR A 1 147 ? 22.486 7.560 22.928 1.00 8.87 ? 233 THR A OG1 1 ATOM 1181 C CG2 . THR A 1 147 ? 20.866 5.995 22.138 1.00 11.18 ? 233 THR A CG2 1 ATOM 1182 N N . ASN A 1 148 ? 22.841 7.402 26.230 1.00 8.44 ? 234 ASN A N 1 ATOM 1183 C CA . ASN A 1 148 ? 24.065 7.807 26.877 1.00 8.53 ? 234 ASN A CA 1 ATOM 1184 C C . ASN A 1 148 ? 23.982 7.831 28.406 1.00 8.58 ? 234 ASN A C 1 ATOM 1185 O O . ASN A 1 148 ? 24.779 8.503 29.058 1.00 9.49 ? 234 ASN A O 1 ATOM 1186 C CB . ASN A 1 148 ? 24.554 9.141 26.353 1.00 8.78 ? 234 ASN A CB 1 ATOM 1187 C CG . ASN A 1 148 ? 24.883 9.106 24.859 1.00 10.29 ? 234 ASN A CG 1 ATOM 1188 O OD1 . ASN A 1 148 ? 25.212 8.027 24.304 1.00 16.25 ? 234 ASN A OD1 1 ATOM 1189 N ND2 . ASN A 1 148 ? 24.778 10.222 24.151 1.00 8.81 ? 234 ASN A ND2 1 ATOM 1190 N N . MET A 1 149 ? 23.091 7.062 28.991 1.00 8.96 ? 235 MET A N 1 ATOM 1191 C CA . MET A 1 149 ? 22.967 7.049 30.456 1.00 9.40 ? 235 MET A CA 1 ATOM 1192 C C . MET A 1 149 ? 24.121 6.328 31.146 1.00 9.69 ? 235 MET A C 1 ATOM 1193 O O . MET A 1 149 ? 24.274 6.435 32.383 1.00 10.23 ? 235 MET A O 1 ATOM 1194 C CB . MET A 1 149 ? 21.668 6.417 30.908 1.00 9.80 ? 235 MET A CB 1 ATOM 1195 C CG . MET A 1 149 ? 20.481 7.323 30.595 1.00 11.08 ? 235 MET A CG 1 ATOM 1196 S SD . MET A 1 149 ? 20.401 8.824 31.586 1.00 10.96 ? 235 MET A SD 1 ATOM 1197 C CE . MET A 1 149 ? 19.881 8.146 33.134 1.00 13.48 ? 235 MET A CE 1 ATOM 1198 N N . ASN A 1 150 ? 24.982 5.687 30.396 1.00 9.84 ? 236 ASN A N 1 ATOM 1199 C CA . ASN A 1 150 ? 26.267 5.173 30.901 1.00 10.63 ? 236 ASN A CA 1 ATOM 1200 C C . ASN A 1 150 ? 27.253 6.279 31.164 1.00 9.92 ? 236 ASN A C 1 ATOM 1201 O O . ASN A 1 150 ? 28.214 6.067 31.924 1.00 11.76 ? 236 ASN A O 1 ATOM 1202 C CB . ASN A 1 150 ? 26.873 4.146 29.929 1.00 12.92 ? 236 ASN A CB 1 ATOM 1203 C CG . ASN A 1 150 ? 27.128 4.738 28.561 1.00 15.12 ? 236 ASN A CG 1 ATOM 1204 O OD1 . ASN A 1 150 ? 26.210 5.153 27.881 1.00 18.17 ? 236 ASN A OD1 1 ATOM 1205 N ND2 . ASN A 1 150 ? 28.365 4.834 28.177 1.00 21.84 ? 236 ASN A ND2 1 ATOM 1206 N N . VAL A 1 151 ? 27.088 7.442 30.550 1.00 9.36 ? 237 VAL A N 1 ATOM 1207 C CA . VAL A 1 151 ? 28.004 8.554 30.763 1.00 9.48 ? 237 VAL A CA 1 ATOM 1208 C C . VAL A 1 151 ? 27.666 9.183 32.129 1.00 9.41 ? 237 VAL A C 1 ATOM 1209 O O . VAL A 1 151 ? 26.508 9.648 32.309 1.00 9.37 ? 237 VAL A O 1 ATOM 1210 C CB . VAL A 1 151 ? 27.895 9.611 29.652 1.00 10.33 ? 237 VAL A CB 1 ATOM 1211 C CG1 . VAL A 1 151 ? 28.773 10.762 29.913 1.00 11.58 ? 237 VAL A CG1 1 ATOM 1212 C CG2 . VAL A 1 151 ? 28.171 8.973 28.275 1.00 11.26 ? 237 VAL A CG2 1 ATOM 1213 N N . PRO A 1 152 ? 28.609 9.264 33.084 1.00 9.17 ? 238 PRO A N 1 ATOM 1214 C CA . PRO A 1 152 ? 28.229 9.775 34.393 1.00 9.31 ? 238 PRO A CA 1 ATOM 1215 C C . PRO A 1 152 ? 27.539 11.120 34.385 1.00 8.43 ? 238 PRO A C 1 ATOM 1216 O O . PRO A 1 152 ? 26.571 11.352 35.106 1.00 9.75 ? 238 PRO A O 1 ATOM 1217 C CB . PRO A 1 152 ? 29.543 9.752 35.181 1.00 10.08 ? 238 PRO A CB 1 ATOM 1218 C CG . PRO A 1 152 ? 30.343 8.608 34.541 1.00 10.86 ? 238 PRO A CG 1 ATOM 1219 C CD . PRO A 1 152 ? 29.988 8.691 33.066 1.00 9.65 ? 238 PRO A CD 1 ATOM 1220 N N . LYS A 1 153 ? 28.054 12.057 33.579 1.00 8.58 ? 239 LYS A N 1 ATOM 1221 C CA . LYS A 1 153 ? 27.451 13.396 33.516 1.00 8.43 ? 239 LYS A CA 1 ATOM 1222 C C . LYS A 1 153 ? 26.028 13.339 33.034 1.00 8.11 ? 239 LYS A C 1 ATOM 1223 O O . LYS A 1 153 ? 25.172 14.112 33.484 1.00 8.88 ? 239 LYS A O 1 ATOM 1224 C CB . LYS A 1 153 ? 28.295 14.316 32.656 1.00 9.23 ? 239 LYS A CB 1 ATOM 1225 C CG . LYS A 1 153 ? 27.832 15.783 32.654 1.00 10.13 ? 239 LYS A CG 1 ATOM 1226 C CD . LYS A 1 153 ? 28.818 16.646 31.955 1.00 12.21 ? 239 LYS A CD 1 ATOM 1227 C CE . LYS A 1 153 ? 28.381 18.081 31.883 1.00 13.23 ? 239 LYS A CE 1 ATOM 1228 N NZ . LYS A 1 153 ? 29.439 18.931 31.239 1.00 17.28 ? 239 LYS A NZ 1 ATOM 1229 N N . CYS A 1 154 ? 25.734 12.443 32.089 1.00 7.76 ? 240 CYS A N 1 ATOM 1230 C CA . CYS A 1 154 ? 24.365 12.293 31.603 1.00 7.84 ? 240 CYS A CA 1 ATOM 1231 C C . CYS A 1 154 ? 23.448 11.695 32.650 1.00 7.87 ? 240 CYS A C 1 ATOM 1232 O O . CYS A 1 154 ? 22.331 12.190 32.889 1.00 8.11 ? 240 CYS A O 1 ATOM 1233 C CB . CYS A 1 154 ? 24.264 11.482 30.327 1.00 8.01 ? 240 CYS A CB 1 ATOM 1234 S SG . CYS A 1 154 ? 25.024 12.254 28.879 1.00 9.11 ? 240 CYS A SG 1 ATOM 1235 N N . SER A 1 155 ? 23.886 10.620 33.319 1.00 8.20 ? 241 SER A N 1 ATOM 1236 C CA . SER A 1 155 ? 23.043 10.056 34.349 1.00 9.59 ? 241 SER A CA 1 ATOM 1237 C C . SER A 1 155 ? 22.815 11.059 35.469 1.00 8.54 ? 241 SER A C 1 ATOM 1238 O O . SER A 1 155 ? 21.691 11.142 36.015 1.00 10.23 ? 241 SER A O 1 ATOM 1239 C CB . SER A 1 155 ? 23.658 8.808 34.891 1.00 10.79 ? 241 SER A CB 1 ATOM 1240 O OG . SER A 1 155 ? 22.778 8.328 35.947 1.00 14.36 ? 241 SER A OG 1 ATOM 1241 N N . GLY A 1 156 ? 23.806 11.824 35.824 1.00 8.34 ? 242 GLY A N 1 ATOM 1242 C CA . GLY A 1 156 ? 23.698 12.827 36.863 1.00 9.09 ? 242 GLY A CA 1 ATOM 1243 C C . GLY A 1 156 ? 22.812 14.011 36.468 1.00 9.05 ? 242 GLY A C 1 ATOM 1244 O O . GLY A 1 156 ? 22.238 14.624 37.374 1.00 10.59 ? 242 GLY A O 1 ATOM 1245 N N . ALA A 1 157 ? 22.684 14.286 35.181 1.00 8.34 ? 243 ALA A N 1 ATOM 1246 C CA . ALA A 1 157 ? 21.885 15.375 34.653 1.00 8.25 ? 243 ALA A CA 1 ATOM 1247 C C . ALA A 1 157 ? 20.468 14.960 34.259 1.00 7.54 ? 243 ALA A C 1 ATOM 1248 O O . ALA A 1 157 ? 19.640 15.852 34.010 1.00 8.03 ? 243 ALA A O 1 ATOM 1249 C CB . ALA A 1 157 ? 22.552 16.047 33.465 1.00 9.48 ? 243 ALA A CB 1 ATOM 1250 N N . ALA A 1 158 ? 20.171 13.697 34.184 1.00 7.84 ? 244 ALA A N 1 ATOM 1251 C CA . ALA A 1 158 ? 18.945 13.230 33.528 1.00 7.65 ? 244 ALA A CA 1 ATOM 1252 C C . ALA A 1 158 ? 17.710 13.842 34.207 1.00 7.61 ? 244 ALA A C 1 ATOM 1253 O O . ALA A 1 158 ? 16.799 14.284 33.494 1.00 7.94 ? 244 ALA A O 1 ATOM 1254 C CB . ALA A 1 158 ? 18.900 11.735 33.525 1.00 8.94 ? 244 ALA A CB 1 ATOM 1255 N N . SER A 1 159 ? 17.615 13.792 35.514 1.00 7.97 ? 245 SER A N 1 ATOM 1256 C CA . SER A 1 159 ? 16.432 14.296 36.180 1.00 8.17 ? 245 SER A CA 1 ATOM 1257 C C . SER A 1 159 ? 16.284 15.791 35.949 1.00 7.80 ? 245 SER A C 1 ATOM 1258 O O . SER A 1 159 ? 15.151 16.296 35.855 1.00 8.84 ? 245 SER A O 1 ATOM 1259 C CB . SER A 1 159 ? 16.399 13.950 37.670 1.00 10.43 ? 245 SER A CB 1 ATOM 1260 O OG . SER A 1 159 ? 17.423 14.543 38.368 1.00 11.95 ? 245 SER A OG 1 ATOM 1261 N N . THR A 1 160 ? 17.385 16.496 35.867 1.00 7.95 ? 246 THR A N 1 ATOM 1262 C CA . THR A 1 160 ? 17.403 17.919 35.601 1.00 7.65 ? 246 THR A CA 1 ATOM 1263 C C . THR A 1 160 ? 16.972 18.197 34.160 1.00 7.23 ? 246 THR A C 1 ATOM 1264 O O . THR A 1 160 ? 16.135 19.094 33.932 1.00 7.78 ? 246 THR A O 1 ATOM 1265 C CB . THR A 1 160 ? 18.799 18.469 35.907 1.00 8.34 ? 246 THR A CB 1 ATOM 1266 O OG1 . THR A 1 160 ? 19.087 18.332 37.299 1.00 9.78 ? 246 THR A OG1 1 ATOM 1267 C CG2 . THR A 1 160 ? 18.846 19.954 35.557 1.00 10.55 ? 246 THR A CG2 1 ATOM 1268 N N . TYR A 1 161 ? 17.510 17.485 33.181 1.00 7.13 ? 247 TYR A N 1 ATOM 1269 C CA . TYR A 1 161 ? 17.063 17.660 31.813 1.00 7.40 ? 247 TYR A CA 1 ATOM 1270 C C . TYR A 1 161 ? 15.565 17.435 31.733 1.00 6.76 ? 247 TYR A C 1 ATOM 1271 O O . TYR A 1 161 ? 14.841 18.199 31.095 1.00 7.43 ? 247 TYR A O 1 ATOM 1272 C CB . TYR A 1 161 ? 17.763 16.706 30.851 1.00 7.13 ? 247 TYR A CB 1 ATOM 1273 C CG . TYR A 1 161 ? 19.181 17.038 30.403 1.00 6.64 ? 247 TYR A CG 1 ATOM 1274 C CD1 . TYR A 1 161 ? 19.991 17.978 31.014 1.00 6.78 ? 247 TYR A CD1 1 ATOM 1275 C CD2 . TYR A 1 161 ? 19.686 16.370 29.317 1.00 6.99 ? 247 TYR A CD2 1 ATOM 1276 C CE1 . TYR A 1 161 ? 21.295 18.192 30.558 1.00 7.12 ? 247 TYR A CE1 1 ATOM 1277 C CE2 . TYR A 1 161 ? 20.971 16.542 28.867 1.00 7.30 ? 247 TYR A CE2 1 ATOM 1278 C CZ . TYR A 1 161 ? 21.785 17.463 29.503 1.00 7.36 ? 247 TYR A CZ 1 ATOM 1279 O OH . TYR A 1 161 ? 23.087 17.605 29.053 1.00 7.94 ? 247 TYR A OH 1 ATOM 1280 N N . ARG A 1 162 ? 15.071 16.387 32.347 1.00 6.89 ? 248 ARG A N 1 ATOM 1281 C CA . ARG A 1 162 ? 13.642 16.110 32.280 1.00 7.77 ? 248 ARG A CA 1 ATOM 1282 C C . ARG A 1 162 ? 12.821 17.192 32.931 1.00 7.57 ? 248 ARG A C 1 ATOM 1283 O O . ARG A 1 162 ? 11.837 17.701 32.345 1.00 8.30 ? 248 ARG A O 1 ATOM 1284 C CB A ARG A 1 162 ? 13.370 14.728 32.862 0.57 8.34 ? 248 ARG A CB 1 ATOM 1285 C CB B ARG A 1 162 ? 13.327 14.761 32.921 0.43 8.81 ? 248 ARG A CB 1 ATOM 1286 C CG A ARG A 1 162 ? 13.972 13.566 32.024 0.57 9.33 ? 248 ARG A CG 1 ATOM 1287 C CG B ARG A 1 162 ? 11.867 14.578 33.264 0.43 10.39 ? 248 ARG A CG 1 ATOM 1288 C CD A ARG A 1 162 ? 13.765 12.235 32.639 0.57 12.55 ? 248 ARG A CD 1 ATOM 1289 C CD B ARG A 1 162 ? 11.501 13.233 33.853 0.43 12.29 ? 248 ARG A CD 1 ATOM 1290 N NE A ARG A 1 162 ? 12.403 11.822 32.521 0.57 15.94 ? 248 ARG A NE 1 ATOM 1291 N NE B ARG A 1 162 ? 10.068 13.138 33.990 0.43 10.68 ? 248 ARG A NE 1 ATOM 1292 C CZ A ARG A 1 162 ? 11.987 10.594 32.181 0.57 15.44 ? 248 ARG A CZ 1 ATOM 1293 C CZ B ARG A 1 162 ? 9.374 13.592 35.043 0.43 12.22 ? 248 ARG A CZ 1 ATOM 1294 N NH1 A ARG A 1 162 ? 12.868 9.632 31.938 0.57 16.96 ? 248 ARG A NH1 1 ATOM 1295 N NH1 B ARG A 1 162 ? 10.014 14.164 36.064 0.43 15.73 ? 248 ARG A NH1 1 ATOM 1296 N NH2 A ARG A 1 162 ? 10.673 10.304 32.085 0.57 18.54 ? 248 ARG A NH2 1 ATOM 1297 N NH2 B ARG A 1 162 ? 8.045 13.509 35.065 0.43 12.79 ? 248 ARG A NH2 1 ATOM 1298 N N . GLU A 1 163 ? 13.135 17.545 34.166 1.00 7.84 ? 249 GLU A N 1 ATOM 1299 C CA . GLU A 1 163 ? 12.340 18.535 34.875 1.00 8.38 ? 249 GLU A CA 1 ATOM 1300 C C . GLU A 1 163 ? 12.373 19.880 34.199 1.00 7.39 ? 249 GLU A C 1 ATOM 1301 O O . GLU A 1 163 ? 11.365 20.566 34.122 1.00 7.91 ? 249 GLU A O 1 ATOM 1302 C CB . GLU A 1 163 ? 12.809 18.579 36.317 1.00 10.66 ? 249 GLU A CB 1 ATOM 1303 C CG . GLU A 1 163 ? 12.418 17.295 37.080 1.00 16.55 ? 249 GLU A CG 1 ATOM 1304 C CD . GLU A 1 163 ? 13.154 17.160 38.421 1.00 21.83 ? 249 GLU A CD 1 ATOM 1305 O OE1 . GLU A 1 163 ? 13.827 18.131 38.859 1.00 26.76 ? 249 GLU A OE1 1 ATOM 1306 O OE2 . GLU A 1 163 ? 12.987 16.064 39.059 1.00 26.92 ? 249 GLU A OE2 1 ATOM 1307 N N . LEU A 1 164 ? 13.537 20.299 33.735 1.00 7.55 ? 250 LEU A N 1 ATOM 1308 C CA . LEU A 1 164 ? 13.647 21.586 33.091 1.00 7.69 ? 250 LEU A CA 1 ATOM 1309 C C . LEU A 1 164 ? 13.037 21.612 31.704 1.00 7.68 ? 250 LEU A C 1 ATOM 1310 O O . LEU A 1 164 ? 12.534 22.671 31.281 1.00 8.07 ? 250 LEU A O 1 ATOM 1311 C CB . LEU A 1 164 ? 15.101 22.051 33.057 1.00 7.31 ? 250 LEU A CB 1 ATOM 1312 C CG . LEU A 1 164 ? 15.709 22.361 34.429 1.00 8.07 ? 250 LEU A CG 1 ATOM 1313 C CD1 . LEU A 1 164 ? 17.152 22.825 34.258 1.00 8.49 ? 250 LEU A CD1 1 ATOM 1314 C CD2 . LEU A 1 164 ? 14.906 23.413 35.197 1.00 9.35 ? 250 LEU A CD2 1 ATOM 1315 N N . THR A 1 165 ? 13.003 20.502 31.002 1.00 7.56 ? 251 THR A N 1 ATOM 1316 C CA . THR A 1 165 ? 12.275 20.419 29.731 1.00 6.97 ? 251 THR A CA 1 ATOM 1317 C C . THR A 1 165 ? 10.787 20.606 29.993 1.00 6.73 ? 251 THR A C 1 ATOM 1318 O O . THR A 1 165 ? 10.133 21.410 29.324 1.00 7.33 ? 251 THR A O 1 ATOM 1319 C CB . THR A 1 165 ? 12.535 19.127 29.010 1.00 7.34 ? 251 THR A CB 1 ATOM 1320 O OG1 . THR A 1 165 ? 13.934 19.008 28.721 1.00 9.68 ? 251 THR A OG1 1 ATOM 1321 C CG2 . THR A 1 165 ? 11.805 19.089 27.666 1.00 8.58 ? 251 THR A CG2 1 ATOM 1322 N N . ILE A 1 166 ? 10.243 19.883 30.990 1.00 6.71 ? 252 ILE A N 1 ATOM 1323 C CA . ILE A 1 166 ? 8.827 20.026 31.320 1.00 7.43 ? 252 ILE A CA 1 ATOM 1324 C C . ILE A 1 166 ? 8.551 21.503 31.725 1.00 7.57 ? 252 ILE A C 1 ATOM 1325 O O . ILE A 1 166 ? 7.542 22.077 31.310 1.00 8.19 ? 252 ILE A O 1 ATOM 1326 C CB . ILE A 1 166 ? 8.451 19.034 32.424 1.00 7.94 ? 252 ILE A CB 1 ATOM 1327 C CG1 . ILE A 1 166 ? 8.479 17.597 31.858 1.00 9.90 ? 252 ILE A CG1 1 ATOM 1328 C CG2 . ILE A 1 166 ? 7.061 19.360 32.995 1.00 8.80 ? 252 ILE A CG2 1 ATOM 1329 C CD1 . ILE A 1 166 ? 8.465 16.507 32.901 1.00 11.25 ? 252 ILE A CD1 1 ATOM 1330 N N . TYR A 1 167 ? 9.460 22.127 32.495 1.00 7.50 ? 253 TYR A N 1 ATOM 1331 C CA . TYR A 1 167 ? 9.297 23.502 32.884 1.00 7.99 ? 253 TYR A CA 1 ATOM 1332 C C . TYR A 1 167 ? 9.189 24.392 31.647 1.00 7.55 ? 253 TYR A C 1 ATOM 1333 O O . TYR A 1 167 ? 8.309 25.267 31.569 1.00 8.31 ? 253 TYR A O 1 ATOM 1334 C CB . TYR A 1 167 ? 10.489 23.928 33.773 1.00 9.07 ? 253 TYR A CB 1 ATOM 1335 C CG . TYR A 1 167 ? 10.321 25.278 34.404 1.00 8.56 ? 253 TYR A CG 1 ATOM 1336 C CD1 . TYR A 1 167 ? 9.569 25.431 35.532 1.00 11.10 ? 253 TYR A CD1 1 ATOM 1337 C CD2 . TYR A 1 167 ? 10.916 26.413 33.882 1.00 8.54 ? 253 TYR A CD2 1 ATOM 1338 C CE1 . TYR A 1 167 ? 9.397 26.696 36.134 1.00 13.05 ? 253 TYR A CE1 1 ATOM 1339 C CE2 . TYR A 1 167 ? 10.728 27.667 34.472 1.00 9.44 ? 253 TYR A CE2 1 ATOM 1340 C CZ . TYR A 1 167 ? 9.999 27.774 35.587 1.00 9.75 ? 253 TYR A CZ 1 ATOM 1341 O OH . TYR A 1 167 ? 9.795 28.995 36.228 1.00 11.95 ? 253 TYR A OH 1 ATOM 1342 N N . ALA A 1 168 ? 10.081 24.215 30.681 1.00 7.41 ? 254 ALA A N 1 ATOM 1343 C CA . ALA A 1 168 ? 10.041 25.014 29.458 1.00 7.72 ? 254 ALA A CA 1 ATOM 1344 C C . ALA A 1 168 ? 8.764 24.771 28.678 1.00 7.04 ? 254 ALA A C 1 ATOM 1345 O O . ALA A 1 168 ? 8.135 25.713 28.166 1.00 7.36 ? 254 ALA A O 1 ATOM 1346 C CB . ALA A 1 168 ? 11.257 24.735 28.576 1.00 8.18 ? 254 ALA A CB 1 ATOM 1347 N N . LEU A 1 169 ? 8.350 23.525 28.535 1.00 6.62 ? 255 LEU A N 1 ATOM 1348 C CA . LEU A 1 169 ? 7.140 23.199 27.772 1.00 6.95 ? 255 LEU A CA 1 ATOM 1349 C C . LEU A 1 169 ? 5.927 23.877 28.378 1.00 6.71 ? 255 LEU A C 1 ATOM 1350 O O . LEU A 1 169 ? 5.025 24.311 27.646 1.00 9.00 ? 255 LEU A O 1 ATOM 1351 C CB . LEU A 1 169 ? 6.914 21.697 27.668 1.00 7.19 ? 255 LEU A CB 1 ATOM 1352 C CG . LEU A 1 169 ? 7.974 20.856 26.952 1.00 8.26 ? 255 LEU A CG 1 ATOM 1353 C CD1 . LEU A 1 169 ? 7.517 19.423 26.900 1.00 10.53 ? 255 LEU A CD1 1 ATOM 1354 C CD2 . LEU A 1 169 ? 8.340 21.357 25.585 1.00 9.76 ? 255 LEU A CD2 1 ATOM 1355 N N . LYS A 1 170 ? 5.846 23.911 29.693 1.00 6.94 ? 256 LYS A N 1 ATOM 1356 C CA . LYS A 1 170 ? 4.704 24.545 30.353 1.00 7.64 ? 256 LYS A CA 1 ATOM 1357 C C . LYS A 1 170 ? 4.777 26.065 30.337 1.00 6.82 ? 256 LYS A C 1 ATOM 1358 O O . LYS A 1 170 ? 3.793 26.763 30.097 1.00 8.40 ? 256 LYS A O 1 ATOM 1359 C CB . LYS A 1 170 ? 4.591 24.032 31.789 1.00 8.57 ? 256 LYS A CB 1 ATOM 1360 C CG . LYS A 1 170 ? 4.140 22.579 31.888 1.00 10.22 ? 256 LYS A CG 1 ATOM 1361 C CD . LYS A 1 170 ? 3.982 22.162 33.368 1.00 14.20 ? 256 LYS A CD 1 ATOM 1362 C CE . LYS A 1 170 ? 3.332 20.817 33.561 1.00 17.08 ? 256 LYS A CE 1 ATOM 1363 N NZ . LYS A 1 170 ? 2.860 20.720 34.967 1.00 22.57 ? 256 LYS A NZ 1 ATOM 1364 N N . GLN A 1 171 ? 5.959 26.610 30.635 1.00 7.14 ? 257 GLN A N 1 ATOM 1365 C CA . GLN A 1 171 ? 6.088 28.071 30.718 1.00 6.94 ? 257 GLN A CA 1 ATOM 1366 C C . GLN A 1 171 ? 5.973 28.733 29.352 1.00 6.88 ? 257 GLN A C 1 ATOM 1367 O O . GLN A 1 171 ? 5.560 29.890 29.246 1.00 8.57 ? 257 GLN A O 1 ATOM 1368 C CB . GLN A 1 171 ? 7.425 28.431 31.357 1.00 7.05 ? 257 GLN A CB 1 ATOM 1369 C CG . GLN A 1 171 ? 7.511 28.112 32.823 1.00 8.89 ? 257 GLN A CG 1 ATOM 1370 C CD . GLN A 1 171 ? 6.396 28.711 33.644 1.00 13.58 ? 257 GLN A CD 1 ATOM 1371 O OE1 . GLN A 1 171 ? 6.047 29.838 33.539 1.00 16.71 ? 257 GLN A OE1 1 ATOM 1372 N NE2 . GLN A 1 171 ? 5.752 27.854 34.400 1.00 21.07 ? 257 GLN A NE2 1 ATOM 1373 N N . LEU A 1 172 ? 6.353 28.038 28.274 1.00 6.64 ? 258 LEU A N 1 ATOM 1374 C CA . LEU A 1 172 ? 6.319 28.597 26.928 1.00 6.66 ? 258 LEU A CA 1 ATOM 1375 C C . LEU A 1 172 ? 5.086 28.135 26.144 1.00 6.76 ? 258 LEU A C 1 ATOM 1376 O O . LEU A 1 172 ? 4.973 28.422 24.946 1.00 7.19 ? 258 LEU A O 1 ATOM 1377 C CB . LEU A 1 172 ? 7.627 28.352 26.190 1.00 7.20 ? 258 LEU A CB 1 ATOM 1378 C CG . LEU A 1 172 ? 8.879 28.801 26.923 1.00 7.36 ? 258 LEU A CG 1 ATOM 1379 C CD1 . LEU A 1 172 ? 10.144 28.505 26.141 1.00 9.10 ? 258 LEU A CD1 1 ATOM 1380 C CD2 . LEU A 1 172 ? 8.842 30.277 27.339 1.00 8.90 ? 258 LEU A CD2 1 ATOM 1381 N N . ASP A 1 173 ? 4.155 27.479 26.817 1.00 6.91 ? 259 ASP A N 1 ATOM 1382 C CA . ASP A 1 173 ? 2.886 27.049 26.219 1.00 7.23 ? 259 ASP A CA 1 ATOM 1383 C C . ASP A 1 173 ? 1.970 28.233 26.120 1.00 7.05 ? 259 ASP A C 1 ATOM 1384 O O . ASP A 1 173 ? 1.093 28.454 26.982 1.00 8.87 ? 259 ASP A O 1 ATOM 1385 C CB . ASP A 1 173 ? 2.279 25.960 27.062 1.00 7.36 ? 259 ASP A CB 1 ATOM 1386 C CG . ASP A 1 173 ? 0.953 25.473 26.529 1.00 7.83 ? 259 ASP A CG 1 ATOM 1387 O OD1 . ASP A 1 173 ? 0.732 25.529 25.292 1.00 7.54 ? 259 ASP A OD1 1 ATOM 1388 O OD2 . ASP A 1 173 ? 0.109 25.035 27.372 1.00 8.97 ? 259 ASP A OD2 1 ATOM 1389 N N . LEU A 1 174 ? 2.147 29.049 25.089 1.00 6.93 ? 260 LEU A N 1 ATOM 1390 C CA . LEU A 1 174 ? 1.424 30.271 24.826 1.00 7.09 ? 260 LEU A CA 1 ATOM 1391 C C . LEU A 1 174 ? 0.723 30.151 23.504 1.00 6.44 ? 260 LEU A C 1 ATOM 1392 O O . LEU A 1 174 ? 1.229 29.524 22.563 1.00 6.83 ? 260 LEU A O 1 ATOM 1393 C CB . LEU A 1 174 ? 2.374 31.467 24.814 1.00 7.66 ? 260 LEU A CB 1 ATOM 1394 C CG . LEU A 1 174 ? 3.209 31.690 26.054 1.00 7.72 ? 260 LEU A CG 1 ATOM 1395 C CD1 . LEU A 1 174 ? 4.333 32.682 25.843 1.00 9.74 ? 260 LEU A CD1 1 ATOM 1396 C CD2 . LEU A 1 174 ? 2.339 32.111 27.239 1.00 8.24 ? 260 LEU A CD2 1 ATOM 1397 N N . PRO A 1 175 ? -0.446 30.787 23.354 1.00 6.37 ? 261 PRO A N 1 ATOM 1398 C CA . PRO A 1 175 ? -1.216 30.608 22.113 1.00 6.52 ? 261 PRO A CA 1 ATOM 1399 C C . PRO A 1 175 ? -0.544 30.990 20.830 1.00 6.23 ? 261 PRO A C 1 ATOM 1400 O O . PRO A 1 175 ? -0.896 30.459 19.773 1.00 7.64 ? 261 PRO A O 1 ATOM 1401 C CB . PRO A 1 175 ? -2.479 31.436 22.380 1.00 7.95 ? 261 PRO A CB 1 ATOM 1402 C CG . PRO A 1 175 ? -2.678 31.312 23.838 1.00 8.97 ? 261 PRO A CG 1 ATOM 1403 C CD . PRO A 1 175 ? -1.282 31.392 24.435 1.00 8.02 ? 261 PRO A CD 1 ATOM 1404 N N . HIS A 1 176 ? 0.441 31.902 20.844 1.00 6.47 ? 262 HIS A N 1 ATOM 1405 C CA . HIS A 1 176 ? 1.131 32.324 19.623 1.00 6.65 ? 262 HIS A CA 1 ATOM 1406 C C . HIS A 1 176 ? 2.416 31.557 19.366 1.00 6.39 ? 262 HIS A C 1 ATOM 1407 O O . HIS A 1 176 ? 3.133 31.863 18.412 1.00 6.65 ? 262 HIS A O 1 ATOM 1408 C CB . HIS A 1 176 ? 1.419 33.819 19.652 1.00 6.72 ? 262 HIS A CB 1 ATOM 1409 C CG . HIS A 1 176 ? 2.498 34.217 20.608 1.00 6.49 ? 262 HIS A CG 1 ATOM 1410 N ND1 . HIS A 1 176 ? 2.344 34.183 21.978 1.00 7.07 ? 262 HIS A ND1 1 ATOM 1411 C CD2 . HIS A 1 176 ? 3.752 34.665 20.324 1.00 6.23 ? 262 HIS A CD2 1 ATOM 1412 C CE1 . HIS A 1 176 ? 3.488 34.628 22.490 1.00 6.88 ? 262 HIS A CE1 1 ATOM 1413 N NE2 . HIS A 1 176 ? 4.348 34.927 21.528 1.00 6.46 ? 262 HIS A NE2 1 ATOM 1414 N N . VAL A 1 177 ? 2.693 30.550 20.195 1.00 6.14 ? 263 VAL A N 1 ATOM 1415 C CA . VAL A 1 177 ? 3.924 29.769 20.138 1.00 6.03 ? 263 VAL A CA 1 ATOM 1416 C C . VAL A 1 177 ? 3.642 28.360 19.650 1.00 5.92 ? 263 VAL A C 1 ATOM 1417 O O . VAL A 1 177 ? 2.608 27.760 19.971 1.00 6.52 ? 263 VAL A O 1 ATOM 1418 C CB . VAL A 1 177 ? 4.583 29.778 21.552 1.00 6.35 ? 263 VAL A CB 1 ATOM 1419 C CG1 . VAL A 1 177 ? 5.752 28.789 21.656 1.00 7.36 ? 263 VAL A CG1 1 ATOM 1420 C CG2 . VAL A 1 177 ? 5.024 31.196 21.903 1.00 7.78 ? 263 VAL A CG2 1 ATOM 1421 N N . ALA A 1 178 ? 4.632 27.806 18.950 1.00 5.91 ? 264 ALA A N 1 ATOM 1422 C CA . ALA A 1 178 ? 4.729 26.374 18.676 1.00 5.89 ? 264 ALA A CA 1 ATOM 1423 C C . ALA A 1 178 ? 6.071 25.866 19.161 1.00 6.30 ? 264 ALA A C 1 ATOM 1424 O O . ALA A 1 178 ? 7.072 26.594 19.068 1.00 7.08 ? 264 ALA A O 1 ATOM 1425 C CB . ALA A 1 178 ? 4.608 26.064 17.200 1.00 6.56 ? 264 ALA A CB 1 ATOM 1426 N N . MET A 1 179 ? 6.116 24.646 19.681 1.00 5.92 ? 265 MET A N 1 ATOM 1427 C CA . MET A 1 179 ? 7.339 24.004 20.132 1.00 6.00 ? 265 MET A CA 1 ATOM 1428 C C . MET A 1 179 ? 7.523 22.636 19.488 1.00 5.39 ? 265 MET A C 1 ATOM 1429 O O . MET A 1 179 ? 6.588 21.839 19.371 1.00 6.31 ? 265 MET A O 1 ATOM 1430 C CB . MET A 1 179 ? 7.366 23.801 21.666 1.00 6.10 ? 265 MET A CB 1 ATOM 1431 C CG . MET A 1 179 ? 7.638 25.099 22.421 1.00 6.50 ? 265 MET A CG 1 ATOM 1432 S SD . MET A 1 179 ? 7.559 24.963 24.198 1.00 6.64 ? 265 MET A SD 1 ATOM 1433 C CE . MET A 1 179 ? 5.767 25.046 24.422 1.00 7.68 ? 265 MET A CE 1 ATOM 1434 N N . TYR A 1 180 ? 8.788 22.374 19.159 1.00 5.42 ? 266 TYR A N 1 ATOM 1435 C CA . TYR A 1 180 ? 9.258 21.094 18.672 1.00 5.71 ? 266 TYR A CA 1 ATOM 1436 C C . TYR A 1 180 ? 10.454 20.687 19.561 1.00 5.48 ? 266 TYR A C 1 ATOM 1437 O O . TYR A 1 180 ? 11.438 21.415 19.586 1.00 6.09 ? 266 TYR A O 1 ATOM 1438 C CB . TYR A 1 180 ? 9.686 21.162 17.212 1.00 5.83 ? 266 TYR A CB 1 ATOM 1439 C CG . TYR A 1 180 ? 8.554 21.541 16.262 1.00 5.70 ? 266 TYR A CG 1 ATOM 1440 C CD1 . TYR A 1 180 ? 8.235 22.873 16.054 1.00 6.23 ? 266 TYR A CD1 1 ATOM 1441 C CD2 . TYR A 1 180 ? 7.825 20.579 15.573 1.00 6.09 ? 266 TYR A CD2 1 ATOM 1442 C CE1 . TYR A 1 180 ? 7.206 23.242 15.209 1.00 6.55 ? 266 TYR A CE1 1 ATOM 1443 C CE2 . TYR A 1 180 ? 6.801 20.952 14.707 1.00 5.92 ? 266 TYR A CE2 1 ATOM 1444 C CZ . TYR A 1 180 ? 6.477 22.264 14.531 1.00 6.09 ? 266 TYR A CZ 1 ATOM 1445 O OH . TYR A 1 180 ? 5.502 22.696 13.689 1.00 6.84 ? 266 TYR A OH 1 ATOM 1446 N N . MET A 1 181 ? 10.352 19.589 20.291 1.00 5.57 ? 267 MET A N 1 ATOM 1447 C CA . MET A 1 181 ? 11.496 19.110 21.063 1.00 5.93 ? 267 MET A CA 1 ATOM 1448 C C . MET A 1 181 ? 12.507 18.472 20.141 1.00 5.37 ? 267 MET A C 1 ATOM 1449 O O . MET A 1 181 ? 12.148 17.732 19.232 1.00 5.73 ? 267 MET A O 1 ATOM 1450 C CB . MET A 1 181 ? 11.093 18.074 22.133 1.00 6.18 ? 267 MET A CB 1 ATOM 1451 C CG . MET A 1 181 ? 10.350 18.632 23.331 1.00 6.63 ? 267 MET A CG 1 ATOM 1452 S SD . MET A 1 181 ? 9.915 17.381 24.537 1.00 7.53 ? 267 MET A SD 1 ATOM 1453 C CE . MET A 1 181 ? 8.478 16.666 23.749 1.00 10.03 ? 267 MET A CE 1 ATOM 1454 N N . ASP A 1 182 ? 13.805 18.687 20.375 1.00 5.66 ? 268 ASP A N 1 ATOM 1455 C CA . ASP A 1 182 ? 14.814 17.980 19.631 1.00 5.90 ? 268 ASP A CA 1 ATOM 1456 C C . ASP A 1 182 ? 14.644 16.471 19.805 1.00 5.23 ? 268 ASP A C 1 ATOM 1457 O O . ASP A 1 182 ? 14.452 15.975 20.919 1.00 6.13 ? 268 ASP A O 1 ATOM 1458 C CB . ASP A 1 182 ? 16.194 18.391 20.105 1.00 5.96 ? 268 ASP A CB 1 ATOM 1459 C CG . ASP A 1 182 ? 17.283 17.707 19.295 1.00 5.62 ? 268 ASP A CG 1 ATOM 1460 O OD1 . ASP A 1 182 ? 17.619 18.272 18.235 1.00 7.53 ? 268 ASP A OD1 1 ATOM 1461 O OD2 . ASP A 1 182 ? 17.735 16.633 19.704 1.00 6.58 ? 268 ASP A OD2 1 ATOM 1462 N N . ALA A 1 183 ? 14.835 15.738 18.704 1.00 5.39 ? 269 ALA A N 1 ATOM 1463 C CA . ALA A 1 183 ? 14.811 14.276 18.761 1.00 5.85 ? 269 ALA A CA 1 ATOM 1464 C C . ALA A 1 183 ? 15.940 13.677 17.942 1.00 5.46 ? 269 ALA A C 1 ATOM 1465 O O . ALA A 1 183 ? 15.765 12.689 17.233 1.00 6.45 ? 269 ALA A O 1 ATOM 1466 C CB . ALA A 1 183 ? 13.453 13.713 18.400 1.00 6.44 ? 269 ALA A CB 1 ATOM 1467 N N . GLY A 1 184 ? 17.135 14.241 18.054 1.00 5.83 ? 270 GLY A N 1 ATOM 1468 C CA . GLY A 1 184 ? 18.254 13.613 17.387 1.00 6.02 ? 270 GLY A CA 1 ATOM 1469 C C . GLY A 1 184 ? 18.062 13.520 15.887 1.00 5.45 ? 270 GLY A C 1 ATOM 1470 O O . GLY A 1 184 ? 17.494 14.398 15.252 1.00 6.03 ? 270 GLY A O 1 ATOM 1471 N N . HIS A 1 185 ? 18.523 12.428 15.296 1.00 5.93 ? 271 HIS A N 1 ATOM 1472 C CA . HIS A 1 185 ? 18.485 12.220 13.850 1.00 6.06 ? 271 HIS A CA 1 ATOM 1473 C C . HIS A 1 185 ? 18.458 10.725 13.562 1.00 5.66 ? 271 HIS A C 1 ATOM 1474 O O . HIS A 1 185 ? 18.640 9.916 14.493 1.00 6.26 ? 271 HIS A O 1 ATOM 1475 C CB . HIS A 1 185 ? 19.643 12.973 13.163 1.00 6.22 ? 271 HIS A CB 1 ATOM 1476 C CG . HIS A 1 185 ? 21.004 12.410 13.431 1.00 6.50 ? 271 HIS A CG 1 ATOM 1477 N ND1 . HIS A 1 185 ? 21.599 11.482 12.599 1.00 6.86 ? 271 HIS A ND1 1 ATOM 1478 C CD2 . HIS A 1 185 ? 21.884 12.721 14.414 1.00 7.29 ? 271 HIS A CD2 1 ATOM 1479 C CE1 . HIS A 1 185 ? 22.795 11.248 13.093 1.00 7.23 ? 271 HIS A CE1 1 ATOM 1480 N NE2 . HIS A 1 185 ? 23.023 11.989 14.188 1.00 7.86 ? 271 HIS A NE2 1 ATOM 1481 N N . ALA A 1 186 ? 18.290 10.387 12.310 1.00 5.91 ? 272 ALA A N 1 ATOM 1482 C CA . ALA A 1 186 ? 18.163 8.979 11.914 1.00 6.25 ? 272 ALA A CA 1 ATOM 1483 C C . ALA A 1 186 ? 19.339 8.126 12.371 1.00 6.27 ? 272 ALA A C 1 ATOM 1484 O O . ALA A 1 186 ? 19.138 6.941 12.702 1.00 7.37 ? 272 ALA A O 1 ATOM 1485 C CB . ALA A 1 186 ? 18.038 8.865 10.389 1.00 6.74 ? 272 ALA A CB 1 ATOM 1486 N N . GLY A 1 187 ? 20.537 8.703 12.375 1.00 6.22 ? 273 GLY A N 1 ATOM 1487 C CA . GLY A 1 187 ? 21.718 7.982 12.746 1.00 6.48 ? 273 GLY A CA 1 ATOM 1488 C C . GLY A 1 187 ? 22.060 8.015 14.195 1.00 6.70 ? 273 GLY A C 1 ATOM 1489 O O . GLY A 1 187 ? 23.122 7.501 14.612 1.00 7.71 ? 273 GLY A O 1 ATOM 1490 N N . TRP A 1 188 ? 21.160 8.543 15.042 1.00 6.64 ? 274 TRP A N 1 ATOM 1491 C CA . TRP A 1 188 ? 21.248 8.478 16.494 1.00 6.32 ? 274 TRP A CA 1 ATOM 1492 C C . TRP A 1 188 ? 20.060 7.678 17.000 1.00 6.77 ? 274 TRP A C 1 ATOM 1493 O O . TRP A 1 188 ? 20.192 6.495 17.316 1.00 8.42 ? 274 TRP A O 1 ATOM 1494 C CB . TRP A 1 188 ? 21.329 9.880 17.094 1.00 6.77 ? 274 TRP A CB 1 ATOM 1495 C CG . TRP A 1 188 ? 21.540 9.887 18.578 1.00 6.99 ? 274 TRP A CG 1 ATOM 1496 C CD1 . TRP A 1 188 ? 21.673 8.825 19.438 1.00 7.20 ? 274 TRP A CD1 1 ATOM 1497 C CD2 . TRP A 1 188 ? 21.698 11.047 19.389 1.00 7.00 ? 274 TRP A CD2 1 ATOM 1498 N NE1 . TRP A 1 188 ? 21.892 9.251 20.718 1.00 7.80 ? 274 TRP A NE1 1 ATOM 1499 C CE2 . TRP A 1 188 ? 21.927 10.609 20.718 1.00 7.37 ? 274 TRP A CE2 1 ATOM 1500 C CE3 . TRP A 1 188 ? 21.655 12.426 19.143 1.00 7.71 ? 274 TRP A CE3 1 ATOM 1501 C CZ2 . TRP A 1 188 ? 22.179 11.508 21.762 1.00 8.28 ? 274 TRP A CZ2 1 ATOM 1502 C CZ3 . TRP A 1 188 ? 21.900 13.293 20.183 1.00 9.19 ? 274 TRP A CZ3 1 ATOM 1503 C CH2 . TRP A 1 188 ? 22.148 12.824 21.473 1.00 8.91 ? 274 TRP A CH2 1 ATOM 1504 N N . LEU A 1 189 ? 18.888 8.271 17.061 1.00 6.89 ? 275 LEU A N 1 ATOM 1505 C CA . LEU A 1 189 ? 17.708 7.613 17.619 1.00 6.79 ? 275 LEU A CA 1 ATOM 1506 C C . LEU A 1 189 ? 16.964 6.735 16.614 1.00 7.46 ? 275 LEU A C 1 ATOM 1507 O O . LEU A 1 189 ? 16.100 5.951 17.039 1.00 8.47 ? 275 LEU A O 1 ATOM 1508 C CB . LEU A 1 189 ? 16.751 8.651 18.228 1.00 7.28 ? 275 LEU A CB 1 ATOM 1509 C CG . LEU A 1 189 ? 17.379 9.506 19.312 1.00 7.15 ? 275 LEU A CG 1 ATOM 1510 C CD1 . LEU A 1 189 ? 16.297 10.418 19.924 1.00 7.11 ? 275 LEU A CD1 1 ATOM 1511 C CD2 . LEU A 1 189 ? 18.055 8.700 20.411 1.00 8.17 ? 275 LEU A CD2 1 ATOM 1512 N N . GLY A 1 190 ? 17.279 6.844 15.315 1.00 7.18 ? 276 GLY A N 1 ATOM 1513 C CA . GLY A 1 190 ? 16.598 6.035 14.332 1.00 7.49 ? 276 GLY A CA 1 ATOM 1514 C C . GLY A 1 190 ? 17.119 4.645 14.162 1.00 7.83 ? 276 GLY A C 1 ATOM 1515 O O . GLY A 1 190 ? 16.462 3.818 13.504 1.00 9.28 ? 276 GLY A O 1 ATOM 1516 N N . TRP A 1 191 ? 18.254 4.295 14.737 1.00 7.50 ? 277 TRP A N 1 ATOM 1517 C CA . TRP A 1 191 ? 18.655 2.904 14.730 1.00 7.86 ? 277 TRP A CA 1 ATOM 1518 C C . TRP A 1 191 ? 17.578 2.052 15.351 1.00 8.49 ? 277 TRP A C 1 ATOM 1519 O O . TRP A 1 191 ? 17.014 2.453 16.410 1.00 8.71 ? 277 TRP A O 1 ATOM 1520 C CB . TRP A 1 191 ? 19.978 2.713 15.517 1.00 8.24 ? 277 TRP A CB 1 ATOM 1521 C CG . TRP A 1 191 ? 21.152 3.264 14.802 1.00 8.37 ? 277 TRP A CG 1 ATOM 1522 C CD1 . TRP A 1 191 ? 21.664 4.527 14.883 1.00 9.19 ? 277 TRP A CD1 1 ATOM 1523 C CD2 . TRP A 1 191 ? 21.951 2.558 13.844 1.00 8.05 ? 277 TRP A CD2 1 ATOM 1524 N NE1 . TRP A 1 191 ? 22.704 4.674 13.992 1.00 8.84 ? 277 TRP A NE1 1 ATOM 1525 C CE2 . TRP A 1 191 ? 22.912 3.471 13.357 1.00 8.67 ? 277 TRP A CE2 1 ATOM 1526 C CE3 . TRP A 1 191 ? 21.988 1.240 13.380 1.00 8.48 ? 277 TRP A CE3 1 ATOM 1527 C CZ2 . TRP A 1 191 ? 23.875 3.092 12.441 1.00 9.43 ? 277 TRP A CZ2 1 ATOM 1528 C CZ3 . TRP A 1 191 ? 22.974 0.874 12.463 1.00 9.55 ? 277 TRP A CZ3 1 ATOM 1529 C CH2 . TRP A 1 191 ? 23.882 1.798 12.019 1.00 9.48 ? 277 TRP A CH2 1 ATOM 1530 N N . PRO A 1 192 ? 17.304 0.873 14.806 1.00 9.59 ? 278 PRO A N 1 ATOM 1531 C CA . PRO A 1 192 ? 16.257 0.016 15.396 1.00 11.32 ? 278 PRO A CA 1 ATOM 1532 C C . PRO A 1 192 ? 16.377 -0.221 16.908 1.00 9.95 ? 278 PRO A C 1 ATOM 1533 O O . PRO A 1 192 ? 15.298 -0.323 17.576 1.00 13.11 ? 278 PRO A O 1 ATOM 1534 C CB . PRO A 1 192 ? 16.367 -1.287 14.574 1.00 13.08 ? 278 PRO A CB 1 ATOM 1535 C CG . PRO A 1 192 ? 16.824 -0.767 13.169 1.00 12.70 ? 278 PRO A CG 1 ATOM 1536 C CD . PRO A 1 192 ? 17.790 0.341 13.521 1.00 11.21 ? 278 PRO A CD 1 ATOM 1537 N N . ALA A 1 193 ? 17.509 -0.365 17.494 1.00 10.94 ? 279 ALA A N 1 ATOM 1538 C CA . ALA A 1 193 ? 17.586 -0.656 18.926 1.00 12.02 ? 279 ALA A CA 1 ATOM 1539 C C . ALA A 1 193 ? 17.190 0.558 19.766 1.00 11.52 ? 279 ALA A C 1 ATOM 1540 O O . ALA A 1 193 ? 16.892 0.419 20.979 1.00 12.93 ? 279 ALA A O 1 ATOM 1541 C CB . ALA A 1 193 ? 19.005 -1.060 19.315 1.00 13.86 ? 279 ALA A CB 1 ATOM 1542 N N . ASN A 1 194 ? 17.215 1.774 19.177 1.00 10.28 ? 280 ASN A N 1 ATOM 1543 C CA . ASN A 1 194 ? 16.992 3.016 19.941 1.00 9.38 ? 280 ASN A CA 1 ATOM 1544 C C . ASN A 1 194 ? 15.620 3.605 19.769 1.00 9.44 ? 280 ASN A C 1 ATOM 1545 O O . ASN A 1 194 ? 15.213 4.432 20.593 1.00 9.94 ? 280 ASN A O 1 ATOM 1546 C CB . ASN A 1 194 ? 18.024 4.052 19.516 1.00 9.22 ? 280 ASN A CB 1 ATOM 1547 C CG . ASN A 1 194 ? 19.435 3.634 19.791 1.00 9.10 ? 280 ASN A CG 1 ATOM 1548 O OD1 . ASN A 1 194 ? 19.670 2.802 20.708 1.00 11.81 ? 280 ASN A OD1 1 ATOM 1549 N ND2 . ASN A 1 194 ? 20.384 4.223 19.093 1.00 9.21 ? 280 ASN A ND2 1 ATOM 1550 N N . ILE A 1 195 ? 14.897 3.242 18.727 1.00 9.15 ? 281 ILE A N 1 ATOM 1551 C CA . ILE A 1 195 ? 13.773 4.009 18.325 1.00 8.95 ? 281 ILE A CA 1 ATOM 1552 C C . ILE A 1 195 ? 12.533 3.840 19.256 1.00 9.19 ? 281 ILE A C 1 ATOM 1553 O O . ILE A 1 195 ? 11.834 4.795 19.562 1.00 9.42 ? 281 ILE A O 1 ATOM 1554 C CB . ILE A 1 195 ? 13.474 3.743 16.844 1.00 9.92 ? 281 ILE A CB 1 ATOM 1555 C CG1 . ILE A 1 195 ? 12.555 4.791 16.262 1.00 9.84 ? 281 ILE A CG1 1 ATOM 1556 C CG2 . ILE A 1 195 ? 12.952 2.327 16.630 1.00 10.83 ? 281 ILE A CG2 1 ATOM 1557 C CD1 . ILE A 1 195 ? 12.384 4.672 14.767 1.00 9.74 ? 281 ILE A CD1 1 ATOM 1558 N N . GLN A 1 196 ? 12.256 2.625 19.752 1.00 10.24 ? 282 GLN A N 1 ATOM 1559 C CA . GLN A 1 196 ? 11.172 2.471 20.720 1.00 9.89 ? 282 GLN A CA 1 ATOM 1560 C C . GLN A 1 196 ? 11.477 3.104 22.093 1.00 9.62 ? 282 GLN A C 1 ATOM 1561 O O . GLN A 1 196 ? 10.626 3.817 22.632 1.00 8.62 ? 282 GLN A O 1 ATOM 1562 C CB . GLN A 1 196 ? 10.685 1.040 20.859 1.00 11.91 ? 282 GLN A CB 1 ATOM 1563 C CG . GLN A 1 196 ? 9.409 0.958 21.716 1.00 16.11 ? 282 GLN A CG 1 ATOM 1564 C CD . GLN A 1 196 ? 8.958 -0.440 21.927 1.00 24.44 ? 282 GLN A CD 1 ATOM 1565 O OE1 . GLN A 1 196 ? 8.699 -1.171 20.966 1.00 31.00 ? 282 GLN A OE1 1 ATOM 1566 N NE2 . GLN A 1 196 ? 8.835 -0.829 23.213 1.00 25.37 ? 282 GLN A NE2 1 ATOM 1567 N N . PRO A 1 197 ? 12.680 2.944 22.639 1.00 8.84 ? 283 PRO A N 1 ATOM 1568 C CA . PRO A 1 197 ? 13.027 3.692 23.871 1.00 8.98 ? 283 PRO A CA 1 ATOM 1569 C C . PRO A 1 197 ? 12.902 5.193 23.679 1.00 7.57 ? 283 PRO A C 1 ATOM 1570 O O . PRO A 1 197 ? 12.464 5.910 24.593 1.00 8.30 ? 283 PRO A O 1 ATOM 1571 C CB . PRO A 1 197 ? 14.436 3.235 24.212 1.00 10.89 ? 283 PRO A CB 1 ATOM 1572 C CG . PRO A 1 197 ? 14.616 1.923 23.519 1.00 13.28 ? 283 PRO A CG 1 ATOM 1573 C CD . PRO A 1 197 ? 13.720 1.930 22.341 1.00 10.06 ? 283 PRO A CD 1 ATOM 1574 N N . ALA A 1 198 ? 13.291 5.706 22.495 1.00 8.02 ? 284 ALA A N 1 ATOM 1575 C CA . ALA A 1 198 ? 13.112 7.126 22.241 1.00 7.45 ? 284 ALA A CA 1 ATOM 1576 C C . ALA A 1 198 ? 11.655 7.539 22.233 1.00 7.00 ? 284 ALA A C 1 ATOM 1577 O O . ALA A 1 198 ? 11.268 8.538 22.823 1.00 7.37 ? 284 ALA A O 1 ATOM 1578 C CB . ALA A 1 198 ? 13.761 7.478 20.906 1.00 7.93 ? 284 ALA A CB 1 ATOM 1579 N N . ALA A 1 199 ? 10.815 6.720 21.589 1.00 7.32 ? 285 ALA A N 1 ATOM 1580 C CA . ALA A 1 199 ? 9.385 7.027 21.560 1.00 7.36 ? 285 ALA A CA 1 ATOM 1581 C C . ALA A 1 199 ? 8.818 7.036 22.982 1.00 6.90 ? 285 ALA A C 1 ATOM 1582 O O . ALA A 1 199 ? 7.999 7.903 23.318 1.00 7.67 ? 285 ALA A O 1 ATOM 1583 C CB . ALA A 1 199 ? 8.649 6.035 20.689 1.00 7.92 ? 285 ALA A CB 1 ATOM 1584 N N . GLU A 1 200 ? 9.179 6.051 23.795 1.00 7.46 ? 286 GLU A N 1 ATOM 1585 C CA . GLU A 1 200 ? 8.709 5.981 25.172 1.00 7.94 ? 286 GLU A CA 1 ATOM 1586 C C . GLU A 1 200 ? 9.096 7.238 25.936 1.00 7.06 ? 286 GLU A C 1 ATOM 1587 O O . GLU A 1 200 ? 8.276 7.807 26.675 1.00 7.97 ? 286 GLU A O 1 ATOM 1588 C CB . GLU A 1 200 ? 9.243 4.729 25.866 1.00 8.82 ? 286 GLU A CB 1 ATOM 1589 C CG . GLU A 1 200 ? 8.648 4.529 27.202 1.00 11.41 ? 286 GLU A CG 1 ATOM 1590 C CD . GLU A 1 200 ? 8.971 3.188 27.830 1.00 13.90 ? 286 GLU A CD 1 ATOM 1591 O OE1 . GLU A 1 200 ? 8.536 2.166 27.258 1.00 15.18 ? 286 GLU A OE1 1 ATOM 1592 O OE2 . GLU A 1 200 ? 9.574 3.189 28.931 1.00 17.49 ? 286 GLU A OE2 1 ATOM 1593 N N . LEU A 1 201 ? 10.344 7.684 25.811 1.00 7.22 ? 287 LEU A N 1 ATOM 1594 C CA . LEU A 1 201 ? 10.825 8.847 26.545 1.00 6.84 ? 287 LEU A CA 1 ATOM 1595 C C . LEU A 1 201 ? 10.063 10.095 26.120 1.00 7.20 ? 287 LEU A C 1 ATOM 1596 O O . LEU A 1 201 ? 9.532 10.823 26.975 1.00 7.32 ? 287 LEU A O 1 ATOM 1597 C CB A LEU A 1 201 ? 12.322 9.021 26.347 0.65 7.63 ? 287 LEU A CB 1 ATOM 1598 C CB B LEU A 1 201 ? 12.325 9.011 26.391 0.35 7.64 ? 287 LEU A CB 1 ATOM 1599 C CG A LEU A 1 201 ? 12.889 10.318 26.969 0.65 8.78 ? 287 LEU A CG 1 ATOM 1600 C CG B LEU A 1 201 ? 12.935 10.167 27.210 0.35 8.80 ? 287 LEU A CG 1 ATOM 1601 C CD1 A LEU A 1 201 ? 12.888 10.334 28.429 0.65 11.70 ? 287 LEU A CD1 1 ATOM 1602 C CD1 B LEU A 1 201 ? 12.814 11.462 26.427 0.35 12.03 ? 287 LEU A CD1 1 ATOM 1603 C CD2 A LEU A 1 201 ? 14.341 10.521 26.508 0.65 9.73 ? 287 LEU A CD2 1 ATOM 1604 C CD2 B LEU A 1 201 ? 12.438 10.360 28.619 0.35 12.40 ? 287 LEU A CD2 1 ATOM 1605 N N . PHE A 1 202 ? 10.025 10.389 24.835 1.00 6.62 ? 288 PHE A N 1 ATOM 1606 C CA . PHE A 1 202 ? 9.419 11.649 24.410 1.00 6.12 ? 288 PHE A CA 1 ATOM 1607 C C . PHE A 1 202 ? 7.922 11.659 24.677 1.00 6.22 ? 288 PHE A C 1 ATOM 1608 O O . PHE A 1 202 ? 7.366 12.691 25.030 1.00 7.13 ? 288 PHE A O 1 ATOM 1609 C CB . PHE A 1 202 ? 9.736 11.946 22.932 1.00 7.09 ? 288 PHE A CB 1 ATOM 1610 C CG . PHE A 1 202 ? 11.157 12.415 22.777 1.00 6.55 ? 288 PHE A CG 1 ATOM 1611 C CD1 . PHE A 1 202 ? 11.529 13.687 23.176 1.00 7.55 ? 288 PHE A CD1 1 ATOM 1612 C CD2 . PHE A 1 202 ? 12.136 11.601 22.254 1.00 8.33 ? 288 PHE A CD2 1 ATOM 1613 C CE1 . PHE A 1 202 ? 12.844 14.122 23.095 1.00 7.61 ? 288 PHE A CE1 1 ATOM 1614 C CE2 . PHE A 1 202 ? 13.475 12.056 22.159 1.00 8.72 ? 288 PHE A CE2 1 ATOM 1615 C CZ . PHE A 1 202 ? 13.797 13.293 22.559 1.00 8.11 ? 288 PHE A CZ 1 ATOM 1616 N N . ALA A 1 203 ? 7.260 10.519 24.486 1.00 6.76 ? 289 ALA A N 1 ATOM 1617 C CA . ALA A 1 203 ? 5.825 10.472 24.780 1.00 7.12 ? 289 ALA A CA 1 ATOM 1618 C C . ALA A 1 203 ? 5.565 10.664 26.301 1.00 7.35 ? 289 ALA A C 1 ATOM 1619 O O . ALA A 1 203 ? 4.582 11.283 26.670 1.00 7.72 ? 289 ALA A O 1 ATOM 1620 C CB . ALA A 1 203 ? 5.227 9.177 24.259 1.00 8.66 ? 289 ALA A CB 1 ATOM 1621 N N . LYS A 1 204 ? 6.419 10.134 27.142 1.00 7.60 ? 290 LYS A N 1 ATOM 1622 C CA . LYS A 1 204 ? 6.255 10.327 28.585 1.00 8.58 ? 290 LYS A CA 1 ATOM 1623 C C . LYS A 1 204 ? 6.441 11.790 28.983 1.00 7.77 ? 290 LYS A C 1 ATOM 1624 O O . LYS A 1 204 ? 5.694 12.345 29.798 1.00 8.26 ? 290 LYS A O 1 ATOM 1625 C CB A LYS A 1 204 ? 7.066 9.361 29.416 0.53 9.74 ? 290 LYS A CB 1 ATOM 1626 C CB B LYS A 1 204 ? 7.239 9.411 29.378 0.47 9.16 ? 290 LYS A CB 1 ATOM 1627 C CG A LYS A 1 204 ? 6.450 9.346 30.813 0.53 11.95 ? 290 LYS A CG 1 ATOM 1628 C CG B LYS A 1 204 ? 7.162 9.513 30.937 0.47 9.69 ? 290 LYS A CG 1 ATOM 1629 C CD A LYS A 1 204 ? 7.052 8.289 31.698 0.53 13.98 ? 290 LYS A CD 1 ATOM 1630 C CD B LYS A 1 204 ? 5.821 8.908 31.461 0.47 13.29 ? 290 LYS A CD 1 ATOM 1631 C CE A LYS A 1 204 ? 6.406 8.181 33.121 0.53 12.38 ? 290 LYS A CE 1 ATOM 1632 C CE B LYS A 1 204 ? 5.702 8.937 32.986 0.47 14.11 ? 290 LYS A CE 1 ATOM 1633 N NZ A LYS A 1 204 ? 6.499 9.465 33.976 0.53 17.06 ? 290 LYS A NZ 1 ATOM 1634 N NZ B LYS A 1 204 ? 7.040 9.292 33.665 0.47 17.53 ? 290 LYS A NZ 1 ATOM 1635 N N . ILE A 1 205 ? 7.478 12.440 28.420 1.00 6.98 ? 291 ILE A N 1 ATOM 1636 C CA . ILE A 1 205 ? 7.675 13.863 28.687 1.00 7.27 ? 291 ILE A CA 1 ATOM 1637 C C . ILE A 1 205 ? 6.450 14.686 28.285 1.00 7.10 ? 291 ILE A C 1 ATOM 1638 O O . ILE A 1 205 ? 5.982 15.549 29.021 1.00 7.15 ? 291 ILE A O 1 ATOM 1639 C CB . ILE A 1 205 ? 8.941 14.361 27.927 1.00 8.18 ? 291 ILE A CB 1 ATOM 1640 C CG1 . ILE A 1 205 ? 10.239 13.751 28.476 1.00 9.68 ? 291 ILE A CG1 1 ATOM 1641 C CG2 . ILE A 1 205 ? 9.016 15.902 27.937 1.00 9.74 ? 291 ILE A CG2 1 ATOM 1642 C CD1 . ILE A 1 205 ? 10.666 14.284 29.843 1.00 11.95 ? 291 ILE A CD1 1 ATOM 1643 N N . TYR A 1 206 ? 5.961 14.423 27.055 1.00 7.48 ? 292 TYR A N 1 ATOM 1644 C CA . TYR A 1 206 ? 4.758 15.051 26.562 1.00 7.79 ? 292 TYR A CA 1 ATOM 1645 C C . TYR A 1 206 ? 3.582 14.898 27.549 1.00 7.81 ? 292 TYR A C 1 ATOM 1646 O O . TYR A 1 206 ? 2.901 15.879 27.876 1.00 8.23 ? 292 TYR A O 1 ATOM 1647 C CB . TYR A 1 206 ? 4.413 14.417 25.196 1.00 8.03 ? 292 TYR A CB 1 ATOM 1648 C CG . TYR A 1 206 ? 3.271 15.087 24.479 1.00 7.60 ? 292 TYR A CG 1 ATOM 1649 C CD1 . TYR A 1 206 ? 3.262 16.414 24.181 1.00 7.84 ? 292 TYR A CD1 1 ATOM 1650 C CD2 . TYR A 1 206 ? 2.203 14.306 24.052 1.00 7.41 ? 292 TYR A CD2 1 ATOM 1651 C CE1 . TYR A 1 206 ? 2.222 17.010 23.483 1.00 8.08 ? 292 TYR A CE1 1 ATOM 1652 C CE2 . TYR A 1 206 ? 1.162 14.873 23.343 1.00 7.57 ? 292 TYR A CE2 1 ATOM 1653 C CZ . TYR A 1 206 ? 1.157 16.221 23.066 1.00 7.32 ? 292 TYR A CZ 1 ATOM 1654 O OH . TYR A 1 206 ? 0.095 16.774 22.360 1.00 8.88 ? 292 TYR A OH 1 ATOM 1655 N N . GLU A 1 207 ? 3.327 13.668 27.995 1.00 8.01 ? 293 GLU A N 1 ATOM 1656 C CA . GLU A 1 207 ? 2.312 13.358 29.014 1.00 9.96 ? 293 GLU A CA 1 ATOM 1657 C C . GLU A 1 207 ? 2.521 14.130 30.279 1.00 9.06 ? 293 GLU A C 1 ATOM 1658 O O . GLU A 1 207 ? 1.572 14.764 30.830 1.00 9.47 ? 293 GLU A O 1 ATOM 1659 C CB . GLU A 1 207 ? 2.403 11.765 29.433 1.00 12.06 ? 293 GLU A CB 1 ATOM 1660 C CG . GLU A 1 207 ? 1.435 10.974 28.723 1.00 13.44 ? 293 GLU A CG 1 ATOM 1661 C CD . GLU A 1 207 ? 1.674 9.552 28.932 1.00 10.01 ? 293 GLU A CD 1 ATOM 1662 O OE1 . GLU A 1 207 ? 2.184 9.080 30.039 1.00 13.20 ? 293 GLU A OE1 1 ATOM 1663 O OE2 . GLU A 1 207 ? 1.360 8.844 28.082 1.00 13.50 ? 293 GLU A OE2 1 ATOM 1664 N N . ASP A 1 208 ? 3.727 14.053 30.799 1.00 9.02 ? 294 ASP A N 1 ATOM 1665 C CA . ASP A 1 208 ? 4.038 14.657 32.089 1.00 9.91 ? 294 ASP A CA 1 ATOM 1666 C C . ASP A 1 208 ? 3.971 16.157 32.039 1.00 9.08 ? 294 ASP A C 1 ATOM 1667 O O . ASP A 1 208 ? 3.699 16.820 33.075 1.00 11.65 ? 294 ASP A O 1 ATOM 1668 C CB . ASP A 1 208 ? 5.359 14.168 32.556 1.00 11.21 ? 294 ASP A CB 1 ATOM 1669 C CG . ASP A 1 208 ? 5.315 12.671 32.969 1.00 12.02 ? 294 ASP A CG 1 ATOM 1670 O OD1 . ASP A 1 208 ? 4.207 12.102 33.044 1.00 14.89 ? 294 ASP A OD1 1 ATOM 1671 O OD2 . ASP A 1 208 ? 6.369 12.078 33.116 1.00 14.61 ? 294 ASP A OD2 1 ATOM 1672 N N . ALA A 1 209 ? 4.131 16.780 30.890 1.00 7.98 ? 295 ALA A N 1 ATOM 1673 C CA . ALA A 1 209 ? 3.944 18.230 30.741 1.00 8.21 ? 295 ALA A CA 1 ATOM 1674 C C . ALA A 1 209 ? 2.495 18.609 30.539 1.00 8.06 ? 295 ALA A C 1 ATOM 1675 O O . ALA A 1 209 ? 2.190 19.786 30.362 1.00 9.05 ? 295 ALA A O 1 ATOM 1676 C CB . ALA A 1 209 ? 4.777 18.713 29.561 1.00 8.57 ? 295 ALA A CB 1 ATOM 1677 N N . GLY A 1 210 ? 1.570 17.639 30.545 1.00 8.19 ? 296 GLY A N 1 ATOM 1678 C CA . GLY A 1 210 ? 0.170 17.941 30.332 1.00 8.95 ? 296 GLY A CA 1 ATOM 1679 C C . GLY A 1 210 ? -0.218 18.094 28.884 1.00 8.21 ? 296 GLY A C 1 ATOM 1680 O O . GLY A 1 210 ? -1.267 18.694 28.598 1.00 9.92 ? 296 GLY A O 1 ATOM 1681 N N . LYS A 1 211 ? 0.540 17.538 27.945 1.00 7.38 ? 297 LYS A N 1 ATOM 1682 C CA . LYS A 1 211 ? 0.249 17.601 26.525 1.00 7.60 ? 297 LYS A CA 1 ATOM 1683 C C . LYS A 1 211 ? -0.046 19.065 26.111 1.00 7.49 ? 297 LYS A C 1 ATOM 1684 O O . LYS A 1 211 ? -1.113 19.359 25.566 1.00 9.14 ? 297 LYS A O 1 ATOM 1685 C CB . LYS A 1 211 ? -0.822 16.630 26.068 1.00 7.69 ? 297 LYS A CB 1 ATOM 1686 C CG . LYS A 1 211 ? -0.518 15.201 26.462 1.00 7.75 ? 297 LYS A CG 1 ATOM 1687 C CD . LYS A 1 211 ? -1.374 14.159 25.763 1.00 7.69 ? 297 LYS A CD 1 ATOM 1688 C CE . LYS A 1 211 ? -0.942 12.764 26.186 1.00 7.60 ? 297 LYS A CE 1 ATOM 1689 N NZ . LYS A 1 211 ? -1.566 11.714 25.334 1.00 8.06 ? 297 LYS A NZ 1 ATOM 1690 N N . PRO A 1 212 ? 0.890 19.969 26.344 1.00 7.54 ? 298 PRO A N 1 ATOM 1691 C CA . PRO A 1 212 ? 0.593 21.388 26.095 1.00 7.97 ? 298 PRO A CA 1 ATOM 1692 C C . PRO A 1 212 ? 0.224 21.643 24.656 1.00 7.54 ? 298 PRO A C 1 ATOM 1693 O O . PRO A 1 212 ? 0.874 21.088 23.739 1.00 7.74 ? 298 PRO A O 1 ATOM 1694 C CB . PRO A 1 212 ? 1.920 22.111 26.460 1.00 8.41 ? 298 PRO A CB 1 ATOM 1695 C CG . PRO A 1 212 ? 2.712 21.149 27.275 1.00 9.76 ? 298 PRO A CG 1 ATOM 1696 C CD . PRO A 1 212 ? 2.287 19.778 26.756 1.00 8.35 ? 298 PRO A CD 1 ATOM 1697 N N . ARG A 1 213 ? -0.784 22.459 24.434 1.00 7.51 ? 299 ARG A N 1 ATOM 1698 C CA . ARG A 1 213 ? -1.251 22.776 23.072 1.00 8.27 ? 299 ARG A CA 1 ATOM 1699 C C . ARG A 1 213 ? -0.147 23.266 22.147 1.00 7.03 ? 299 ARG A C 1 ATOM 1700 O O . ARG A 1 213 ? -0.153 22.983 20.968 1.00 7.81 ? 299 ARG A O 1 ATOM 1701 C CB . ARG A 1 213 ? -2.387 23.796 23.155 1.00 9.67 ? 299 ARG A CB 1 ATOM 1702 C CG . ARG A 1 213 ? -2.869 24.334 21.807 1.00 13.39 ? 299 ARG A CG 1 ATOM 1703 C CD . ARG A 1 213 ? -3.956 25.343 21.903 1.00 17.71 ? 299 ARG A CD 1 ATOM 1704 N NE . ARG A 1 213 ? -4.318 25.920 20.620 1.00 17.83 ? 299 ARG A NE 1 ATOM 1705 C CZ . ARG A 1 213 ? -5.567 26.256 20.228 1.00 19.86 ? 299 ARG A CZ 1 ATOM 1706 N NH1 . ARG A 1 213 ? -6.596 26.070 21.054 1.00 21.97 ? 299 ARG A NH1 1 ATOM 1707 N NH2 . ARG A 1 213 ? -5.761 26.811 19.017 1.00 21.56 ? 299 ARG A NH2 1 ATOM 1708 N N . ALA A 1 214 ? 0.771 24.067 22.679 1.00 7.15 ? 300 ALA A N 1 ATOM 1709 C CA . ALA A 1 214 ? 1.817 24.636 21.840 1.00 6.99 ? 300 ALA A CA 1 ATOM 1710 C C . ALA A 1 214 ? 2.770 23.572 21.288 1.00 7.01 ? 300 ALA A C 1 ATOM 1711 O O . ALA A 1 214 ? 3.459 23.877 20.308 1.00 7.68 ? 300 ALA A O 1 ATOM 1712 C CB . ALA A 1 214 ? 2.599 25.685 22.618 1.00 7.42 ? 300 ALA A CB 1 ATOM 1713 N N . VAL A 1 215 ? 2.880 22.409 21.897 1.00 6.76 ? 301 VAL A N 1 ATOM 1714 C CA . VAL A 1 215 ? 3.810 21.382 21.409 1.00 6.91 ? 301 VAL A CA 1 ATOM 1715 C C . VAL A 1 215 ? 3.230 20.728 20.164 1.00 7.28 ? 301 VAL A C 1 ATOM 1716 O O . VAL A 1 215 ? 2.244 19.982 20.234 1.00 8.75 ? 301 VAL A O 1 ATOM 1717 C CB . VAL A 1 215 ? 4.141 20.387 22.498 1.00 7.92 ? 301 VAL A CB 1 ATOM 1718 C CG1 . VAL A 1 215 ? 5.003 19.260 21.929 1.00 9.47 ? 301 VAL A CG1 1 ATOM 1719 C CG2 . VAL A 1 215 ? 4.814 21.058 23.656 1.00 8.96 ? 301 VAL A CG2 1 ATOM 1720 N N . ARG A 1 216 ? 3.865 20.939 19.015 1.00 6.89 ? 302 ARG A N 1 ATOM 1721 C CA . ARG A 1 216 ? 3.492 20.289 17.788 1.00 7.36 ? 302 ARG A CA 1 ATOM 1722 C C . ARG A 1 216 ? 4.144 18.957 17.601 1.00 6.07 ? 302 ARG A C 1 ATOM 1723 O O . ARG A 1 216 ? 3.604 18.112 16.891 1.00 7.57 ? 302 ARG A O 1 ATOM 1724 C CB . ARG A 1 216 ? 3.838 21.128 16.531 1.00 8.89 ? 302 ARG A CB 1 ATOM 1725 C CG . ARG A 1 216 ? 2.928 22.307 16.258 1.00 9.25 ? 302 ARG A CG 1 ATOM 1726 C CD . ARG A 1 216 ? 1.553 21.888 15.771 1.00 10.16 ? 302 ARG A CD 1 ATOM 1727 N NE . ARG A 1 216 ? 1.559 21.242 14.426 1.00 9.14 ? 302 ARG A NE 1 ATOM 1728 C CZ . ARG A 1 216 ? 0.441 20.781 13.810 1.00 8.65 ? 302 ARG A CZ 1 ATOM 1729 N NH1 . ARG A 1 216 ? -0.723 20.818 14.468 1.00 10.00 ? 302 ARG A NH1 1 ATOM 1730 N NH2 . ARG A 1 216 ? 0.493 20.349 12.585 1.00 8.37 ? 302 ARG A NH2 1 ATOM 1731 N N . GLY A 1 217 ? 5.334 18.744 18.162 1.00 6.29 ? 303 GLY A N 1 ATOM 1732 C CA . GLY A 1 217 ? 6.070 17.526 17.922 1.00 6.07 ? 303 GLY A CA 1 ATOM 1733 C C . GLY A 1 217 ? 7.540 17.687 18.183 1.00 5.34 ? 303 GLY A C 1 ATOM 1734 O O . GLY A 1 217 ? 7.936 18.147 19.253 1.00 5.54 ? 303 GLY A O 1 ATOM 1735 N N . LEU A 1 218 ? 8.325 17.236 17.199 1.00 5.76 ? 304 LEU A N 1 ATOM 1736 C CA . LEU A 1 218 ? 9.750 17.015 17.340 1.00 5.39 ? 304 LEU A CA 1 ATOM 1737 C C . LEU A 1 218 ? 10.499 17.606 16.161 1.00 5.23 ? 304 LEU A C 1 ATOM 1738 O O . LEU A 1 218 ? 9.972 17.714 15.037 1.00 6.25 ? 304 LEU A O 1 ATOM 1739 C CB . LEU A 1 218 ? 10.030 15.499 17.424 1.00 5.93 ? 304 LEU A CB 1 ATOM 1740 C CG . LEU A 1 218 ? 9.352 14.755 18.589 1.00 6.15 ? 304 LEU A CG 1 ATOM 1741 C CD1 . LEU A 1 218 ? 9.594 13.284 18.461 1.00 6.97 ? 304 LEU A CD1 1 ATOM 1742 C CD2 . LEU A 1 218 ? 9.780 15.251 19.935 1.00 5.95 ? 304 LEU A CD2 1 ATOM 1743 N N . ALA A 1 219 ? 11.769 17.958 16.415 1.00 5.28 ? 305 ALA A N 1 ATOM 1744 C CA . ALA A 1 219 ? 12.696 18.425 15.381 1.00 5.53 ? 305 ALA A CA 1 ATOM 1745 C C . ALA A 1 219 ? 13.784 17.390 15.180 1.00 5.56 ? 305 ALA A C 1 ATOM 1746 O O . ALA A 1 219 ? 14.334 16.902 16.185 1.00 6.67 ? 305 ALA A O 1 ATOM 1747 C CB . ALA A 1 219 ? 13.323 19.755 15.787 1.00 6.02 ? 305 ALA A CB 1 ATOM 1748 N N . THR A 1 220 ? 14.120 17.067 13.931 1.00 5.24 ? 306 THR A N 1 ATOM 1749 C CA . THR A 1 220 ? 15.183 16.106 13.676 1.00 5.43 ? 306 THR A CA 1 ATOM 1750 C C . THR A 1 220 ? 16.246 16.701 12.753 1.00 5.28 ? 306 THR A C 1 ATOM 1751 O O . THR A 1 220 ? 16.018 17.658 12.014 1.00 5.58 ? 306 THR A O 1 ATOM 1752 C CB . THR A 1 220 ? 14.650 14.787 13.106 1.00 5.62 ? 306 THR A CB 1 ATOM 1753 O OG1 . THR A 1 220 ? 14.215 14.969 11.760 1.00 7.33 ? 306 THR A OG1 1 ATOM 1754 C CG2 . THR A 1 220 ? 13.586 14.177 14.007 1.00 8.38 ? 306 THR A CG2 1 ATOM 1755 N N . ASN A 1 221 ? 17.425 16.064 12.821 1.00 5.51 ? 307 ASN A N 1 ATOM 1756 C CA . ASN A 1 221 ? 18.564 16.413 11.998 1.00 5.39 ? 307 ASN A CA 1 ATOM 1757 C C . ASN A 1 221 ? 19.159 17.778 12.341 1.00 5.07 ? 307 ASN A C 1 ATOM 1758 O O . ASN A 1 221 ? 19.968 18.271 11.563 1.00 5.47 ? 307 ASN A O 1 ATOM 1759 C CB . ASN A 1 221 ? 18.299 16.299 10.501 1.00 5.62 ? 307 ASN A CB 1 ATOM 1760 C CG . ASN A 1 221 ? 19.551 16.171 9.668 1.00 5.62 ? 307 ASN A CG 1 ATOM 1761 O OD1 . ASN A 1 221 ? 20.454 15.378 9.980 1.00 6.05 ? 307 ASN A OD1 1 ATOM 1762 N ND2 . ASN A 1 221 ? 19.581 16.895 8.544 1.00 6.68 ? 307 ASN A ND2 1 ATOM 1763 N N . VAL A 1 222 ? 18.795 18.363 13.480 1.00 5.42 ? 308 VAL A N 1 ATOM 1764 C CA . VAL A 1 222 ? 19.327 19.674 13.873 1.00 5.86 ? 308 VAL A CA 1 ATOM 1765 C C . VAL A 1 222 ? 20.852 19.617 13.885 1.00 4.97 ? 308 VAL A C 1 ATOM 1766 O O . VAL A 1 222 ? 21.438 18.757 14.582 1.00 6.06 ? 308 VAL A O 1 ATOM 1767 C CB . VAL A 1 222 ? 18.789 20.113 15.218 1.00 5.94 ? 308 VAL A CB 1 ATOM 1768 C CG1 . VAL A 1 222 ? 19.483 21.409 15.666 1.00 6.53 ? 308 VAL A CG1 1 ATOM 1769 C CG2 . VAL A 1 222 ? 17.267 20.282 15.175 1.00 6.61 ? 308 VAL A CG2 1 ATOM 1770 N N . ALA A 1 223 ? 21.493 20.507 13.140 1.00 5.45 ? 309 ALA A N 1 ATOM 1771 C CA . ALA A 1 223 ? 22.947 20.620 13.068 1.00 6.46 ? 309 ALA A CA 1 ATOM 1772 C C . ALA A 1 223 ? 23.611 19.422 12.432 1.00 5.89 ? 309 ALA A C 1 ATOM 1773 O O . ALA A 1 223 ? 24.840 19.342 12.420 1.00 7.36 ? 309 ALA A O 1 ATOM 1774 C CB . ALA A 1 223 ? 23.572 20.951 14.424 1.00 6.52 ? 309 ALA A CB 1 ATOM 1775 N N . ASN A 1 224 ? 22.850 18.513 11.845 1.00 5.59 ? 310 ASN A N 1 ATOM 1776 C CA . ASN A 1 224 ? 23.397 17.372 11.155 1.00 5.72 ? 310 ASN A CA 1 ATOM 1777 C C . ASN A 1 224 ? 23.147 17.517 9.659 1.00 5.68 ? 310 ASN A C 1 ATOM 1778 O O . ASN A 1 224 ? 22.695 18.569 9.185 1.00 6.10 ? 310 ASN A O 1 ATOM 1779 C CB . ASN A 1 224 ? 22.892 16.086 11.794 1.00 6.41 ? 310 ASN A CB 1 ATOM 1780 C CG . ASN A 1 224 ? 23.737 15.688 12.923 1.00 7.78 ? 310 ASN A CG 1 ATOM 1781 O OD1 . ASN A 1 224 ? 24.637 14.808 12.707 1.00 11.02 ? 310 ASN A OD1 1 ATOM 1782 N ND2 . ASN A 1 224 ? 23.581 16.343 14.068 1.00 10.56 ? 310 ASN A ND2 1 ATOM 1783 N N . TYR A 1 225 ? 23.490 16.474 8.875 1.00 5.66 ? 311 TYR A N 1 ATOM 1784 C CA . TYR A 1 225 ? 23.651 16.631 7.416 1.00 5.95 ? 311 TYR A CA 1 ATOM 1785 C C . TYR A 1 225 ? 22.814 15.619 6.649 1.00 5.32 ? 311 TYR A C 1 ATOM 1786 O O . TYR A 1 225 ? 22.994 15.449 5.434 1.00 6.21 ? 311 TYR A O 1 ATOM 1787 C CB . TYR A 1 225 ? 25.125 16.468 7.016 1.00 6.00 ? 311 TYR A CB 1 ATOM 1788 C CG . TYR A 1 225 ? 26.087 17.267 7.849 1.00 5.56 ? 311 TYR A CG 1 ATOM 1789 C CD1 . TYR A 1 225 ? 26.424 18.557 7.528 1.00 6.26 ? 311 TYR A CD1 1 ATOM 1790 C CD2 . TYR A 1 225 ? 26.709 16.693 8.977 1.00 6.26 ? 311 TYR A CD2 1 ATOM 1791 C CE1 . TYR A 1 225 ? 27.347 19.283 8.278 1.00 6.13 ? 311 TYR A CE1 1 ATOM 1792 C CE2 . TYR A 1 225 ? 27.604 17.416 9.734 1.00 6.51 ? 311 TYR A CE2 1 ATOM 1793 C CZ . TYR A 1 225 ? 27.941 18.687 9.388 1.00 6.30 ? 311 TYR A CZ 1 ATOM 1794 O OH . TYR A 1 225 ? 28.899 19.408 10.069 1.00 6.77 ? 311 TYR A OH 1 ATOM 1795 N N . ASN A 1 226 ? 21.893 14.947 7.319 1.00 5.62 ? 312 ASN A N 1 ATOM 1796 C CA . ASN A 1 226 ? 21.231 13.791 6.723 1.00 5.58 ? 312 ASN A CA 1 ATOM 1797 C C . ASN A 1 226 ? 20.327 14.195 5.571 1.00 5.37 ? 312 ASN A C 1 ATOM 1798 O O . ASN A 1 226 ? 19.746 15.293 5.512 1.00 6.13 ? 312 ASN A O 1 ATOM 1799 C CB . ASN A 1 226 ? 20.398 13.034 7.749 1.00 5.87 ? 312 ASN A CB 1 ATOM 1800 C CG . ASN A 1 226 ? 21.196 12.443 8.868 1.00 5.62 ? 312 ASN A CG 1 ATOM 1801 O OD1 . ASN A 1 226 ? 22.446 12.471 8.862 1.00 6.72 ? 312 ASN A OD1 1 ATOM 1802 N ND2 . ASN A 1 226 ? 20.534 11.864 9.832 1.00 6.86 ? 312 ASN A ND2 1 ATOM 1803 N N . ALA A 1 227 ? 20.102 13.224 4.685 1.00 6.06 ? 313 ALA A N 1 ATOM 1804 C CA . ALA A 1 227 ? 19.101 13.400 3.632 1.00 6.16 ? 313 ALA A CA 1 ATOM 1805 C C . ALA A 1 227 ? 17.707 13.349 4.248 1.00 6.02 ? 313 ALA A C 1 ATOM 1806 O O . ALA A 1 227 ? 17.451 12.652 5.223 1.00 6.26 ? 313 ALA A O 1 ATOM 1807 C CB . ALA A 1 227 ? 19.216 12.250 2.632 1.00 7.51 ? 313 ALA A CB 1 ATOM 1808 N N . TRP A 1 228 ? 16.777 14.062 3.606 1.00 7.11 ? 314 TRP A N 1 ATOM 1809 C CA . TRP A 1 228 ? 15.341 13.824 3.798 1.00 6.98 ? 314 TRP A CA 1 ATOM 1810 C C . TRP A 1 228 ? 14.986 12.490 3.173 1.00 6.74 ? 314 TRP A C 1 ATOM 1811 O O . TRP A 1 228 ? 14.559 11.549 3.852 1.00 7.38 ? 314 TRP A O 1 ATOM 1812 C CB . TRP A 1 228 ? 14.502 14.983 3.308 1.00 7.16 ? 314 TRP A CB 1 ATOM 1813 C CG . TRP A 1 228 ? 13.065 14.603 3.034 1.00 6.94 ? 314 TRP A CG 1 ATOM 1814 C CD1 . TRP A 1 228 ? 12.486 14.604 1.802 1.00 7.42 ? 314 TRP A CD1 1 ATOM 1815 C CD2 . TRP A 1 228 ? 12.112 14.085 3.953 1.00 6.61 ? 314 TRP A CD2 1 ATOM 1816 N NE1 . TRP A 1 228 ? 11.195 14.135 1.911 1.00 7.88 ? 314 TRP A NE1 1 ATOM 1817 C CE2 . TRP A 1 228 ? 10.934 13.828 3.219 1.00 7.32 ? 314 TRP A CE2 1 ATOM 1818 C CE3 . TRP A 1 228 ? 12.084 13.880 5.348 1.00 6.81 ? 314 TRP A CE3 1 ATOM 1819 C CZ2 . TRP A 1 228 ? 9.785 13.332 3.811 1.00 7.91 ? 314 TRP A CZ2 1 ATOM 1820 C CZ3 . TRP A 1 228 ? 10.935 13.413 5.908 1.00 7.63 ? 314 TRP A CZ3 1 ATOM 1821 C CH2 . TRP A 1 228 ? 9.805 13.116 5.150 1.00 7.90 ? 314 TRP A CH2 1 ATOM 1822 N N . SER A 1 229 ? 15.207 12.360 1.854 1.00 7.47 ? 315 SER A N 1 ATOM 1823 C CA . SER A 1 229 ? 14.846 11.160 1.157 1.00 8.13 ? 315 SER A CA 1 ATOM 1824 C C . SER A 1 229 ? 15.728 10.908 -0.026 1.00 9.67 ? 315 SER A C 1 ATOM 1825 O O . SER A 1 229 ? 15.708 11.684 -1.003 1.00 12.00 ? 315 SER A O 1 ATOM 1826 C CB . SER A 1 229 ? 13.410 11.231 0.669 1.00 9.86 ? 315 SER A CB 1 ATOM 1827 O OG . SER A 1 229 ? 13.003 10.013 0.009 1.00 11.38 ? 315 SER A OG 1 ATOM 1828 N N . VAL A 1 230 ? 16.531 9.866 0.032 1.00 9.66 ? 316 VAL A N 1 ATOM 1829 C CA . VAL A 1 230 ? 17.390 9.454 -1.093 1.00 10.85 ? 316 VAL A CA 1 ATOM 1830 C C . VAL A 1 230 ? 17.205 8.006 -1.400 1.00 10.66 ? 316 VAL A C 1 ATOM 1831 O O . VAL A 1 230 ? 16.751 7.235 -0.568 1.00 11.14 ? 316 VAL A O 1 ATOM 1832 C CB . VAL A 1 230 ? 18.854 9.769 -0.827 1.00 13.11 ? 316 VAL A CB 1 ATOM 1833 C CG1 . VAL A 1 230 ? 19.056 11.235 -0.912 1.00 14.75 ? 316 VAL A CG1 1 ATOM 1834 C CG2 . VAL A 1 230 ? 19.361 9.141 0.456 1.00 12.45 ? 316 VAL A CG2 1 ATOM 1835 N N . SER A 1 231 ? 17.533 7.655 -2.664 1.00 12.12 ? 317 SER A N 1 ATOM 1836 C CA . SER A 1 231 ? 17.273 6.311 -3.174 1.00 13.77 ? 317 SER A CA 1 ATOM 1837 C C . SER A 1 231 ? 18.240 5.288 -2.641 1.00 12.21 ? 317 SER A C 1 ATOM 1838 O O . SER A 1 231 ? 17.857 4.144 -2.520 1.00 18.43 ? 317 SER A O 1 ATOM 1839 C CB A SER A 1 231 ? 17.333 6.289 -4.723 0.52 14.62 ? 317 SER A CB 1 ATOM 1840 C CB B SER A 1 231 ? 17.302 6.270 -4.730 0.48 15.28 ? 317 SER A CB 1 ATOM 1841 O OG A SER A 1 231 ? 16.233 7.013 -5.202 0.52 15.71 ? 317 SER A OG 1 ATOM 1842 O OG B SER A 1 231 ? 18.542 6.758 -5.203 0.48 20.82 ? 317 SER A OG 1 ATOM 1843 N N . SER A 1 232 ? 19.483 5.675 -2.442 1.00 13.21 ? 318 SER A N 1 ATOM 1844 C CA A SER A 1 232 ? 20.583 4.781 -2.073 0.60 13.92 ? 318 SER A CA 1 ATOM 1845 C CA B SER A 1 232 ? 20.410 4.684 -1.920 0.40 13.64 ? 318 SER A CA 1 ATOM 1846 C C . SER A 1 232 ? 21.061 5.126 -0.644 1.00 11.55 ? 318 SER A C 1 ATOM 1847 O O . SER A 1 232 ? 21.323 6.319 -0.427 1.00 12.47 ? 318 SER A O 1 ATOM 1848 C CB A SER A 1 232 ? 21.749 4.922 -3.066 0.60 13.80 ? 318 SER A CB 1 ATOM 1849 C CB B SER A 1 232 ? 21.460 4.294 -2.915 0.40 13.69 ? 318 SER A CB 1 ATOM 1850 O OG A SER A 1 232 ? 22.714 3.874 -2.861 0.60 21.29 ? 318 SER A OG 1 ATOM 1851 O OG B SER A 1 232 ? 22.355 5.374 -3.156 0.40 18.36 ? 318 SER A OG 1 ATOM 1852 N N . PRO A 1 233 ? 21.225 4.163 0.260 1.00 11.19 ? 319 PRO A N 1 ATOM 1853 C CA . PRO A 1 233 ? 21.796 4.508 1.576 1.00 10.16 ? 319 PRO A CA 1 ATOM 1854 C C . PRO A 1 233 ? 23.206 5.038 1.429 1.00 9.19 ? 319 PRO A C 1 ATOM 1855 O O . PRO A 1 233 ? 24.062 4.398 0.805 1.00 9.87 ? 319 PRO A O 1 ATOM 1856 C CB A PRO A 1 233 ? 21.757 3.184 2.305 0.70 12.17 ? 319 PRO A CB 1 ATOM 1857 C CB B PRO A 1 233 ? 21.823 3.170 2.336 0.30 11.20 ? 319 PRO A CB 1 ATOM 1858 C CG A PRO A 1 233 ? 20.674 2.417 1.528 0.70 13.50 ? 319 PRO A CG 1 ATOM 1859 C CG B PRO A 1 233 ? 21.818 2.092 1.295 0.30 10.53 ? 319 PRO A CG 1 ATOM 1860 C CD A PRO A 1 233 ? 20.893 2.737 0.146 0.70 13.34 ? 319 PRO A CD 1 ATOM 1861 C CD B PRO A 1 233 ? 20.924 2.717 0.207 0.30 12.02 ? 319 PRO A CD 1 ATOM 1862 N N . PRO A 1 234 ? 23.529 6.189 2.007 1.00 8.76 ? 320 PRO A N 1 ATOM 1863 C CA . PRO A 1 234 ? 24.937 6.623 2.012 1.00 8.88 ? 320 PRO A CA 1 ATOM 1864 C C . PRO A 1 234 ? 25.790 5.612 2.695 1.00 8.71 ? 320 PRO A C 1 ATOM 1865 O O . PRO A 1 234 ? 25.362 4.931 3.639 1.00 9.13 ? 320 PRO A O 1 ATOM 1866 C CB . PRO A 1 234 ? 24.875 7.957 2.749 1.00 9.25 ? 320 PRO A CB 1 ATOM 1867 C CG . PRO A 1 234 ? 23.476 8.499 2.467 1.00 9.95 ? 320 PRO A CG 1 ATOM 1868 C CD . PRO A 1 234 ? 22.642 7.233 2.538 1.00 9.42 ? 320 PRO A CD 1 ATOM 1869 N N . PRO A 1 235 ? 27.060 5.491 2.290 1.00 9.55 ? 321 PRO A N 1 ATOM 1870 C CA . PRO A 1 235 ? 27.882 4.399 2.798 1.00 10.86 ? 321 PRO A CA 1 ATOM 1871 C C . PRO A 1 235 ? 28.057 4.393 4.325 1.00 10.27 ? 321 PRO A C 1 ATOM 1872 O O . PRO A 1 235 ? 28.112 3.337 4.955 1.00 11.16 ? 321 PRO A O 1 ATOM 1873 C CB . PRO A 1 235 ? 29.226 4.579 2.063 1.00 12.65 ? 321 PRO A CB 1 ATOM 1874 C CG . PRO A 1 235 ? 29.260 6.018 1.621 1.00 15.27 ? 321 PRO A CG 1 ATOM 1875 C CD . PRO A 1 235 ? 27.771 6.303 1.287 1.00 12.49 ? 321 PRO A CD 1 ATOM 1876 N N . TYR A 1 236 ? 28.151 5.574 4.938 1.00 8.04 ? 322 TYR A N 1 ATOM 1877 C CA . TYR A 1 236 ? 28.369 5.663 6.372 1.00 8.04 ? 322 TYR A CA 1 ATOM 1878 C C . TYR A 1 236 ? 27.103 5.334 7.193 1.00 7.47 ? 322 TYR A C 1 ATOM 1879 O O . TYR A 1 236 ? 27.172 5.312 8.421 1.00 8.26 ? 322 TYR A O 1 ATOM 1880 C CB . TYR A 1 236 ? 28.902 7.053 6.724 1.00 8.34 ? 322 TYR A CB 1 ATOM 1881 C CG . TYR A 1 236 ? 28.170 8.133 5.981 1.00 7.55 ? 322 TYR A CG 1 ATOM 1882 C CD1 . TYR A 1 236 ? 26.945 8.625 6.452 1.00 7.30 ? 322 TYR A CD1 1 ATOM 1883 C CD2 . TYR A 1 236 ? 28.668 8.656 4.792 1.00 8.32 ? 322 TYR A CD2 1 ATOM 1884 C CE1 . TYR A 1 236 ? 26.248 9.595 5.738 1.00 7.00 ? 322 TYR A CE1 1 ATOM 1885 C CE2 . TYR A 1 236 ? 27.988 9.629 4.088 1.00 7.89 ? 322 TYR A CE2 1 ATOM 1886 C CZ . TYR A 1 236 ? 26.766 10.072 4.555 1.00 7.13 ? 322 TYR A CZ 1 ATOM 1887 O OH . TYR A 1 236 ? 26.086 11.000 3.781 1.00 7.55 ? 322 TYR A OH 1 ATOM 1888 N N . THR A 1 237 ? 25.982 5.104 6.534 1.00 7.64 ? 323 THR A N 1 ATOM 1889 C CA . THR A 1 237 ? 24.750 4.762 7.274 1.00 8.53 ? 323 THR A CA 1 ATOM 1890 C C . THR A 1 237 ? 24.574 3.271 7.528 1.00 8.07 ? 323 THR A C 1 ATOM 1891 O O . THR A 1 237 ? 23.730 2.859 8.318 1.00 8.71 ? 323 THR A O 1 ATOM 1892 C CB . THR A 1 237 ? 23.489 5.289 6.585 1.00 7.72 ? 323 THR A CB 1 ATOM 1893 O OG1 . THR A 1 237 ? 23.257 4.578 5.353 1.00 8.07 ? 323 THR A OG1 1 ATOM 1894 C CG2 . THR A 1 237 ? 23.524 6.783 6.347 1.00 8.39 ? 323 THR A CG2 1 ATOM 1895 N N . SER A 1 238 ? 25.374 2.444 6.846 1.00 9.35 ? 324 SER A N 1 ATOM 1896 C CA . SER A 1 238 ? 25.130 1.012 6.931 1.00 10.35 ? 324 SER A CA 1 ATOM 1897 C C . SER A 1 238 ? 25.447 0.480 8.322 1.00 10.70 ? 324 SER A C 1 ATOM 1898 O O . SER A 1 238 ? 26.453 0.898 8.912 1.00 11.52 ? 324 SER A O 1 ATOM 1899 C CB . SER A 1 238 ? 26.068 0.317 5.947 1.00 13.33 ? 324 SER A CB 1 ATOM 1900 O OG . SER A 1 238 ? 25.867 -1.080 5.953 1.00 17.48 ? 324 SER A OG 1 ATOM 1901 N N . PRO A 1 239 ? 24.683 -0.469 8.864 1.00 10.33 ? 325 PRO A N 1 ATOM 1902 C CA . PRO A 1 239 ? 23.536 -1.132 8.262 1.00 10.58 ? 325 PRO A CA 1 ATOM 1903 C C . PRO A 1 239 ? 22.190 -0.615 8.765 1.00 9.88 ? 325 PRO A C 1 ATOM 1904 O O . PRO A 1 239 ? 21.233 -1.383 8.888 1.00 12.25 ? 325 PRO A O 1 ATOM 1905 C CB . PRO A 1 239 ? 23.768 -2.604 8.719 1.00 13.49 ? 325 PRO A CB 1 ATOM 1906 C CG . PRO A 1 239 ? 24.253 -2.385 10.117 1.00 14.48 ? 325 PRO A CG 1 ATOM 1907 C CD . PRO A 1 239 ? 25.137 -1.203 10.074 1.00 12.71 ? 325 PRO A CD 1 ATOM 1908 N N . ASN A 1 240 ? 22.057 0.661 9.079 1.00 8.52 ? 326 ASN A N 1 ATOM 1909 C CA . ASN A 1 240 ? 20.783 1.193 9.608 1.00 8.11 ? 326 ASN A CA 1 ATOM 1910 C C . ASN A 1 240 ? 19.747 1.171 8.468 1.00 7.98 ? 326 ASN A C 1 ATOM 1911 O O . ASN A 1 240 ? 19.956 1.826 7.447 1.00 8.72 ? 326 ASN A O 1 ATOM 1912 C CB . ASN A 1 240 ? 20.991 2.599 10.095 1.00 7.59 ? 326 ASN A CB 1 ATOM 1913 C CG . ASN A 1 240 ? 19.842 3.145 10.900 1.00 7.24 ? 326 ASN A CG 1 ATOM 1914 O OD1 . ASN A 1 240 ? 18.741 2.581 10.901 1.00 7.72 ? 326 ASN A OD1 1 ATOM 1915 N ND2 . ASN A 1 240 ? 20.077 4.267 11.603 1.00 7.64 ? 326 ASN A ND2 1 ATOM 1916 N N . PRO A 1 241 ? 18.601 0.494 8.640 1.00 8.57 ? 327 PRO A N 1 ATOM 1917 C CA . PRO A 1 241 ? 17.564 0.606 7.610 1.00 9.11 ? 327 PRO A CA 1 ATOM 1918 C C . PRO A 1 241 ? 16.983 2.022 7.517 1.00 8.51 ? 327 PRO A C 1 ATOM 1919 O O . PRO A 1 241 ? 16.443 2.412 6.475 1.00 9.47 ? 327 PRO A O 1 ATOM 1920 C CB . PRO A 1 241 ? 16.515 -0.417 8.071 1.00 10.55 ? 327 PRO A CB 1 ATOM 1921 C CG . PRO A 1 241 ? 16.697 -0.482 9.524 1.00 11.73 ? 327 PRO A CG 1 ATOM 1922 C CD . PRO A 1 241 ? 18.189 -0.375 9.741 1.00 9.59 ? 327 PRO A CD 1 ATOM 1923 N N . ASN A 1 242 ? 17.059 2.786 8.599 1.00 7.92 ? 328 ASN A N 1 ATOM 1924 C CA . ASN A 1 242 ? 16.553 4.166 8.640 1.00 7.87 ? 328 ASN A CA 1 ATOM 1925 C C . ASN A 1 242 ? 17.683 5.087 8.280 1.00 7.05 ? 328 ASN A C 1 ATOM 1926 O O . ASN A 1 242 ? 18.277 5.734 9.126 1.00 7.88 ? 328 ASN A O 1 ATOM 1927 C CB . ASN A 1 242 ? 15.924 4.438 9.976 1.00 8.00 ? 328 ASN A CB 1 ATOM 1928 C CG . ASN A 1 242 ? 14.745 3.533 10.219 1.00 8.63 ? 328 ASN A CG 1 ATOM 1929 O OD1 . ASN A 1 242 ? 13.984 3.252 9.261 1.00 10.01 ? 328 ASN A OD1 1 ATOM 1930 N ND2 . ASN A 1 242 ? 14.561 3.070 11.462 1.00 10.46 ? 328 ASN A ND2 1 ATOM 1931 N N . TYR A 1 243 ? 17.992 5.149 6.980 1.00 7.25 ? 329 TYR A N 1 ATOM 1932 C CA . TYR A 1 243 ? 19.216 5.797 6.510 1.00 7.38 ? 329 TYR A CA 1 ATOM 1933 C C . TYR A 1 243 ? 19.019 7.225 6.109 1.00 6.71 ? 329 TYR A C 1 ATOM 1934 O O . TYR A 1 243 ? 19.982 7.912 5.754 1.00 8.24 ? 329 TYR A O 1 ATOM 1935 C CB . TYR A 1 243 ? 19.856 4.965 5.362 1.00 7.71 ? 329 TYR A CB 1 ATOM 1936 C CG . TYR A 1 243 ? 18.965 4.807 4.149 1.00 8.23 ? 329 TYR A CG 1 ATOM 1937 C CD1 . TYR A 1 243 ? 18.833 5.861 3.262 1.00 9.48 ? 329 TYR A CD1 1 ATOM 1938 C CD2 . TYR A 1 243 ? 18.231 3.675 3.914 1.00 11.49 ? 329 TYR A CD2 1 ATOM 1939 C CE1 . TYR A 1 243 ? 18.060 5.842 2.147 1.00 13.02 ? 329 TYR A CE1 1 ATOM 1940 C CE2 . TYR A 1 243 ? 17.361 3.628 2.729 1.00 13.94 ? 329 TYR A CE2 1 ATOM 1941 C CZ . TYR A 1 243 ? 17.320 4.760 1.922 1.00 13.26 ? 329 TYR A CZ 1 ATOM 1942 O OH . TYR A 1 243 ? 16.471 4.737 0.801 1.00 17.11 ? 329 TYR A OH 1 ATOM 1943 N N . ASP A 1 244 ? 17.799 7.722 6.174 1.00 6.84 ? 330 ASP A N 1 ATOM 1944 C CA . ASP A 1 244 ? 17.440 9.108 5.897 1.00 6.53 ? 330 ASP A CA 1 ATOM 1945 C C . ASP A 1 244 ? 16.309 9.502 6.862 1.00 6.08 ? 330 ASP A C 1 ATOM 1946 O O . ASP A 1 244 ? 15.759 8.658 7.603 1.00 6.51 ? 330 ASP A O 1 ATOM 1947 C CB . ASP A 1 244 ? 17.136 9.355 4.417 1.00 6.80 ? 330 ASP A CB 1 ATOM 1948 C CG . ASP A 1 244 ? 15.992 8.557 3.853 1.00 7.22 ? 330 ASP A CG 1 ATOM 1949 O OD1 . ASP A 1 244 ? 15.139 8.070 4.644 1.00 7.59 ? 330 ASP A OD1 1 ATOM 1950 O OD2 . ASP A 1 244 ? 15.915 8.414 2.585 1.00 7.90 ? 330 ASP A OD2 1 ATOM 1951 N N . GLU A 1 245 ? 16.006 10.791 6.882 1.00 6.10 ? 331 GLU A N 1 ATOM 1952 C CA . GLU A 1 245 ? 15.044 11.292 7.848 1.00 5.94 ? 331 GLU A CA 1 ATOM 1953 C C . GLU A 1 245 ? 13.629 10.807 7.530 1.00 5.94 ? 331 GLU A C 1 ATOM 1954 O O . GLU A 1 245 ? 12.840 10.602 8.466 1.00 6.29 ? 331 GLU A O 1 ATOM 1955 C CB . GLU A 1 245 ? 15.118 12.812 7.983 1.00 6.05 ? 331 GLU A CB 1 ATOM 1956 C CG . GLU A 1 245 ? 16.452 13.252 8.568 1.00 6.19 ? 331 GLU A CG 1 ATOM 1957 C CD . GLU A 1 245 ? 16.678 12.761 9.981 1.00 6.14 ? 331 GLU A CD 1 ATOM 1958 O OE1 . GLU A 1 245 ? 15.805 12.981 10.828 1.00 7.74 ? 331 GLU A OE1 1 ATOM 1959 O OE2 . GLU A 1 245 ? 17.758 12.166 10.219 1.00 7.54 ? 331 GLU A OE2 1 ATOM 1960 N N . LYS A 1 246 ? 13.280 10.613 6.259 1.00 5.98 ? 332 LYS A N 1 ATOM 1961 C CA . LYS A 1 246 ? 11.935 10.070 5.949 1.00 6.35 ? 332 LYS A CA 1 ATOM 1962 C C . LYS A 1 246 ? 11.777 8.696 6.553 1.00 6.21 ? 332 LYS A C 1 ATOM 1963 O O . LYS A 1 246 ? 10.743 8.392 7.134 1.00 6.65 ? 332 LYS A O 1 ATOM 1964 C CB . LYS A 1 246 ? 11.753 10.062 4.415 1.00 6.43 ? 332 LYS A CB 1 ATOM 1965 C CG . LYS A 1 246 ? 10.405 9.483 3.997 1.00 7.26 ? 332 LYS A CG 1 ATOM 1966 C CD . LYS A 1 246 ? 10.186 9.587 2.521 1.00 8.14 ? 332 LYS A CD 1 ATOM 1967 C CE . LYS A 1 246 ? 8.865 8.988 2.031 1.00 8.62 ? 332 LYS A CE 1 ATOM 1968 N NZ . LYS A 1 246 ? 8.818 7.499 2.215 1.00 9.23 ? 332 LYS A NZ 1 ATOM 1969 N N . HIS A 1 247 ? 12.763 7.820 6.373 1.00 6.54 ? 333 HIS A N 1 ATOM 1970 C CA . HIS A 1 247 ? 12.656 6.490 6.983 1.00 6.65 ? 333 HIS A CA 1 ATOM 1971 C C . HIS A 1 247 ? 12.516 6.582 8.505 1.00 6.33 ? 333 HIS A C 1 ATOM 1972 O O . HIS A 1 247 ? 11.700 5.888 9.109 1.00 7.01 ? 333 HIS A O 1 ATOM 1973 C CB . HIS A 1 247 ? 13.831 5.571 6.662 1.00 6.72 ? 333 HIS A CB 1 ATOM 1974 C CG . HIS A 1 247 ? 13.836 4.974 5.288 1.00 7.59 ? 333 HIS A CG 1 ATOM 1975 N ND1 . HIS A 1 247 ? 14.199 5.678 4.153 1.00 8.26 ? 333 HIS A ND1 1 ATOM 1976 C CD2 . HIS A 1 247 ? 13.521 3.717 4.882 1.00 9.37 ? 333 HIS A CD2 1 ATOM 1977 C CE1 . HIS A 1 247 ? 14.122 4.837 3.106 1.00 9.04 ? 333 HIS A CE1 1 ATOM 1978 N NE2 . HIS A 1 247 ? 13.709 3.659 3.517 1.00 10.02 ? 333 HIS A NE2 1 ATOM 1979 N N . TYR A 1 248 ? 13.350 7.414 9.135 1.00 6.29 ? 334 TYR A N 1 ATOM 1980 C CA . TYR A 1 248 ? 13.308 7.587 10.566 1.00 6.06 ? 334 TYR A CA 1 ATOM 1981 C C . TYR A 1 248 ? 11.917 8.034 11.023 1.00 6.11 ? 334 TYR A C 1 ATOM 1982 O O . TYR A 1 248 ? 11.308 7.402 11.902 1.00 6.53 ? 334 TYR A O 1 ATOM 1983 C CB . TYR A 1 248 ? 14.380 8.583 10.979 1.00 6.80 ? 334 TYR A CB 1 ATOM 1984 C CG . TYR A 1 248 ? 14.388 9.052 12.425 1.00 6.04 ? 334 TYR A CG 1 ATOM 1985 C CD1 . TYR A 1 248 ? 14.037 8.230 13.490 1.00 6.37 ? 334 TYR A CD1 1 ATOM 1986 C CD2 . TYR A 1 248 ? 14.839 10.334 12.739 1.00 6.12 ? 334 TYR A CD2 1 ATOM 1987 C CE1 . TYR A 1 248 ? 14.105 8.687 14.795 1.00 6.13 ? 334 TYR A CE1 1 ATOM 1988 C CE2 . TYR A 1 248 ? 14.912 10.786 14.043 1.00 6.01 ? 334 TYR A CE2 1 ATOM 1989 C CZ . TYR A 1 248 ? 14.549 9.949 15.080 1.00 5.85 ? 334 TYR A CZ 1 ATOM 1990 O OH . TYR A 1 248 ? 14.567 10.364 16.388 1.00 6.95 ? 334 TYR A OH 1 ATOM 1991 N N . ILE A 1 249 ? 11.397 9.099 10.428 1.00 5.76 ? 335 ILE A N 1 ATOM 1992 C CA . ILE A 1 249 ? 10.105 9.663 10.835 1.00 6.34 ? 335 ILE A CA 1 ATOM 1993 C C . ILE A 1 249 ? 8.995 8.703 10.598 1.00 6.18 ? 335 ILE A C 1 ATOM 1994 O O . ILE A 1 249 ? 8.087 8.584 11.442 1.00 7.30 ? 335 ILE A O 1 ATOM 1995 C CB . ILE A 1 249 ? 9.926 11.030 10.205 1.00 7.23 ? 335 ILE A CB 1 ATOM 1996 C CG1 . ILE A 1 249 ? 10.890 12.027 10.887 1.00 7.53 ? 335 ILE A CG1 1 ATOM 1997 C CG2 . ILE A 1 249 ? 8.485 11.508 10.208 1.00 8.80 ? 335 ILE A CG2 1 ATOM 1998 C CD1 . ILE A 1 249 ? 11.101 13.318 10.157 1.00 8.81 ? 335 ILE A CD1 1 ATOM 1999 N N . GLU A 1 250 ? 8.992 8.008 9.468 1.00 6.85 ? 336 GLU A N 1 ATOM 2000 C CA . GLU A 1 250 ? 7.909 7.052 9.194 1.00 6.97 ? 336 GLU A CA 1 ATOM 2001 C C . GLU A 1 250 ? 7.939 5.876 10.162 1.00 7.51 ? 336 GLU A C 1 ATOM 2002 O O . GLU A 1 250 ? 6.871 5.318 10.453 1.00 9.04 ? 336 GLU A O 1 ATOM 2003 C CB . GLU A 1 250 ? 7.944 6.623 7.720 1.00 7.30 ? 336 GLU A CB 1 ATOM 2004 C CG . GLU A 1 250 ? 7.509 7.741 6.802 1.00 7.81 ? 336 GLU A CG 1 ATOM 2005 C CD . GLU A 1 250 ? 7.502 7.461 5.329 1.00 7.52 ? 336 GLU A CD 1 ATOM 2006 O OE1 . GLU A 1 250 ? 8.152 6.535 4.865 1.00 9.39 ? 336 GLU A OE1 1 ATOM 2007 O OE2 . GLU A 1 250 ? 6.840 8.226 4.579 1.00 9.40 ? 336 GLU A OE2 1 ATOM 2008 N N . ALA A 1 251 ? 9.112 5.500 10.653 1.00 6.82 ? 337 ALA A N 1 ATOM 2009 C CA . ALA A 1 251 ? 9.186 4.464 11.672 1.00 7.57 ? 337 ALA A CA 1 ATOM 2010 C C . ALA A 1 251 ? 8.881 4.969 13.067 1.00 7.09 ? 337 ALA A C 1 ATOM 2011 O O . ALA A 1 251 ? 8.353 4.235 13.939 1.00 8.80 ? 337 ALA A O 1 ATOM 2012 C CB . ALA A 1 251 ? 10.589 3.821 11.665 1.00 8.28 ? 337 ALA A CB 1 ATOM 2013 N N . PHE A 1 252 ? 9.224 6.222 13.346 1.00 6.67 ? 338 PHE A N 1 ATOM 2014 C CA . PHE A 1 252 ? 9.144 6.773 14.693 1.00 6.73 ? 338 PHE A CA 1 ATOM 2015 C C . PHE A 1 252 ? 7.743 7.242 15.054 1.00 6.43 ? 338 PHE A C 1 ATOM 2016 O O . PHE A 1 252 ? 7.259 6.975 16.171 1.00 6.79 ? 338 PHE A O 1 ATOM 2017 C CB . PHE A 1 252 ? 10.152 7.941 14.745 1.00 6.84 ? 338 PHE A CB 1 ATOM 2018 C CG . PHE A 1 252 ? 10.499 8.552 16.074 1.00 6.75 ? 338 PHE A CG 1 ATOM 2019 C CD1 . PHE A 1 252 ? 10.427 7.867 17.290 1.00 7.24 ? 338 PHE A CD1 1 ATOM 2020 C CD2 . PHE A 1 252 ? 11.038 9.826 16.077 1.00 6.73 ? 338 PHE A CD2 1 ATOM 2021 C CE1 . PHE A 1 252 ? 10.867 8.482 18.452 1.00 7.35 ? 338 PHE A CE1 1 ATOM 2022 C CE2 . PHE A 1 252 ? 11.467 10.420 17.240 1.00 7.51 ? 338 PHE A CE2 1 ATOM 2023 C CZ . PHE A 1 252 ? 11.403 9.740 18.409 1.00 8.05 ? 338 PHE A CZ 1 ATOM 2024 N N . ARG A 1 253 ? 7.079 7.912 14.124 1.00 6.94 ? 339 ARG A N 1 ATOM 2025 C CA . ARG A 1 253 ? 5.742 8.461 14.399 1.00 7.39 ? 339 ARG A CA 1 ATOM 2026 C C . ARG A 1 253 ? 4.765 7.392 14.908 1.00 6.97 ? 339 ARG A C 1 ATOM 2027 O O . ARG A 1 253 ? 4.068 7.652 15.891 1.00 7.52 ? 339 ARG A O 1 ATOM 2028 C CB . ARG A 1 253 ? 5.206 9.211 13.159 1.00 7.70 ? 339 ARG A CB 1 ATOM 2029 C CG . ARG A 1 253 ? 3.725 9.562 13.233 1.00 8.50 ? 339 ARG A CG 1 ATOM 2030 C CD . ARG A 1 253 ? 3.337 10.444 14.424 1.00 7.84 ? 339 ARG A CD 1 ATOM 2031 N NE . ARG A 1 253 ? 1.892 10.751 14.340 1.00 8.27 ? 339 ARG A NE 1 ATOM 2032 C CZ . ARG A 1 253 ? 1.374 11.719 13.595 1.00 8.36 ? 339 ARG A CZ 1 ATOM 2033 N NH1 . ARG A 1 253 ? 2.117 12.718 13.174 1.00 9.01 ? 339 ARG A NH1 1 ATOM 2034 N NH2 . ARG A 1 253 ? 0.079 11.706 13.306 1.00 10.92 ? 339 ARG A NH2 1 ATOM 2035 N N . PRO A 1 254 ? 4.656 6.203 14.316 1.00 7.45 ? 340 PRO A N 1 ATOM 2036 C CA . PRO A 1 254 ? 3.631 5.266 14.834 1.00 8.38 ? 340 PRO A CA 1 ATOM 2037 C C . PRO A 1 254 ? 3.931 4.865 16.271 1.00 7.82 ? 340 PRO A C 1 ATOM 2038 O O . PRO A 1 254 ? 2.988 4.626 17.044 1.00 8.81 ? 340 PRO A O 1 ATOM 2039 C CB . PRO A 1 254 ? 3.708 4.056 13.887 1.00 8.71 ? 340 PRO A CB 1 ATOM 2040 C CG . PRO A 1 254 ? 4.907 4.271 13.107 1.00 13.91 ? 340 PRO A CG 1 ATOM 2041 C CD . PRO A 1 254 ? 5.223 5.741 13.045 1.00 8.07 ? 340 PRO A CD 1 ATOM 2042 N N . LEU A 1 255 ? 5.210 4.755 16.644 1.00 7.44 ? 341 LEU A N 1 ATOM 2043 C CA . LEU A 1 255 ? 5.591 4.408 18.003 1.00 8.23 ? 341 LEU A CA 1 ATOM 2044 C C . LEU A 1 255 ? 5.204 5.514 18.993 1.00 7.43 ? 341 LEU A C 1 ATOM 2045 O O . LEU A 1 255 ? 4.745 5.244 20.106 1.00 8.51 ? 341 LEU A O 1 ATOM 2046 C CB . LEU A 1 255 ? 7.072 4.080 18.079 1.00 8.43 ? 341 LEU A CB 1 ATOM 2047 C CG . LEU A 1 255 ? 7.582 2.935 17.161 1.00 10.89 ? 341 LEU A CG 1 ATOM 2048 C CD1 . LEU A 1 255 ? 9.113 2.896 17.125 1.00 12.09 ? 341 LEU A CD1 1 ATOM 2049 C CD2 . LEU A 1 255 ? 7.029 1.630 17.653 1.00 15.32 ? 341 LEU A CD2 1 ATOM 2050 N N . LEU A 1 256 ? 5.488 6.750 18.613 1.00 7.25 ? 342 LEU A N 1 ATOM 2051 C CA . LEU A 1 256 ? 5.124 7.914 19.427 1.00 6.94 ? 342 LEU A CA 1 ATOM 2052 C C . LEU A 1 256 ? 3.603 8.010 19.585 1.00 7.18 ? 342 LEU A C 1 ATOM 2053 O O . LEU A 1 256 ? 3.094 8.249 20.689 1.00 7.29 ? 342 LEU A O 1 ATOM 2054 C CB . LEU A 1 256 ? 5.645 9.182 18.757 1.00 6.85 ? 342 LEU A CB 1 ATOM 2055 C CG . LEU A 1 256 ? 7.157 9.385 18.816 1.00 6.54 ? 342 LEU A CG 1 ATOM 2056 C CD1 . LEU A 1 256 ? 7.619 10.261 17.697 1.00 6.48 ? 342 LEU A CD1 1 ATOM 2057 C CD2 . LEU A 1 256 ? 7.557 9.977 20.170 1.00 7.39 ? 342 LEU A CD2 1 ATOM 2058 N N . GLU A 1 257 ? 2.880 7.809 18.494 1.00 7.21 ? 343 GLU A N 1 ATOM 2059 C CA . GLU A 1 257 ? 1.435 7.969 18.470 1.00 7.32 ? 343 GLU A CA 1 ATOM 2060 C C . GLU A 1 257 ? 0.756 6.912 19.349 1.00 8.06 ? 343 GLU A C 1 ATOM 2061 O O . GLU A 1 257 ? -0.173 7.258 20.104 1.00 8.33 ? 343 GLU A O 1 ATOM 2062 C CB A GLU A 1 257 ? 0.906 8.013 17.066 0.50 8.80 ? 343 GLU A CB 1 ATOM 2063 C CB B GLU A 1 257 ? 0.951 7.834 17.026 0.50 8.19 ? 343 GLU A CB 1 ATOM 2064 C CG A GLU A 1 257 ? -0.604 8.150 17.046 0.50 10.07 ? 343 GLU A CG 1 ATOM 2065 C CG B GLU A 1 257 ? -0.536 8.105 16.800 0.50 10.03 ? 343 GLU A CG 1 ATOM 2066 C CD A GLU A 1 257 ? -1.121 8.801 15.798 0.50 9.42 ? 343 GLU A CD 1 ATOM 2067 C CD B GLU A 1 257 ? -0.909 8.162 15.324 0.50 11.34 ? 343 GLU A CD 1 ATOM 2068 O OE1 A GLU A 1 257 ? -0.356 9.001 14.811 0.50 12.08 ? 343 GLU A OE1 1 ATOM 2069 O OE1 B GLU A 1 257 ? -0.212 8.865 14.563 0.50 10.76 ? 343 GLU A OE1 1 ATOM 2070 O OE2 A GLU A 1 257 ? -2.351 9.089 15.752 0.50 11.82 ? 343 GLU A OE2 1 ATOM 2071 O OE2 B GLU A 1 257 ? -1.956 7.582 14.912 0.50 15.44 ? 343 GLU A OE2 1 ATOM 2072 N N . ALA A 1 258 ? 1.210 5.677 19.285 1.00 7.55 ? 344 ALA A N 1 ATOM 2073 C CA . ALA A 1 258 ? 0.624 4.639 20.156 1.00 8.16 ? 344 ALA A CA 1 ATOM 2074 C C . ALA A 1 258 ? 0.844 4.958 21.622 1.00 7.83 ? 344 ALA A C 1 ATOM 2075 O O . ALA A 1 258 ? 0.088 4.444 22.460 1.00 8.84 ? 344 ALA A O 1 ATOM 2076 C CB . ALA A 1 258 ? 1.218 3.303 19.819 1.00 8.76 ? 344 ALA A CB 1 ATOM 2077 N N . ARG A 1 259 ? 1.836 5.780 21.914 1.00 7.64 ? 345 ARG A N 1 ATOM 2078 C CA . ARG A 1 259 ? 2.205 6.188 23.248 1.00 8.15 ? 345 ARG A CA 1 ATOM 2079 C C . ARG A 1 259 ? 1.620 7.562 23.595 1.00 7.84 ? 345 ARG A C 1 ATOM 2080 O O . ARG A 1 259 ? 2.011 8.140 24.633 1.00 8.76 ? 345 ARG A O 1 ATOM 2081 C CB . ARG A 1 259 ? 3.707 6.058 23.455 1.00 8.24 ? 345 ARG A CB 1 ATOM 2082 C CG . ARG A 1 259 ? 4.110 4.601 23.389 1.00 8.35 ? 345 ARG A CG 1 ATOM 2083 C CD . ARG A 1 259 ? 5.595 4.354 23.305 1.00 9.95 ? 345 ARG A CD 1 ATOM 2084 N NE . ARG A 1 259 ? 5.871 2.910 23.278 1.00 10.51 ? 345 ARG A NE 1 ATOM 2085 C CZ . ARG A 1 259 ? 5.583 2.101 22.257 1.00 10.48 ? 345 ARG A CZ 1 ATOM 2086 N NH1 . ARG A 1 259 ? 5.241 2.546 21.064 1.00 10.48 ? 345 ARG A NH1 1 ATOM 2087 N NH2 . ARG A 1 259 ? 5.718 0.759 22.461 1.00 12.50 ? 345 ARG A NH2 1 ATOM 2088 N N . GLY A 1 260 ? 0.708 8.075 22.805 1.00 7.90 ? 346 GLY A N 1 ATOM 2089 C CA . GLY A 1 260 ? -0.020 9.259 23.168 1.00 7.80 ? 346 GLY A CA 1 ATOM 2090 C C . GLY A 1 260 ? 0.425 10.542 22.541 1.00 7.33 ? 346 GLY A C 1 ATOM 2091 O O . GLY A 1 260 ? -0.160 11.593 22.813 1.00 7.68 ? 346 GLY A O 1 ATOM 2092 N N . PHE A 1 261 ? 1.457 10.495 21.672 1.00 7.25 ? 347 PHE A N 1 ATOM 2093 C CA . PHE A 1 261 ? 2.095 11.720 21.168 1.00 6.94 ? 347 PHE A CA 1 ATOM 2094 C C . PHE A 1 261 ? 2.135 11.660 19.636 1.00 7.21 ? 347 PHE A C 1 ATOM 2095 O O . PHE A 1 261 ? 3.093 11.126 19.048 1.00 7.63 ? 347 PHE A O 1 ATOM 2096 C CB . PHE A 1 261 ? 3.503 11.834 21.727 1.00 7.28 ? 347 PHE A CB 1 ATOM 2097 C CG . PHE A 1 261 ? 4.254 13.100 21.426 1.00 6.91 ? 347 PHE A CG 1 ATOM 2098 C CD1 . PHE A 1 261 ? 3.666 14.240 20.885 1.00 7.34 ? 347 PHE A CD1 1 ATOM 2099 C CD2 . PHE A 1 261 ? 5.598 13.171 21.763 1.00 6.94 ? 347 PHE A CD2 1 ATOM 2100 C CE1 . PHE A 1 261 ? 4.388 15.413 20.702 1.00 7.17 ? 347 PHE A CE1 1 ATOM 2101 C CE2 . PHE A 1 261 ? 6.325 14.335 21.566 1.00 7.37 ? 347 PHE A CE2 1 ATOM 2102 C CZ . PHE A 1 261 ? 5.722 15.448 21.060 1.00 7.03 ? 347 PHE A CZ 1 ATOM 2103 N N . PRO A 1 262 ? 1.114 12.162 18.950 1.00 7.75 ? 348 PRO A N 1 ATOM 2104 C CA . PRO A 1 262 ? 1.038 12.106 17.476 1.00 8.28 ? 348 PRO A CA 1 ATOM 2105 C C . PRO A 1 262 ? 1.882 13.235 16.920 1.00 7.81 ? 348 PRO A C 1 ATOM 2106 O O . PRO A 1 262 ? 1.404 14.182 16.294 1.00 8.51 ? 348 PRO A O 1 ATOM 2107 C CB . PRO A 1 262 ? -0.453 12.254 17.195 1.00 9.78 ? 348 PRO A CB 1 ATOM 2108 C CG . PRO A 1 262 ? -0.937 13.101 18.284 1.00 11.51 ? 348 PRO A CG 1 ATOM 2109 C CD . PRO A 1 262 ? -0.176 12.644 19.521 1.00 10.02 ? 348 PRO A CD 1 ATOM 2110 N N . ALA A 1 263 ? 3.203 13.151 17.109 1.00 7.23 ? 349 ALA A N 1 ATOM 2111 C CA . ALA A 1 263 ? 4.112 14.237 16.842 1.00 6.46 ? 349 ALA A CA 1 ATOM 2112 C C . ALA A 1 263 ? 4.191 14.563 15.373 1.00 6.54 ? 349 ALA A C 1 ATOM 2113 O O . ALA A 1 263 ? 4.413 13.664 14.530 1.00 7.46 ? 349 ALA A O 1 ATOM 2114 C CB . ALA A 1 263 ? 5.473 13.853 17.361 1.00 6.84 ? 349 ALA A CB 1 ATOM 2115 N N . GLN A 1 264 ? 4.089 15.846 15.041 1.00 6.24 ? 350 GLN A N 1 ATOM 2116 C CA . GLN A 1 264 ? 4.513 16.364 13.762 1.00 6.36 ? 350 GLN A CA 1 ATOM 2117 C C . GLN A 1 264 ? 5.982 16.757 13.807 1.00 6.16 ? 350 GLN A C 1 ATOM 2118 O O . GLN A 1 264 ? 6.507 17.034 14.903 1.00 8.13 ? 350 GLN A O 1 ATOM 2119 C CB . GLN A 1 264 ? 3.649 17.550 13.342 1.00 6.51 ? 350 GLN A CB 1 ATOM 2120 C CG . GLN A 1 264 ? 2.204 17.159 13.077 1.00 7.41 ? 350 GLN A CG 1 ATOM 2121 C CD . GLN A 1 264 ? 2.045 16.383 11.789 1.00 7.20 ? 350 GLN A CD 1 ATOM 2122 O OE1 . GLN A 1 264 ? 1.675 15.206 11.787 1.00 9.41 ? 350 GLN A OE1 1 ATOM 2123 N NE2 . GLN A 1 264 ? 2.291 17.015 10.656 1.00 8.42 ? 350 GLN A NE2 1 ATOM 2124 N N . PHE A 1 265 ? 6.639 16.804 12.683 1.00 5.70 ? 351 PHE A N 1 ATOM 2125 C CA . PHE A 1 265 ? 8.078 17.009 12.639 1.00 5.66 ? 351 PHE A CA 1 ATOM 2126 C C . PHE A 1 265 ? 8.478 18.216 11.849 1.00 5.83 ? 351 PHE A C 1 ATOM 2127 O O . PHE A 1 265 ? 7.822 18.598 10.870 1.00 6.17 ? 351 PHE A O 1 ATOM 2128 C CB . PHE A 1 265 ? 8.774 15.775 11.992 1.00 5.78 ? 351 PHE A CB 1 ATOM 2129 C CG . PHE A 1 265 ? 8.705 14.562 12.878 1.00 5.96 ? 351 PHE A CG 1 ATOM 2130 C CD1 . PHE A 1 265 ? 7.581 13.760 12.975 1.00 7.13 ? 351 PHE A CD1 1 ATOM 2131 C CD2 . PHE A 1 265 ? 9.799 14.222 13.642 1.00 6.51 ? 351 PHE A CD2 1 ATOM 2132 C CE1 . PHE A 1 265 ? 7.553 12.683 13.866 1.00 8.25 ? 351 PHE A CE1 1 ATOM 2133 C CE2 . PHE A 1 265 ? 9.773 13.116 14.492 1.00 7.04 ? 351 PHE A CE2 1 ATOM 2134 C CZ . PHE A 1 265 ? 8.653 12.362 14.590 1.00 8.28 ? 351 PHE A CZ 1 ATOM 2135 N N . ILE A 1 266 ? 9.615 18.799 12.235 1.00 5.60 ? 352 ILE A N 1 ATOM 2136 C CA . ILE A 1 266 ? 10.365 19.675 11.372 1.00 5.37 ? 352 ILE A CA 1 ATOM 2137 C C . ILE A 1 266 ? 11.718 19.052 11.184 1.00 5.39 ? 352 ILE A C 1 ATOM 2138 O O . ILE A 1 266 ? 12.275 18.438 12.122 1.00 6.19 ? 352 ILE A O 1 ATOM 2139 C CB . ILE A 1 266 ? 10.430 21.135 11.845 1.00 5.80 ? 352 ILE A CB 1 ATOM 2140 C CG1 . ILE A 1 266 ? 11.124 21.300 13.182 1.00 6.54 ? 352 ILE A CG1 1 ATOM 2141 C CG2 . ILE A 1 266 ? 9.022 21.718 11.878 1.00 6.71 ? 352 ILE A CG2 1 ATOM 2142 C CD1 . ILE A 1 266 ? 11.243 22.769 13.637 1.00 7.60 ? 352 ILE A CD1 1 ATOM 2143 N N . VAL A 1 267 ? 12.292 19.182 9.988 1.00 5.65 ? 353 VAL A N 1 ATOM 2144 C CA . VAL A 1 267 ? 13.539 18.504 9.619 1.00 5.32 ? 353 VAL A CA 1 ATOM 2145 C C . VAL A 1 267 ? 14.527 19.533 9.147 1.00 5.28 ? 353 VAL A C 1 ATOM 2146 O O . VAL A 1 267 ? 14.279 20.231 8.133 1.00 5.73 ? 353 VAL A O 1 ATOM 2147 C CB . VAL A 1 267 ? 13.295 17.412 8.555 1.00 5.91 ? 353 VAL A CB 1 ATOM 2148 C CG1 . VAL A 1 267 ? 14.597 16.727 8.259 1.00 7.19 ? 353 VAL A CG1 1 ATOM 2149 C CG2 . VAL A 1 267 ? 12.263 16.421 9.016 1.00 6.62 ? 353 VAL A CG2 1 ATOM 2150 N N . ASP A 1 268 ? 15.689 19.629 9.817 1.00 5.40 ? 354 ASP A N 1 ATOM 2151 C CA . ASP A 1 268 ? 16.765 20.507 9.334 1.00 5.65 ? 354 ASP A CA 1 ATOM 2152 C C . ASP A 1 268 ? 17.269 19.969 8.006 1.00 5.24 ? 354 ASP A C 1 ATOM 2153 O O . ASP A 1 268 ? 17.578 18.777 7.888 1.00 6.09 ? 354 ASP A O 1 ATOM 2154 C CB . ASP A 1 268 ? 17.890 20.543 10.410 1.00 5.48 ? 354 ASP A CB 1 ATOM 2155 C CG . ASP A 1 268 ? 18.840 21.704 10.318 1.00 5.46 ? 354 ASP A CG 1 ATOM 2156 O OD1 . ASP A 1 268 ? 18.780 22.470 9.303 1.00 5.77 ? 354 ASP A OD1 1 ATOM 2157 O OD2 . ASP A 1 268 ? 19.611 21.921 11.293 1.00 5.81 ? 354 ASP A OD2 1 ATOM 2158 N N . GLN A 1 269 ? 17.399 20.861 7.041 1.00 5.32 ? 355 GLN A N 1 ATOM 2159 C CA . GLN A 1 269 ? 18.005 20.579 5.745 1.00 5.67 ? 355 GLN A CA 1 ATOM 2160 C C . GLN A 1 269 ? 19.050 21.626 5.377 1.00 5.56 ? 355 GLN A C 1 ATOM 2161 O O . GLN A 1 269 ? 19.507 21.651 4.217 1.00 6.38 ? 355 GLN A O 1 ATOM 2162 C CB . GLN A 1 269 ? 16.948 20.422 4.630 1.00 6.31 ? 355 GLN A CB 1 ATOM 2163 C CG . GLN A 1 269 ? 16.074 19.167 4.773 1.00 6.02 ? 355 GLN A CG 1 ATOM 2164 C CD . GLN A 1 269 ? 16.838 17.915 4.434 1.00 6.98 ? 355 GLN A CD 1 ATOM 2165 O OE1 . GLN A 1 269 ? 17.070 17.635 3.239 1.00 8.46 ? 355 GLN A OE1 1 ATOM 2166 N NE2 . GLN A 1 269 ? 17.263 17.162 5.441 1.00 7.13 ? 355 GLN A NE2 1 ATOM 2167 N N . GLY A 1 270 ? 19.422 22.484 6.312 1.00 5.75 ? 356 GLY A N 1 ATOM 2168 C CA . GLY A 1 270 ? 20.300 23.565 5.986 1.00 6.06 ? 356 GLY A CA 1 ATOM 2169 C C . GLY A 1 270 ? 21.681 23.180 5.510 1.00 5.29 ? 356 GLY A C 1 ATOM 2170 O O . GLY A 1 270 ? 22.336 24.007 4.848 1.00 6.74 ? 356 GLY A O 1 ATOM 2171 N N . ARG A 1 271 ? 22.154 21.974 5.820 1.00 5.55 ? 357 ARG A N 1 ATOM 2172 C CA . ARG A 1 271 ? 23.433 21.464 5.333 1.00 5.72 ? 357 ARG A CA 1 ATOM 2173 C C . ARG A 1 271 ? 23.297 20.089 4.709 1.00 5.81 ? 357 ARG A C 1 ATOM 2174 O O . ARG A 1 271 ? 24.222 19.284 4.725 1.00 5.90 ? 357 ARG A O 1 ATOM 2175 C CB . ARG A 1 271 ? 24.505 21.541 6.433 1.00 5.73 ? 357 ARG A CB 1 ATOM 2176 C CG . ARG A 1 271 ? 24.690 22.905 7.006 1.00 6.38 ? 357 ARG A CG 1 ATOM 2177 C CD . ARG A 1 271 ? 25.896 23.040 7.912 1.00 6.82 ? 357 ARG A CD 1 ATOM 2178 N NE . ARG A 1 271 ? 25.732 22.299 9.162 1.00 6.14 ? 357 ARG A NE 1 ATOM 2179 C CZ . ARG A 1 271 ? 26.712 22.097 10.040 1.00 6.04 ? 357 ARG A CZ 1 ATOM 2180 N NH1 . ARG A 1 271 ? 27.900 22.623 9.841 1.00 7.16 ? 357 ARG A NH1 1 ATOM 2181 N NH2 . ARG A 1 271 ? 26.512 21.370 11.116 1.00 6.63 ? 357 ARG A NH2 1 ATOM 2182 N N . SER A 1 272 ? 22.122 19.838 4.099 1.00 5.53 ? 358 SER A N 1 ATOM 2183 C CA . SER A 1 272 ? 21.764 18.535 3.550 1.00 5.76 ? 358 SER A CA 1 ATOM 2184 C C . SER A 1 272 ? 21.691 18.473 2.044 1.00 5.93 ? 358 SER A C 1 ATOM 2185 O O . SER A 1 272 ? 21.293 17.447 1.485 1.00 6.71 ? 358 SER A O 1 ATOM 2186 C CB . SER A 1 272 ? 20.419 18.094 4.106 1.00 5.83 ? 358 SER A CB 1 ATOM 2187 O OG . SER A 1 272 ? 20.496 17.867 5.520 1.00 6.50 ? 358 SER A OG 1 ATOM 2188 N N . GLY A 1 273 ? 22.029 19.559 1.329 1.00 5.75 ? 359 GLY A N 1 ATOM 2189 C CA . GLY A 1 273 ? 21.794 19.561 -0.095 1.00 6.34 ? 359 GLY A CA 1 ATOM 2190 C C . GLY A 1 273 ? 22.589 18.559 -0.898 1.00 6.73 ? 359 GLY A C 1 ATOM 2191 O O . GLY A 1 273 ? 22.098 18.086 -1.965 1.00 8.53 ? 359 GLY A O 1 ATOM 2192 N N . LYS A 1 274 ? 23.793 18.251 -0.481 1.00 6.50 ? 360 LYS A N 1 ATOM 2193 C CA . LYS A 1 274 ? 24.639 17.253 -1.137 1.00 6.91 ? 360 LYS A CA 1 ATOM 2194 C C . LYS A 1 274 ? 24.562 15.926 -0.408 1.00 6.05 ? 360 LYS A C 1 ATOM 2195 O O . LYS A 1 274 ? 24.828 15.829 0.782 1.00 6.67 ? 360 LYS A O 1 ATOM 2196 C CB . LYS A 1 274 ? 26.067 17.747 -1.207 1.00 7.09 ? 360 LYS A CB 1 ATOM 2197 C CG . LYS A 1 274 ? 26.988 16.706 -1.836 1.00 7.21 ? 360 LYS A CG 1 ATOM 2198 C CD . LYS A 1 274 ? 28.398 17.181 -2.036 1.00 8.03 ? 360 LYS A CD 1 ATOM 2199 C CE . LYS A 1 274 ? 29.365 16.044 -2.293 1.00 8.96 ? 360 LYS A CE 1 ATOM 2200 N NZ . LYS A 1 274 ? 29.470 15.142 -1.113 1.00 9.24 ? 360 LYS A NZ 1 ATOM 2201 N N . GLN A 1 275 ? 24.188 14.889 -1.171 1.00 6.97 ? 361 GLN A N 1 ATOM 2202 C CA . GLN A 1 275 ? 24.076 13.538 -0.644 1.00 7.05 ? 361 GLN A CA 1 ATOM 2203 C C . GLN A 1 275 ? 24.763 12.601 -1.624 1.00 7.11 ? 361 GLN A C 1 ATOM 2204 O O . GLN A 1 275 ? 24.532 12.713 -2.852 1.00 8.89 ? 361 GLN A O 1 ATOM 2205 C CB . GLN A 1 275 ? 22.637 13.086 -0.463 1.00 7.11 ? 361 GLN A CB 1 ATOM 2206 C CG . GLN A 1 275 ? 21.891 13.969 0.498 1.00 6.60 ? 361 GLN A CG 1 ATOM 2207 C CD . GLN A 1 275 ? 22.380 13.873 1.934 1.00 6.41 ? 361 GLN A CD 1 ATOM 2208 O OE1 . GLN A 1 275 ? 22.919 12.821 2.323 1.00 7.24 ? 361 GLN A OE1 1 ATOM 2209 N NE2 . GLN A 1 275 ? 22.182 14.938 2.717 1.00 6.44 ? 361 GLN A NE2 1 ATOM 2210 N N . PRO A 1 276 ? 25.522 11.623 -1.168 1.00 7.60 ? 362 PRO A N 1 ATOM 2211 C CA . PRO A 1 276 ? 26.022 11.543 0.217 1.00 7.41 ? 362 PRO A CA 1 ATOM 2212 C C . PRO A 1 276 ? 26.936 12.709 0.529 1.00 6.60 ? 362 PRO A C 1 ATOM 2213 O O . PRO A 1 276 ? 27.348 13.455 -0.366 1.00 7.42 ? 362 PRO A O 1 ATOM 2214 C CB . PRO A 1 276 ? 26.795 10.233 0.195 1.00 8.72 ? 362 PRO A CB 1 ATOM 2215 C CG . PRO A 1 276 ? 27.322 10.159 -1.204 1.00 10.95 ? 362 PRO A CG 1 ATOM 2216 C CD . PRO A 1 276 ? 26.220 10.656 -2.059 1.00 9.27 ? 362 PRO A CD 1 ATOM 2217 N N . THR A 1 277 ? 27.243 12.889 1.806 1.00 6.58 ? 363 THR A N 1 ATOM 2218 C CA . THR A 1 277 ? 28.146 13.918 2.256 1.00 6.39 ? 363 THR A CA 1 ATOM 2219 C C . THR A 1 277 ? 29.610 13.420 2.153 1.00 6.45 ? 363 THR A C 1 ATOM 2220 O O . THR A 1 277 ? 29.877 12.303 1.700 1.00 7.66 ? 363 THR A O 1 ATOM 2221 C CB . THR A 1 277 ? 27.820 14.316 3.691 1.00 6.89 ? 363 THR A CB 1 ATOM 2222 O OG1 . THR A 1 277 ? 28.254 13.220 4.521 1.00 7.03 ? 363 THR A OG1 1 ATOM 2223 C CG2 . THR A 1 277 ? 26.358 14.638 3.913 1.00 7.22 ? 363 THR A CG2 1 ATOM 2224 N N . GLY A 1 278 ? 30.538 14.253 2.604 1.00 6.70 ? 364 GLY A N 1 ATOM 2225 C CA . GLY A 1 278 ? 31.931 13.845 2.796 1.00 6.98 ? 364 GLY A CA 1 ATOM 2226 C C . GLY A 1 278 ? 32.231 13.295 4.177 1.00 7.03 ? 364 GLY A C 1 ATOM 2227 O O . GLY A 1 278 ? 33.415 13.108 4.520 1.00 7.85 ? 364 GLY A O 1 ATOM 2228 N N . GLN A 1 279 ? 31.233 13.024 5.005 1.00 6.97 ? 365 GLN A N 1 ATOM 2229 C CA . GLN A 1 279 ? 31.473 12.327 6.258 1.00 7.17 ? 365 GLN A CA 1 ATOM 2230 C C . GLN A 1 279 ? 32.054 10.958 5.988 1.00 7.22 ? 365 GLN A C 1 ATOM 2231 O O . GLN A 1 279 ? 31.511 10.206 5.181 1.00 8.29 ? 365 GLN A O 1 ATOM 2232 C CB . GLN A 1 279 ? 30.156 12.171 7.039 1.00 6.99 ? 365 GLN A CB 1 ATOM 2233 C CG . GLN A 1 279 ? 29.584 13.494 7.553 1.00 7.16 ? 365 GLN A CG 1 ATOM 2234 C CD . GLN A 1 279 ? 28.135 13.355 7.951 1.00 6.59 ? 365 GLN A CD 1 ATOM 2235 O OE1 . GLN A 1 279 ? 27.265 13.216 7.089 1.00 7.28 ? 365 GLN A OE1 1 ATOM 2236 N NE2 . GLN A 1 279 ? 27.854 13.326 9.267 1.00 7.29 ? 365 GLN A NE2 1 ATOM 2237 N N . LYS A 1 280 ? 33.061 10.571 6.768 1.00 7.14 ? 366 LYS A N 1 ATOM 2238 C CA . LYS A 1 280 ? 33.583 9.212 6.735 1.00 8.05 ? 366 LYS A CA 1 ATOM 2239 C C . LYS A 1 280 ? 32.804 8.302 7.637 1.00 7.41 ? 366 LYS A C 1 ATOM 2240 O O . LYS A 1 280 ? 32.787 7.068 7.439 1.00 8.97 ? 366 LYS A O 1 ATOM 2241 C CB . LYS A 1 280 ? 35.050 9.189 7.079 1.00 8.96 ? 366 LYS A CB 1 ATOM 2242 C CG . LYS A 1 280 ? 35.904 9.851 6.030 1.00 12.74 ? 366 LYS A CG 1 ATOM 2243 C CD . LYS A 1 280 ? 35.938 9.026 4.783 1.00 20.41 ? 366 LYS A CD 1 ATOM 2244 C CE . LYS A 1 280 ? 36.901 7.813 4.924 1.00 28.58 ? 366 LYS A CE 1 ATOM 2245 N NZ . LYS A 1 280 ? 38.309 8.145 4.572 1.00 35.06 ? 366 LYS A NZ 1 ATOM 2246 N N . GLU A 1 281 ? 32.202 8.864 8.682 1.00 6.74 ? 367 GLU A N 1 ATOM 2247 C CA . GLU A 1 281 ? 31.341 8.111 9.613 1.00 6.60 ? 367 GLU A CA 1 ATOM 2248 C C . GLU A 1 281 ? 30.174 9.023 9.958 1.00 6.34 ? 367 GLU A C 1 ATOM 2249 O O . GLU A 1 281 ? 30.282 10.238 9.965 1.00 6.98 ? 367 GLU A O 1 ATOM 2250 C CB . GLU A 1 281 ? 32.054 7.720 10.911 1.00 7.22 ? 367 GLU A CB 1 ATOM 2251 C CG . GLU A 1 281 ? 33.333 6.935 10.690 1.00 8.18 ? 367 GLU A CG 1 ATOM 2252 C CD . GLU A 1 281 ? 33.132 5.538 10.175 1.00 9.21 ? 367 GLU A CD 1 ATOM 2253 O OE1 . GLU A 1 281 ? 32.013 5.010 10.141 1.00 10.34 ? 367 GLU A OE1 1 ATOM 2254 O OE2 . GLU A 1 281 ? 34.200 4.949 9.790 1.00 10.02 ? 367 GLU A OE2 1 ATOM 2255 N N . TRP A 1 282 ? 29.055 8.393 10.308 1.00 6.64 ? 368 TRP A N 1 ATOM 2256 C CA . TRP A 1 282 ? 27.817 9.123 10.524 1.00 7.07 ? 368 TRP A CA 1 ATOM 2257 C C . TRP A 1 282 ? 27.888 10.048 11.715 1.00 6.60 ? 368 TRP A C 1 ATOM 2258 O O . TRP A 1 282 ? 27.270 11.122 11.726 1.00 7.87 ? 368 TRP A O 1 ATOM 2259 C CB . TRP A 1 282 ? 26.659 8.140 10.653 1.00 6.91 ? 368 TRP A CB 1 ATOM 2260 C CG . TRP A 1 282 ? 25.316 8.654 10.259 1.00 6.36 ? 368 TRP A CG 1 ATOM 2261 C CD1 . TRP A 1 282 ? 24.940 9.909 9.909 1.00 7.21 ? 368 TRP A CD1 1 ATOM 2262 C CD2 . TRP A 1 282 ? 24.166 7.837 10.097 1.00 6.77 ? 368 TRP A CD2 1 ATOM 2263 N NE1 . TRP A 1 282 ? 23.615 9.930 9.537 1.00 7.22 ? 368 TRP A NE1 1 ATOM 2264 C CE2 . TRP A 1 282 ? 23.113 8.655 9.621 1.00 6.66 ? 368 TRP A CE2 1 ATOM 2265 C CE3 . TRP A 1 282 ? 23.908 6.464 10.261 1.00 7.27 ? 368 TRP A CE3 1 ATOM 2266 C CZ2 . TRP A 1 282 ? 21.843 8.143 9.349 1.00 7.89 ? 368 TRP A CZ2 1 ATOM 2267 C CZ3 . TRP A 1 282 ? 22.679 5.968 9.989 1.00 7.49 ? 368 TRP A CZ3 1 ATOM 2268 C CH2 . TRP A 1 282 ? 21.639 6.802 9.541 1.00 7.50 ? 368 TRP A CH2 1 ATOM 2269 N N . GLY A 1 283 ? 28.638 9.645 12.740 1.00 7.00 ? 369 GLY A N 1 ATOM 2270 C CA . GLY A 1 283 ? 28.789 10.408 13.942 1.00 7.74 ? 369 GLY A CA 1 ATOM 2271 C C . GLY A 1 283 ? 29.765 11.556 13.863 1.00 7.45 ? 369 GLY A C 1 ATOM 2272 O O . GLY A 1 283 ? 29.996 12.226 14.892 1.00 7.96 ? 369 GLY A O 1 ATOM 2273 N N . HIS A 1 284 ? 30.350 11.814 12.709 1.00 6.93 ? 370 HIS A N 1 ATOM 2274 C CA . HIS A 1 284 ? 31.270 12.919 12.513 1.00 6.69 ? 370 HIS A CA 1 ATOM 2275 C C . HIS A 1 284 ? 30.412 14.140 12.207 1.00 6.71 ? 370 HIS A C 1 ATOM 2276 O O . HIS A 1 284 ? 30.030 14.400 11.044 1.00 8.09 ? 370 HIS A O 1 ATOM 2277 C CB . HIS A 1 284 ? 32.237 12.609 11.390 1.00 6.92 ? 370 HIS A CB 1 ATOM 2278 C CG . HIS A 1 284 ? 33.180 11.508 11.727 1.00 7.21 ? 370 HIS A CG 1 ATOM 2279 N ND1 . HIS A 1 284 ? 34.149 11.110 10.838 1.00 7.44 ? 370 HIS A ND1 1 ATOM 2280 C CD2 . HIS A 1 284 ? 33.317 10.704 12.809 1.00 8.02 ? 370 HIS A CD2 1 ATOM 2281 C CE1 . HIS A 1 284 ? 34.862 10.129 11.370 1.00 8.69 ? 370 HIS A CE1 1 ATOM 2282 N NE2 . HIS A 1 284 ? 34.377 9.847 12.560 1.00 8.06 ? 370 HIS A NE2 1 ATOM 2283 N N . TRP A 1 285 ? 30.106 14.913 13.237 1.00 6.66 ? 371 TRP A N 1 ATOM 2284 C CA . TRP A 1 285 ? 29.201 16.053 13.138 1.00 6.89 ? 371 TRP A CA 1 ATOM 2285 C C . TRP A 1 285 ? 29.885 17.360 12.912 1.00 6.41 ? 371 TRP A C 1 ATOM 2286 O O . TRP A 1 285 ? 29.188 18.345 12.587 1.00 6.61 ? 371 TRP A O 1 ATOM 2287 C CB . TRP A 1 285 ? 28.296 16.143 14.384 1.00 6.81 ? 371 TRP A CB 1 ATOM 2288 C CG . TRP A 1 285 ? 29.029 16.158 15.691 1.00 6.96 ? 371 TRP A CG 1 ATOM 2289 C CD1 . TRP A 1 285 ? 29.236 15.082 16.501 1.00 8.06 ? 371 TRP A CD1 1 ATOM 2290 C CD2 . TRP A 1 285 ? 29.723 17.234 16.313 1.00 7.01 ? 371 TRP A CD2 1 ATOM 2291 N NE1 . TRP A 1 285 ? 30.011 15.421 17.585 1.00 8.66 ? 371 TRP A NE1 1 ATOM 2292 C CE2 . TRP A 1 285 ? 30.324 16.737 17.482 1.00 7.22 ? 371 TRP A CE2 1 ATOM 2293 C CE3 . TRP A 1 285 ? 29.883 18.602 16.016 1.00 7.32 ? 371 TRP A CE3 1 ATOM 2294 C CZ2 . TRP A 1 285 ? 31.088 17.548 18.319 1.00 7.67 ? 371 TRP A CZ2 1 ATOM 2295 C CZ3 . TRP A 1 285 ? 30.656 19.396 16.851 1.00 7.77 ? 371 TRP A CZ3 1 ATOM 2296 C CH2 . TRP A 1 285 ? 31.245 18.831 17.999 1.00 8.57 ? 371 TRP A CH2 1 ATOM 2297 N N . CYS A 1 286 ? 31.194 17.465 13.135 1.00 6.69 ? 372 CYS A N 1 ATOM 2298 C CA . CYS A 1 286 ? 31.823 18.790 13.206 1.00 6.54 ? 372 CYS A CA 1 ATOM 2299 C C . CYS A 1 286 ? 32.366 19.266 11.861 1.00 6.46 ? 372 CYS A C 1 ATOM 2300 O O . CYS A 1 286 ? 33.280 18.664 11.295 1.00 7.32 ? 372 CYS A O 1 ATOM 2301 C CB . CYS A 1 286 ? 32.957 18.767 14.230 1.00 7.03 ? 372 CYS A CB 1 ATOM 2302 S SG . CYS A 1 286 ? 33.549 20.470 14.470 1.00 7.26 ? 372 CYS A SG 1 ATOM 2303 N N . ASN A 1 287 ? 31.803 20.365 11.361 1.00 6.34 ? 373 ASN A N 1 ATOM 2304 C CA . ASN A 1 287 ? 32.338 21.045 10.189 1.00 6.29 ? 373 ASN A CA 1 ATOM 2305 C C . ASN A 1 287 ? 32.602 20.059 9.039 1.00 6.37 ? 373 ASN A C 1 ATOM 2306 O O . ASN A 1 287 ? 33.667 20.072 8.405 1.00 6.83 ? 373 ASN A O 1 ATOM 2307 C CB . ASN A 1 287 ? 33.611 21.836 10.510 1.00 6.98 ? 373 ASN A CB 1 ATOM 2308 C CG . ASN A 1 287 ? 33.418 22.842 11.634 1.00 6.76 ? 373 ASN A CG 1 ATOM 2309 O OD1 . ASN A 1 287 ? 32.375 23.502 11.747 1.00 7.41 ? 373 ASN A OD1 1 ATOM 2310 N ND2 . ASN A 1 287 ? 34.461 22.996 12.456 1.00 7.46 ? 373 ASN A ND2 1 ATOM 2311 N N . ALA A 1 288 ? 31.640 19.193 8.737 1.00 6.29 ? 374 ALA A N 1 ATOM 2312 C CA . ALA A 1 288 ? 31.906 18.081 7.819 1.00 6.38 ? 374 ALA A CA 1 ATOM 2313 C C . ALA A 1 288 ? 32.121 18.582 6.385 1.00 6.22 ? 374 ALA A C 1 ATOM 2314 O O . ALA A 1 288 ? 31.369 19.424 5.890 1.00 6.68 ? 374 ALA A O 1 ATOM 2315 C CB . ALA A 1 288 ? 30.782 17.088 7.862 1.00 7.12 ? 374 ALA A CB 1 ATOM 2316 N N . ILE A 1 289 ? 33.119 18.016 5.732 1.00 6.79 ? 375 ILE A N 1 ATOM 2317 C CA . ILE A 1 289 ? 33.399 18.359 4.337 1.00 6.84 ? 375 ILE A CA 1 ATOM 2318 C C . ILE A 1 289 ? 32.336 17.717 3.416 1.00 6.74 ? 375 ILE A C 1 ATOM 2319 O O . ILE A 1 289 ? 31.601 16.811 3.777 1.00 6.79 ? 375 ILE A O 1 ATOM 2320 C CB . ILE A 1 289 ? 34.833 17.990 3.956 1.00 7.67 ? 375 ILE A CB 1 ATOM 2321 C CG1 . ILE A 1 289 ? 35.105 16.528 3.975 1.00 8.37 ? 375 ILE A CG1 1 ATOM 2322 C CG2 . ILE A 1 289 ? 35.780 18.818 4.792 1.00 8.46 ? 375 ILE A CG2 1 ATOM 2323 C CD1 . ILE A 1 289 ? 36.541 16.184 3.580 1.00 9.29 ? 375 ILE A CD1 1 ATOM 2324 N N . GLY A 1 290 ? 32.278 18.223 2.179 1.00 7.08 ? 376 GLY A N 1 ATOM 2325 C CA . GLY A 1 290 ? 31.424 17.599 1.208 1.00 6.64 ? 376 GLY A CA 1 ATOM 2326 C C . GLY A 1 290 ? 29.940 17.765 1.480 1.00 6.28 ? 376 GLY A C 1 ATOM 2327 O O . GLY A 1 290 ? 29.154 16.883 1.133 1.00 7.67 ? 376 GLY A O 1 ATOM 2328 N N . THR A 1 291 ? 29.551 18.891 2.061 1.00 6.50 ? 377 THR A N 1 ATOM 2329 C CA . THR A 1 291 ? 28.165 19.211 2.350 1.00 6.33 ? 377 THR A CA 1 ATOM 2330 C C . THR A 1 291 ? 27.768 20.497 1.621 1.00 6.21 ? 377 THR A C 1 ATOM 2331 O O . THR A 1 291 ? 28.625 21.329 1.286 1.00 6.93 ? 377 THR A O 1 ATOM 2332 C CB . THR A 1 291 ? 27.929 19.374 3.857 1.00 6.64 ? 377 THR A CB 1 ATOM 2333 O OG1 . THR A 1 291 ? 28.669 20.531 4.252 1.00 6.81 ? 377 THR A OG1 1 ATOM 2334 C CG2 . THR A 1 291 ? 28.320 18.147 4.638 1.00 7.02 ? 377 THR A CG2 1 ATOM 2335 N N . GLY A 1 292 ? 26.472 20.675 1.414 1.00 6.14 ? 378 GLY A N 1 ATOM 2336 C CA . GLY A 1 292 ? 25.899 21.829 0.744 1.00 6.39 ? 378 GLY A CA 1 ATOM 2337 C C . GLY A 1 292 ? 24.665 22.359 1.419 1.00 6.18 ? 378 GLY A C 1 ATOM 2338 O O . GLY A 1 292 ? 23.936 21.618 2.089 1.00 6.25 ? 378 GLY A O 1 ATOM 2339 N N . PHE A 1 293 ? 24.368 23.624 1.189 1.00 6.41 ? 379 PHE A N 1 ATOM 2340 C CA . PHE A 1 293 ? 23.064 24.184 1.550 1.00 6.40 ? 379 PHE A CA 1 ATOM 2341 C C . PHE A 1 293 ? 21.982 23.294 0.890 1.00 6.52 ? 379 PHE A C 1 ATOM 2342 O O . PHE A 1 293 ? 22.137 22.909 -0.274 1.00 6.91 ? 379 PHE A O 1 ATOM 2343 C CB . PHE A 1 293 ? 22.896 25.625 1.079 1.00 6.72 ? 379 PHE A CB 1 ATOM 2344 C CG . PHE A 1 293 ? 23.702 26.625 1.864 1.00 6.87 ? 379 PHE A CG 1 ATOM 2345 C CD1 . PHE A 1 293 ? 23.494 26.785 3.220 1.00 7.18 ? 379 PHE A CD1 1 ATOM 2346 C CD2 . PHE A 1 293 ? 24.634 27.447 1.244 1.00 7.66 ? 379 PHE A CD2 1 ATOM 2347 C CE1 . PHE A 1 293 ? 24.176 27.751 3.929 1.00 7.97 ? 379 PHE A CE1 1 ATOM 2348 C CE2 . PHE A 1 293 ? 25.356 28.385 1.978 1.00 8.77 ? 379 PHE A CE2 1 ATOM 2349 C CZ . PHE A 1 293 ? 25.114 28.535 3.311 1.00 8.52 ? 379 PHE A CZ 1 ATOM 2350 N N . GLY A 1 294 ? 20.898 23.050 1.596 1.00 6.76 ? 380 GLY A N 1 ATOM 2351 C CA . GLY A 1 294 ? 19.848 22.164 1.109 1.00 7.18 ? 380 GLY A CA 1 ATOM 2352 C C . GLY A 1 294 ? 18.534 22.848 0.784 1.00 6.94 ? 380 GLY A C 1 ATOM 2353 O O . GLY A 1 294 ? 18.440 24.041 0.500 1.00 8.09 ? 380 GLY A O 1 ATOM 2354 N N . MET A 1 295 ? 17.488 22.023 0.768 1.00 8.13 ? 381 MET A N 1 ATOM 2355 C CA . MET A 1 295 ? 16.190 22.513 0.315 1.00 9.05 ? 381 MET A CA 1 ATOM 2356 C C . MET A 1 295 ? 15.735 23.682 1.179 1.00 7.67 ? 381 MET A C 1 ATOM 2357 O O . MET A 1 295 ? 15.971 23.731 2.402 1.00 8.00 ? 381 MET A O 1 ATOM 2358 C CB A MET A 1 295 ? 15.184 21.383 0.380 0.60 11.53 ? 381 MET A CB 1 ATOM 2359 C CB B MET A 1 295 ? 15.184 21.415 0.277 0.40 11.80 ? 381 MET A CB 1 ATOM 2360 C CG A MET A 1 295 ? 14.902 20.886 1.662 0.60 10.38 ? 381 MET A CG 1 ATOM 2361 C CG B MET A 1 295 ? 15.001 20.736 1.511 0.40 12.95 ? 381 MET A CG 1 ATOM 2362 S SD A MET A 1 295 ? 13.648 19.605 1.725 0.60 13.99 ? 381 MET A SD 1 ATOM 2363 S SD B MET A 1 295 ? 13.699 19.478 1.461 0.40 14.45 ? 381 MET A SD 1 ATOM 2364 C CE A MET A 1 295 ? 14.516 18.269 1.038 0.60 10.05 ? 381 MET A CE 1 ATOM 2365 C CE B MET A 1 295 ? 13.633 19.088 -0.067 0.40 5.48 ? 381 MET A CE 1 ATOM 2366 N N . ARG A 1 296 ? 15.111 24.646 0.525 1.00 8.20 ? 382 ARG A N 1 ATOM 2367 C CA . ARG A 1 296 ? 14.765 25.888 1.180 1.00 7.92 ? 382 ARG A CA 1 ATOM 2368 C C . ARG A 1 296 ? 13.653 25.666 2.185 1.00 6.71 ? 382 ARG A C 1 ATOM 2369 O O . ARG A 1 296 ? 12.756 24.837 1.968 1.00 7.94 ? 382 ARG A O 1 ATOM 2370 C CB . ARG A 1 296 ? 14.342 26.926 0.145 1.00 9.07 ? 382 ARG A CB 1 ATOM 2371 C CG A ARG A 1 296 ? 15.323 27.195 -0.953 0.55 10.06 ? 382 ARG A CG 1 ATOM 2372 C CG B ARG A 1 296 ? 15.453 27.047 -0.970 0.45 11.09 ? 382 ARG A CG 1 ATOM 2373 C CD A ARG A 1 296 ? 16.716 27.510 -0.490 0.55 9.29 ? 382 ARG A CD 1 ATOM 2374 C CD B ARG A 1 296 ? 16.760 27.595 -0.503 0.45 9.78 ? 382 ARG A CD 1 ATOM 2375 N NE A ARG A 1 296 ? 17.521 27.981 -1.618 0.55 10.80 ? 382 ARG A NE 1 ATOM 2376 N NE B ARG A 1 296 ? 17.781 27.465 -1.569 0.45 9.70 ? 382 ARG A NE 1 ATOM 2377 C CZ A ARG A 1 296 ? 18.404 27.217 -2.254 0.55 10.65 ? 382 ARG A CZ 1 ATOM 2378 C CZ B ARG A 1 296 ? 17.809 28.261 -2.634 0.45 9.31 ? 382 ARG A CZ 1 ATOM 2379 N NH1 A ARG A 1 296 ? 18.728 26.018 -1.803 0.55 10.10 ? 382 ARG A NH1 1 ATOM 2380 N NH1 B ARG A 1 296 ? 16.992 29.288 -2.715 0.45 11.11 ? 382 ARG A NH1 1 ATOM 2381 N NH2 A ARG A 1 296 ? 19.009 27.656 -3.374 0.55 10.54 ? 382 ARG A NH2 1 ATOM 2382 N NH2 B ARG A 1 296 ? 18.686 28.073 -3.569 0.45 8.97 ? 382 ARG A NH2 1 ATOM 2383 N N . PRO A 1 297 ? 13.593 26.428 3.263 1.00 6.87 ? 383 PRO A N 1 ATOM 2384 C CA . PRO A 1 297 ? 12.513 26.272 4.256 1.00 7.16 ? 383 PRO A CA 1 ATOM 2385 C C . PRO A 1 297 ? 11.165 26.421 3.612 1.00 6.94 ? 383 PRO A C 1 ATOM 2386 O O . PRO A 1 297 ? 10.928 27.329 2.788 1.00 7.56 ? 383 PRO A O 1 ATOM 2387 C CB . PRO A 1 297 ? 12.790 27.387 5.257 1.00 7.32 ? 383 PRO A CB 1 ATOM 2388 C CG . PRO A 1 297 ? 14.315 27.543 5.182 1.00 7.21 ? 383 PRO A CG 1 ATOM 2389 C CD . PRO A 1 297 ? 14.626 27.369 3.710 1.00 7.13 ? 383 PRO A CD 1 ATOM 2390 N N . THR A 1 298 ? 10.238 25.553 3.999 1.00 6.97 ? 384 THR A N 1 ATOM 2391 C CA . THR A 1 298 ? 8.882 25.573 3.462 1.00 6.98 ? 384 THR A CA 1 ATOM 2392 C C . THR A 1 298 ? 7.956 24.787 4.343 1.00 7.09 ? 384 THR A C 1 ATOM 2393 O O . THR A 1 298 ? 8.314 23.720 4.891 1.00 7.47 ? 384 THR A O 1 ATOM 2394 C CB . THR A 1 298 ? 8.854 24.997 2.030 1.00 8.19 ? 384 THR A CB 1 ATOM 2395 O OG1 . THR A 1 298 ? 7.530 25.156 1.490 1.00 9.18 ? 384 THR A OG1 1 ATOM 2396 C CG2 . THR A 1 298 ? 9.240 23.565 1.932 1.00 8.99 ? 384 THR A CG2 1 ATOM 2397 N N . ALA A 1 299 ? 6.702 25.227 4.394 1.00 7.01 ? 385 ALA A N 1 ATOM 2398 C CA . ALA A 1 299 ? 5.601 24.452 4.939 1.00 7.51 ? 385 ALA A CA 1 ATOM 2399 C C . ALA A 1 299 ? 5.096 23.411 3.938 1.00 7.43 ? 385 ALA A C 1 ATOM 2400 O O . ALA A 1 299 ? 4.383 22.470 4.334 1.00 9.13 ? 385 ALA A O 1 ATOM 2401 C CB . ALA A 1 299 ? 4.434 25.351 5.304 1.00 8.85 ? 385 ALA A CB 1 ATOM 2402 N N . ASN A 1 300 ? 5.427 23.572 2.661 1.00 7.51 ? 386 ASN A N 1 ATOM 2403 C CA . ASN A 1 300 ? 4.874 22.698 1.623 1.00 8.71 ? 386 ASN A CA 1 ATOM 2404 C C . ASN A 1 300 ? 5.742 21.479 1.426 1.00 8.72 ? 386 ASN A C 1 ATOM 2405 O O . ASN A 1 300 ? 6.383 21.280 0.409 1.00 9.37 ? 386 ASN A O 1 ATOM 2406 C CB . ASN A 1 300 ? 4.724 23.502 0.331 1.00 9.88 ? 386 ASN A CB 1 ATOM 2407 C CG . ASN A 1 300 ? 3.717 24.610 0.498 1.00 12.18 ? 386 ASN A CG 1 ATOM 2408 O OD1 . ASN A 1 300 ? 2.699 24.436 1.162 1.00 14.24 ? 386 ASN A OD1 1 ATOM 2409 N ND2 . ASN A 1 300 ? 3.977 25.771 -0.114 1.00 15.32 ? 386 ASN A ND2 1 ATOM 2410 N N . THR A 1 301 ? 5.765 20.644 2.466 1.00 8.20 ? 387 THR A N 1 ATOM 2411 C CA . THR A 1 301 ? 6.648 19.510 2.534 1.00 7.69 ? 387 THR A CA 1 ATOM 2412 C C . THR A 1 301 ? 6.162 18.377 1.642 1.00 7.33 ? 387 THR A C 1 ATOM 2413 O O . THR A 1 301 ? 6.985 17.545 1.251 1.00 8.66 ? 387 THR A O 1 ATOM 2414 C CB . THR A 1 301 ? 6.800 18.983 3.948 1.00 8.06 ? 387 THR A CB 1 ATOM 2415 O OG1 . THR A 1 301 ? 5.517 18.436 4.329 1.00 8.02 ? 387 THR A OG1 1 ATOM 2416 C CG2 . THR A 1 301 ? 7.229 20.089 4.924 1.00 8.97 ? 387 THR A CG2 1 ATOM 2417 N N . GLY A 1 302 ? 4.856 18.282 1.432 1.00 7.38 ? 388 GLY A N 1 ATOM 2418 C CA . GLY A 1 302 ? 4.298 17.145 0.744 1.00 7.61 ? 388 GLY A CA 1 ATOM 2419 C C . GLY A 1 302 ? 4.159 15.909 1.567 1.00 6.85 ? 388 GLY A C 1 ATOM 2420 O O . GLY A 1 302 ? 3.635 14.919 1.037 1.00 7.95 ? 388 GLY A O 1 ATOM 2421 N N . HIS A 1 303 ? 4.562 15.902 2.830 1.00 7.34 ? 389 HIS A N 1 ATOM 2422 C CA . HIS A 1 303 ? 4.542 14.706 3.670 1.00 7.38 ? 389 HIS A CA 1 ATOM 2423 C C . HIS A 1 303 ? 3.649 14.938 4.877 1.00 6.84 ? 389 HIS A C 1 ATOM 2424 O O . HIS A 1 303 ? 3.770 15.970 5.596 1.00 7.69 ? 389 HIS A O 1 ATOM 2425 C CB . HIS A 1 303 ? 5.948 14.330 4.155 1.00 7.46 ? 389 HIS A CB 1 ATOM 2426 C CG . HIS A 1 303 ? 6.001 12.970 4.751 1.00 7.07 ? 389 HIS A CG 1 ATOM 2427 N ND1 . HIS A 1 303 ? 5.544 12.698 6.021 1.00 7.78 ? 389 HIS A ND1 1 ATOM 2428 C CD2 . HIS A 1 303 ? 6.433 11.817 4.191 1.00 7.26 ? 389 HIS A CD2 1 ATOM 2429 C CE1 . HIS A 1 303 ? 5.685 11.397 6.206 1.00 8.16 ? 389 HIS A CE1 1 ATOM 2430 N NE2 . HIS A 1 303 ? 6.215 10.839 5.114 1.00 7.66 ? 389 HIS A NE2 1 ATOM 2431 N N . GLN A 1 304 ? 2.772 13.998 5.147 1.00 7.35 ? 390 GLN A N 1 ATOM 2432 C CA . GLN A 1 304 ? 1.762 14.126 6.179 1.00 8.02 ? 390 GLN A CA 1 ATOM 2433 C C . GLN A 1 304 ? 2.345 14.420 7.574 1.00 7.62 ? 390 GLN A C 1 ATOM 2434 O O . GLN A 1 304 ? 1.689 15.107 8.366 1.00 9.40 ? 390 GLN A O 1 ATOM 2435 C CB . GLN A 1 304 ? 0.933 12.813 6.244 1.00 10.29 ? 390 GLN A CB 1 ATOM 2436 C CG . GLN A 1 304 ? -0.178 12.850 7.243 1.00 15.11 ? 390 GLN A CG 1 ATOM 2437 C CD . GLN A 1 304 ? -1.248 13.722 6.770 1.00 19.95 ? 390 GLN A CD 1 ATOM 2438 O OE1 . GLN A 1 304 ? -1.552 13.742 5.557 1.00 24.36 ? 390 GLN A OE1 1 ATOM 2439 N NE2 . GLN A 1 304 ? -1.830 14.506 7.698 1.00 26.84 ? 390 GLN A NE2 1 ATOM 2440 N N . TYR A 1 305 ? 3.502 13.886 7.890 1.00 6.70 ? 391 TYR A N 1 ATOM 2441 C CA . TYR A 1 305 ? 4.051 14.005 9.240 1.00 6.63 ? 391 TYR A CA 1 ATOM 2442 C C . TYR A 1 305 ? 5.001 15.154 9.408 1.00 6.80 ? 391 TYR A C 1 ATOM 2443 O O . TYR A 1 305 ? 5.534 15.343 10.529 1.00 7.28 ? 391 TYR A O 1 ATOM 2444 C CB . TYR A 1 305 ? 4.730 12.709 9.661 1.00 7.23 ? 391 TYR A CB 1 ATOM 2445 C CG . TYR A 1 305 ? 3.872 11.472 9.716 1.00 8.24 ? 391 TYR A CG 1 ATOM 2446 C CD1 . TYR A 1 305 ? 2.521 11.539 9.931 1.00 8.56 ? 391 TYR A CD1 1 ATOM 2447 C CD2 . TYR A 1 305 ? 4.436 10.212 9.606 1.00 9.41 ? 391 TYR A CD2 1 ATOM 2448 C CE1 . TYR A 1 305 ? 1.725 10.377 10.000 1.00 10.16 ? 391 TYR A CE1 1 ATOM 2449 C CE2 . TYR A 1 305 ? 3.674 9.065 9.701 1.00 10.55 ? 391 TYR A CE2 1 ATOM 2450 C CZ . TYR A 1 305 ? 2.344 9.175 9.906 1.00 10.58 ? 391 TYR A CZ 1 ATOM 2451 O OH . TYR A 1 305 ? 1.564 8.000 10.026 1.00 13.23 ? 391 TYR A OH 1 ATOM 2452 N N . VAL A 1 306 ? 5.253 15.930 8.360 1.00 6.12 ? 392 VAL A N 1 ATOM 2453 C CA . VAL A 1 306 ? 6.305 16.951 8.386 1.00 6.13 ? 392 VAL A CA 1 ATOM 2454 C C . VAL A 1 306 ? 5.640 18.307 8.200 1.00 6.01 ? 392 VAL A C 1 ATOM 2455 O O . VAL A 1 306 ? 5.136 18.642 7.118 1.00 6.96 ? 392 VAL A O 1 ATOM 2456 C CB . VAL A 1 306 ? 7.419 16.675 7.362 1.00 7.00 ? 392 VAL A CB 1 ATOM 2457 C CG1 . VAL A 1 306 ? 8.542 17.714 7.551 1.00 7.25 ? 392 VAL A CG1 1 ATOM 2458 C CG2 . VAL A 1 306 ? 7.924 15.282 7.466 1.00 7.94 ? 392 VAL A CG2 1 ATOM 2459 N N . ASP A 1 307 ? 5.620 19.104 9.269 1.00 5.97 ? 393 ASP A N 1 ATOM 2460 C CA . ASP A 1 307 ? 5.099 20.458 9.200 1.00 6.46 ? 393 ASP A CA 1 ATOM 2461 C C . ASP A 1 307 ? 5.968 21.364 8.339 1.00 6.25 ? 393 ASP A C 1 ATOM 2462 O O . ASP A 1 307 ? 5.435 22.285 7.706 1.00 7.59 ? 393 ASP A O 1 ATOM 2463 C CB . ASP A 1 307 ? 5.012 21.055 10.618 1.00 6.50 ? 393 ASP A CB 1 ATOM 2464 C CG . ASP A 1 307 ? 3.834 20.625 11.441 1.00 6.82 ? 393 ASP A CG 1 ATOM 2465 O OD1 . ASP A 1 307 ? 2.874 19.978 10.900 1.00 7.15 ? 393 ASP A OD1 1 ATOM 2466 O OD2 . ASP A 1 307 ? 3.827 20.946 12.663 1.00 7.04 ? 393 ASP A OD2 1 ATOM 2467 N N . ALA A 1 308 ? 7.302 21.190 8.359 1.00 6.15 ? 394 ALA A N 1 ATOM 2468 C CA . ALA A 1 308 ? 8.176 22.051 7.574 1.00 6.11 ? 394 ALA A CA 1 ATOM 2469 C C . ALA A 1 308 ? 9.520 21.405 7.398 1.00 6.20 ? 394 ALA A C 1 ATOM 2470 O O . ALA A 1 308 ? 10.037 20.712 8.287 1.00 6.42 ? 394 ALA A O 1 ATOM 2471 C CB . ALA A 1 308 ? 8.357 23.417 8.231 1.00 7.11 ? 394 ALA A CB 1 ATOM 2472 N N . PHE A 1 309 ? 10.138 21.720 6.238 1.00 5.79 ? 395 PHE A N 1 ATOM 2473 C CA . PHE A 1 309 ? 11.573 21.636 6.094 1.00 5.89 ? 395 PHE A CA 1 ATOM 2474 C C . PHE A 1 309 ? 12.132 22.973 6.517 1.00 6.36 ? 395 PHE A C 1 ATOM 2475 O O . PHE A 1 309 ? 11.568 24.020 6.156 1.00 6.66 ? 395 PHE A O 1 ATOM 2476 C CB . PHE A 1 309 ? 11.985 21.291 4.653 1.00 6.13 ? 395 PHE A CB 1 ATOM 2477 C CG . PHE A 1 309 ? 11.503 19.933 4.276 1.00 6.88 ? 395 PHE A CG 1 ATOM 2478 C CD1 . PHE A 1 309 ? 11.977 18.834 4.964 1.00 7.84 ? 395 PHE A CD1 1 ATOM 2479 C CD2 . PHE A 1 309 ? 10.623 19.723 3.258 1.00 9.27 ? 395 PHE A CD2 1 ATOM 2480 C CE1 . PHE A 1 309 ? 11.607 17.567 4.649 1.00 9.97 ? 395 PHE A CE1 1 ATOM 2481 C CE2 . PHE A 1 309 ? 10.205 18.376 2.937 1.00 11.01 ? 395 PHE A CE2 1 ATOM 2482 C CZ . PHE A 1 309 ? 10.710 17.367 3.670 1.00 11.11 ? 395 PHE A CZ 1 ATOM 2483 N N . VAL A 1 310 ? 13.199 22.978 7.317 1.00 5.88 ? 396 VAL A N 1 ATOM 2484 C CA . VAL A 1 310 ? 13.732 24.170 7.933 1.00 5.73 ? 396 VAL A CA 1 ATOM 2485 C C . VAL A 1 310 ? 15.241 24.187 7.832 1.00 5.56 ? 396 VAL A C 1 ATOM 2486 O O . VAL A 1 310 ? 15.872 23.166 7.525 1.00 6.07 ? 396 VAL A O 1 ATOM 2487 C CB . VAL A 1 310 ? 13.289 24.271 9.410 1.00 6.07 ? 396 VAL A CB 1 ATOM 2488 C CG1 . VAL A 1 310 ? 11.804 24.601 9.524 1.00 7.53 ? 396 VAL A CG1 1 ATOM 2489 C CG2 . VAL A 1 310 ? 13.575 22.987 10.191 1.00 6.74 ? 396 VAL A CG2 1 ATOM 2490 N N . TRP A 1 311 ? 15.824 25.350 8.104 1.00 5.60 ? 397 TRP A N 1 ATOM 2491 C CA . TRP A 1 311 ? 17.268 25.509 8.293 1.00 5.87 ? 397 TRP A CA 1 ATOM 2492 C C . TRP A 1 311 ? 17.431 25.850 9.770 1.00 5.58 ? 397 TRP A C 1 ATOM 2493 O O . TRP A 1 311 ? 17.180 26.991 10.161 1.00 6.61 ? 397 TRP A O 1 ATOM 2494 C CB . TRP A 1 311 ? 17.868 26.583 7.410 1.00 6.08 ? 397 TRP A CB 1 ATOM 2495 C CG . TRP A 1 311 ? 17.966 26.227 5.955 1.00 6.24 ? 397 TRP A CG 1 ATOM 2496 C CD1 . TRP A 1 311 ? 17.391 25.210 5.255 1.00 6.21 ? 397 TRP A CD1 1 ATOM 2497 C CD2 . TRP A 1 311 ? 18.809 26.911 5.021 1.00 6.45 ? 397 TRP A CD2 1 ATOM 2498 N NE1 . TRP A 1 311 ? 17.834 25.201 3.965 1.00 6.83 ? 397 TRP A NE1 1 ATOM 2499 C CE2 . TRP A 1 311 ? 18.692 26.237 3.780 1.00 6.44 ? 397 TRP A CE2 1 ATOM 2500 C CE3 . TRP A 1 311 ? 19.656 28.014 5.111 1.00 6.78 ? 397 TRP A CE3 1 ATOM 2501 C CZ2 . TRP A 1 311 ? 19.404 26.647 2.657 1.00 7.41 ? 397 TRP A CZ2 1 ATOM 2502 C CZ3 . TRP A 1 311 ? 20.355 28.427 4.020 1.00 8.11 ? 397 TRP A CZ3 1 ATOM 2503 C CH2 . TRP A 1 311 ? 20.230 27.712 2.789 1.00 7.61 ? 397 TRP A CH2 1 ATOM 2504 N N . VAL A 1 312 ? 17.775 24.879 10.595 1.00 5.71 ? 398 VAL A N 1 ATOM 2505 C CA . VAL A 1 312 ? 17.914 25.115 12.025 1.00 6.07 ? 398 VAL A CA 1 ATOM 2506 C C . VAL A 1 312 ? 19.328 25.613 12.310 1.00 5.61 ? 398 VAL A C 1 ATOM 2507 O O . VAL A 1 312 ? 19.504 26.756 12.730 1.00 6.20 ? 398 VAL A O 1 ATOM 2508 C CB . VAL A 1 312 ? 17.478 23.923 12.929 1.00 6.11 ? 398 VAL A CB 1 ATOM 2509 C CG1 . VAL A 1 312 ? 17.437 24.416 14.364 1.00 6.34 ? 398 VAL A CG1 1 ATOM 2510 C CG2 . VAL A 1 312 ? 16.157 23.388 12.492 1.00 6.78 ? 398 VAL A CG2 1 ATOM 2511 N N . LYS A 1 313 ? 20.342 24.779 12.118 1.00 6.39 ? 399 LYS A N 1 ATOM 2512 C CA . LYS A 1 313 ? 21.713 25.251 12.230 1.00 6.35 ? 399 LYS A CA 1 ATOM 2513 C C . LYS A 1 313 ? 22.077 26.123 11.048 1.00 6.70 ? 399 LYS A C 1 ATOM 2514 O O . LYS A 1 313 ? 21.993 25.698 9.897 1.00 7.68 ? 399 LYS A O 1 ATOM 2515 C CB . LYS A 1 313 ? 22.636 24.042 12.289 1.00 7.42 ? 399 LYS A CB 1 ATOM 2516 C CG . LYS A 1 313 ? 24.122 24.359 12.242 1.00 9.22 ? 399 LYS A CG 1 ATOM 2517 C CD . LYS A 1 313 ? 24.676 25.108 13.393 1.00 10.67 ? 399 LYS A CD 1 ATOM 2518 C CE . LYS A 1 313 ? 26.046 25.658 13.019 1.00 11.90 ? 399 LYS A CE 1 ATOM 2519 N NZ . LYS A 1 313 ? 26.695 26.277 14.187 1.00 14.09 ? 399 LYS A NZ 1 ATOM 2520 N N . PRO A 1 314 ? 22.518 27.381 11.266 1.00 6.36 ? 400 PRO A N 1 ATOM 2521 C CA . PRO A 1 314 ? 22.776 28.266 10.140 1.00 7.14 ? 400 PRO A CA 1 ATOM 2522 C C . PRO A 1 314 ? 24.145 27.957 9.539 1.00 6.53 ? 400 PRO A C 1 ATOM 2523 O O . PRO A 1 314 ? 25.157 28.076 10.180 1.00 8.53 ? 400 PRO A O 1 ATOM 2524 C CB . PRO A 1 314 ? 22.687 29.664 10.759 1.00 8.10 ? 400 PRO A CB 1 ATOM 2525 C CG . PRO A 1 314 ? 22.049 29.488 12.097 1.00 8.98 ? 400 PRO A CG 1 ATOM 2526 C CD . PRO A 1 314 ? 22.532 28.135 12.559 1.00 7.30 ? 400 PRO A CD 1 ATOM 2527 N N . GLY A 1 315 ? 24.172 27.597 8.271 1.00 7.92 ? 401 GLY A N 1 ATOM 2528 C CA . GLY A 1 315 ? 25.415 27.213 7.603 1.00 8.18 ? 401 GLY A CA 1 ATOM 2529 C C . GLY A 1 315 ? 26.386 28.373 7.515 1.00 7.85 ? 401 GLY A C 1 ATOM 2530 O O . GLY A 1 315 ? 26.031 29.472 7.086 1.00 8.74 ? 401 GLY A O 1 ATOM 2531 N N . GLY A 1 316 ? 27.635 28.113 7.855 1.00 7.81 ? 402 GLY A N 1 ATOM 2532 C CA . GLY A 1 316 ? 28.676 29.114 7.926 1.00 8.54 ? 402 GLY A CA 1 ATOM 2533 C C . GLY A 1 316 ? 29.107 29.430 9.340 1.00 8.41 ? 402 GLY A C 1 ATOM 2534 O O . GLY A 1 316 ? 30.220 29.875 9.566 1.00 9.79 ? 402 GLY A O 1 ATOM 2535 N N . GLU A 1 317 ? 28.236 29.188 10.334 1.00 8.13 ? 403 GLU A N 1 ATOM 2536 C CA . GLU A 1 317 ? 28.595 29.363 11.731 1.00 8.71 ? 403 GLU A CA 1 ATOM 2537 C C . GLU A 1 317 ? 29.308 28.133 12.206 1.00 9.20 ? 403 GLU A C 1 ATOM 2538 O O . GLU A 1 317 ? 28.767 27.012 12.068 1.00 11.33 ? 403 GLU A O 1 ATOM 2539 C CB . GLU A 1 317 ? 27.359 29.696 12.569 1.00 8.73 ? 403 GLU A CB 1 ATOM 2540 C CG . GLU A 1 317 ? 26.712 31.003 12.151 1.00 9.13 ? 403 GLU A CG 1 ATOM 2541 C CD . GLU A 1 317 ? 25.435 31.336 12.856 1.00 8.91 ? 403 GLU A CD 1 ATOM 2542 O OE1 . GLU A 1 317 ? 24.931 30.539 13.712 1.00 11.70 ? 403 GLU A OE1 1 ATOM 2543 O OE2 . GLU A 1 317 ? 24.807 32.385 12.535 1.00 8.52 ? 403 GLU A OE2 1 ATOM 2544 N N . CYS A 1 318 ? 30.503 28.268 12.719 1.00 9.19 ? 404 CYS A N 1 ATOM 2545 C CA . CYS A 1 318 ? 31.370 27.114 13.024 1.00 9.33 ? 404 CYS A CA 1 ATOM 2546 C C . CYS A 1 318 ? 30.800 26.200 14.091 1.00 9.82 ? 404 CYS A C 1 ATOM 2547 O O . CYS A 1 318 ? 30.169 26.665 15.065 1.00 12.25 ? 404 CYS A O 1 ATOM 2548 C CB . CYS A 1 318 ? 32.737 27.626 13.465 1.00 9.12 ? 404 CYS A CB 1 ATOM 2549 S SG . CYS A 1 318 ? 33.963 26.316 13.413 1.00 9.20 ? 404 CYS A SG 1 ATOM 2550 N N . ASN A 1 319 ? 31.060 24.904 13.961 1.00 8.32 ? 405 ASN A N 1 ATOM 2551 C CA . ASN A 1 319 ? 30.637 23.921 14.956 1.00 7.74 ? 405 ASN A CA 1 ATOM 2552 C C . ASN A 1 319 ? 31.644 23.707 16.098 1.00 7.77 ? 405 ASN A C 1 ATOM 2553 O O . ASN A 1 319 ? 31.356 23.043 17.078 1.00 8.63 ? 405 ASN A O 1 ATOM 2554 C CB . ASN A 1 319 ? 30.455 22.593 14.242 1.00 7.99 ? 405 ASN A CB 1 ATOM 2555 C CG . ASN A 1 319 ? 29.362 22.585 13.235 1.00 9.04 ? 405 ASN A CG 1 ATOM 2556 O OD1 . ASN A 1 319 ? 29.430 21.846 12.249 1.00 7.80 ? 405 ASN A OD1 1 ATOM 2557 N ND2 . ASN A 1 319 ? 28.321 23.342 13.507 1.00 12.74 ? 405 ASN A ND2 1 ATOM 2558 N N . GLY A 1 320 ? 32.860 24.239 15.904 1.00 7.85 ? 406 GLY A N 1 ATOM 2559 C CA . GLY A 1 320 ? 33.933 24.034 16.880 1.00 7.80 ? 406 GLY A CA 1 ATOM 2560 C C . GLY A 1 320 ? 35.283 24.237 16.267 1.00 7.58 ? 406 GLY A C 1 ATOM 2561 O O . GLY A 1 320 ? 35.519 23.983 15.070 1.00 8.24 ? 406 GLY A O 1 ATOM 2562 N N . THR A 1 321 ? 36.252 24.648 17.094 1.00 8.41 ? 407 THR A N 1 ATOM 2563 C CA . THR A 1 321 ? 37.583 24.888 16.651 1.00 8.87 ? 407 THR A CA 1 ATOM 2564 C C . THR A 1 321 ? 38.359 23.630 16.323 1.00 8.43 ? 407 THR A C 1 ATOM 2565 O O . THR A 1 321 ? 38.180 22.600 16.952 1.00 8.73 ? 407 THR A O 1 ATOM 2566 C CB . THR A 1 321 ? 38.355 25.733 17.692 1.00 9.63 ? 407 THR A CB 1 ATOM 2567 O OG1 . THR A 1 321 ? 39.632 26.069 17.154 1.00 11.87 ? 407 THR A OG1 1 ATOM 2568 C CG2 . THR A 1 321 ? 38.605 25.026 19.020 1.00 10.90 ? 407 THR A CG2 1 ATOM 2569 N N . SER A 1 322 ? 39.258 23.755 15.360 1.00 9.19 ? 408 SER A N 1 ATOM 2570 C CA . SER A 1 322 ? 40.200 22.690 15.078 1.00 9.26 ? 408 SER A CA 1 ATOM 2571 C C . SER A 1 322 ? 41.538 22.864 15.793 1.00 9.96 ? 408 SER A C 1 ATOM 2572 O O . SER A 1 322 ? 42.424 22.031 15.630 1.00 11.83 ? 408 SER A O 1 ATOM 2573 C CB . SER A 1 322 ? 40.405 22.594 13.561 1.00 10.75 ? 408 SER A CB 1 ATOM 2574 O OG . SER A 1 322 ? 40.976 23.771 13.007 1.00 11.48 ? 408 SER A OG 1 ATOM 2575 N N . ASP A 1 323 ? 41.652 23.885 16.611 1.00 10.08 ? 409 ASP A N 1 ATOM 2576 C CA . ASP A 1 323 ? 42.889 24.132 17.391 1.00 11.36 ? 409 ASP A CA 1 ATOM 2577 C C . ASP A 1 323 ? 42.878 23.194 18.599 1.00 10.98 ? 409 ASP A C 1 ATOM 2578 O O . ASP A 1 323 ? 42.131 23.383 19.555 1.00 10.43 ? 409 ASP A O 1 ATOM 2579 C CB . ASP A 1 323 ? 42.920 25.571 17.840 1.00 11.39 ? 409 ASP A CB 1 ATOM 2580 C CG . ASP A 1 323 ? 44.150 25.951 18.674 1.00 13.50 ? 409 ASP A CG 1 ATOM 2581 O OD1 . ASP A 1 323 ? 44.932 25.069 19.003 1.00 13.44 ? 409 ASP A OD1 1 ATOM 2582 O OD2 . ASP A 1 323 ? 44.257 27.135 19.001 1.00 17.00 ? 409 ASP A OD2 1 ATOM 2583 N N . THR A 1 324 ? 43.742 22.185 18.526 1.00 11.50 ? 410 THR A N 1 ATOM 2584 C CA . THR A 1 324 ? 43.780 21.170 19.530 1.00 12.58 ? 410 THR A CA 1 ATOM 2585 C C . THR A 1 324 ? 44.212 21.650 20.893 1.00 14.19 ? 410 THR A C 1 ATOM 2586 O O . THR A 1 324 ? 43.996 20.904 21.877 1.00 15.67 ? 410 THR A O 1 ATOM 2587 C CB . THR A 1 324 ? 44.699 20.027 19.104 1.00 13.70 ? 410 THR A CB 1 ATOM 2588 O OG1 . THR A 1 324 ? 46.063 20.514 19.079 1.00 16.81 ? 410 THR A OG1 1 ATOM 2589 C CG2 . THR A 1 324 ? 44.375 19.417 17.767 1.00 14.46 ? 410 THR A CG2 1 ATOM 2590 N N . THR A 1 325 ? 44.741 22.849 20.969 1.00 13.28 ? 411 THR A N 1 ATOM 2591 C CA . THR A 1 325 ? 45.161 23.443 22.242 1.00 15.05 ? 411 THR A CA 1 ATOM 2592 C C . THR A 1 325 ? 44.115 24.292 22.916 1.00 14.19 ? 411 THR A C 1 ATOM 2593 O O . THR A 1 325 ? 44.312 24.716 24.066 1.00 16.28 ? 411 THR A O 1 ATOM 2594 C CB . THR A 1 325 ? 46.444 24.358 22.050 1.00 15.98 ? 411 THR A CB 1 ATOM 2595 O OG1 . THR A 1 325 ? 46.150 25.605 21.401 1.00 17.83 ? 411 THR A OG1 1 ATOM 2596 C CG2 . THR A 1 325 ? 47.493 23.632 21.332 1.00 18.32 ? 411 THR A CG2 1 ATOM 2597 N N . ALA A 1 326 ? 42.978 24.510 22.249 1.00 13.11 ? 412 ALA A N 1 ATOM 2598 C CA . ALA A 1 326 ? 42.005 25.433 22.780 1.00 13.18 ? 412 ALA A CA 1 ATOM 2599 C C . ALA A 1 326 ? 41.238 24.797 23.944 1.00 12.26 ? 412 ALA A C 1 ATOM 2600 O O . ALA A 1 326 ? 41.030 23.609 24.009 1.00 12.90 ? 412 ALA A O 1 ATOM 2601 C CB . ALA A 1 326 ? 41.029 25.765 21.648 1.00 13.52 ? 412 ALA A CB 1 ATOM 2602 N N . ALA A 1 327 ? 40.788 25.613 24.889 1.00 14.53 ? 413 ALA A N 1 ATOM 2603 C CA . ALA A 1 327 ? 40.135 25.082 26.115 1.00 14.81 ? 413 ALA A CA 1 ATOM 2604 C C . ALA A 1 327 ? 38.944 24.142 25.864 1.00 15.96 ? 413 ALA A C 1 ATOM 2605 O O . ALA A 1 327 ? 38.752 23.128 26.518 1.00 18.11 ? 413 ALA A O 1 ATOM 2606 C CB . ALA A 1 327 ? 39.691 26.244 27.037 1.00 16.87 ? 413 ALA A CB 1 ATOM 2607 N N . ARG A 1 328 ? 38.131 24.505 24.943 1.00 13.95 ? 414 ARG A N 1 ATOM 2608 C CA . ARG A 1 328 ? 36.893 23.701 24.691 1.00 14.11 ? 414 ARG A CA 1 ATOM 2609 C C . ARG A 1 328 ? 37.024 22.923 23.366 1.00 10.59 ? 414 ARG A C 1 ATOM 2610 O O . ARG A 1 328 ? 35.999 22.602 22.723 1.00 10.12 ? 414 ARG A O 1 ATOM 2611 C CB . ARG A 1 328 ? 35.616 24.479 24.839 1.00 15.31 ? 414 ARG A CB 1 ATOM 2612 C CG . ARG A 1 328 ? 35.423 24.981 26.324 1.00 18.77 ? 414 ARG A CG 1 ATOM 2613 C CD . ARG A 1 328 ? 34.236 25.815 26.504 1.00 21.11 ? 414 ARG A CD 1 ATOM 2614 N NE . ARG A 1 328 ? 34.367 26.994 25.671 1.00 27.50 ? 414 ARG A NE 1 ATOM 2615 C CZ . ARG A 1 328 ? 34.972 28.141 26.028 1.00 30.95 ? 414 ARG A CZ 1 ATOM 2616 N NH1 . ARG A 1 328 ? 35.426 28.355 27.275 1.00 28.13 ? 414 ARG A NH1 1 ATOM 2617 N NH2 . ARG A 1 328 ? 35.074 29.119 25.118 1.00 33.31 ? 414 ARG A NH2 1 ATOM 2618 N N . TYR A 1 329 ? 38.240 22.543 23.017 1.00 10.39 ? 415 TYR A N 1 ATOM 2619 C CA . TYR A 1 329 ? 38.446 21.720 21.835 1.00 9.33 ? 415 TYR A CA 1 ATOM 2620 C C . TYR A 1 329 ? 37.721 20.388 21.932 1.00 8.30 ? 415 TYR A C 1 ATOM 2621 O O . TYR A 1 329 ? 37.867 19.651 22.931 1.00 9.35 ? 415 TYR A O 1 ATOM 2622 C CB . TYR A 1 329 ? 39.956 21.485 21.633 1.00 9.65 ? 415 TYR A CB 1 ATOM 2623 C CG . TYR A 1 329 ? 40.261 20.505 20.532 1.00 9.09 ? 415 TYR A CG 1 ATOM 2624 C CD1 . TYR A 1 329 ? 40.037 20.800 19.206 1.00 10.15 ? 415 TYR A CD1 1 ATOM 2625 C CD2 . TYR A 1 329 ? 40.740 19.259 20.813 1.00 9.41 ? 415 TYR A CD2 1 ATOM 2626 C CE1 . TYR A 1 329 ? 40.308 19.899 18.219 1.00 9.65 ? 415 TYR A CE1 1 ATOM 2627 C CE2 . TYR A 1 329 ? 41.042 18.347 19.836 1.00 8.94 ? 415 TYR A CE2 1 ATOM 2628 C CZ . TYR A 1 329 ? 40.805 18.678 18.527 1.00 9.51 ? 415 TYR A CZ 1 ATOM 2629 O OH . TYR A 1 329 ? 41.115 17.790 17.498 1.00 11.46 ? 415 TYR A OH 1 ATOM 2630 N N . ASP A 1 330 ? 36.991 20.055 20.875 1.00 7.61 ? 416 ASP A N 1 ATOM 2631 C CA . ASP A 1 330 ? 36.283 18.796 20.719 1.00 7.34 ? 416 ASP A CA 1 ATOM 2632 C C . ASP A 1 330 ? 36.972 18.012 19.606 1.00 7.41 ? 416 ASP A C 1 ATOM 2633 O O . ASP A 1 330 ? 37.043 18.489 18.469 1.00 7.59 ? 416 ASP A O 1 ATOM 2634 C CB . ASP A 1 330 ? 34.829 19.086 20.368 1.00 7.28 ? 416 ASP A CB 1 ATOM 2635 C CG . ASP A 1 330 ? 33.969 17.838 20.426 1.00 7.13 ? 416 ASP A CG 1 ATOM 2636 O OD1 . ASP A 1 330 ? 34.351 16.837 19.799 1.00 7.66 ? 416 ASP A OD1 1 ATOM 2637 O OD2 . ASP A 1 330 ? 32.903 17.860 21.084 1.00 8.64 ? 416 ASP A OD2 1 ATOM 2638 N N . TYR A 1 331 ? 37.491 16.823 19.934 1.00 7.68 ? 417 TYR A N 1 ATOM 2639 C CA . TYR A 1 331 ? 38.259 16.066 18.955 1.00 7.90 ? 417 TYR A CA 1 ATOM 2640 C C . TYR A 1 331 ? 37.504 15.807 17.658 1.00 6.84 ? 417 TYR A C 1 ATOM 2641 O O . TYR A 1 331 ? 38.117 15.522 16.608 1.00 7.41 ? 417 TYR A O 1 ATOM 2642 C CB . TYR A 1 331 ? 38.759 14.746 19.550 1.00 8.77 ? 417 TYR A CB 1 ATOM 2643 C CG . TYR A 1 331 ? 37.708 13.715 19.715 1.00 8.06 ? 417 TYR A CG 1 ATOM 2644 C CD1 . TYR A 1 331 ? 37.417 12.823 18.687 1.00 8.72 ? 417 TYR A CD1 1 ATOM 2645 C CD2 . TYR A 1 331 ? 36.964 13.623 20.895 1.00 10.26 ? 417 TYR A CD2 1 ATOM 2646 C CE1 . TYR A 1 331 ? 36.445 11.872 18.820 1.00 9.89 ? 417 TYR A CE1 1 ATOM 2647 C CE2 . TYR A 1 331 ? 36.019 12.654 21.022 1.00 10.88 ? 417 TYR A CE2 1 ATOM 2648 C CZ . TYR A 1 331 ? 35.741 11.776 20.009 1.00 10.86 ? 417 TYR A CZ 1 ATOM 2649 O OH . TYR A 1 331 ? 34.732 10.810 20.158 1.00 12.35 ? 417 TYR A OH 1 ATOM 2650 N N . HIS A 1 332 ? 36.171 15.843 17.676 1.00 6.93 ? 418 HIS A N 1 ATOM 2651 C CA . HIS A 1 332 ? 35.415 15.649 16.432 1.00 6.80 ? 418 HIS A CA 1 ATOM 2652 C C . HIS A 1 332 ? 35.820 16.673 15.372 1.00 6.64 ? 418 HIS A C 1 ATOM 2653 O O . HIS A 1 332 ? 35.709 16.429 14.169 1.00 7.11 ? 418 HIS A O 1 ATOM 2654 C CB . HIS A 1 332 ? 33.916 15.706 16.685 1.00 7.06 ? 418 HIS A CB 1 ATOM 2655 C CG . HIS A 1 332 ? 33.433 14.534 17.459 1.00 7.73 ? 418 HIS A CG 1 ATOM 2656 N ND1 . HIS A 1 332 ? 33.328 14.533 18.834 1.00 7.86 ? 418 HIS A ND1 1 ATOM 2657 C CD2 . HIS A 1 332 ? 33.034 13.298 17.044 1.00 9.49 ? 418 HIS A CD2 1 ATOM 2658 C CE1 . HIS A 1 332 ? 32.879 13.333 19.219 1.00 9.18 ? 418 HIS A CE1 1 ATOM 2659 N NE2 . HIS A 1 332 ? 32.689 12.569 18.159 1.00 10.21 ? 418 HIS A NE2 1 ATOM 2660 N N . CYS A 1 333 ? 36.222 17.856 15.835 1.00 6.73 ? 419 CYS A N 1 ATOM 2661 C CA . CYS A 1 333 ? 36.553 18.965 14.950 1.00 6.82 ? 419 CYS A CA 1 ATOM 2662 C C . CYS A 1 333 ? 37.987 18.885 14.391 1.00 7.02 ? 419 CYS A C 1 ATOM 2663 O O . CYS A 1 333 ? 38.383 19.693 13.569 1.00 8.23 ? 419 CYS A O 1 ATOM 2664 C CB . CYS A 1 333 ? 36.317 20.281 15.678 1.00 7.45 ? 419 CYS A CB 1 ATOM 2665 S SG . CYS A 1 333 ? 34.597 20.450 16.228 1.00 7.76 ? 419 CYS A SG 1 ATOM 2666 N N . GLY A 1 334 ? 38.716 17.865 14.838 1.00 7.61 ? 420 GLY A N 1 ATOM 2667 C CA . GLY A 1 334 ? 40.063 17.590 14.359 1.00 8.21 ? 420 GLY A CA 1 ATOM 2668 C C . GLY A 1 334 ? 40.125 16.423 13.416 1.00 7.91 ? 420 GLY A C 1 ATOM 2669 O O . GLY A 1 334 ? 41.256 16.057 12.990 1.00 10.02 ? 420 GLY A O 1 ATOM 2670 N N . LEU A 1 335 ? 39.018 15.775 13.110 1.00 7.51 ? 421 LEU A N 1 ATOM 2671 C CA . LEU A 1 335 ? 39.028 14.582 12.278 1.00 7.76 ? 421 LEU A CA 1 ATOM 2672 C C . LEU A 1 335 ? 39.293 14.919 10.824 1.00 8.01 ? 421 LEU A C 1 ATOM 2673 O O . LEU A 1 335 ? 39.198 16.064 10.385 1.00 8.63 ? 421 LEU A O 1 ATOM 2674 C CB . LEU A 1 335 ? 37.686 13.839 12.416 1.00 8.19 ? 421 LEU A CB 1 ATOM 2675 C CG . LEU A 1 335 ? 37.376 13.416 13.835 1.00 7.93 ? 421 LEU A CG 1 ATOM 2676 C CD1 . LEU A 1 335 ? 35.999 12.709 13.853 1.00 9.57 ? 421 LEU A CD1 1 ATOM 2677 C CD2 . LEU A 1 335 ? 38.428 12.512 14.437 1.00 10.57 ? 421 LEU A CD2 1 ATOM 2678 N N . GLU A 1 336 ? 39.649 13.885 10.056 1.00 8.73 ? 422 GLU A N 1 ATOM 2679 C CA . GLU A 1 336 ? 40.068 14.087 8.667 1.00 9.58 ? 422 GLU A CA 1 ATOM 2680 C C . GLU A 1 336 ? 38.974 14.681 7.771 1.00 8.73 ? 422 GLU A C 1 ATOM 2681 O O . GLU A 1 336 ? 39.298 15.251 6.730 1.00 11.23 ? 422 GLU A O 1 ATOM 2682 C CB . GLU A 1 336 ? 40.577 12.758 8.065 1.00 11.89 ? 422 GLU A CB 1 ATOM 2683 C CG . GLU A 1 336 ? 39.491 11.657 7.973 1.00 15.26 ? 422 GLU A CG 1 ATOM 2684 C CD . GLU A 1 336 ? 39.894 10.255 7.484 1.00 20.32 ? 422 GLU A CD 1 ATOM 2685 O OE1 . GLU A 1 336 ? 40.909 10.177 6.780 1.00 23.38 ? 422 GLU A OE1 1 ATOM 2686 O OE2 . GLU A 1 336 ? 39.138 9.218 7.763 1.00 20.92 ? 422 GLU A OE2 1 ATOM 2687 N N . ASP A 1 337 ? 37.712 14.492 8.118 1.00 8.02 ? 423 ASP A N 1 ATOM 2688 C CA . ASP A 1 337 ? 36.578 14.975 7.354 1.00 7.39 ? 423 ASP A CA 1 ATOM 2689 C C . ASP A 1 337 ? 35.985 16.243 7.950 1.00 7.29 ? 423 ASP A C 1 ATOM 2690 O O . ASP A 1 337 ? 34.895 16.616 7.536 1.00 8.10 ? 423 ASP A O 1 ATOM 2691 C CB . ASP A 1 337 ? 35.530 13.885 7.211 1.00 7.77 ? 423 ASP A CB 1 ATOM 2692 C CG . ASP A 1 337 ? 35.044 13.336 8.539 1.00 7.45 ? 423 ASP A CG 1 ATOM 2693 O OD1 . ASP A 1 337 ? 35.348 13.961 9.582 1.00 8.29 ? 423 ASP A OD1 1 ATOM 2694 O OD2 . ASP A 1 337 ? 34.338 12.279 8.524 1.00 8.04 ? 423 ASP A OD2 1 ATOM 2695 N N . ALA A 1 338 ? 36.711 16.931 8.825 1.00 7.11 ? 424 ALA A N 1 ATOM 2696 C CA . ALA A 1 338 ? 36.299 18.206 9.416 1.00 6.92 ? 424 ALA A CA 1 ATOM 2697 C C . ALA A 1 338 ? 37.170 19.292 8.684 1.00 7.24 ? 424 ALA A C 1 ATOM 2698 O O . ALA A 1 338 ? 38.401 19.147 8.608 1.00 9.14 ? 424 ALA A O 1 ATOM 2699 C CB . ALA A 1 338 ? 36.512 18.236 10.889 1.00 7.37 ? 424 ALA A CB 1 ATOM 2700 N N . LEU A 1 339 ? 36.536 20.315 8.159 1.00 7.24 ? 425 LEU A N 1 ATOM 2701 C CA . LEU A 1 339 ? 37.246 21.348 7.453 1.00 7.42 ? 425 LEU A CA 1 ATOM 2702 C C . LEU A 1 339 ? 38.103 22.168 8.433 1.00 7.34 ? 425 LEU A C 1 ATOM 2703 O O . LEU A 1 339 ? 37.675 22.527 9.503 1.00 8.12 ? 425 LEU A O 1 ATOM 2704 C CB . LEU A 1 339 ? 36.267 22.270 6.713 1.00 7.45 ? 425 LEU A CB 1 ATOM 2705 C CG . LEU A 1 339 ? 36.901 23.200 5.664 1.00 8.21 ? 425 LEU A CG 1 ATOM 2706 C CD1 . LEU A 1 339 ? 37.532 22.473 4.504 1.00 10.57 ? 425 LEU A CD1 1 ATOM 2707 C CD2 . LEU A 1 339 ? 35.850 24.147 5.124 1.00 9.29 ? 425 LEU A CD2 1 ATOM 2708 N N . LYS A 1 340 ? 39.320 22.473 7.987 1.00 8.58 ? 426 LYS A N 1 ATOM 2709 C CA . LYS A 1 340 ? 40.288 23.174 8.838 1.00 9.76 ? 426 LYS A CA 1 ATOM 2710 C C . LYS A 1 340 ? 41.041 24.254 8.031 1.00 11.81 ? 426 LYS A C 1 ATOM 2711 O O . LYS A 1 340 ? 41.144 24.144 6.795 1.00 12.48 ? 426 LYS A O 1 ATOM 2712 C CB . LYS A 1 340 ? 41.354 22.245 9.331 1.00 12.06 ? 426 LYS A CB 1 ATOM 2713 C CG . LYS A 1 340 ? 40.811 21.116 10.052 1.00 11.87 ? 426 LYS A CG 1 ATOM 2714 C CD . LYS A 1 340 ? 41.929 20.163 10.552 1.00 14.47 ? 426 LYS A CD 1 ATOM 2715 C CE . LYS A 1 340 ? 41.295 18.970 11.060 1.00 14.00 ? 426 LYS A CE 1 ATOM 2716 N NZ . LYS A 1 340 ? 40.814 18.123 9.886 1.00 16.48 ? 426 LYS A NZ 1 ATOM 2717 N N . PRO A 1 341 ? 41.589 25.287 8.671 1.00 12.04 ? 427 PRO A N 1 ATOM 2718 C CA . PRO A 1 341 ? 41.437 25.579 10.092 1.00 10.97 ? 427 PRO A CA 1 ATOM 2719 C C . PRO A 1 341 ? 40.093 26.180 10.382 1.00 11.06 ? 427 PRO A C 1 ATOM 2720 O O . PRO A 1 341 ? 39.585 27.021 9.619 1.00 12.37 ? 427 PRO A O 1 ATOM 2721 C CB . PRO A 1 341 ? 42.579 26.599 10.327 1.00 11.69 ? 427 PRO A CB 1 ATOM 2722 C CG . PRO A 1 341 ? 42.676 27.345 8.992 1.00 13.33 ? 427 PRO A CG 1 ATOM 2723 C CD . PRO A 1 341 ? 42.460 26.277 7.975 1.00 13.61 ? 427 PRO A CD 1 ATOM 2724 N N . ALA A 1 342 ? 39.526 25.737 11.484 1.00 9.88 ? 428 ALA A N 1 ATOM 2725 C CA . ALA A 1 342 ? 38.203 26.167 11.905 1.00 9.62 ? 428 ALA A CA 1 ATOM 2726 C C . ALA A 1 342 ? 38.316 27.029 13.163 1.00 9.50 ? 428 ALA A C 1 ATOM 2727 O O . ALA A 1 342 ? 39.036 26.647 14.113 1.00 10.35 ? 428 ALA A O 1 ATOM 2728 C CB . ALA A 1 342 ? 37.345 24.961 12.185 1.00 8.99 ? 428 ALA A CB 1 ATOM 2729 N N . PRO A 1 343 ? 37.566 28.116 13.269 1.00 9.87 ? 429 PRO A N 1 ATOM 2730 C CA . PRO A 1 343 ? 37.599 28.990 14.449 1.00 10.74 ? 429 PRO A CA 1 ATOM 2731 C C . PRO A 1 343 ? 36.708 28.408 15.570 1.00 10.93 ? 429 PRO A C 1 ATOM 2732 O O . PRO A 1 343 ? 36.118 27.343 15.485 1.00 10.63 ? 429 PRO A O 1 ATOM 2733 C CB . PRO A 1 343 ? 37.039 30.286 13.863 1.00 12.25 ? 429 PRO A CB 1 ATOM 2734 C CG . PRO A 1 343 ? 35.979 29.809 12.896 1.00 11.46 ? 429 PRO A CG 1 ATOM 2735 C CD . PRO A 1 343 ? 36.659 28.628 12.221 1.00 10.24 ? 429 PRO A CD 1 ATOM 2736 N N . GLU A 1 344 ? 36.587 29.142 16.692 1.00 12.80 ? 430 GLU A N 1 ATOM 2737 C CA . GLU A 1 344 ? 35.739 28.703 17.784 1.00 13.21 ? 430 GLU A CA 1 ATOM 2738 C C . GLU A 1 344 ? 34.306 28.540 17.382 1.00 12.26 ? 430 GLU A C 1 ATOM 2739 O O . GLU A 1 344 ? 33.799 29.246 16.457 1.00 12.07 ? 430 GLU A O 1 ATOM 2740 C CB . GLU A 1 344 ? 35.803 29.678 18.972 1.00 15.55 ? 430 GLU A CB 1 ATOM 2741 C CG . GLU A 1 344 ? 37.104 29.673 19.707 1.00 20.43 ? 430 GLU A CG 1 ATOM 2742 C CD . GLU A 1 344 ? 37.393 28.482 20.637 1.00 23.57 ? 430 GLU A CD 1 ATOM 2743 O OE1 . GLU A 1 344 ? 36.490 27.756 21.169 1.00 25.32 ? 430 GLU A OE1 1 ATOM 2744 O OE2 . GLU A 1 344 ? 38.634 28.338 20.911 1.00 28.14 ? 430 GLU A OE2 1 ATOM 2745 N N . ALA A 1 345 ? 33.605 27.661 18.061 1.00 12.65 ? 431 ALA A N 1 ATOM 2746 C CA . ALA A 1 345 ? 32.223 27.414 17.860 1.00 13.02 ? 431 ALA A CA 1 ATOM 2747 C C . ALA A 1 345 ? 31.451 28.720 17.874 1.00 13.50 ? 431 ALA A C 1 ATOM 2748 O O . ALA A 1 345 ? 31.634 29.601 18.765 1.00 15.43 ? 431 ALA A O 1 ATOM 2749 C CB . ALA A 1 345 ? 31.674 26.457 18.907 1.00 14.25 ? 431 ALA A CB 1 ATOM 2750 N N . GLY A 1 346 ? 30.593 28.904 16.884 1.00 12.40 ? 432 GLY A N 1 ATOM 2751 C CA . GLY A 1 346 ? 29.748 30.099 16.785 1.00 13.25 ? 432 GLY A CA 1 ATOM 2752 C C . GLY A 1 346 ? 30.389 31.196 16.007 1.00 14.00 ? 432 GLY A C 1 ATOM 2753 O O . GLY A 1 346 ? 29.705 32.175 15.652 1.00 17.59 ? 432 GLY A O 1 ATOM 2754 N N . GLN A 1 347 ? 31.658 31.190 15.749 1.00 13.29 ? 433 GLN A N 1 ATOM 2755 C CA . GLN A 1 347 ? 32.288 32.188 14.921 1.00 12.88 ? 433 GLN A CA 1 ATOM 2756 C C . GLN A 1 347 ? 32.059 31.855 13.453 1.00 10.61 ? 433 GLN A C 1 ATOM 2757 O O . GLN A 1 347 ? 31.889 30.694 13.050 1.00 11.02 ? 433 GLN A O 1 ATOM 2758 C CB . GLN A 1 347 ? 33.790 32.303 15.204 1.00 13.07 ? 433 GLN A CB 1 ATOM 2759 C CG . GLN A 1 347 ? 34.013 32.799 16.580 1.00 15.89 ? 433 GLN A CG 1 ATOM 2760 C CD . GLN A 1 347 ? 35.451 33.026 16.865 1.00 17.61 ? 433 GLN A CD 1 ATOM 2761 O OE1 . GLN A 1 347 ? 36.298 33.251 15.976 1.00 19.66 ? 433 GLN A OE1 1 ATOM 2762 N NE2 . GLN A 1 347 ? 35.758 33.035 18.194 1.00 20.56 ? 433 GLN A NE2 1 ATOM 2763 N N . TRP A 1 348 ? 32.057 32.892 12.627 1.00 10.29 ? 434 TRP A N 1 ATOM 2764 C CA . TRP A 1 348 ? 31.920 32.703 11.170 1.00 9.22 ? 434 TRP A CA 1 ATOM 2765 C C . TRP A 1 348 ? 33.107 31.933 10.622 1.00 9.18 ? 434 TRP A C 1 ATOM 2766 O O . TRP A 1 348 ? 34.270 32.246 10.938 1.00 11.41 ? 434 TRP A O 1 ATOM 2767 C CB . TRP A 1 348 ? 31.742 34.065 10.504 1.00 10.05 ? 434 TRP A CB 1 ATOM 2768 C CG . TRP A 1 348 ? 31.304 33.916 9.076 1.00 8.87 ? 434 TRP A CG 1 ATOM 2769 C CD1 . TRP A 1 348 ? 32.051 34.089 7.945 1.00 9.73 ? 434 TRP A CD1 1 ATOM 2770 C CD2 . TRP A 1 348 ? 29.991 33.524 8.648 1.00 8.92 ? 434 TRP A CD2 1 ATOM 2771 N NE1 . TRP A 1 348 ? 31.270 33.837 6.823 1.00 8.97 ? 434 TRP A NE1 1 ATOM 2772 C CE2 . TRP A 1 348 ? 30.005 33.484 7.236 1.00 8.43 ? 434 TRP A CE2 1 ATOM 2773 C CE3 . TRP A 1 348 ? 28.815 33.194 9.315 1.00 9.28 ? 434 TRP A CE3 1 ATOM 2774 C CZ2 . TRP A 1 348 ? 28.865 33.168 6.507 1.00 8.25 ? 434 TRP A CZ2 1 ATOM 2775 C CZ3 . TRP A 1 348 ? 27.702 32.875 8.582 1.00 8.50 ? 434 TRP A CZ3 1 ATOM 2776 C CH2 . TRP A 1 348 ? 27.741 32.861 7.201 1.00 8.18 ? 434 TRP A CH2 1 ATOM 2777 N N . PHE A 1 349 ? 32.822 30.978 9.749 1.00 8.62 ? 435 PHE A N 1 ATOM 2778 C CA . PHE A 1 349 ? 33.806 30.095 9.145 1.00 8.12 ? 435 PHE A CA 1 ATOM 2779 C C . PHE A 1 349 ? 33.670 30.199 7.629 1.00 7.90 ? 435 PHE A C 1 ATOM 2780 O O . PHE A 1 349 ? 32.944 29.469 6.995 1.00 7.87 ? 435 PHE A O 1 ATOM 2781 C CB . PHE A 1 349 ? 33.595 28.678 9.669 1.00 8.48 ? 435 PHE A CB 1 ATOM 2782 C CG . PHE A 1 349 ? 34.592 27.636 9.250 1.00 8.40 ? 435 PHE A CG 1 ATOM 2783 C CD1 . PHE A 1 349 ? 35.699 27.912 8.483 1.00 8.94 ? 435 PHE A CD1 1 ATOM 2784 C CD2 . PHE A 1 349 ? 34.439 26.330 9.694 1.00 7.82 ? 435 PHE A CD2 1 ATOM 2785 C CE1 . PHE A 1 349 ? 36.586 26.938 8.136 1.00 9.67 ? 435 PHE A CE1 1 ATOM 2786 C CE2 . PHE A 1 349 ? 35.333 25.346 9.354 1.00 8.99 ? 435 PHE A CE2 1 ATOM 2787 C CZ . PHE A 1 349 ? 36.419 25.654 8.587 1.00 9.58 ? 435 PHE A CZ 1 ATOM 2788 N N . ASN A 1 350 ? 34.344 31.213 7.041 1.00 8.70 ? 436 ASN A N 1 ATOM 2789 C CA . ASN A 1 350 ? 34.021 31.545 5.669 1.00 8.57 ? 436 ASN A CA 1 ATOM 2790 C C . ASN A 1 350 ? 34.318 30.437 4.656 1.00 8.21 ? 436 ASN A C 1 ATOM 2791 O O . ASN A 1 350 ? 33.576 30.274 3.705 1.00 9.02 ? 436 ASN A O 1 ATOM 2792 C CB . ASN A 1 350 ? 34.666 32.849 5.208 1.00 10.23 ? 436 ASN A CB 1 ATOM 2793 C CG . ASN A 1 350 ? 33.873 33.441 4.072 1.00 10.60 ? 436 ASN A CG 1 ATOM 2794 O OD1 . ASN A 1 350 ? 32.684 33.668 4.174 1.00 11.32 ? 436 ASN A OD1 1 ATOM 2795 N ND2 . ASN A 1 350 ? 34.585 33.675 2.937 1.00 13.04 ? 436 ASN A ND2 1 ATOM 2796 N N . GLU A 1 351 ? 35.407 29.690 4.841 1.00 8.39 ? 437 GLU A N 1 ATOM 2797 C CA . GLU A 1 351 ? 35.702 28.603 3.918 1.00 8.38 ? 437 GLU A CA 1 ATOM 2798 C C . GLU A 1 351 ? 34.578 27.587 3.905 1.00 6.99 ? 437 GLU A C 1 ATOM 2799 O O . GLU A 1 351 ? 34.301 26.957 2.890 1.00 8.36 ? 437 GLU A O 1 ATOM 2800 C CB . GLU A 1 351 ? 37.074 28.009 4.176 1.00 9.01 ? 437 GLU A CB 1 ATOM 2801 C CG . GLU A 1 351 ? 38.195 28.938 3.719 1.00 12.75 ? 437 GLU A CG 1 ATOM 2802 C CD . GLU A 1 351 ? 38.224 29.073 2.184 1.00 16.62 ? 437 GLU A CD 1 ATOM 2803 O OE1 . GLU A 1 351 ? 38.454 28.052 1.534 1.00 19.75 ? 437 GLU A OE1 1 ATOM 2804 O OE2 . GLU A 1 351 ? 37.941 30.183 1.682 1.00 22.32 ? 437 GLU A OE2 1 ATOM 2805 N N . TYR A 1 352 ? 33.994 27.355 5.074 1.00 7.34 ? 438 TYR A N 1 ATOM 2806 C CA . TYR A 1 352 ? 32.883 26.417 5.186 1.00 7.13 ? 438 TYR A CA 1 ATOM 2807 C C . TYR A 1 352 ? 31.630 26.963 4.484 1.00 6.98 ? 438 TYR A C 1 ATOM 2808 O O . TYR A 1 352 ? 30.923 26.250 3.795 1.00 6.79 ? 438 TYR A O 1 ATOM 2809 C CB . TYR A 1 352 ? 32.612 26.090 6.670 1.00 7.10 ? 438 TYR A CB 1 ATOM 2810 C CG . TYR A 1 352 ? 31.804 24.824 6.792 1.00 7.37 ? 438 TYR A CG 1 ATOM 2811 C CD1 . TYR A 1 352 ? 30.417 24.794 6.728 1.00 6.84 ? 438 TYR A CD1 1 ATOM 2812 C CD2 . TYR A 1 352 ? 32.477 23.607 6.838 1.00 6.79 ? 438 TYR A CD2 1 ATOM 2813 C CE1 . TYR A 1 352 ? 29.734 23.589 6.743 1.00 6.99 ? 438 TYR A CE1 1 ATOM 2814 C CE2 . TYR A 1 352 ? 31.795 22.412 6.839 1.00 6.90 ? 438 TYR A CE2 1 ATOM 2815 C CZ . TYR A 1 352 ? 30.418 22.397 6.822 1.00 6.07 ? 438 TYR A CZ 1 ATOM 2816 O OH . TYR A 1 352 ? 29.704 21.228 6.833 1.00 6.73 ? 438 TYR A OH 1 ATOM 2817 N N . PHE A 1 353 ? 31.355 28.258 4.686 1.00 7.32 ? 439 PHE A N 1 ATOM 2818 C CA . PHE A 1 353 ? 30.292 28.922 3.946 1.00 6.99 ? 439 PHE A CA 1 ATOM 2819 C C . PHE A 1 353 ? 30.447 28.749 2.433 1.00 7.42 ? 439 PHE A C 1 ATOM 2820 O O . PHE A 1 353 ? 29.497 28.424 1.720 1.00 7.55 ? 439 PHE A O 1 ATOM 2821 C CB . PHE A 1 353 ? 30.258 30.402 4.332 1.00 7.45 ? 439 PHE A CB 1 ATOM 2822 C CG . PHE A 1 353 ? 29.197 31.199 3.631 1.00 7.25 ? 439 PHE A CG 1 ATOM 2823 C CD1 . PHE A 1 353 ? 27.865 31.085 3.984 1.00 7.17 ? 439 PHE A CD1 1 ATOM 2824 C CD2 . PHE A 1 353 ? 29.528 32.125 2.701 1.00 8.84 ? 439 PHE A CD2 1 ATOM 2825 C CE1 . PHE A 1 353 ? 26.895 31.874 3.412 1.00 7.75 ? 439 PHE A CE1 1 ATOM 2826 C CE2 . PHE A 1 353 ? 28.565 32.950 2.127 1.00 9.88 ? 439 PHE A CE2 1 ATOM 2827 C CZ . PHE A 1 353 ? 27.250 32.816 2.472 1.00 9.60 ? 439 PHE A CZ 1 ATOM 2828 N N . ILE A 1 354 ? 31.671 28.926 1.922 1.00 7.30 ? 440 ILE A N 1 ATOM 2829 C CA . ILE A 1 354 ? 31.891 28.784 0.493 1.00 8.14 ? 440 ILE A CA 1 ATOM 2830 C C . ILE A 1 354 ? 31.659 27.333 0.043 1.00 7.29 ? 440 ILE A C 1 ATOM 2831 O O . ILE A 1 354 ? 31.051 27.104 -0.983 1.00 7.91 ? 440 ILE A O 1 ATOM 2832 C CB . ILE A 1 354 ? 33.329 29.238 0.116 1.00 8.68 ? 440 ILE A CB 1 ATOM 2833 C CG1 . ILE A 1 354 ? 33.477 30.753 0.294 1.00 10.69 ? 440 ILE A CG1 1 ATOM 2834 C CG2 . ILE A 1 354 ? 33.657 28.897 -1.316 1.00 10.17 ? 440 ILE A CG2 1 ATOM 2835 C CD1 . ILE A 1 354 ? 34.870 31.304 0.210 1.00 14.49 ? 440 ILE A CD1 1 ATOM 2836 N N . GLN A 1 355 ? 32.125 26.345 0.840 1.00 7.67 ? 441 GLN A N 1 ATOM 2837 C CA . GLN A 1 355 ? 31.834 24.948 0.543 1.00 7.52 ? 441 GLN A CA 1 ATOM 2838 C C . GLN A 1 355 ? 30.308 24.738 0.381 1.00 7.03 ? 441 GLN A C 1 ATOM 2839 O O . GLN A 1 355 ? 29.849 24.090 -0.540 1.00 7.07 ? 441 GLN A O 1 ATOM 2840 C CB . GLN A 1 355 ? 32.373 24.066 1.689 1.00 7.52 ? 441 GLN A CB 1 ATOM 2841 C CG . GLN A 1 355 ? 32.036 22.586 1.520 1.00 7.69 ? 441 GLN A CG 1 ATOM 2842 C CD . GLN A 1 355 ? 32.334 21.803 2.756 1.00 7.42 ? 441 GLN A CD 1 ATOM 2843 O OE1 . GLN A 1 355 ? 33.489 21.592 3.136 1.00 8.46 ? 441 GLN A OE1 1 ATOM 2844 N NE2 . GLN A 1 355 ? 31.276 21.364 3.452 1.00 7.66 ? 441 GLN A NE2 1 ATOM 2845 N N . LEU A 1 356 ? 29.554 25.265 1.385 1.00 7.12 ? 442 LEU A N 1 ATOM 2846 C CA . LEU A 1 356 ? 28.098 25.071 1.374 1.00 7.04 ? 442 LEU A CA 1 ATOM 2847 C C . LEU A 1 356 ? 27.477 25.699 0.132 1.00 6.62 ? 442 LEU A C 1 ATOM 2848 O O . LEU A 1 356 ? 26.524 25.147 -0.426 1.00 7.32 ? 442 LEU A O 1 ATOM 2849 C CB . LEU A 1 356 ? 27.491 25.659 2.651 1.00 7.00 ? 442 LEU A CB 1 ATOM 2850 C CG . LEU A 1 356 ? 27.738 24.871 3.920 1.00 6.72 ? 442 LEU A CG 1 ATOM 2851 C CD1 . LEU A 1 356 ? 27.217 25.732 5.078 1.00 7.08 ? 442 LEU A CD1 1 ATOM 2852 C CD2 . LEU A 1 356 ? 27.072 23.503 3.898 1.00 7.60 ? 442 LEU A CD2 1 ATOM 2853 N N . LEU A 1 357 ? 27.984 26.854 -0.290 1.00 7.83 ? 443 LEU A N 1 ATOM 2854 C CA . LEU A 1 357 ? 27.498 27.518 -1.529 1.00 7.94 ? 443 LEU A CA 1 ATOM 2855 C C . LEU A 1 357 ? 27.832 26.685 -2.740 1.00 7.94 ? 443 LEU A C 1 ATOM 2856 O O . LEU A 1 357 ? 26.978 26.484 -3.619 1.00 9.12 ? 443 LEU A O 1 ATOM 2857 C CB . LEU A 1 357 ? 28.122 28.893 -1.694 1.00 10.60 ? 443 LEU A CB 1 ATOM 2858 C CG . LEU A 1 357 ? 27.535 30.013 -0.862 1.00 12.52 ? 443 LEU A CG 1 ATOM 2859 C CD1 . LEU A 1 357 ? 28.381 31.279 -1.170 1.00 15.32 ? 443 LEU A CD1 1 ATOM 2860 C CD2 . LEU A 1 357 ? 26.087 30.299 -1.182 1.00 14.30 ? 443 LEU A CD2 1 ATOM 2861 N N . ARG A 1 358 ? 29.046 26.216 -2.861 1.00 7.99 ? 444 ARG A N 1 ATOM 2862 C CA . ARG A 1 358 ? 29.428 25.412 -4.042 1.00 8.69 ? 444 ARG A CA 1 ATOM 2863 C C . ARG A 1 358 ? 28.595 24.201 -4.184 1.00 7.78 ? 444 ARG A C 1 ATOM 2864 O O . ARG A 1 358 ? 28.248 23.807 -5.323 1.00 9.26 ? 444 ARG A O 1 ATOM 2865 C CB . ARG A 1 358 ? 30.909 25.013 -3.936 1.00 9.82 ? 444 ARG A CB 1 ATOM 2866 C CG . ARG A 1 358 ? 31.926 26.114 -4.150 1.00 11.92 ? 444 ARG A CG 1 ATOM 2867 C CD . ARG A 1 358 ? 33.337 25.529 -4.108 1.00 16.44 ? 444 ARG A CD 1 ATOM 2868 N NE . ARG A 1 358 ? 34.419 26.493 -4.292 1.00 21.24 ? 444 ARG A NE 1 ATOM 2869 C CZ . ARG A 1 358 ? 34.920 26.851 -5.424 1.00 27.30 ? 444 ARG A CZ 1 ATOM 2870 N NH1 . ARG A 1 358 ? 34.432 26.356 -6.573 1.00 28.44 ? 444 ARG A NH1 1 ATOM 2871 N NH2 . ARG A 1 358 ? 35.941 27.719 -5.390 1.00 30.03 ? 444 ARG A NH2 1 ATOM 2872 N N . ASN A 1 359 ? 28.262 23.534 -3.074 1.00 7.66 ? 445 ASN A N 1 ATOM 2873 C CA . ASN A 1 359 ? 27.518 22.291 -3.075 1.00 7.98 ? 445 ASN A CA 1 ATOM 2874 C C . ASN A 1 359 ? 26.022 22.502 -2.900 1.00 7.50 ? 445 ASN A C 1 ATOM 2875 O O . ASN A 1 359 ? 25.304 21.525 -2.712 1.00 8.57 ? 445 ASN A O 1 ATOM 2876 C CB . ASN A 1 359 ? 28.044 21.368 -1.977 1.00 7.81 ? 445 ASN A CB 1 ATOM 2877 C CG . ASN A 1 359 ? 29.391 20.830 -2.238 1.00 8.63 ? 445 ASN A CG 1 ATOM 2878 O OD1 . ASN A 1 359 ? 29.654 20.350 -3.388 1.00 10.27 ? 445 ASN A OD1 1 ATOM 2879 N ND2 . ASN A 1 359 ? 30.244 20.766 -1.232 1.00 10.39 ? 445 ASN A ND2 1 ATOM 2880 N N . ALA A 1 360 ? 25.525 23.741 -2.971 1.00 7.88 ? 446 ALA A N 1 ATOM 2881 C CA . ALA A 1 360 ? 24.117 23.998 -2.676 1.00 7.30 ? 446 ALA A CA 1 ATOM 2882 C C . ALA A 1 360 ? 23.227 23.231 -3.651 1.00 7.75 ? 446 ALA A C 1 ATOM 2883 O O . ALA A 1 360 ? 23.468 23.246 -4.898 1.00 8.23 ? 446 ALA A O 1 ATOM 2884 C CB . ALA A 1 360 ? 23.831 25.477 -2.748 1.00 8.22 ? 446 ALA A CB 1 ATOM 2885 N N . ASN A 1 361 ? 22.142 22.709 -3.142 1.00 7.80 ? 447 ASN A N 1 ATOM 2886 C CA . ASN A 1 361 ? 21.141 22.048 -3.935 1.00 8.83 ? 447 ASN A CA 1 ATOM 2887 C C . ASN A 1 361 ? 19.802 22.222 -3.291 1.00 8.73 ? 447 ASN A C 1 ATOM 2888 O O . ASN A 1 361 ? 19.536 21.642 -2.216 1.00 9.55 ? 447 ASN A O 1 ATOM 2889 C CB . ASN A 1 361 ? 21.483 20.574 -4.031 1.00 10.10 ? 447 ASN A CB 1 ATOM 2890 C CG . ASN A 1 361 ? 20.478 19.794 -4.769 1.00 13.16 ? 447 ASN A CG 1 ATOM 2891 O OD1 . ASN A 1 361 ? 19.832 20.325 -5.671 1.00 15.77 ? 447 ASN A OD1 1 ATOM 2892 N ND2 . ASN A 1 361 ? 20.243 18.526 -4.318 1.00 15.51 ? 447 ASN A ND2 1 ATOM 2893 N N . PRO A 1 362 ? 18.913 23.020 -3.837 1.00 9.84 ? 448 PRO A N 1 ATOM 2894 C CA . PRO A 1 362 ? 19.087 23.736 -5.113 1.00 9.81 ? 448 PRO A CA 1 ATOM 2895 C C . PRO A 1 362 ? 20.184 24.780 -5.074 1.00 9.47 ? 448 PRO A C 1 ATOM 2896 O O . PRO A 1 362 ? 20.423 25.403 -4.026 1.00 9.48 ? 448 PRO A O 1 ATOM 2897 C CB . PRO A 1 362 ? 17.715 24.403 -5.322 1.00 12.09 ? 448 PRO A CB 1 ATOM 2898 C CG . PRO A 1 362 ? 16.759 23.487 -4.538 1.00 15.42 ? 448 PRO A CG 1 ATOM 2899 C CD . PRO A 1 362 ? 17.551 23.211 -3.287 1.00 11.62 ? 448 PRO A CD 1 ATOM 2900 N N . PRO A 1 363 ? 20.844 25.019 -6.199 1.00 9.68 ? 449 PRO A N 1 ATOM 2901 C CA . PRO A 1 363 ? 21.896 26.001 -6.256 1.00 9.68 ? 449 PRO A CA 1 ATOM 2902 C C . PRO A 1 363 ? 21.336 27.417 -6.072 1.00 9.98 ? 449 PRO A C 1 ATOM 2903 O O . PRO A 1 363 ? 20.191 27.695 -6.317 1.00 10.95 ? 449 PRO A O 1 ATOM 2904 C CB . PRO A 1 363 ? 22.508 25.808 -7.634 1.00 11.18 ? 449 PRO A CB 1 ATOM 2905 C CG . PRO A 1 363 ? 21.420 25.254 -8.439 1.00 14.78 ? 449 PRO A CG 1 ATOM 2906 C CD . PRO A 1 363 ? 20.641 24.362 -7.514 1.00 11.63 ? 449 PRO A CD 1 ATOM 2907 N N . PHE A 1 364 ? 22.217 28.309 -5.653 1.00 10.76 ? 450 PHE A N 1 ATOM 2908 C CA . PHE A 1 364 ? 21.969 29.750 -5.574 1.00 12.36 ? 450 PHE A CA 1 ATOM 2909 C C . PHE A 1 364 ? 22.432 30.476 -6.828 1.00 16.83 ? 450 PHE A C 1 ATOM 2910 O O . PHE A 1 364 ? 23.246 29.959 -7.562 1.00 17.65 ? 450 PHE A O 1 ATOM 2911 C CB . PHE A 1 364 ? 22.632 30.341 -4.322 1.00 12.37 ? 450 PHE A CB 1 ATOM 2912 C CG . PHE A 1 364 ? 21.917 29.979 -3.088 1.00 11.05 ? 450 PHE A CG 1 ATOM 2913 C CD1 . PHE A 1 364 ? 20.785 30.667 -2.626 1.00 10.59 ? 450 PHE A CD1 1 ATOM 2914 C CD2 . PHE A 1 364 ? 22.313 28.862 -2.356 1.00 10.72 ? 450 PHE A CD2 1 ATOM 2915 C CE1 . PHE A 1 364 ? 20.104 30.289 -1.514 1.00 10.78 ? 450 PHE A CE1 1 ATOM 2916 C CE2 . PHE A 1 364 ? 21.630 28.514 -1.212 1.00 10.40 ? 450 PHE A CE2 1 ATOM 2917 C CZ . PHE A 1 364 ? 20.529 29.205 -0.804 1.00 10.40 ? 450 PHE A CZ 1 ATOM 2918 O OXT . PHE A 1 364 ? 21.879 31.566 -7.023 1.00 21.33 ? 450 PHE A OXT 1 HETATM 2919 C C1 . NAG B 2 . ? 20.669 36.085 32.216 1.00 7.11 ? 500 NAG A C1 1 HETATM 2920 C C2 . NAG B 2 . ? 21.381 36.392 33.519 1.00 7.26 ? 500 NAG A C2 1 HETATM 2921 C C3 . NAG B 2 . ? 20.520 37.301 34.395 1.00 7.73 ? 500 NAG A C3 1 HETATM 2922 C C4 . NAG B 2 . ? 19.989 38.475 33.649 1.00 8.08 ? 500 NAG A C4 1 HETATM 2923 C C5 . NAG B 2 . ? 19.356 38.033 32.346 1.00 8.06 ? 500 NAG A C5 1 HETATM 2924 C C6 . NAG B 2 . ? 18.845 39.139 31.479 1.00 8.59 ? 500 NAG A C6 1 HETATM 2925 C C7 . NAG B 2 . ? 22.811 34.820 34.828 1.00 8.50 ? 500 NAG A C7 1 HETATM 2926 C C8 . NAG B 2 . ? 22.861 33.523 35.552 1.00 9.17 ? 500 NAG A C8 1 HETATM 2927 N N2 . NAG B 2 . ? 21.667 35.151 34.213 1.00 7.82 ? 500 NAG A N2 1 HETATM 2928 O O3 . NAG B 2 . ? 21.268 37.765 35.524 1.00 8.61 ? 500 NAG A O3 1 HETATM 2929 O O4 . NAG B 2 . ? 18.993 39.177 34.420 1.00 9.93 ? 500 NAG A O4 1 HETATM 2930 O O5 . NAG B 2 . ? 20.290 37.301 31.572 1.00 7.65 ? 500 NAG A O5 1 HETATM 2931 O O6 . NAG B 2 . ? 18.155 38.616 30.356 1.00 8.17 ? 500 NAG A O6 1 HETATM 2932 O O7 . NAG B 2 . ? 23.789 35.604 34.810 1.00 9.56 ? 500 NAG A O7 1 HETATM 2933 MG MG . MG C 3 . ? 11.624 35.804 2.516 1.00 11.08 ? 501 MG A MG 1 HETATM 2934 C C . ACT D 4 . ? 9.493 31.678 3.522 1.00 11.82 ? 502 ACT A C 1 HETATM 2935 O O . ACT D 4 . ? 8.920 32.735 3.879 1.00 12.47 ? 502 ACT A O 1 HETATM 2936 O OXT . ACT D 4 . ? 10.619 31.731 2.930 1.00 14.77 ? 502 ACT A OXT 1 HETATM 2937 C CH3 . ACT D 4 . ? 8.857 30.361 3.755 1.00 14.44 ? 502 ACT A CH3 1 HETATM 2938 C C1 . DMF E 5 . ? 13.390 39.940 3.961 1.00 13.31 ? 503 DMF A C1 1 HETATM 2939 C C2 . DMF E 5 . ? 14.223 41.507 5.793 1.00 14.00 ? 503 DMF A C2 1 HETATM 2940 C C . DMF E 5 . ? 13.495 39.231 6.288 1.00 10.36 ? 503 DMF A C 1 HETATM 2941 O O . DMF E 5 . ? 13.066 38.105 5.984 1.00 10.08 ? 503 DMF A O 1 HETATM 2942 N N . DMF E 5 . ? 13.657 40.196 5.370 1.00 11.42 ? 503 DMF A N 1 HETATM 2943 C C1 . DMF F 5 . ? 3.504 8.498 5.487 1.00 16.60 ? 504 DMF A C1 1 HETATM 2944 C C2 . DMF F 5 . ? 1.265 8.727 6.564 1.00 13.49 ? 504 DMF A C2 1 HETATM 2945 C C . DMF F 5 . ? 2.919 6.968 7.211 1.00 16.34 ? 504 DMF A C 1 HETATM 2946 O O . DMF F 5 . ? 4.028 6.412 7.031 1.00 16.37 ? 504 DMF A O 1 HETATM 2947 N N . DMF F 5 . ? 2.544 8.013 6.457 1.00 15.38 ? 504 DMF A N 1 HETATM 2948 C C1 . GOL G 6 . ? -0.263 19.034 18.417 1.00 18.74 ? 505 GOL A C1 1 HETATM 2949 O O1 . GOL G 6 . ? -0.879 19.965 17.599 1.00 21.05 ? 505 GOL A O1 1 HETATM 2950 C C2 . GOL G 6 . ? 0.134 17.734 17.817 1.00 15.87 ? 505 GOL A C2 1 HETATM 2951 O O2 . GOL G 6 . ? 0.546 17.841 16.408 1.00 20.66 ? 505 GOL A O2 1 HETATM 2952 C C3 . GOL G 6 . ? 1.030 16.919 18.773 1.00 14.39 ? 505 GOL A C3 1 HETATM 2953 O O3 . GOL G 6 . ? 0.705 15.806 19.633 1.00 25.40 ? 505 GOL A O3 1 HETATM 2954 C C1 . GOL H 6 . ? 16.998 14.777 -0.432 1.00 17.99 ? 506 GOL A C1 1 HETATM 2955 O O1 . GOL H 6 . ? 15.775 14.691 0.247 1.00 17.01 ? 506 GOL A O1 1 HETATM 2956 C C2 . GOL H 6 . ? 17.783 15.987 0.144 1.00 15.17 ? 506 GOL A C2 1 HETATM 2957 O O2 . GOL H 6 . ? 18.045 15.702 1.547 1.00 14.12 ? 506 GOL A O2 1 HETATM 2958 C C3 . GOL H 6 . ? 19.085 16.230 -0.634 1.00 16.31 ? 506 GOL A C3 1 HETATM 2959 O O3 . GOL H 6 . ? 18.803 16.687 -1.972 1.00 19.04 ? 506 GOL A O3 1 HETATM 2960 C C2 . BGC I 7 . ? 28.119 21.894 20.106 0.70 12.71 ? 601 BGC A C2 1 HETATM 2961 C C3 . BGC I 7 . ? 27.470 23.239 20.361 0.70 15.10 ? 601 BGC A C3 1 HETATM 2962 C C4 . BGC I 7 . ? 26.635 23.655 19.158 0.70 15.28 ? 601 BGC A C4 1 HETATM 2963 C C5 . BGC I 7 . ? 25.561 22.561 18.871 0.70 14.40 ? 601 BGC A C5 1 HETATM 2964 C C6 . BGC I 7 . ? 24.705 22.747 17.624 0.70 12.66 ? 601 BGC A C6 1 HETATM 2965 C C1 . BGC I 7 . ? 27.036 20.861 19.734 0.70 13.80 ? 601 BGC A C1 1 HETATM 2966 O O2 . BGC I 7 . ? 28.800 21.526 21.316 0.70 13.28 ? 601 BGC A O2 1 HETATM 2967 O O3 . BGC I 7 . ? 28.550 24.124 20.657 0.70 14.46 ? 601 BGC A O3 1 HETATM 2968 O O4 . BGC I 7 . ? 26.075 24.915 19.422 0.70 15.47 ? 601 BGC A O4 1 HETATM 2969 O O5 . BGC I 7 . ? 26.217 21.294 18.651 0.70 15.28 ? 601 BGC A O5 1 HETATM 2970 O O6 . BGC I 7 . ? 25.486 22.879 16.511 0.70 15.10 ? 601 BGC A O6 1 HETATM 2971 C C1 . SGC J 8 . ? 25.770 15.444 18.572 0.70 11.38 ? 602 SGC A C1 1 HETATM 2972 C C2 . SGC J 8 . ? 24.862 16.585 18.222 0.70 10.56 ? 602 SGC A C2 1 HETATM 2973 O O2 . SGC J 8 . ? 24.272 16.332 16.977 0.70 14.06 ? 602 SGC A O2 1 HETATM 2974 C C3 . SGC J 8 . ? 25.725 17.858 18.130 0.70 12.49 ? 602 SGC A C3 1 HETATM 2975 O O3 . SGC J 8 . ? 24.868 18.962 17.938 0.70 15.50 ? 602 SGC A O3 1 HETATM 2976 C C4 . SGC J 8 . ? 26.625 18.112 19.365 0.70 11.98 ? 602 SGC A C4 1 HETATM 2977 C C5 . SGC J 8 . ? 27.376 16.844 19.672 0.70 12.18 ? 602 SGC A C5 1 HETATM 2978 O O5 . SGC J 8 . ? 26.452 15.747 19.796 0.70 13.15 ? 602 SGC A O5 1 HETATM 2979 C C6 . SGC J 8 . ? 28.234 16.908 20.950 0.70 11.57 ? 602 SGC A C6 1 HETATM 2980 O O6 . SGC J 8 . ? 28.970 15.646 21.043 0.70 12.09 ? 602 SGC A O6 1 HETATM 2981 S S4 . SGC J 8 . ? 27.895 19.397 19.121 0.70 12.50 ? 602 SGC A S4 1 HETATM 2982 C C1 . SGC K 8 . ? 25.924 9.652 18.835 0.70 13.16 ? 603 SGC A C1 1 HETATM 2983 C C2 . SGC K 8 . ? 26.166 10.417 20.128 0.70 13.79 ? 603 SGC A C2 1 HETATM 2984 O O2 . SGC K 8 . ? 25.709 9.661 21.267 0.70 17.35 ? 603 SGC A O2 1 HETATM 2985 C C3 . SGC K 8 . ? 25.366 11.693 20.136 0.70 13.59 ? 603 SGC A C3 1 HETATM 2986 O O3 . SGC K 8 . ? 25.607 12.441 21.342 0.70 16.95 ? 603 SGC A O3 1 HETATM 2987 C C4 . SGC K 8 . ? 25.686 12.605 18.958 0.70 12.76 ? 603 SGC A C4 1 HETATM 2988 C C5 . SGC K 8 . ? 25.507 11.769 17.696 0.70 11.91 ? 603 SGC A C5 1 HETATM 2989 O O5 . SGC K 8 . ? 26.285 10.553 17.785 0.70 13.61 ? 603 SGC A O5 1 HETATM 2990 C C6 . SGC K 8 . ? 25.830 12.535 16.435 0.70 11.60 ? 603 SGC A C6 1 HETATM 2991 O O6 . SGC K 8 . ? 25.575 11.723 15.315 0.70 10.91 ? 603 SGC A O6 1 HETATM 2992 S S4 . SGC K 8 . ? 24.623 14.061 18.913 0.70 13.70 ? 603 SGC A S4 1 HETATM 2993 C C1 . SGC L 8 . ? 26.063 4.372 16.523 0.70 13.05 ? 604 SGC A C1 1 HETATM 2994 C C2 . SGC L 8 . ? 26.749 5.459 15.728 0.70 14.05 ? 604 SGC A C2 1 HETATM 2995 O O2 . SGC L 8 . ? 27.854 4.981 14.946 0.70 15.78 ? 604 SGC A O2 1 HETATM 2996 C C3 . SGC L 8 . ? 27.237 6.591 16.614 0.70 14.89 ? 604 SGC A C3 1 HETATM 2997 O O3 . SGC L 8 . ? 27.754 7.618 15.725 0.70 13.04 ? 604 SGC A O3 1 HETATM 2998 C C4 . SGC L 8 . ? 26.124 7.079 17.608 0.70 13.32 ? 604 SGC A C4 1 HETATM 2999 C C5 . SGC L 8 . ? 25.428 5.888 18.247 0.70 14.35 ? 604 SGC A C5 1 HETATM 3000 O O5 . SGC L 8 . ? 24.991 4.999 17.237 0.70 15.67 ? 604 SGC A O5 1 HETATM 3001 C C6 . SGC L 8 . ? 24.176 6.328 18.973 0.70 15.12 ? 604 SGC A C6 1 HETATM 3002 O O6 . SGC L 8 . ? 23.463 5.164 19.517 0.70 16.92 ? 604 SGC A O6 1 HETATM 3003 S S4 . SGC L 8 . ? 26.948 8.160 18.834 0.70 16.71 ? 604 SGC A S4 1 HETATM 3004 C C1 . MA3 M 9 . ? 24.081 -0.939 16.862 0.70 23.63 ? 605 MA3 A C1 1 HETATM 3005 C C2 . MA3 M 9 . ? 23.578 0.203 17.737 0.70 22.46 ? 605 MA3 A C2 1 HETATM 3006 C C3 . MA3 M 9 . ? 23.812 1.560 17.069 0.70 19.48 ? 605 MA3 A C3 1 HETATM 3007 C C4 . MA3 M 9 . ? 25.208 1.667 16.443 0.70 17.28 ? 605 MA3 A C4 1 HETATM 3008 C C5 . MA3 M 9 . ? 25.506 0.437 15.527 0.70 19.39 ? 605 MA3 A C5 1 HETATM 3009 C C6 . MA3 M 9 . ? 26.942 0.365 15.012 0.70 20.13 ? 605 MA3 A C6 1 HETATM 3010 C C7 . MA3 M 9 . ? 23.340 -2.127 14.849 0.70 24.24 ? 605 MA3 A C7 1 HETATM 3011 O O1 . MA3 M 9 . ? 23.220 -0.964 15.711 0.70 22.47 ? 605 MA3 A O1 1 HETATM 3012 O O2 . MA3 M 9 . ? 22.210 0.036 18.003 0.70 24.19 ? 605 MA3 A O2 1 HETATM 3013 O O3 . MA3 M 9 . ? 23.613 2.616 18.031 0.70 20.25 ? 605 MA3 A O3 1 HETATM 3014 S S4 . MA3 M 9 . ? 25.386 3.140 15.404 0.70 15.68 ? 605 MA3 A S4 1 HETATM 3015 O O5 . MA3 M 9 . ? 25.310 -0.845 16.163 0.70 21.28 ? 605 MA3 A O5 1 HETATM 3016 O O6 . MA3 M 9 . ? 27.859 0.526 16.107 0.70 19.28 ? 605 MA3 A O6 1 HETATM 3017 O O . HOH N 10 . ? -1.910 35.203 21.477 1.00 11.91 ? 2001 HOH A O 1 HETATM 3018 O O . HOH N 10 . ? -0.038 33.406 15.944 1.00 14.63 ? 2002 HOH A O 1 HETATM 3019 O O . HOH N 10 . ? -4.560 34.275 21.824 1.00 11.31 ? 2003 HOH A O 1 HETATM 3020 O O . HOH N 10 . ? -2.753 33.368 13.574 1.00 24.66 ? 2004 HOH A O 1 HETATM 3021 O O . HOH N 10 . ? -5.656 34.482 15.112 1.00 26.76 ? 2005 HOH A O 1 HETATM 3022 O O . HOH N 10 . ? 0.445 23.769 18.295 1.00 12.43 ? 2006 HOH A O 1 HETATM 3023 O O . HOH N 10 . ? -3.053 25.310 17.731 0.30 16.02 ? 2007 HOH A O 1 HETATM 3024 O O . HOH N 10 . ? -4.632 29.495 12.123 1.00 17.20 ? 2008 HOH A O 1 HETATM 3025 O O . HOH N 10 . ? -1.798 27.549 10.956 1.00 20.37 ? 2009 HOH A O 1 HETATM 3026 O O . HOH N 10 . ? -7.415 29.478 17.211 1.00 33.61 ? 2010 HOH A O 1 HETATM 3027 O O . HOH N 10 . ? -1.605 23.428 16.479 1.00 16.56 ? 2011 HOH A O 1 HETATM 3028 O O . HOH N 10 . ? 5.948 29.339 6.045 1.00 12.65 ? 2012 HOH A O 1 HETATM 3029 O O . HOH N 10 . ? 1.340 28.511 3.933 0.50 16.53 ? 2013 HOH A O 1 HETATM 3030 O O . HOH N 10 . ? 0.551 22.071 6.412 0.55 17.56 ? 2014 HOH A O 1 HETATM 3031 O O . HOH N 10 . ? -2.525 23.011 9.391 1.00 20.32 ? 2015 HOH A O 1 HETATM 3032 O O . HOH N 10 . ? 1.238 25.919 2.986 0.50 22.76 ? 2016 HOH A O 1 HETATM 3033 O O . HOH N 10 . ? -1.426 34.396 8.757 0.60 27.08 ? 2017 HOH A O 1 HETATM 3034 O O . HOH N 10 . ? -1.909 33.891 5.240 1.00 34.49 ? 2018 HOH A O 1 HETATM 3035 O O . HOH N 10 . ? 9.709 35.194 2.956 1.00 12.38 ? 2019 HOH A O 1 HETATM 3036 O O . HOH N 10 . ? 6.509 40.749 2.673 1.00 25.97 ? 2020 HOH A O 1 HETATM 3037 O O . HOH N 10 . ? 7.793 38.722 0.836 1.00 28.64 ? 2021 HOH A O 1 HETATM 3038 O O . HOH N 10 . ? 11.898 32.957 11.074 1.00 7.99 ? 2022 HOH A O 1 HETATM 3039 O O . HOH N 10 . ? 21.642 42.822 8.572 1.00 20.44 ? 2023 HOH A O 1 HETATM 3040 O O . HOH N 10 . ? 14.678 44.909 9.891 1.00 21.29 ? 2024 HOH A O 1 HETATM 3041 O O . HOH N 10 . ? 15.697 44.007 7.769 1.00 32.20 ? 2025 HOH A O 1 HETATM 3042 O O . HOH N 10 . ? 23.433 42.365 13.176 0.50 18.94 ? 2026 HOH A O 1 HETATM 3043 O O . HOH N 10 . ? 25.148 42.072 13.575 0.50 21.50 ? 2027 HOH A O 1 HETATM 3044 O O . HOH N 10 . ? 21.675 43.408 12.875 0.50 29.50 ? 2028 HOH A O 1 HETATM 3045 O O . HOH N 10 . ? 25.301 44.764 9.800 1.00 30.34 ? 2029 HOH A O 1 HETATM 3046 O O . HOH N 10 . ? 29.677 43.474 1.807 1.00 20.23 ? 2030 HOH A O 1 HETATM 3047 O O . HOH N 10 . ? 27.186 43.402 0.796 1.00 22.19 ? 2031 HOH A O 1 HETATM 3048 O O . HOH N 10 . ? 29.748 43.046 11.435 0.50 16.69 ? 2032 HOH A O 1 HETATM 3049 O O . HOH N 10 . ? 33.198 44.196 6.774 1.00 20.57 ? 2033 HOH A O 1 HETATM 3050 O O . HOH N 10 . ? 35.240 41.469 8.479 0.50 27.42 ? 2034 HOH A O 1 HETATM 3051 O O . HOH N 10 . ? 35.563 39.850 6.669 0.50 19.95 ? 2035 HOH A O 1 HETATM 3052 O O . HOH N 10 . ? 38.596 32.405 5.389 1.00 21.02 ? 2036 HOH A O 1 HETATM 3053 O O . HOH N 10 . ? 34.911 35.642 9.410 1.00 20.70 ? 2037 HOH A O 1 HETATM 3054 O O . HOH N 10 . ? 36.603 37.877 8.978 1.00 30.07 ? 2038 HOH A O 1 HETATM 3055 O O . HOH N 10 . ? 38.124 34.318 7.158 1.00 31.31 ? 2039 HOH A O 1 HETATM 3056 O O . HOH N 10 . ? 36.594 39.433 -9.196 1.00 20.09 ? 2040 HOH A O 1 HETATM 3057 O O . HOH N 10 . ? 35.760 34.536 -4.508 1.00 22.61 ? 2041 HOH A O 1 HETATM 3058 O O . HOH N 10 . ? 3.351 28.374 2.723 0.50 21.56 ? 2042 HOH A O 1 HETATM 3059 O O . HOH N 10 . ? 36.138 34.964 -10.199 1.00 26.33 ? 2043 HOH A O 1 HETATM 3060 O O . HOH N 10 . ? 31.466 31.216 -9.486 1.00 39.02 ? 2044 HOH A O 1 HETATM 3061 O O . HOH N 10 . ? 31.488 35.060 -11.538 1.00 24.11 ? 2045 HOH A O 1 HETATM 3062 O O . HOH N 10 . ? -0.767 35.160 10.214 0.40 25.33 ? 2046 HOH A O 1 HETATM 3063 O O . HOH N 10 . ? -2.571 36.342 5.553 1.00 40.90 ? 2047 HOH A O 1 HETATM 3064 O O . HOH N 10 . ? 11.249 35.765 0.465 1.00 13.41 ? 2048 HOH A O 1 HETATM 3065 O O . HOH N 10 . ? 7.702 42.892 3.700 1.00 28.76 ? 2049 HOH A O 1 HETATM 3066 O O . HOH N 10 . ? 27.750 39.863 -7.653 1.00 18.11 ? 2050 HOH A O 1 HETATM 3067 O O . HOH N 10 . ? 25.187 33.915 -8.704 1.00 18.84 ? 2051 HOH A O 1 HETATM 3068 O O . HOH N 10 . ? 23.525 43.200 6.626 1.00 23.12 ? 2052 HOH A O 1 HETATM 3069 O O . HOH N 10 . ? 31.953 43.364 -0.101 1.00 19.77 ? 2053 HOH A O 1 HETATM 3070 O O . HOH N 10 . ? 28.279 42.945 -4.346 1.00 32.78 ? 2054 HOH A O 1 HETATM 3071 O O . HOH N 10 . ? 22.554 41.028 15.190 1.00 29.45 ? 2055 HOH A O 1 HETATM 3072 O O . HOH N 10 . ? 27.584 43.644 11.939 0.50 22.83 ? 2056 HOH A O 1 HETATM 3073 O O . HOH N 10 . ? 21.742 37.871 -5.099 1.00 18.79 ? 2057 HOH A O 1 HETATM 3074 O O . HOH N 10 . ? 41.109 31.571 4.539 1.00 35.54 ? 2058 HOH A O 1 HETATM 3075 O O . HOH N 10 . ? 26.080 42.041 -1.902 0.50 24.90 ? 2059 HOH A O 1 HETATM 3076 O O . HOH N 10 . ? 26.594 40.795 -3.094 0.50 26.83 ? 2060 HOH A O 1 HETATM 3077 O O . HOH N 10 . ? 20.532 42.025 -0.251 1.00 30.32 ? 2061 HOH A O 1 HETATM 3078 O O . HOH N 10 . ? 20.118 38.844 -2.964 1.00 30.33 ? 2062 HOH A O 1 HETATM 3079 O O . HOH N 10 . ? 30.248 33.196 -13.270 1.00 32.61 ? 2063 HOH A O 1 HETATM 3080 O O . HOH N 10 . ? 32.563 36.575 -13.555 1.00 33.54 ? 2064 HOH A O 1 HETATM 3081 O O . HOH N 10 . ? 25.758 40.589 -5.861 1.00 30.17 ? 2065 HOH A O 1 HETATM 3082 O O . HOH N 10 . ? 17.280 33.535 -1.483 1.00 22.75 ? 2066 HOH A O 1 HETATM 3083 O O . HOH N 10 . ? 22.341 43.952 4.104 1.00 35.51 ? 2067 HOH A O 1 HETATM 3084 O O . HOH N 10 . ? 20.928 36.049 -6.759 1.00 32.10 ? 2068 HOH A O 1 HETATM 3085 O O . HOH N 10 . ? 19.094 35.740 7.436 1.00 8.70 ? 2069 HOH A O 1 HETATM 3086 O O . HOH N 10 . ? 16.424 41.875 2.776 1.00 19.48 ? 2070 HOH A O 1 HETATM 3087 O O . HOH N 10 . ? 21.129 39.684 1.137 1.00 10.90 ? 2071 HOH A O 1 HETATM 3088 O O . HOH N 10 . ? 14.539 38.595 0.896 1.00 13.86 ? 2072 HOH A O 1 HETATM 3089 O O . HOH N 10 . ? 13.586 36.322 2.100 1.00 12.10 ? 2073 HOH A O 1 HETATM 3090 O O . HOH N 10 . ? 14.332 33.216 0.919 1.00 14.24 ? 2074 HOH A O 1 HETATM 3091 O O . HOH N 10 . ? 17.560 37.189 -2.680 1.00 34.50 ? 2075 HOH A O 1 HETATM 3092 O O . HOH N 10 . ? 13.328 35.312 -1.213 1.00 42.57 ? 2076 HOH A O 1 HETATM 3093 O O . HOH N 10 . ? 11.976 39.606 0.574 1.00 21.31 ? 2077 HOH A O 1 HETATM 3094 O O . HOH N 10 . ? 15.120 37.658 -1.668 1.00 28.89 ? 2078 HOH A O 1 HETATM 3095 O O . HOH N 10 . ? 14.308 30.493 0.901 1.00 14.19 ? 2079 HOH A O 1 HETATM 3096 O O . HOH N 10 . ? 14.187 43.270 2.202 1.00 29.29 ? 2080 HOH A O 1 HETATM 3097 O O . HOH N 10 . ? 11.065 39.043 -1.793 1.00 42.17 ? 2081 HOH A O 1 HETATM 3098 O O . HOH N 10 . ? 17.694 33.826 8.835 1.00 8.50 ? 2082 HOH A O 1 HETATM 3099 O O . HOH N 10 . ? 15.249 33.956 11.410 1.00 8.00 ? 2083 HOH A O 1 HETATM 3100 O O . HOH N 10 . ? 19.991 31.377 6.647 1.00 8.50 ? 2084 HOH A O 1 HETATM 3101 O O . HOH N 10 . ? 20.024 32.301 11.660 1.00 7.54 ? 2085 HOH A O 1 HETATM 3102 O O . HOH N 10 . ? 21.123 34.309 15.127 0.50 16.24 ? 2086 HOH A O 1 HETATM 3103 O O . HOH N 10 . ? 25.387 38.771 19.590 1.00 26.32 ? 2087 HOH A O 1 HETATM 3104 O O . HOH N 10 . ? 13.656 42.599 32.756 1.00 22.83 ? 2088 HOH A O 1 HETATM 3105 O O . HOH N 10 . ? 13.150 44.727 26.166 1.00 32.06 ? 2089 HOH A O 1 HETATM 3106 O O . HOH N 10 . ? 9.777 48.356 7.243 1.00 38.66 ? 2090 HOH A O 1 HETATM 3107 O O . HOH N 10 . ? 23.111 33.274 18.466 0.50 19.18 ? 2091 HOH A O 1 HETATM 3108 O O . HOH N 10 . ? 21.753 32.146 15.850 0.50 10.19 ? 2092 HOH A O 1 HETATM 3109 O O . HOH N 10 . ? 25.238 19.599 41.683 1.00 36.47 ? 2093 HOH A O 1 HETATM 3110 O O . HOH N 10 . ? 25.023 32.961 19.521 0.50 17.32 ? 2094 HOH A O 1 HETATM 3111 O O . HOH N 10 . ? 27.529 30.834 19.673 0.50 22.45 ? 2095 HOH A O 1 HETATM 3112 O O . HOH N 10 . ? 26.769 27.860 22.790 1.00 16.19 ? 2096 HOH A O 1 HETATM 3113 O O . HOH N 10 . ? 8.133 49.270 15.063 0.40 18.50 ? 2097 HOH A O 1 HETATM 3114 O O . HOH N 10 . ? 17.225 35.469 38.524 0.50 18.82 ? 2098 HOH A O 1 HETATM 3115 O O . HOH N 10 . ? 28.516 38.616 23.988 1.00 23.18 ? 2099 HOH A O 1 HETATM 3116 O O . HOH N 10 . ? 26.794 36.510 19.065 1.00 27.84 ? 2100 HOH A O 1 HETATM 3117 O O . HOH N 10 . ? 10.865 45.936 7.998 1.00 27.18 ? 2101 HOH A O 1 HETATM 3118 O O . HOH N 10 . ? 8.681 47.228 5.145 1.00 25.32 ? 2102 HOH A O 1 HETATM 3119 O O . HOH N 10 . ? 11.387 37.496 40.047 1.00 33.64 ? 2103 HOH A O 1 HETATM 3120 O O . HOH N 10 . ? 24.423 35.519 31.340 1.00 14.92 ? 2104 HOH A O 1 HETATM 3121 O O . HOH N 10 . ? 19.891 38.421 28.188 1.00 8.52 ? 2105 HOH A O 1 HETATM 3122 O O . HOH N 10 . ? 17.499 35.780 30.531 1.00 8.68 ? 2106 HOH A O 1 HETATM 3123 O O . HOH N 10 . ? -0.820 46.224 6.941 1.00 36.69 ? 2107 HOH A O 1 HETATM 3124 O O . HOH N 10 . ? 5.983 52.399 13.682 1.00 33.69 ? 2108 HOH A O 1 HETATM 3125 O O . HOH N 10 . ? 11.652 42.241 1.593 1.00 23.24 ? 2109 HOH A O 1 HETATM 3126 O O . HOH N 10 . ? 11.349 44.026 5.881 1.00 35.79 ? 2110 HOH A O 1 HETATM 3127 O O . HOH N 10 . ? 14.442 11.328 36.119 1.00 34.00 ? 2111 HOH A O 1 HETATM 3128 O O . HOH N 10 . ? 16.056 43.912 26.155 0.55 13.27 ? 2112 HOH A O 1 HETATM 3129 O O . HOH N 10 . ? 16.185 41.742 31.904 1.00 13.15 ? 2113 HOH A O 1 HETATM 3130 O O . HOH N 10 . ? 19.294 44.962 23.963 0.50 18.91 ? 2114 HOH A O 1 HETATM 3131 O O . HOH N 10 . ? 17.258 45.050 25.684 0.45 12.93 ? 2115 HOH A O 1 HETATM 3132 O O . HOH N 10 . ? 15.353 44.484 27.565 0.45 11.72 ? 2116 HOH A O 1 HETATM 3133 O O . HOH N 10 . ? 28.185 15.582 36.769 0.50 20.85 ? 2117 HOH A O 1 HETATM 3134 O O . HOH N 10 . ? 29.512 14.944 36.193 0.50 22.51 ? 2118 HOH A O 1 HETATM 3135 O O . HOH N 10 . ? 26.575 18.608 39.296 1.00 25.64 ? 2119 HOH A O 1 HETATM 3136 O O . HOH N 10 . ? 30.210 20.932 37.504 1.00 25.02 ? 2120 HOH A O 1 HETATM 3137 O O . HOH N 10 . ? 30.435 11.320 20.951 0.70 17.88 ? 2121 HOH A O 1 HETATM 3138 O O . HOH N 10 . ? 16.574 46.547 15.635 0.70 29.20 ? 2122 HOH A O 1 HETATM 3139 O O . HOH N 10 . ? 19.915 41.321 15.708 1.00 27.92 ? 2123 HOH A O 1 HETATM 3140 O O . HOH N 10 . ? 17.881 44.599 22.008 1.00 40.87 ? 2124 HOH A O 1 HETATM 3141 O O . HOH N 10 . ? 16.080 45.896 20.602 1.00 43.26 ? 2125 HOH A O 1 HETATM 3142 O O . HOH N 10 . ? 20.893 44.786 21.842 0.30 11.48 ? 2126 HOH A O 1 HETATM 3143 O O . HOH N 10 . ? 27.939 35.688 28.061 0.50 18.62 ? 2127 HOH A O 1 HETATM 3144 O O . HOH N 10 . ? 18.580 39.304 14.553 1.00 21.29 ? 2128 HOH A O 1 HETATM 3145 O O . HOH N 10 . ? 20.312 21.611 41.368 1.00 18.57 ? 2129 HOH A O 1 HETATM 3146 O O . HOH N 10 . ? 27.930 29.873 35.853 1.00 26.40 ? 2130 HOH A O 1 HETATM 3147 O O . HOH N 10 . ? 11.338 46.544 21.214 1.00 36.43 ? 2131 HOH A O 1 HETATM 3148 O O . HOH N 10 . ? 8.874 47.032 16.602 1.00 14.06 ? 2132 HOH A O 1 HETATM 3149 O O . HOH N 10 . ? 24.838 8.723 -5.277 1.00 44.51 ? 2133 HOH A O 1 HETATM 3150 O O . HOH N 10 . ? 19.308 43.570 14.321 0.70 25.17 ? 2134 HOH A O 1 HETATM 3151 O O . HOH N 10 . ? 16.300 40.041 12.789 1.00 10.01 ? 2135 HOH A O 1 HETATM 3152 O O . HOH N 10 . ? 14.864 34.010 39.193 1.00 25.40 ? 2136 HOH A O 1 HETATM 3153 O O . HOH N 10 . ? 17.881 22.323 42.369 1.00 42.26 ? 2137 HOH A O 1 HETATM 3154 O O . HOH N 10 . ? 19.149 34.209 37.068 1.00 11.81 ? 2138 HOH A O 1 HETATM 3155 O O . HOH N 10 . ? 8.152 47.148 19.225 1.00 18.88 ? 2139 HOH A O 1 HETATM 3156 O O . HOH N 10 . ? 4.313 48.057 20.662 1.00 38.29 ? 2140 HOH A O 1 HETATM 3157 O O . HOH N 10 . ? 10.890 35.189 38.881 1.00 22.91 ? 2141 HOH A O 1 HETATM 3158 O O . HOH N 10 . ? 7.402 41.826 31.152 1.00 30.53 ? 2142 HOH A O 1 HETATM 3159 O O . HOH N 10 . ? -0.285 28.003 31.158 1.00 26.66 ? 2143 HOH A O 1 HETATM 3160 O O . HOH N 10 . ? -1.265 31.462 33.041 1.00 37.59 ? 2144 HOH A O 1 HETATM 3161 O O . HOH N 10 . ? 6.289 49.346 10.824 1.00 13.47 ? 2145 HOH A O 1 HETATM 3162 O O . HOH N 10 . ? 12.016 45.363 10.358 1.00 14.25 ? 2146 HOH A O 1 HETATM 3163 O O . HOH N 10 . ? 7.263 44.815 5.509 1.00 18.11 ? 2147 HOH A O 1 HETATM 3164 O O . HOH N 10 . ? 3.269 40.805 13.930 1.00 18.53 ? 2148 HOH A O 1 HETATM 3165 O O . HOH N 10 . ? -3.734 30.613 7.946 1.00 30.57 ? 2149 HOH A O 1 HETATM 3166 O O . HOH N 10 . ? 6.818 48.436 15.443 0.60 22.27 ? 2150 HOH A O 1 HETATM 3167 O O . HOH N 10 . ? 5.985 49.786 13.444 1.00 23.35 ? 2151 HOH A O 1 HETATM 3168 O O . HOH N 10 . ? 0.027 48.321 10.929 1.00 28.38 ? 2152 HOH A O 1 HETATM 3169 O O . HOH N 10 . ? 0.835 48.445 6.903 1.00 18.51 ? 2153 HOH A O 1 HETATM 3170 O O . HOH N 10 . ? 6.693 48.537 3.897 1.00 26.04 ? 2154 HOH A O 1 HETATM 3171 O O . HOH N 10 . ? 45.462 27.901 12.055 1.00 37.78 ? 2155 HOH A O 1 HETATM 3172 O O . HOH N 10 . ? 0.421 44.471 2.470 1.00 27.54 ? 2156 HOH A O 1 HETATM 3173 O O . HOH N 10 . ? 41.394 26.181 30.627 1.00 44.94 ? 2157 HOH A O 1 HETATM 3174 O O . HOH N 10 . ? 1.404 42.170 8.051 1.00 21.03 ? 2158 HOH A O 1 HETATM 3175 O O . HOH N 10 . ? -1.334 41.669 5.626 1.00 49.63 ? 2159 HOH A O 1 HETATM 3176 O O . HOH N 10 . ? 4.457 41.581 1.468 1.00 27.10 ? 2160 HOH A O 1 HETATM 3177 O O . HOH N 10 . ? 17.131 5.175 31.739 1.00 34.85 ? 2161 HOH A O 1 HETATM 3178 O O . HOH N 10 . ? 43.122 8.527 9.802 1.00 56.68 ? 2162 HOH A O 1 HETATM 3179 O O . HOH N 10 . ? 28.780 7.374 21.960 1.00 32.52 ? 2163 HOH A O 1 HETATM 3180 O O . HOH N 10 . ? -0.051 37.093 14.369 1.00 22.51 ? 2164 HOH A O 1 HETATM 3181 O O . HOH N 10 . ? -0.487 41.471 9.795 1.00 30.30 ? 2165 HOH A O 1 HETATM 3182 O O . HOH N 10 . ? -0.777 36.988 7.534 1.00 23.35 ? 2166 HOH A O 1 HETATM 3183 O O . HOH N 10 . ? 3.389 36.451 13.064 1.00 10.58 ? 2167 HOH A O 1 HETATM 3184 O O . HOH N 10 . ? 10.990 37.762 2.472 1.00 12.06 ? 2168 HOH A O 1 HETATM 3185 O O . HOH N 10 . ? 10.246 42.061 3.904 1.00 23.62 ? 2169 HOH A O 1 HETATM 3186 O O . HOH N 10 . ? 32.707 10.546 31.120 1.00 20.57 ? 2170 HOH A O 1 HETATM 3187 O O . HOH N 10 . ? 31.715 13.677 34.457 0.50 18.11 ? 2171 HOH A O 1 HETATM 3188 O O . HOH N 10 . ? 32.548 16.044 33.198 1.00 36.25 ? 2172 HOH A O 1 HETATM 3189 O O . HOH N 10 . ? 17.899 10.155 37.042 1.00 22.13 ? 2173 HOH A O 1 HETATM 3190 O O . HOH N 10 . ? 21.701 17.261 40.904 1.00 29.83 ? 2174 HOH A O 1 HETATM 3191 O O . HOH N 10 . ? 13.983 27.475 8.569 1.00 7.28 ? 2175 HOH A O 1 HETATM 3192 O O . HOH N 10 . ? 13.703 34.084 13.817 1.00 9.30 ? 2176 HOH A O 1 HETATM 3193 O O . HOH N 10 . ? 16.222 9.645 34.966 1.00 39.33 ? 2177 HOH A O 1 HETATM 3194 O O . HOH N 10 . ? 6.982 22.310 35.474 1.00 16.72 ? 2178 HOH A O 1 HETATM 3195 O O . HOH N 10 . ? 8.665 17.979 36.523 1.00 34.16 ? 2179 HOH A O 1 HETATM 3196 O O . HOH N 10 . ? 7.293 32.885 37.210 0.60 23.58 ? 2180 HOH A O 1 HETATM 3197 O O . HOH N 10 . ? 1.204 25.513 34.248 1.00 29.99 ? 2181 HOH A O 1 HETATM 3198 O O . HOH N 10 . ? -1.439 20.565 32.392 1.00 41.38 ? 2182 HOH A O 1 HETATM 3199 O O . HOH N 10 . ? 1.857 19.994 38.495 1.00 26.58 ? 2183 HOH A O 1 HETATM 3200 O O . HOH N 10 . ? 3.466 24.318 37.748 0.50 18.07 ? 2184 HOH A O 1 HETATM 3201 O O . HOH N 10 . ? 6.817 25.646 38.154 1.00 32.42 ? 2185 HOH A O 1 HETATM 3202 O O . HOH N 10 . ? -4.323 25.205 25.997 1.00 21.71 ? 2186 HOH A O 1 HETATM 3203 O O . HOH N 10 . ? -3.363 27.644 25.092 1.00 19.31 ? 2187 HOH A O 1 HETATM 3204 O O . HOH N 10 . ? 24.428 25.966 29.846 1.00 9.77 ? 2188 HOH A O 1 HETATM 3205 O O . HOH N 10 . ? 25.500 16.008 35.597 1.00 11.78 ? 2189 HOH A O 1 HETATM 3206 O O . HOH N 10 . ? 28.866 21.125 33.825 1.00 21.51 ? 2190 HOH A O 1 HETATM 3207 O O . HOH N 10 . ? 27.422 20.470 37.528 1.00 13.36 ? 2191 HOH A O 1 HETATM 3208 O O . HOH N 10 . ? 28.949 17.902 35.724 1.00 23.59 ? 2192 HOH A O 1 HETATM 3209 O O . HOH N 10 . ? 22.112 19.333 26.525 1.00 7.54 ? 2193 HOH A O 1 HETATM 3210 O O . HOH N 10 . ? 29.877 17.711 28.341 1.00 19.80 ? 2194 HOH A O 1 HETATM 3211 O O . HOH N 10 . ? 10.966 -0.640 16.671 0.50 28.97 ? 2195 HOH A O 1 HETATM 3212 O O . HOH N 10 . ? 20.405 -2.022 13.012 1.00 37.46 ? 2196 HOH A O 1 HETATM 3213 O O . HOH N 10 . ? 30.660 13.804 30.027 0.50 11.61 ? 2197 HOH A O 1 HETATM 3214 O O . HOH N 10 . ? 28.878 10.914 23.113 0.50 14.83 ? 2198 HOH A O 1 HETATM 3215 O O . HOH N 10 . ? 30.121 12.287 21.903 0.30 13.58 ? 2199 HOH A O 1 HETATM 3216 O O . HOH N 10 . ? 32.295 11.990 24.877 1.00 24.66 ? 2200 HOH A O 1 HETATM 3217 O O . HOH N 10 . ? 30.879 14.092 28.483 0.50 14.17 ? 2201 HOH A O 1 HETATM 3218 O O . HOH N 10 . ? 36.957 18.746 27.165 1.00 23.20 ? 2202 HOH A O 1 HETATM 3219 O O . HOH N 10 . ? 33.209 17.298 29.200 1.00 49.57 ? 2203 HOH A O 1 HETATM 3220 O O . HOH N 10 . ? 37.785 15.864 25.499 0.50 26.47 ? 2204 HOH A O 1 HETATM 3221 O O . HOH N 10 . ? 31.391 20.273 21.293 1.00 12.88 ? 2205 HOH A O 1 HETATM 3222 O O . HOH N 10 . ? 33.141 20.338 28.762 1.00 29.41 ? 2206 HOH A O 1 HETATM 3223 O O . HOH N 10 . ? -3.090 19.499 21.210 1.00 32.87 ? 2207 HOH A O 1 HETATM 3224 O O . HOH N 10 . ? -2.998 16.545 19.245 1.00 27.95 ? 2208 HOH A O 1 HETATM 3225 O O . HOH N 10 . ? -4.013 16.245 23.588 1.00 25.37 ? 2209 HOH A O 1 HETATM 3226 O O . HOH N 10 . ? 28.029 29.028 25.023 1.00 23.92 ? 2210 HOH A O 1 HETATM 3227 O O . HOH N 10 . ? 34.052 27.491 22.556 1.00 31.84 ? 2211 HOH A O 1 HETATM 3228 O O . HOH N 10 . ? -0.044 13.674 34.481 1.00 37.24 ? 2212 HOH A O 1 HETATM 3229 O O . HOH N 10 . ? 2.609 7.912 34.688 1.00 23.17 ? 2213 HOH A O 1 HETATM 3230 O O . HOH N 10 . ? 31.459 25.347 28.662 1.00 25.12 ? 2214 HOH A O 1 HETATM 3231 O O . HOH N 10 . ? 25.823 28.651 26.991 1.00 11.89 ? 2215 HOH A O 1 HETATM 3232 O O . HOH N 10 . ? 30.028 26.186 33.683 1.00 41.00 ? 2216 HOH A O 1 HETATM 3233 O O . HOH N 10 . ? 28.807 32.508 28.194 1.00 33.91 ? 2217 HOH A O 1 HETATM 3234 O O . HOH N 10 . ? 25.437 34.613 28.461 1.00 12.08 ? 2218 HOH A O 1 HETATM 3235 O O . HOH N 10 . ? 26.634 23.576 30.390 1.00 14.65 ? 2219 HOH A O 1 HETATM 3236 O O . HOH N 10 . ? 25.716 33.577 33.032 1.00 15.68 ? 2220 HOH A O 1 HETATM 3237 O O . HOH N 10 . ? 21.449 23.817 40.100 1.00 11.06 ? 2221 HOH A O 1 HETATM 3238 O O . HOH N 10 . ? 27.616 22.782 44.122 1.00 33.34 ? 2222 HOH A O 1 HETATM 3239 O O . HOH N 10 . ? 31.954 24.735 41.731 1.00 39.73 ? 2223 HOH A O 1 HETATM 3240 O O . HOH N 10 . ? 28.953 27.858 42.708 1.00 31.39 ? 2224 HOH A O 1 HETATM 3241 O O . HOH N 10 . ? 31.337 23.480 38.138 1.00 33.83 ? 2225 HOH A O 1 HETATM 3242 O O . HOH N 10 . ? 26.173 27.839 36.230 1.00 14.65 ? 2226 HOH A O 1 HETATM 3243 O O . HOH N 10 . ? 30.219 27.073 36.183 1.00 27.87 ? 2227 HOH A O 1 HETATM 3244 O O . HOH N 10 . ? 8.519 11.786 0.075 0.50 21.13 ? 2228 HOH A O 1 HETATM 3245 O O . HOH N 10 . ? 20.095 26.068 41.065 1.00 10.51 ? 2229 HOH A O 1 HETATM 3246 O O . HOH N 10 . ? 19.365 31.626 42.837 1.00 28.78 ? 2230 HOH A O 1 HETATM 3247 O O . HOH N 10 . ? 23.997 25.059 42.813 1.00 22.68 ? 2231 HOH A O 1 HETATM 3248 O O . HOH N 10 . ? 22.449 9.248 -3.378 0.50 20.47 ? 2232 HOH A O 1 HETATM 3249 O O . HOH N 10 . ? 25.432 6.901 -1.632 1.00 25.61 ? 2233 HOH A O 1 HETATM 3250 O O . HOH N 10 . ? 33.262 6.601 3.161 1.00 27.03 ? 2234 HOH A O 1 HETATM 3251 O O . HOH N 10 . ? 15.309 31.106 39.109 1.00 18.51 ? 2235 HOH A O 1 HETATM 3252 O O . HOH N 10 . ? 17.980 24.858 42.668 1.00 29.29 ? 2236 HOH A O 1 HETATM 3253 O O . HOH N 10 . ? 13.111 0.085 6.151 1.00 28.70 ? 2237 HOH A O 1 HETATM 3254 O O . HOH N 10 . ? 19.258 33.434 34.322 1.00 8.21 ? 2238 HOH A O 1 HETATM 3255 O O . HOH N 10 . ? 19.610 32.231 38.912 1.00 14.29 ? 2239 HOH A O 1 HETATM 3256 O O . HOH N 10 . ? 25.672 30.966 38.177 1.00 21.46 ? 2240 HOH A O 1 HETATM 3257 O O . HOH N 10 . ? 10.844 0.158 10.231 1.00 30.63 ? 2241 HOH A O 1 HETATM 3258 O O . HOH N 10 . ? 10.307 0.499 14.211 1.00 32.20 ? 2242 HOH A O 1 HETATM 3259 O O . HOH N 10 . ? 13.122 21.783 38.900 0.50 22.15 ? 2243 HOH A O 1 HETATM 3260 O O . HOH N 10 . ? 10.174 26.329 39.883 0.60 21.45 ? 2244 HOH A O 1 HETATM 3261 O O . HOH N 10 . ? 10.478 25.314 42.705 1.00 40.01 ? 2245 HOH A O 1 HETATM 3262 O O . HOH N 10 . ? 10.353 22.293 38.105 1.00 33.29 ? 2246 HOH A O 1 HETATM 3263 O O . HOH N 10 . ? 5.492 0.578 14.383 1.00 27.64 ? 2247 HOH A O 1 HETATM 3264 O O . HOH N 10 . ? 8.126 1.034 10.777 1.00 25.38 ? 2248 HOH A O 1 HETATM 3265 O O . HOH N 10 . ? 17.400 35.110 33.235 1.00 8.89 ? 2249 HOH A O 1 HETATM 3266 O O . HOH N 10 . ? 13.613 35.717 34.910 1.00 12.41 ? 2250 HOH A O 1 HETATM 3267 O O . HOH N 10 . ? -3.912 12.521 16.213 0.50 23.82 ? 2251 HOH A O 1 HETATM 3268 O O . HOH N 10 . ? -3.200 13.834 15.403 0.50 23.51 ? 2252 HOH A O 1 HETATM 3269 O O . HOH N 10 . ? 12.886 34.467 37.239 1.00 14.01 ? 2253 HOH A O 1 HETATM 3270 O O . HOH N 10 . ? 7.758 34.710 33.221 1.00 12.84 ? 2254 HOH A O 1 HETATM 3271 O O . HOH N 10 . ? 10.791 30.818 39.022 1.00 26.03 ? 2255 HOH A O 1 HETATM 3272 O O . HOH N 10 . ? 11.413 44.142 28.087 1.00 28.41 ? 2256 HOH A O 1 HETATM 3273 O O . HOH N 10 . ? 9.573 42.566 29.485 0.50 21.21 ? 2257 HOH A O 1 HETATM 3274 O O . HOH N 10 . ? -0.283 30.594 30.735 1.00 23.38 ? 2258 HOH A O 1 HETATM 3275 O O . HOH N 10 . ? 5.335 35.831 32.348 1.00 18.95 ? 2259 HOH A O 1 HETATM 3276 O O . HOH N 10 . ? 1.135 29.707 33.381 1.00 36.51 ? 2260 HOH A O 1 HETATM 3277 O O . HOH N 10 . ? 3.007 35.095 33.018 0.70 23.90 ? 2261 HOH A O 1 HETATM 3278 O O . HOH N 10 . ? 20.930 13.545 -4.000 1.00 34.68 ? 2262 HOH A O 1 HETATM 3279 O O . HOH N 10 . ? 37.933 12.535 4.517 1.00 20.15 ? 2263 HOH A O 1 HETATM 3280 O O . HOH N 10 . ? 6.192 38.793 34.588 1.00 30.34 ? 2264 HOH A O 1 HETATM 3281 O O . HOH N 10 . ? 11.156 36.810 34.604 1.00 32.20 ? 2265 HOH A O 1 HETATM 3282 O O . HOH N 10 . ? 12.128 40.674 34.082 1.00 21.39 ? 2266 HOH A O 1 HETATM 3283 O O . HOH N 10 . ? 8.671 36.245 35.116 1.00 38.47 ? 2267 HOH A O 1 HETATM 3284 O O . HOH N 10 . ? 5.727 40.341 29.501 1.00 13.04 ? 2268 HOH A O 1 HETATM 3285 O O . HOH N 10 . ? 9.519 40.234 36.190 0.50 24.14 ? 2269 HOH A O 1 HETATM 3286 O O . HOH N 10 . ? 39.404 8.800 0.654 0.40 16.88 ? 2270 HOH A O 1 HETATM 3287 O O . HOH N 10 . ? 5.816 45.037 23.211 1.00 16.85 ? 2271 HOH A O 1 HETATM 3288 O O . HOH N 10 . ? 6.256 44.467 27.433 1.00 32.65 ? 2272 HOH A O 1 HETATM 3289 O O . HOH N 10 . ? 4.418 42.503 28.486 1.00 18.51 ? 2273 HOH A O 1 HETATM 3290 O O . HOH N 10 . ? 10.115 42.974 25.766 0.50 23.92 ? 2274 HOH A O 1 HETATM 3291 O O . HOH N 10 . ? 9.518 42.420 27.503 0.50 24.40 ? 2275 HOH A O 1 HETATM 3292 O O . HOH N 10 . ? 0.504 35.957 16.834 1.00 12.39 ? 2276 HOH A O 1 HETATM 3293 O O . HOH N 10 . ? 14.150 21.500 -3.321 1.00 16.31 ? 2277 HOH A O 1 HETATM 3294 O O . HOH N 10 . ? 13.427 25.790 -4.007 1.00 23.19 ? 2278 HOH A O 1 HETATM 3295 O O . HOH N 10 . ? 10.263 25.783 -1.461 1.00 28.50 ? 2279 HOH A O 1 HETATM 3296 O O . HOH N 10 . ? 2.686 43.096 14.703 1.00 18.44 ? 2280 HOH A O 1 HETATM 3297 O O . HOH N 10 . ? 1.194 44.827 18.554 1.00 17.01 ? 2281 HOH A O 1 HETATM 3298 O O . HOH N 10 . ? -0.291 40.197 14.810 1.00 25.32 ? 2282 HOH A O 1 HETATM 3299 O O . HOH N 10 . ? 10.637 18.828 -0.979 0.40 19.63 ? 2283 HOH A O 1 HETATM 3300 O O . HOH N 10 . ? -0.021 17.533 4.779 0.50 19.41 ? 2284 HOH A O 1 HETATM 3301 O O . HOH N 10 . ? -2.497 30.035 10.429 1.00 17.56 ? 2285 HOH A O 1 HETATM 3302 O O . HOH N 10 . ? -1.032 5.355 9.855 1.00 37.65 ? 2286 HOH A O 1 HETATM 3303 O O . HOH N 10 . ? -2.238 8.991 7.521 1.00 33.95 ? 2287 HOH A O 1 HETATM 3304 O O . HOH N 10 . ? 13.662 18.946 24.027 1.00 8.11 ? 2288 HOH A O 1 HETATM 3305 O O . HOH N 10 . ? 20.484 21.132 25.316 1.00 7.22 ? 2289 HOH A O 1 HETATM 3306 O O . HOH N 10 . ? 43.967 25.913 13.900 1.00 25.40 ? 2290 HOH A O 1 HETATM 3307 O O . HOH N 10 . ? 41.014 16.429 22.641 0.50 15.13 ? 2291 HOH A O 1 HETATM 3308 O O . HOH N 10 . ? 41.312 19.597 25.739 1.00 26.34 ? 2292 HOH A O 1 HETATM 3309 O O . HOH N 10 . ? 42.797 26.157 28.238 1.00 32.57 ? 2293 HOH A O 1 HETATM 3310 O O . HOH N 10 . ? 43.051 29.213 22.248 0.50 27.45 ? 2294 HOH A O 1 HETATM 3311 O O . HOH N 10 . ? 37.898 25.212 30.218 1.00 44.87 ? 2295 HOH A O 1 HETATM 3312 O O . HOH N 10 . ? 44.443 15.094 16.756 1.00 37.63 ? 2296 HOH A O 1 HETATM 3313 O O . HOH N 10 . ? 39.740 18.692 3.645 1.00 28.45 ? 2297 HOH A O 1 HETATM 3314 O O . HOH N 10 . ? 43.614 6.691 7.627 1.00 36.06 ? 2298 HOH A O 1 HETATM 3315 O O . HOH N 10 . ? 40.106 16.193 2.293 1.00 22.69 ? 2299 HOH A O 1 HETATM 3316 O O . HOH N 10 . ? 25.760 15.007 24.475 1.00 12.48 ? 2300 HOH A O 1 HETATM 3317 O O . HOH N 10 . ? 41.005 29.735 12.782 1.00 29.12 ? 2301 HOH A O 1 HETATM 3318 O O . HOH N 10 . ? 37.392 30.922 9.403 1.00 18.67 ? 2302 HOH A O 1 HETATM 3319 O O . HOH N 10 . ? 41.744 29.502 6.141 1.00 23.88 ? 2303 HOH A O 1 HETATM 3320 O O . HOH N 10 . ? 16.689 7.404 30.464 1.00 19.80 ? 2304 HOH A O 1 HETATM 3321 O O . HOH N 10 . ? 16.908 4.044 26.928 1.00 32.21 ? 2305 HOH A O 1 HETATM 3322 O O . HOH N 10 . ? 40.292 31.853 14.440 1.00 33.00 ? 2306 HOH A O 1 HETATM 3323 O O . HOH N 10 . ? 24.191 3.145 24.144 1.00 37.19 ? 2307 HOH A O 1 HETATM 3324 O O . HOH N 10 . ? 25.560 7.083 22.207 1.00 26.57 ? 2308 HOH A O 1 HETATM 3325 O O . HOH N 10 . ? 39.487 23.420 1.315 0.50 17.34 ? 2309 HOH A O 1 HETATM 3326 O O . HOH N 10 . ? 21.194 5.157 27.827 1.00 15.90 ? 2310 HOH A O 1 HETATM 3327 O O . HOH N 10 . ? 25.376 5.493 34.766 1.00 10.17 ? 2311 HOH A O 1 HETATM 3328 O O . HOH N 10 . ? 29.911 2.587 29.949 0.50 18.02 ? 2312 HOH A O 1 HETATM 3329 O O . HOH N 10 . ? 26.946 5.976 25.316 1.00 30.10 ? 2313 HOH A O 1 HETATM 3330 O O . HOH N 10 . ? 23.821 3.489 28.031 1.00 30.23 ? 2314 HOH A O 1 HETATM 3331 O O . HOH N 10 . ? 28.054 5.947 34.685 1.00 11.02 ? 2315 HOH A O 1 HETATM 3332 O O . HOH N 10 . ? 26.367 27.220 -7.308 0.50 29.43 ? 2316 HOH A O 1 HETATM 3333 O O . HOH N 10 . ? 27.056 29.215 -6.632 0.50 31.19 ? 2317 HOH A O 1 HETATM 3334 O O . HOH N 10 . ? 30.406 27.387 -7.397 1.00 27.69 ? 2318 HOH A O 1 HETATM 3335 O O . HOH N 10 . ? 15.882 19.588 -3.102 1.00 21.81 ? 2319 HOH A O 1 HETATM 3336 O O . HOH N 10 . ? 30.784 12.058 32.479 1.00 13.10 ? 2320 HOH A O 1 HETATM 3337 O O . HOH N 10 . ? 31.933 18.569 32.471 1.00 26.52 ? 2321 HOH A O 1 HETATM 3338 O O . HOH N 10 . ? 28.154 21.085 30.195 1.00 13.08 ? 2322 HOH A O 1 HETATM 3339 O O . HOH N 10 . ? 15.541 26.263 -7.091 1.00 32.09 ? 2323 HOH A O 1 HETATM 3340 O O . HOH N 10 . ? 19.518 12.331 37.235 1.00 11.19 ? 2324 HOH A O 1 HETATM 3341 O O . HOH N 10 . ? 23.217 5.754 36.323 1.00 16.47 ? 2325 HOH A O 1 HETATM 3342 O O . HOH N 10 . ? 20.155 8.455 36.918 1.00 23.05 ? 2326 HOH A O 1 HETATM 3343 O O . HOH N 10 . ? 23.455 15.421 39.748 1.00 22.90 ? 2327 HOH A O 1 HETATM 3344 O O . HOH N 10 . ? 16.275 16.704 39.715 1.00 24.85 ? 2328 HOH A O 1 HETATM 3345 O O . HOH N 10 . ? 19.868 12.963 39.882 0.50 17.77 ? 2329 HOH A O 1 HETATM 3346 O O . HOH N 10 . ? 19.550 19.303 39.831 0.50 17.27 ? 2330 HOH A O 1 HETATM 3347 O O . HOH N 10 . ? 19.762 15.753 37.507 1.00 11.03 ? 2331 HOH A O 1 HETATM 3348 O O . HOH N 10 . ? 17.389 19.299 39.153 0.50 14.52 ? 2332 HOH A O 1 HETATM 3349 O O . HOH N 10 . ? 10.443 7.588 30.132 0.50 23.73 ? 2333 HOH A O 1 HETATM 3350 O O . HOH N 10 . ? 8.755 12.272 31.748 1.00 20.88 ? 2334 HOH A O 1 HETATM 3351 O O . HOH N 10 . ? 10.109 10.542 29.883 0.30 11.37 ? 2335 HOH A O 1 HETATM 3352 O O . HOH N 10 . ? 15.842 9.481 32.100 1.00 24.35 ? 2336 HOH A O 1 HETATM 3353 O O . HOH N 10 . ? 9.300 20.820 35.929 1.00 15.63 ? 2337 HOH A O 1 HETATM 3354 O O . HOH N 10 . ? 15.023 20.283 38.220 0.50 17.88 ? 2338 HOH A O 1 HETATM 3355 O O . HOH N 10 . ? 14.981 19.309 26.312 1.00 9.57 ? 2339 HOH A O 1 HETATM 3356 O O . HOH N 10 . ? 7.868 31.546 37.879 0.40 25.26 ? 2340 HOH A O 1 HETATM 3357 O O . HOH N 10 . ? 1.597 22.591 37.277 1.00 33.76 ? 2341 HOH A O 1 HETATM 3358 O O . HOH N 10 . ? 0.456 18.663 34.125 1.00 44.46 ? 2342 HOH A O 1 HETATM 3359 O O . HOH N 10 . ? 1.357 26.111 31.512 1.00 23.23 ? 2343 HOH A O 1 HETATM 3360 O O . HOH N 10 . ? 5.267 20.425 36.263 1.00 34.61 ? 2344 HOH A O 1 HETATM 3361 O O . HOH N 10 . ? 1.889 28.742 29.710 1.00 17.76 ? 2345 HOH A O 1 HETATM 3362 O O . HOH N 10 . ? 17.229 36.451 37.284 0.50 16.57 ? 2346 HOH A O 1 HETATM 3363 O O . HOH N 10 . ? 3.495 30.886 34.350 1.00 25.63 ? 2347 HOH A O 1 HETATM 3364 O O . HOH N 10 . ? 6.079 25.113 35.462 1.00 25.97 ? 2348 HOH A O 1 HETATM 3365 O O . HOH N 10 . ? 6.560 32.904 34.740 0.50 19.67 ? 2349 HOH A O 1 HETATM 3366 O O . HOH N 10 . ? 7.725 31.813 33.536 0.50 16.56 ? 2350 HOH A O 1 HETATM 3367 O O . HOH N 10 . ? 14.677 17.106 -3.294 1.00 39.00 ? 2351 HOH A O 1 HETATM 3368 O O . HOH N 10 . ? -0.932 27.361 23.928 1.00 12.43 ? 2352 HOH A O 1 HETATM 3369 O O . HOH N 10 . ? -2.079 23.706 26.659 1.00 10.20 ? 2353 HOH A O 1 HETATM 3370 O O . HOH N 10 . ? -0.840 30.106 27.983 1.00 24.03 ? 2354 HOH A O 1 HETATM 3371 O O . HOH N 10 . ? -1.433 26.851 29.031 1.00 30.02 ? 2355 HOH A O 1 HETATM 3372 O O . HOH N 10 . ? 0.979 24.083 29.833 1.00 16.77 ? 2356 HOH A O 1 HETATM 3373 O O . HOH N 10 . ? -0.174 27.204 21.172 1.00 9.82 ? 2357 HOH A O 1 HETATM 3374 O O . HOH N 10 . ? -3.205 29.070 19.464 1.00 11.55 ? 2358 HOH A O 1 HETATM 3375 O O . HOH N 10 . ? -0.072 34.394 23.290 1.00 9.18 ? 2359 HOH A O 1 HETATM 3376 O O . HOH N 10 . ? 6.768 36.173 20.517 1.00 7.05 ? 2360 HOH A O 1 HETATM 3377 O O . HOH N 10 . ? 20.452 16.910 18.802 1.00 10.67 ? 2361 HOH A O 1 HETATM 3378 O O . HOH N 10 . ? 15.251 16.713 23.405 1.00 6.66 ? 2362 HOH A O 1 HETATM 3379 O O . HOH N 10 . ? 17.732 15.994 22.461 1.00 6.60 ? 2363 HOH A O 1 HETATM 3380 O O . HOH N 10 . ? 17.889 17.014 15.907 1.00 7.41 ? 2364 HOH A O 1 HETATM 3381 O O . HOH N 10 . ? 13.050 -1.465 16.278 0.50 19.21 ? 2365 HOH A O 1 HETATM 3382 O O . HOH N 10 . ? 13.454 -0.021 19.504 1.00 16.35 ? 2366 HOH A O 1 HETATM 3383 O O . HOH N 10 . ? 19.944 -0.885 15.998 1.00 15.09 ? 2367 HOH A O 1 HETATM 3384 O O . HOH N 10 . ? 14.640 -1.510 21.850 1.00 21.12 ? 2368 HOH A O 1 HETATM 3385 O O . HOH N 10 . ? 18.635 0.555 23.305 1.00 41.46 ? 2369 HOH A O 1 HETATM 3386 O O . HOH N 10 . ? 21.917 1.233 20.574 1.00 21.48 ? 2370 HOH A O 1 HETATM 3387 O O . HOH N 10 . ? 8.030 -3.195 24.559 1.00 33.76 ? 2371 HOH A O 1 HETATM 3388 O O . HOH N 10 . ? 11.491 -2.106 19.589 1.00 32.33 ? 2372 HOH A O 1 HETATM 3389 O O . HOH N 10 . ? 6.079 -1.189 20.246 1.00 32.00 ? 2373 HOH A O 1 HETATM 3390 O O . HOH N 10 . ? 12.893 5.283 27.324 1.00 22.34 ? 2374 HOH A O 1 HETATM 3391 O O . HOH N 10 . ? 6.091 2.033 26.005 1.00 13.73 ? 2375 HOH A O 1 HETATM 3392 O O . HOH N 10 . ? 5.788 6.563 27.302 1.00 13.23 ? 2376 HOH A O 1 HETATM 3393 O O . HOH N 10 . ? 8.008 -0.341 28.322 1.00 21.58 ? 2377 HOH A O 1 HETATM 3394 O O . HOH N 10 . ? 11.114 6.395 29.106 0.50 24.21 ? 2378 HOH A O 1 HETATM 3395 O O . HOH N 10 . ? 9.243 5.226 30.647 1.00 36.92 ? 2379 HOH A O 1 HETATM 3396 O O . HOH N 10 . ? 2.147 11.014 25.166 1.00 8.34 ? 2380 HOH A O 1 HETATM 3397 O O . HOH N 10 . ? -2.248 15.386 21.720 1.00 18.84 ? 2381 HOH A O 1 HETATM 3398 O O . HOH N 10 . ? 0.162 19.300 21.825 1.00 8.75 ? 2382 HOH A O 1 HETATM 3399 O O . HOH N 10 . ? 3.338 7.755 26.958 1.00 13.96 ? 2383 HOH A O 1 HETATM 3400 O O . HOH N 10 . ? 2.680 9.663 32.675 1.00 20.18 ? 2384 HOH A O 1 HETATM 3401 O O . HOH N 10 . ? 0.289 15.948 33.384 1.00 27.59 ? 2385 HOH A O 1 HETATM 3402 O O . HOH N 10 . ? 4.283 16.089 35.574 1.00 38.36 ? 2386 HOH A O 1 HETATM 3403 O O . HOH N 10 . ? 0.154 21.594 30.370 1.00 17.54 ? 2387 HOH A O 1 HETATM 3404 O O . HOH N 10 . ? -2.210 21.701 28.719 1.00 20.40 ? 2388 HOH A O 1 HETATM 3405 O O . HOH N 10 . ? -3.312 18.666 30.550 1.00 16.75 ? 2389 HOH A O 1 HETATM 3406 O O . HOH N 10 . ? -3.143 18.825 23.844 1.00 22.81 ? 2390 HOH A O 1 HETATM 3407 O O . HOH N 10 . ? -2.026 26.449 19.087 0.70 13.34 ? 2391 HOH A O 1 HETATM 3408 O O . HOH N 10 . ? -5.326 29.449 21.356 1.00 16.29 ? 2392 HOH A O 1 HETATM 3409 O O . HOH N 10 . ? -8.701 26.559 18.623 0.50 20.16 ? 2393 HOH A O 1 HETATM 3410 O O . HOH N 10 . ? -2.941 19.810 12.850 1.00 26.99 ? 2394 HOH A O 1 HETATM 3411 O O . HOH N 10 . ? 20.407 16.118 14.926 1.00 8.46 ? 2395 HOH A O 1 HETATM 3412 O O . HOH N 10 . ? 21.875 18.889 17.432 1.00 11.28 ? 2396 HOH A O 1 HETATM 3413 O O . HOH N 10 . ? 27.174 19.810 13.737 1.00 8.96 ? 2397 HOH A O 1 HETATM 3414 O O . HOH N 10 . ? 24.702 13.892 9.925 1.00 8.28 ? 2398 HOH A O 1 HETATM 3415 O O . HOH N 10 . ? 9.510 14.050 -0.384 0.50 8.50 ? 2399 HOH A O 1 HETATM 3416 O O . HOH N 10 . ? 14.054 13.567 -2.166 0.30 16.03 ? 2400 HOH A O 1 HETATM 3417 O O . HOH N 10 . ? 10.384 10.222 -1.273 1.00 30.10 ? 2401 HOH A O 1 HETATM 3418 O O . HOH N 10 . ? 16.454 12.492 -3.551 1.00 28.79 ? 2402 HOH A O 1 HETATM 3419 O O . HOH N 10 . ? 13.719 7.690 -3.096 1.00 40.62 ? 2403 HOH A O 1 HETATM 3420 O O . HOH N 10 . ? 16.232 8.025 -7.821 1.00 38.94 ? 2404 HOH A O 1 HETATM 3421 O O . HOH N 10 . ? 18.310 9.985 -4.453 1.00 22.36 ? 2405 HOH A O 1 HETATM 3422 O O . HOH N 10 . ? 14.236 5.522 -4.972 1.00 25.96 ? 2406 HOH A O 1 HETATM 3423 O O . HOH N 10 . ? 24.955 4.239 -1.732 1.00 49.50 ? 2407 HOH A O 1 HETATM 3424 O O . HOH N 10 . ? 20.969 8.023 -3.613 0.50 20.71 ? 2408 HOH A O 1 HETATM 3425 O O . HOH N 10 . ? 23.229 8.213 -1.102 1.00 19.22 ? 2409 HOH A O 1 HETATM 3426 O O . HOH N 10 . ? 25.802 1.983 1.415 1.00 38.96 ? 2410 HOH A O 1 HETATM 3427 O O . HOH N 10 . ? 29.001 0.985 3.913 1.00 27.05 ? 2411 HOH A O 1 HETATM 3428 O O . HOH N 10 . ? 31.497 4.701 4.866 0.50 20.72 ? 2412 HOH A O 1 HETATM 3429 O O . HOH N 10 . ? 26.683 3.319 10.309 1.00 23.49 ? 2413 HOH A O 1 HETATM 3430 O O . HOH N 10 . ? 23.623 11.569 4.607 1.00 6.94 ? 2414 HOH A O 1 HETATM 3431 O O . HOH N 10 . ? 29.221 5.558 10.313 1.00 9.53 ? 2415 HOH A O 1 HETATM 3432 O O . HOH N 10 . ? 22.925 -0.023 4.089 1.00 32.32 ? 2416 HOH A O 1 HETATM 3433 O O . HOH N 10 . ? 22.053 1.979 5.632 1.00 10.33 ? 2417 HOH A O 1 HETATM 3434 O O . HOH N 10 . ? 15.654 0.648 4.528 1.00 18.86 ? 2418 HOH A O 1 HETATM 3435 O O . HOH N 10 . ? 12.639 0.885 12.277 1.00 17.76 ? 2419 HOH A O 1 HETATM 3436 O O . HOH N 10 . ? 12.178 1.639 8.194 1.00 19.30 ? 2420 HOH A O 1 HETATM 3437 O O . HOH N 10 . ? 16.993 1.597 -0.234 1.00 40.27 ? 2421 HOH A O 1 HETATM 3438 O O . HOH N 10 . ? 21.049 10.579 5.421 1.00 8.23 ? 2422 HOH A O 1 HETATM 3439 O O . HOH N 10 . ? 13.640 7.722 1.403 1.00 11.84 ? 2423 HOH A O 1 HETATM 3440 O O . HOH N 10 . ? 8.011 6.618 -0.391 0.50 14.21 ? 2424 HOH A O 1 HETATM 3441 O O . HOH N 10 . ? 6.610 6.396 0.536 0.50 11.27 ? 2425 HOH A O 1 HETATM 3442 O O . HOH N 10 . ? 11.318 6.293 1.649 1.00 19.96 ? 2426 HOH A O 1 HETATM 3443 O O . HOH N 10 . ? 9.414 7.754 -1.032 0.50 15.93 ? 2427 HOH A O 1 HETATM 3444 O O . HOH N 10 . ? 10.482 3.755 7.773 1.00 11.13 ? 2428 HOH A O 1 HETATM 3445 O O . HOH N 10 . ? 10.474 3.909 2.536 0.50 21.07 ? 2429 HOH A O 1 HETATM 3446 O O . HOH N 10 . ? 13.422 1.641 1.688 1.00 28.65 ? 2430 HOH A O 1 HETATM 3447 O O . HOH N 10 . ? 5.303 7.611 2.399 1.00 16.53 ? 2431 HOH A O 1 HETATM 3448 O O . HOH N 10 . ? 10.109 4.767 5.177 1.00 14.04 ? 2432 HOH A O 1 HETATM 3449 O O . HOH N 10 . ? 7.935 1.574 13.487 1.00 15.78 ? 2433 HOH A O 1 HETATM 3450 O O . HOH N 10 . ? 0.429 3.878 16.125 1.00 18.22 ? 2434 HOH A O 1 HETATM 3451 O O . HOH N 10 . ? 3.446 1.397 16.743 1.00 30.24 ? 2435 HOH A O 1 HETATM 3452 O O . HOH N 10 . ? -2.932 10.921 14.049 1.00 37.97 ? 2436 HOH A O 1 HETATM 3453 O O . HOH N 10 . ? -4.755 8.433 16.941 1.00 19.36 ? 2437 HOH A O 1 HETATM 3454 O O . HOH N 10 . ? 1.190 6.983 13.038 1.00 27.21 ? 2438 HOH A O 1 HETATM 3455 O O . HOH N 10 . ? 5.604 -1.347 24.631 1.00 18.23 ? 2439 HOH A O 1 HETATM 3456 O O . HOH N 10 . ? 4.020 0.751 19.227 1.00 19.58 ? 2440 HOH A O 1 HETATM 3457 O O . HOH N 10 . ? -2.598 12.766 22.032 1.00 12.90 ? 2441 HOH A O 1 HETATM 3458 O O . HOH N 10 . ? -0.826 14.963 14.742 1.00 20.37 ? 2442 HOH A O 1 HETATM 3459 O O . HOH N 10 . ? -0.523 13.805 10.865 1.00 24.94 ? 2443 HOH A O 1 HETATM 3460 O O . HOH N 10 . ? 18.247 19.306 1.345 1.00 8.73 ? 2444 HOH A O 1 HETATM 3461 O O . HOH N 10 . ? 23.228 21.262 9.904 1.00 6.46 ? 2445 HOH A O 1 HETATM 3462 O O . HOH N 10 . ? 20.944 19.884 7.387 1.00 6.46 ? 2446 HOH A O 1 HETATM 3463 O O . HOH N 10 . ? 25.038 18.186 2.246 1.00 6.45 ? 2447 HOH A O 1 HETATM 3464 O O . HOH N 10 . ? 30.248 12.732 -2.492 1.00 13.13 ? 2448 HOH A O 1 HETATM 3465 O O . HOH N 10 . ? 22.672 15.627 -3.570 1.00 18.70 ? 2449 HOH A O 1 HETATM 3466 O O . HOH N 10 . ? 27.716 13.431 -3.199 0.50 15.59 ? 2450 HOH A O 1 HETATM 3467 O O . HOH N 10 . ? 30.151 9.595 1.104 1.00 13.74 ? 2451 HOH A O 1 HETATM 3468 O O . HOH N 10 . ? 35.568 12.643 2.950 1.00 13.49 ? 2452 HOH A O 1 HETATM 3469 O O . HOH N 10 . ? 32.233 8.976 2.864 1.00 14.76 ? 2453 HOH A O 1 HETATM 3470 O O . HOH N 10 . ? 24.549 12.751 6.835 1.00 7.99 ? 2454 HOH A O 1 HETATM 3471 O O . HOH N 10 . ? 31.329 4.558 7.297 0.50 14.13 ? 2455 HOH A O 1 HETATM 3472 O O . HOH N 10 . ? 40.408 9.845 2.319 0.40 21.92 ? 2456 HOH A O 1 HETATM 3473 O O . HOH N 10 . ? 39.841 6.006 4.836 1.00 45.76 ? 2457 HOH A O 1 HETATM 3474 O O . HOH N 10 . ? 30.844 3.590 8.000 0.50 16.81 ? 2458 HOH A O 1 HETATM 3475 O O . HOH N 10 . ? 34.167 2.359 9.019 1.00 11.96 ? 2459 HOH A O 1 HETATM 3476 O O . HOH N 10 . ? 36.430 5.989 10.942 1.00 10.48 ? 2460 HOH A O 1 HETATM 3477 O O . HOH N 10 . ? 35.509 5.385 7.144 1.00 30.47 ? 2461 HOH A O 1 HETATM 3478 O O . HOH N 10 . ? 29.803 7.198 13.720 1.00 12.03 ? 2462 HOH A O 1 HETATM 3479 O O . HOH N 10 . ? 29.200 11.325 17.369 1.00 16.24 ? 2463 HOH A O 1 HETATM 3480 O O . HOH N 10 . ? 34.030 9.680 15.929 1.00 21.37 ? 2464 HOH A O 1 HETATM 3481 O O . HOH N 10 . ? 29.511 13.184 19.287 1.00 15.00 ? 2465 HOH A O 1 HETATM 3482 O O . HOH N 10 . ? 33.418 15.878 10.555 1.00 8.43 ? 2466 HOH A O 1 HETATM 3483 O O . HOH N 10 . ? 30.670 24.398 9.894 1.00 12.94 ? 2467 HOH A O 1 HETATM 3484 O O . HOH N 10 . ? 34.473 19.310 0.453 1.00 15.86 ? 2468 HOH A O 1 HETATM 3485 O O . HOH N 10 . ? 11.929 23.805 -0.409 1.00 14.52 ? 2469 HOH A O 1 HETATM 3486 O O . HOH N 10 . ? 16.728 30.791 -2.126 0.50 16.55 ? 2470 HOH A O 1 HETATM 3487 O O . HOH N 10 . ? 14.060 23.976 -2.156 1.00 10.79 ? 2471 HOH A O 1 HETATM 3488 O O . HOH N 10 . ? 19.842 25.549 -1.187 0.45 8.47 ? 2472 HOH A O 1 HETATM 3489 O O . HOH N 10 . ? 17.926 30.293 -4.940 1.00 23.52 ? 2473 HOH A O 1 HETATM 3490 O O . HOH N 10 . ? 14.307 30.037 -1.777 1.00 24.24 ? 2474 HOH A O 1 HETATM 3491 O O . HOH N 10 . ? 9.977 28.140 0.273 1.00 24.85 ? 2475 HOH A O 1 HETATM 3492 O O . HOH N 10 . ? 7.286 27.951 0.838 1.00 25.77 ? 2476 HOH A O 1 HETATM 3493 O O . HOH N 10 . ? 3.206 20.543 5.938 1.00 16.11 ? 2477 HOH A O 1 HETATM 3494 O O . HOH N 10 . ? 6.110 27.909 3.615 1.00 12.96 ? 2478 HOH A O 1 HETATM 3495 O O . HOH N 10 . ? 5.538 19.477 -1.706 1.00 14.80 ? 2479 HOH A O 1 HETATM 3496 O O . HOH N 10 . ? 1.463 21.919 1.309 1.00 19.08 ? 2480 HOH A O 1 HETATM 3497 O O . HOH N 10 . ? 7.703 22.800 -1.622 1.00 26.53 ? 2481 HOH A O 1 HETATM 3498 O O . HOH N 10 . ? 2.405 28.206 -0.123 1.00 27.91 ? 2482 HOH A O 1 HETATM 3499 O O . HOH N 10 . ? 6.440 26.095 -1.660 1.00 39.77 ? 2483 HOH A O 1 HETATM 3500 O O . HOH N 10 . ? 7.354 15.773 -0.775 1.00 12.89 ? 2484 HOH A O 1 HETATM 3501 O O . HOH N 10 . ? 9.204 19.359 -0.592 0.60 21.29 ? 2485 HOH A O 1 HETATM 3502 O O . HOH N 10 . ? 6.062 13.146 0.384 0.40 13.97 ? 2486 HOH A O 1 HETATM 3503 O O . HOH N 10 . ? 5.551 13.857 -0.700 0.60 14.95 ? 2487 HOH A O 1 HETATM 3504 O O . HOH N 10 . ? 2.549 19.870 2.274 1.00 19.27 ? 2488 HOH A O 1 HETATM 3505 O O . HOH N 10 . ? 2.052 18.132 6.359 1.00 21.48 ? 2489 HOH A O 1 HETATM 3506 O O . HOH N 10 . ? -2.309 16.118 4.718 0.50 24.32 ? 2490 HOH A O 1 HETATM 3507 O O . HOH N 10 . ? -1.076 8.238 10.045 1.00 21.46 ? 2491 HOH A O 1 HETATM 3508 O O . HOH N 10 . ? 1.351 19.621 8.587 1.00 15.03 ? 2492 HOH A O 1 HETATM 3509 O O . HOH N 10 . ? 21.500 23.159 8.926 1.00 6.65 ? 2493 HOH A O 1 HETATM 3510 O O . HOH N 10 . ? 21.853 29.148 7.022 1.00 29.57 ? 2494 HOH A O 1 HETATM 3511 O O . HOH N 10 . ? 22.231 26.436 6.447 1.00 8.89 ? 2495 HOH A O 1 HETATM 3512 O O . HOH N 10 . ? 28.217 25.644 9.374 1.00 9.37 ? 2496 HOH A O 1 HETATM 3513 O O . HOH N 10 . ? 25.317 28.349 15.037 0.50 10.71 ? 2497 HOH A O 1 HETATM 3514 O O . HOH N 10 . ? 23.812 30.894 15.994 0.50 19.55 ? 2498 HOH A O 1 HETATM 3515 O O . HOH N 10 . ? 24.312 28.228 16.173 0.50 19.47 ? 2499 HOH A O 1 HETATM 3516 O O . HOH N 10 . ? 22.205 32.980 13.198 1.00 10.88 ? 2500 HOH A O 1 HETATM 3517 O O . HOH N 10 . ? 32.145 22.474 19.758 1.00 14.40 ? 2501 HOH A O 1 HETATM 3518 O O . HOH N 10 . ? 40.084 28.651 18.111 0.50 18.89 ? 2502 HOH A O 1 HETATM 3519 O O . HOH N 10 . ? 40.469 28.599 16.856 0.50 18.87 ? 2503 HOH A O 1 HETATM 3520 O O . HOH N 10 . ? 36.357 21.892 18.851 1.00 9.68 ? 2504 HOH A O 1 HETATM 3521 O O . HOH N 10 . ? 43.562 23.571 12.530 1.00 18.36 ? 2505 HOH A O 1 HETATM 3522 O O . HOH N 10 . ? 42.826 19.709 14.088 1.00 18.39 ? 2506 HOH A O 1 HETATM 3523 O O . HOH N 10 . ? 44.896 21.387 13.377 1.00 25.47 ? 2507 HOH A O 1 HETATM 3524 O O . HOH N 10 . ? 42.533 29.111 18.545 0.50 17.09 ? 2508 HOH A O 1 HETATM 3525 O O . HOH N 10 . ? 47.152 24.573 17.403 0.50 20.80 ? 2509 HOH A O 1 HETATM 3526 O O . HOH N 10 . ? 46.710 28.239 18.919 1.00 27.17 ? 2510 HOH A O 1 HETATM 3527 O O . HOH N 10 . ? 42.737 21.427 24.278 1.00 19.16 ? 2511 HOH A O 1 HETATM 3528 O O . HOH N 10 . ? 45.628 22.327 16.150 1.00 24.04 ? 2512 HOH A O 1 HETATM 3529 O O . HOH N 10 . ? 43.867 18.172 22.301 1.00 28.29 ? 2513 HOH A O 1 HETATM 3530 O O . HOH N 10 . ? 47.539 19.788 21.236 1.00 39.17 ? 2514 HOH A O 1 HETATM 3531 O O . HOH N 10 . ? 48.211 27.417 21.744 1.00 29.72 ? 2515 HOH A O 1 HETATM 3532 O O . HOH N 10 . ? 43.531 24.092 26.650 1.00 36.47 ? 2516 HOH A O 1 HETATM 3533 O O . HOH N 10 . ? 41.385 28.489 24.520 1.00 27.05 ? 2517 HOH A O 1 HETATM 3534 O O . HOH N 10 . ? 40.192 22.109 28.503 1.00 40.10 ? 2518 HOH A O 1 HETATM 3535 O O . HOH N 10 . ? 34.603 23.399 20.444 1.00 13.91 ? 2519 HOH A O 1 HETATM 3536 O O . HOH N 10 . ? 33.068 22.483 23.026 1.00 24.39 ? 2520 HOH A O 1 HETATM 3537 O O . HOH N 10 . ? 35.486 27.058 29.700 1.00 32.82 ? 2521 HOH A O 1 HETATM 3538 O O . HOH N 10 . ? 38.555 20.251 25.522 1.00 16.37 ? 2522 HOH A O 1 HETATM 3539 O O . HOH N 10 . ? 42.388 15.471 18.310 1.00 16.97 ? 2523 HOH A O 1 HETATM 3540 O O . HOH N 10 . ? 38.111 16.795 22.801 1.00 11.99 ? 2524 HOH A O 1 HETATM 3541 O O . HOH N 10 . ? 31.751 15.438 21.403 1.00 10.30 ? 2525 HOH A O 1 HETATM 3542 O O . HOH N 10 . ? 40.694 14.380 16.328 1.00 12.63 ? 2526 HOH A O 1 HETATM 3543 O O . HOH N 10 . ? 34.973 8.735 18.493 1.00 14.02 ? 2527 HOH A O 1 HETATM 3544 O O . HOH N 10 . ? 32.805 11.779 22.173 1.00 17.93 ? 2528 HOH A O 1 HETATM 3545 O O . HOH N 10 . ? 31.500 10.093 18.314 1.00 17.49 ? 2529 HOH A O 1 HETATM 3546 O O . HOH N 10 . ? 33.260 15.372 13.245 1.00 7.62 ? 2530 HOH A O 1 HETATM 3547 O O . HOH N 10 . ? 43.545 17.087 14.311 1.00 23.89 ? 2531 HOH A O 1 HETATM 3548 O O . HOH N 10 . ? 42.401 13.340 13.536 1.00 28.57 ? 2532 HOH A O 1 HETATM 3549 O O . HOH N 10 . ? 40.441 11.439 11.289 1.00 12.94 ? 2533 HOH A O 1 HETATM 3550 O O . HOH N 10 . ? 37.194 8.442 9.738 1.00 14.01 ? 2534 HOH A O 1 HETATM 3551 O O . HOH N 10 . ? 39.792 14.363 4.249 1.00 20.95 ? 2535 HOH A O 1 HETATM 3552 O O . HOH N 10 . ? 42.275 8.094 5.930 1.00 23.06 ? 2536 HOH A O 1 HETATM 3553 O O . HOH N 10 . ? 39.223 17.984 6.048 1.00 25.32 ? 2537 HOH A O 1 HETATM 3554 O O . HOH N 10 . ? 36.860 21.526 12.026 1.00 8.26 ? 2538 HOH A O 1 HETATM 3555 O O . HOH N 10 . ? 39.395 25.894 5.388 1.00 16.91 ? 2539 HOH A O 1 HETATM 3556 O O . HOH N 10 . ? 40.557 20.917 5.786 1.00 17.64 ? 2540 HOH A O 1 HETATM 3557 O O . HOH N 10 . ? 39.615 28.103 7.039 1.00 14.89 ? 2541 HOH A O 1 HETATM 3558 O O . HOH N 10 . ? 39.531 29.696 10.382 1.00 23.22 ? 2542 HOH A O 1 HETATM 3559 O O . HOH N 10 . ? 44.455 23.732 9.827 1.00 28.62 ? 2543 HOH A O 1 HETATM 3560 O O . HOH N 10 . ? 41.765 27.419 14.302 1.00 20.18 ? 2544 HOH A O 1 HETATM 3561 O O . HOH N 10 . ? 35.256 25.830 19.689 1.00 12.17 ? 2545 HOH A O 1 HETATM 3562 O O . HOH N 10 . ? 38.889 31.034 16.819 1.00 19.15 ? 2546 HOH A O 1 HETATM 3563 O O . HOH N 10 . ? 38.271 27.304 23.707 1.00 22.90 ? 2547 HOH A O 1 HETATM 3564 O O . HOH N 10 . ? 27.250 33.097 15.077 1.00 18.07 ? 2548 HOH A O 1 HETATM 3565 O O . HOH N 10 . ? 38.633 33.254 18.524 1.00 35.36 ? 2549 HOH A O 1 HETATM 3566 O O . HOH N 10 . ? 35.839 33.724 12.710 1.00 25.57 ? 2550 HOH A O 1 HETATM 3567 O O . HOH N 10 . ? 35.945 33.143 8.453 1.00 16.92 ? 2551 HOH A O 1 HETATM 3568 O O . HOH N 10 . ? 37.613 30.183 6.782 1.00 12.35 ? 2552 HOH A O 1 HETATM 3569 O O . HOH N 10 . ? 35.882 26.117 0.692 1.00 17.02 ? 2553 HOH A O 1 HETATM 3570 O O . HOH N 10 . ? 37.326 32.609 2.806 1.00 18.73 ? 2554 HOH A O 1 HETATM 3571 O O . HOH N 10 . ? 40.066 26.310 -0.883 0.50 18.66 ? 2555 HOH A O 1 HETATM 3572 O O . HOH N 10 . ? 39.585 25.863 2.700 1.00 23.70 ? 2556 HOH A O 1 HETATM 3573 O O . HOH N 10 . ? 35.515 21.551 1.387 1.00 12.40 ? 2557 HOH A O 1 HETATM 3574 O O . HOH N 10 . ? 25.080 27.692 -5.238 1.00 15.81 ? 2558 HOH A O 1 HETATM 3575 O O . HOH N 10 . ? 36.713 27.378 -8.494 0.50 14.24 ? 2559 HOH A O 1 HETATM 3576 O O . HOH N 10 . ? 29.008 25.046 -7.731 1.00 21.02 ? 2560 HOH A O 1 HETATM 3577 O O . HOH N 10 . ? 31.637 18.426 -3.507 1.00 9.54 ? 2561 HOH A O 1 HETATM 3578 O O . HOH N 10 . ? 27.428 19.416 -5.121 0.50 15.09 ? 2562 HOH A O 1 HETATM 3579 O O . HOH N 10 . ? 33.085 19.968 -1.523 1.00 14.36 ? 2563 HOH A O 1 HETATM 3580 O O . HOH N 10 . ? 25.108 19.271 -4.295 1.00 23.38 ? 2564 HOH A O 1 HETATM 3581 O O . HOH N 10 . ? 25.609 23.768 -6.371 1.00 16.61 ? 2565 HOH A O 1 HETATM 3582 O O . HOH N 10 . ? 23.218 21.502 -7.252 1.00 33.97 ? 2566 HOH A O 1 HETATM 3583 O O . HOH N 10 . ? 16.966 19.795 -5.604 1.00 31.83 ? 2567 HOH A O 1 HETATM 3584 O O . HOH N 10 . ? 18.358 16.656 -5.698 1.00 30.98 ? 2568 HOH A O 1 HETATM 3585 O O . HOH N 10 . ? 18.088 27.037 -7.857 1.00 19.20 ? 2569 HOH A O 1 HETATM 3586 O O . HOH N 10 . ? 22.851 34.009 -7.363 1.00 22.57 ? 2570 HOH A O 1 HETATM 3587 O O . HOH N 10 . ? 19.475 32.306 -5.826 1.00 23.39 ? 2571 HOH A O 1 HETATM 3588 O O . HOH N 10 . ? 25.203 31.279 -8.874 1.00 28.58 ? 2572 HOH A O 1 HETATM 3589 O O . HOH N 10 . ? 26.421 34.865 35.474 1.00 13.01 ? 2573 HOH A O 1 HETATM 3590 O O . HOH N 10 . ? 24.820 38.057 34.231 1.00 14.97 ? 2574 HOH A O 1 HETATM 3591 O O . HOH N 10 . ? 19.344 40.050 36.979 1.00 16.34 ? 2575 HOH A O 1 HETATM 3592 O O . HOH N 10 . ? 16.061 37.033 34.701 1.00 17.83 ? 2576 HOH A O 1 HETATM 3593 O O . HOH N 10 . ? 16.368 39.722 33.909 1.00 18.79 ? 2577 HOH A O 1 HETATM 3594 O O . HOH N 10 . ? 12.153 33.848 2.493 1.00 12.07 ? 2578 HOH A O 1 HETATM 3595 O O . HOH N 10 . ? 12.371 29.700 2.435 1.00 12.91 ? 2579 HOH A O 1 HETATM 3596 O O . HOH N 10 . ? 6.641 32.475 2.164 1.00 28.47 ? 2580 HOH A O 1 HETATM 3597 O O . HOH N 10 . ? 12.079 35.999 4.544 1.00 11.94 ? 2581 HOH A O 1 HETATM 3598 O O . HOH N 10 . ? 4.512 4.965 9.217 1.00 21.54 ? 2582 HOH A O 1 HETATM 3599 O O . HOH N 10 . ? -1.929 21.316 19.631 1.00 19.02 ? 2583 HOH A O 1 HETATM 3600 O O . HOH N 10 . ? 18.195 19.291 -1.487 1.00 11.56 ? 2584 HOH A O 1 HETATM 3601 O O . HOH N 10 . ? 13.747 15.359 -1.454 0.70 20.12 ? 2585 HOH A O 1 HETATM 3602 O O . HOH N 10 . ? 28.134 22.817 23.581 1.00 11.72 ? 2586 HOH A O 1 HETATM 3603 O O . HOH N 10 . ? 27.405 21.195 15.989 1.00 18.03 ? 2587 HOH A O 1 HETATM 3604 O O . HOH N 10 . ? 25.499 23.649 17.739 0.30 21.01 ? 2588 HOH A O 1 HETATM 3605 O O . HOH N 10 . ? 27.275 24.443 16.032 1.00 19.90 ? 2589 HOH A O 1 HETATM 3606 O O . HOH N 10 . ? 28.631 27.005 20.978 1.00 26.42 ? 2590 HOH A O 1 HETATM 3607 O O . HOH N 10 . ? 21.672 15.099 17.122 1.00 9.62 ? 2591 HOH A O 1 HETATM 3608 O O . HOH N 10 . ? 24.342 14.738 16.572 0.30 20.21 ? 2592 HOH A O 1 HETATM 3609 O O . HOH N 10 . ? 27.644 13.827 22.530 1.00 21.83 ? 2593 HOH A O 1 HETATM 3610 O O . HOH N 10 . ? 26.766 13.183 13.479 1.00 12.26 ? 2594 HOH A O 1 HETATM 3611 O O . HOH N 10 . ? 27.535 9.586 20.143 0.30 6.36 ? 2595 HOH A O 1 HETATM 3612 O O . HOH N 10 . ? 26.298 11.400 22.067 0.30 13.19 ? 2596 HOH A O 1 HETATM 3613 O O . HOH N 10 . ? 25.644 8.950 14.520 1.00 14.30 ? 2597 HOH A O 1 HETATM 3614 O O . HOH N 10 . ? 23.406 5.397 17.826 0.30 9.27 ? 2598 HOH A O 1 HETATM 3615 O O . HOH N 10 . ? 23.067 3.867 19.668 0.30 17.44 ? 2599 HOH A O 1 HETATM 3616 O O . HOH N 10 . ? 27.473 4.492 12.350 1.00 20.71 ? 2600 HOH A O 1 HETATM 3617 O O . HOH N 10 . ? 25.165 4.469 21.684 1.00 32.41 ? 2601 HOH A O 1 HETATM 3618 O O . HOH N 10 . ? 22.120 -1.072 17.093 0.30 21.91 ? 2602 HOH A O 1 HETATM 3619 O O . HOH N 10 . ? 29.257 2.849 16.460 1.00 23.98 ? 2603 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 . ALA A 1 ? 0.1359 0.1260 0.1597 0.0102 -0.0093 -0.0067 87 ALA A N 2 C CA . ALA A 1 ? 0.1540 0.1184 0.1445 0.0141 -0.0134 -0.0097 87 ALA A CA 3 C C . ALA A 1 ? 0.1274 0.1019 0.1242 0.0210 0.0028 -0.0093 87 ALA A C 4 O O . ALA A 1 ? 0.1198 0.1264 0.1486 0.0126 -0.0198 -0.0162 87 ALA A O 5 C CB . ALA A 1 ? 0.1764 0.1592 0.1547 0.0142 -0.0168 0.0027 87 ALA A CB 6 N N . PRO A 2 ? 0.1300 0.1372 0.1346 0.0160 -0.0069 -0.0112 88 PRO A N 7 C CA . PRO A 2 ? 0.1429 0.1406 0.1393 -0.0050 -0.0097 -0.0065 88 PRO A CA 8 C C . PRO A 2 ? 0.1339 0.1244 0.1263 0.0135 -0.0044 -0.0043 88 PRO A C 9 O O . PRO A 2 ? 0.1645 0.1327 0.1463 0.0101 -0.0095 -0.0009 88 PRO A O 10 C CB . PRO A 2 ? 0.1796 0.1758 0.1656 -0.0057 -0.0005 -0.0056 88 PRO A CB 11 C CG . PRO A 2 ? 0.1668 0.1956 0.1977 -0.0001 -0.0044 -0.0116 88 PRO A CG 12 C CD . PRO A 2 ? 0.1392 0.1596 0.1489 0.0204 0.0012 -0.0098 88 PRO A CD 13 N N . TYR A 3 ? 0.1464 0.1313 0.1374 -0.0024 -0.0233 -0.0153 89 TYR A N 14 C CA . TYR A 3 ? 0.1408 0.1247 0.1457 0.0104 -0.0183 -0.0141 89 TYR A CA 15 C C . TYR A 3 ? 0.1054 0.1348 0.1403 0.0083 -0.0122 -0.0103 89 TYR A C 16 O O . TYR A 3 ? 0.1492 0.1418 0.1651 -0.0029 -0.0051 -0.0153 89 TYR A O 17 C CB . TYR A 3 ? 0.1484 0.1258 0.1191 0.0000 -0.0135 -0.0118 89 TYR A CB 18 C CG . TYR A 3 ? 0.1196 0.1145 0.1170 0.0009 -0.0132 -0.0085 89 TYR A CG 19 C CD1 . TYR A 3 ? 0.1201 0.1053 0.1089 0.0008 -0.0125 -0.0208 89 TYR A CD1 20 C CD2 . TYR A 3 ? 0.1213 0.1202 0.1073 -0.0012 0.0015 -0.0191 89 TYR A CD2 21 C CE1 . TYR A 3 ? 0.1069 0.1034 0.1060 0.0094 -0.0048 -0.0148 89 TYR A CE1 22 C CE2 . TYR A 3 ? 0.1046 0.1111 0.1146 0.0007 0.0062 -0.0243 89 TYR A CE2 23 C CZ . TYR A 3 ? 0.1065 0.1031 0.1057 0.0027 -0.0021 -0.0142 89 TYR A CZ 24 O OH . TYR A 3 ? 0.0990 0.1006 0.1308 0.0048 -0.0047 -0.0111 89 TYR A OH 25 N N . ASN A 4 ? 0.1470 0.1414 0.1609 0.0041 -0.0083 -0.0132 90 ASN A N 26 C CA . ASN A 4 ? 0.1276 0.1478 0.1753 0.0002 -0.0037 -0.0189 90 ASN A CA 27 C C . ASN A 4 ? 0.1336 0.1362 0.1429 0.0036 -0.0037 -0.0131 90 ASN A C 28 O O . ASN A 4 ? 0.1824 0.1533 0.1699 0.0026 0.0000 -0.0113 90 ASN A O 29 C CB . ASN A 4 ? 0.1491 0.1867 0.2010 -0.0027 0.0000 -0.0212 90 ASN A CB 30 C CG . ASN A 4 ? 0.1585 0.2612 0.2403 0.0029 0.0033 -0.0219 90 ASN A CG 31 O OD1 . ASN A 4 ? 0.2383 0.3354 0.2952 0.0118 0.0166 -0.0256 90 ASN A OD1 32 N ND2 . ASN A 4 ? 0.3228 0.3583 0.3696 0.0322 -0.0251 -0.0027 90 ASN A ND2 33 N N . GLY A 5 ? 0.1252 0.1322 0.1402 0.0010 0.0173 -0.0120 91 GLY A N 34 C CA . GLY A 5 ? 0.1109 0.1263 0.1274 0.0100 0.0115 -0.0140 91 GLY A CA 35 C C . GLY A 5 ? 0.1087 0.1137 0.1129 0.0049 -0.0072 -0.0124 91 GLY A C 36 O O . GLY A 5 ? 0.1164 0.1369 0.1271 0.0012 0.0011 -0.0187 91 GLY A O 37 N N . ASN A 6 ? 0.1012 0.1062 0.1143 -0.0035 -0.0036 -0.0104 92 ASN A N 38 C CA . ASN A 6 ? 0.0921 0.1042 0.1055 0.0012 -0.0099 -0.0083 92 ASN A CA 39 C C . ASN A 6 ? 0.0816 0.0897 0.0987 0.0030 -0.0104 -0.0028 92 ASN A C 40 O O . ASN A 6 ? 0.0950 0.1013 0.1033 0.0087 -0.0134 -0.0010 92 ASN A O 41 C CB . ASN A 6 ? 0.0885 0.0995 0.1066 0.0017 -0.0120 -0.0083 92 ASN A CB 42 C CG . ASN A 6 ? 0.0854 0.0904 0.0954 0.0005 -0.0117 -0.0069 92 ASN A CG 43 O OD1 . ASN A 6 ? 0.0903 0.0965 0.1150 0.0019 -0.0077 -0.0131 92 ASN A OD1 44 N ND2 . ASN A 6 ? 0.0961 0.1113 0.1185 0.0085 -0.0083 -0.0085 92 ASN A ND2 45 N N . PRO A 7 ? 0.0838 0.0937 0.0962 0.0056 -0.0112 -0.0060 93 PRO A N 46 C CA . PRO A 7 ? 0.0890 0.0964 0.0977 0.0077 -0.0105 -0.0102 93 PRO A CA 47 C C . PRO A 7 ? 0.0986 0.0948 0.1012 0.0029 -0.0067 -0.0037 93 PRO A C 48 O O . PRO A 7 ? 0.1075 0.0966 0.1062 0.0061 -0.0005 -0.0022 93 PRO A O 49 C CB . PRO A 7 ? 0.0955 0.0992 0.0925 0.0077 -0.0071 -0.0096 93 PRO A CB 50 C CG . PRO A 7 ? 0.0914 0.0919 0.0917 0.0006 0.0007 -0.0030 93 PRO A CG 51 C CD . PRO A 7 ? 0.0936 0.0924 0.1004 0.0086 -0.0088 0.0027 93 PRO A CD 52 N N . PHE A 8 ? 0.0916 0.0903 0.0905 0.0062 -0.0082 -0.0053 94 PHE A N 53 C CA . PHE A 8 ? 0.0990 0.0905 0.0982 0.0007 -0.0112 -0.0072 94 PHE A CA 54 C C . PHE A 8 ? 0.1084 0.1025 0.1091 0.0031 -0.0115 0.0026 94 PHE A C 55 O O . PHE A 8 ? 0.1126 0.1076 0.1043 0.0046 -0.0075 -0.0002 94 PHE A O 56 C CB . PHE A 8 ? 0.1092 0.0806 0.1006 0.0000 -0.0029 0.0020 94 PHE A CB 57 C CG . PHE A 8 ? 0.0909 0.0857 0.0887 0.0091 0.0030 -0.0091 94 PHE A CG 58 C CD1 . PHE A 8 ? 0.0920 0.0877 0.0903 -0.0022 -0.0006 -0.0086 94 PHE A CD1 59 C CD2 . PHE A 8 ? 0.1015 0.0832 0.0944 0.0062 -0.0037 -0.0002 94 PHE A CD2 60 C CE1 . PHE A 8 ? 0.0989 0.0874 0.0996 0.0107 0.0047 -0.0055 94 PHE A CE1 61 C CE2 . PHE A 8 ? 0.0878 0.0891 0.0937 0.0046 0.0092 -0.0086 94 PHE A CE2 62 C CZ . PHE A 8 ? 0.0887 0.0926 0.0903 0.0066 -0.0065 -0.0123 94 PHE A CZ 63 N N . GLU A 9 ? 0.1106 0.1148 0.1055 0.0069 -0.0192 0.0014 95 GLU A N 64 C CA . GLU A 9 ? 0.1235 0.1319 0.1271 0.0006 -0.0282 0.0006 95 GLU A CA 65 C C . GLU A 9 ? 0.1178 0.1413 0.1322 0.0001 -0.0345 0.0091 95 GLU A C 66 O O . GLU A 9 ? 0.1361 0.1514 0.1685 0.0252 -0.0192 0.0005 95 GLU A O 67 C CB A GLU A 9 ? 0.1323 0.1485 0.1343 -0.0078 -0.0399 0.0031 95 GLU A CB 68 C CB B GLU A 9 ? 0.1354 0.1470 0.1413 -0.0061 -0.0344 -0.0004 95 GLU A CB 69 C CG A GLU A 9 ? 0.1884 0.1888 0.1644 0.0072 -0.0225 -0.0011 95 GLU A CG 70 C CG B GLU A 9 ? 0.1565 0.1618 0.1629 -0.0072 -0.0291 0.0037 95 GLU A CG 71 C CD A GLU A 9 ? 0.2444 0.2470 0.2748 -0.0032 0.0028 -0.0061 95 GLU A CD 72 C CD B GLU A 9 ? 0.2341 0.2371 0.2155 -0.0106 -0.0083 -0.0268 95 GLU A CD 73 O OE1 A GLU A 9 ? 0.2237 0.2824 0.2864 -0.0243 -0.0157 -0.0141 95 GLU A OE1 74 O OE1 B GLU A 9 ? 0.2992 0.2908 0.2697 -0.0028 -0.0196 0.0181 95 GLU A OE1 75 O OE2 A GLU A 9 ? 0.2745 0.2595 0.2661 0.0043 -0.0145 -0.0117 95 GLU A OE2 76 O OE2 B GLU A 9 ? 0.3303 0.3065 0.3069 -0.0026 0.0146 0.0151 95 GLU A OE2 77 N N . GLY A 10 ? 0.1484 0.1549 0.1625 -0.0026 -0.0274 0.0142 96 GLY A N 78 C CA . GLY A 10 ? 0.1513 0.1650 0.1917 0.0021 -0.0277 0.0211 96 GLY A CA 79 C C . GLY A 10 ? 0.1280 0.1500 0.1840 -0.0002 -0.0200 0.0157 96 GLY A C 80 O O . GLY A 10 ? 0.1564 0.1678 0.2421 0.0182 -0.0273 0.0311 96 GLY A O 81 N N . VAL A 11 ? 0.1156 0.1328 0.1514 0.0043 -0.0263 0.0128 97 VAL A N 82 C CA . VAL A 11 ? 0.1126 0.1096 0.1347 0.0051 -0.0199 0.0108 97 VAL A CA 83 C C . VAL A 11 ? 0.1256 0.1112 0.1069 0.0185 -0.0151 0.0037 97 VAL A C 84 O O . VAL A 11 ? 0.1733 0.1310 0.1474 0.0123 -0.0015 -0.0080 97 VAL A O 85 C CB . VAL A 11 ? 0.1148 0.1001 0.1152 0.0068 -0.0029 0.0032 97 VAL A CB 86 C CG1 . VAL A 11 ? 0.1567 0.1514 0.1614 0.0179 0.0005 0.0178 97 VAL A CG1 87 C CG2 . VAL A 11 ? 0.1345 0.1135 0.1268 0.0122 -0.0178 -0.0016 97 VAL A CG2 88 N N . GLN A 12 ? 0.1025 0.1122 0.1193 0.0186 -0.0052 0.0030 98 GLN A N 89 C CA . GLN A 12 ? 0.1257 0.1344 0.1078 0.0123 -0.0036 0.0075 98 GLN A CA 90 C C . GLN A 12 ? 0.1091 0.0975 0.0905 0.0088 -0.0059 0.0070 98 GLN A C 91 O O . GLN A 12 ? 0.1181 0.1172 0.1050 0.0205 -0.0075 -0.0066 98 GLN A O 92 C CB . GLN A 12 ? 0.1424 0.1675 0.1425 0.0042 0.0011 0.0065 98 GLN A CB 93 C CG . GLN A 12 ? 0.1585 0.1591 0.1626 0.0068 -0.0109 0.0225 98 GLN A CG 94 C CD . GLN A 12 ? 0.1750 0.1608 0.2002 0.0240 0.0015 0.0136 98 GLN A CD 95 O OE1 . GLN A 12 ? 0.1701 0.1711 0.1828 0.0195 0.0166 0.0131 98 GLN A OE1 96 N NE2 . GLN A 12 ? 0.1904 0.1457 0.1507 0.0226 -0.0083 0.0235 98 GLN A NE2 97 N N . LEU A 13 ? 0.1047 0.0989 0.0939 0.0058 -0.0044 0.0012 99 LEU A N 98 C CA . LEU A 13 ? 0.0919 0.0953 0.0915 0.0124 -0.0046 -0.0009 99 LEU A CA 99 C C . LEU A 13 ? 0.0962 0.0893 0.0862 0.0171 0.0015 0.0018 99 LEU A C 100 O O . LEU A 13 ? 0.1043 0.0977 0.0979 0.0032 0.0028 0.0080 99 LEU A O 101 C CB . LEU A 13 ? 0.0963 0.0891 0.0957 0.0096 -0.0027 -0.0012 99 LEU A CB 102 C CG . LEU A 13 ? 0.1018 0.0962 0.0962 0.0044 -0.0085 -0.0040 99 LEU A CG 103 C CD1 . LEU A 13 ? 0.1176 0.1040 0.1191 0.0050 0.0131 0.0033 99 LEU A CD1 104 C CD2 . LEU A 13 ? 0.1187 0.0978 0.1143 -0.0073 0.0094 -0.0046 99 LEU A CD2 105 N N . TRP A 14 ? 0.0986 0.0929 0.0801 0.0006 0.0042 0.0036 100 TRP A N 106 C CA . TRP A 14 ? 0.0948 0.0920 0.0903 0.0083 -0.0021 0.0018 100 TRP A CA 107 C C . TRP A 14 ? 0.0991 0.0817 0.0893 0.0028 0.0031 0.0026 100 TRP A C 108 O O . TRP A 14 ? 0.1040 0.0917 0.0977 0.0050 0.0026 0.0021 100 TRP A O 109 C CB . TRP A 14 ? 0.1089 0.0928 0.1028 0.0098 0.0033 0.0042 100 TRP A CB 110 C CG . TRP A 14 ? 0.1092 0.1035 0.0986 0.0084 0.0100 -0.0010 100 TRP A CG 111 C CD1 . TRP A 14 ? 0.1167 0.0949 0.1074 0.0056 0.0000 -0.0095 100 TRP A CD1 112 C CD2 . TRP A 14 ? 0.1123 0.0981 0.1037 0.0074 -0.0016 0.0001 100 TRP A CD2 113 N NE1 . TRP A 14 ? 0.1151 0.1041 0.1130 -0.0020 0.0003 -0.0119 100 TRP A NE1 114 C CE2 . TRP A 14 ? 0.1242 0.1004 0.1173 0.0016 0.0139 0.0009 100 TRP A CE2 115 C CE3 . TRP A 14 ? 0.1335 0.1055 0.1236 0.0024 0.0045 -0.0006 100 TRP A CE3 116 C CZ2 . TRP A 14 ? 0.1331 0.1094 0.1336 -0.0061 0.0038 -0.0037 100 TRP A CZ2 117 C CZ3 . TRP A 14 ? 0.1361 0.1242 0.1404 0.0156 -0.0076 0.0119 100 TRP A CZ3 118 C CH2 . TRP A 14 ? 0.1434 0.0993 0.1575 0.0010 -0.0039 0.0040 100 TRP A CH2 119 N N . ALA A 15 ? 0.0986 0.0868 0.0915 0.0048 -0.0025 0.0044 101 ALA A N 120 C CA . ALA A 15 ? 0.1005 0.0992 0.1006 -0.0020 -0.0028 0.0013 101 ALA A CA 121 C C . ALA A 15 ? 0.1097 0.0934 0.1136 0.0058 0.0016 0.0045 101 ALA A C 122 O O . ALA A 15 ? 0.1194 0.1021 0.1244 0.0008 -0.0087 0.0023 101 ALA A O 123 C CB . ALA A 15 ? 0.0987 0.0916 0.1101 0.0017 0.0036 -0.0002 101 ALA A CB 124 N N . ASN A 16 ? 0.1072 0.0862 0.1028 -0.0018 -0.0021 -0.0079 102 ASN A N 125 C CA . ASN A 16 ? 0.1070 0.0941 0.1133 0.0040 -0.0034 -0.0110 102 ASN A CA 126 C C . ASN A 16 ? 0.1112 0.0890 0.0939 -0.0017 0.0064 -0.0114 102 ASN A C 127 O O . ASN A 16 ? 0.1065 0.1008 0.1107 -0.0056 0.0019 -0.0090 102 ASN A O 128 C CB . ASN A 16 ? 0.1091 0.1024 0.1079 0.0033 0.0007 -0.0102 102 ASN A CB 129 C CG . ASN A 16 ? 0.1029 0.0934 0.0988 0.0014 0.0030 0.0023 102 ASN A CG 130 O OD1 . ASN A 16 ? 0.1117 0.1002 0.1104 0.0013 -0.0009 -0.0074 102 ASN A OD1 131 N ND2 . ASN A 16 ? 0.1144 0.0971 0.1043 -0.0021 0.0005 -0.0050 102 ASN A ND2 132 N N . ASN A 17 ? 0.1194 0.0940 0.1177 -0.0067 0.0075 -0.0170 103 ASN A N 133 C CA . ASN A 17 ? 0.1339 0.0969 0.1180 -0.0014 0.0085 -0.0058 103 ASN A CA 134 C C . ASN A 17 ? 0.1340 0.1011 0.1187 -0.0119 0.0080 -0.0119 103 ASN A C 135 O O . ASN A 17 ? 0.1250 0.1044 0.1354 -0.0092 0.0088 -0.0086 103 ASN A O 136 C CB . ASN A 17 ? 0.1466 0.1060 0.1278 -0.0006 0.0029 -0.0127 103 ASN A CB 137 C CG . ASN A 17 ? 0.1655 0.1423 0.1594 -0.0118 0.0079 -0.0090 103 ASN A CG 138 O OD1 . ASN A 17 ? 0.2106 0.1373 0.1654 0.0004 0.0081 0.0077 103 ASN A OD1 139 N ND2 . ASN A 17 ? 0.1689 0.1445 0.1923 -0.0076 -0.0099 -0.0004 103 ASN A ND2 140 N N . TYR A 18 ? 0.1220 0.1091 0.1083 -0.0017 0.0133 -0.0120 104 TYR A N 141 C CA . TYR A 18 ? 0.1247 0.1097 0.1191 -0.0070 0.0003 -0.0130 104 TYR A CA 142 C C . TYR A 18 ? 0.1062 0.0998 0.1044 0.0009 -0.0030 -0.0050 104 TYR A C 143 O O . TYR A 18 ? 0.1157 0.1007 0.1084 -0.0058 -0.0004 -0.0094 104 TYR A O 144 C CB . TYR A 18 ? 0.1295 0.1169 0.1135 -0.0152 0.0116 -0.0116 104 TYR A CB 145 C CG . TYR A 18 ? 0.1214 0.1119 0.1070 -0.0219 0.0089 -0.0099 104 TYR A CG 146 C CD1 . TYR A 18 ? 0.1464 0.1308 0.1177 0.0091 0.0016 0.0004 104 TYR A CD1 147 C CD2 . TYR A 18 ? 0.1267 0.1252 0.1148 -0.0189 0.0083 -0.0071 104 TYR A CD2 148 C CE1 . TYR A 18 ? 0.1562 0.1523 0.1286 0.0057 0.0087 -0.0166 104 TYR A CE1 149 C CE2 . TYR A 18 ? 0.1369 0.1411 0.1379 -0.0302 -0.0087 -0.0157 104 TYR A CE2 150 C CZ . TYR A 18 ? 0.1146 0.1366 0.1291 -0.0085 0.0048 0.0164 104 TYR A CZ 151 O OH . TYR A 18 ? 0.1520 0.1825 0.1817 -0.0209 -0.0102 0.0229 104 TYR A OH 152 N N . TYR A 19 ? 0.1058 0.0993 0.0968 -0.0083 -0.0030 -0.0041 105 TYR A N 153 C CA . TYR A 19 ? 0.0961 0.0939 0.0946 -0.0041 -0.0066 -0.0003 105 TYR A CA 154 C C . TYR A 19 ? 0.1017 0.0891 0.1017 -0.0087 -0.0068 -0.0101 105 TYR A C 155 O O . TYR A 19 ? 0.1045 0.0926 0.0965 -0.0103 -0.0031 -0.0038 105 TYR A O 156 C CB . TYR A 19 ? 0.1098 0.0924 0.0966 -0.0012 -0.0001 -0.0018 105 TYR A CB 157 C CG . TYR A 19 ? 0.0955 0.0820 0.0997 -0.0051 -0.0020 -0.0036 105 TYR A CG 158 C CD1 . TYR A 19 ? 0.0932 0.0930 0.0946 0.0012 -0.0086 -0.0005 105 TYR A CD1 159 C CD2 . TYR A 19 ? 0.1046 0.0859 0.1001 -0.0052 -0.0023 -0.0054 105 TYR A CD2 160 C CE1 . TYR A 19 ? 0.1041 0.1051 0.0897 0.0091 -0.0109 0.0014 105 TYR A CE1 161 C CE2 . TYR A 19 ? 0.0979 0.0921 0.0936 -0.0025 -0.0065 0.0061 105 TYR A CE2 162 C CZ . TYR A 19 ? 0.1009 0.0896 0.0957 -0.0027 0.0034 0.0017 105 TYR A CZ 163 O OH . TYR A 19 ? 0.1155 0.1029 0.0985 0.0031 0.0101 -0.0041 105 TYR A OH 164 N N . ARG A 20 ? 0.1063 0.0957 0.1021 -0.0083 0.0028 -0.0026 106 ARG A N 165 C CA . ARG A 20 ? 0.1099 0.0958 0.0922 -0.0007 -0.0019 0.0004 106 ARG A CA 166 C C . ARG A 20 ? 0.1225 0.1154 0.1040 0.0013 0.0028 0.0021 106 ARG A C 167 O O . ARG A 20 ? 0.1158 0.1045 0.1160 -0.0070 0.0058 0.0088 106 ARG A O 168 C CB . ARG A 20 ? 0.1223 0.1064 0.1154 -0.0027 0.0034 0.0056 106 ARG A CB 169 C CG . ARG A 20 ? 0.1180 0.1117 0.1171 -0.0089 0.0040 -0.0022 106 ARG A CG 170 C CD . ARG A 20 ? 0.1304 0.1059 0.1341 -0.0009 -0.0046 0.0205 106 ARG A CD 171 N NE . ARG A 20 ? 0.1296 0.1104 0.1212 0.0073 0.0009 0.0102 106 ARG A NE 172 C CZ . ARG A 20 ? 0.1193 0.1088 0.1373 0.0110 -0.0059 0.0067 106 ARG A CZ 173 N NH1 . ARG A 20 ? 0.1301 0.1155 0.1327 0.0036 -0.0005 0.0037 106 ARG A NH1 174 N NH2 . ARG A 20 ? 0.1356 0.1185 0.1388 -0.0020 -0.0035 0.0018 106 ARG A NH2 175 N N . SER A 21 ? 0.1182 0.0999 0.1117 -0.0120 0.0044 -0.0084 107 SER A N 176 C CA . SER A 21 ? 0.1231 0.1022 0.1221 -0.0143 0.0063 -0.0037 107 SER A CA 177 C C . SER A 21 ? 0.1150 0.0939 0.1064 -0.0127 0.0005 0.0017 107 SER A C 178 O O . SER A 21 ? 0.1222 0.1153 0.1252 -0.0173 0.0011 -0.0013 107 SER A O 179 C CB A SER A 21 ? 0.1266 0.1141 0.1469 -0.0092 0.0046 -0.0098 107 SER A CB 180 C CB B SER A 21 ? 0.1257 0.1145 0.1424 -0.0115 0.0017 -0.0091 107 SER A CB 181 O OG A SER A 21 ? 0.1396 0.1304 0.1455 -0.0161 -0.0002 -0.0099 107 SER A OG 182 O OG B SER A 21 ? 0.1660 0.1435 0.1840 0.0064 0.0062 -0.0051 107 SER A OG 183 N N . GLU A 22 ? 0.1159 0.0968 0.1092 -0.0150 -0.0028 0.0011 108 GLU A N 184 C CA . GLU A 22 ? 0.1019 0.1084 0.1027 -0.0123 -0.0076 -0.0012 108 GLU A CA 185 C C . GLU A 22 ? 0.1055 0.0948 0.1141 -0.0075 -0.0022 0.0033 108 GLU A C 186 O O . GLU A 22 ? 0.1132 0.1084 0.1089 -0.0149 -0.0026 0.0002 108 GLU A O 187 C CB . GLU A 22 ? 0.1132 0.1025 0.0947 -0.0090 -0.0001 -0.0059 108 GLU A CB 188 C CG . GLU A 22 ? 0.1108 0.1069 0.1009 -0.0030 -0.0110 0.0023 108 GLU A CG 189 C CD . GLU A 22 ? 0.1163 0.1059 0.0919 -0.0049 -0.0057 -0.0091 108 GLU A CD 190 O OE1 . GLU A 22 ? 0.1059 0.1084 0.1095 -0.0039 -0.0073 -0.0031 108 GLU A OE1 191 O OE2 . GLU A 22 ? 0.1204 0.1163 0.1092 -0.0043 -0.0121 -0.0002 108 GLU A OE2 192 N N . VAL A 23 ? 0.1068 0.0999 0.1059 -0.0111 -0.0019 0.0022 109 VAL A N 193 C CA . VAL A 23 ? 0.1033 0.0985 0.1014 -0.0097 -0.0022 0.0109 109 VAL A CA 194 C C . VAL A 23 ? 0.0997 0.1116 0.1060 -0.0061 0.0008 0.0010 109 VAL A C 195 O O . VAL A 23 ? 0.1229 0.1141 0.1198 -0.0090 0.0078 0.0091 109 VAL A O 196 C CB . VAL A 23 ? 0.1085 0.0953 0.1088 -0.0071 -0.0035 0.0044 109 VAL A CB 197 C CG1 . VAL A 23 ? 0.1201 0.1120 0.1167 -0.0088 -0.0014 0.0167 109 VAL A CG1 198 C CG2 . VAL A 23 ? 0.1065 0.1015 0.1063 -0.0128 0.0004 0.0023 109 VAL A CG2 199 N N . HIS A 24 ? 0.1198 0.1010 0.1182 -0.0149 0.0090 0.0097 110 HIS A N 200 C CA . HIS A 24 ? 0.1305 0.1109 0.1188 -0.0141 0.0017 0.0129 110 HIS A CA 201 C C . HIS A 24 ? 0.1338 0.1120 0.1342 -0.0168 0.0071 0.0133 110 HIS A C 202 O O . HIS A 24 ? 0.1611 0.1337 0.1612 -0.0299 0.0102 0.0213 110 HIS A O 203 C CB . HIS A 24 ? 0.1435 0.1200 0.1193 -0.0064 -0.0020 0.0133 110 HIS A CB 204 C CG . HIS A 24 ? 0.1262 0.1207 0.1254 0.0064 -0.0035 0.0199 110 HIS A CG 205 N ND1 . HIS A 24 ? 0.1708 0.1761 0.1628 -0.0230 -0.0227 0.0353 110 HIS A ND1 206 C CD2 . HIS A 24 ? 0.1521 0.1356 0.1468 -0.0118 -0.0060 0.0005 110 HIS A CD2 207 C CE1 . HIS A 24 ? 0.1709 0.1816 0.1605 -0.0172 -0.0123 0.0138 110 HIS A CE1 208 N NE2 . HIS A 24 ? 0.1518 0.1327 0.1509 -0.0106 -0.0012 0.0161 110 HIS A NE2 209 N N . THR A 25 ? 0.1324 0.1209 0.1396 -0.0135 0.0032 0.0022 111 THR A N 210 C CA . THR A 25 ? 0.1404 0.1184 0.1504 -0.0278 -0.0057 -0.0019 111 THR A CA 211 C C . THR A 25 ? 0.1298 0.1186 0.1325 -0.0279 0.0013 -0.0010 111 THR A C 212 O O . THR A 25 ? 0.1450 0.1319 0.1634 -0.0383 -0.0180 0.0131 111 THR A O 213 C CB . THR A 25 ? 0.1849 0.1593 0.1770 -0.0347 -0.0250 -0.0319 111 THR A CB 214 O OG1 . THR A 25 ? 0.2242 0.2179 0.2003 -0.0212 -0.0202 -0.0136 111 THR A OG1 215 C CG2 . THR A 25 ? 0.1976 0.1685 0.1935 -0.0113 -0.0087 -0.0139 111 THR A CG2 216 N N . LEU A 26 ? 0.1302 0.1156 0.1244 -0.0136 -0.0112 0.0031 112 LEU A N 217 C CA . LEU A 26 ? 0.1148 0.1178 0.1274 -0.0223 -0.0049 0.0020 112 LEU A CA 218 C C . LEU A 26 ? 0.1103 0.1368 0.1239 -0.0111 0.0058 0.0110 112 LEU A C 219 O O . LEU A 26 ? 0.1428 0.1791 0.1618 -0.0146 -0.0016 -0.0222 112 LEU A O 220 C CB . LEU A 26 ? 0.1127 0.1170 0.1149 -0.0085 -0.0083 0.0033 112 LEU A CB 221 C CG . LEU A 26 ? 0.1289 0.1181 0.1169 -0.0198 -0.0141 -0.0067 112 LEU A CG 222 C CD1 . LEU A 26 ? 0.1354 0.1127 0.1108 -0.0101 -0.0059 -0.0081 112 LEU A CD1 223 C CD2 . LEU A 26 ? 0.1591 0.1270 0.1364 -0.0254 -0.0157 -0.0035 112 LEU A CD2 224 N N . ALA A 27 ? 0.1125 0.1106 0.1141 -0.0126 -0.0014 0.0057 113 ALA A N 225 C CA . ALA A 27 ? 0.1081 0.1081 0.1135 -0.0084 0.0024 0.0108 113 ALA A CA 226 C C . ALA A 27 ? 0.1123 0.1164 0.1170 -0.0107 0.0026 0.0094 113 ALA A C 227 O O . ALA A 27 ? 0.1315 0.1355 0.1325 -0.0091 0.0078 0.0126 113 ALA A O 228 C CB . ALA A 27 ? 0.1157 0.1113 0.1003 -0.0101 -0.0057 0.0109 113 ALA A CB 229 N N . ILE A 28 ? 0.1193 0.1203 0.1171 -0.0147 0.0067 0.0177 114 ILE A N 230 C CA . ILE A 28 ? 0.1334 0.1123 0.1162 -0.0116 0.0045 0.0076 114 ILE A CA 231 C C . ILE A 28 ? 0.1506 0.1194 0.1216 -0.0093 0.0114 0.0085 114 ILE A C 232 O O . ILE A 28 ? 0.1460 0.1559 0.1353 -0.0168 0.0176 0.0088 114 ILE A O 233 C CB . ILE A 28 ? 0.1480 0.1175 0.1230 -0.0174 0.0003 0.0155 114 ILE A CB 234 C CG1 . ILE A 28 ? 0.1420 0.1238 0.1124 -0.0143 -0.0064 0.0071 114 ILE A CG1 235 C CG2 . ILE A 28 ? 0.1729 0.1459 0.1501 -0.0065 0.0019 0.0289 114 ILE A CG2 236 C CD1 . ILE A 28 ? 0.1619 0.1376 0.1186 -0.0134 -0.0074 0.0152 114 ILE A CD1 237 N N . PRO A 29 ? 0.1442 0.1234 0.1468 -0.0359 0.0076 0.0124 115 PRO A N 238 C CA . PRO A 29 ? 0.1764 0.1499 0.1703 -0.0377 -0.0005 0.0039 115 PRO A CA 239 C C . PRO A 29 ? 0.1600 0.1779 0.1948 -0.0458 0.0180 0.0064 115 PRO A C 240 O O . PRO A 29 ? 0.1908 0.2413 0.2420 -0.0520 0.0275 0.0127 115 PRO A O 241 C CB . PRO A 29 ? 0.1974 0.1696 0.1734 -0.0270 -0.0028 -0.0011 115 PRO A CB 242 C CG . PRO A 29 ? 0.1874 0.1617 0.1617 -0.0301 -0.0049 -0.0024 115 PRO A CG 243 C CD . PRO A 29 ? 0.1645 0.1335 0.1415 -0.0215 -0.0010 0.0078 115 PRO A CD 244 N N . GLN A 30 ? 0.1662 0.1809 0.1841 -0.0130 0.0107 0.0025 116 GLN A N 245 C CA . GLN A 30 ? 0.1745 0.1978 0.1837 -0.0159 0.0001 -0.0073 116 GLN A CA 246 C C . GLN A 30 ? 0.1800 0.2069 0.1952 0.0033 0.0103 -0.0005 116 GLN A C 247 O O . GLN A 30 ? 0.2242 0.2485 0.2298 0.0205 -0.0106 -0.0299 116 GLN A O 248 C CB . GLN A 30 ? 0.1764 0.1942 0.2121 -0.0045 -0.0090 0.0004 116 GLN A CB 249 C CG . GLN A 30 ? 0.2202 0.2367 0.2370 -0.0041 -0.0077 -0.0061 116 GLN A CG 250 C CD . GLN A 30 ? 0.2894 0.2885 0.2879 0.0129 0.0039 0.0154 116 GLN A CD 251 O OE1 . GLN A 30 ? 0.2971 0.3494 0.3567 0.0327 0.0263 0.0111 116 GLN A OE1 252 N NE2 . GLN A 30 ? 0.2607 0.2921 0.2599 0.0128 -0.0185 -0.0120 116 GLN A NE2 253 N N . ILE A 31 ? 0.1649 0.1714 0.1599 -0.0069 0.0136 0.0008 117 ILE A N 254 C CA . ILE A 31 ? 0.1658 0.1714 0.1652 -0.0098 0.0154 0.0035 117 ILE A CA 255 C C . ILE A 31 ? 0.1637 0.1713 0.1696 -0.0013 0.0123 0.0017 117 ILE A C 256 O O . ILE A 31 ? 0.1824 0.1692 0.1933 -0.0073 0.0143 0.0063 117 ILE A O 257 C CB . ILE A 31 ? 0.1629 0.1577 0.1621 -0.0172 0.0137 0.0040 117 ILE A CB 258 C CG1 . ILE A 31 ? 0.1561 0.1937 0.1659 -0.0160 0.0244 0.0074 117 ILE A CG1 259 C CG2 . ILE A 31 ? 0.1666 0.1754 0.1667 -0.0075 0.0123 0.0022 117 ILE A CG2 260 C CD1 . ILE A 31 ? 0.1746 0.1887 0.1828 -0.0348 0.0155 0.0035 117 ILE A CD1 261 N N . THR A 32 ? 0.1979 0.1934 0.1828 -0.0027 0.0159 0.0006 118 THR A N 262 C CA . THR A 32 ? 0.1916 0.1947 0.1883 -0.0138 0.0144 0.0107 118 THR A CA 263 C C . THR A 32 ? 0.1765 0.1858 0.1865 -0.0182 0.0077 0.0061 118 THR A C 264 O O . THR A 32 ? 0.2230 0.2016 0.1885 -0.0127 0.0069 0.0133 118 THR A O 265 C CB . THR A 32 ? 0.2060 0.2166 0.2097 -0.0194 0.0213 0.0132 118 THR A CB 266 O OG1 . THR A 32 ? 0.2232 0.2595 0.2641 -0.0077 0.0373 0.0062 118 THR A OG1 267 C CG2 . THR A 32 ? 0.2309 0.2649 0.2618 -0.0153 0.0065 0.0007 118 THR A CG2 268 N N . ASP A 33 ? 0.1863 0.1779 0.1724 -0.0086 0.0202 0.0052 119 ASP A N 269 C CA . ASP A 33 ? 0.1814 0.1906 0.1792 -0.0110 0.0220 0.0087 119 ASP A CA 270 C C . ASP A 33 ? 0.1747 0.1836 0.1798 -0.0216 0.0267 -0.0003 119 ASP A C 271 O O . ASP A 33 ? 0.1716 0.1872 0.1761 -0.0182 0.0405 -0.0027 119 ASP A O 272 C CB . ASP A 33 ? 0.2065 0.1917 0.2102 -0.0099 0.0263 -0.0006 119 ASP A CB 273 C CG . ASP A 33 ? 0.2197 0.2387 0.2283 -0.0201 0.0319 -0.0123 119 ASP A CG 274 O OD1 . ASP A 33 ? 0.2846 0.3091 0.2537 -0.0239 0.0486 -0.0130 119 ASP A OD1 275 O OD2 . ASP A 33 ? 0.2235 0.2555 0.2724 -0.0237 0.0369 -0.0565 119 ASP A OD2 276 N N . PRO A 34 ? 0.1733 0.1861 0.1735 -0.0240 0.0304 0.0063 120 PRO A N 277 C CA . PRO A 34 ? 0.1916 0.1878 0.1795 -0.0205 0.0055 0.0108 120 PRO A CA 278 C C . PRO A 34 ? 0.1778 0.1930 0.1822 -0.0127 0.0161 -0.0068 120 PRO A C 279 O O . PRO A 34 ? 0.1922 0.1912 0.1638 -0.0110 0.0225 -0.0005 120 PRO A O 280 C CB . PRO A 34 ? 0.2000 0.2092 0.1971 -0.0178 0.0041 0.0062 120 PRO A CB 281 C CG . PRO A 34 ? 0.2001 0.2181 0.1830 -0.0206 0.0222 -0.0003 120 PRO A CG 282 C CD . PRO A 34 ? 0.1737 0.2086 0.1736 -0.0249 0.0392 0.0179 120 PRO A CD 283 N N . ALA A 35 ? 0.2004 0.2034 0.1841 -0.0299 0.0268 -0.0085 121 ALA A N 284 C CA . ALA A 35 ? 0.1954 0.2047 0.1869 -0.0229 0.0196 -0.0149 121 ALA A CA 285 C C . ALA A 35 ? 0.1870 0.1911 0.1783 -0.0185 0.0248 -0.0193 121 ALA A C 286 O O . ALA A 35 ? 0.1743 0.1960 0.1949 -0.0347 0.0248 -0.0129 121 ALA A O 287 C CB . ALA A 35 ? 0.2132 0.2110 0.2013 -0.0371 0.0235 -0.0293 121 ALA A CB 288 N N . LEU A 36 ? 0.1766 0.1771 0.1791 -0.0098 0.0257 -0.0126 122 LEU A N 289 C CA . LEU A 36 ? 0.1732 0.1536 0.1831 -0.0139 0.0306 -0.0116 122 LEU A CA 290 C C . LEU A 36 ? 0.1634 0.1543 0.1586 -0.0114 0.0187 -0.0089 122 LEU A C 291 O O . LEU A 36 ? 0.1541 0.1555 0.1574 -0.0079 0.0276 0.0064 122 LEU A O 292 C CB . LEU A 36 ? 0.1939 0.1606 0.2082 -0.0152 0.0209 -0.0080 122 LEU A CB 293 C CG . LEU A 36 ? 0.2236 0.1888 0.2353 -0.0045 0.0298 -0.0064 122 LEU A CG 294 C CD1 . LEU A 36 ? 0.2844 0.2602 0.3011 -0.0201 0.0018 0.0199 122 LEU A CD1 295 C CD2 . LEU A 36 ? 0.2524 0.2466 0.2894 -0.0376 0.0064 0.0070 122 LEU A CD2 296 N N . ARG A 37 ? 0.1392 0.1456 0.1523 -0.0145 0.0192 0.0031 123 ARG A N 297 C CA . ARG A 37 ? 0.1360 0.1215 0.1305 -0.0172 0.0111 0.0126 123 ARG A CA 298 C C . ARG A 37 ? 0.1517 0.1287 0.1382 -0.0130 0.0128 -0.0003 123 ARG A C 299 O O . ARG A 37 ? 0.1519 0.1328 0.1419 -0.0142 0.0205 0.0003 123 ARG A O 300 C CB . ARG A 37 ? 0.1515 0.1238 0.1535 -0.0190 0.0154 0.0103 123 ARG A CB 301 C CG . ARG A 37 ? 0.1563 0.1455 0.1581 -0.0155 0.0165 0.0131 123 ARG A CG 302 C CD . ARG A 37 ? 0.1542 0.1525 0.1486 -0.0256 0.0170 0.0097 123 ARG A CD 303 N NE . ARG A 37 ? 0.1653 0.1499 0.1679 -0.0262 0.0181 0.0261 123 ARG A NE 304 C CZ . ARG A 37 ? 0.1571 0.1520 0.1624 -0.0150 0.0332 0.0289 123 ARG A CZ 305 N NH1 . ARG A 37 ? 0.1949 0.1698 0.1515 -0.0159 0.0191 0.0113 123 ARG A NH1 306 N NH2 . ARG A 37 ? 0.1948 0.1689 0.1589 -0.0125 0.0359 0.0262 123 ARG A NH2 307 N N . ALA A 38 ? 0.1468 0.1486 0.1381 -0.0210 0.0105 0.0102 124 ALA A N 308 C CA . ALA A 38 ? 0.1620 0.1489 0.1350 -0.0119 0.0082 0.0130 124 ALA A CA 309 C C . ALA A 38 ? 0.1372 0.1503 0.1387 0.0000 -0.0023 0.0071 124 ALA A C 310 O O . ALA A 38 ? 0.1583 0.1439 0.1458 -0.0110 0.0059 0.0073 124 ALA A O 311 C CB . ALA A 38 ? 0.1805 0.1670 0.1509 -0.0184 0.0055 0.0194 124 ALA A CB 312 N N . ALA A 39 ? 0.1479 0.1472 0.1221 -0.0168 0.0185 0.0072 125 ALA A N 313 C CA . ALA A 39 ? 0.1437 0.1243 0.1470 -0.0124 0.0131 0.0029 125 ALA A CA 314 C C . ALA A 39 ? 0.1238 0.1160 0.1322 -0.0065 0.0202 -0.0061 125 ALA A C 315 O O . ALA A 39 ? 0.1366 0.1286 0.1391 -0.0161 0.0083 -0.0029 125 ALA A O 316 C CB . ALA A 39 ? 0.1631 0.1499 0.1722 -0.0094 0.0052 -0.0051 125 ALA A CB 317 N N . ALA A 40 ? 0.1345 0.1145 0.1311 -0.0141 0.0120 0.0055 126 ALA A N 318 C CA . ALA A 40 ? 0.1378 0.1241 0.1333 -0.0159 -0.0048 0.0121 126 ALA A CA 319 C C . ALA A 40 ? 0.1226 0.1069 0.1151 -0.0180 -0.0016 0.0052 126 ALA A C 320 O O . ALA A 40 ? 0.1302 0.1207 0.1168 -0.0178 -0.0019 0.0106 126 ALA A O 321 C CB . ALA A 40 ? 0.1373 0.1205 0.1308 -0.0174 -0.0060 0.0191 126 ALA A CB 322 N N . SER A 41 ? 0.1286 0.1216 0.1197 -0.0195 0.0025 0.0170 127 SER A N 323 C CA . SER A 41 ? 0.1432 0.1178 0.1243 -0.0146 -0.0016 0.0122 127 SER A CA 324 C C . SER A 41 ? 0.1312 0.0987 0.1226 -0.0126 0.0022 0.0076 127 SER A C 325 O O . SER A 41 ? 0.1405 0.1266 0.1303 -0.0055 -0.0030 -0.0015 127 SER A O 326 C CB A SER A 41 ? 0.1618 0.1337 0.1533 -0.0087 0.0050 0.0084 127 SER A CB 327 C CB B SER A 41 ? 0.1584 0.1275 0.1449 -0.0051 0.0053 0.0069 127 SER A CB 328 O OG A SER A 41 ? 0.1827 0.1445 0.1655 0.0034 0.0038 0.0117 127 SER A OG 329 O OG B SER A 41 ? 0.1821 0.1680 0.1775 -0.0099 -0.0063 0.0101 127 SER A OG 330 N N . ALA A 42 ? 0.1292 0.1072 0.1051 -0.0062 -0.0022 0.0123 128 ALA A N 331 C CA . ALA A 42 ? 0.1060 0.1063 0.0984 0.0014 -0.0079 0.0023 128 ALA A CA 332 C C . ALA A 42 ? 0.1053 0.0860 0.0949 -0.0044 -0.0004 0.0000 128 ALA A C 333 O O . ALA A 42 ? 0.1107 0.1175 0.1122 -0.0025 -0.0045 -0.0063 128 ALA A O 334 C CB . ALA A 42 ? 0.1296 0.1096 0.1107 -0.0038 -0.0046 0.0142 128 ALA A CB 335 N N . VAL A 43 ? 0.1126 0.0977 0.0920 0.0023 -0.0019 0.0092 129 VAL A N 336 C CA A VAL A 43 ? 0.1147 0.0861 0.0979 0.0022 0.0016 0.0062 129 VAL A CA 337 C CA B VAL A 43 ? 0.1189 0.0898 0.0992 0.0044 0.0000 0.0068 129 VAL A CA 338 C C . VAL A 43 ? 0.0986 0.0872 0.0985 -0.0062 -0.0001 0.0088 129 VAL A C 339 O O . VAL A 43 ? 0.1012 0.0998 0.0965 0.0056 0.0022 0.0123 129 VAL A O 340 C CB A VAL A 43 ? 0.1225 0.1056 0.1008 0.0100 0.0060 0.0204 129 VAL A CB 341 C CB B VAL A 43 ? 0.1175 0.1005 0.1013 0.0067 0.0027 0.0102 129 VAL A CB 342 C CG1 A VAL A 43 ? 0.1124 0.0811 0.1037 0.0092 0.0100 0.0179 129 VAL A CG1 343 C CG1 B VAL A 43 ? 0.1589 0.1272 0.1360 0.0301 0.0125 0.0247 129 VAL A CG1 344 C CG2 A VAL A 43 ? 0.1074 0.0953 0.1196 -0.0128 -0.0122 -0.0023 129 VAL A CG2 345 C CG2 B VAL A 43 ? 0.1507 0.1292 0.1428 0.0142 -0.0031 -0.0046 129 VAL A CG2 346 N N . ALA A 44 ? 0.1021 0.0940 0.0974 0.0004 0.0049 0.0022 130 ALA A N 347 C CA . ALA A 44 ? 0.1174 0.0992 0.0950 -0.0011 -0.0052 0.0058 130 ALA A CA 348 C C . ALA A 44 ? 0.1213 0.1003 0.0951 0.0017 0.0013 0.0064 130 ALA A C 349 O O . ALA A 44 ? 0.1296 0.1118 0.1101 0.0043 0.0034 -0.0034 130 ALA A O 350 C CB . ALA A 44 ? 0.1223 0.1073 0.1247 -0.0046 -0.0015 -0.0034 130 ALA A CB 351 N N . GLU A 45 ? 0.1096 0.0981 0.0981 -0.0017 -0.0002 0.0136 131 GLU A N 352 C CA . GLU A 45 ? 0.1129 0.0922 0.1071 0.0049 0.0020 0.0196 131 GLU A CA 353 C C . GLU A 45 ? 0.0988 0.0959 0.1034 0.0026 0.0003 0.0098 131 GLU A C 354 O O . GLU A 45 ? 0.1038 0.0992 0.1219 0.0078 0.0025 0.0172 131 GLU A O 355 C CB . GLU A 45 ? 0.1162 0.1044 0.1104 -0.0004 -0.0075 0.0154 131 GLU A CB 356 C CG . GLU A 45 ? 0.1167 0.1078 0.1147 0.0081 -0.0034 0.0273 131 GLU A CG 357 C CD . GLU A 45 ? 0.1239 0.1050 0.1297 -0.0004 -0.0077 0.0174 131 GLU A CD 358 O OE1 . GLU A 45 ? 0.1381 0.1189 0.1533 0.0048 0.0025 0.0067 131 GLU A OE1 359 O OE2 . GLU A 45 ? 0.1449 0.1289 0.1477 -0.0040 -0.0040 0.0008 131 GLU A OE2 360 N N . VAL A 46 ? 0.0912 0.0857 0.0912 0.0050 0.0006 0.0103 132 VAL A N 361 C CA . VAL A 46 ? 0.0900 0.0849 0.0850 0.0012 -0.0006 0.0093 132 VAL A CA 362 C C . VAL A 46 ? 0.0907 0.0856 0.0881 0.0006 -0.0047 0.0063 132 VAL A C 363 O O . VAL A 46 ? 0.1079 0.1051 0.1014 -0.0082 -0.0064 0.0107 132 VAL A O 364 C CB . VAL A 46 ? 0.1006 0.0924 0.1080 0.0044 0.0023 0.0109 132 VAL A CB 365 C CG1 . VAL A 46 ? 0.0948 0.0966 0.1121 0.0047 0.0032 0.0151 132 VAL A CG1 366 C CG2 . VAL A 46 ? 0.1132 0.1025 0.1165 -0.0017 0.0072 0.0035 132 VAL A CG2 367 N N . PRO A 47 ? 0.0881 0.0850 0.0821 -0.0009 -0.0015 0.0063 133 PRO A N 368 C CA . PRO A 47 ? 0.0945 0.0898 0.0880 0.0012 0.0032 0.0035 133 PRO A CA 369 C C . PRO A 47 ? 0.0903 0.0793 0.0817 -0.0032 -0.0017 -0.0019 133 PRO A C 370 O O . PRO A 47 ? 0.1121 0.0965 0.1047 -0.0024 -0.0102 0.0087 133 PRO A O 371 C CB . PRO A 47 ? 0.1025 0.0959 0.0879 0.0015 0.0038 0.0065 133 PRO A CB 372 C CG . PRO A 47 ? 0.1012 0.1069 0.0962 0.0010 -0.0023 0.0040 133 PRO A CG 373 C CD . PRO A 47 ? 0.0917 0.0920 0.0941 0.0054 -0.0056 0.0039 133 PRO A CD 374 N N . SER A 48 ? 0.0965 0.0844 0.0828 -0.0009 -0.0016 0.0072 134 SER A N 375 C CA . SER A 48 ? 0.0931 0.0706 0.0725 0.0007 -0.0039 0.0047 134 SER A CA 376 C C . SER A 48 ? 0.0883 0.0763 0.0794 0.0018 -0.0012 0.0009 134 SER A C 377 O O . SER A 48 ? 0.0989 0.0829 0.0831 0.0065 -0.0014 0.0023 134 SER A O 378 C CB . SER A 48 ? 0.0993 0.0887 0.0807 -0.0053 0.0033 0.0021 134 SER A CB 379 O OG . SER A 48 ? 0.0995 0.0912 0.0881 -0.0026 -0.0015 -0.0059 134 SER A OG 380 N N . PHE A 49 ? 0.0929 0.0735 0.0747 0.0023 0.0057 -0.0020 135 PHE A N 381 C CA . PHE A 49 ? 0.0830 0.0769 0.0756 0.0097 -0.0006 0.0034 135 PHE A CA 382 C C . PHE A 49 ? 0.0882 0.0754 0.0742 0.0010 -0.0003 0.0030 135 PHE A C 383 O O . PHE A 49 ? 0.0864 0.0857 0.0864 0.0047 -0.0036 0.0012 135 PHE A O 384 C CB . PHE A 49 ? 0.0845 0.0748 0.0802 0.0045 -0.0049 -0.0036 135 PHE A CB 385 C CG . PHE A 49 ? 0.0797 0.0736 0.0786 0.0098 -0.0030 0.0019 135 PHE A CG 386 C CD1 . PHE A 49 ? 0.0785 0.0709 0.0652 0.0067 -0.0002 -0.0015 135 PHE A CD1 387 C CD2 . PHE A 49 ? 0.0840 0.0768 0.0676 0.0012 -0.0083 0.0000 135 PHE A CD2 388 C CE1 . PHE A 49 ? 0.0900 0.0733 0.0758 0.0009 -0.0023 -0.0009 135 PHE A CE1 389 C CE2 . PHE A 49 ? 0.0880 0.0787 0.0794 0.0060 0.0069 0.0057 135 PHE A CE2 390 C CZ . PHE A 49 ? 0.0859 0.0792 0.0892 0.0019 -0.0044 -0.0022 135 PHE A CZ 391 N N . GLN A 50 ? 0.0879 0.0797 0.0834 -0.0042 0.0007 0.0004 136 GLN A N 392 C CA . GLN A 50 ? 0.0996 0.0903 0.0870 -0.0134 0.0032 -0.0072 136 GLN A CA 393 C C . GLN A 50 ? 0.0835 0.0842 0.0839 -0.0074 0.0000 -0.0051 136 GLN A C 394 O O . GLN A 50 ? 0.0928 0.0981 0.0962 -0.0117 0.0046 0.0096 136 GLN A O 395 C CB A GLN A 50 ? 0.1381 0.0930 0.0966 -0.0154 0.0018 0.0029 136 GLN A CB 396 C CB B GLN A 50 ? 0.1357 0.0872 0.0864 -0.0138 0.0019 0.0013 136 GLN A CB 397 C CG A GLN A 50 ? 0.1510 0.1128 0.1245 -0.0142 -0.0034 0.0031 136 GLN A CG 398 C CG B GLN A 50 ? 0.1438 0.1249 0.1398 -0.0184 -0.0052 -0.0078 136 GLN A CG 399 C CD A GLN A 50 ? 0.1385 0.1073 0.1618 -0.0106 -0.0033 0.0005 136 GLN A CD 400 C CD B GLN A 50 ? 0.1847 0.1394 0.1655 -0.0090 -0.0023 -0.0042 136 GLN A CD 401 O OE1 A GLN A 50 ? 0.1735 0.1611 0.2040 0.0019 0.0094 -0.0229 136 GLN A OE1 402 O OE1 B GLN A 50 ? 0.1912 0.1498 0.1486 0.0179 -0.0038 -0.0041 136 GLN A OE1 403 N NE2 A GLN A 50 ? 0.1476 0.1409 0.1433 0.0116 0.0205 0.0182 136 GLN A NE2 404 N NE2 B GLN A 50 ? 0.1450 0.0836 0.1286 -0.0043 0.0040 0.0000 136 GLN A NE2 405 N N . TRP A 51 ? 0.0897 0.1027 0.0834 -0.0115 0.0092 -0.0028 137 TRP A N 406 C CA . TRP A 51 ? 0.0886 0.1002 0.0841 -0.0099 0.0065 -0.0030 137 TRP A CA 407 C C . TRP A 51 ? 0.0785 0.0893 0.0897 -0.0183 -0.0023 -0.0008 137 TRP A C 408 O O . TRP A 51 ? 0.1120 0.1040 0.1022 -0.0273 0.0086 -0.0060 137 TRP A O 409 C CB . TRP A 51 ? 0.0980 0.1051 0.0975 0.0001 0.0006 -0.0051 137 TRP A CB 410 C CG . TRP A 51 ? 0.0941 0.1130 0.0879 -0.0047 0.0013 -0.0120 137 TRP A CG 411 C CD1 . TRP A 51 ? 0.0971 0.0917 0.0910 -0.0033 0.0042 -0.0039 137 TRP A CD1 412 C CD2 . TRP A 51 ? 0.0888 0.1070 0.0795 -0.0031 -0.0012 -0.0085 137 TRP A CD2 413 N NE1 . TRP A 51 ? 0.0964 0.1053 0.0900 0.0006 0.0016 -0.0115 137 TRP A NE1 414 C CE2 . TRP A 51 ? 0.0837 0.1062 0.0881 -0.0009 -0.0027 -0.0071 137 TRP A CE2 415 C CE3 . TRP A 51 ? 0.1015 0.1138 0.0963 0.0049 -0.0070 -0.0158 137 TRP A CE3 416 C CZ2 . TRP A 51 ? 0.0968 0.1173 0.0909 -0.0036 0.0059 -0.0128 137 TRP A CZ2 417 C CZ3 . TRP A 51 ? 0.1129 0.1242 0.1111 -0.0017 -0.0071 -0.0137 137 TRP A CZ3 418 C CH2 . TRP A 51 ? 0.0950 0.1147 0.1018 -0.0002 0.0071 -0.0112 137 TRP A CH2 419 N N . LEU A 52 ? 0.0808 0.0877 0.0870 -0.0102 0.0012 -0.0083 138 LEU A N 420 C CA . LEU A 52 ? 0.0869 0.0898 0.0758 -0.0014 0.0042 -0.0068 138 LEU A CA 421 C C . LEU A 52 ? 0.0834 0.0820 0.0786 0.0004 0.0057 -0.0020 138 LEU A C 422 O O . LEU A 52 ? 0.1012 0.1095 0.0997 0.0129 0.0077 0.0102 138 LEU A O 423 C CB . LEU A 52 ? 0.0856 0.0927 0.0833 -0.0007 0.0007 -0.0053 138 LEU A CB 424 C CG . LEU A 52 ? 0.0962 0.0958 0.1019 0.0024 -0.0022 -0.0117 138 LEU A CG 425 C CD1 . LEU A 52 ? 0.0936 0.1166 0.1064 0.0132 -0.0058 -0.0199 138 LEU A CD1 426 C CD2 . LEU A 52 ? 0.1100 0.1119 0.1162 0.0145 -0.0142 -0.0082 138 LEU A CD2 427 N N . ASP A 53 ? 0.0849 0.0926 0.0850 -0.0002 0.0024 0.0013 139 ASP A N 428 C CA . ASP A 53 ? 0.0913 0.0954 0.0816 -0.0013 0.0087 -0.0063 139 ASP A CA 429 C C . ASP A 53 ? 0.0917 0.0852 0.0911 0.0029 -0.0065 -0.0017 139 ASP A C 430 O O . ASP A 53 ? 0.1112 0.1107 0.1172 0.0073 -0.0233 -0.0064 139 ASP A O 431 C CB . ASP A 53 ? 0.1069 0.1075 0.1055 0.0160 -0.0016 -0.0071 139 ASP A CB 432 C CG . ASP A 53 ? 0.1055 0.1569 0.1479 0.0326 0.0360 0.0049 139 ASP A CG 433 O OD1 . ASP A 53 ? 0.1404 0.1582 0.1871 -0.0097 0.0445 0.0323 139 ASP A OD1 434 O OD2 . ASP A 53 ? 0.1925 0.2924 0.3461 0.0385 0.0748 0.0266 139 ASP A OD2 435 N N . ARG A 54 ? 0.0948 0.1041 0.0972 0.0048 -0.0036 -0.0109 140 ARG A N 436 C CA . ARG A 54 ? 0.1131 0.1199 0.1226 -0.0012 -0.0026 -0.0231 140 ARG A CA 437 C C . ARG A 54 ? 0.0899 0.1007 0.1038 0.0040 -0.0037 -0.0124 140 ARG A C 438 O O . ARG A 54 ? 0.1124 0.1111 0.1069 0.0087 -0.0065 -0.0170 140 ARG A O 439 C CB . ARG A 54 ? 0.1130 0.1614 0.1612 0.0043 0.0124 -0.0421 140 ARG A CB 440 C CG . ARG A 54 ? 0.1700 0.2195 0.2498 0.0036 0.0135 -0.0342 140 ARG A CG 441 C CD . ARG A 54 ? 0.2817 0.3053 0.3176 -0.0071 0.0373 0.0009 140 ARG A CD 442 N NE . ARG A 54 ? 0.3308 0.3894 0.3399 0.0003 0.0099 -0.0107 140 ARG A NE 443 C CZ . ARG A 54 ? 0.4011 0.4168 0.4143 0.0100 0.0172 0.0110 140 ARG A CZ 444 N NH1 . ARG A 54 ? 0.4466 0.4638 0.4307 0.0083 0.0078 -0.0084 140 ARG A NH1 445 N NH2 . ARG A 54 ? 0.4573 0.5086 0.4630 0.0073 -0.0077 0.0066 140 ARG A NH2 446 N N . ASN A 55 ? 0.0931 0.0985 0.1057 0.0025 -0.0053 -0.0133 141 ASN A N 447 C CA . ASN A 55 ? 0.0936 0.1046 0.1019 0.0030 -0.0055 -0.0111 141 ASN A CA 448 C C . ASN A 55 ? 0.0879 0.0986 0.0925 -0.0015 -0.0040 -0.0062 141 ASN A C 449 O O . ASN A 55 ? 0.0911 0.0948 0.1007 0.0027 -0.0043 -0.0070 141 ASN A O 450 C CB . ASN A 55 ? 0.1002 0.1041 0.1082 0.0036 -0.0039 -0.0094 141 ASN A CB 451 C CG . ASN A 55 ? 0.0971 0.1024 0.0925 0.0012 -0.0097 -0.0077 141 ASN A CG 452 O OD1 . ASN A 55 ? 0.0971 0.0996 0.1108 -0.0032 -0.0050 -0.0126 141 ASN A OD1 453 N ND2 . ASN A 55 ? 0.0904 0.0982 0.0968 -0.0060 -0.0037 -0.0062 141 ASN A ND2 454 N N . VAL A 56 ? 0.0935 0.1048 0.1081 -0.0016 -0.0004 -0.0133 142 VAL A N 455 C CA . VAL A 56 ? 0.0962 0.1116 0.1063 -0.0089 -0.0046 -0.0096 142 VAL A CA 456 C C . VAL A 56 ? 0.0948 0.1129 0.1118 -0.0036 -0.0011 -0.0071 142 VAL A C 457 O O . VAL A 56 ? 0.1174 0.1139 0.1169 -0.0013 -0.0043 -0.0063 142 VAL A O 458 C CB A VAL A 56 ? 0.1120 0.1289 0.1278 -0.0149 0.0041 -0.0122 142 VAL A CB 459 C CB B VAL A 56 ? 0.1098 0.1351 0.1204 -0.0227 0.0023 -0.0130 142 VAL A CB 460 C CG1 A VAL A 56 ? 0.1023 0.1068 0.1347 -0.0145 0.0000 -0.0184 142 VAL A CG1 461 C CG1 B VAL A 56 ? 0.0973 0.1282 0.1423 -0.0138 0.0048 -0.0085 142 VAL A CG1 462 C CG2 A VAL A 56 ? 0.1053 0.1310 0.1490 -0.0188 0.0044 -0.0057 142 VAL A CG2 463 C CG2 B VAL A 56 ? 0.1379 0.1555 0.1483 -0.0025 0.0026 0.0019 142 VAL A CG2 464 N N . THR A 57 ? 0.0899 0.1011 0.0964 -0.0053 -0.0034 -0.0023 143 THR A N 465 C CA . THR A 57 ? 0.0947 0.0995 0.0962 -0.0086 -0.0016 -0.0075 143 THR A CA 466 C C . THR A 57 ? 0.0938 0.0990 0.0984 -0.0046 -0.0048 -0.0021 143 THR A C 467 O O . THR A 57 ? 0.1085 0.1160 0.1038 -0.0122 0.0020 0.0106 143 THR A O 468 C CB . THR A 57 ? 0.1055 0.1073 0.0988 -0.0013 0.0036 -0.0142 143 THR A CB 469 O OG1 . THR A 57 ? 0.1085 0.1060 0.1124 -0.0076 -0.0023 -0.0095 143 THR A OG1 470 C CG2 . THR A 57 ? 0.1259 0.1319 0.1241 -0.0018 0.0074 -0.0141 143 THR A CG2 471 N N . VAL A 58 ? 0.0857 0.0951 0.0910 -0.0102 -0.0006 -0.0057 144 VAL A N 472 C CA . VAL A 58 ? 0.0782 0.0923 0.0921 -0.0015 -0.0003 -0.0038 144 VAL A CA 473 C C . VAL A 58 ? 0.0851 0.0980 0.0907 -0.0060 -0.0066 -0.0019 144 VAL A C 474 O O . VAL A 58 ? 0.1055 0.0990 0.1100 -0.0059 -0.0140 -0.0063 144 VAL A O 475 C CB . VAL A 58 ? 0.0871 0.0915 0.0936 -0.0029 -0.0005 -0.0024 144 VAL A CB 476 C CG1 . VAL A 58 ? 0.0911 0.0929 0.0974 -0.0049 -0.0028 0.0056 144 VAL A CG1 477 C CG2 . VAL A 58 ? 0.0872 0.1054 0.1077 -0.0063 0.0009 -0.0079 144 VAL A CG2 478 N N . ASP A 59 ? 0.0917 0.0878 0.0952 -0.0037 -0.0045 -0.0042 145 ASP A N 479 C CA . ASP A 59 ? 0.0996 0.0944 0.0986 -0.0122 -0.0062 -0.0036 145 ASP A CA 480 C C . ASP A 59 ? 0.1239 0.1059 0.1154 -0.0067 -0.0004 -0.0067 145 ASP A C 481 O O . ASP A 59 ? 0.1713 0.1270 0.1450 -0.0008 0.0227 0.0055 145 ASP A O 482 C CB . ASP A 59 ? 0.1019 0.0942 0.1005 -0.0046 0.0036 -0.0044 145 ASP A CB 483 C CG . ASP A 59 ? 0.0936 0.1053 0.1040 0.0033 -0.0073 0.0042 145 ASP A CG 484 O OD1 . ASP A 59 ? 0.1307 0.1395 0.1432 0.0086 0.0112 0.0163 145 ASP A OD1 485 O OD2 . ASP A 59 ? 0.1035 0.1129 0.1214 0.0104 0.0063 0.0091 145 ASP A OD2 486 N N . THR A 60 ? 0.1153 0.1064 0.1041 -0.0159 0.0044 -0.0017 146 THR A N 487 C CA . THR A 60 ? 0.1066 0.1098 0.1089 -0.0109 0.0026 0.0034 146 THR A CA 488 C C . THR A 60 ? 0.1116 0.1152 0.1140 -0.0168 0.0032 0.0021 146 THR A C 489 O O . THR A 60 ? 0.1367 0.1282 0.1236 -0.0028 0.0005 0.0010 146 THR A O 490 C CB . THR A 60 ? 0.1242 0.1342 0.1163 -0.0177 0.0012 0.0076 146 THR A CB 491 O OG1 . THR A 60 ? 0.1163 0.1300 0.1315 -0.0171 0.0027 0.0010 146 THR A OG1 492 C CG2 . THR A 60 ? 0.1377 0.1404 0.1475 -0.0173 -0.0136 0.0025 146 THR A CG2 493 N N . LEU A 61 ? 0.1077 0.1145 0.1066 -0.0083 0.0041 0.0065 147 LEU A N 494 C CA . LEU A 61 ? 0.1194 0.1202 0.1085 0.0009 0.0038 -0.0012 147 LEU A CA 495 C C . LEU A 61 ? 0.1087 0.1070 0.1036 0.0061 -0.0036 -0.0065 147 LEU A C 496 O O . LEU A 61 ? 0.1189 0.1053 0.1093 0.0093 -0.0001 0.0009 147 LEU A O 497 C CB . LEU A 61 ? 0.1227 0.1519 0.1225 0.0104 0.0073 -0.0060 147 LEU A CB 498 C CG . LEU A 61 ? 0.1439 0.1769 0.1422 0.0110 -0.0004 -0.0010 147 LEU A CG 499 C CD1 . LEU A 61 ? 0.1856 0.1896 0.1740 0.0214 0.0116 0.0193 147 LEU A CD1 500 C CD2 . LEU A 61 ? 0.1532 0.2001 0.2212 -0.0179 0.0299 0.0017 147 LEU A CD2 501 N N . LEU A 62 ? 0.1068 0.1009 0.0947 -0.0016 -0.0048 -0.0022 148 LEU A N 502 C CA . LEU A 62 ? 0.1001 0.0961 0.0980 0.0015 -0.0071 -0.0126 148 LEU A CA 503 C C . LEU A 62 ? 0.0996 0.0965 0.1031 -0.0005 -0.0034 -0.0004 148 LEU A C 504 O O . LEU A 62 ? 0.1055 0.0975 0.0977 0.0003 -0.0052 0.0025 148 LEU A O 505 C CB . LEU A 62 ? 0.0975 0.0905 0.0855 0.0041 -0.0087 -0.0048 148 LEU A CB 506 C CG . LEU A 62 ? 0.0978 0.0928 0.0954 0.0105 -0.0042 0.0006 148 LEU A CG 507 C CD1 . LEU A 62 ? 0.0941 0.1025 0.0950 0.0044 -0.0025 -0.0042 148 LEU A CD1 508 C CD2 . LEU A 62 ? 0.1082 0.1043 0.1016 0.0096 0.0017 -0.0020 148 LEU A CD2 509 N N . VAL A 63 ? 0.1063 0.0974 0.1068 0.0029 -0.0091 -0.0010 149 VAL A N 510 C CA . VAL A 63 ? 0.0960 0.0992 0.1153 0.0039 -0.0058 -0.0033 149 VAL A CA 511 C C . VAL A 63 ? 0.1102 0.1001 0.1148 0.0032 -0.0053 -0.0019 149 VAL A C 512 O O . VAL A 63 ? 0.1155 0.1050 0.1153 0.0059 -0.0019 0.0000 149 VAL A O 513 C CB . VAL A 63 ? 0.1229 0.1085 0.1161 0.0093 -0.0056 -0.0065 149 VAL A CB 514 C CG1 . VAL A 63 ? 0.1525 0.1285 0.1257 0.0081 0.0062 -0.0112 149 VAL A CG1 515 C CG2 . VAL A 63 ? 0.1295 0.1142 0.1313 0.0127 -0.0007 -0.0126 149 VAL A CG2 516 N N . GLN A 64 ? 0.1184 0.1069 0.1082 -0.0036 -0.0024 0.0059 150 GLN A N 517 C CA . GLN A 64 ? 0.1273 0.1078 0.1279 -0.0141 -0.0041 0.0104 150 GLN A CA 518 C C . GLN A 64 ? 0.1092 0.1095 0.1106 0.0029 0.0072 0.0075 150 GLN A C 519 O O . GLN A 64 ? 0.1346 0.1244 0.1256 -0.0058 -0.0038 0.0120 150 GLN A O 520 C CB A GLN A 64 ? 0.1588 0.1568 0.1427 -0.0207 0.0033 0.0258 150 GLN A CB 521 C CB B GLN A 64 ? 0.1365 0.1303 0.1206 -0.0184 0.0010 0.0177 150 GLN A CB 522 C CG A GLN A 64 ? 0.2140 0.1841 0.2033 -0.0128 0.0032 0.0114 150 GLN A CG 523 C CG B GLN A 64 ? 0.1162 0.1397 0.1153 -0.0221 0.0098 0.0212 150 GLN A CG 524 C CD A GLN A 64 ? 0.2448 0.2195 0.2430 -0.0030 -0.0111 0.0110 150 GLN A CD 525 C CD B GLN A 64 ? 0.2093 0.1922 0.2052 0.0002 0.0023 0.0054 150 GLN A CD 526 O OE1 A GLN A 64 ? 0.2799 0.2876 0.2829 -0.0367 -0.0148 -0.0122 150 GLN A OE1 527 O OE1 B GLN A 64 ? 0.2691 0.2363 0.2314 -0.0078 -0.0059 -0.0022 150 GLN A OE1 528 N NE2 A GLN A 64 ? 0.2247 0.2294 0.2492 -0.0179 0.0044 0.0060 150 GLN A NE2 529 N NE2 B GLN A 64 ? 0.2327 0.2142 0.2006 -0.0063 -0.0148 0.0108 150 GLN A NE2 530 N N . THR A 65 ? 0.1105 0.1041 0.1014 0.0019 0.0039 0.0064 151 THR A N 531 C CA . THR A 65 ? 0.1168 0.1037 0.1015 0.0070 0.0064 0.0025 151 THR A CA 532 C C . THR A 65 ? 0.1036 0.0963 0.0915 0.0053 0.0030 0.0028 151 THR A C 533 O O . THR A 65 ? 0.1154 0.1016 0.1006 0.0040 0.0005 0.0039 151 THR A O 534 C CB . THR A 65 ? 0.1201 0.1145 0.1191 0.0083 0.0082 -0.0052 151 THR A CB 535 O OG1 . THR A 65 ? 0.1496 0.1552 0.1814 0.0068 0.0011 -0.0442 151 THR A OG1 536 C CG2 . THR A 65 ? 0.1378 0.1291 0.1307 0.0162 -0.0067 -0.0060 151 THR A CG2 537 N N . LEU A 66 ? 0.1016 0.0998 0.0850 0.0025 0.0003 0.0063 152 LEU A N 538 C CA . LEU A 66 ? 0.1074 0.0874 0.0907 0.0086 -0.0045 0.0064 152 LEU A CA 540 O O . LEU A 66 ? 0.1167 0.1009 0.1060 0.0091 0.0018 0.0085 152 LEU A O 541 C CB . LEU A 66 ? 0.1037 0.0942 0.0908 0.0043 0.0068 0.0040 152 LEU A CB 542 C CG . LEU A 66 ? 0.0943 0.0811 0.0934 0.0063 0.0021 -0.0043 152 LEU A CG 543 C CD1 . LEU A 66 ? 0.1054 0.0976 0.1078 0.0111 0.0043 0.0028 152 LEU A CD1 544 C CD2 . LEU A 66 ? 0.1457 0.1178 0.1206 0.0052 -0.0097 0.0034 152 LEU A CD2 545 N N . SER A 67 ? 0.1127 0.0949 0.1059 0.0128 -0.0066 0.0090 153 SER A N 546 C CA . SER A 67 ? 0.1337 0.1012 0.1142 0.0101 -0.0015 0.0038 153 SER A CA 547 C C . SER A 67 ? 0.1311 0.0976 0.1210 0.0103 -0.0066 0.0045 153 SER A C 548 O O . SER A 67 ? 0.1343 0.1042 0.1164 0.0084 -0.0039 0.0045 153 SER A O 549 C CB . SER A 67 ? 0.1760 0.1086 0.1269 0.0171 -0.0095 0.0027 153 SER A CB 550 O OG . SER A 67 ? 0.1845 0.1543 0.1598 0.0013 -0.0005 -0.0032 153 SER A OG 551 N N . GLU A 68 ? 0.1222 0.0959 0.1138 0.0063 -0.0034 0.0123 154 GLU A N 552 C CA . GLU A 68 ? 0.1336 0.0985 0.1197 0.0032 0.0015 0.0095 154 GLU A CA 553 C C . GLU A 68 ? 0.1379 0.1132 0.1103 0.0083 0.0010 0.0112 154 GLU A C 554 O O . GLU A 68 ? 0.1370 0.1069 0.1183 0.0067 -0.0081 0.0119 154 GLU A O 555 C CB . GLU A 68 ? 0.1284 0.1089 0.1119 0.0032 -0.0046 0.0024 154 GLU A CB 556 C CG . GLU A 68 ? 0.1442 0.1003 0.1337 0.0059 0.0115 0.0015 154 GLU A CG 557 C CD . GLU A 68 ? 0.1563 0.1453 0.1575 -0.0091 -0.0061 -0.0205 154 GLU A CD 558 O OE1 . GLU A 68 ? 0.1672 0.1475 0.1895 0.0149 0.0228 -0.0130 154 GLU A OE1 559 O OE2 . GLU A 68 ? 0.1695 0.1928 0.2478 -0.0145 0.0043 -0.0127 154 GLU A OE2 560 N N . ILE A 69 ? 0.1148 0.0921 0.1012 0.0058 0.0051 0.0088 155 ILE A N 561 C CA . ILE A 69 ? 0.1285 0.0891 0.0991 0.0031 -0.0026 0.0090 155 ILE A CA 562 C C . ILE A 69 ? 0.1121 0.1007 0.0986 0.0064 -0.0066 -0.0017 155 ILE A C 563 O O . ILE A 69 ? 0.1280 0.0982 0.1072 0.0116 0.0013 0.0079 155 ILE A O 564 C CB . ILE A 69 ? 0.1168 0.0922 0.0887 0.0033 0.0023 0.0086 155 ILE A CB 565 C CG1 . ILE A 69 ? 0.1206 0.0974 0.0939 0.0072 -0.0036 0.0024 155 ILE A CG1 566 C CG2 . ILE A 69 ? 0.1232 0.1071 0.0946 0.0162 0.0053 0.0059 155 ILE A CG2 567 C CD1 . ILE A 69 ? 0.1068 0.0972 0.1135 0.0104 -0.0035 0.0075 155 ILE A CD1 568 N N . ARG A 70 ? 0.1237 0.0955 0.1017 0.0168 -0.0086 0.0094 156 ARG A N 569 C CA . ARG A 70 ? 0.1204 0.0971 0.1006 0.0073 -0.0031 0.0113 156 ARG A CA 570 C C . ARG A 70 ? 0.1307 0.1097 0.1149 0.0137 -0.0026 -0.0043 156 ARG A C 571 O O . ARG A 70 ? 0.1411 0.1152 0.1151 0.0175 -0.0096 0.0039 156 ARG A O 572 C CB . ARG A 70 ? 0.1423 0.1136 0.1132 0.0139 -0.0043 -0.0018 156 ARG A CB 573 C CG . ARG A 70 ? 0.1351 0.0962 0.1066 0.0062 -0.0028 0.0126 156 ARG A CG 574 C CD . ARG A 70 ? 0.1439 0.1018 0.1336 0.0041 0.0091 0.0016 156 ARG A CD 575 N NE . ARG A 70 ? 0.1383 0.1083 0.1084 0.0082 0.0083 0.0037 156 ARG A NE 576 C CZ . ARG A 70 ? 0.1358 0.1084 0.1142 -0.0038 0.0067 -0.0074 156 ARG A CZ 577 N NH1 . ARG A 70 ? 0.1745 0.1445 0.1328 -0.0226 0.0016 0.0154 156 ARG A NH1 578 N NH2 . ARG A 70 ? 0.1262 0.1147 0.1148 -0.0008 0.0026 0.0012 156 ARG A NH2 579 N N . GLU A 71 ? 0.1280 0.1050 0.1097 0.0162 -0.0061 0.0125 157 GLU A N 580 C CA . GLU A 71 ? 0.1502 0.1131 0.1245 0.0157 0.0014 0.0097 157 GLU A CA 581 C C . GLU A 71 ? 0.1403 0.1117 0.1218 0.0167 -0.0128 0.0054 157 GLU A C 582 O O . GLU A 71 ? 0.1611 0.1165 0.1278 0.0250 -0.0119 0.0118 157 GLU A O 583 C CB . GLU A 71 ? 0.1756 0.1145 0.1281 0.0123 -0.0039 0.0134 157 GLU A CB 584 C CG . GLU A 71 ? 0.1904 0.1691 0.1735 -0.0075 -0.0006 0.0310 157 GLU A CG 585 C CD . GLU A 71 ? 0.2108 0.1840 0.2374 -0.0026 -0.0085 0.0157 157 GLU A CD 586 O OE1 . GLU A 71 ? 0.2457 0.2153 0.2936 -0.0086 0.0138 -0.0028 157 GLU A OE1 587 O OE2 . GLU A 71 ? 0.2978 0.2335 0.3441 -0.0163 -0.0117 -0.0112 157 GLU A OE2 588 N N . ALA A 72 ? 0.1407 0.1160 0.1171 0.0145 -0.0058 0.0104 158 ALA A N 589 C CA . ALA A 72 ? 0.1497 0.1094 0.1169 0.0082 0.0034 0.0145 158 ALA A CA 590 C C . ALA A 72 ? 0.1481 0.1161 0.1110 0.0177 -0.0051 -0.0023 158 ALA A C 591 O O . ALA A 72 ? 0.1484 0.1221 0.1201 0.0227 -0.0137 0.0113 158 ALA A O 592 C CB . ALA A 72 ? 0.1529 0.1299 0.1219 0.0117 0.0082 0.0078 158 ALA A CB 593 N N . ASN A 73 ? 0.1447 0.1026 0.1109 0.0190 -0.0060 0.0093 159 ASN A N 594 C CA . ASN A 73 ? 0.1396 0.0970 0.1052 0.0234 -0.0106 0.0073 159 ASN A CA 595 C C . ASN A 73 ? 0.1306 0.1294 0.1227 0.0134 -0.0111 0.0051 159 ASN A C 596 O O . ASN A 73 ? 0.1494 0.1292 0.1347 0.0301 -0.0223 0.0045 159 ASN A O 597 C CB . ASN A 73 ? 0.1221 0.1109 0.1083 0.0265 -0.0015 0.0047 159 ASN A CB 598 C CG . ASN A 73 ? 0.1231 0.1054 0.0986 0.0106 -0.0039 0.0081 159 ASN A CG 599 O OD1 . ASN A 73 ? 0.1367 0.1130 0.1169 0.0170 0.0001 0.0036 159 ASN A OD1 600 N ND2 . ASN A 73 ? 0.1248 0.1115 0.1136 0.0136 -0.0052 0.0187 159 ASN A ND2 601 N N . GLN A 74 ? 0.1427 0.1098 0.1285 0.0346 -0.0120 0.0055 160 GLN A N 602 C CA . GLN A 74 ? 0.1485 0.1129 0.1427 0.0325 -0.0043 0.0038 160 GLN A CA 603 C C . GLN A 74 ? 0.1709 0.1374 0.1548 0.0403 -0.0173 0.0119 160 GLN A C 604 O O . GLN A 74 ? 0.1990 0.1540 0.1744 0.0657 -0.0066 0.0196 160 GLN A O 605 C CB . GLN A 74 ? 0.1620 0.1297 0.1410 0.0286 -0.0018 -0.0017 160 GLN A CB 606 C CG . GLN A 74 ? 0.1618 0.1327 0.1458 0.0122 -0.0025 -0.0001 160 GLN A CG 607 C CD . GLN A 74 ? 0.1374 0.1558 0.1393 0.0139 0.0064 0.0047 160 GLN A CD 608 O OE1 . GLN A 74 ? 0.2147 0.1920 0.1786 -0.0255 0.0182 -0.0249 160 GLN A OE1 609 N NE2 . GLN A 74 ? 0.1570 0.1796 0.1524 0.0207 0.0044 0.0000 160 GLN A NE2 610 N N . ALA A 75 ? 0.1788 0.1292 0.1281 0.0276 -0.0039 0.0205 161 ALA A N 611 C CA . ALA A 75 ? 0.1909 0.1344 0.1416 0.0210 -0.0100 0.0128 161 ALA A CA 612 C C . ALA A 75 ? 0.1730 0.1437 0.1346 0.0235 -0.0104 0.0061 161 ALA A C 613 O O . ALA A 75 ? 0.2054 0.1756 0.1563 0.0207 -0.0090 0.0086 161 ALA A O 614 C CB . ALA A 75 ? 0.2132 0.1437 0.1422 0.0100 0.0000 0.0161 161 ALA A CB 615 N N . GLY A 76 ? 0.1820 0.1520 0.1448 0.0245 -0.0185 0.0023 162 GLY A N 616 C CA . GLY A 76 ? 0.1814 0.1352 0.1457 0.0300 -0.0184 0.0126 162 GLY A CA 617 C C . GLY A 76 ? 0.1771 0.1492 0.1469 0.0294 -0.0227 -0.0002 162 GLY A C 618 O O . GLY A 76 ? 0.2094 0.1547 0.1425 0.0343 -0.0370 0.0131 162 GLY A O 619 N N . ALA A 77 ? 0.1736 0.1311 0.1342 0.0294 -0.0185 0.0115 163 ALA A N 620 C CA . ALA A 77 ? 0.1714 0.1368 0.1341 0.0253 -0.0007 0.0104 163 ALA A CA 621 C C . ALA A 77 ? 0.1648 0.1270 0.1258 0.0336 -0.0164 0.0187 163 ALA A C 622 O O . ALA A 77 ? 0.1766 0.1509 0.1695 0.0240 0.0018 0.0034 163 ALA A O 623 C CB . ALA A 77 ? 0.1623 0.1370 0.1458 0.0331 -0.0018 0.0143 163 ALA A CB 624 N N . ASN A 78 ? 0.1881 0.1405 0.1515 0.0251 -0.0141 0.0123 164 ASN A N 625 C CA . ASN A 78 ? 0.1841 0.1648 0.1723 0.0244 -0.0170 0.0121 164 ASN A CA 626 C C . ASN A 78 ? 0.1948 0.1803 0.1661 0.0115 -0.0080 -0.0058 164 ASN A C 627 O O . ASN A 78 ? 0.2538 0.2117 0.1761 0.0107 -0.0107 -0.0055 164 ASN A O 628 C CB . ASN A 78 ? 0.2069 0.1772 0.2084 0.0265 -0.0288 0.0162 164 ASN A CB 629 C CG . ASN A 78 ? 0.2525 0.2826 0.2758 -0.0016 -0.0352 0.0110 164 ASN A CG 630 O OD1 . ASN A 78 ? 0.3676 0.3871 0.4081 0.0249 -0.0653 0.0340 164 ASN A OD1 631 N ND2 . ASN A 78 ? 0.2204 0.2877 0.3014 0.0119 -0.0588 0.0082 164 ASN A ND2 632 N N . PRO A 79 ? 0.1834 0.1512 0.1651 0.0191 -0.0278 -0.0099 165 PRO A N 633 C CA . PRO A 79 ? 0.1655 0.1513 0.1648 0.0156 -0.0230 0.0058 165 PRO A CA 634 C C . PRO A 79 ? 0.1482 0.1288 0.1384 0.0201 -0.0283 0.0111 165 PRO A C 635 O O . PRO A 79 ? 0.1540 0.1359 0.1262 0.0177 -0.0169 0.0070 165 PRO A O 636 C CB . PRO A 79 ? 0.2199 0.1999 0.1806 -0.0176 -0.0421 0.0168 165 PRO A CB 637 C CG . PRO A 79 ? 0.2266 0.2230 0.2659 0.0153 -0.0064 0.0244 165 PRO A CG 638 C CD . PRO A 79 ? 0.2061 0.1753 0.1848 0.0246 -0.0142 -0.0208 165 PRO A CD 639 N N . GLN A 80 ? 0.1217 0.1244 0.1525 0.0194 -0.0131 0.0015 166 GLN A N 640 C CA . GLN A 80 ? 0.1352 0.1243 0.1322 0.0234 -0.0108 -0.0053 166 GLN A CA 641 C C . GLN A 80 ? 0.1178 0.1024 0.1091 0.0230 -0.0004 0.0105 166 GLN A C 642 O O . GLN A 80 ? 0.1286 0.1040 0.1171 0.0165 -0.0080 0.0004 166 GLN A O 643 C CB . GLN A 80 ? 0.1492 0.2031 0.1704 0.0301 0.0097 -0.0194 166 GLN A CB 644 C CG . GLN A 80 ? 0.2473 0.2354 0.2599 0.0007 0.0170 0.0035 166 GLN A CG 645 C CD . GLN A 80 ? 0.2906 0.2441 0.2578 0.0314 0.0040 0.0168 166 GLN A CD 646 O OE1 . GLN A 80 ? 0.2446 0.3170 0.2308 0.0489 0.0169 0.0674 166 GLN A OE1 647 N NE2 . GLN A 80 ? 0.3007 0.2483 0.2489 0.0464 0.0149 0.0068 166 GLN A NE2 648 N N . TYR A 81 ? 0.1199 0.0931 0.1058 0.0171 -0.0034 0.0046 167 TYR A N 649 C CA . TYR A 81 ? 0.1126 0.1015 0.0987 0.0211 -0.0042 0.0032 167 TYR A CA 650 C C . TYR A 81 ? 0.1050 0.0958 0.0796 0.0179 0.0093 -0.0111 167 TYR A C 651 O O . TYR A 81 ? 0.1110 0.1006 0.1114 0.0087 -0.0086 0.0168 167 TYR A O 652 C CB . TYR A 81 ? 0.1135 0.1012 0.0986 0.0158 -0.0086 0.0074 167 TYR A CB 653 C CG . TYR A 81 ? 0.1178 0.0929 0.1158 0.0061 -0.0002 0.0142 167 TYR A CG 654 C CD1 . TYR A 81 ? 0.1217 0.1079 0.1107 0.0052 0.0043 0.0057 167 TYR A CD1 655 C CD2 . TYR A 81 ? 0.1374 0.1148 0.1197 0.0131 -0.0047 0.0081 167 TYR A CD2 656 C CE1 . TYR A 81 ? 0.1497 0.1255 0.1334 0.0066 -0.0086 0.0113 167 TYR A CE1 657 C CE2 . TYR A 81 ? 0.1460 0.1186 0.1431 0.0008 0.0084 0.0300 167 TYR A CE2 658 C CZ . TYR A 81 ? 0.1541 0.1474 0.1097 0.0157 0.0243 0.0119 167 TYR A CZ 659 O OH . TYR A 81 ? 0.1910 0.1630 0.1454 0.0150 0.0307 0.0169 167 TYR A OH 660 N N . ALA A 82 ? 0.1052 0.0842 0.0918 0.0195 -0.0002 0.0059 168 ALA A N 661 C CA . ALA A 82 ? 0.0951 0.0805 0.0898 0.0150 0.0022 0.0047 168 ALA A CA 662 C C . ALA A 82 ? 0.0856 0.0767 0.0819 0.0106 0.0042 -0.0054 168 ALA A C 663 O O . ALA A 82 ? 0.0977 0.0931 0.0911 0.0077 0.0016 0.0030 168 ALA A O 664 C CB . ALA A 82 ? 0.1002 0.0992 0.0912 0.0030 -0.0025 0.0002 168 ALA A CB 665 N N . ALA A 83 ? 0.0872 0.0786 0.0767 0.0116 0.0065 -0.0006 169 ALA A N 666 C CA . ALA A 83 ? 0.0887 0.0795 0.0811 0.0061 0.0030 0.0040 169 ALA A CA 667 C C . ALA A 83 ? 0.0843 0.0790 0.0813 0.0062 -0.0033 0.0046 169 ALA A C 668 O O . ALA A 83 ? 0.0836 0.0835 0.0908 0.0102 0.0049 0.0012 169 ALA A O 669 C CB . ALA A 83 ? 0.0979 0.0774 0.0898 0.0079 0.0004 -0.0021 169 ALA A CB 670 N N . GLN A 84 ? 0.0816 0.0716 0.0793 0.0020 -0.0038 0.0029 170 GLN A N 671 C CA . GLN A 84 ? 0.0831 0.0718 0.0799 0.0027 0.0018 0.0007 170 GLN A CA 672 C C . GLN A 84 ? 0.0787 0.0739 0.0809 0.0056 -0.0003 -0.0035 170 GLN A C 673 O O . GLN A 84 ? 0.0900 0.0799 0.0787 0.0060 0.0013 0.0004 170 GLN A O 674 C CB . GLN A 84 ? 0.0910 0.0826 0.0830 0.0105 -0.0087 0.0001 170 GLN A CB 675 C CG . GLN A 84 ? 0.0922 0.0935 0.0876 0.0142 -0.0007 0.0014 170 GLN A CG 676 C CD . GLN A 84 ? 0.0919 0.0818 0.0832 0.0032 -0.0064 -0.0020 170 GLN A CD 677 O OE1 . GLN A 84 ? 0.1024 0.0890 0.0898 0.0075 -0.0010 -0.0049 170 GLN A OE1 678 N NE2 . GLN A 84 ? 0.1031 0.0900 0.0903 0.0047 0.0044 0.0042 170 GLN A NE2 679 N N . ILE A 85 ? 0.0723 0.0736 0.0724 -0.0001 -0.0042 0.0006 171 ILE A N 680 C CA . ILE A 85 ? 0.0733 0.0767 0.0781 -0.0032 -0.0012 -0.0034 171 ILE A CA 681 C C . ILE A 85 ? 0.0700 0.0667 0.0623 -0.0018 0.0010 -0.0001 171 ILE A C 682 O O . ILE A 85 ? 0.0744 0.0763 0.0799 -0.0017 -0.0053 0.0041 171 ILE A O 683 C CB . ILE A 85 ? 0.0828 0.0774 0.0670 0.0014 -0.0015 -0.0062 171 ILE A CB 684 C CG1 . ILE A 85 ? 0.1266 0.0975 0.0921 0.0147 -0.0018 -0.0126 171 ILE A CG1 685 C CG2 . ILE A 85 ? 0.1098 0.1122 0.1002 0.0087 -0.0013 -0.0125 171 ILE A CG2 686 C CD1 . ILE A 85 ? 0.1646 0.1154 0.1156 0.0090 0.0139 -0.0076 171 ILE A CD1 687 N N . VAL A 86 ? 0.0729 0.0721 0.0746 -0.0045 0.0003 0.0062 172 VAL A N 688 C CA . VAL A 86 ? 0.0762 0.0722 0.0750 -0.0007 -0.0034 0.0036 172 VAL A CA 689 C C . VAL A 86 ? 0.0710 0.0686 0.0777 -0.0014 -0.0015 0.0033 172 VAL A C 690 O O . VAL A 86 ? 0.0809 0.0833 0.0827 -0.0116 -0.0049 0.0019 172 VAL A O 691 C CB . VAL A 86 ? 0.0735 0.0716 0.0754 -0.0035 -0.0036 0.0009 172 VAL A CB 692 C CG1 . VAL A 86 ? 0.0876 0.0849 0.0858 0.0120 -0.0036 -0.0088 172 VAL A CG1 693 C CG2 . VAL A 86 ? 0.0780 0.0887 0.0892 0.0047 -0.0047 0.0044 172 VAL A CG2 694 N N . VAL A 87 ? 0.0766 0.0722 0.0657 -0.0060 -0.0031 -0.0015 173 VAL A N 695 C CA . VAL A 87 ? 0.0876 0.0730 0.0686 -0.0019 -0.0035 -0.0038 173 VAL A CA 696 C C . VAL A 87 ? 0.0838 0.0751 0.0730 -0.0104 -0.0003 0.0001 173 VAL A C 697 O O . VAL A 87 ? 0.0832 0.0785 0.0882 0.0025 -0.0089 0.0002 173 VAL A O 698 C CB . VAL A 87 ? 0.0789 0.0678 0.0743 -0.0013 -0.0050 -0.0042 173 VAL A CB 699 C CG1 . VAL A 87 ? 0.0999 0.0930 0.0878 0.0025 -0.0020 -0.0033 173 VAL A CG1 700 C CG2 . VAL A 87 ? 0.0932 0.0940 0.0938 -0.0013 -0.0077 0.0048 173 VAL A CG2 701 N N . TYR A 88 ? 0.0812 0.0718 0.0797 -0.0031 -0.0040 0.0014 174 TYR A N 702 C CA . TYR A 88 ? 0.0798 0.0766 0.0753 -0.0015 -0.0089 -0.0024 174 TYR A CA 703 C C . TYR A 88 ? 0.0734 0.0807 0.0684 -0.0045 -0.0058 0.0002 174 TYR A C 704 O O . TYR A 88 ? 0.0892 0.0927 0.0863 -0.0080 -0.0086 -0.0005 174 TYR A O 705 C CB . TYR A 88 ? 0.0832 0.0850 0.0789 -0.0069 -0.0104 -0.0019 174 TYR A CB 706 C CG . TYR A 88 ? 0.0829 0.0822 0.0759 -0.0052 -0.0112 -0.0018 174 TYR A CG 707 C CD1 . TYR A 88 ? 0.0914 0.0958 0.0982 -0.0037 0.0057 0.0038 174 TYR A CD1 708 C CD2 . TYR A 88 ? 0.1077 0.0980 0.1002 0.0024 -0.0007 0.0034 174 TYR A CD2 709 C CE1 . TYR A 88 ? 0.0967 0.0951 0.1065 0.0000 -0.0028 0.0081 174 TYR A CE1 710 C CE2 . TYR A 88 ? 0.1041 0.1112 0.0952 0.0001 0.0046 0.0148 174 TYR A CE2 711 C CZ . TYR A 88 ? 0.0944 0.0970 0.1031 0.0092 -0.0018 -0.0008 174 TYR A CZ 712 O OH . TYR A 88 ? 0.1175 0.1209 0.1221 0.0136 0.0143 0.0126 174 TYR A OH 713 N N . ASP A 89 ? 0.0759 0.0830 0.0766 -0.0066 -0.0074 -0.0009 175 ASP A N 714 C CA . ASP A 89 ? 0.0817 0.0871 0.0835 -0.0030 -0.0050 -0.0036 175 ASP A CA 715 C C . ASP A 89 ? 0.0769 0.0980 0.0724 -0.0010 -0.0133 -0.0111 175 ASP A C 716 O O . ASP A 89 ? 0.0862 0.0981 0.0823 -0.0021 -0.0105 -0.0106 175 ASP A O 717 C CB . ASP A 89 ? 0.0826 0.0962 0.0958 -0.0044 -0.0018 -0.0037 175 ASP A CB 718 C CG . ASP A 89 ? 0.0951 0.0867 0.0828 0.0029 -0.0056 -0.0032 175 ASP A CG 719 O OD1 . ASP A 89 ? 0.0939 0.1007 0.1005 -0.0015 -0.0021 -0.0057 175 ASP A OD1 720 O OD2 . ASP A 89 ? 0.1017 0.1012 0.1108 0.0044 -0.0052 -0.0172 175 ASP A OD2 721 N N . LEU A 90 ? 0.0847 0.0886 0.0756 0.0012 -0.0114 -0.0011 176 LEU A N 722 C CA . LEU A 90 ? 0.0725 0.0832 0.0738 0.0007 -0.0064 -0.0044 176 LEU A CA 723 C C . LEU A 90 ? 0.0826 0.0818 0.0749 0.0045 -0.0051 0.0015 176 LEU A C 724 O O . LEU A 90 ? 0.0895 0.0945 0.0858 -0.0006 -0.0044 0.0011 176 LEU A O 725 C CB . LEU A 90 ? 0.0884 0.0883 0.0750 -0.0021 -0.0076 -0.0007 176 LEU A CB 726 C CG . LEU A 90 ? 0.0954 0.0889 0.0852 -0.0072 -0.0101 -0.0027 176 LEU A CG 727 C CD1 . LEU A 90 ? 0.1011 0.0924 0.0890 -0.0025 -0.0044 0.0020 176 LEU A CD1 728 C CD2 . LEU A 90 ? 0.0846 0.0993 0.0911 0.0000 -0.0115 -0.0039 176 LEU A CD2 729 N N . PRO A 91 ? 0.0798 0.0878 0.0804 0.0026 -0.0045 -0.0038 177 PRO A N 730 C CA . PRO A 91 ? 0.0772 0.0952 0.0774 -0.0027 -0.0041 -0.0018 177 PRO A CA 731 C C . PRO A 91 ? 0.0836 0.0950 0.0821 -0.0029 -0.0089 0.0049 177 PRO A C 732 O O . PRO A 91 ? 0.0945 0.0933 0.0991 0.0024 -0.0067 0.0009 177 PRO A O 733 C CB . PRO A 91 ? 0.1047 0.1022 0.0826 0.0076 -0.0101 -0.0032 177 PRO A CB 734 C CG . PRO A 91 ? 0.1041 0.1013 0.0763 0.0087 -0.0014 -0.0011 177 PRO A CG 735 C CD . PRO A 91 ? 0.0954 0.0898 0.0743 0.0043 -0.0034 -0.0060 177 PRO A CD 736 N N . ASP A 92 ? 0.0884 0.0962 0.0892 0.0028 -0.0088 -0.0038 178 ASP A N 737 C CA . ASP A 92 ? 0.0879 0.1003 0.0934 0.0015 -0.0069 0.0032 178 ASP A CA 738 C C . ASP A 92 ? 0.0832 0.0947 0.0966 0.0031 0.0002 0.0030 178 ASP A C 739 O O . ASP A 92 ? 0.1002 0.1058 0.1071 0.0041 -0.0063 -0.0018 178 ASP A O 740 C CB . ASP A 92 ? 0.1025 0.1053 0.0912 0.0074 -0.0134 -0.0037 178 ASP A CB 741 C CG . ASP A 92 ? 0.1297 0.1012 0.1040 0.0059 -0.0176 0.0172 178 ASP A CG 742 O OD1 . ASP A 92 ? 0.1247 0.1279 0.1162 0.0023 -0.0180 0.0013 178 ASP A OD1 743 O OD2 . ASP A 92 ? 0.1803 0.1464 0.1347 -0.0082 -0.0503 0.0165 178 ASP A OD2 744 N N . ARG A 93 ? 0.1023 0.0981 0.0971 -0.0044 0.0029 -0.0053 179 ARG A N 745 C CA . ARG A 93 ? 0.0971 0.0976 0.0914 -0.0035 0.0000 -0.0035 179 ARG A CA 746 C C . ARG A 93 ? 0.0824 0.1065 0.0970 -0.0019 -0.0028 0.0024 179 ARG A C 747 O O . ARG A 93 ? 0.0906 0.1131 0.1081 -0.0014 0.0023 -0.0134 179 ARG A O 748 C CB . ARG A 93 ? 0.0889 0.0976 0.1019 -0.0017 0.0013 -0.0021 179 ARG A CB 749 C CG . ARG A 93 ? 0.1015 0.1044 0.0962 -0.0043 0.0022 -0.0011 179 ARG A CG 750 C CD . ARG A 93 ? 0.0939 0.0938 0.0965 -0.0093 0.0005 -0.0110 179 ARG A CD 751 N NE . ARG A 93 ? 0.0920 0.0957 0.0932 0.0023 0.0022 -0.0018 179 ARG A NE 752 C CZ . ARG A 93 ? 0.0935 0.1037 0.0967 -0.0051 -0.0036 -0.0056 179 ARG A CZ 753 N NH1 . ARG A 93 ? 0.0941 0.0966 0.1057 -0.0062 -0.0008 0.0041 179 ARG A NH1 754 N NH2 . ARG A 93 ? 0.1083 0.1108 0.1240 0.0062 0.0068 0.0170 179 ARG A NH2 755 N N . ASP A 94 ? 0.0871 0.0997 0.0842 -0.0014 -0.0006 -0.0005 180 ASP A N 756 C CA . ASP A 94 ? 0.0825 0.0906 0.0886 0.0006 0.0044 0.0004 180 ASP A CA 757 C C . ASP A 94 ? 0.0887 0.1069 0.1002 0.0021 0.0040 0.0002 180 ASP A C 758 O O . ASP A 94 ? 0.0983 0.1161 0.1081 0.0054 0.0067 0.0037 180 ASP A O 759 C CB . ASP A 94 ? 0.0898 0.0985 0.0979 -0.0017 0.0132 0.0020 180 ASP A CB 760 C CG . ASP A 94 ? 0.1123 0.1145 0.1020 -0.0048 0.0182 0.0018 180 ASP A CG 761 O OD1 . ASP A 94 ? 0.1086 0.1061 0.1195 0.0078 0.0090 0.0041 180 ASP A OD1 762 O OD2 . ASP A 94 ? 0.1525 0.1213 0.1113 -0.0088 0.0237 0.0057 180 ASP A OD2 763 N N . CYS A 95 ? 0.0868 0.1068 0.1003 0.0013 0.0005 0.0119 181 CYS A N 764 C CA . CYS A 95 ? 0.0932 0.1059 0.1010 -0.0044 -0.0002 0.0049 181 CYS A CA 765 C C . CYS A 95 ? 0.0993 0.1101 0.1024 0.0006 -0.0026 0.0099 181 CYS A C 766 O O . CYS A 95 ? 0.1047 0.1223 0.1091 0.0091 -0.0005 -0.0005 181 CYS A O 767 C CB . CYS A 95 ? 0.0857 0.1159 0.1045 0.0034 0.0001 0.0149 181 CYS A CB 768 S SG . CYS A 95 ? 0.1098 0.1232 0.1072 -0.0020 -0.0027 0.0121 181 CYS A SG 769 N N . ALA A 96 ? 0.0848 0.1076 0.1009 0.0095 -0.0035 -0.0017 182 ALA A N 770 C CA . ALA A 96 ? 0.1119 0.1192 0.1228 0.0103 -0.0020 -0.0012 182 ALA A CA 771 C C . ALA A 96 ? 0.1124 0.1321 0.1218 0.0180 0.0062 -0.0115 182 ALA A C 772 O O . ALA A 96 ? 0.1403 0.1520 0.1538 0.0172 0.0222 -0.0147 182 ALA A O 773 C CB . ALA A 96 ? 0.1203 0.1274 0.1179 0.0045 0.0042 -0.0069 182 ALA A CB 774 N N . ALA A 97 ? 0.0973 0.1327 0.1094 0.0058 0.0111 -0.0064 183 ALA A N 775 C CA . ALA A 97 ? 0.1099 0.1472 0.1033 0.0021 0.0084 0.0007 183 ALA A CA 776 C C . ALA A 97 ? 0.1027 0.1294 0.1085 -0.0020 0.0109 0.0006 183 ALA A C 777 O O . ALA A 97 ? 0.1142 0.1751 0.1322 0.0026 -0.0035 0.0049 183 ALA A O 778 C CB . ALA A 97 ? 0.1108 0.1531 0.1198 0.0025 0.0152 0.0082 183 ALA A CB 779 N N . ALA A 98 ? 0.1014 0.1183 0.1109 0.0051 0.0015 0.0062 184 ALA A N 780 C CA . ALA A 98 ? 0.0997 0.1272 0.1219 0.0052 0.0039 0.0168 184 ALA A CA 781 C C . ALA A 98 ? 0.1045 0.1377 0.1149 0.0131 -0.0132 0.0056 184 ALA A C 782 O O . ALA A 98 ? 0.1378 0.1713 0.1481 0.0202 -0.0155 -0.0045 184 ALA A O 783 C CB . ALA A 98 ? 0.1037 0.1314 0.1415 0.0135 0.0046 0.0099 184 ALA A CB 784 N N . ALA A 99 ? 0.1204 0.1235 0.1302 0.0097 -0.0045 -0.0009 185 ALA A N 785 C CA . ALA A 99 ? 0.1222 0.1405 0.1259 0.0103 -0.0043 -0.0015 185 ALA A CA 786 C C . ALA A 99 ? 0.1322 0.1373 0.1293 0.0160 -0.0082 -0.0054 185 ALA A C 787 O O . ALA A 99 ? 0.1915 0.2224 0.1796 0.0685 -0.0152 -0.0158 185 ALA A O 788 C CB . ALA A 99 ? 0.1362 0.1460 0.1586 -0.0029 0.0053 -0.0170 185 ALA A CB 789 N N . SER A 100 ? 0.1234 0.1594 0.1358 0.0147 -0.0122 -0.0153 186 SER A N 790 C CA . SER A 100 ? 0.1269 0.1543 0.1469 0.0168 0.0058 -0.0027 186 SER A CA 791 C C . SER A 100 ? 0.1139 0.1508 0.1374 -0.0025 -0.0044 -0.0098 186 SER A C 792 O O . SER A 100 ? 0.1388 0.1642 0.1634 -0.0128 -0.0192 -0.0146 186 SER A O 793 C CB . SER A 100 ? 0.1318 0.1641 0.1692 0.0036 0.0173 -0.0132 186 SER A CB 794 O OG . SER A 100 ? 0.1219 0.1492 0.1872 0.0004 0.0212 -0.0102 186 SER A OG 795 N N . ASN A 101 ? 0.1302 0.1432 0.1329 0.0000 0.0079 -0.0025 187 ASN A N 796 C CA . ASN A 101 ? 0.1291 0.1545 0.1377 -0.0069 0.0102 0.0034 187 ASN A CA 797 C C . ASN A 101 ? 0.1212 0.1403 0.1428 0.0025 0.0022 -0.0045 187 ASN A C 798 O O . ASN A 101 ? 0.1592 0.1528 0.1819 -0.0101 0.0234 -0.0076 187 ASN A O 799 C CB . ASN A 101 ? 0.1407 0.1759 0.1604 0.0014 0.0125 -0.0014 187 ASN A CB 800 C CG . ASN A 101 ? 0.1820 0.1816 0.1871 -0.0113 0.0115 0.0081 187 ASN A CG 801 O OD1 . ASN A 101 ? 0.2493 0.2636 0.1936 -0.0052 0.0414 0.0023 187 ASN A OD1 802 N ND2 . ASN A 101 ? 0.1828 0.2274 0.1976 -0.0063 0.0330 0.0373 187 ASN A ND2 803 N N . GLY A 102 ? 0.1155 0.1227 0.1219 -0.0016 0.0029 -0.0093 188 GLY A N 804 C CA . GLY A 102 ? 0.1088 0.1185 0.1222 -0.0057 0.0006 -0.0067 188 GLY A CA 805 C C . GLY A 102 ? 0.1073 0.1152 0.1151 0.0032 -0.0029 0.0042 188 GLY A C 806 O O . GLY A 102 ? 0.1347 0.1383 0.1395 0.0085 -0.0128 -0.0108 188 GLY A O 807 N N . GLU A 103 ? 0.1005 0.1168 0.1196 0.0047 -0.0119 -0.0097 189 GLU A N 808 C CA . GLU A 103 ? 0.0899 0.1172 0.1148 0.0059 -0.0049 -0.0048 189 GLU A CA 809 C C . GLU A 103 ? 0.0921 0.1207 0.1167 0.0003 -0.0045 -0.0095 189 GLU A C 810 O O . GLU A 103 ? 0.1118 0.1318 0.1182 -0.0115 -0.0094 -0.0017 189 GLU A O 811 C CB . GLU A 103 ? 0.1027 0.1244 0.1234 0.0008 -0.0079 -0.0009 189 GLU A CB 812 C CG . GLU A 103 ? 0.0959 0.1140 0.1034 -0.0008 -0.0039 -0.0105 189 GLU A CG 813 C CD . GLU A 103 ? 0.0948 0.1061 0.1305 -0.0108 -0.0004 -0.0163 189 GLU A CD 814 O OE1 . GLU A 103 ? 0.1290 0.1474 0.2124 -0.0012 -0.0170 0.0212 189 GLU A OE1 815 O OE2 . GLU A 103 ? 0.0987 0.1037 0.1236 0.0017 -0.0095 -0.0082 189 GLU A OE2 816 N N . TRP A 104 ? 0.1017 0.1027 0.1061 0.0000 -0.0119 -0.0049 190 TRP A N 817 C CA . TRP A 104 ? 0.1035 0.1146 0.1150 0.0000 -0.0055 -0.0018 190 TRP A CA 818 C C . TRP A 104 ? 0.1070 0.1124 0.1038 0.0044 -0.0078 -0.0072 190 TRP A C 819 O O . TRP A 104 ? 0.1183 0.1176 0.1077 0.0040 -0.0137 -0.0070 190 TRP A O 820 C CB . TRP A 104 ? 0.1135 0.1057 0.1152 -0.0008 -0.0045 -0.0017 190 TRP A CB 821 C CG . TRP A 104 ? 0.1014 0.0964 0.1084 -0.0038 0.0074 -0.0043 190 TRP A CG 822 C CD1 . TRP A 104 ? 0.0921 0.1104 0.1029 0.0028 -0.0112 -0.0045 190 TRP A CD1 823 C CD2 . TRP A 104 ? 0.0961 0.1044 0.0929 -0.0087 0.0075 -0.0066 190 TRP A CD2 824 N NE1 . TRP A 104 ? 0.1015 0.1012 0.1112 -0.0042 -0.0023 -0.0089 190 TRP A NE1 825 C CE2 . TRP A 104 ? 0.0958 0.1029 0.0993 -0.0012 0.0006 -0.0129 190 TRP A CE2 826 C CE3 . TRP A 104 ? 0.1020 0.0972 0.1009 -0.0047 -0.0063 -0.0084 190 TRP A CE3 827 C CZ2 . TRP A 104 ? 0.1013 0.0960 0.1071 -0.0088 0.0040 -0.0086 190 TRP A CZ2 828 C CZ3 . TRP A 104 ? 0.0908 0.1181 0.1166 -0.0047 -0.0097 -0.0049 190 TRP A CZ3 829 C CH2 . TRP A 104 ? 0.0910 0.1143 0.1222 0.0057 0.0039 -0.0011 190 TRP A CH2 830 N N . ALA A 105 ? 0.1361 0.1148 0.1123 0.0029 -0.0131 -0.0104 191 ALA A N 831 C CA . ALA A 105 ? 0.1176 0.1224 0.1165 0.0072 -0.0153 -0.0084 191 ALA A CA 832 C C . ALA A 105 ? 0.1161 0.1167 0.1091 0.0069 -0.0174 0.0002 191 ALA A C 833 O O . ALA A 105 ? 0.1178 0.1318 0.1151 0.0095 -0.0170 -0.0059 191 ALA A O 834 C CB . ALA A 105 ? 0.1208 0.1366 0.1313 0.0031 -0.0138 -0.0058 191 ALA A CB 835 N N . ILE A 106 ? 0.1058 0.1238 0.1073 0.0009 -0.0153 0.0006 192 ILE A N 836 C CA . ILE A 106 ? 0.1150 0.1261 0.1085 0.0092 -0.0172 0.0043 192 ILE A CA 837 C C . ILE A 106 ? 0.1301 0.1477 0.1216 0.0080 -0.0101 -0.0025 192 ILE A C 838 O O . ILE A 106 ? 0.1528 0.1622 0.1275 0.0105 -0.0091 -0.0031 192 ILE A O 839 C CB . ILE A 106 ? 0.1283 0.1341 0.1194 0.0040 -0.0062 0.0096 192 ILE A CB 840 C CG1 . ILE A 106 ? 0.1144 0.1217 0.1242 -0.0069 -0.0069 0.0055 192 ILE A CG1 841 C CG2 . ILE A 106 ? 0.1746 0.1574 0.1539 -0.0085 0.0011 0.0030 192 ILE A CG2 842 C CD1 . ILE A 106 ? 0.1382 0.1464 0.1335 0.0004 -0.0007 0.0034 192 ILE A CD1 843 N N . ALA A 107 ? 0.1484 0.1652 0.1120 0.0164 -0.0195 -0.0035 193 ALA A N 844 C CA . ALA A 107 ? 0.1576 0.1696 0.1317 0.0127 -0.0241 0.0022 193 ALA A CA 845 C C . ALA A 107 ? 0.1718 0.1702 0.1165 0.0100 -0.0192 -0.0144 193 ALA A C 846 O O . ALA A 107 ? 0.2022 0.2075 0.1379 0.0080 -0.0400 -0.0132 193 ALA A O 847 C CB . ALA A 107 ? 0.1846 0.1963 0.1519 0.0150 -0.0391 -0.0066 193 ALA A CB 848 N N . ASN A 108 ? 0.1574 0.1659 0.1384 0.0081 -0.0266 0.0027 194 ASN A N 849 C CA . ASN A 108 ? 0.1519 0.1700 0.1269 0.0030 -0.0259 -0.0035 194 ASN A CA 850 C C . ASN A 108 ? 0.1371 0.1358 0.1153 -0.0014 -0.0146 -0.0030 194 ASN A C 851 O O . ASN A 108 ? 0.1350 0.1310 0.1318 -0.0079 -0.0088 -0.0017 194 ASN A O 852 C CB . ASN A 108 ? 0.1546 0.1927 0.1794 -0.0085 -0.0081 0.0009 194 ASN A CB 853 C CG . ASN A 108 ? 0.1904 0.2166 0.2079 -0.0102 -0.0076 -0.0098 194 ASN A CG 854 O OD1 . ASN A 108 ? 0.2425 0.2718 0.2742 -0.0197 0.0149 -0.0275 194 ASN A OD1 855 N ND2 . ASN A 108 ? 0.2406 0.2950 0.2385 -0.0013 -0.0158 0.0210 194 ASN A ND2 856 N N . ASN A 109 ? 0.1305 0.1385 0.1110 -0.0028 -0.0208 -0.0061 195 ASN A N 857 C CA . ASN A 109 ? 0.1284 0.1276 0.1041 0.0013 -0.0097 -0.0145 195 ASN A CA 858 C C . ASN A 109 ? 0.1137 0.1151 0.0938 -0.0007 -0.0016 -0.0065 195 ASN A C 859 O O . ASN A 109 ? 0.1185 0.1149 0.1013 0.0012 -0.0107 -0.0101 195 ASN A O 860 C CB . ASN A 109 ? 0.1368 0.1476 0.1197 -0.0090 -0.0237 -0.0169 195 ASN A CB 861 C CG . ASN A 109 ? 0.1633 0.1588 0.1412 -0.0038 -0.0158 -0.0096 195 ASN A CG 862 O OD1 . ASN A 109 ? 0.1875 0.1785 0.1593 0.0028 -0.0053 0.0033 195 ASN A OD1 863 N ND2 . ASN A 109 ? 0.1926 0.1738 0.1492 0.0143 -0.0071 -0.0121 195 ASN A ND2 864 N N . GLY A 110 ? 0.1114 0.1100 0.1024 0.0040 -0.0168 -0.0080 196 GLY A N 865 C CA . GLY A 110 ? 0.1071 0.1085 0.0878 0.0085 -0.0080 -0.0047 196 GLY A CA 866 C C . GLY A 110 ? 0.1047 0.1050 0.0984 0.0124 -0.0094 -0.0061 196 GLY A C 867 O O . GLY A 110 ? 0.1079 0.1006 0.0931 0.0082 -0.0135 -0.0030 196 GLY A O 868 N N . VAL A 111 ? 0.1145 0.1040 0.0934 0.0047 -0.0183 -0.0020 197 VAL A N 869 C CA . VAL A 111 ? 0.1285 0.1129 0.0843 -0.0054 -0.0132 -0.0003 197 VAL A CA 870 C C . VAL A 111 ? 0.0917 0.1074 0.0968 -0.0053 -0.0082 -0.0008 197 VAL A C 871 O O . VAL A 111 ? 0.1020 0.1132 0.0981 -0.0017 -0.0038 0.0083 197 VAL A O 872 C CB . VAL A 111 ? 0.1214 0.1255 0.1126 -0.0140 -0.0192 0.0063 197 VAL A CB 873 C CG1 . VAL A 111 ? 0.1604 0.1492 0.1324 -0.0239 -0.0134 0.0202 197 VAL A CG1 874 C CG2 . VAL A 111 ? 0.1810 0.1581 0.1303 -0.0068 -0.0184 0.0150 197 VAL A CG2 875 N N . ASN A 112 ? 0.1025 0.1062 0.0988 -0.0002 -0.0082 0.0029 198 ASN A N 876 C CA . ASN A 112 ? 0.1038 0.1123 0.0883 0.0011 0.0013 -0.0030 198 ASN A CA 877 C C . ASN A 112 ? 0.0998 0.1000 0.0838 -0.0028 -0.0029 -0.0052 198 ASN A C 878 O O . ASN A 112 ? 0.1000 0.1044 0.0926 0.0032 -0.0002 -0.0054 198 ASN A O 879 C CB . ASN A 112 ? 0.1409 0.1378 0.1052 0.0061 0.0015 -0.0020 198 ASN A CB 880 C CG . ASN A 112 ? 0.1836 0.1783 0.1334 0.0067 0.0005 0.0004 198 ASN A CG 881 O OD1 . ASN A 112 ? 0.2114 0.2324 0.1538 -0.0088 0.0329 0.0372 198 ASN A OD1 882 N ND2 . ASN A 112 ? 0.2533 0.2304 0.1630 0.0000 -0.0097 0.0000 198 ASN A ND2 883 N N . ASN A 113 ? 0.0889 0.1026 0.0863 -0.0008 -0.0081 -0.0076 199 ASN A N 884 C CA . ASN A 113 ? 0.0885 0.0909 0.0906 -0.0013 -0.0038 -0.0052 199 ASN A CA 885 C C . ASN A 113 ? 0.0899 0.0893 0.0784 0.0049 0.0012 0.0002 199 ASN A C 886 O O . ASN A 113 ? 0.0885 0.0845 0.0862 0.0018 -0.0018 -0.0039 199 ASN A O 887 C CB . ASN A 113 ? 0.1011 0.0967 0.0915 -0.0048 -0.0083 -0.0049 199 ASN A CB 888 C CG . ASN A 113 ? 0.0964 0.1086 0.0981 -0.0039 -0.0035 0.0030 199 ASN A CG 889 O OD1 . ASN A 113 ? 0.1020 0.1185 0.1010 -0.0099 -0.0084 -0.0100 199 ASN A OD1 890 N ND2 . ASN A 113 ? 0.1047 0.1263 0.1186 0.0042 -0.0097 -0.0039 199 ASN A ND2 891 N N . TYR A 114 ? 0.0833 0.0864 0.0793 -0.0021 -0.0075 -0.0008 200 TYR A N 892 C CA . TYR A 114 ? 0.0884 0.0873 0.0760 0.0004 -0.0051 -0.0022 200 TYR A CA 893 C C . TYR A 114 ? 0.0840 0.0792 0.0760 -0.0029 -0.0045 -0.0019 200 TYR A C 894 O O . TYR A 114 ? 0.0900 0.0854 0.0796 0.0000 -0.0065 -0.0022 200 TYR A O 895 C CB . TYR A 114 ? 0.0791 0.0842 0.0784 0.0024 0.0003 -0.0023 200 TYR A CB 896 C CG . TYR A 114 ? 0.0799 0.0750 0.0789 0.0038 -0.0028 -0.0009 200 TYR A CG 897 C CD1 . TYR A 114 ? 0.0836 0.0858 0.0803 -0.0015 -0.0043 -0.0052 200 TYR A CD1 898 C CD2 . TYR A 114 ? 0.0796 0.0901 0.0789 0.0066 0.0004 -0.0020 200 TYR A CD2 899 C CE1 . TYR A 114 ? 0.0876 0.0841 0.0763 -0.0004 -0.0001 -0.0034 200 TYR A CE1 900 C CE2 . TYR A 114 ? 0.0756 0.0887 0.0850 -0.0012 -0.0034 -0.0100 200 TYR A CE2 901 C CZ . TYR A 114 ? 0.0852 0.0749 0.0739 -0.0029 -0.0067 -0.0068 200 TYR A CZ 902 O OH . TYR A 114 ? 0.0895 0.0937 0.0878 0.0037 -0.0094 -0.0097 200 TYR A OH 903 N N . LYS A 115 ? 0.0819 0.0942 0.0806 0.0003 -0.0012 -0.0018 201 LYS A N 904 C CA . LYS A 115 ? 0.0851 0.0877 0.0746 -0.0037 -0.0008 -0.0020 201 LYS A CA 905 C C . LYS A 115 ? 0.0818 0.0887 0.0768 0.0007 0.0105 -0.0039 201 LYS A C 906 O O . LYS A 115 ? 0.0873 0.0924 0.0876 0.0022 -0.0010 0.0000 201 LYS A O 907 C CB . LYS A 115 ? 0.0907 0.1026 0.0954 -0.0023 0.0060 0.0053 201 LYS A CB 908 C CG . LYS A 115 ? 0.1051 0.1104 0.1075 0.0063 0.0057 0.0196 201 LYS A CG 909 C CD A LYS A 115 ? 0.1712 0.1466 0.1424 0.0079 0.0153 0.0307 201 LYS A CD 910 C CD B LYS A 115 ? 0.1903 0.1628 0.1480 -0.0026 0.0125 0.0245 201 LYS A CD 911 C CE A LYS A 115 ? 0.1942 0.1641 0.1932 0.0160 0.0380 0.0227 201 LYS A CE 912 C CE B LYS A 115 ? 0.2056 0.1929 0.2106 -0.0039 0.0085 0.0157 201 LYS A CE 913 N NZ A LYS A 115 ? 0.2686 0.2601 0.2295 -0.0019 0.0399 0.0399 201 LYS A NZ 914 N NZ B LYS A 115 ? 0.2760 0.2652 0.2143 -0.0038 0.0148 0.0056 201 LYS A NZ 915 N N . ALA A 116 ? 0.0874 0.0936 0.0794 0.0017 0.0022 0.0002 202 ALA A N 916 C CA . ALA A 116 ? 0.0854 0.0934 0.0850 0.0019 0.0054 -0.0083 202 ALA A CA 917 C C . ALA A 116 ? 0.0749 0.0805 0.0782 -0.0066 -0.0022 -0.0072 202 ALA A C 918 O O . ALA A 116 ? 0.0871 0.0860 0.0889 -0.0024 -0.0008 -0.0093 202 ALA A O 919 C CB . ALA A 116 ? 0.1019 0.0992 0.0903 -0.0004 -0.0089 -0.0101 202 ALA A CB 920 N N . TYR A 117 ? 0.0781 0.0844 0.0803 0.0023 0.0016 -0.0025 203 TYR A N 921 C CA . TYR A 117 ? 0.0762 0.0877 0.0820 -0.0047 -0.0032 -0.0015 203 TYR A CA 922 C C . TYR A 117 ? 0.0695 0.0755 0.0775 -0.0040 0.0036 -0.0054 203 TYR A C 923 O O . TYR A 117 ? 0.0764 0.0876 0.0847 -0.0012 -0.0024 -0.0027 203 TYR A O 924 C CB . TYR A 117 ? 0.0761 0.0888 0.0889 -0.0017 -0.0018 0.0013 203 TYR A CB 925 C CG . TYR A 117 ? 0.0635 0.0858 0.0807 -0.0002 0.0013 -0.0013 203 TYR A CG 926 C CD1 . TYR A 117 ? 0.0772 0.0819 0.0817 -0.0021 0.0010 -0.0007 203 TYR A CD1 927 C CD2 . TYR A 117 ? 0.0710 0.0834 0.0841 -0.0020 0.0007 0.0036 203 TYR A CD2 928 C CE1 . TYR A 117 ? 0.0859 0.0892 0.0768 -0.0074 0.0030 0.0037 203 TYR A CE1 929 C CE2 . TYR A 117 ? 0.0657 0.0815 0.0855 -0.0082 -0.0007 -0.0069 203 TYR A CE2 930 C CZ . TYR A 117 ? 0.0794 0.0845 0.0711 -0.0046 -0.0051 -0.0041 203 TYR A CZ 931 O OH . TYR A 117 ? 0.0944 0.0908 0.0877 0.0001 0.0009 -0.0108 203 TYR A OH 932 N N . ILE A 118 ? 0.0725 0.0814 0.0799 0.0035 -0.0068 0.0059 204 ILE A N 933 C CA . ILE A 118 ? 0.0743 0.0821 0.0806 -0.0039 -0.0032 -0.0088 204 ILE A CA 934 C C . ILE A 118 ? 0.0798 0.0745 0.0806 -0.0075 0.0000 0.0020 204 ILE A C 935 O O . ILE A 118 ? 0.0812 0.0880 0.0885 0.0035 -0.0005 -0.0003 204 ILE A O 936 C CB . ILE A 118 ? 0.0760 0.0874 0.0783 -0.0035 0.0018 -0.0041 204 ILE A CB 937 C CG1 . ILE A 118 ? 0.0760 0.0787 0.0888 -0.0074 -0.0082 0.0007 204 ILE A CG1 938 C CG2 . ILE A 118 ? 0.0821 0.0828 0.0939 -0.0056 0.0000 -0.0029 204 ILE A CG2 939 C CD1 . ILE A 118 ? 0.0953 0.0920 0.0946 0.0043 -0.0011 -0.0018 204 ILE A CD1 940 N N . ASN A 119 ? 0.0766 0.0814 0.0802 0.0043 0.0038 -0.0026 205 ASN A N 941 C CA . ASN A 119 ? 0.0824 0.0948 0.0923 0.0055 0.0038 -0.0076 205 ASN A CA 942 C C . ASN A 119 ? 0.0778 0.0863 0.0799 0.0028 -0.0012 -0.0027 205 ASN A C 943 O O . ASN A 119 ? 0.0820 0.0866 0.0950 0.0028 0.0012 0.0015 205 ASN A O 944 C CB . ASN A 119 ? 0.1041 0.0995 0.1080 0.0109 0.0087 -0.0003 205 ASN A CB 945 C CG . ASN A 119 ? 0.1122 0.1259 0.1033 0.0121 0.0118 -0.0165 205 ASN A CG 946 O OD1 . ASN A 119 ? 0.1117 0.1260 0.1361 -0.0032 0.0132 0.0045 205 ASN A OD1 947 N ND2 . ASN A 119 ? 0.1443 0.1466 0.1214 -0.0061 0.0105 -0.0135 205 ASN A ND2 948 N N . ARG A 120 ? 0.0830 0.0891 0.0852 0.0014 -0.0032 -0.0049 206 ARG A N 949 C CA . ARG A 120 ? 0.0767 0.0833 0.0882 0.0001 -0.0038 -0.0038 206 ARG A CA 950 C C . ARG A 120 ? 0.0732 0.0749 0.0852 0.0000 0.0014 -0.0041 206 ARG A C 951 O O . ARG A 120 ? 0.0841 0.0857 0.0933 0.0027 -0.0008 -0.0040 206 ARG A O 952 C CB . ARG A 120 ? 0.0828 0.0954 0.0893 -0.0034 0.0028 -0.0120 206 ARG A CB 953 C CG . ARG A 120 ? 0.0843 0.0952 0.0908 -0.0050 0.0004 -0.0068 206 ARG A CG 954 C CD . ARG A 120 ? 0.1266 0.1114 0.1129 -0.0044 0.0043 -0.0084 206 ARG A CD 955 N NE . ARG A 120 ? 0.0949 0.0996 0.1233 0.0017 0.0014 -0.0076 206 ARG A NE 956 C CZ . ARG A 120 ? 0.1032 0.1093 0.1368 -0.0065 0.0090 -0.0002 206 ARG A CZ 957 N NH1 . ARG A 120 ? 0.1213 0.1492 0.1759 0.0034 0.0118 0.0128 206 ARG A NH1 958 N NH2 . ARG A 120 ? 0.1305 0.1290 0.1703 0.0086 0.0029 0.0156 206 ARG A NH2 959 N N . ILE A 121 ? 0.0767 0.0833 0.0811 0.0033 -0.0012 -0.0014 207 ILE A N 960 C CA . ILE A 121 ? 0.0812 0.0828 0.0797 0.0057 0.0029 -0.0061 207 ILE A CA 961 C C . ILE A 121 ? 0.0825 0.0787 0.0775 0.0026 -0.0010 -0.0012 207 ILE A C 962 O O . ILE A 121 ? 0.0839 0.0875 0.0872 0.0059 0.0008 -0.0005 207 ILE A O 963 C CB . ILE A 121 ? 0.0770 0.0752 0.0750 -0.0028 -0.0007 -0.0036 207 ILE A CB 964 C CG1 . ILE A 121 ? 0.0828 0.0855 0.0812 -0.0015 0.0002 -0.0006 207 ILE A CG1 965 C CG2 . ILE A 121 ? 0.0848 0.0839 0.0873 0.0004 -0.0016 -0.0070 207 ILE A CG2 966 C CD1 . ILE A 121 ? 0.0872 0.0962 0.0913 0.0035 0.0000 -0.0011 207 ILE A CD1 967 N N . ARG A 122 ? 0.0766 0.0878 0.0822 0.0055 -0.0043 0.0006 208 ARG A N 968 C CA . ARG A 122 ? 0.0762 0.0837 0.0854 -0.0024 0.0013 0.0006 208 ARG A CA 969 C C . ARG A 122 ? 0.0765 0.0927 0.0870 -0.0003 0.0001 -0.0030 208 ARG A C 970 O O . ARG A 122 ? 0.0825 0.0879 0.0925 0.0019 -0.0033 0.0010 208 ARG A O 971 C CB . ARG A 122 ? 0.0866 0.0857 0.0773 -0.0019 -0.0025 -0.0005 208 ARG A CB 972 C CG . ARG A 122 ? 0.0955 0.0981 0.1041 -0.0034 0.0035 -0.0027 208 ARG A CG 973 C CD A ARG A 122 ? 0.0956 0.1071 0.1161 -0.0059 0.0028 -0.0031 208 ARG A CD 974 C CD B ARG A 122 ? 0.0848 0.0937 0.1107 -0.0047 0.0033 -0.0031 208 ARG A CD 975 N NE A ARG A 122 ? 0.1222 0.1078 0.1195 0.0105 0.0217 -0.0148 208 ARG A NE 976 N NE B ARG A 122 ? 0.0995 0.0920 0.0974 -0.0069 0.0116 -0.0192 208 ARG A NE 977 C CZ A ARG A 122 ? 0.0995 0.1181 0.1112 0.0103 0.0101 -0.0039 208 ARG A CZ 978 C CZ B ARG A 122 ? 0.1114 0.1288 0.1208 -0.0046 0.0055 -0.0065 208 ARG A CZ 979 N NH1 A ARG A 122 ? 0.1009 0.1181 0.1199 -0.0001 -0.0013 -0.0009 208 ARG A NH1 980 N NH1 B ARG A 122 ? 0.1000 0.1098 0.1184 0.0173 0.0082 -0.0003 208 ARG A NH1 981 N NH2 A ARG A 122 ? 0.1174 0.1552 0.1685 0.0168 0.0341 0.0048 208 ARG A NH2 982 N NH2 B ARG A 122 ? 0.1196 0.1188 0.1337 -0.0075 0.0078 -0.0090 208 ARG A NH2 983 N N . GLU A 123 ? 0.0783 0.0834 0.0860 0.0023 -0.0014 -0.0032 209 GLU A N 984 C CA . GLU A 123 ? 0.0782 0.0925 0.0883 0.0124 -0.0014 -0.0067 209 GLU A CA 985 C C . GLU A 123 ? 0.0804 0.0807 0.0869 0.0011 0.0022 -0.0071 209 GLU A C 986 O O . GLU A 123 ? 0.0869 0.0829 0.0914 0.0032 0.0047 -0.0077 209 GLU A O 987 C CB . GLU A 123 ? 0.0941 0.0912 0.0904 0.0038 0.0002 -0.0140 209 GLU A CB 988 C CG . GLU A 123 ? 0.1041 0.0984 0.1062 0.0003 0.0065 -0.0071 209 GLU A CG 989 C CD . GLU A 123 ? 0.1441 0.1567 0.1015 -0.0133 0.0198 -0.0118 209 GLU A CD 990 O OE1 . GLU A 123 ? 0.1417 0.1644 0.1312 -0.0281 0.0021 -0.0197 209 GLU A OE1 991 O OE2 . GLU A 123 ? 0.2221 0.2591 0.1466 -0.0548 0.0090 -0.0190 209 GLU A OE2 992 N N . ILE A 124 ? 0.0763 0.0863 0.0884 0.0061 0.0027 -0.0034 210 ILE A N 993 C CA . ILE A 124 ? 0.0820 0.0795 0.0907 0.0047 -0.0009 -0.0030 210 ILE A CA 994 C C . ILE A 124 ? 0.0822 0.0814 0.0920 0.0035 0.0083 -0.0006 210 ILE A C 995 O O . ILE A 124 ? 0.0826 0.0862 0.0887 0.0021 -0.0027 -0.0042 210 ILE A O 996 C CB . ILE A 124 ? 0.0714 0.0804 0.0884 0.0056 -0.0026 0.0010 210 ILE A CB 997 C CG1 . ILE A 124 ? 0.0863 0.0983 0.0946 -0.0068 0.0061 0.0035 210 ILE A CG1 998 C CG2 . ILE A 124 ? 0.0853 0.0890 0.0996 0.0042 0.0002 -0.0065 210 ILE A CG2 999 C CD1 . ILE A 124 ? 0.0863 0.1001 0.1046 -0.0060 0.0027 0.0014 210 ILE A CD1 1000 N N . LEU A 125 ? 0.0768 0.0764 0.0847 -0.0001 -0.0037 -0.0055 211 LEU A N 1001 C CA . LEU A 125 ? 0.0852 0.0821 0.0810 0.0086 -0.0040 -0.0069 211 LEU A CA 1002 C C . LEU A 125 ? 0.0873 0.0755 0.0868 -0.0006 -0.0021 -0.0065 211 LEU A C 1003 O O . LEU A 125 ? 0.0908 0.0874 0.0909 0.0058 -0.0041 -0.0038 211 LEU A O 1004 C CB . LEU A 125 ? 0.0893 0.0738 0.0878 0.0013 -0.0049 -0.0041 211 LEU A CB 1005 C CG . LEU A 125 ? 0.0922 0.0828 0.0931 0.0085 -0.0051 -0.0084 211 LEU A CG 1006 C CD1 . LEU A 125 ? 0.1107 0.1114 0.1445 0.0103 -0.0144 -0.0142 211 LEU A CD1 1007 C CD2 . LEU A 125 ? 0.1288 0.1251 0.1252 0.0423 0.0038 0.0040 211 LEU A CD2 1008 N N . ILE A 126 ? 0.0759 0.0840 0.0868 0.0078 0.0057 -0.0013 212 ILE A N 1009 C CA . ILE A 126 ? 0.0879 0.0942 0.0983 0.0010 0.0065 -0.0024 212 ILE A CA 1010 C C . ILE A 126 ? 0.0804 0.0862 0.0823 0.0042 0.0062 -0.0013 212 ILE A C 1011 O O . ILE A 126 ? 0.0871 0.1008 0.0913 0.0072 -0.0001 -0.0053 212 ILE A O 1012 C CB . ILE A 126 ? 0.0946 0.1110 0.1193 0.0099 0.0155 0.0136 212 ILE A CB 1013 C CG1 . ILE A 126 ? 0.0893 0.1170 0.1298 0.0048 0.0010 0.0054 212 ILE A CG1 1014 C CG2 . ILE A 126 ? 0.1012 0.1234 0.1255 0.0084 0.0029 0.0052 212 ILE A CG2 1015 C CD1 . ILE A 126 ? 0.1274 0.1217 0.1479 0.0155 0.0123 0.0047 212 ILE A CD1 1016 N N . SER A 127 ? 0.0817 0.0908 0.0910 0.0023 0.0039 -0.0037 213 SER A N 1017 C CA A SER A 127 ? 0.0833 0.0876 0.0931 0.0023 0.0126 -0.0085 213 SER A CA 1018 C CA B SER A 127 ? 0.0856 0.0895 0.0934 0.0026 0.0083 -0.0055 213 SER A CA 1019 C CA C SER A 127 ? 0.0866 0.0904 0.0954 0.0024 0.0102 -0.0071 213 SER A CA 1020 C C . SER A 127 ? 0.0848 0.0836 0.0929 0.0067 0.0044 -0.0042 213 SER A C 1021 O O . SER A 127 ? 0.0896 0.0884 0.0987 0.0086 0.0051 0.0002 213 SER A O 1022 C CB A SER A 127 ? 0.0986 0.0956 0.1122 0.0008 -0.0028 -0.0099 213 SER A CB 1023 C CB B SER A 127 ? 0.0852 0.1010 0.1001 0.0001 0.0057 -0.0061 213 SER A CB 1024 C CB C SER A 127 ? 0.0986 0.0898 0.1123 0.0001 -0.0037 -0.0087 213 SER A CB 1025 O OG A SER A 127 ? 0.1101 0.0940 0.1156 0.0087 -0.0085 -0.0045 213 SER A OG 1026 O OG B SER A 127 ? 0.0820 0.0948 0.0834 -0.0028 0.0091 0.0060 213 SER A OG 1027 O OG C SER A 127 ? 0.1338 0.1434 0.1268 0.0004 -0.0007 0.0006 213 SER A OG 1028 N N . PHE A 128 ? 0.0895 0.0830 0.0858 0.0085 -0.0003 -0.0040 214 PHE A N 1029 C CA . PHE A 128 ? 0.0878 0.0899 0.0863 0.0105 0.0084 -0.0046 214 PHE A CA 1030 C C . PHE A 128 ? 0.0859 0.0820 0.0844 0.0118 0.0019 -0.0049 214 PHE A C 1031 O O . PHE A 128 ? 0.0911 0.0955 0.0940 0.0110 -0.0002 -0.0060 214 PHE A O 1032 C CB . PHE A 128 ? 0.0965 0.0956 0.0969 0.0120 0.0161 -0.0049 214 PHE A CB 1033 C CG . PHE A 128 ? 0.0936 0.1068 0.0963 0.0094 0.0124 -0.0017 214 PHE A CG 1034 C CD1 . PHE A 128 ? 0.1100 0.1179 0.1221 0.0045 0.0048 0.0011 214 PHE A CD1 1035 C CD2 . PHE A 128 ? 0.0994 0.1104 0.1151 -0.0088 0.0128 0.0034 214 PHE A CD2 1036 C CE1 . PHE A 128 ? 0.1519 0.1357 0.1444 -0.0060 0.0168 0.0262 214 PHE A CE1 1037 C CE2 . PHE A 128 ? 0.1215 0.1420 0.1234 -0.0137 -0.0038 -0.0006 214 PHE A CE2 1038 C CZ . PHE A 128 ? 0.1631 0.1538 0.1975 -0.0302 0.0102 0.0136 214 PHE A CZ 1039 N N . SER A 129 ? 0.0820 0.0761 0.0912 0.0093 0.0014 -0.0104 215 SER A N 1040 C CA . SER A 129 ? 0.0855 0.0790 0.0944 0.0090 0.0003 -0.0055 215 SER A CA 1041 C C . SER A 129 ? 0.0948 0.0820 0.0959 0.0008 -0.0043 -0.0094 215 SER A C 1042 O O . SER A 129 ? 0.1047 0.0882 0.1014 0.0047 -0.0105 -0.0058 215 SER A O 1043 C CB . SER A 129 ? 0.0881 0.0896 0.0963 0.0038 -0.0025 -0.0012 215 SER A CB 1044 O OG . SER A 129 ? 0.0916 0.0954 0.0978 0.0106 0.0007 -0.0069 215 SER A OG 1045 N N . ASP A 130 ? 0.0883 0.0891 0.0861 0.0126 -0.0015 -0.0047 216 ASP A N 1046 C CA . ASP A 130 ? 0.0973 0.0933 0.0967 0.0092 -0.0044 0.0008 216 ASP A CA 1047 C C . ASP A 130 ? 0.1017 0.0891 0.0799 0.0100 -0.0035 -0.0017 216 ASP A C 1048 O O . ASP A 130 ? 0.1300 0.1262 0.1085 0.0279 -0.0080 -0.0006 216 ASP A O 1049 C CB . ASP A 130 ? 0.1064 0.0984 0.0948 0.0219 0.0005 0.0028 216 ASP A CB 1050 C CG . ASP A 130 ? 0.1213 0.1006 0.1027 0.0044 -0.0020 0.0132 216 ASP A CG 1051 O OD1 . ASP A 130 ? 0.1335 0.1110 0.1401 -0.0008 -0.0273 0.0128 216 ASP A OD1 1052 O OD2 . ASP A 130 ? 0.1523 0.1330 0.1309 -0.0056 -0.0061 0.0156 216 ASP A OD2 1053 N N . VAL A 131 ? 0.0954 0.0878 0.0890 0.0124 0.0006 -0.0050 217 VAL A N 1054 C CA . VAL A 131 ? 0.1025 0.0834 0.0860 0.0149 0.0055 -0.0016 217 VAL A CA 1055 C C . VAL A 131 ? 0.0924 0.0816 0.0793 0.0201 -0.0041 -0.0033 217 VAL A C 1056 O O . VAL A 131 ? 0.0987 0.0855 0.0853 0.0161 0.0070 0.0011 217 VAL A O 1057 C CB . VAL A 131 ? 0.1051 0.0867 0.0940 0.0151 0.0019 -0.0065 217 VAL A CB 1058 C CG1 . VAL A 131 ? 0.1096 0.0998 0.1041 0.0019 0.0130 0.0052 217 VAL A CG1 1059 C CG2 . VAL A 131 ? 0.1184 0.0955 0.1064 0.0041 0.0055 -0.0014 217 VAL A CG2 1060 N N . ARG A 132 ? 0.0953 0.0837 0.0944 0.0141 -0.0079 0.0035 218 ARG A N 1061 C CA . ARG A 132 ? 0.0877 0.0834 0.0918 0.0129 -0.0007 -0.0014 218 ARG A CA 1062 C C . ARG A 132 ? 0.0842 0.0833 0.0806 0.0052 0.0019 -0.0009 218 ARG A C 1063 O O . ARG A 132 ? 0.0965 0.0902 0.0902 0.0120 -0.0001 0.0008 218 ARG A O 1064 C CB . ARG A 132 ? 0.0908 0.0941 0.1082 0.0103 -0.0058 -0.0033 218 ARG A CB 1065 C CG . ARG A 132 ? 0.1048 0.0999 0.1104 0.0085 0.0002 -0.0035 218 ARG A CG 1066 C CD . ARG A 132 ? 0.1014 0.1049 0.1213 0.0085 -0.0097 -0.0063 218 ARG A CD 1067 N NE . ARG A 132 ? 0.0994 0.1111 0.1384 0.0196 -0.0073 -0.0116 218 ARG A NE 1068 C CZ . ARG A 132 ? 0.1187 0.1173 0.1250 0.0169 -0.0073 0.0042 218 ARG A CZ 1069 N NH1 . ARG A 132 ? 0.1233 0.1277 0.1315 0.0035 -0.0214 -0.0080 218 ARG A NH1 1070 N NH2 . ARG A 132 ? 0.1276 0.1438 0.1561 0.0212 -0.0127 -0.0038 218 ARG A NH2 1071 N N . THR A 133 ? 0.0796 0.0807 0.0891 0.0078 -0.0008 -0.0014 219 THR A N 1072 C CA . THR A 133 ? 0.0779 0.0734 0.0855 0.0086 -0.0002 -0.0007 219 THR A CA 1073 C C . THR A 133 ? 0.0692 0.0727 0.0804 0.0045 0.0000 -0.0011 219 THR A C 1074 O O . THR A 133 ? 0.0919 0.0823 0.0979 0.0079 0.0085 -0.0022 219 THR A O 1075 C CB . THR A 133 ? 0.0845 0.0839 0.0975 0.0049 -0.0040 0.0004 219 THR A CB 1076 O OG1 . THR A 133 ? 0.0998 0.0792 0.0888 0.0025 0.0002 -0.0040 219 THR A OG1 1077 C CG2 . THR A 133 ? 0.1074 0.1024 0.0966 0.0090 -0.0134 -0.0017 219 THR A CG2 1078 N N . ILE A 134 ? 0.0728 0.0740 0.0772 0.0050 0.0005 0.0024 220 ILE A N 1079 C CA . ILE A 134 ? 0.0725 0.0718 0.0766 0.0069 -0.0004 -0.0013 220 ILE A CA 1080 C C . ILE A 134 ? 0.0673 0.0700 0.0690 0.0029 -0.0036 -0.0048 220 ILE A C 1081 O O . ILE A 134 ? 0.0785 0.0788 0.0825 0.0020 -0.0047 0.0023 220 ILE A O 1082 C CB . ILE A 134 ? 0.0814 0.0834 0.0854 0.0061 -0.0008 -0.0065 220 ILE A CB 1083 C CG1 . ILE A 134 ? 0.1027 0.1050 0.0977 0.0046 -0.0126 -0.0085 220 ILE A CG1 1084 C CG2 . ILE A 134 ? 0.0991 0.0981 0.0932 0.0045 0.0002 -0.0170 220 ILE A CG2 1085 C CD1 . ILE A 134 ? 0.1093 0.0961 0.1127 0.0159 -0.0067 0.0001 220 ILE A CD1 1086 N N . LEU A 135 ? 0.0689 0.0719 0.0811 0.0021 0.0028 0.0009 221 LEU A N 1087 C CA . LEU A 135 ? 0.0734 0.0778 0.0803 0.0054 -0.0021 -0.0004 221 LEU A CA 1088 C C . LEU A 135 ? 0.0657 0.0695 0.0758 -0.0003 -0.0026 0.0025 221 LEU A C 1089 O O . LEU A 135 ? 0.0737 0.0749 0.0885 -0.0009 0.0022 0.0054 221 LEU A O 1090 C CB . LEU A 135 ? 0.0772 0.0826 0.0798 0.0035 -0.0001 0.0007 221 LEU A CB 1091 C CG . LEU A 135 ? 0.0807 0.0816 0.0837 0.0016 -0.0054 -0.0014 221 LEU A CG 1092 C CD1 . LEU A 135 ? 0.0937 0.0854 0.0841 -0.0049 0.0015 0.0005 221 LEU A CD1 1093 C CD2 . LEU A 135 ? 0.0954 0.0870 0.1065 0.0046 0.0009 -0.0015 221 LEU A CD2 1094 N N . VAL A 136 ? 0.0648 0.0651 0.0743 -0.0034 -0.0040 0.0028 222 VAL A N 1095 C CA . VAL A 136 ? 0.0687 0.0630 0.0666 0.0031 -0.0002 0.0018 222 VAL A CA 1096 C C . VAL A 136 ? 0.0711 0.0643 0.0716 -0.0003 -0.0003 -0.0052 222 VAL A C 1097 O O . VAL A 136 ? 0.0841 0.0799 0.0813 -0.0064 -0.0031 -0.0024 222 VAL A O 1098 C CB . VAL A 136 ? 0.0843 0.0765 0.0744 -0.0010 -0.0012 -0.0020 222 VAL A CB 1099 C CG1 . VAL A 136 ? 0.0802 0.0865 0.0826 0.0063 0.0036 -0.0078 222 VAL A CG1 1100 C CG2 . VAL A 136 ? 0.0842 0.0816 0.0763 0.0029 0.0012 -0.0054 222 VAL A CG2 1101 N N . ILE A 137 ? 0.0663 0.0685 0.0695 -0.0002 -0.0019 -0.0016 223 ILE A N 1102 C CA . ILE A 137 ? 0.0760 0.0737 0.0729 -0.0030 0.0028 -0.0012 223 ILE A CA 1103 C C . ILE A 137 ? 0.0750 0.0734 0.0672 -0.0060 0.0012 0.0023 223 ILE A C 1104 O O . ILE A 137 ? 0.0806 0.0751 0.0713 -0.0001 -0.0052 -0.0026 223 ILE A O 1105 C CB . ILE A 137 ? 0.0783 0.0762 0.0716 -0.0023 0.0025 0.0048 223 ILE A CB 1106 C CG1 . ILE A 137 ? 0.0796 0.0965 0.0870 -0.0035 0.0027 -0.0051 223 ILE A CG1 1107 C CG2 . ILE A 137 ? 0.0883 0.0850 0.0820 0.0001 0.0032 -0.0017 223 ILE A CG2 1108 C CD1 . ILE A 137 ? 0.0940 0.0901 0.1043 0.0031 -0.0050 0.0046 223 ILE A CD1 1109 N N . GLU A 138 ? 0.0689 0.0653 0.0715 0.0000 -0.0014 0.0000 224 GLU A N 1110 C CA . GLU A 138 ? 0.0723 0.0684 0.0702 0.0007 -0.0030 -0.0003 224 GLU A CA 1111 C C . GLU A 138 ? 0.0686 0.0664 0.0715 -0.0005 -0.0022 -0.0022 224 GLU A C 1112 O O . GLU A 138 ? 0.0748 0.0740 0.0721 -0.0008 -0.0012 0.0001 224 GLU A O 1113 C CB . GLU A 138 ? 0.0778 0.0794 0.0794 -0.0001 -0.0018 0.0055 224 GLU A CB 1114 C CG . GLU A 138 ? 0.0844 0.0797 0.0704 -0.0004 0.0007 0.0019 224 GLU A CG 1115 C CD . GLU A 138 ? 0.0816 0.0811 0.0724 0.0038 -0.0072 0.0024 224 GLU A CD 1116 O OE1 . GLU A 138 ? 0.0823 0.0846 0.0851 0.0017 -0.0058 -0.0039 224 GLU A OE1 1117 O OE2 . GLU A 138 ? 0.0835 0.0822 0.0771 0.0018 -0.0031 -0.0066 224 GLU A OE2 1118 N N . PRO A 139 ? 0.0797 0.0716 0.0755 -0.0014 -0.0038 0.0057 225 PRO A N 1119 C CA . PRO A 139 ? 0.0742 0.0813 0.0756 -0.0065 0.0023 0.0031 225 PRO A CA 1120 C C . PRO A 139 ? 0.0828 0.0790 0.0709 0.0012 0.0027 -0.0051 225 PRO A C 1121 O O . PRO A 139 ? 0.0757 0.0878 0.0799 0.0019 -0.0043 -0.0017 225 PRO A O 1122 C CB . PRO A 139 ? 0.0933 0.0977 0.0809 0.0070 0.0004 0.0062 225 PRO A CB 1123 C CG . PRO A 139 ? 0.0999 0.0862 0.0816 0.0021 0.0045 0.0020 225 PRO A CG 1124 C CD . PRO A 139 ? 0.0844 0.0801 0.0814 0.0004 -0.0009 0.0003 225 PRO A CD 1125 N N . ASP A 140 ? 0.0832 0.0840 0.0737 0.0027 -0.0031 -0.0055 226 ASP A N 1126 C CA . ASP A 140 ? 0.0831 0.0799 0.0781 -0.0009 0.0018 0.0018 226 ASP A CA 1127 C C . ASP A 140 ? 0.0788 0.0761 0.0829 0.0002 -0.0087 0.0037 226 ASP A C 1128 O O . ASP A 140 ? 0.0842 0.0857 0.0826 -0.0027 -0.0005 0.0053 226 ASP A O 1129 C CB . ASP A 140 ? 0.0882 0.0983 0.0910 0.0054 0.0027 -0.0020 226 ASP A CB 1130 C CG . ASP A 140 ? 0.0973 0.0981 0.0912 0.0052 0.0002 -0.0052 226 ASP A CG 1131 O OD1 . ASP A 140 ? 0.1145 0.1229 0.1334 0.0136 0.0022 -0.0152 226 ASP A OD1 1132 O OD2 . ASP A 140 ? 0.0986 0.1053 0.1003 0.0092 0.0000 -0.0030 226 ASP A OD2 1133 N N . SER A 141 ? 0.0789 0.0808 0.0711 0.0001 -0.0083 0.0049 227 SER A N 1134 C CA . SER A 141 ? 0.0802 0.0783 0.0758 -0.0001 -0.0031 0.0026 227 SER A CA 1135 C C . SER A 141 ? 0.0839 0.0790 0.0769 0.0022 0.0000 0.0010 227 SER A C 1136 O O . SER A 141 ? 0.0813 0.0866 0.0820 0.0040 -0.0069 0.0034 227 SER A O 1137 C CB . SER A 141 ? 0.0850 0.0857 0.0803 -0.0082 0.0035 0.0074 227 SER A CB 1138 O OG . SER A 141 ? 0.0762 0.0795 0.0789 0.0040 0.0035 -0.0017 227 SER A OG 1139 N N . LEU A 142 ? 0.0784 0.0821 0.0807 0.0020 -0.0027 0.0093 228 LEU A N 1140 C CA . LEU A 142 ? 0.0815 0.0855 0.0817 0.0012 0.0014 0.0097 228 LEU A CA 1141 C C . LEU A 142 ? 0.0766 0.0739 0.0818 0.0000 -0.0008 0.0095 228 LEU A C 1142 O O . LEU A 142 ? 0.0872 0.0798 0.0884 0.0038 -0.0019 0.0075 228 LEU A O 1143 C CB . LEU A 142 ? 0.0836 0.0853 0.0932 0.0069 0.0054 0.0020 228 LEU A CB 1144 C CG . LEU A 142 ? 0.1000 0.1006 0.1157 -0.0051 0.0098 -0.0070 228 LEU A CG 1145 C CD1 . LEU A 142 ? 0.1162 0.1248 0.1497 0.0058 0.0202 0.0039 228 LEU A CD1 1146 C CD2 . LEU A 142 ? 0.1268 0.1407 0.1305 0.0007 0.0144 -0.0146 228 LEU A CD2 1147 N N . ALA A 143 ? 0.0848 0.0811 0.0852 -0.0003 -0.0032 0.0074 229 ALA A N 1148 C CA . ALA A 143 ? 0.0856 0.0792 0.0854 -0.0035 -0.0001 -0.0004 229 ALA A CA 1149 C C . ALA A 143 ? 0.0817 0.0765 0.0905 -0.0013 0.0050 -0.0002 229 ALA A C 1150 O O . ALA A 143 ? 0.0979 0.0882 0.0920 -0.0007 0.0025 0.0019 229 ALA A O 1151 C CB . ALA A 143 ? 0.1080 0.0940 0.0867 0.0072 -0.0029 -0.0027 229 ALA A CB 1152 N N . ASN A 144 ? 0.0853 0.0827 0.0794 0.0052 -0.0039 0.0041 230 ASN A N 1153 C CA . ASN A 144 ? 0.0885 0.0883 0.0941 0.0063 -0.0049 0.0061 230 ASN A CA 1154 C C . ASN A 144 ? 0.0885 0.0826 0.0850 0.0038 -0.0106 0.0018 230 ASN A C 1155 O O . ASN A 144 ? 0.1022 0.0991 0.1039 0.0083 -0.0034 0.0085 230 ASN A O 1156 C CB . ASN A 144 ? 0.0857 0.0885 0.0933 0.0095 -0.0120 0.0034 230 ASN A CB 1157 C CG . ASN A 144 ? 0.0904 0.0863 0.0935 0.0136 -0.0050 -0.0006 230 ASN A CG 1158 O OD1 . ASN A 144 ? 0.0993 0.1005 0.1061 0.0042 0.0010 0.0111 230 ASN A OD1 1159 N ND2 . ASN A 144 ? 0.1078 0.0932 0.0991 0.0012 -0.0114 0.0089 230 ASN A ND2 1160 N N . MET A 145 ? 0.0948 0.0896 0.0892 0.0007 0.0006 0.0156 231 MET A N 1161 C CA . MET A 145 ? 0.0946 0.0930 0.0950 0.0000 -0.0012 0.0192 231 MET A CA 1162 C C . MET A 145 ? 0.1108 0.0972 0.0905 0.0007 -0.0009 0.0195 231 MET A C 1163 O O . MET A 145 ? 0.1595 0.1233 0.1254 -0.0191 -0.0172 0.0270 231 MET A O 1164 C CB . MET A 145 ? 0.1134 0.1126 0.1038 -0.0023 -0.0037 0.0262 231 MET A CB 1165 C CG . MET A 145 ? 0.1083 0.1254 0.1125 0.0107 0.0044 0.0173 231 MET A CG 1166 S SD . MET A 145 ? 0.1126 0.1094 0.1038 0.0071 -0.0009 0.0139 231 MET A SD 1167 C CE . MET A 145 ? 0.1134 0.1057 0.0994 0.0034 -0.0077 -0.0003 231 MET A CE 1168 N N . VAL A 146 ? 0.1173 0.0994 0.0961 -0.0081 -0.0123 0.0114 232 VAL A N 1169 C CA . VAL A 146 ? 0.1216 0.1111 0.1007 -0.0136 -0.0034 0.0125 232 VAL A CA 1170 C C . VAL A 146 ? 0.1455 0.1015 0.1208 -0.0109 -0.0111 0.0197 232 VAL A C 1171 O O . VAL A 146 ? 0.1679 0.1187 0.1756 -0.0122 0.0018 0.0208 232 VAL A O 1172 C CB . VAL A 146 ? 0.1290 0.1125 0.1095 -0.0150 -0.0094 0.0071 232 VAL A CB 1173 C CG1 . VAL A 146 ? 0.1347 0.1370 0.1143 -0.0241 -0.0091 0.0091 232 VAL A CG1 1174 C CG2 . VAL A 146 ? 0.1305 0.1300 0.1217 -0.0213 -0.0038 0.0117 232 VAL A CG2 1175 N N . THR A 147 ? 0.1172 0.1040 0.1088 -0.0078 -0.0143 0.0029 233 THR A N 1176 C CA . THR A 147 ? 0.1315 0.1096 0.1028 -0.0032 -0.0094 0.0105 233 THR A CA 1177 C C . THR A 147 ? 0.1240 0.1174 0.1023 0.0128 -0.0088 0.0049 233 THR A C 1178 O O . THR A 147 ? 0.1518 0.1177 0.1299 0.0182 -0.0180 -0.0069 233 THR A O 1179 C CB . THR A 147 ? 0.1355 0.1157 0.1216 0.0065 -0.0095 0.0024 233 THR A CB 1180 O OG1 . THR A 147 ? 0.1278 0.1081 0.1009 0.0039 -0.0150 0.0072 233 THR A OG1 1181 C CG2 . THR A 147 ? 0.1585 0.1487 0.1175 -0.0029 -0.0072 0.0044 233 THR A CG2 1182 N N . ASN A 148 ? 0.1161 0.1069 0.0974 0.0070 -0.0095 0.0090 234 ASN A N 1183 C CA . ASN A 148 ? 0.1160 0.1022 0.1056 0.0060 -0.0052 0.0039 234 ASN A CA 1184 C C . ASN A 148 ? 0.1099 0.1049 0.1110 0.0066 -0.0154 0.0055 234 ASN A C 1185 O O . ASN A 148 ? 0.1246 0.1173 0.1187 0.0055 -0.0190 0.0075 234 ASN A O 1186 C CB . ASN A 148 ? 0.1143 0.1107 0.1086 0.0010 -0.0066 0.0119 234 ASN A CB 1187 C CG . ASN A 148 ? 0.1382 0.1105 0.1421 0.0261 0.0166 -0.0017 234 ASN A CG 1188 O OD1 . ASN A 148 ? 0.2830 0.1407 0.1936 0.0305 0.0656 0.0097 234 ASN A OD1 1189 N ND2 . ASN A 148 ? 0.1191 0.1093 0.1062 0.0015 -0.0084 0.0110 234 ASN A ND2 1190 N N . MET A 149 ? 0.1263 0.1121 0.1020 0.0060 -0.0093 0.0044 235 MET A N 1191 C CA . MET A 149 ? 0.1285 0.1176 0.1108 0.0127 -0.0094 0.0038 235 MET A CA 1192 C C . MET A 149 ? 0.1392 0.1145 0.1144 0.0157 -0.0114 0.0053 235 MET A C 1193 O O . MET A 149 ? 0.1383 0.1365 0.1139 0.0215 -0.0146 0.0174 235 MET A O 1194 C CB . MET A 149 ? 0.1269 0.1234 0.1219 0.0128 0.0050 0.0059 235 MET A CB 1195 C CG . MET A 149 ? 0.1356 0.1554 0.1300 0.0123 -0.0151 0.0132 235 MET A CG 1196 S SD . MET A 149 ? 0.1511 0.1337 0.1317 0.0194 -0.0057 0.0135 235 MET A SD 1197 C CE . MET A 149 ? 0.1861 0.1731 0.1530 -0.0031 -0.0140 0.0029 235 MET A CE 1198 N N . ASN A 150 ? 0.1286 0.1245 0.1207 0.0181 -0.0191 0.0128 236 ASN A N 1199 C CA . ASN A 150 ? 0.1348 0.1340 0.1349 0.0295 -0.0114 0.0082 236 ASN A CA 1200 C C . ASN A 150 ? 0.1234 0.1387 0.1147 0.0229 -0.0128 0.0162 236 ASN A C 1201 O O . ASN A 150 ? 0.1384 0.1559 0.1523 0.0219 -0.0221 0.0230 236 ASN A O 1202 C CB . ASN A 150 ? 0.1681 0.1557 0.1668 0.0304 0.0000 -0.0044 236 ASN A CB 1203 C CG . ASN A 150 ? 0.1977 0.2088 0.1677 0.0395 -0.0010 -0.0305 236 ASN A CG 1204 O OD1 . ASN A 150 ? 0.2447 0.2502 0.1952 0.0575 -0.0106 0.0155 236 ASN A OD1 1205 N ND2 . ASN A 150 ? 0.2633 0.3235 0.2430 -0.0088 0.0180 -0.0066 236 ASN A ND2 1206 N N . VAL A 151 ? 0.1266 0.1162 0.1125 0.0210 -0.0019 0.0092 237 VAL A N 1207 C CA . VAL A 151 ? 0.1149 0.1342 0.1110 0.0159 -0.0051 0.0154 237 VAL A CA 1208 C C . VAL A 151 ? 0.1115 0.1319 0.1140 0.0114 -0.0059 0.0077 237 VAL A C 1209 O O . VAL A 151 ? 0.1130 0.1273 0.1156 0.0184 -0.0083 0.0045 237 VAL A O 1210 C CB . VAL A 151 ? 0.1325 0.1444 0.1153 0.0189 -0.0002 0.0154 237 VAL A CB 1211 C CG1 . VAL A 151 ? 0.1386 0.1658 0.1355 0.0110 -0.0006 0.0109 237 VAL A CG1 1212 C CG2 . VAL A 151 ? 0.1394 0.1553 0.1330 0.0041 0.0018 0.0102 237 VAL A CG2 1213 N N . PRO A 152 ? 0.1103 0.1254 0.1127 0.0107 -0.0041 0.0114 238 PRO A N 1214 C CA . PRO A 152 ? 0.1160 0.1225 0.1149 0.0110 -0.0145 0.0101 238 PRO A CA 1215 C C . PRO A 152 ? 0.1020 0.1157 0.1023 0.0153 -0.0138 0.0075 238 PRO A C 1216 O O . PRO A 152 ? 0.1187 0.1367 0.1151 0.0136 -0.0160 0.0074 238 PRO A O 1217 C CB . PRO A 152 ? 0.1315 0.1269 0.1246 0.0160 -0.0146 0.0218 238 PRO A CB 1218 C CG . PRO A 152 ? 0.1353 0.1407 0.1364 0.0159 -0.0061 0.0119 238 PRO A CG 1219 C CD . PRO A 152 ? 0.1130 0.1250 0.1284 0.0177 -0.0081 0.0148 238 PRO A CD 1220 N N . LYS A 153 ? 0.0978 0.1240 0.1042 0.0142 -0.0101 0.0053 239 LYS A N 1221 C CA . LYS A 153 ? 0.0963 0.1102 0.1136 0.0069 -0.0068 0.0032 239 LYS A CA 1222 C C . LYS A 153 ? 0.0909 0.1023 0.1148 0.0079 -0.0015 0.0031 239 LYS A C 1223 O O . LYS A 153 ? 0.1085 0.1123 0.1162 0.0125 -0.0061 -0.0061 239 LYS A O 1224 C CB . LYS A 153 ? 0.1067 0.1177 0.1261 -0.0040 -0.0151 0.0091 239 LYS A CB 1225 C CG . LYS A 153 ? 0.1175 0.1330 0.1344 0.0090 -0.0138 0.0059 239 LYS A CG 1226 C CD . LYS A 153 ? 0.1255 0.1446 0.1938 0.0126 -0.0171 0.0048 239 LYS A CD 1227 C CE . LYS A 153 ? 0.1478 0.1559 0.1989 0.0174 -0.0265 0.0252 239 LYS A CE 1228 N NZ . LYS A 153 ? 0.1791 0.1870 0.2902 -0.0117 -0.0225 0.0248 239 LYS A NZ 1229 N N . CYS A 154 ? 0.0863 0.1078 0.1005 0.0073 -0.0055 -0.0003 240 CYS A N 1230 C CA . CYS A 154 ? 0.1002 0.1037 0.0939 0.0085 -0.0046 0.0031 240 CYS A CA 1231 C C . CYS A 154 ? 0.0978 0.1004 0.1008 0.0110 -0.0076 0.0094 240 CYS A C 1232 O O . CYS A 154 ? 0.0981 0.1096 0.1003 0.0084 -0.0039 0.0122 240 CYS A O 1233 C CB . CYS A 154 ? 0.1036 0.1125 0.0880 0.0066 -0.0108 0.0074 240 CYS A CB 1234 S SG . CYS A 154 ? 0.1156 0.1276 0.1027 -0.0011 0.0000 0.0058 240 CYS A SG 1235 N N . SER A 155 ? 0.1015 0.1057 0.1041 0.0058 -0.0015 0.0064 241 SER A N 1236 C CA . SER A 155 ? 0.1244 0.1286 0.1111 -0.0008 -0.0057 0.0117 241 SER A CA 1237 C C . SER A 155 ? 0.1104 0.1090 0.1050 0.0043 0.0027 0.0180 241 SER A C 1238 O O . SER A 155 ? 0.1294 0.1443 0.1150 -0.0012 0.0090 0.0072 241 SER A O 1239 C CB . SER A 155 ? 0.1566 0.1325 0.1208 -0.0020 0.0083 -0.0047 241 SER A CB 1240 O OG . SER A 155 ? 0.2033 0.1761 0.1660 -0.0069 0.0010 0.0185 241 SER A OG 1241 N N . GLY A 156 ? 0.1102 0.1160 0.0905 0.0097 -0.0028 0.0100 242 GLY A N 1242 C CA . GLY A 156 ? 0.1174 0.1249 0.1031 0.0168 -0.0079 0.0095 242 GLY A CA 1243 C C . GLY A 156 ? 0.1159 0.1199 0.1079 0.0145 -0.0064 0.0006 242 GLY A C 1244 O O . GLY A 156 ? 0.1390 0.1465 0.1167 0.0293 -0.0093 0.0090 242 GLY A O 1245 N N . ALA A 157 ? 0.1083 0.1046 0.1037 0.0125 -0.0070 0.0087 243 ALA A N 1246 C CA . ALA A 157 ? 0.1035 0.1003 0.1097 0.0098 -0.0067 0.0134 243 ALA A CA 1247 C C . ALA A 157 ? 0.0941 0.1017 0.0907 0.0081 -0.0018 0.0094 243 ALA A C 1248 O O . ALA A 157 ? 0.0960 0.1038 0.1051 0.0146 -0.0019 0.0086 243 ALA A O 1249 C CB . ALA A 157 ? 0.1151 0.1157 0.1293 0.0021 0.0015 0.0136 243 ALA A CB 1250 N N . ALA A 158 ? 0.0964 0.0984 0.1029 0.0075 -0.0034 0.0107 244 ALA A N 1251 C CA . ALA A 158 ? 0.0989 0.0996 0.0921 0.0067 0.0006 0.0019 244 ALA A CA 1252 C C . ALA A 158 ? 0.0943 0.1025 0.0923 0.0056 -0.0034 0.0069 244 ALA A C 1253 O O . ALA A 158 ? 0.0934 0.1057 0.1025 0.0066 -0.0058 0.0055 244 ALA A O 1254 C CB . ALA A 158 ? 0.1202 0.1129 0.1065 0.0060 0.0000 0.0005 244 ALA A CB 1255 N N . SER A 159 ? 0.1019 0.1041 0.0967 0.0053 0.0028 0.0124 245 SER A N 1256 C CA . SER A 159 ? 0.1076 0.1085 0.0940 -0.0032 0.0091 0.0163 245 SER A CA 1257 C C . SER A 159 ? 0.1009 0.1051 0.0904 0.0061 0.0008 0.0034 245 SER A C 1258 O O . SER A 159 ? 0.0997 0.1218 0.1144 0.0107 -0.0006 0.0059 245 SER A O 1259 C CB . SER A 159 ? 0.1383 0.1426 0.1151 0.0012 0.0130 0.0129 245 SER A CB 1260 O OG . SER A 159 ? 0.1548 0.1669 0.1321 0.0144 -0.0015 0.0197 245 SER A OG 1261 N N . THR A 160 ? 0.0961 0.1100 0.0959 0.0030 -0.0033 0.0080 246 THR A N 1262 C CA . THR A 160 ? 0.0893 0.1020 0.0992 0.0032 0.0017 -0.0008 246 THR A CA 1263 C C . THR A 160 ? 0.0883 0.0928 0.0934 0.0027 0.0002 -0.0002 246 THR A C 1264 O O . THR A 160 ? 0.0921 0.1010 0.1023 0.0074 -0.0009 0.0043 246 THR A O 1265 C CB . THR A 160 ? 0.1046 0.1152 0.0970 0.0052 -0.0144 -0.0037 246 THR A CB 1266 O OG1 . THR A 160 ? 0.1229 0.1375 0.1110 0.0089 -0.0149 -0.0063 246 THR A OG1 1267 C CG2 . THR A 160 ? 0.1220 0.1344 0.1442 0.0000 -0.0194 -0.0127 246 THR A CG2 1268 N N . TYR A 161 ? 0.0884 0.0925 0.0900 0.0060 0.0013 0.0075 247 TYR A N 1269 C CA . TYR A 161 ? 0.0942 0.0964 0.0904 0.0070 -0.0037 0.0110 247 TYR A CA 1270 C C . TYR A 161 ? 0.0808 0.0891 0.0866 0.0088 -0.0016 0.0071 247 TYR A C 1271 O O . TYR A 161 ? 0.0926 0.1008 0.0888 0.0092 0.0021 0.0147 247 TYR A O 1272 C CB . TYR A 161 ? 0.0877 0.0983 0.0848 -0.0007 -0.0005 0.0074 247 TYR A CB 1273 C CG . TYR A 161 ? 0.0822 0.0899 0.0799 0.0048 -0.0015 0.0089 247 TYR A CG 1274 C CD1 . TYR A 161 ? 0.0863 0.0892 0.0820 0.0091 0.0090 -0.0001 247 TYR A CD1 1275 C CD2 . TYR A 161 ? 0.0834 0.0956 0.0864 -0.0061 -0.0041 0.0063 247 TYR A CD2 1276 C CE1 . TYR A 161 ? 0.0836 0.0975 0.0895 -0.0011 -0.0054 0.0011 247 TYR A CE1 1277 C CE2 . TYR A 161 ? 0.0917 0.0998 0.0857 0.0026 0.0046 0.0021 247 TYR A CE2 1278 C CZ . TYR A 161 ? 0.0853 0.1000 0.0941 0.0007 -0.0045 0.0056 247 TYR A CZ 1279 O OH . TYR A 161 ? 0.0944 0.1137 0.0934 0.0006 0.0054 -0.0019 247 TYR A OH 1280 N N . ARG A 162 ? 0.0780 0.0932 0.0905 0.0024 -0.0060 0.0084 248 ARG A N 1281 C CA . ARG A 162 ? 0.0896 0.1012 0.1043 -0.0054 -0.0029 0.0054 248 ARG A CA 1282 C C . ARG A 162 ? 0.0864 0.1014 0.0998 -0.0015 -0.0046 0.0114 248 ARG A C 1283 O O . ARG A 162 ? 0.0936 0.1126 0.1089 0.0083 0.0005 0.0155 248 ARG A O 1284 C CB A ARG A 162 ? 0.0932 0.1065 0.1168 -0.0052 -0.0031 0.0056 248 ARG A CB 1285 C CB B ARG A 162 ? 0.0990 0.1095 0.1261 -0.0051 -0.0056 0.0076 248 ARG A CB 1286 C CG A ARG A 162 ? 0.1051 0.1188 0.1303 -0.0015 0.0041 -0.0078 248 ARG A CG 1287 C CG B ARG A 162 ? 0.1249 0.1342 0.1358 0.0005 0.0151 0.0001 248 ARG A CG 1288 C CD A ARG A 162 ? 0.1670 0.1484 0.1612 0.0172 -0.0063 0.0066 248 ARG A CD 1289 C CD B ARG A 162 ? 0.1627 0.1384 0.1656 -0.0034 -0.0113 -0.0022 248 ARG A CD 1290 N NE A ARG A 162 ? 0.2011 0.1891 0.2154 -0.0054 0.0016 -0.0056 248 ARG A NE 1291 N NE B ARG A 162 ? 0.1496 0.1244 0.1316 -0.0091 0.0067 0.0050 248 ARG A NE 1292 C CZ A ARG A 162 ? 0.1802 0.1778 0.2283 -0.0151 0.0082 -0.0039 248 ARG A CZ 1293 C CZ B ARG A 162 ? 0.1590 0.1491 0.1560 -0.0014 0.0020 0.0040 248 ARG A CZ 1294 N NH1 A ARG A 162 ? 0.2100 0.1992 0.2351 0.0106 -0.0097 0.0014 248 ARG A NH1 1295 N NH1 B ARG A 162 ? 0.1874 0.2164 0.1937 -0.0107 -0.0055 0.0016 248 ARG A NH1 1296 N NH2 A ARG A 162 ? 0.1945 0.2137 0.2960 -0.0044 0.0007 0.0138 248 ARG A NH2 1297 N NH2 B ARG A 162 ? 0.1627 0.1737 0.1493 -0.0067 0.0041 0.0063 248 ARG A NH2 1298 N N . GLU A 163 ? 0.0939 0.0985 0.1054 0.0059 0.0024 0.0135 249 GLU A N 1299 C CA . GLU A 163 ? 0.1033 0.1105 0.1044 0.0108 0.0094 0.0114 249 GLU A CA 1300 C C . GLU A 163 ? 0.0895 0.1023 0.0889 0.0072 0.0003 0.0112 249 GLU A C 1301 O O . GLU A 163 ? 0.0956 0.1080 0.0968 0.0093 0.0053 0.0054 249 GLU A O 1302 C CB . GLU A 163 ? 0.1503 0.1383 0.1164 0.0136 0.0102 0.0065 249 GLU A CB 1303 C CG . GLU A 163 ? 0.2124 0.2269 0.1894 0.0090 0.0102 0.0218 249 GLU A CG 1304 C CD . GLU A 163 ? 0.3114 0.2731 0.2448 0.0037 -0.0162 0.0330 249 GLU A CD 1305 O OE1 . GLU A 163 ? 0.3718 0.3668 0.2779 -0.0369 -0.0228 0.0199 249 GLU A OE1 1306 O OE2 . GLU A 163 ? 0.3837 0.3183 0.3206 -0.0295 -0.0042 0.0568 249 GLU A OE2 1307 N N . LEU A 164 ? 0.0862 0.0989 0.1016 0.0025 -0.0029 0.0042 250 LEU A N 1308 C CA . LEU A 164 ? 0.0970 0.0964 0.0985 0.0000 -0.0046 -0.0025 250 LEU A CA 1309 C C . LEU A 164 ? 0.0946 0.0980 0.0990 -0.0015 0.0012 0.0065 250 LEU A C 1310 O O . LEU A 164 ? 0.0936 0.1020 0.1108 0.0017 -0.0110 0.0044 250 LEU A O 1311 C CB . LEU A 164 ? 0.0904 0.0955 0.0918 0.0021 -0.0029 0.0005 250 LEU A CB 1312 C CG . LEU A 164 ? 0.1067 0.1046 0.0951 -0.0006 -0.0070 0.0000 250 LEU A CG 1313 C CD1 . LEU A 164 ? 0.1124 0.1027 0.1074 -0.0063 -0.0037 -0.0006 250 LEU A CD1 1314 C CD2 . LEU A 164 ? 0.1244 0.1230 0.1078 0.0004 -0.0079 0.0064 250 LEU A CD2 1315 N N . THR A 165 ? 0.0973 0.0945 0.0952 0.0068 -0.0052 0.0073 251 THR A N 1316 C CA . THR A 165 ? 0.0898 0.0926 0.0822 -0.0016 -0.0036 0.0128 251 THR A CA 1317 C C . THR A 165 ? 0.0848 0.0879 0.0828 0.0044 -0.0045 0.0000 251 THR A C 1318 O O . THR A 165 ? 0.0940 0.0929 0.0916 0.0068 -0.0061 0.0015 251 THR A O 1319 C CB . THR A 165 ? 0.0853 0.1018 0.0916 0.0102 0.0066 0.0097 251 THR A CB 1320 O OG1 . THR A 165 ? 0.1121 0.1472 0.1085 0.0267 0.0057 0.0100 251 THR A OG1 1321 C CG2 . THR A 165 ? 0.1188 0.1096 0.0974 0.0239 0.0046 -0.0026 251 THR A CG2 1322 N N . ILE A 166 ? 0.0819 0.0864 0.0865 0.0071 -0.0029 -0.0005 252 ILE A N 1323 C CA . ILE A 166 ? 0.0898 0.1003 0.0920 0.0053 -0.0049 0.0003 252 ILE A CA 1324 C C . ILE A 166 ? 0.0902 0.1006 0.0965 0.0049 0.0047 0.0045 252 ILE A C 1325 O O . ILE A 166 ? 0.0977 0.1070 0.1063 0.0092 -0.0033 -0.0024 252 ILE A O 1326 C CB . ILE A 166 ? 0.0925 0.1054 0.1034 0.0019 0.0005 0.0026 252 ILE A CB 1327 C CG1 . ILE A 166 ? 0.1146 0.1189 0.1426 -0.0087 -0.0006 0.0076 252 ILE A CG1 1328 C CG2 . ILE A 166 ? 0.0975 0.1242 0.1127 -0.0060 -0.0018 -0.0073 252 ILE A CG2 1329 C CD1 . ILE A 166 ? 0.1398 0.1262 0.1614 -0.0152 0.0113 0.0042 252 ILE A CD1 1330 N N . TYR A 167 ? 0.0922 0.1004 0.0921 0.0111 0.0008 0.0004 253 TYR A N 1331 C CA . TYR A 167 ? 0.0992 0.1111 0.0932 0.0046 -0.0054 -0.0087 253 TYR A CA 1332 C C . TYR A 167 ? 0.0889 0.0980 0.0998 0.0044 -0.0110 -0.0089 253 TYR A C 1333 O O . TYR A 167 ? 0.1078 0.1023 0.1056 0.0139 -0.0042 -0.0082 253 TYR A O 1334 C CB . TYR A 167 ? 0.1160 0.1196 0.1089 0.0101 -0.0052 -0.0053 253 TYR A CB 1335 C CG . TYR A 167 ? 0.1157 0.1158 0.0935 0.0087 -0.0064 -0.0079 253 TYR A CG 1336 C CD1 . TYR A 167 ? 0.1838 0.1148 0.1231 -0.0045 0.0201 -0.0024 253 TYR A CD1 1337 C CD2 . TYR A 167 ? 0.0995 0.1117 0.1131 0.0118 -0.0077 -0.0040 253 TYR A CD2 1338 C CE1 . TYR A 167 ? 0.2124 0.1462 0.1371 -0.0050 0.0289 -0.0199 253 TYR A CE1 1339 C CE2 . TYR A 167 ? 0.1128 0.1265 0.1193 -0.0029 -0.0022 -0.0026 253 TYR A CE2 1340 C CZ . TYR A 167 ? 0.1456 0.1123 0.1125 -0.0055 0.0040 -0.0107 253 TYR A CZ 1341 O OH . TYR A 167 ? 0.1825 0.1445 0.1269 0.0057 0.0061 -0.0270 253 TYR A OH 1342 N N . ALA A 168 ? 0.0931 0.0959 0.0923 0.0084 -0.0048 -0.0033 254 ALA A N 1343 C CA . ALA A 168 ? 0.0969 0.0887 0.1075 0.0023 -0.0017 -0.0008 254 ALA A CA 1344 C C . ALA A 168 ? 0.0927 0.0888 0.0858 0.0033 -0.0003 0.0004 254 ALA A C 1345 O O . ALA A 168 ? 0.0918 0.0872 0.1003 0.0068 -0.0011 0.0026 254 ALA A O 1346 C CB . ALA A 168 ? 0.0981 0.0971 0.1154 -0.0079 -0.0007 0.0017 254 ALA A CB 1347 N N . LEU A 169 ? 0.0804 0.0818 0.0893 0.0056 -0.0020 0.0016 255 LEU A N 1348 C CA . LEU A 169 ? 0.0840 0.0918 0.0880 0.0028 -0.0012 0.0009 255 LEU A CA 1349 C C . LEU A 169 ? 0.0786 0.0829 0.0932 -0.0011 -0.0043 0.0058 255 LEU A C 1350 O O . LEU A 169 ? 0.1042 0.1295 0.1081 0.0167 -0.0032 0.0099 255 LEU A O 1351 C CB . LEU A 169 ? 0.0898 0.0955 0.0875 -0.0054 0.0018 -0.0073 255 LEU A CB 1352 C CG . LEU A 169 ? 0.1112 0.0959 0.1068 -0.0038 0.0089 -0.0044 255 LEU A CG 1353 C CD1 . LEU A 169 ? 0.1456 0.1152 0.1391 -0.0033 0.0335 -0.0069 255 LEU A CD1 1354 C CD2 . LEU A 169 ? 0.1293 0.1163 0.1250 0.0090 0.0126 -0.0042 255 LEU A CD2 1355 N N . LYS A 170 ? 0.0805 0.0862 0.0971 0.0071 0.0000 0.0000 256 LYS A N 1356 C CA . LYS A 170 ? 0.0913 0.0983 0.1004 0.0033 0.0039 0.0063 256 LYS A CA 1357 C C . LYS A 170 ? 0.0893 0.0831 0.0865 0.0032 -0.0029 -0.0056 256 LYS A C 1358 O O . LYS A 170 ? 0.0946 0.0992 0.1252 0.0057 -0.0013 -0.0004 256 LYS A O 1359 C CB . LYS A 170 ? 0.1029 0.1057 0.1170 0.0047 0.0175 0.0008 256 LYS A CB 1360 C CG . LYS A 170 ? 0.1258 0.1235 0.1389 -0.0070 0.0146 0.0026 256 LYS A CG 1361 C CD . LYS A 170 ? 0.1943 0.1593 0.1857 -0.0107 0.0136 0.0339 256 LYS A CD 1362 C CE . LYS A 170 ? 0.2523 0.1983 0.1982 0.0022 0.0217 0.0136 256 LYS A CE 1363 N NZ . LYS A 170 ? 0.3203 0.3137 0.2235 -0.0154 0.0441 0.0008 256 LYS A NZ 1364 N N . GLN A 171 ? 0.0859 0.0918 0.0936 0.0048 0.0010 -0.0032 257 GLN A N 1365 C CA . GLN A 171 ? 0.0864 0.0924 0.0849 -0.0046 0.0004 -0.0029 257 GLN A CA 1366 C C . GLN A 171 ? 0.0835 0.0908 0.0871 0.0084 -0.0044 -0.0043 257 GLN A C 1367 O O . GLN A 171 ? 0.1247 0.0974 0.1034 0.0135 0.0011 -0.0090 257 GLN A O 1368 C CB . GLN A 171 ? 0.0868 0.0868 0.0942 -0.0018 -0.0028 -0.0076 257 GLN A CB 1369 C CG . GLN A 171 ? 0.1045 0.1229 0.1103 0.0085 -0.0115 -0.0207 257 GLN A CG 1370 C CD . GLN A 171 ? 0.1993 0.1865 0.1302 0.0103 -0.0025 -0.0051 257 GLN A CD 1371 O OE1 . GLN A 171 ? 0.2706 0.2022 0.1618 0.0338 0.0131 -0.0245 257 GLN A OE1 1372 N NE2 . GLN A 171 ? 0.2905 0.2489 0.2610 0.0146 0.0597 -0.0033 257 GLN A NE2 1373 N N . LEU A 172 ? 0.0829 0.0822 0.0870 0.0007 -0.0007 -0.0009 258 LEU A N 1374 C CA . LEU A 172 ? 0.0888 0.0767 0.0876 -0.0001 -0.0062 0.0053 258 LEU A CA 1375 C C . LEU A 172 ? 0.0879 0.0819 0.0869 -0.0019 0.0019 -0.0050 258 LEU A C 1376 O O . LEU A 172 ? 0.0870 0.0953 0.0908 0.0103 -0.0029 -0.0049 258 LEU A O 1377 C CB . LEU A 172 ? 0.0907 0.0912 0.0916 0.0031 -0.0072 -0.0054 258 LEU A CB 1378 C CG . LEU A 172 ? 0.1001 0.0888 0.0908 -0.0040 -0.0014 -0.0008 258 LEU A CG 1379 C CD1 . LEU A 172 ? 0.1128 0.1245 0.1085 0.0012 -0.0081 -0.0030 258 LEU A CD1 1380 C CD2 . LEU A 172 ? 0.1118 0.1070 0.1192 -0.0220 -0.0027 -0.0010 258 LEU A CD2 1381 N N . ASP A 173 ? 0.0847 0.0895 0.0883 -0.0008 -0.0069 -0.0009 259 ASP A N 1382 C CA . ASP A 173 ? 0.0855 0.0922 0.0968 -0.0026 -0.0046 -0.0039 259 ASP A CA 1383 C C . ASP A 173 ? 0.0839 0.0946 0.0895 0.0007 0.0046 -0.0045 259 ASP A C 1384 O O . ASP A 173 ? 0.1145 0.1111 0.1113 0.0088 0.0152 0.0021 259 ASP A O 1385 C CB . ASP A 173 ? 0.0857 0.0943 0.0997 -0.0023 -0.0056 0.0018 259 ASP A CB 1386 C CG . ASP A 173 ? 0.1020 0.0941 0.1012 0.0035 0.0079 0.0011 259 ASP A CG 1387 O OD1 . ASP A 173 ? 0.0911 0.0968 0.0986 -0.0007 -0.0002 -0.0007 259 ASP A OD1 1388 O OD2 . ASP A 173 ? 0.1089 0.1204 0.1115 -0.0063 0.0042 0.0081 259 ASP A OD2 1389 N N . LEU A 174 ? 0.0859 0.0869 0.0903 0.0039 0.0032 -0.0027 260 LEU A N 1390 C CA . LEU A 174 ? 0.0875 0.0903 0.0914 0.0011 0.0035 -0.0115 260 LEU A CA 1391 C C . LEU A 174 ? 0.0751 0.0818 0.0878 0.0018 -0.0011 -0.0065 260 LEU A C 1392 O O . LEU A 174 ? 0.0827 0.0871 0.0897 0.0046 -0.0019 -0.0051 260 LEU A O 1393 C CB . LEU A 174 ? 0.0985 0.0966 0.0956 -0.0031 -0.0065 -0.0031 260 LEU A CB 1394 C CG . LEU A 174 ? 0.0992 0.0996 0.0944 0.0032 -0.0107 -0.0064 260 LEU A CG 1395 C CD1 . LEU A 174 ? 0.1187 0.1327 0.1186 -0.0240 -0.0113 -0.0132 260 LEU A CD1 1396 C CD2 . LEU A 174 ? 0.1055 0.1048 0.1026 0.0087 -0.0091 -0.0063 260 LEU A CD2 1397 N N . PRO A 175 ? 0.0792 0.0821 0.0804 0.0084 0.0021 -0.0038 261 PRO A N 1398 C CA . PRO A 175 ? 0.0748 0.0844 0.0882 0.0094 -0.0051 -0.0065 261 PRO A CA 1399 C C . PRO A 175 ? 0.0709 0.0805 0.0850 0.0083 -0.0085 -0.0137 261 PRO A C 1400 O O . PRO A 175 ? 0.0914 0.1045 0.0943 -0.0047 -0.0087 -0.0109 261 PRO A O 1401 C CB . PRO A 175 ? 0.0963 0.0974 0.1081 0.0112 -0.0057 -0.0075 261 PRO A CB 1402 C CG . PRO A 175 ? 0.1071 0.1089 0.1246 0.0163 -0.0022 -0.0087 261 PRO A CG 1403 C CD . PRO A 175 ? 0.0968 0.1101 0.0977 0.0059 0.0061 -0.0133 261 PRO A CD 1404 N N . HIS A 176 ? 0.0772 0.0791 0.0895 0.0031 0.0005 -0.0053 262 HIS A N 1405 C CA . HIS A 176 ? 0.0843 0.0753 0.0928 0.0097 -0.0048 -0.0021 262 HIS A CA 1406 C C . HIS A 176 ? 0.0772 0.0808 0.0845 0.0071 -0.0054 -0.0052 262 HIS A C 1407 O O . HIS A 176 ? 0.0840 0.0839 0.0848 0.0081 -0.0014 -0.0032 262 HIS A O 1408 C CB . HIS A 176 ? 0.0851 0.0772 0.0931 0.0092 -0.0004 -0.0033 262 HIS A CB 1409 C CG . HIS A 176 ? 0.0839 0.0784 0.0840 0.0166 -0.0021 -0.0050 262 HIS A CG 1410 N ND1 . HIS A 176 ? 0.0888 0.0895 0.0901 0.0064 0.0026 -0.0044 262 HIS A ND1 1411 C CD2 . HIS A 176 ? 0.0868 0.0694 0.0806 0.0078 0.0047 -0.0044 262 HIS A CD2 1412 C CE1 . HIS A 176 ? 0.0833 0.0891 0.0886 0.0026 -0.0039 0.0007 262 HIS A CE1 1413 N NE2 . HIS A 176 ? 0.0830 0.0785 0.0838 0.0019 -0.0006 -0.0063 262 HIS A NE2 1414 N N . VAL A 177 ? 0.0722 0.0776 0.0833 0.0072 0.0026 -0.0045 263 VAL A N 1415 C CA . VAL A 177 ? 0.0736 0.0698 0.0855 0.0087 -0.0030 -0.0060 263 VAL A CA 1416 C C . VAL A 177 ? 0.0733 0.0730 0.0783 0.0059 0.0032 -0.0069 263 VAL A C 1417 O O . VAL A 177 ? 0.0808 0.0760 0.0908 0.0036 0.0042 -0.0059 263 VAL A O 1418 C CB . VAL A 177 ? 0.0789 0.0779 0.0843 -0.0002 0.0011 -0.0010 263 VAL A CB 1419 C CG1 . VAL A 177 ? 0.0831 0.1051 0.0912 0.0141 0.0015 -0.0072 263 VAL A CG1 1420 C CG2 . VAL A 177 ? 0.0929 0.1026 0.1000 -0.0006 -0.0025 -0.0107 263 VAL A CG2 1421 N N . ALA A 178 ? 0.0719 0.0730 0.0796 0.0032 0.0037 -0.0036 264 ALA A N 1422 C CA . ALA A 178 ? 0.0741 0.0701 0.0793 0.0022 0.0012 -0.0016 264 ALA A CA 1423 C C . ALA A 178 ? 0.0772 0.0767 0.0853 -0.0011 0.0023 -0.0020 264 ALA A C 1424 O O . ALA A 178 ? 0.0786 0.0807 0.1097 0.0038 0.0032 0.0036 264 ALA A O 1425 C CB . ALA A 178 ? 0.0840 0.0766 0.0885 0.0037 0.0044 0.0014 264 ALA A CB 1426 N N . MET A 179 ? 0.0692 0.0744 0.0812 0.0015 -0.0009 -0.0009 265 MET A N 1427 C CA . MET A 179 ? 0.0720 0.0748 0.0809 0.0047 0.0006 -0.0027 265 MET A CA 1428 C C . MET A 179 ? 0.0660 0.0682 0.0706 0.0008 -0.0008 -0.0025 265 MET A C 1429 O O . MET A 179 ? 0.0711 0.0776 0.0909 0.0001 0.0017 0.0019 265 MET A O 1430 C CB . MET A 179 ? 0.0729 0.0708 0.0878 0.0102 0.0055 -0.0074 265 MET A CB 1431 C CG . MET A 179 ? 0.0768 0.0754 0.0946 -0.0046 0.0030 -0.0071 265 MET A CG 1432 S SD . MET A 179 ? 0.0835 0.0874 0.0813 0.0046 0.0018 -0.0022 265 MET A SD 1433 C CE . MET A 179 ? 0.1006 0.0929 0.0979 0.0105 0.0023 -0.0052 265 MET A CE 1434 N N . TYR A 180 ? 0.0660 0.0691 0.0709 0.0032 -0.0012 -0.0033 266 TYR A N 1435 C CA . TYR A 180 ? 0.0712 0.0696 0.0760 0.0010 -0.0028 -0.0033 266 TYR A CA 1436 C C . TYR A 180 ? 0.0683 0.0671 0.0726 -0.0019 -0.0012 -0.0011 266 TYR A C 1437 O O . TYR A 180 ? 0.0721 0.0738 0.0853 0.0020 -0.0072 0.0030 266 TYR A O 1438 C CB . TYR A 180 ? 0.0719 0.0739 0.0755 -0.0001 -0.0009 -0.0023 266 TYR A CB 1439 C CG . TYR A 180 ? 0.0714 0.0709 0.0741 0.0027 -0.0002 -0.0025 266 TYR A CG 1440 C CD1 . TYR A 180 ? 0.0757 0.0825 0.0783 0.0066 0.0001 -0.0066 266 TYR A CD1 1441 C CD2 . TYR A 180 ? 0.0733 0.0754 0.0825 0.0063 0.0008 -0.0055 266 TYR A CD2 1442 C CE1 . TYR A 180 ? 0.0861 0.0756 0.0869 0.0082 -0.0064 -0.0001 266 TYR A CE1 1443 C CE2 . TYR A 180 ? 0.0731 0.0772 0.0744 -0.0006 0.0033 -0.0046 266 TYR A CE2 1444 C CZ . TYR A 180 ? 0.0699 0.0855 0.0759 0.0034 -0.0042 0.0004 266 TYR A CZ 1445 O OH . TYR A 180 ? 0.0855 0.0845 0.0897 0.0060 -0.0089 0.0051 266 TYR A OH 1446 N N . MET A 181 ? 0.0631 0.0724 0.0758 -0.0003 -0.0014 0.0012 267 MET A N 1447 C CA . MET A 181 ? 0.0745 0.0732 0.0776 0.0015 -0.0043 0.0004 267 MET A CA 1448 C C . MET A 181 ? 0.0686 0.0683 0.0671 0.0009 -0.0009 0.0018 267 MET A C 1449 O O . MET A 181 ? 0.0677 0.0740 0.0757 -0.0005 -0.0010 -0.0032 267 MET A O 1450 C CB . MET A 181 ? 0.0729 0.0854 0.0765 -0.0012 0.0066 -0.0028 267 MET A CB 1451 C CG . MET A 181 ? 0.0845 0.0821 0.0850 0.0019 0.0029 -0.0062 267 MET A CG 1452 S SD . MET A 181 ? 0.1014 0.0990 0.0855 -0.0070 0.0063 0.0019 267 MET A SD 1453 C CE . MET A 181 ? 0.1241 0.1388 0.1183 -0.0165 0.0077 0.0083 267 MET A CE 1454 N N . ASP A 182 ? 0.0703 0.0734 0.0710 0.0010 0.0009 -0.0034 268 ASP A N 1455 C CA . ASP A 182 ? 0.0707 0.0762 0.0772 -0.0027 0.0010 -0.0019 268 ASP A CA 1456 C C . ASP A 182 ? 0.0686 0.0686 0.0615 0.0067 0.0018 0.0046 268 ASP A C 1458 C CB . ASP A 182 ? 0.0772 0.0763 0.0727 -0.0044 -0.0019 -0.0091 268 ASP A CB 1459 C CG . ASP A 182 ? 0.0774 0.0680 0.0678 -0.0017 -0.0033 0.0002 268 ASP A CG 1460 O OD1 . ASP A 182 ? 0.1024 0.0938 0.0899 -0.0035 0.0146 -0.0056 268 ASP A OD1 1461 O OD2 . ASP A 182 ? 0.0819 0.0866 0.0813 0.0087 -0.0044 -0.0069 268 ASP A OD2 1462 N N . ALA A 183 ? 0.0726 0.0682 0.0637 0.0012 0.0012 0.0020 269 ALA A N 1463 C CA . ALA A 183 ? 0.0747 0.0730 0.0742 -0.0044 -0.0023 0.0037 269 ALA A CA 1464 C C . ALA A 183 ? 0.0783 0.0656 0.0633 -0.0017 -0.0049 0.0013 269 ALA A C 1465 O O . ALA A 183 ? 0.0871 0.0771 0.0807 -0.0028 0.0043 -0.0029 269 ALA A O 1466 C CB . ALA A 183 ? 0.0792 0.0792 0.0863 0.0001 -0.0044 0.0028 269 ALA A CB 1467 N N . GLY A 184 ? 0.0758 0.0767 0.0689 0.0020 0.0022 -0.0036 270 GLY A N 1468 C CA . GLY A 184 ? 0.0772 0.0741 0.0773 0.0044 -0.0021 -0.0003 270 GLY A CA 1469 C C . GLY A 184 ? 0.0665 0.0676 0.0730 0.0065 -0.0023 0.0005 270 GLY A C 1470 O O . GLY A 184 ? 0.0804 0.0735 0.0751 0.0042 0.0016 0.0040 270 GLY A O 1471 N N . HIS A 185 ? 0.0765 0.0742 0.0744 0.0076 -0.0009 0.0030 271 HIS A N 1472 C CA . HIS A 185 ? 0.0824 0.0738 0.0740 0.0088 -0.0020 0.0046 271 HIS A CA 1473 C C . HIS A 185 ? 0.0712 0.0749 0.0687 0.0076 -0.0021 0.0026 271 HIS A C 1474 O O . HIS A 185 ? 0.0847 0.0790 0.0739 0.0056 0.0005 0.0030 271 HIS A O 1475 C CB . HIS A 185 ? 0.0820 0.0723 0.0820 0.0039 0.0037 -0.0036 271 HIS A CB 1476 C CG . HIS A 185 ? 0.0886 0.0839 0.0744 -0.0017 0.0045 -0.0039 271 HIS A CG 1477 N ND1 . HIS A 185 ? 0.0884 0.0840 0.0880 0.0052 0.0036 0.0016 271 HIS A ND1 1478 C CD2 . HIS A 185 ? 0.0840 0.0941 0.0987 0.0074 0.0033 -0.0058 271 HIS A CD2 1479 C CE1 . HIS A 185 ? 0.0883 0.0878 0.0985 0.0008 0.0022 0.0040 271 HIS A CE1 1480 N NE2 . HIS A 185 ? 0.0904 0.1082 0.0997 0.0037 0.0011 -0.0020 271 HIS A NE2 1481 N N . ALA A 186 ? 0.0790 0.0714 0.0740 0.0031 -0.0004 -0.0010 272 ALA A N 1482 C CA . ALA A 186 ? 0.0797 0.0777 0.0800 -0.0006 0.0003 0.0000 272 ALA A CA 1483 C C . ALA A 186 ? 0.0857 0.0753 0.0770 -0.0021 0.0045 0.0017 272 ALA A C 1484 O O . ALA A 186 ? 0.0944 0.0850 0.1003 0.0025 -0.0012 0.0048 272 ALA A O 1485 C CB . ALA A 186 ? 0.0823 0.0822 0.0915 0.0074 -0.0010 -0.0039 272 ALA A CB 1486 N N . GLY A 187 ? 0.0805 0.0751 0.0804 0.0095 0.0022 -0.0016 273 GLY A N 1487 C CA . GLY A 187 ? 0.0786 0.0813 0.0861 0.0049 0.0043 -0.0005 273 GLY A CA 1488 C C . GLY A 187 ? 0.0795 0.0837 0.0912 0.0052 -0.0016 0.0008 273 GLY A C 1489 O O . GLY A 187 ? 0.0906 0.1015 0.1008 0.0041 -0.0056 0.0008 273 GLY A O 1490 N N . TRP A 188 ? 0.0862 0.0819 0.0841 0.0027 -0.0009 0.0048 274 TRP A N 1491 C CA . TRP A 188 ? 0.0818 0.0812 0.0771 0.0035 -0.0069 0.0068 274 TRP A CA 1492 C C . TRP A 188 ? 0.0952 0.0755 0.0864 0.0046 -0.0023 0.0049 274 TRP A C 1493 O O . TRP A 188 ? 0.1131 0.0974 0.1093 0.0072 0.0145 0.0134 274 TRP A O 1494 C CB . TRP A 188 ? 0.0793 0.0903 0.0877 -0.0016 -0.0023 0.0098 274 TRP A CB 1495 C CG . TRP A 188 ? 0.0900 0.0891 0.0864 0.0083 0.0022 0.0104 274 TRP A CG 1496 C CD1 . TRP A 188 ? 0.1008 0.0915 0.0813 0.0001 -0.0102 -0.0038 274 TRP A CD1 1497 C CD2 . TRP A 188 ? 0.0910 0.0874 0.0875 0.0000 0.0070 0.0073 274 TRP A CD2 1498 N NE1 . TRP A 188 ? 0.1064 0.1041 0.0858 0.0054 -0.0013 0.0095 274 TRP A NE1 1499 C CE2 . TRP A 188 ? 0.0920 0.0936 0.0941 0.0093 -0.0019 -0.0033 274 TRP A CE2 1500 C CE3 . TRP A 188 ? 0.1058 0.0987 0.0884 -0.0019 0.0025 -0.0014 274 TRP A CE3 1501 C CZ2 . TRP A 188 ? 0.1097 0.1110 0.0936 0.0077 -0.0067 0.0053 274 TRP A CZ2 1502 C CZ3 . TRP A 188 ? 0.1348 0.1073 0.1068 -0.0013 -0.0063 0.0053 274 TRP A CZ3 1503 C CH2 . TRP A 188 ? 0.1231 0.1149 0.1003 -0.0077 -0.0069 -0.0046 274 TRP A CH2 1504 N N . LEU A 189 ? 0.0879 0.0821 0.0916 0.0011 0.0038 0.0087 275 LEU A N 1505 C CA . LEU A 189 ? 0.0892 0.0832 0.0855 0.0015 -0.0032 0.0079 275 LEU A CA 1506 C C . LEU A 189 ? 0.0926 0.0861 0.1046 0.0021 0.0064 0.0045 275 LEU A C 1507 O O . LEU A 189 ? 0.1079 0.1042 0.1094 -0.0061 0.0111 -0.0060 275 LEU A O 1508 C CB . LEU A 189 ? 0.0856 0.0933 0.0976 -0.0010 0.0037 0.0032 275 LEU A CB 1509 C CG . LEU A 189 ? 0.0956 0.0876 0.0884 -0.0001 0.0000 0.0097 275 LEU A CG 1510 C CD1 . LEU A 189 ? 0.0850 0.0908 0.0942 -0.0051 -0.0024 0.0068 275 LEU A CD1 1511 C CD2 . LEU A 189 ? 0.1015 0.1127 0.0961 0.0091 -0.0022 0.0000 275 LEU A CD2 1512 N N . GLY A 190 ? 0.0923 0.0869 0.0935 -0.0008 0.0008 0.0033 276 GLY A N 1513 C CA . GLY A 190 ? 0.0965 0.0923 0.0956 0.0102 0.0030 0.0004 276 GLY A CA 1514 C C . GLY A 190 ? 0.0900 0.1007 0.1067 0.0027 0.0041 -0.0052 276 GLY A C 1515 O O . GLY A 190 ? 0.1207 0.1156 0.1161 0.0142 -0.0041 -0.0116 276 GLY A O 1516 N N . TRP A 191 ? 0.0995 0.0859 0.0992 0.0050 -0.0012 0.0027 277 TRP A N 1517 C CA . TRP A 191 ? 0.1091 0.0945 0.0948 0.0085 0.0004 0.0055 277 TRP A CA 1518 C C . TRP A 191 ? 0.1176 0.0992 0.1055 0.0026 0.0150 -0.0058 277 TRP A C 1519 O O . TRP A 191 ? 0.1148 0.1074 0.1087 0.0092 0.0119 -0.0020 277 TRP A O 1520 C CB . TRP A 191 ? 0.1170 0.0885 0.1074 0.0108 0.0007 0.0048 277 TRP A CB 1521 C CG . TRP A 191 ? 0.1066 0.1023 0.1090 0.0060 -0.0007 -0.0003 277 TRP A CG 1522 C CD1 . TRP A 191 ? 0.1120 0.1105 0.1264 0.0076 -0.0121 -0.0018 277 TRP A CD1 1523 C CD2 . TRP A 191 ? 0.1061 0.0887 0.1109 0.0150 0.0000 0.0054 277 TRP A CD2 1524 N NE1 . TRP A 191 ? 0.1131 0.1016 0.1209 0.0025 0.0020 -0.0017 277 TRP A NE1 1525 C CE2 . TRP A 191 ? 0.1074 0.1078 0.1141 0.0080 0.0051 0.0000 277 TRP A CE2 1526 C CE3 . TRP A 191 ? 0.1090 0.1020 0.1109 0.0117 0.0070 -0.0029 277 TRP A CE3 1527 C CZ2 . TRP A 191 ? 0.1090 0.1166 0.1324 -0.0005 0.0032 0.0023 277 TRP A CZ2 1528 C CZ3 . TRP A 191 ? 0.1274 0.1048 0.1306 0.0081 0.0097 -0.0070 277 TRP A CZ3 1529 C CH2 . TRP A 191 ? 0.1122 0.1258 0.1220 0.0131 0.0152 -0.0050 277 TRP A CH2 1530 N N . PRO A 192 ? 0.1312 0.1159 0.1172 -0.0098 0.0236 -0.0080 278 PRO A N 1531 C CA . PRO A 192 ? 0.1512 0.1315 0.1474 -0.0166 0.0093 -0.0143 278 PRO A CA 1532 C C . PRO A 192 ? 0.1438 0.1132 0.1210 -0.0095 0.0354 -0.0097 278 PRO A C 1533 O O . PRO A 192 ? 0.1593 0.1638 0.1749 -0.0080 0.0329 -0.0070 278 PRO A O 1534 C CB . PRO A 192 ? 0.1858 0.1488 0.1621 -0.0291 0.0188 -0.0199 278 PRO A CB 1535 C CG . PRO A 192 ? 0.1845 0.1500 0.1479 -0.0141 0.0229 -0.0259 278 PRO A CG 1536 C CD . PRO A 192 ? 0.1646 0.1220 0.1391 -0.0062 0.0225 -0.0108 278 PRO A CD 1537 N N . ALA A 193 ? 0.1586 0.1250 0.1318 -0.0097 0.0337 0.0002 279 ALA A N 1538 C CA . ALA A 193 ? 0.1715 0.1450 0.1401 -0.0096 0.0239 -0.0022 279 ALA A CA 1539 C C . ALA A 193 ? 0.1759 0.1410 0.1206 0.0000 0.0356 0.0083 279 ALA A C 1540 O O . ALA A 193 ? 0.2140 0.1412 0.1359 -0.0133 0.0285 0.0141 279 ALA A O 1541 C CB . ALA A 193 ? 0.2025 0.1500 0.1739 0.0135 0.0114 0.0044 279 ALA A CB 1542 N N . ASN A 194 ? 0.1514 0.1109 0.1282 0.0000 0.0230 0.0101 280 ASN A N 1543 C CA . ASN A 194 ? 0.1342 0.1063 0.1159 -0.0005 0.0248 -0.0034 280 ASN A CA 1544 C C . ASN A 194 ? 0.1394 0.1087 0.1104 -0.0147 0.0190 -0.0046 280 ASN A C 1545 O O . ASN A 194 ? 0.1437 0.1129 0.1208 -0.0035 0.0242 -0.0059 280 ASN A O 1546 C CB . ASN A 194 ? 0.1359 0.1019 0.1124 0.0013 0.0215 0.0068 280 ASN A CB 1547 C CG . ASN A 194 ? 0.1343 0.1032 0.1080 0.0065 0.0017 0.0151 280 ASN A CG 1548 O OD1 . ASN A 194 ? 0.1722 0.1445 0.1319 0.0023 -0.0008 0.0299 280 ASN A OD1 1549 N ND2 . ASN A 194 ? 0.1297 0.1062 0.1137 -0.0059 0.0091 0.0013 280 ASN A ND2 1550 N N . ILE A 195 ? 0.1337 0.0996 0.1142 0.0061 0.0110 0.0015 281 ILE A N 1551 C CA . ILE A 195 ? 0.1303 0.1132 0.0963 -0.0129 0.0044 -0.0101 281 ILE A CA 1552 C C . ILE A 195 ? 0.1260 0.1041 0.1189 -0.0047 0.0010 0.0049 281 ILE A C 1553 O O . ILE A 195 ? 0.1272 0.1167 0.1138 0.0014 0.0003 0.0000 281 ILE A O 1554 C CB . ILE A 195 ? 0.1421 0.1154 0.1193 0.0037 -0.0042 -0.0032 281 ILE A CB 1555 C CG1 . ILE A 195 ? 0.1247 0.1118 0.1372 0.0044 -0.0051 -0.0019 281 ILE A CG1 1556 C CG2 . ILE A 195 ? 0.1482 0.1288 0.1342 -0.0057 0.0030 -0.0033 281 ILE A CG2 1557 C CD1 . ILE A 195 ? 0.1332 0.1189 0.1180 0.0046 0.0028 0.0074 281 ILE A CD1 1558 N N . GLN A 196 ? 0.1495 0.1103 0.1291 -0.0027 0.0211 -0.0087 282 GLN A N 1559 C CA . GLN A 196 ? 0.1367 0.1095 0.1293 -0.0062 0.0070 -0.0016 282 GLN A CA 1560 C C . GLN A 196 ? 0.1332 0.1102 0.1219 -0.0123 0.0079 0.0134 282 GLN A C 1561 O O . GLN A 196 ? 0.1156 0.0937 0.1181 -0.0003 0.0071 0.0055 282 GLN A O 1562 C CB . GLN A 196 ? 0.1603 0.1355 0.1565 -0.0297 0.0189 -0.0127 282 GLN A CB 1563 C CG . GLN A 196 ? 0.1954 0.2064 0.2103 -0.0127 0.0047 -0.0020 282 GLN A CG 1564 C CD . GLN A 196 ? 0.3191 0.2865 0.3228 -0.0147 0.0113 0.0035 282 GLN A CD 1565 O OE1 . GLN A 196 ? 0.4188 0.3677 0.3913 -0.0379 -0.0092 -0.0181 282 GLN A OE1 1566 N NE2 . GLN A 196 ? 0.3150 0.3129 0.3357 -0.0033 0.0002 0.0245 282 GLN A NE2 1567 N N . PRO A 197 ? 0.1171 0.1036 0.1149 0.0023 0.0155 -0.0033 283 PRO A N 1568 C CA . PRO A 197 ? 0.1186 0.1074 0.1148 0.0038 0.0069 0.0133 283 PRO A CA 1569 C C . PRO A 197 ? 0.1000 0.0930 0.0945 0.0040 0.0115 0.0068 283 PRO A C 1570 O O . PRO A 197 ? 0.1165 0.1042 0.0944 0.0046 0.0081 0.0061 283 PRO A O 1571 C CB . PRO A 197 ? 0.1399 0.1194 0.1542 -0.0004 -0.0063 0.0099 283 PRO A CB 1572 C CG . PRO A 197 ? 0.1743 0.1728 0.1573 0.0241 0.0137 -0.0050 283 PRO A CG 1573 C CD . PRO A 197 ? 0.1231 0.1157 0.1432 -0.0028 0.0153 0.0077 283 PRO A CD 1574 N N . ALA A 198 ? 0.1071 0.0985 0.0989 0.0011 0.0058 0.0018 284 ALA A N 1575 C CA . ALA A 198 ? 0.1038 0.0902 0.0891 -0.0093 0.0075 0.0081 284 ALA A CA 1576 C C . ALA A 198 ? 0.0993 0.0845 0.0821 -0.0060 0.0058 0.0062 284 ALA A C 1577 O O . ALA A 198 ? 0.0996 0.0896 0.0907 -0.0033 0.0060 0.0028 284 ALA A O 1578 C CB . ALA A 198 ? 0.1020 0.0979 0.1012 -0.0060 0.0036 0.0040 284 ALA A CB 1579 N N . ALA A 199 ? 0.1020 0.0865 0.0895 0.0010 0.0035 -0.0018 285 ALA A N 1580 C CA . ALA A 199 ? 0.0985 0.0905 0.0906 -0.0072 -0.0035 -0.0058 285 ALA A CA 1581 C C . ALA A 199 ? 0.0856 0.0820 0.0946 -0.0051 -0.0066 -0.0004 285 ALA A C 1582 O O . ALA A 199 ? 0.0947 0.0908 0.1057 -0.0029 0.0061 0.0020 285 ALA A O 1583 C CB . ALA A 199 ? 0.1027 0.0985 0.0994 0.0015 0.0013 -0.0012 285 ALA A CB 1584 N N . GLU A 200 ? 0.0941 0.0896 0.0997 0.0021 0.0029 0.0003 286 GLU A N 1585 C CA . GLU A 200 ? 0.1035 0.1000 0.0981 -0.0029 0.0035 0.0075 286 GLU A CA 1586 C C . GLU A 200 ? 0.0906 0.0884 0.0890 0.0022 0.0083 0.0058 286 GLU A C 1587 O O . GLU A 200 ? 0.1001 0.0998 0.1029 -0.0086 0.0060 -0.0010 286 GLU A O 1588 C CB . GLU A 200 ? 0.1193 0.1057 0.1098 -0.0039 0.0019 0.0077 286 GLU A CB 1589 C CG . GLU A 200 ? 0.1608 0.1332 0.1394 0.0001 0.0096 0.0098 286 GLU A CG 1590 C CD . GLU A 200 ? 0.1899 0.1613 0.1767 0.0005 -0.0087 0.0186 286 GLU A CD 1591 O OE1 . GLU A 200 ? 0.1916 0.1814 0.2034 -0.0097 -0.0082 0.0086 286 GLU A OE1 1592 O OE2 . GLU A 200 ? 0.2084 0.2263 0.2299 -0.0106 -0.0256 0.0182 286 GLU A OE2 1593 N N . LEU A 201 ? 0.0921 0.0871 0.0951 0.0024 0.0038 -0.0058 287 LEU A N 1594 C CA . LEU A 201 ? 0.0892 0.0890 0.0816 -0.0003 0.0046 0.0005 287 LEU A CA 1595 C C . LEU A 201 ? 0.0874 0.0907 0.0954 -0.0016 0.0036 -0.0040 287 LEU A C 1596 O O . LEU A 201 ? 0.0937 0.0915 0.0929 -0.0052 0.0041 -0.0009 287 LEU A O 1597 C CB A LEU A 201 ? 0.0884 0.0995 0.1019 0.0088 -0.0009 0.0020 287 LEU A CB 1598 C CB B LEU A 201 ? 0.0879 0.0988 0.1035 0.0081 -0.0006 0.0022 287 LEU A CB 1599 C CG A LEU A 201 ? 0.0888 0.1146 0.1302 0.0097 -0.0037 -0.0024 287 LEU A CG 1600 C CG B LEU A 201 ? 0.0904 0.1179 0.1259 0.0051 -0.0133 -0.0056 287 LEU A CG 1601 C CD1 A LEU A 201 ? 0.1303 0.1535 0.1607 -0.0160 0.0089 0.0042 287 LEU A CD1 1602 C CD1 B LEU A 201 ? 0.1613 0.1373 0.1581 -0.0085 -0.0042 0.0019 287 LEU A CD1 1603 C CD2 A LEU A 201 ? 0.0921 0.1238 0.1537 -0.0140 -0.0076 -0.0084 287 LEU A CD2 1604 C CD2 B LEU A 201 ? 0.1400 0.1612 0.1698 -0.0044 -0.0028 -0.0027 287 LEU A CD2 1605 N N . PHE A 202 ? 0.0782 0.0858 0.0875 0.0061 0.0002 -0.0008 288 PHE A N 1606 C CA . PHE A 202 ? 0.0749 0.0768 0.0805 -0.0040 -0.0028 -0.0038 288 PHE A CA 1607 C C . PHE A 202 ? 0.0730 0.0798 0.0835 -0.0044 -0.0025 0.0007 288 PHE A C 1608 O O . PHE A 202 ? 0.0879 0.0878 0.0952 -0.0032 -0.0009 -0.0023 288 PHE A O 1609 C CB . PHE A 202 ? 0.0857 0.0890 0.0948 -0.0077 -0.0095 -0.0027 288 PHE A CB 1610 C CG . PHE A 202 ? 0.0793 0.0823 0.0868 -0.0053 0.0022 0.0019 288 PHE A CG 1611 C CD1 . PHE A 202 ? 0.0895 0.0958 0.1016 -0.0005 -0.0022 -0.0005 288 PHE A CD1 1612 C CD2 . PHE A 202 ? 0.1043 0.0954 0.1167 -0.0087 0.0081 0.0043 288 PHE A CD2 1613 C CE1 . PHE A 202 ? 0.0975 0.0836 0.1079 -0.0134 0.0074 0.0000 288 PHE A CE1 1614 C CE2 . PHE A 202 ? 0.1007 0.1098 0.1207 0.0038 0.0166 0.0057 288 PHE A CE2 1615 C CZ . PHE A 202 ? 0.0956 0.1042 0.1083 -0.0059 0.0066 0.0095 288 PHE A CZ 1616 N N . ALA A 203 ? 0.0773 0.0856 0.0939 -0.0071 0.0071 0.0009 289 ALA A N 1617 C CA . ALA A 203 ? 0.0832 0.0884 0.0989 -0.0047 0.0044 0.0000 289 ALA A CA 1618 C C . ALA A 203 ? 0.0844 0.0848 0.1098 -0.0094 0.0059 -0.0024 289 ALA A C 1619 O O . ALA A 203 ? 0.0916 0.0927 0.1087 -0.0045 0.0083 -0.0067 289 ALA A O 1620 C CB . ALA A 203 ? 0.0989 0.1068 0.1229 -0.0184 0.0081 -0.0054 289 ALA A CB 1621 N N . LYS A 204 ? 0.0989 0.0944 0.0954 0.0011 0.0080 -0.0016 290 LYS A N 1622 C CA . LYS A 204 ? 0.1106 0.1028 0.1125 0.0030 0.0095 0.0082 290 LYS A CA 1623 C C . LYS A 204 ? 0.1024 0.0968 0.0960 -0.0021 0.0047 0.0068 290 LYS A C 1624 O O . LYS A 204 ? 0.1058 0.1021 0.1059 -0.0027 0.0114 -0.0013 290 LYS A O 1625 C CB A LYS A 204 ? 0.1471 0.1047 0.1183 0.0084 0.0059 0.0022 290 LYS A CB 1626 C CB B LYS A 204 ? 0.1422 0.0939 0.1116 0.0087 0.0055 0.0001 290 LYS A CB 1627 C CG A LYS A 204 ? 0.1618 0.1425 0.1497 0.0025 0.0087 0.0135 290 LYS A CG 1628 C CG B LYS A 204 ? 0.1229 0.1250 0.1199 0.0148 0.0012 0.0011 290 LYS A CG 1629 C CD A LYS A 204 ? 0.1913 0.1736 0.1661 0.0145 -0.0009 0.0109 290 LYS A CD 1630 C CD B LYS A 204 ? 0.1531 0.1906 0.1611 -0.0004 -0.0042 0.0130 290 LYS A CD 1631 C CE A LYS A 204 ? 0.1571 0.1464 0.1665 -0.0025 0.0087 0.0158 290 LYS A CE 1632 C CE B LYS A 204 ? 0.1850 0.1840 0.1670 0.0030 0.0038 0.0079 290 LYS A CE 1633 N NZ A LYS A 204 ? 0.2256 0.2057 0.2168 0.0090 -0.0005 -0.0045 290 LYS A NZ 1634 N NZ B LYS A 204 ? 0.2153 0.2423 0.2082 0.0064 -0.0065 0.0148 290 LYS A NZ 1635 N N . ILE A 205 ? 0.0847 0.0882 0.0922 0.0013 0.0057 -0.0014 291 ILE A N 1636 C CA . ILE A 205 ? 0.0974 0.0951 0.0835 -0.0108 0.0020 -0.0023 291 ILE A CA 1637 C C . ILE A 205 ? 0.0895 0.0862 0.0940 -0.0168 0.0072 0.0031 291 ILE A C 1638 O O . ILE A 205 ? 0.0912 0.0901 0.0903 -0.0014 0.0009 -0.0035 291 ILE A O 1639 C CB . ILE A 205 ? 0.0958 0.0975 0.1171 -0.0055 0.0043 -0.0009 291 ILE A CB 1640 C CG1 . ILE A 205 ? 0.1178 0.1184 0.1314 -0.0009 0.0086 -0.0041 291 ILE A CG1 1641 C CG2 . ILE A 205 ? 0.1205 0.1282 0.1212 -0.0159 0.0135 0.0137 291 ILE A CG2 1642 C CD1 . ILE A 205 ? 0.1283 0.1622 0.1635 0.0065 -0.0138 -0.0067 291 ILE A CD1 1643 N N . TYR A 206 ? 0.0930 0.0998 0.0915 0.0019 0.0010 -0.0062 292 TYR A N 1644 C CA . TYR A 206 ? 0.0971 0.0981 0.1006 0.0064 -0.0045 -0.0072 292 TYR A CA 1645 C C . TYR A 206 ? 0.0960 0.1065 0.0942 0.0157 0.0023 -0.0133 292 TYR A C 1646 O O . TYR A 206 ? 0.0987 0.0996 0.1142 0.0069 0.0019 -0.0141 292 TYR A O 1647 C CB . TYR A 206 ? 0.0973 0.1108 0.0969 0.0098 -0.0013 -0.0103 292 TYR A CB 1648 C CG . TYR A 206 ? 0.0970 0.0914 0.1000 0.0108 0.0022 0.0034 292 TYR A CG 1649 C CD1 . TYR A 206 ? 0.0859 0.1159 0.0959 0.0016 -0.0098 -0.0135 292 TYR A CD1 1650 C CD2 . TYR A 206 ? 0.0883 0.0971 0.0957 -0.0048 0.0026 -0.0128 292 TYR A CD2 1651 C CE1 . TYR A 206 ? 0.1021 0.0913 0.1135 -0.0161 0.0010 -0.0007 292 TYR A CE1 1652 C CE2 . TYR A 206 ? 0.0864 0.1005 0.1007 -0.0094 0.0101 0.0030 292 TYR A CE2 1653 C CZ . TYR A 206 ? 0.0882 0.0992 0.0907 0.0055 -0.0070 0.0062 292 TYR A CZ 1654 O OH . TYR A 206 ? 0.1010 0.1143 0.1218 -0.0046 -0.0018 0.0048 292 TYR A OH 1655 N N . GLU A 207 ? 0.0930 0.1027 0.1087 -0.0062 0.0089 -0.0108 293 GLU A N 1656 C CA . GLU A 207 ? 0.1217 0.1118 0.1448 -0.0201 0.0144 -0.0210 293 GLU A CA 1657 C C . GLU A 207 ? 0.1150 0.1073 0.1217 0.0039 0.0316 0.0026 293 GLU A C 1658 O O . GLU A 207 ? 0.1238 0.1093 0.1266 -0.0032 0.0251 0.0024 293 GLU A O 1659 C CB . GLU A 207 ? 0.1576 0.1518 0.1489 0.0068 -0.0105 -0.0164 293 GLU A CB 1660 C CG . GLU A 207 ? 0.1852 0.1623 0.1629 0.0004 0.0038 -0.0067 293 GLU A CG 1661 C CD . GLU A 207 ? 0.1184 0.1096 0.1520 0.0157 0.0315 0.0291 293 GLU A CD 1662 O OE1 . GLU A 207 ? 0.1773 0.1509 0.1732 -0.0328 -0.0334 -0.0172 293 GLU A OE1 1663 O OE2 . GLU A 207 ? 0.1516 0.2055 0.1556 -0.0032 -0.0270 0.0037 293 GLU A OE2 1664 N N . ASP A 208 ? 0.1153 0.1112 0.1161 -0.0021 0.0226 0.0052 294 ASP A N 1665 C CA . ASP A 208 ? 0.1365 0.1218 0.1181 0.0019 0.0208 0.0039 294 ASP A CA 1666 C C . ASP A 208 ? 0.1283 0.1144 0.1021 0.0038 0.0114 -0.0144 294 ASP A C 1667 O O . ASP A 208 ? 0.1740 0.1415 0.1269 0.0117 0.0205 -0.0010 294 ASP A O 1668 C CB . ASP A 208 ? 0.1645 0.1329 0.1284 0.0097 0.0054 0.0036 294 ASP A CB 1669 C CG . ASP A 208 ? 0.1551 0.1603 0.1413 0.0092 -0.0037 0.0018 294 ASP A CG 1670 O OD1 . ASP A 208 ? 0.2221 0.1771 0.1665 -0.0007 0.0050 0.0308 294 ASP A OD1 1671 O OD2 . ASP A 208 ? 0.2063 0.1767 0.1718 0.0158 0.0071 0.0196 294 ASP A OD2 1672 N N . ALA A 209 ? 0.1082 0.0981 0.0967 -0.0051 0.0093 -0.0032 295 ALA A N 1673 C CA . ALA A 209 ? 0.1035 0.1024 0.1058 -0.0004 0.0038 0.0010 295 ALA A CA 1674 C C . ALA A 209 ? 0.1005 0.0958 0.1098 0.0035 0.0062 -0.0010 295 ALA A C 1675 O O . ALA A 209 ? 0.1119 0.1051 0.1268 0.0028 0.0045 -0.0060 295 ALA A O 1676 C CB . ALA A 209 ? 0.1079 0.1028 0.1147 -0.0008 -0.0028 0.0039 295 ALA A CB 1677 N N . GLY A 210 ? 0.0991 0.0995 0.1125 -0.0001 0.0082 -0.0042 296 GLY A N 1678 C CA . GLY A 210 ? 0.1009 0.1155 0.1234 -0.0039 0.0133 -0.0034 296 GLY A CA 1679 C C . GLY A 210 ? 0.0953 0.1061 0.1104 -0.0041 0.0051 -0.0079 296 GLY A C 1680 O O . GLY A 210 ? 0.1108 0.1324 0.1338 0.0135 0.0117 -0.0179 296 GLY A O 1681 N N . LYS A 211 ? 0.0878 0.0907 0.1020 -0.0049 0.0127 0.0000 297 LYS A N 1682 C CA . LYS A 211 ? 0.0875 0.0956 0.1056 -0.0058 0.0113 -0.0097 297 LYS A CA 1683 C C . LYS A 211 ? 0.0882 0.0961 0.1002 -0.0042 0.0018 -0.0046 297 LYS A C 1684 O O . LYS A 211 ? 0.1061 0.1075 0.1335 -0.0014 -0.0033 0.0003 297 LYS A O 1685 C CB . LYS A 211 ? 0.0930 0.1007 0.0983 -0.0074 0.0064 -0.0072 297 LYS A CB 1686 C CG . LYS A 211 ? 0.0891 0.0943 0.1110 -0.0099 0.0070 -0.0036 297 LYS A CG 1687 C CD . LYS A 211 ? 0.0920 0.0977 0.1022 -0.0112 0.0118 -0.0082 297 LYS A CD 1688 C CE . LYS A 211 ? 0.0872 0.0944 0.1070 -0.0086 0.0043 -0.0046 297 LYS A CE 1689 N NZ . LYS A 211 ? 0.0953 0.1001 0.1105 -0.0182 0.0066 -0.0080 297 LYS A NZ 1690 N N . PRO A 212 ? 0.0932 0.0888 0.1044 -0.0014 -0.0002 0.0025 298 PRO A N 1691 C CA . PRO A 212 ? 0.0959 0.0954 0.1114 -0.0012 0.0067 0.0032 298 PRO A CA 1692 C C . PRO A 212 ? 0.0910 0.0910 0.1043 -0.0061 0.0052 0.0008 298 PRO A C 1693 O O . PRO A 212 ? 0.0969 0.0915 0.1055 -0.0013 0.0089 -0.0054 298 PRO A O 1694 C CB . PRO A 212 ? 0.1002 0.1005 0.1186 -0.0005 0.0044 0.0020 298 PRO A CB 1695 C CG . PRO A 212 ? 0.1147 0.1071 0.1489 -0.0173 -0.0037 0.0068 298 PRO A CG 1696 C CD . PRO A 212 ? 0.1003 0.0993 0.1175 -0.0032 0.0017 -0.0022 298 PRO A CD 1697 N N . ARG A 213 ? 0.0841 0.0952 0.1059 -0.0032 0.0085 -0.0044 299 ARG A N 1698 C CA . ARG A 213 ? 0.0908 0.1104 0.1127 -0.0064 -0.0002 -0.0061 299 ARG A CA 1699 C C . ARG A 213 ? 0.0779 0.0936 0.0955 -0.0021 0.0011 -0.0017 299 ARG A C 1700 O O . ARG A 213 ? 0.0924 0.1019 0.1025 -0.0042 0.0005 -0.0046 299 ARG A O 1701 C CB . ARG A 213 ? 0.1026 0.1359 0.1289 0.0094 0.0050 0.0102 299 ARG A CB 1702 C CG . ARG A 213 ? 0.1484 0.1872 0.1729 0.0182 -0.0015 -0.0062 299 ARG A CG 1703 C CD . ARG A 213 ? 0.2176 0.2309 0.2242 0.0375 -0.0056 0.0058 299 ARG A CD 1704 N NE . ARG A 213 ? 0.2026 0.2564 0.2182 0.0171 -0.0076 0.0150 299 ARG A NE 1705 C CZ . ARG A 213 ? 0.2243 0.2757 0.2544 0.0109 0.0037 0.0096 299 ARG A CZ 1706 N NH1 . ARG A 213 ? 0.2041 0.3051 0.3255 0.0031 0.0159 -0.0020 299 ARG A NH1 1707 N NH2 . ARG A 213 ? 0.2573 0.2899 0.2717 0.0023 0.0054 0.0194 299 ARG A NH2 1708 N N . ALA A 214 ? 0.0787 0.0949 0.0979 -0.0005 -0.0003 -0.0047 300 ALA A N 1709 C CA . ALA A 214 ? 0.0858 0.0872 0.0925 0.0025 0.0046 0.0016 300 ALA A CA 1710 C C . ALA A 214 ? 0.0861 0.0870 0.0930 0.0004 0.0034 0.0045 300 ALA A C 1711 O O . ALA A 214 ? 0.0900 0.0959 0.1056 0.0038 0.0123 -0.0015 300 ALA A O 1712 C CB . ALA A 214 ? 0.0866 0.0975 0.0976 -0.0067 -0.0009 -0.0040 300 ALA A CB 1713 N N . VAL A 215 ? 0.0814 0.0832 0.0919 0.0008 0.0092 -0.0011 301 VAL A N 1714 C CA . VAL A 215 ? 0.0777 0.0838 0.1008 0.0041 0.0085 -0.0037 301 VAL A CA 1715 C C . VAL A 215 ? 0.0825 0.0865 0.1076 -0.0091 0.0079 -0.0076 301 VAL A C 1716 O O . VAL A 215 ? 0.0960 0.1161 0.1201 -0.0210 0.0160 -0.0146 301 VAL A O 1717 C CB . VAL A 215 ? 0.0890 0.0964 0.1153 0.0081 0.0067 -0.0036 301 VAL A CB 1718 C CG1 . VAL A 215 ? 0.1102 0.1079 0.1416 0.0173 0.0121 0.0102 301 VAL A CG1 1719 C CG2 . VAL A 215 ? 0.1029 0.1085 0.1289 0.0023 -0.0042 0.0148 301 VAL A CG2 1720 N N . ARG A 216 ? 0.0713 0.0874 0.1030 0.0019 0.0097 -0.0001 302 ARG A N 1721 C CA . ARG A 216 ? 0.0789 0.0927 0.1079 -0.0013 0.0042 0.0048 302 ARG A CA 1722 C C . ARG A 216 ? 0.0717 0.0773 0.0813 0.0001 0.0051 0.0027 302 ARG A C 1723 O O . ARG A 216 ? 0.0795 0.1061 0.1020 0.0008 -0.0012 -0.0097 302 ARG A O 1724 C CB . ARG A 216 ? 0.0916 0.1088 0.1374 -0.0001 0.0120 0.0075 302 ARG A CB 1725 C CG . ARG A 216 ? 0.1190 0.1241 0.1082 0.0127 0.0002 -0.0004 302 ARG A CG 1726 C CD . ARG A 216 ? 0.1147 0.1471 0.1240 0.0052 -0.0011 0.0096 302 ARG A CD 1727 N NE . ARG A 216 ? 0.0950 0.1334 0.1186 0.0034 0.0055 0.0074 302 ARG A NE 1728 C CZ . ARG A 216 ? 0.0951 0.1160 0.1174 0.0030 0.0025 0.0130 302 ARG A CZ 1729 N NH1 . ARG A 216 ? 0.1023 0.1502 0.1273 0.0053 0.0101 -0.0025 302 ARG A NH1 1730 N NH2 . ARG A 216 ? 0.0839 0.1083 0.1257 0.0048 0.0100 -0.0062 302 ARG A NH2 1731 N N . GLY A 217 ? 0.0757 0.0780 0.0850 0.0012 -0.0025 -0.0055 303 GLY A N 1732 C CA . GLY A 217 ? 0.0770 0.0733 0.0804 -0.0002 0.0055 0.0000 303 GLY A CA 1733 C C . GLY A 217 ? 0.0637 0.0662 0.0729 0.0005 -0.0006 -0.0005 303 GLY A C 1734 O O . GLY A 217 ? 0.0691 0.0715 0.0696 -0.0005 0.0053 -0.0015 303 GLY A O 1735 N N . LEU A 218 ? 0.0695 0.0781 0.0712 -0.0012 -0.0040 -0.0026 304 LEU A N 1736 C CA . LEU A 218 ? 0.0672 0.0699 0.0676 0.0019 -0.0050 -0.0007 304 LEU A CA 1737 C C . LEU A 218 ? 0.0704 0.0618 0.0662 -0.0059 -0.0020 -0.0002 304 LEU A C 1738 O O . LEU A 218 ? 0.0767 0.0865 0.0741 -0.0022 -0.0002 0.0033 304 LEU A O 1739 C CB . LEU A 218 ? 0.0730 0.0782 0.0739 0.0035 -0.0009 -0.0041 304 LEU A CB 1740 C CG . LEU A 218 ? 0.0745 0.0803 0.0787 0.0026 0.0001 0.0020 304 LEU A CG 1741 C CD1 . LEU A 218 ? 0.0945 0.0856 0.0847 -0.0109 -0.0026 0.0000 304 LEU A CD1 1742 C CD2 . LEU A 218 ? 0.0769 0.0760 0.0731 0.0021 0.0039 0.0030 304 LEU A CD2 1743 N N . ALA A 219 ? 0.0663 0.0726 0.0616 0.0030 -0.0002 -0.0019 305 ALA A N 1744 C CA . ALA A 219 ? 0.0656 0.0763 0.0683 0.0000 0.0000 -0.0020 305 ALA A CA 1745 C C . ALA A 219 ? 0.0684 0.0729 0.0699 -0.0005 -0.0054 0.0094 305 ALA A C 1746 O O . ALA A 219 ? 0.0865 0.0895 0.0771 0.0154 0.0012 0.0011 305 ALA A O 1747 C CB . ALA A 219 ? 0.0726 0.0784 0.0777 -0.0015 -0.0028 0.0004 305 ALA A CB 1748 N N . THR A 220 ? 0.0654 0.0632 0.0702 0.0046 -0.0018 0.0027 306 THR A N 1749 C CA . THR A 220 ? 0.0631 0.0692 0.0738 0.0000 -0.0062 0.0024 306 THR A CA 1750 C C . THR A 220 ? 0.0657 0.0684 0.0664 0.0003 -0.0037 0.0022 306 THR A C 1751 O O . THR A 220 ? 0.0690 0.0716 0.0710 0.0069 -0.0006 0.0051 306 THR A O 1752 C CB . THR A 220 ? 0.0698 0.0700 0.0736 -0.0015 -0.0042 0.0060 306 THR A CB 1753 O OG1 . THR A 220 ? 0.0926 0.0919 0.0938 0.0001 -0.0142 0.0043 306 THR A OG1 1754 C CG2 . THR A 220 ? 0.0996 0.0978 0.1208 -0.0055 0.0021 -0.0037 306 THR A CG2 1755 N N . ASN A 221 ? 0.0680 0.0688 0.0723 0.0036 0.0029 0.0073 307 ASN A N 1756 C CA . ASN A 221 ? 0.0649 0.0711 0.0687 0.0040 0.0016 0.0064 307 ASN A CA 1757 C C . ASN A 221 ? 0.0645 0.0680 0.0601 0.0006 -0.0036 0.0005 307 ASN A C 1758 O O . ASN A 221 ? 0.0666 0.0719 0.0692 0.0001 0.0018 -0.0012 307 ASN A O 1759 C CB . ASN A 221 ? 0.0717 0.0685 0.0732 0.0008 0.0015 -0.0041 307 ASN A CB 1760 C CG . ASN A 221 ? 0.0778 0.0701 0.0654 0.0067 -0.0055 0.0020 307 ASN A CG 1761 O OD1 . ASN A 221 ? 0.0767 0.0782 0.0749 0.0081 0.0029 -0.0011 307 ASN A OD1 1762 N ND2 . ASN A 221 ? 0.0851 0.0846 0.0840 0.0079 0.0041 0.0031 307 ASN A ND2 1763 N N . VAL A 222 ? 0.0691 0.0690 0.0677 -0.0001 0.0048 0.0023 308 VAL A N 1764 C CA . VAL A 222 ? 0.0788 0.0721 0.0718 0.0053 -0.0050 -0.0008 308 VAL A CA 1765 C C . VAL A 222 ? 0.0663 0.0677 0.0548 0.0016 -0.0009 0.0027 308 VAL A C 1766 O O . VAL A 222 ? 0.0758 0.0780 0.0761 0.0010 -0.0009 0.0068 308 VAL A O 1767 C CB . VAL A 222 ? 0.0739 0.0778 0.0740 0.0081 0.0036 0.0004 308 VAL A CB 1768 C CG1 . VAL A 222 ? 0.0862 0.0887 0.0729 0.0008 0.0063 -0.0035 308 VAL A CG1 1769 C CG2 . VAL A 222 ? 0.0897 0.0823 0.0792 0.0048 0.0075 -0.0017 308 VAL A CG2 1770 N N . ALA A 223 ? 0.0651 0.0698 0.0721 -0.0014 0.0006 0.0005 309 ALA A N 1771 C CA . ALA A 223 ? 0.0806 0.0840 0.0809 -0.0001 -0.0008 0.0003 309 ALA A CA 1772 C C . ALA A 223 ? 0.0667 0.0807 0.0764 0.0004 -0.0013 -0.0018 309 ALA A C 1773 O O . ALA A 223 ? 0.0819 0.1016 0.0960 -0.0016 -0.0055 -0.0097 309 ALA A O 1774 C CB . ALA A 223 ? 0.0742 0.0864 0.0870 -0.0022 -0.0020 -0.0060 309 ALA A CB 1775 N N . ASN A 224 ? 0.0650 0.0787 0.0686 -0.0004 0.0068 -0.0022 310 ASN A N 1776 C CA . ASN A 224 ? 0.0646 0.0718 0.0806 0.0004 0.0027 -0.0039 310 ASN A CA 1777 C C . ASN A 224 ? 0.0679 0.0701 0.0777 0.0039 -0.0003 0.0000 310 ASN A C 1778 O O . ASN A 224 ? 0.0796 0.0754 0.0765 0.0114 0.0002 -0.0013 310 ASN A O 1779 C CB . ASN A 224 ? 0.0859 0.0848 0.0728 0.0117 0.0009 -0.0007 310 ASN A CB 1780 C CG . ASN A 224 ? 0.0864 0.1003 0.1090 0.0130 0.0033 0.0084 310 ASN A CG 1781 O OD1 . ASN A 224 ? 0.1320 0.1254 0.1611 0.0160 -0.0129 0.0133 310 ASN A OD1 1782 N ND2 . ASN A 224 ? 0.1288 0.1617 0.1105 -0.0052 -0.0141 0.0220 310 ASN A ND2 1783 N N . TYR A 225 ? 0.0760 0.0685 0.0706 0.0029 0.0039 0.0008 311 TYR A N 1784 C CA . TYR A 225 ? 0.0726 0.0785 0.0750 0.0063 0.0011 0.0011 311 TYR A CA 1785 C C . TYR A 225 ? 0.0658 0.0692 0.0670 0.0059 0.0052 0.0011 311 TYR A C 1786 O O . TYR A 225 ? 0.0796 0.0817 0.0744 0.0008 0.0025 -0.0041 311 TYR A O 1787 C CB . TYR A 225 ? 0.0760 0.0758 0.0760 -0.0004 0.0044 0.0008 311 TYR A CB 1788 C CG . TYR A 225 ? 0.0654 0.0737 0.0721 0.0013 0.0041 0.0002 311 TYR A CG 1789 C CD1 . TYR A 225 ? 0.0767 0.0847 0.0764 0.0077 -0.0035 0.0041 311 TYR A CD1 1790 C CD2 . TYR A 225 ? 0.0790 0.0774 0.0811 -0.0046 0.0043 -0.0011 311 TYR A CD2 1791 C CE1 . TYR A 225 ? 0.0809 0.0757 0.0761 -0.0007 0.0053 0.0064 311 TYR A CE1 1792 C CE2 . TYR A 225 ? 0.0809 0.0888 0.0776 0.0010 -0.0060 0.0021 311 TYR A CE2 1793 C CZ . TYR A 225 ? 0.0751 0.0824 0.0819 -0.0017 0.0025 0.0026 311 TYR A CZ 1794 O OH . TYR A 225 ? 0.0786 0.0885 0.0900 -0.0020 -0.0028 -0.0049 311 TYR A OH 1795 N N . ASN A 226 ? 0.0723 0.0683 0.0728 0.0027 0.0026 -0.0014 312 ASN A N 1796 C CA . ASN A 226 ? 0.0729 0.0691 0.0701 -0.0023 0.0023 -0.0019 312 ASN A CA 1797 C C . ASN A 226 ? 0.0705 0.0668 0.0666 0.0003 0.0022 0.0005 312 ASN A C 1798 O O . ASN A 226 ? 0.0794 0.0779 0.0755 0.0032 0.0000 0.0043 312 ASN A O 1799 C CB . ASN A 226 ? 0.0773 0.0730 0.0725 0.0056 -0.0007 -0.0004 312 ASN A CB 1800 C CG . ASN A 226 ? 0.0775 0.0679 0.0678 0.0063 0.0034 0.0078 312 ASN A CG 1801 O OD1 . ASN A 226 ? 0.0883 0.0876 0.0793 0.0058 -0.0019 -0.0002 312 ASN A OD1 1802 N ND2 . ASN A 226 ? 0.0940 0.0900 0.0765 0.0039 0.0036 0.0064 312 ASN A ND2 1803 N N . ALA A 227 ? 0.0745 0.0791 0.0763 0.0015 0.0002 -0.0008 313 ALA A N 1804 C CA . ALA A 227 ? 0.0783 0.0797 0.0761 -0.0012 -0.0001 0.0008 313 ALA A CA 1805 C C . ALA A 227 ? 0.0729 0.0806 0.0750 -0.0003 -0.0002 0.0047 313 ALA A C 1806 O O . ALA A 227 ? 0.0798 0.0814 0.0764 -0.0040 0.0006 0.0000 313 ALA A O 1807 C CB . ALA A 227 ? 0.0968 0.1061 0.0823 -0.0037 0.0000 -0.0088 313 ALA A CB 1808 N N . TRP A 228 ? 0.0844 0.0953 0.0901 -0.0048 0.0020 0.0128 314 TRP A N 1809 C CA . TRP A 228 ? 0.0845 0.0911 0.0896 -0.0003 -0.0006 0.0080 314 TRP A CA 1810 C C . TRP A 228 ? 0.0809 0.0915 0.0834 0.0013 0.0028 0.0063 314 TRP A C 1811 O O . TRP A 228 ? 0.0937 0.0943 0.0923 -0.0032 -0.0048 0.0031 314 TRP A O 1812 C CB . TRP A 228 ? 0.0884 0.0933 0.0902 -0.0016 -0.0076 0.0022 314 TRP A CB 1813 C CG . TRP A 228 ? 0.0855 0.0854 0.0925 0.0027 -0.0033 0.0036 314 TRP A CG 1814 C CD1 . TRP A 228 ? 0.0957 0.0933 0.0929 0.0028 0.0019 -0.0026 314 TRP A CD1 1815 C CD2 . TRP A 228 ? 0.0847 0.0791 0.0874 0.0069 -0.0079 -0.0002 314 TRP A CD2 1816 N NE1 . TRP A 228 ? 0.0933 0.1103 0.0956 0.0129 -0.0159 -0.0078 314 TRP A NE1 1817 C CE2 . TRP A 228 ? 0.0941 0.0937 0.0902 -0.0013 0.0001 -0.0093 314 TRP A CE2 1818 C CE3 . TRP A 228 ? 0.0867 0.0810 0.0910 0.0020 -0.0020 -0.0006 314 TRP A CE3 1819 C CZ2 . TRP A 228 ? 0.0937 0.0983 0.1085 -0.0032 -0.0105 -0.0143 314 TRP A CZ2 1820 C CZ3 . TRP A 228 ? 0.0976 0.0938 0.0984 0.0044 -0.0014 -0.0014 314 TRP A CZ3 1821 C CH2 . TRP A 228 ? 0.0915 0.0952 0.1134 -0.0002 0.0022 -0.0028 314 TRP A CH2 1822 N N . SER A 229 ? 0.1033 0.0945 0.0860 0.0004 0.0043 0.0031 315 SER A N 1823 C CA . SER A 229 ? 0.1033 0.1070 0.0985 0.0000 0.0116 0.0040 315 SER A CA 1824 C C . SER A 229 ? 0.1434 0.1217 0.1021 0.0109 0.0177 0.0179 315 SER A C 1825 O O . SER A 229 ? 0.1811 0.1443 0.1306 0.0155 0.0288 0.0133 315 SER A O 1826 C CB . SER A 229 ? 0.1406 0.1249 0.1091 -0.0061 -0.0081 -0.0054 315 SER A CB 1827 O OG . SER A 229 ? 0.1701 0.1386 0.1234 -0.0125 -0.0217 -0.0119 315 SER A OG 1828 N N . VAL A 230 ? 0.1356 0.1219 0.1092 0.0124 0.0243 -0.0091 316 VAL A N 1829 C CA . VAL A 230 ? 0.1499 0.1430 0.1192 0.0066 0.0170 -0.0027 316 VAL A CA 1830 C C . VAL A 230 ? 0.1501 0.1389 0.1158 0.0121 0.0094 -0.0140 316 VAL A C 1831 O O . VAL A 230 ? 0.1596 0.1403 0.1230 0.0000 0.0068 -0.0105 316 VAL A O 1832 C CB . VAL A 230 ? 0.1601 0.1570 0.1808 0.0014 0.0236 -0.0090 316 VAL A CB 1833 C CG1 . VAL A 230 ? 0.2013 0.1813 0.1777 -0.0153 0.0216 -0.0042 316 VAL A CG1 1834 C CG2 . VAL A 230 ? 0.1254 0.1645 0.1831 0.0049 0.0052 -0.0473 316 VAL A CG2 1835 N N . SER A 231 ? 0.1729 0.1568 0.1305 0.0256 0.0095 -0.0080 317 SER A N 1836 C CA . SER A 231 ? 0.1874 0.1810 0.1546 0.0174 -0.0128 -0.0230 317 SER A CA 1837 C C . SER A 231 ? 0.1551 0.1623 0.1465 0.0049 0.0003 -0.0109 317 SER A C 1838 O O . SER A 231 ? 0.2255 0.2052 0.2693 0.0040 0.0207 -0.0131 317 SER A O 1839 C CB A SER A 231 ? 0.1912 0.1978 0.1664 0.0214 -0.0050 -0.0138 317 SER A CB 1840 C CB B SER A 231 ? 0.2061 0.2031 0.1714 0.0242 -0.0082 -0.0152 317 SER A CB 1841 O OG A SER A 231 ? 0.2034 0.2192 0.1741 0.0202 -0.0271 -0.0199 317 SER A OG 1842 O OG B SER A 231 ? 0.2671 0.2691 0.2546 0.0100 0.0087 -0.0134 317 SER A OG 1843 N N . SER A 232 ? 0.1718 0.1656 0.1644 0.0141 -0.0094 -0.0310 318 SER A N 1844 C CA A SER A 232 ? 0.1732 0.1800 0.1755 0.0039 -0.0169 -0.0217 318 SER A CA 1845 C CA B SER A 232 ? 0.1768 0.1734 0.1681 0.0072 -0.0163 -0.0223 318 SER A CA 1846 C C . SER A 232 ? 0.1365 0.1581 0.1443 0.0018 -0.0112 -0.0317 318 SER A C 1847 O O . SER A 232 ? 0.1694 0.1444 0.1598 0.0120 -0.0240 -0.0212 318 SER A O 1848 C CB A SER A 232 ? 0.1807 0.1844 0.1591 -0.0092 -0.0110 -0.0292 318 SER A CB 1849 C CB B SER A 232 ? 0.1787 0.1846 0.1567 0.0159 -0.0179 -0.0192 318 SER A CB 1850 O OG A SER A 232 ? 0.2530 0.2832 0.2727 0.0302 -0.0053 -0.0123 318 SER A OG 1851 O OG B SER A 232 ? 0.2602 0.2251 0.2120 -0.0107 0.0094 -0.0091 318 SER A OG 1852 N N . PRO A 233 ? 0.1374 0.1391 0.1487 -0.0071 0.0005 -0.0346 319 PRO A N 1853 C CA . PRO A 233 ? 0.1279 0.1288 0.1293 -0.0003 0.0073 -0.0252 319 PRO A CA 1854 C C . PRO A 233 ? 0.1129 0.1201 0.1159 0.0138 0.0074 -0.0129 319 PRO A C 1855 O O . PRO A 233 ? 0.1223 0.1290 0.1236 0.0073 0.0085 -0.0236 319 PRO A O 1856 C CB A PRO A 233 ? 0.1516 0.1597 0.1510 -0.0089 0.0166 -0.0192 319 PRO A CB 1857 C CB B PRO A 233 ? 0.1402 0.1440 0.1413 -0.0072 0.0124 -0.0177 319 PRO A CB 1858 C CG A PRO A 233 ? 0.1633 0.1515 0.1982 -0.0198 0.0083 -0.0025 319 PRO A CG 1859 C CG B PRO A 233 ? 0.1259 0.1167 0.1572 -0.0070 0.0026 -0.0167 319 PRO A CG 1860 C CD A PRO A 233 ? 0.1680 0.1562 0.1824 -0.0034 0.0039 -0.0351 319 PRO A CD 1861 C CD B PRO A 233 ? 0.1494 0.1463 0.1610 0.0000 0.0000 -0.0279 319 PRO A CD 1862 N N . PRO A 234 ? 0.1093 0.1159 0.1076 -0.0020 0.0044 -0.0096 320 PRO A N 1863 C CA . PRO A 234 ? 0.1168 0.1168 0.1037 -0.0091 0.0127 -0.0049 320 PRO A CA 1864 C C . PRO A 234 ? 0.1066 0.1152 0.1089 -0.0067 0.0102 -0.0129 320 PRO A C 1865 O O . PRO A 234 ? 0.1225 0.1157 0.1085 0.0011 0.0070 -0.0059 320 PRO A O 1866 C CB . PRO A 234 ? 0.1301 0.1201 0.1012 -0.0098 0.0065 -0.0115 320 PRO A CB 1867 C CG . PRO A 234 ? 0.1384 0.1279 0.1115 -0.0033 0.0037 -0.0106 320 PRO A CG 1868 C CD . PRO A 234 ? 0.1201 0.1228 0.1147 0.0095 -0.0019 -0.0083 320 PRO A CD 1869 N N . PRO A 235 ? 0.1205 0.1392 0.1031 0.0023 0.0116 -0.0040 321 PRO A N 1870 C CA . PRO A 235 ? 0.1448 0.1379 0.1299 0.0148 0.0124 -0.0266 321 PRO A CA 1871 C C . PRO A 235 ? 0.1372 0.1241 0.1287 0.0111 0.0049 0.0047 321 PRO A C 1872 O O . PRO A 235 ? 0.1541 0.1253 0.1444 0.0160 0.0031 -0.0114 321 PRO A O 1873 C CB . PRO A 235 ? 0.1560 0.1728 0.1518 0.0241 0.0175 -0.0193 321 PRO A CB 1874 C CG . PRO A 235 ? 0.1846 0.2081 0.1874 0.0046 0.0192 -0.0001 321 PRO A CG 1875 C CD . PRO A 235 ? 0.1570 0.1753 0.1422 0.0033 0.0232 0.0061 321 PRO A CD 1876 N N . TYR A 236 ? 0.1064 0.0981 0.1010 0.0098 0.0038 -0.0070 322 TYR A N 1877 C CA . TYR A 236 ? 0.1026 0.1035 0.0994 0.0109 0.0068 -0.0040 322 TYR A CA 1878 C C . TYR A 236 ? 0.0952 0.0895 0.0989 -0.0001 0.0017 -0.0059 322 TYR A C 1879 O O . TYR A 236 ? 0.1017 0.1072 0.1048 0.0060 -0.0002 0.0018 322 TYR A O 1880 C CB . TYR A 236 ? 0.1014 0.1092 0.1060 0.0081 0.0029 0.0052 322 TYR A CB 1881 C CG . TYR A 236 ? 0.0885 0.0925 0.1057 0.0023 0.0006 0.0019 322 TYR A CG 1882 C CD1 . TYR A 236 ? 0.0926 0.0949 0.0898 0.0031 0.0031 0.0024 322 TYR A CD1 1883 C CD2 . TYR A 236 ? 0.0947 0.1181 0.1030 0.0167 0.0113 -0.0004 322 TYR A CD2 1884 C CE1 . TYR A 236 ? 0.0833 0.0934 0.0892 0.0006 0.0049 -0.0008 322 TYR A CE1 1885 C CE2 . TYR A 236 ? 0.0988 0.0973 0.1037 0.0042 0.0173 -0.0028 322 TYR A CE2 1886 C CZ . TYR A 236 ? 0.0881 0.0930 0.0895 0.0051 0.0008 0.0075 322 TYR A CZ 1887 O OH . TYR A 236 ? 0.1007 0.0880 0.0979 0.0009 0.0079 0.0019 322 TYR A OH 1888 N N . THR A 237 ? 0.1006 0.1020 0.0877 0.0027 0.0077 -0.0091 323 THR A N 1889 C CA . THR A 237 ? 0.1026 0.1167 0.1047 0.0011 0.0170 -0.0088 323 THR A CA 1890 C C . THR A 237 ? 0.0930 0.1086 0.1049 0.0083 0.0057 -0.0089 323 THR A C 1891 O O . THR A 237 ? 0.1110 0.1015 0.1184 0.0066 0.0131 0.0000 323 THR A O 1892 C CB . THR A 237 ? 0.1041 0.1013 0.0878 -0.0027 0.0083 -0.0060 323 THR A CB 1893 O OG1 . THR A 237 ? 0.1007 0.1059 0.0997 0.0006 0.0039 -0.0072 323 THR A OG1 1894 C CG2 . THR A 237 ? 0.1037 0.1122 0.1028 0.0069 0.0050 -0.0042 323 THR A CG2 1895 N N . SER A 238 ? 0.1199 0.1102 0.1251 0.0059 0.0137 -0.0117 324 SER A N 1896 C CA . SER A 238 ? 0.1330 0.1155 0.1447 0.0155 0.0149 -0.0140 324 SER A CA 1897 C C . SER A 238 ? 0.1318 0.1218 0.1530 0.0245 0.0036 -0.0210 324 SER A C 1898 O O . SER A 238 ? 0.1425 0.1356 0.1595 0.0243 -0.0007 -0.0064 324 SER A O 1899 C CB . SER A 238 ? 0.1734 0.1514 0.1817 0.0239 0.0163 -0.0230 324 SER A CB 1900 O OG . SER A 238 ? 0.2397 0.1981 0.2263 0.0190 0.0121 -0.0158 324 SER A OG 1901 N N . PRO A 239 ? 0.1327 0.1181 0.1414 0.0343 0.0007 -0.0061 325 PRO A N 1902 C CA . PRO A 239 ? 0.1428 0.1063 0.1528 0.0295 0.0117 -0.0045 325 PRO A CA 1903 C C . PRO A 239 ? 0.1244 0.0971 0.1536 0.0153 0.0103 -0.0050 325 PRO A C 1904 O O . PRO A 239 ? 0.1498 0.1112 0.2041 0.0087 0.0158 -0.0125 325 PRO A O 1905 C CB . PRO A 239 ? 0.1656 0.1254 0.2215 0.0415 0.0197 -0.0065 325 PRO A CB 1906 C CG . PRO A 239 ? 0.1709 0.1558 0.2231 0.0434 0.0139 0.0224 325 PRO A CG 1907 C CD . PRO A 239 ? 0.1618 0.1464 0.1745 0.0406 0.0092 -0.0002 325 PRO A CD 1908 N N . ASN A 240 ? 0.1068 0.0930 0.1240 0.0166 0.0020 -0.0066 326 ASN A N 1909 C CA . ASN A 240 ? 0.1068 0.0908 0.1103 0.0073 0.0084 0.0014 326 ASN A CA 1910 C C . ASN A 240 ? 0.1102 0.0906 0.1023 0.0101 0.0031 0.0016 326 ASN A C 1911 O O . ASN A 240 ? 0.1200 0.1019 0.1094 0.0078 0.0081 -0.0050 326 ASN A O 1912 C CB . ASN A 240 ? 0.0977 0.0874 0.1033 0.0017 0.0003 -0.0001 326 ASN A CB 1913 C CG . ASN A 240 ? 0.0946 0.0850 0.0955 0.0032 -0.0064 -0.0009 326 ASN A CG 1914 O OD1 . ASN A 240 ? 0.1004 0.0905 0.1021 -0.0006 0.0004 0.0006 326 ASN A OD1 1915 N ND2 . ASN A 240 ? 0.1069 0.0894 0.0938 -0.0010 0.0002 -0.0005 326 ASN A ND2 1916 N N . PRO A 241 ? 0.1166 0.1038 0.1051 0.0022 -0.0021 -0.0016 327 PRO A N 1917 C CA . PRO A 241 ? 0.1243 0.1032 0.1186 -0.0027 0.0010 -0.0018 327 PRO A CA 1918 C C . PRO A 241 ? 0.1101 0.1041 0.1090 0.0009 0.0011 0.0005 327 PRO A C 1919 O O . PRO A 241 ? 0.1295 0.1054 0.1248 0.0044 -0.0075 -0.0031 327 PRO A O 1920 C CB . PRO A 241 ? 0.1346 0.1200 0.1461 -0.0098 -0.0011 0.0094 327 PRO A CB 1921 C CG . PRO A 241 ? 0.1496 0.1336 0.1624 -0.0183 -0.0070 0.0135 327 PRO A CG 1922 C CD . PRO A 241 ? 0.1195 0.1098 0.1348 -0.0098 -0.0125 0.0066 327 PRO A CD 1923 N N . ASN A 242 ? 0.1015 0.0929 0.1065 -0.0021 -0.0060 -0.0018 328 ASN A N 1924 C CA . ASN A 242 ? 0.1008 0.0914 0.1067 0.0056 -0.0085 -0.0014 328 ASN A CA 1925 C C . ASN A 242 ? 0.0897 0.0816 0.0962 0.0119 -0.0087 0.0016 328 ASN A C 1926 O O . ASN A 242 ? 0.1013 0.0944 0.1034 0.0021 0.0001 -0.0007 328 ASN A O 1927 C CB . ASN A 242 ? 0.1039 0.0968 0.1030 0.0024 -0.0067 0.0042 328 ASN A CB 1928 C CG . ASN A 242 ? 0.1124 0.1044 0.1110 0.0000 -0.0102 0.0047 328 ASN A CG 1929 O OD1 . ASN A 242 ? 0.1196 0.1312 0.1295 -0.0107 -0.0065 0.0103 328 ASN A OD1 1930 N ND2 . ASN A 242 ? 0.1334 0.1304 0.1335 -0.0185 0.0027 0.0179 328 ASN A ND2 1931 N N . TYR A 243 ? 0.0906 0.0891 0.0958 0.0028 -0.0062 -0.0029 329 TYR A N 1932 C CA . TYR A 243 ? 0.0915 0.0856 0.1033 0.0096 -0.0043 -0.0002 329 TYR A CA 1933 C C . TYR A 243 ? 0.0848 0.0773 0.0928 0.0021 0.0023 -0.0043 329 TYR A C 1934 O O . TYR A 243 ? 0.0928 0.0960 0.1243 -0.0015 0.0038 -0.0025 329 TYR A O 1935 C CB . TYR A 243 ? 0.0953 0.0883 0.1093 -0.0005 0.0066 -0.0006 329 TYR A CB 1936 C CG . TYR A 243 ? 0.1005 0.1014 0.1105 0.0076 0.0101 -0.0154 329 TYR A CG 1937 C CD1 . TYR A 243 ? 0.1171 0.1302 0.1129 0.0159 0.0057 -0.0076 329 TYR A CD1 1938 C CD2 . TYR A 243 ? 0.1576 0.1485 0.1304 -0.0236 0.0106 -0.0109 329 TYR A CD2 1939 C CE1 . TYR A 243 ? 0.1636 0.1776 0.1533 0.0177 0.0103 -0.0037 329 TYR A CE1 1940 C CE2 . TYR A 243 ? 0.1685 0.1869 0.1740 -0.0242 -0.0011 -0.0192 329 TYR A CE2 1941 C CZ . TYR A 243 ? 0.1712 0.2124 0.1202 -0.0034 -0.0111 -0.0100 329 TYR A CZ 1942 O OH . TYR A 243 ? 0.2123 0.2421 0.1955 -0.0143 -0.0381 0.0013 329 TYR A OH 1943 N N . ASP A 244 ? 0.0874 0.0801 0.0924 0.0067 0.0057 0.0001 330 ASP A N 1944 C CA . ASP A 244 ? 0.0790 0.0798 0.0891 0.0079 0.0037 0.0052 330 ASP A CA 1945 C C . ASP A 244 ? 0.0754 0.0796 0.0759 -0.0025 0.0009 -0.0028 330 ASP A C 1946 O O . ASP A 244 ? 0.0813 0.0767 0.0894 -0.0001 0.0065 -0.0008 330 ASP A O 1947 C CB . ASP A 244 ? 0.0837 0.0840 0.0904 0.0059 0.0110 0.0002 330 ASP A CB 1948 C CG . ASP A 244 ? 0.1007 0.0941 0.0793 0.0003 0.0070 0.0043 330 ASP A CG 1949 O OD1 . ASP A 244 ? 0.0965 0.0968 0.0950 -0.0010 0.0073 -0.0042 330 ASP A OD1 1950 O OD2 . ASP A 244 ? 0.1066 0.1006 0.0929 0.0000 0.0026 -0.0090 330 ASP A OD2 1951 N N . GLU A 245 ? 0.0783 0.0795 0.0738 0.0067 0.0070 -0.0007 331 GLU A N 1952 C CA . GLU A 245 ? 0.0738 0.0768 0.0749 0.0069 -0.0013 -0.0037 331 GLU A CA 1953 C C . GLU A 245 ? 0.0807 0.0725 0.0722 0.0003 0.0000 -0.0013 331 GLU A C 1954 O O . GLU A 245 ? 0.0825 0.0795 0.0769 -0.0013 0.0004 -0.0017 331 GLU A O 1955 C CB . GLU A 245 ? 0.0750 0.0764 0.0783 0.0034 0.0026 0.0020 331 GLU A CB 1956 C CG . GLU A 245 ? 0.0781 0.0750 0.0820 -0.0008 -0.0005 0.0043 331 GLU A CG 1957 C CD . GLU A 245 ? 0.0733 0.0786 0.0813 0.0014 0.0060 0.0018 331 GLU A CD 1958 O OE1 . GLU A 245 ? 0.1114 0.0956 0.0869 0.0125 0.0065 -0.0015 331 GLU A OE1 1959 O OE2 . GLU A 245 ? 0.0894 0.1027 0.0942 0.0014 0.0040 0.0127 331 GLU A OE2 1960 N N . LYS A 246 ? 0.0750 0.0771 0.0749 -0.0003 -0.0009 0.0043 332 LYS A N 1961 C CA . LYS A 246 ? 0.0792 0.0809 0.0810 -0.0002 0.0017 -0.0003 332 LYS A CA 1962 C C . LYS A 246 ? 0.0815 0.0844 0.0697 -0.0026 -0.0047 -0.0053 332 LYS A C 1963 O O . LYS A 246 ? 0.0847 0.0835 0.0842 -0.0023 -0.0008 -0.0024 332 LYS A O 1964 C CB . LYS A 246 ? 0.0829 0.0802 0.0809 0.0014 0.0000 -0.0045 332 LYS A CB 1965 C CG . LYS A 246 ? 0.0927 0.0913 0.0918 0.0018 -0.0039 -0.0025 332 LYS A CG 1966 C CD . LYS A 246 ? 0.1101 0.0956 0.1034 -0.0066 -0.0117 -0.0091 332 LYS A CD 1967 C CE . LYS A 246 ? 0.1097 0.1201 0.0976 -0.0012 -0.0144 -0.0060 332 LYS A CE 1968 N NZ . LYS A 246 ? 0.1172 0.1205 0.1130 -0.0008 -0.0120 -0.0036 332 LYS A NZ 1969 N N . HIS A 247 ? 0.0801 0.0822 0.0859 -0.0036 0.0027 0.0029 333 HIS A N 1970 C CA . HIS A 247 ? 0.0857 0.0800 0.0869 0.0015 -0.0034 -0.0004 333 HIS A CA 1971 C C . HIS A 247 ? 0.0730 0.0812 0.0863 -0.0051 -0.0021 0.0001 333 HIS A C 1972 O O . HIS A 247 ? 0.0892 0.0871 0.0901 -0.0048 0.0018 -0.0020 333 HIS A O 1973 C CB . HIS A 247 ? 0.0924 0.0790 0.0840 0.0051 0.0008 -0.0023 333 HIS A CB 1974 C CG . HIS A 247 ? 0.0996 0.0873 0.1014 -0.0023 0.0066 -0.0044 333 HIS A CG 1975 N ND1 . HIS A 247 ? 0.1132 0.1088 0.0918 0.0036 -0.0009 -0.0121 333 HIS A ND1 1976 C CD2 . HIS A 247 ? 0.1327 0.1082 0.1152 -0.0038 0.0087 -0.0081 333 HIS A CD2 1977 C CE1 . HIS A 247 ? 0.1249 0.1255 0.0930 -0.0011 0.0126 -0.0099 333 HIS A CE1 1978 N NE2 . HIS A 247 ? 0.1493 0.1174 0.1139 0.0084 0.0050 -0.0242 333 HIS A NE2 1979 N N . TYR A 248 ? 0.0789 0.0783 0.0815 -0.0062 0.0055 -0.0011 334 TYR A N 1980 C CA . TYR A 248 ? 0.0807 0.0768 0.0728 0.0021 0.0022 0.0051 334 TYR A CA 1981 C C . TYR A 248 ? 0.0777 0.0766 0.0776 -0.0021 0.0004 -0.0036 334 TYR A C 1982 O O . TYR A 248 ? 0.0821 0.0823 0.0834 -0.0058 0.0084 0.0043 334 TYR A O 1983 C CB . TYR A 248 ? 0.0813 0.0855 0.0913 -0.0025 0.0012 -0.0001 334 TYR A CB 1984 C CG . TYR A 248 ? 0.0700 0.0782 0.0811 0.0013 -0.0019 0.0000 334 TYR A CG 1985 C CD1 . TYR A 248 ? 0.0789 0.0789 0.0840 -0.0012 0.0014 -0.0028 334 TYR A CD1 1986 C CD2 . TYR A 248 ? 0.0735 0.0784 0.0806 0.0003 0.0063 0.0068 334 TYR A CD2 1987 C CE1 . TYR A 248 ? 0.0782 0.0747 0.0797 -0.0021 -0.0015 0.0069 334 TYR A CE1 1988 C CE2 . TYR A 248 ? 0.0744 0.0713 0.0824 -0.0048 0.0014 0.0009 334 TYR A CE2 1989 C CZ . TYR A 248 ? 0.0763 0.0780 0.0679 -0.0038 -0.0026 0.0000 334 TYR A CZ 1990 O OH . TYR A 248 ? 0.0894 0.0918 0.0827 -0.0033 -0.0042 -0.0022 334 TYR A OH 1991 N N . ILE A 249 ? 0.0706 0.0721 0.0762 0.0035 0.0025 -0.0004 335 ILE A N 1992 C CA . ILE A 249 ? 0.0809 0.0784 0.0813 0.0083 0.0007 -0.0029 335 ILE A CA 1993 C C . ILE A 249 ? 0.0750 0.0813 0.0785 0.0097 0.0037 0.0011 335 ILE A C 1994 O O . ILE A 249 ? 0.0920 0.0959 0.0893 -0.0021 0.0064 0.0039 335 ILE A O 1995 C CB . ILE A 249 ? 0.0895 0.0926 0.0924 0.0087 0.0088 0.0031 335 ILE A CB 1996 C CG1 . ILE A 249 ? 0.1076 0.0928 0.0858 0.0062 0.0090 0.0009 335 ILE A CG1 1997 C CG2 . ILE A 249 ? 0.1080 0.1050 0.1211 0.0118 0.0034 0.0121 335 ILE A CG2 1998 C CD1 . ILE A 249 ? 0.1189 0.1092 0.1064 -0.0012 0.0113 0.0048 335 ILE A CD1 1999 N N . GLU A 250 ? 0.0815 0.0901 0.0884 -0.0028 0.0022 0.0003 336 GLU A N 2000 C CA . GLU A 250 ? 0.0828 0.0917 0.0902 -0.0061 -0.0046 0.0003 336 GLU A CA 2001 C C . GLU A 250 ? 0.0945 0.0973 0.0934 -0.0118 -0.0007 -0.0054 336 GLU A C 2002 O O . GLU A 250 ? 0.1077 0.1230 0.1125 -0.0170 0.0024 0.0013 336 GLU A O 2003 C CB . GLU A 250 ? 0.0864 0.0937 0.0972 -0.0048 -0.0058 -0.0069 336 GLU A CB 2004 C CG . GLU A 250 ? 0.0974 0.1047 0.0943 -0.0014 -0.0055 -0.0080 336 GLU A CG 2005 C CD . GLU A 250 ? 0.0980 0.0912 0.0963 0.0046 -0.0106 -0.0077 336 GLU A CD 2006 O OE1 . GLU A 250 ? 0.1321 0.1177 0.1068 0.0138 -0.0076 -0.0100 336 GLU A OE1 2007 O OE2 . GLU A 250 ? 0.1384 0.1127 0.1059 0.0069 -0.0137 -0.0111 336 GLU A OE2 2008 N N . ALA A 251 ? 0.0893 0.0811 0.0886 -0.0073 0.0017 -0.0033 337 ALA A N 2009 C CA . ALA A 251 ? 0.1024 0.0895 0.0956 -0.0085 0.0020 -0.0059 337 ALA A CA 2010 C C . ALA A 251 ? 0.0918 0.0842 0.0932 -0.0032 0.0055 0.0044 337 ALA A C 2011 O O . ALA A 251 ? 0.1221 0.1058 0.1061 -0.0234 0.0102 -0.0021 337 ALA A O 2012 C CB . ALA A 251 ? 0.1150 0.0987 0.1007 0.0010 0.0039 -0.0022 337 ALA A CB 2013 N N . PHE A 252 ? 0.0837 0.0841 0.0854 -0.0070 0.0016 -0.0007 338 PHE A N 2014 C CA . PHE A 252 ? 0.0831 0.0827 0.0897 -0.0030 0.0022 0.0013 338 PHE A CA 2015 C C . PHE A 252 ? 0.0843 0.0788 0.0812 -0.0043 0.0037 0.0015 338 PHE A C 2016 O O . PHE A 252 ? 0.0798 0.0922 0.0858 -0.0077 0.0043 -0.0049 338 PHE A O 2017 C CB . PHE A 252 ? 0.0836 0.0851 0.0913 -0.0036 0.0068 0.0052 338 PHE A CB 2018 C CG . PHE A 252 ? 0.0805 0.0855 0.0905 -0.0033 0.0066 0.0042 338 PHE A CG 2019 C CD1 . PHE A 252 ? 0.0929 0.0911 0.0907 -0.0009 0.0078 -0.0075 338 PHE A CD1 2020 C CD2 . PHE A 252 ? 0.0794 0.0870 0.0893 0.0044 -0.0056 0.0008 338 PHE A CD2 2021 C CE1 . PHE A 252 ? 0.0959 0.0944 0.0890 -0.0033 -0.0055 0.0031 338 PHE A CE1 2022 C CE2 . PHE A 252 ? 0.0817 0.0924 0.1110 -0.0085 -0.0014 -0.0073 338 PHE A CE2 2023 C CZ . PHE A 252 ? 0.1009 0.1052 0.0994 -0.0027 -0.0086 -0.0143 338 PHE A CZ 2024 N N . ARG A 253 ? 0.0846 0.0905 0.0884 -0.0020 0.0088 -0.0002 339 ARG A N 2025 C CA . ARG A 253 ? 0.0942 0.0951 0.0915 -0.0021 0.0116 -0.0015 339 ARG A CA 2026 C C . ARG A 253 ? 0.0845 0.0926 0.0876 0.0010 0.0061 -0.0020 339 ARG A C 2027 O O . ARG A 253 ? 0.0923 0.0998 0.0935 -0.0005 0.0070 -0.0020 339 ARG A O 2028 C CB . ARG A 253 ? 0.1016 0.0976 0.0933 0.0039 0.0096 0.0064 339 ARG A CB 2029 C CG . ARG A 253 ? 0.1052 0.1088 0.1088 -0.0006 0.0003 0.0002 339 ARG A CG 2030 C CD . ARG A 253 ? 0.0987 0.0996 0.0994 0.0023 0.0006 0.0068 339 ARG A CD 2031 N NE . ARG A 253 ? 0.0917 0.1117 0.1107 0.0045 0.0063 0.0060 339 ARG A NE 2032 C CZ . ARG A 253 ? 0.0958 0.1131 0.1085 0.0017 -0.0051 0.0002 339 ARG A CZ 2033 N NH1 . ARG A 253 ? 0.1090 0.1212 0.1122 0.0080 -0.0051 0.0062 339 ARG A NH1 2034 N NH2 . ARG A 253 ? 0.1111 0.1573 0.1463 0.0058 -0.0042 0.0061 339 ARG A NH2 2035 N N . PRO A 254 ? 0.0883 0.1001 0.0946 -0.0072 0.0039 0.0006 340 PRO A N 2036 C CA . PRO A 254 ? 0.0974 0.1076 0.1135 -0.0170 0.0034 -0.0017 340 PRO A CA 2037 C C . PRO A 254 ? 0.0992 0.0933 0.1045 -0.0071 0.0094 -0.0063 340 PRO A C 2038 O O . PRO A 254 ? 0.1082 0.1094 0.1170 -0.0137 0.0111 -0.0073 340 PRO A O 2039 C CB . PRO A 254 ? 0.1153 0.1073 0.1083 -0.0087 0.0080 -0.0023 340 PRO A CB 2040 C CG . PRO A 254 ? 0.1790 0.1691 0.1803 -0.0241 0.0217 -0.0265 340 PRO A CG 2041 C CD . PRO A 254 ? 0.1023 0.1044 0.0999 -0.0117 -0.0046 -0.0104 340 PRO A CD 2042 N N . LEU A 255 ? 0.0930 0.0918 0.0977 -0.0050 0.0100 -0.0019 341 LEU A N 2043 C CA . LEU A 255 ? 0.1067 0.0951 0.1105 -0.0081 0.0017 0.0082 341 LEU A CA 2044 C C . LEU A 255 ? 0.0960 0.0960 0.0901 -0.0129 0.0072 0.0080 341 LEU A C 2045 O O . LEU A 255 ? 0.1180 0.1028 0.1024 -0.0141 0.0117 0.0026 341 LEU A O 2046 C CB . LEU A 255 ? 0.1113 0.0988 0.1101 -0.0031 -0.0032 -0.0108 341 LEU A CB 2047 C CG . LEU A 255 ? 0.1368 0.1223 0.1545 -0.0009 -0.0038 -0.0033 341 LEU A CG 2048 C CD1 . LEU A 255 ? 0.1508 0.1490 0.1596 0.0184 0.0052 -0.0178 341 LEU A CD1 2049 C CD2 . LEU A 255 ? 0.1910 0.1612 0.2297 -0.0158 0.0127 -0.0003 341 LEU A CD2 2050 N N . LEU A 256 ? 0.0949 0.0848 0.0958 -0.0089 0.0092 0.0000 342 LEU A N 2051 C CA . LEU A 256 ? 0.0786 0.0933 0.0915 -0.0107 0.0121 0.0039 342 LEU A CA 2052 C C . LEU A 256 ? 0.0892 0.0881 0.0952 -0.0089 0.0124 0.0015 342 LEU A C 2053 O O . LEU A 256 ? 0.0909 0.0922 0.0938 -0.0096 0.0126 0.0019 342 LEU A O 2054 C CB . LEU A 256 ? 0.0834 0.0855 0.0911 -0.0107 0.0071 0.0030 342 LEU A CB 2055 C CG . LEU A 256 ? 0.0806 0.0785 0.0892 0.0013 0.0058 -0.0003 342 LEU A CG 2056 C CD1 . LEU A 256 ? 0.0774 0.0806 0.0883 -0.0067 0.0011 0.0048 342 LEU A CD1 2057 C CD2 . LEU A 256 ? 0.0907 0.0945 0.0956 -0.0044 0.0093 -0.0009 342 LEU A CD2 2058 N N . GLU A 257 ? 0.0813 0.0948 0.0979 -0.0080 0.0100 0.0000 343 GLU A N 2059 C CA . GLU A 257 ? 0.0815 0.0964 0.0999 -0.0039 0.0117 0.0000 343 GLU A CA 2060 C C . GLU A 257 ? 0.0859 0.1096 0.1107 -0.0044 0.0094 -0.0004 343 GLU A C 2061 O O . GLU A 257 ? 0.0921 0.1142 0.1102 -0.0165 0.0148 -0.0062 343 GLU A O 2062 C CB A GLU A 257 ? 0.0931 0.1203 0.1209 -0.0082 0.0088 0.0090 343 GLU A CB 2063 C CB B GLU A 257 ? 0.0887 0.1104 0.1119 -0.0111 0.0133 0.0080 343 GLU A CB 2064 C CG A GLU A 257 ? 0.1026 0.1311 0.1487 -0.0137 -0.0025 0.0150 343 GLU A CG 2065 C CG B GLU A 257 ? 0.1039 0.1371 0.1401 -0.0162 -0.0006 0.0139 343 GLU A CG 2066 C CD A GLU A 257 ? 0.1017 0.1157 0.1404 -0.0102 0.0023 0.0076 343 GLU A CD 2067 C CD B GLU A 257 ? 0.1221 0.1563 0.1524 -0.0278 -0.0029 0.0069 343 GLU A CD 2068 O OE1 A GLU A 257 ? 0.1270 0.1871 0.1448 -0.0203 -0.0190 0.0292 343 GLU A OE1 2069 O OE1 B GLU A 257 ? 0.1114 0.1612 0.1361 -0.0179 -0.0192 0.0189 343 GLU A OE1 2070 O OE2 A GLU A 257 ? 0.1225 0.1751 0.1515 -0.0108 -0.0134 0.0232 343 GLU A OE2 2071 O OE2 B GLU A 257 ? 0.1625 0.2287 0.1955 -0.0401 -0.0115 0.0084 343 GLU A OE2 2072 N N . ALA A 258 ? 0.0878 0.0994 0.0994 -0.0096 0.0163 -0.0019 344 ALA A N 2073 C CA . ALA A 258 ? 0.0926 0.1047 0.1126 -0.0186 0.0164 -0.0014 344 ALA A CA 2074 C C . ALA A 258 ? 0.0960 0.0975 0.1038 -0.0203 0.0097 0.0069 344 ALA A C 2075 O O . ALA A 258 ? 0.1089 0.1171 0.1097 -0.0224 0.0148 0.0018 344 ALA A O 2076 C CB . ALA A 258 ? 0.1141 0.1102 0.1085 -0.0166 0.0086 -0.0024 344 ALA A CB 2077 N N . ARG A 259 ? 0.0935 0.0952 0.1017 -0.0228 0.0110 -0.0022 345 ARG A N 2078 C CA . ARG A 259 ? 0.0966 0.1017 0.1111 -0.0182 0.0118 0.0073 345 ARG A CA 2079 C C . ARG A 259 ? 0.0965 0.1080 0.0934 -0.0177 0.0105 -0.0016 345 ARG A C 2080 O O . ARG A 259 ? 0.1031 0.1136 0.1159 -0.0177 0.0084 -0.0109 345 ARG A O 2081 C CB . ARG A 259 ? 0.1009 0.1032 0.1089 -0.0085 0.0073 -0.0051 345 ARG A CB 2082 C CG . ARG A 259 ? 0.1077 0.1075 0.1020 -0.0043 0.0034 0.0069 345 ARG A CG 2083 C CD . ARG A 259 ? 0.1243 0.1263 0.1272 -0.0015 0.0044 0.0040 345 ARG A CD 2084 N NE . ARG A 259 ? 0.1284 0.1367 0.1340 0.0067 -0.0020 0.0037 345 ARG A NE 2085 C CZ . ARG A 259 ? 0.1437 0.1266 0.1277 -0.0010 0.0110 0.0040 345 ARG A CZ 2086 N NH1 . ARG A 259 ? 0.1580 0.1180 0.1223 -0.0075 0.0092 0.0040 345 ARG A NH1 2087 N NH2 . ARG A 259 ? 0.1749 0.1410 0.1588 0.0025 0.0205 0.0107 345 ARG A NH2 2088 N N . GLY A 260 ? 0.0939 0.1014 0.1047 -0.0176 0.0117 -0.0065 346 GLY A N 2089 C CA . GLY A 260 ? 0.0836 0.1092 0.1035 -0.0175 0.0057 -0.0014 346 GLY A CA 2090 C C . GLY A 260 ? 0.0854 0.0931 0.1001 -0.0074 0.0032 0.0009 346 GLY A C 2091 O O . GLY A 260 ? 0.0912 0.1006 0.1000 -0.0080 0.0105 0.0066 346 GLY A O 2092 N N . PHE A 261 ? 0.0862 0.0966 0.0925 -0.0091 0.0072 -0.0031 347 PHE A N 2093 C CA . PHE A 261 ? 0.0776 0.0876 0.0982 -0.0032 0.0064 0.0029 347 PHE A CA 2094 C C . PHE A 261 ? 0.0803 0.0950 0.0985 -0.0082 0.0064 -0.0026 347 PHE A C 2095 O O . PHE A 261 ? 0.0947 0.0926 0.1024 -0.0045 0.0089 0.0016 347 PHE A O 2096 C CB . PHE A 261 ? 0.0838 0.0993 0.0932 -0.0090 0.0024 -0.0005 347 PHE A CB 2097 C CG . PHE A 261 ? 0.0830 0.0863 0.0929 -0.0029 0.0040 -0.0042 347 PHE A CG 2098 C CD1 . PHE A 261 ? 0.0881 0.0961 0.0946 -0.0041 0.0034 0.0008 347 PHE A CD1 2099 C CD2 . PHE A 261 ? 0.0824 0.0905 0.0906 -0.0016 0.0026 0.0020 347 PHE A CD2 2100 C CE1 . PHE A 261 ? 0.0914 0.0954 0.0855 0.0036 0.0104 -0.0044 347 PHE A CE1 2101 C CE2 . PHE A 261 ? 0.0853 0.0961 0.0983 -0.0055 0.0013 -0.0061 347 PHE A CE2 2102 C CZ . PHE A 261 ? 0.0950 0.0875 0.0845 -0.0155 0.0038 -0.0055 347 PHE A CZ 2103 N N . PRO A 262 ? 0.0909 0.1114 0.0922 -0.0016 0.0118 0.0032 348 PRO A N 2104 C CA . PRO A 262 ? 0.0902 0.1167 0.1076 -0.0133 -0.0032 -0.0076 348 PRO A CA 2105 C C . PRO A 262 ? 0.0870 0.1061 0.1034 -0.0009 0.0001 -0.0007 348 PRO A C 2106 O O . PRO A 262 ? 0.0971 0.1207 0.1054 -0.0004 0.0000 0.0059 348 PRO A O 2107 C CB . PRO A 262 ? 0.1028 0.1548 0.1137 -0.0267 -0.0058 0.0189 348 PRO A CB 2108 C CG . PRO A 262 ? 0.1031 0.1810 0.1531 0.0005 0.0009 0.0155 348 PRO A CG 2109 C CD . PRO A 262 ? 0.0993 0.1564 0.1250 0.0071 0.0029 0.0098 348 PRO A CD 2110 N N . ALA A 263 ? 0.0832 0.0927 0.0985 -0.0019 -0.0022 0.0003 349 ALA A N 2111 C CA . ALA A 263 ? 0.0742 0.0826 0.0886 -0.0023 0.0032 -0.0060 349 ALA A CA 2112 C C . ALA A 263 ? 0.0702 0.0882 0.0900 -0.0072 -0.0026 -0.0027 349 ALA A C 2113 O O . ALA A 263 ? 0.0964 0.0906 0.0963 -0.0059 0.0057 0.0014 349 ALA A O 2114 C CB . ALA A 263 ? 0.0869 0.0891 0.0838 -0.0061 0.0063 0.0039 349 ALA A CB 2115 N N . GLN A 264 ? 0.0763 0.0819 0.0787 -0.0003 0.0050 -0.0030 350 GLN A N 2116 C CA . GLN A 264 ? 0.0715 0.0885 0.0813 0.0020 -0.0043 -0.0018 350 GLN A CA 2117 C C . GLN A 264 ? 0.0749 0.0862 0.0728 -0.0022 -0.0086 -0.0028 350 GLN A C 2118 O O . GLN A 264 ? 0.0897 0.1248 0.0943 -0.0154 0.0010 -0.0115 350 GLN A O 2119 C CB . GLN A 264 ? 0.0782 0.0839 0.0851 -0.0019 -0.0020 -0.0009 350 GLN A CB 2120 C CG . GLN A 264 ? 0.0830 0.1023 0.0961 0.0111 -0.0027 0.0042 350 GLN A CG 2121 C CD . GLN A 264 ? 0.0776 0.0935 0.1021 0.0028 -0.0092 0.0014 350 GLN A CD 2122 O OE1 . GLN A 264 ? 0.1181 0.1176 0.1217 -0.0079 -0.0185 0.0020 350 GLN A OE1 2123 N NE2 . GLN A 264 ? 0.0986 0.1153 0.1060 0.0074 -0.0017 -0.0066 350 GLN A NE2 2124 N N . PHE A 265 ? 0.0720 0.0755 0.0690 -0.0035 -0.0053 -0.0030 351 PHE A N 2125 C CA . PHE A 265 ? 0.0696 0.0722 0.0730 0.0037 0.0007 -0.0024 351 PHE A CA 2126 C C . PHE A 265 ? 0.0733 0.0794 0.0685 0.0056 0.0022 -0.0036 351 PHE A C 2127 O O . PHE A 265 ? 0.0762 0.0769 0.0812 -0.0019 -0.0069 0.0019 351 PHE A O 2128 C CB . PHE A 265 ? 0.0680 0.0780 0.0737 -0.0013 -0.0046 -0.0009 351 PHE A CB 2129 C CG . PHE A 265 ? 0.0746 0.0795 0.0723 0.0004 0.0003 -0.0027 351 PHE A CG 2130 C CD1 . PHE A 265 ? 0.0903 0.0887 0.0916 0.0012 0.0000 0.0034 351 PHE A CD1 2131 C CD2 . PHE A 265 ? 0.0840 0.0825 0.0807 -0.0020 -0.0034 -0.0045 351 PHE A CD2 2132 C CE1 . PHE A 265 ? 0.1043 0.0979 0.1110 -0.0047 0.0038 0.0042 351 PHE A CE1 2133 C CE2 . PHE A 265 ? 0.0901 0.0947 0.0825 0.0102 -0.0102 0.0000 351 PHE A CE2 2134 C CZ . PHE A 265 ? 0.1176 0.1008 0.0960 0.0134 0.0043 0.0105 351 PHE A CZ 2135 N N . ILE A 266 ? 0.0686 0.0765 0.0677 0.0041 0.0003 0.0011 352 ILE A N 2136 C CA . ILE A 266 ? 0.0664 0.0684 0.0692 0.0018 -0.0023 0.0023 352 ILE A CA 2137 C C . ILE A 266 ? 0.0670 0.0717 0.0661 0.0037 -0.0015 0.0040 352 ILE A C 2138 O O . ILE A 266 ? 0.0782 0.0847 0.0722 0.0053 0.0010 0.0034 352 ILE A O 2139 C CB . ILE A 266 ? 0.0742 0.0741 0.0719 0.0045 -0.0042 0.0034 352 ILE A CB 2140 C CG1 . ILE A 266 ? 0.0825 0.0805 0.0853 0.0004 -0.0030 -0.0038 352 ILE A CG1 2141 C CG2 . ILE A 266 ? 0.0841 0.0903 0.0804 0.0095 -0.0016 -0.0051 352 ILE A CG2 2142 C CD1 . ILE A 266 ? 0.1011 0.0982 0.0895 0.0003 -0.0062 -0.0085 352 ILE A CD1 2143 N N . VAL A 267 ? 0.0710 0.0700 0.0737 0.0039 -0.0021 0.0040 353 VAL A N 2144 C CA . VAL A 267 ? 0.0658 0.0696 0.0665 0.0050 -0.0004 0.0041 353 VAL A CA 2145 C C . VAL A 267 ? 0.0695 0.0718 0.0591 0.0066 0.0019 0.0007 353 VAL A C 2146 O O . VAL A 267 ? 0.0747 0.0707 0.0722 0.0015 -0.0004 0.0051 353 VAL A O 2147 C CB . VAL A 267 ? 0.0754 0.0762 0.0729 0.0076 -0.0011 0.0041 353 VAL A CB 2148 C CG1 . VAL A 267 ? 0.0940 0.0832 0.0958 0.0020 0.0032 -0.0074 353 VAL A CG1 2149 C CG2 . VAL A 267 ? 0.0827 0.0861 0.0827 0.0042 0.0014 -0.0037 353 VAL A CG2 2150 N N . ASP A 268 ? 0.0649 0.0701 0.0700 0.0013 0.0017 0.0031 354 ASP A N 2151 C CA . ASP A 268 ? 0.0705 0.0698 0.0743 -0.0006 0.0006 0.0022 354 ASP A CA 2152 C C . ASP A 268 ? 0.0650 0.0664 0.0677 0.0054 -0.0007 0.0023 354 ASP A C 2153 O O . ASP A 268 ? 0.0786 0.0746 0.0781 0.0097 0.0042 0.0031 354 ASP A O 2154 C CB . ASP A 268 ? 0.0700 0.0735 0.0644 0.0039 -0.0018 0.0032 354 ASP A CB 2155 C CG . ASP A 268 ? 0.0717 0.0748 0.0607 0.0070 0.0000 -0.0043 354 ASP A CG 2156 O OD1 . ASP A 268 ? 0.0758 0.0721 0.0711 0.0021 -0.0020 0.0008 354 ASP A OD1 2157 O OD2 . ASP A 268 ? 0.0756 0.0720 0.0729 -0.0005 -0.0029 0.0016 354 ASP A OD2 2158 N N . GLN A 269 ? 0.0661 0.0678 0.0680 0.0048 0.0055 0.0010 355 GLN A N 2159 C CA . GLN A 269 ? 0.0719 0.0694 0.0739 0.0067 0.0023 -0.0095 355 GLN A CA 2160 C C . GLN A 269 ? 0.0673 0.0681 0.0758 0.0064 -0.0034 -0.0023 355 GLN A C 2161 O O . GLN A 269 ? 0.0794 0.0819 0.0809 0.0023 -0.0027 0.0019 355 GLN A O 2162 C CB . GLN A 269 ? 0.0846 0.0827 0.0724 0.0025 0.0003 -0.0009 355 GLN A CB 2163 C CG . GLN A 269 ? 0.0773 0.0855 0.0659 0.0059 -0.0028 -0.0012 355 GLN A CG 2164 C CD . GLN A 269 ? 0.0915 0.0945 0.0792 -0.0054 -0.0006 -0.0054 355 GLN A CD 2165 O OE1 . GLN A 269 ? 0.1215 0.1020 0.0976 -0.0097 -0.0002 -0.0121 355 GLN A OE1 2166 N NE2 . GLN A 269 ? 0.0922 0.0862 0.0923 0.0010 -0.0006 -0.0017 355 GLN A NE2 2167 N N . GLY A 270 ? 0.0765 0.0744 0.0673 -0.0004 0.0033 0.0031 356 GLY A N 2168 C CA . GLY A 270 ? 0.0763 0.0728 0.0809 0.0031 -0.0031 -0.0033 356 GLY A CA 2169 C C . GLY A 270 ? 0.0665 0.0652 0.0690 0.0008 0.0007 0.0007 356 GLY A C 2170 O O . GLY A 270 ? 0.0864 0.0786 0.0910 0.0051 0.0095 0.0057 356 GLY A O 2171 N N . ARG A 271 ? 0.0702 0.0717 0.0689 0.0018 0.0041 0.0050 357 ARG A N 2172 C CA . ARG A 271 ? 0.0712 0.0751 0.0710 0.0043 -0.0001 0.0035 357 ARG A CA 2173 C C . ARG A 271 ? 0.0712 0.0771 0.0722 0.0024 0.0081 0.0059 357 ARG A C 2174 O O . ARG A 271 ? 0.0739 0.0769 0.0734 0.0085 0.0036 -0.0024 357 ARG A O 2175 C CB . ARG A 271 ? 0.0726 0.0700 0.0750 -0.0032 0.0041 0.0056 357 ARG A CB 2176 C CG . ARG A 271 ? 0.0784 0.0868 0.0771 0.0014 0.0010 0.0017 357 ARG A CG 2177 C CD . ARG A 271 ? 0.0923 0.0846 0.0821 0.0019 0.0002 0.0050 357 ARG A CD 2178 N NE . ARG A 271 ? 0.0742 0.0837 0.0753 -0.0006 0.0026 0.0017 357 ARG A NE 2179 C CZ . ARG A 271 ? 0.0786 0.0823 0.0684 -0.0061 0.0028 0.0054 357 ARG A CZ 2180 N NH1 . ARG A 271 ? 0.0838 0.1043 0.0839 -0.0036 -0.0124 0.0059 357 ARG A NH1 2181 N NH2 . ARG A 271 ? 0.0809 0.0877 0.0831 0.0016 0.0021 0.0093 357 ARG A NH2 2182 N N . SER A 272 ? 0.0684 0.0736 0.0680 0.0041 0.0009 -0.0013 358 SER A N 2183 C CA . SER A 272 ? 0.0763 0.0713 0.0710 0.0048 0.0013 0.0021 358 SER A CA 2184 C C . SER A 272 ? 0.0799 0.0697 0.0755 0.0065 0.0052 -0.0015 358 SER A C 2185 O O . SER A 272 ? 0.0926 0.0842 0.0780 -0.0011 0.0001 -0.0031 358 SER A O 2186 C CB . SER A 272 ? 0.0757 0.0753 0.0704 0.0000 0.0006 -0.0008 358 SER A CB 2187 O OG . SER A 272 ? 0.0868 0.0841 0.0760 -0.0009 0.0035 0.0005 358 SER A OG 2188 N N . GLY A 273 ? 0.0780 0.0738 0.0666 0.0030 0.0066 -0.0032 359 GLY A N 2189 C CA . GLY A 273 ? 0.0828 0.0821 0.0760 0.0044 0.0012 0.0001 359 GLY A CA 2190 C C . GLY A 273 ? 0.0989 0.0875 0.0690 0.0003 -0.0035 0.0006 359 GLY A C 2191 O O . GLY A 273 ? 0.1141 0.1123 0.0976 0.0172 -0.0091 -0.0098 359 GLY A O 2192 N N . LYS A 274 ? 0.0855 0.0870 0.0743 0.0016 0.0060 -0.0078 360 LYS A N 2193 C CA . LYS A 274 ? 0.0862 0.0915 0.0847 0.0020 0.0117 -0.0042 360 LYS A CA 2194 C C . LYS A 274 ? 0.0741 0.0797 0.0760 -0.0029 0.0015 -0.0066 360 LYS A C 2195 O O . LYS A 274 ? 0.0926 0.0801 0.0804 0.0004 0.0015 0.0009 360 LYS A O 2196 C CB . LYS A 274 ? 0.0936 0.0905 0.0854 0.0024 0.0143 -0.0013 360 LYS A CB 2197 C CG . LYS A 274 ? 0.0889 0.0918 0.0932 0.0030 0.0034 -0.0040 360 LYS A CG 2198 C CD . LYS A 274 ? 0.1044 0.1046 0.0960 -0.0005 0.0137 0.0087 360 LYS A CD 2199 C CE . LYS A 274 ? 0.1051 0.1222 0.1129 0.0068 0.0138 0.0106 360 LYS A CE 2200 N NZ . LYS A 274 ? 0.1166 0.1224 0.1118 0.0083 0.0257 0.0132 360 LYS A NZ 2201 N N . GLN A 275 ? 0.0994 0.0913 0.0740 -0.0062 0.0077 -0.0082 361 GLN A N 2202 C CA . GLN A 275 ? 0.0997 0.0930 0.0752 0.0063 0.0013 -0.0086 361 GLN A CA 2203 C C . GLN A 275 ? 0.0976 0.0954 0.0768 0.0023 -0.0018 -0.0071 361 GLN A C 2204 O O . GLN A 275 ? 0.1232 0.1182 0.0961 0.0130 0.0028 -0.0089 361 GLN A O 2205 C CB . GLN A 275 ? 0.1018 0.0914 0.0769 -0.0028 -0.0048 -0.0076 361 GLN A CB 2206 C CG . GLN A 275 ? 0.0834 0.0858 0.0814 -0.0018 0.0002 -0.0006 361 GLN A CG 2207 C CD . GLN A 275 ? 0.0856 0.0739 0.0840 -0.0045 -0.0004 0.0009 361 GLN A CD 2208 O OE1 . GLN A 275 ? 0.0977 0.0902 0.0870 0.0068 -0.0014 -0.0022 361 GLN A OE1 2209 N NE2 . GLN A 275 ? 0.0810 0.0863 0.0772 -0.0046 0.0070 -0.0052 361 GLN A NE2 2210 N N . PRO A 276 ? 0.1024 0.0984 0.0877 0.0060 0.0091 -0.0151 362 PRO A N 2211 C CA . PRO A 276 ? 0.0982 0.0956 0.0876 0.0011 0.0065 -0.0035 362 PRO A CA 2212 C C . PRO A 276 ? 0.0844 0.0846 0.0817 0.0012 0.0053 0.0012 362 PRO A C 2213 O O . PRO A 276 ? 0.0975 0.0998 0.0846 -0.0013 0.0052 0.0029 362 PRO A O 2214 C CB . PRO A 276 ? 0.1196 0.1051 0.1067 -0.0045 0.0065 -0.0047 362 PRO A CB 2215 C CG . PRO A 276 ? 0.1423 0.1299 0.1437 0.0263 0.0055 -0.0075 362 PRO A CG 2216 C CD . PRO A 276 ? 0.1235 0.1204 0.1083 0.0177 0.0016 -0.0140 362 PRO A CD 2217 N N . THR A 277 ? 0.0831 0.0856 0.0811 0.0058 0.0126 0.0000 363 THR A N 2218 C CA . THR A 277 ? 0.0883 0.0822 0.0721 0.0074 0.0065 -0.0047 363 THR A CA 2219 C C . THR A 277 ? 0.0904 0.0772 0.0772 0.0067 -0.0004 -0.0004 363 THR A C 2220 O O . THR A 277 ? 0.0969 0.0954 0.0984 0.0102 0.0024 -0.0104 363 THR A O 2221 C CB . THR A 277 ? 0.0906 0.0826 0.0882 0.0056 0.0029 -0.0042 363 THR A CB 2222 O OG1 . THR A 277 ? 0.0957 0.0926 0.0786 0.0091 0.0035 0.0006 363 THR A OG1 2223 C CG2 . THR A 277 ? 0.0972 0.0909 0.0862 0.0105 0.0150 0.0038 363 THR A CG2 2224 N N . GLY A 278 ? 0.0856 0.0839 0.0847 0.0083 0.0037 0.0001 364 GLY A N 2225 C CA . GLY A 278 ? 0.0903 0.0930 0.0818 0.0064 0.0084 0.0067 364 GLY A CA 2226 C C . GLY A 278 ? 0.0840 0.0947 0.0884 0.0095 0.0012 0.0038 364 GLY A C 2227 O O . GLY A 278 ? 0.0931 0.1097 0.0952 0.0017 0.0010 0.0015 364 GLY A O 2228 N N . GLN A 279 ? 0.0874 0.0990 0.0782 0.0084 0.0014 0.0071 365 GLN A N 2229 C CA . GLN A 279 ? 0.0937 0.0949 0.0836 0.0073 0.0008 0.0060 365 GLN A CA 2230 C C . GLN A 279 ? 0.0933 0.0919 0.0888 0.0051 0.0020 0.0035 365 GLN A C 2231 O O . GLN A 279 ? 0.1056 0.1045 0.1049 0.0099 -0.0051 -0.0018 365 GLN A O 2232 C CB . GLN A 279 ? 0.0919 0.0926 0.0811 0.0080 -0.0003 0.0024 365 GLN A CB 2233 C CG . GLN A 279 ? 0.1005 0.0857 0.0858 0.0041 -0.0151 0.0000 365 GLN A CG 2234 C CD . GLN A 279 ? 0.0938 0.0795 0.0768 0.0066 0.0008 0.0013 365 GLN A CD 2235 O OE1 . GLN A 279 ? 0.0924 0.0979 0.0861 -0.0018 0.0002 -0.0019 365 GLN A OE1 2236 N NE2 . GLN A 279 ? 0.1050 0.0948 0.0770 0.0118 0.0015 0.0018 365 GLN A NE2 2237 N N . LYS A 280 ? 0.0870 0.0896 0.0946 0.0081 0.0009 0.0010 366 LYS A N 2238 C CA . LYS A 280 ? 0.0942 0.1021 0.1095 0.0109 -0.0006 -0.0023 366 LYS A CA 2239 C C . LYS A 280 ? 0.0921 0.0876 0.1017 0.0086 -0.0012 -0.0085 366 LYS A C 2240 O O . LYS A 280 ? 0.1153 0.1088 0.1164 0.0117 0.0112 -0.0059 366 LYS A O 2241 C CB . LYS A 280 ? 0.1028 0.1134 0.1243 0.0150 0.0063 0.0040 366 LYS A CB 2242 C CG . LYS A 280 ? 0.1436 0.1564 0.1841 0.0165 0.0109 -0.0007 366 LYS A CG 2243 C CD . LYS A 280 ? 0.2582 0.2653 0.2518 -0.0139 0.0255 -0.0099 366 LYS A CD 2244 C CE . LYS A 280 ? 0.3607 0.3612 0.3637 0.0144 0.0069 0.0036 366 LYS A CE 2245 N NZ . LYS A 280 ? 0.4134 0.4562 0.4623 -0.0156 0.0139 -0.0010 366 LYS A NZ 2246 N N . GLU A 281 ? 0.0883 0.0835 0.0842 0.0099 0.0052 0.0034 367 GLU A N 2247 C CA . GLU A 281 ? 0.0811 0.0850 0.0844 0.0075 0.0014 0.0006 367 GLU A CA 2248 C C . GLU A 281 ? 0.0794 0.0823 0.0791 0.0008 -0.0034 0.0045 367 GLU A C 2249 O O . GLU A 281 ? 0.0881 0.0883 0.0887 0.0097 0.0010 0.0000 367 GLU A O 2250 C CB . GLU A 281 ? 0.0881 0.0952 0.0910 0.0050 0.0008 0.0051 367 GLU A CB 2251 C CG . GLU A 281 ? 0.0953 0.1076 0.1079 0.0107 -0.0097 0.0124 367 GLU A CG 2252 C CD . GLU A 281 ? 0.1048 0.1165 0.1287 0.0256 0.0075 0.0060 367 GLU A CD 2253 O OE1 . GLU A 281 ? 0.1337 0.1067 0.1522 0.0117 0.0027 0.0034 367 GLU A OE1 2254 O OE2 . GLU A 281 ? 0.1197 0.1283 0.1327 0.0213 0.0055 0.0053 367 GLU A OE2 2255 N N . TRP A 282 ? 0.0811 0.0782 0.0928 0.0083 -0.0021 0.0084 368 TRP A N 2256 C CA . TRP A 282 ? 0.0820 0.0863 0.1001 0.0078 -0.0002 0.0039 368 TRP A CA 2257 C C . TRP A 282 ? 0.0765 0.0848 0.0893 0.0022 0.0086 0.0067 368 TRP A C 2258 O O . TRP A 282 ? 0.0937 0.0970 0.1083 0.0081 0.0028 -0.0011 368 TRP A O 2259 C CB . TRP A 282 ? 0.0853 0.0747 0.1024 0.0091 0.0010 0.0032 368 TRP A CB 2260 C CG . TRP A 282 ? 0.0769 0.0795 0.0852 0.0017 0.0047 0.0085 368 TRP A CG 2261 C CD1 . TRP A 282 ? 0.0810 0.0909 0.1020 0.0018 -0.0028 0.0033 368 TRP A CD1 2262 C CD2 . TRP A 282 ? 0.0841 0.0862 0.0869 0.0023 0.0045 0.0007 368 TRP A CD2 2263 N NE1 . TRP A 282 ? 0.0850 0.0875 0.1015 0.0087 -0.0001 0.0106 368 TRP A NE1 2264 C CE2 . TRP A 282 ? 0.0792 0.0878 0.0857 0.0016 0.0051 -0.0081 368 TRP A CE2 2265 C CE3 . TRP A 282 ? 0.0875 0.0907 0.0980 0.0000 0.0055 -0.0021 368 TRP A CE3 2266 C CZ2 . TRP A 282 ? 0.0938 0.1110 0.0948 0.0000 0.0073 0.0029 368 TRP A CZ2 2267 C CZ3 . TRP A 282 ? 0.0973 0.0943 0.0927 -0.0043 0.0091 0.0001 368 TRP A CZ3 2268 C CH2 . TRP A 282 ? 0.0845 0.1055 0.0950 -0.0113 0.0025 -0.0044 368 TRP A CH2 2269 N N . GLY A 283 ? 0.0902 0.0864 0.0891 -0.0016 -0.0015 0.0028 369 GLY A N 2270 C CA . GLY A 283 ? 0.0981 0.1036 0.0922 0.0100 0.0019 0.0037 369 GLY A CA 2271 C C . GLY A 283 ? 0.1011 0.0964 0.0854 0.0047 0.0017 -0.0028 369 GLY A C 2272 O O . GLY A 283 ? 0.1090 0.0987 0.0947 -0.0025 0.0019 0.0023 369 GLY A O 2273 N N . HIS A 284 ? 0.0942 0.0871 0.0819 -0.0016 0.0013 -0.0015 370 HIS A N 2274 C CA . HIS A 284 ? 0.0854 0.0862 0.0824 -0.0002 -0.0030 -0.0058 370 HIS A CA 2275 C C . HIS A 284 ? 0.0866 0.0905 0.0776 0.0047 -0.0002 0.0069 370 HIS A C 2276 O O . HIS A 284 ? 0.1086 0.1067 0.0918 0.0093 -0.0060 0.0017 370 HIS A O 2277 C CB . HIS A 284 ? 0.0867 0.0851 0.0912 0.0036 -0.0084 0.0034 370 HIS A CB 2278 C CG . HIS A 284 ? 0.0955 0.0894 0.0887 0.0023 -0.0072 -0.0045 370 HIS A CG 2279 N ND1 . HIS A 284 ? 0.0949 0.0915 0.0962 0.0105 -0.0031 0.0022 370 HIS A ND1 2280 C CD2 . HIS A 284 ? 0.0958 0.1056 0.1030 -0.0025 -0.0066 0.0027 370 HIS A CD2 2281 C CE1 . HIS A 284 ? 0.1003 0.1024 0.1272 0.0080 0.0021 -0.0001 370 HIS A CE1 2282 N NE2 . HIS A 284 ? 0.0945 0.0960 0.1157 -0.0023 -0.0092 0.0073 370 HIS A NE2 2283 N N . TRP A 285 ? 0.0856 0.0871 0.0803 0.0053 -0.0109 0.0010 371 TRP A N 2284 C CA . TRP A 285 ? 0.0866 0.0911 0.0838 0.0020 -0.0021 0.0048 371 TRP A CA 2285 C C . TRP A 285 ? 0.0817 0.0881 0.0736 0.0059 -0.0057 -0.0019 371 TRP A C 2286 O O . TRP A 285 ? 0.0822 0.0860 0.0827 0.0044 -0.0033 -0.0006 371 TRP A O 2287 C CB . TRP A 285 ? 0.0808 0.0900 0.0880 -0.0030 0.0063 -0.0044 371 TRP A CB 2288 C CG . TRP A 285 ? 0.0842 0.0945 0.0857 0.0047 0.0021 0.0022 371 TRP A CG 2289 C CD1 . TRP A 285 ? 0.1040 0.1023 0.0998 0.0044 0.0068 -0.0037 371 TRP A CD1 2290 C CD2 . TRP A 285 ? 0.0907 0.0975 0.0778 0.0031 0.0014 0.0015 371 TRP A CD2 2291 N NE1 . TRP A 285 ? 0.1140 0.1182 0.0967 0.0135 -0.0017 0.0051 371 TRP A NE1 2292 C CE2 . TRP A 285 ? 0.0886 0.1047 0.0809 0.0065 0.0062 -0.0041 371 TRP A CE2 2293 C CE3 . TRP A 285 ? 0.0941 0.1039 0.0799 -0.0019 0.0033 -0.0077 371 TRP A CE3 2294 C CZ2 . TRP A 285 ? 0.0877 0.1124 0.0912 0.0060 0.0001 -0.0019 371 TRP A CZ2 2295 C CZ3 . TRP A 285 ? 0.0964 0.1016 0.0972 -0.0038 0.0032 0.0020 371 TRP A CZ3 2296 C CH2 . TRP A 285 ? 0.0961 0.1212 0.1081 -0.0120 -0.0056 -0.0138 371 TRP A CH2 2297 N N . CYS A 286 ? 0.0788 0.0869 0.0885 0.0029 0.0010 -0.0037 372 CYS A N 2298 C CA . CYS A 286 ? 0.0762 0.0888 0.0833 -0.0012 -0.0010 -0.0021 372 CYS A CA 2299 C C . CYS A 286 ? 0.0767 0.0867 0.0820 0.0020 -0.0018 -0.0068 372 CYS A C 2300 O O . CYS A 286 ? 0.0897 0.0953 0.0931 0.0066 0.0055 0.0026 372 CYS A O 2301 C CB . CYS A 286 ? 0.0835 0.0951 0.0883 -0.0035 0.0000 -0.0001 372 CYS A CB 2302 S SG . CYS A 286 ? 0.0870 0.0921 0.0967 0.0011 -0.0076 0.0012 372 CYS A SG 2303 N N . ASN A 287 ? 0.0731 0.0853 0.0824 0.0036 0.0023 -0.0007 373 ASN A N 2304 C CA . ASN A 287 ? 0.0755 0.0859 0.0776 0.0053 0.0020 0.0003 373 ASN A CA 2305 C C . ASN A 287 ? 0.0811 0.0823 0.0786 0.0056 0.0019 0.0049 373 ASN A C 2306 O O . ASN A 287 ? 0.0800 0.0921 0.0872 0.0016 0.0012 0.0043 373 ASN A O 2307 C CB . ASN A 287 ? 0.0867 0.0943 0.0842 0.0030 -0.0019 -0.0008 373 ASN A CB 2308 C CG . ASN A 287 ? 0.0875 0.0853 0.0840 0.0042 -0.0006 -0.0029 373 ASN A CG 2309 O OD1 . ASN A 287 ? 0.0857 0.0965 0.0993 -0.0014 -0.0056 -0.0065 373 ASN A OD1 2310 N ND2 . ASN A 287 ? 0.0883 0.0977 0.0971 -0.0087 -0.0052 -0.0054 373 ASN A ND2 2311 N N . ALA A 288 ? 0.0793 0.0812 0.0784 0.0013 0.0033 0.0008 374 ALA A N 2312 C CA . ALA A 288 ? 0.0810 0.0814 0.0798 0.0037 0.0007 0.0043 374 ALA A CA 2313 C C . ALA A 288 ? 0.0680 0.0832 0.0850 0.0030 0.0049 0.0041 374 ALA A C 2314 O O . ALA A 288 ? 0.0872 0.0825 0.0839 0.0089 0.0044 0.0004 374 ALA A O 2315 C CB . ALA A 288 ? 0.0938 0.0882 0.0883 -0.0036 0.0055 0.0023 374 ALA A CB 2316 N N . ILE A 289 ? 0.0852 0.0881 0.0846 0.0040 0.0038 -0.0008 375 ILE A N 2317 C CA . ILE A 289 ? 0.0853 0.0894 0.0850 0.0044 0.0038 0.0010 375 ILE A CA 2318 C C . ILE A 289 ? 0.0848 0.0856 0.0855 0.0017 0.0076 0.0027 375 ILE A C 2319 O O . ILE A 289 ? 0.0875 0.0886 0.0818 0.0000 0.0061 0.0007 375 ILE A O 2320 C CB . ILE A 289 ? 0.0946 0.1083 0.0883 0.0013 0.0004 -0.0065 375 ILE A CB 2321 C CG1 . ILE A 289 ? 0.1022 0.1153 0.1002 0.0096 0.0015 -0.0013 375 ILE A CG1 2322 C CG2 . ILE A 289 ? 0.0994 0.1114 0.1105 -0.0050 0.0030 0.0007 375 ILE A CG2 2323 C CD1 . ILE A 289 ? 0.1101 0.1265 0.1162 0.0077 0.0058 -0.0030 375 ILE A CD1 2324 N N . GLY A 290 ? 0.0893 0.0922 0.0875 0.0009 0.0082 0.0056 376 GLY A N 2325 C CA . GLY A 290 ? 0.0906 0.0854 0.0763 0.0066 0.0046 0.0043 376 GLY A CA 2326 C C . GLY A 290 ? 0.0867 0.0806 0.0713 0.0018 0.0032 0.0084 376 GLY A C 2327 O O . GLY A 290 ? 0.0895 0.0981 0.1038 0.0037 0.0059 -0.0058 376 GLY A O 2328 N N . THR A 291 ? 0.0770 0.0901 0.0799 0.0033 0.0069 0.0006 377 THR A N 2329 C CA . THR A 291 ? 0.0837 0.0791 0.0777 0.0025 0.0028 0.0006 377 THR A CA 2330 C C . THR A 291 ? 0.0829 0.0824 0.0705 -0.0042 0.0023 -0.0008 377 THR A C 2331 O O . THR A 291 ? 0.0913 0.0892 0.0826 -0.0009 0.0045 0.0005 377 THR A O 2332 C CB . THR A 291 ? 0.0853 0.0881 0.0786 -0.0021 0.0041 0.0054 377 THR A CB 2333 O OG1 . THR A 291 ? 0.0888 0.0887 0.0811 0.0006 0.0028 -0.0005 377 THR A OG1 2334 C CG2 . THR A 291 ? 0.0885 0.0978 0.0802 0.0090 0.0016 0.0126 377 THR A CG2 2335 N N . GLY A 292 ? 0.0798 0.0811 0.0722 0.0043 0.0041 0.0008 378 GLY A N 2336 C CA . GLY A 292 ? 0.0871 0.0800 0.0755 0.0000 0.0008 0.0010 378 GLY A CA 2337 C C . GLY A 292 ? 0.0807 0.0805 0.0735 0.0014 -0.0019 0.0008 378 GLY A C 2338 O O . GLY A 292 ? 0.0778 0.0814 0.0782 0.0027 0.0022 0.0020 378 GLY A O 2339 N N . PHE A 293 ? 0.0829 0.0812 0.0794 -0.0012 0.0029 0.0012 379 PHE A N 2340 C CA . PHE A 293 ? 0.0883 0.0781 0.0766 0.0051 0.0005 -0.0007 379 PHE A CA 2341 C C . PHE A 293 ? 0.0904 0.0831 0.0740 0.0059 0.0001 0.0008 379 PHE A C 2342 O O . PHE A 293 ? 0.0952 0.0908 0.0765 0.0001 -0.0003 0.0002 379 PHE A O 2343 C CB . PHE A 293 ? 0.0927 0.0880 0.0745 0.0051 0.0054 0.0081 379 PHE A CB 2344 C CG . PHE A 293 ? 0.0911 0.0870 0.0826 0.0105 0.0012 0.0096 379 PHE A CG 2345 C CD1 . PHE A 293 ? 0.1047 0.0832 0.0849 0.0001 -0.0069 0.0013 379 PHE A CD1 2346 C CD2 . PHE A 293 ? 0.1043 0.0929 0.0935 0.0041 -0.0018 0.0063 379 PHE A CD2 2347 C CE1 . PHE A 293 ? 0.1131 0.0939 0.0957 0.0006 -0.0057 0.0019 379 PHE A CE1 2348 C CE2 . PHE A 293 ? 0.1138 0.1011 0.1181 0.0000 -0.0012 0.0087 379 PHE A CE2 2349 C CZ . PHE A 293 ? 0.1127 0.0970 0.1139 -0.0011 -0.0173 -0.0020 379 PHE A CZ 2350 N N . GLY A 294 ? 0.0887 0.0869 0.0810 0.0045 0.0025 -0.0020 380 GLY A N 2351 C CA . GLY A 294 ? 0.0951 0.0916 0.0858 0.0067 -0.0062 0.0044 380 GLY A CA 2352 C C . GLY A 294 ? 0.0940 0.0854 0.0841 0.0022 0.0022 -0.0034 380 GLY A C 2353 O O . GLY A 294 ? 0.1025 0.1091 0.0955 0.0113 -0.0030 -0.0040 380 GLY A O 2354 N N . MET A 295 ? 0.0956 0.1032 0.1098 0.0055 -0.0039 -0.0067 381 MET A N 2355 C CA . MET A 295 ? 0.1025 0.1265 0.1146 0.0078 -0.0027 -0.0148 381 MET A CA 2356 C C . MET A 295 ? 0.1011 0.1013 0.0888 0.0003 0.0000 -0.0044 381 MET A C 2357 O O . MET A 295 ? 0.0924 0.1104 0.1011 0.0083 -0.0067 -0.0054 381 MET A O 2358 C CB A MET A 295 ? 0.1285 0.1361 0.1733 0.0045 0.0024 -0.0169 381 MET A CB 2359 C CB B MET A 295 ? 0.1355 0.1411 0.1715 0.0028 0.0032 -0.0157 381 MET A CB 2360 C CG A MET A 295 ? 0.1189 0.1190 0.1565 0.0209 -0.0142 -0.0174 381 MET A CG 2361 C CG B MET A 295 ? 0.1501 0.1790 0.1627 0.0090 -0.0016 -0.0245 381 MET A CG 2362 S SD A MET A 295 ? 0.1614 0.1922 0.1778 -0.0193 0.0007 0.0122 381 MET A SD 2363 S SD B MET A 295 ? 0.1831 0.2384 0.1274 -0.0317 0.0200 -0.0067 381 MET A SD 2364 C CE A MET A 295 ? 0.1421 0.1012 0.1384 -0.0270 -0.0456 0.0233 381 MET A CE 2365 C CE B MET A 295 ? 0.0749 0.0656 0.0676 -0.0152 -0.0328 0.0021 381 MET A CE 2366 N N . ARG A 296 ? 0.1040 0.1076 0.0998 0.0099 -0.0105 -0.0063 382 ARG A N 2367 C CA . ARG A 296 ? 0.1034 0.0984 0.0987 0.0033 -0.0059 -0.0069 382 ARG A CA 2368 C C . ARG A 296 ? 0.0832 0.0803 0.0912 0.0025 -0.0082 0.0010 382 ARG A C 2369 O O . ARG A 296 ? 0.0970 0.0994 0.1051 0.0071 -0.0060 -0.0076 382 ARG A O 2370 C CB . ARG A 296 ? 0.1108 0.1227 0.1108 0.0017 0.0008 0.0075 382 ARG A CB 2371 C CG A ARG A 296 ? 0.1382 0.1250 0.1188 -0.0036 -0.0040 0.0096 382 ARG A CG 2372 C CG B ARG A 296 ? 0.1471 0.1431 0.1309 -0.0007 0.0000 0.0073 382 ARG A CG 2373 C CD A ARG A 296 ? 0.1257 0.1180 0.1091 -0.0133 0.0085 -0.0013 382 ARG A CD 2374 C CD B ARG A 296 ? 0.1352 0.1250 0.1113 -0.0109 0.0088 0.0023 382 ARG A CD 2375 N NE A ARG A 296 ? 0.1539 0.1324 0.1239 0.0012 0.0189 0.0228 382 ARG A NE 2376 N NE B ARG A 296 ? 0.1229 0.1299 0.1155 0.0128 0.0097 0.0148 382 ARG A NE 2377 C CZ A ARG A 296 ? 0.1339 0.1265 0.1441 -0.0053 0.0026 0.0012 382 ARG A CZ 2378 C CZ B ARG A 296 ? 0.1147 0.1222 0.1169 -0.0044 0.0030 0.0061 382 ARG A CZ 2379 N NH1 A ARG A 296 ? 0.1447 0.1206 0.1186 -0.0046 0.0051 0.0065 382 ARG A NH1 2380 N NH1 B ARG A 296 ? 0.1550 0.1251 0.1417 0.0063 0.0193 0.0101 382 ARG A NH1 2381 N NH2 A ARG A 296 ? 0.1593 0.1132 0.1277 0.0031 0.0159 -0.0042 382 ARG A NH2 2382 N NH2 B ARG A 296 ? 0.1345 0.1070 0.0993 0.0088 -0.0041 0.0072 382 ARG A NH2 2383 N N . PRO A 297 ? 0.0872 0.0863 0.0875 0.0012 -0.0048 -0.0003 383 PRO A N 2384 C CA . PRO A 297 ? 0.0853 0.0906 0.0959 0.0082 -0.0069 0.0052 383 PRO A CA 2385 C C . PRO A 297 ? 0.0883 0.0887 0.0865 0.0034 -0.0040 0.0062 383 PRO A C 2386 O O . PRO A 297 ? 0.0943 0.0903 0.1025 0.0049 -0.0105 0.0136 383 PRO A O 2387 C CB . PRO A 297 ? 0.0891 0.0966 0.0922 0.0049 -0.0068 0.0037 383 PRO A CB 2388 C CG . PRO A 297 ? 0.0940 0.0923 0.0876 0.0039 -0.0116 0.0034 383 PRO A CG 2389 C CD . PRO A 297 ? 0.0885 0.0869 0.0952 -0.0042 -0.0014 -0.0004 383 PRO A CD 2390 N N . THR A 298 ? 0.0835 0.0891 0.0919 0.0062 -0.0059 0.0074 384 THR A N 2391 C CA . THR A 298 ? 0.0827 0.0916 0.0909 0.0098 -0.0139 0.0052 384 THR A CA 2392 C C . THR A 298 ? 0.0910 0.0864 0.0919 0.0052 -0.0112 -0.0020 384 THR A C 2393 O O . THR A 298 ? 0.0885 0.0937 0.1014 0.0011 -0.0108 0.0047 384 THR A O 2394 C CB . THR A 298 ? 0.0967 0.1143 0.1001 -0.0039 -0.0106 0.0045 384 THR A CB 2395 O OG1 . THR A 298 ? 0.1082 0.1263 0.1140 -0.0001 -0.0173 0.0054 384 THR A OG1 2396 C CG2 . THR A 298 ? 0.1073 0.1248 0.1092 -0.0068 -0.0120 -0.0127 384 THR A CG2 2397 N N . ALA A 299 ? 0.0896 0.0871 0.0896 0.0076 -0.0116 0.0059 385 ALA A N 2398 C CA . ALA A 299 ? 0.0867 0.1070 0.0915 0.0028 -0.0157 -0.0015 385 ALA A CA 2399 C C . ALA A 299 ? 0.0899 0.0939 0.0983 -0.0025 -0.0072 0.0069 385 ALA A C 2400 O O . ALA A 299 ? 0.1144 0.1196 0.1126 -0.0044 -0.0056 0.0044 385 ALA A O 2401 C CB . ALA A 299 ? 0.1091 0.1197 0.1074 0.0067 -0.0083 -0.0019 385 ALA A CB 2402 N N . ASN A 300 ? 0.0928 0.0929 0.0994 -0.0058 -0.0134 -0.0021 386 ASN A N 2403 C CA . ASN A 300 ? 0.1146 0.1139 0.1024 -0.0040 -0.0192 0.0000 386 ASN A CA 2404 C C . ASN A 300 ? 0.1198 0.1163 0.0952 -0.0092 -0.0137 -0.0064 386 ASN A C 2405 O O . ASN A 300 ? 0.1344 0.1198 0.1015 -0.0033 -0.0039 0.0037 386 ASN A O 2406 C CB . ASN A 300 ? 0.1336 0.1300 0.1118 -0.0054 -0.0292 -0.0065 386 ASN A CB 2407 C CG . ASN A 300 ? 0.1771 0.1541 0.1314 -0.0071 -0.0355 0.0116 386 ASN A CG 2408 O OD1 . ASN A 300 ? 0.1715 0.1790 0.1903 0.0200 -0.0317 0.0131 386 ASN A OD1 2409 N ND2 . ASN A 300 ? 0.2181 0.1715 0.1925 -0.0079 -0.0290 0.0089 386 ASN A ND2 2410 N N . THR A 301 ? 0.1121 0.1081 0.0913 -0.0076 -0.0057 -0.0001 387 THR A N 2411 C CA . THR A 301 ? 0.0959 0.1085 0.0875 -0.0169 -0.0085 -0.0066 387 THR A CA 2412 C C . THR A 301 ? 0.0976 0.0936 0.0871 -0.0070 -0.0059 0.0015 387 THR A C 2413 O O . THR A 301 ? 0.1038 0.1203 0.1047 -0.0031 -0.0086 -0.0061 387 THR A O 2414 C CB . THR A 301 ? 0.1098 0.1050 0.0913 -0.0079 -0.0180 -0.0056 387 THR A CB 2415 O OG1 . THR A 301 ? 0.1105 0.1033 0.0908 -0.0117 -0.0075 -0.0007 387 THR A OG1 2416 C CG2 . THR A 301 ? 0.1339 0.1109 0.0957 -0.0198 -0.0206 -0.0081 387 THR A CG2 2417 N N . GLY A 302 ? 0.0954 0.0974 0.0875 -0.0048 -0.0165 -0.0075 388 GLY A N 2418 C CA . GLY A 302 ? 0.0998 0.0972 0.0920 -0.0077 -0.0060 -0.0095 388 GLY A CA 2419 C C . GLY A 302 ? 0.0873 0.0892 0.0836 -0.0098 -0.0100 -0.0095 388 GLY A C 2420 O O . GLY A 302 ? 0.1053 0.1021 0.0943 -0.0112 -0.0104 -0.0064 388 GLY A O 2421 N N . HIS A 303 ? 0.0990 0.0937 0.0860 -0.0095 -0.0098 -0.0035 389 HIS A N 2422 C CA . HIS A 303 ? 0.0930 0.0985 0.0888 -0.0052 -0.0159 -0.0018 389 HIS A CA 2423 C C . HIS A 303 ? 0.0885 0.0861 0.0850 -0.0041 -0.0146 -0.0030 389 HIS A C 2424 O O . HIS A 303 ? 0.1033 0.0948 0.0941 -0.0005 -0.0095 -0.0075 389 HIS A O 2425 C CB . HIS A 303 ? 0.0960 0.1011 0.0863 -0.0030 -0.0068 -0.0103 389 HIS A CB 2426 C CG . HIS A 303 ? 0.0851 0.0967 0.0868 -0.0029 -0.0025 -0.0063 389 HIS A CG 2427 N ND1 . HIS A 303 ? 0.1030 0.1010 0.0916 0.0059 -0.0132 -0.0065 389 HIS A ND1 2428 C CD2 . HIS A 303 ? 0.0932 0.0961 0.0864 -0.0081 -0.0144 -0.0065 389 HIS A CD2 2429 C CE1 . HIS A 303 ? 0.1040 0.1082 0.0976 0.0024 -0.0027 0.0009 389 HIS A CE1 2430 N NE2 . HIS A 303 ? 0.0902 0.1080 0.0926 -0.0025 -0.0098 0.0031 389 HIS A NE2 2431 N N . GLN A 304 ? 0.0919 0.0954 0.0919 -0.0053 -0.0129 -0.0027 390 GLN A N 2432 C CA . GLN A 304 ? 0.0969 0.1036 0.1042 -0.0064 -0.0163 -0.0046 390 GLN A CA 2433 C C . GLN A 304 ? 0.0961 0.1007 0.0927 0.0021 -0.0007 -0.0060 390 GLN A C 2434 O O . GLN A 304 ? 0.1106 0.1352 0.1113 0.0109 -0.0083 -0.0108 390 GLN A O 2435 C CB . GLN A 304 ? 0.1154 0.1410 0.1345 -0.0122 -0.0130 -0.0122 390 GLN A CB 2436 C CG . GLN A 304 ? 0.1820 0.1957 0.1964 -0.0131 -0.0057 -0.0061 390 GLN A CG 2437 C CD . GLN A 304 ? 0.2333 0.2751 0.2496 0.0096 0.0044 -0.0019 390 GLN A CD 2438 O OE1 . GLN A 304 ? 0.2793 0.3758 0.2703 0.0244 -0.0219 -0.0137 390 GLN A OE1 2439 N NE2 . GLN A 304 ? 0.3261 0.3554 0.3379 0.0422 0.0308 -0.0264 390 GLN A NE2 2440 N N . TYR A 305 ? 0.0837 0.0889 0.0819 0.0003 -0.0092 -0.0081 391 TYR A N 2441 C CA . TYR A 305 ? 0.0809 0.0889 0.0818 -0.0048 -0.0128 -0.0076 391 TYR A CA 2442 C C . TYR A 305 ? 0.0901 0.0906 0.0775 0.0039 -0.0147 -0.0056 391 TYR A C 2443 O O . TYR A 305 ? 0.0985 0.0943 0.0838 -0.0042 -0.0138 -0.0100 391 TYR A O 2444 C CB . TYR A 305 ? 0.0901 0.0937 0.0906 -0.0115 -0.0067 -0.0051 391 TYR A CB 2445 C CG . TYR A 305 ? 0.1202 0.1038 0.0891 -0.0093 -0.0108 -0.0091 391 TYR A CG 2446 C CD1 . TYR A 305 ? 0.1192 0.1061 0.0998 -0.0130 -0.0124 0.0037 391 TYR A CD1 2447 C CD2 . TYR A 305 ? 0.1316 0.1223 0.1033 -0.0116 -0.0085 -0.0072 391 TYR A CD2 2448 C CE1 . TYR A 305 ? 0.1239 0.1432 0.1190 -0.0126 -0.0048 0.0158 391 TYR A CE1 2449 C CE2 . TYR A 305 ? 0.1651 0.1205 0.1151 -0.0012 0.0019 -0.0096 391 TYR A CE2 2450 C CZ . TYR A 305 ? 0.1535 0.1286 0.1196 -0.0390 -0.0057 0.0064 391 TYR A CZ 2451 O OH . TYR A 305 ? 0.1946 0.1417 0.1661 -0.0550 0.0021 -0.0029 391 TYR A OH 2452 N N . VAL A 306 ? 0.0827 0.0790 0.0708 0.0026 -0.0115 -0.0070 392 VAL A N 2453 C CA . VAL A 306 ? 0.0801 0.0757 0.0770 0.0040 -0.0110 -0.0057 392 VAL A CA 2454 C C . VAL A 306 ? 0.0738 0.0859 0.0686 -0.0009 -0.0085 -0.0032 392 VAL A C 2455 O O . VAL A 306 ? 0.0930 0.0903 0.0808 0.0031 -0.0146 -0.0030 392 VAL A O 2456 C CB . VAL A 306 ? 0.0879 0.0893 0.0888 0.0018 -0.0115 -0.0095 392 VAL A CB 2457 C CG1 . VAL A 306 ? 0.0892 0.0966 0.0894 0.0037 0.0014 -0.0123 392 VAL A CG1 2458 C CG2 . VAL A 306 ? 0.1047 0.1006 0.0962 0.0083 -0.0046 -0.0143 392 VAL A CG2 2459 N N . ASP A 307 ? 0.0721 0.0759 0.0786 0.0017 -0.0064 -0.0075 393 ASP A N 2460 C CA . ASP A 307 ? 0.0770 0.0736 0.0949 0.0083 -0.0069 -0.0016 393 ASP A CA 2461 C C . ASP A 307 ? 0.0767 0.0783 0.0822 0.0034 -0.0128 -0.0041 393 ASP A C 2462 O O . ASP A 307 ? 0.0906 0.0952 0.1026 0.0049 -0.0068 0.0013 393 ASP A O 2463 C CB . ASP A 307 ? 0.0761 0.0833 0.0876 0.0028 -0.0029 -0.0051 393 ASP A CB 2464 C CG . ASP A 307 ? 0.0805 0.0865 0.0920 0.0007 -0.0075 -0.0145 393 ASP A CG 2465 O OD1 . ASP A 307 ? 0.0829 0.0964 0.0921 -0.0048 -0.0021 -0.0060 393 ASP A OD1 2466 O OD2 . ASP A 307 ? 0.0807 0.0944 0.0922 0.0017 -0.0072 -0.0070 393 ASP A OD2 2467 N N . ALA A 308 ? 0.0756 0.0786 0.0793 0.0047 -0.0001 -0.0031 394 ALA A N 2468 C CA . ALA A 308 ? 0.0781 0.0745 0.0794 0.0026 -0.0028 -0.0048 394 ALA A CA 2469 C C . ALA A 308 ? 0.0789 0.0802 0.0765 -0.0003 -0.0077 -0.0003 394 ALA A C 2470 O O . ALA A 308 ? 0.0864 0.0815 0.0760 0.0001 -0.0041 0.0038 394 ALA A O 2471 C CB . ALA A 308 ? 0.0932 0.0828 0.0941 0.0027 -0.0036 -0.0049 394 ALA A CB 2472 N N . PHE A 309 ? 0.0778 0.0720 0.0702 0.0019 -0.0062 -0.0003 395 PHE A N 2473 C CA . PHE A 309 ? 0.0791 0.0735 0.0708 0.0003 -0.0025 -0.0005 395 PHE A CA 2474 C C . PHE A 309 ? 0.0813 0.0793 0.0808 0.0085 -0.0019 -0.0011 395 PHE A C 2475 O O . PHE A 309 ? 0.0816 0.0801 0.0910 0.0040 -0.0097 0.0000 395 PHE A O 2476 C CB . PHE A 309 ? 0.0772 0.0790 0.0765 -0.0031 0.0006 -0.0039 395 PHE A CB 2477 C CG . PHE A 309 ? 0.0852 0.0916 0.0845 0.0026 -0.0100 -0.0074 395 PHE A CG 2478 C CD1 . PHE A 309 ? 0.1163 0.0881 0.0935 -0.0012 -0.0008 -0.0084 395 PHE A CD1 2479 C CD2 . PHE A 309 ? 0.1219 0.1071 0.1232 0.0125 -0.0237 -0.0205 395 PHE A CD2 2480 C CE1 . PHE A 309 ? 0.1447 0.1120 0.1221 -0.0012 -0.0032 -0.0098 395 PHE A CE1 2481 C CE2 . PHE A 309 ? 0.1395 0.1468 0.1321 -0.0067 -0.0213 -0.0387 395 PHE A CE2 2482 C CZ . PHE A 309 ? 0.1377 0.1230 0.1612 -0.0061 0.0050 -0.0351 395 PHE A CZ 2483 N N . VAL A 310 ? 0.0773 0.0690 0.0770 0.0046 -0.0046 -0.0024 396 VAL A N 2484 C CA . VAL A 310 ? 0.0760 0.0662 0.0754 0.0008 -0.0010 -0.0012 396 VAL A CA 2485 C C . VAL A 310 ? 0.0733 0.0726 0.0654 0.0074 0.0002 -0.0009 396 VAL A C 2486 O O . VAL A 310 ? 0.0753 0.0755 0.0798 0.0023 -0.0004 -0.0012 396 VAL A O 2487 C CB . VAL A 310 ? 0.0758 0.0730 0.0817 0.0070 0.0030 -0.0129 396 VAL A CB 2488 C CG1 . VAL A 310 ? 0.0951 0.0972 0.0936 0.0069 0.0051 -0.0089 396 VAL A CG1 2489 C CG2 . VAL A 310 ? 0.0793 0.0910 0.0856 0.0021 0.0001 -0.0014 396 VAL A CG2 2490 N N . TRP A 311 ? 0.0686 0.0689 0.0751 0.0084 0.0011 -0.0003 397 TRP A N 2491 C CA . TRP A 311 ? 0.0766 0.0768 0.0696 0.0047 -0.0018 0.0063 397 TRP A CA 2492 C C . TRP A 311 ? 0.0755 0.0680 0.0683 -0.0035 0.0039 -0.0024 397 TRP A C 2493 O O . TRP A 311 ? 0.0959 0.0784 0.0766 0.0069 -0.0039 -0.0016 397 TRP A O 2494 C CB . TRP A 311 ? 0.0804 0.0750 0.0754 0.0043 0.0027 -0.0042 397 TRP A CB 2495 C CG . TRP A 311 ? 0.0810 0.0818 0.0743 0.0071 -0.0100 0.0032 397 TRP A CG 2496 C CD1 . TRP A 311 ? 0.0797 0.0818 0.0745 0.0019 0.0013 0.0073 397 TRP A CD1 2497 C CD2 . TRP A 311 ? 0.0819 0.0817 0.0812 0.0143 -0.0050 0.0021 397 TRP A CD2 2498 N NE1 . TRP A 311 ? 0.0909 0.0882 0.0804 0.0125 -0.0050 -0.0046 397 TRP A NE1 2499 C CE2 . TRP A 311 ? 0.0860 0.0842 0.0744 0.0117 0.0049 0.0017 397 TRP A CE2 2500 C CE3 . TRP A 311 ? 0.0843 0.0898 0.0835 0.0083 0.0035 0.0041 397 TRP A CE3 2501 C CZ2 . TRP A 311 ? 0.0954 0.0951 0.0909 0.0171 0.0081 -0.0036 397 TRP A CZ2 2502 C CZ3 . TRP A 311 ? 0.0991 0.1041 0.1048 0.0035 0.0140 0.0041 397 TRP A CZ3 2503 C CH2 . TRP A 311 ? 0.0996 0.0975 0.0920 0.0141 0.0189 0.0157 397 TRP A CH2 2504 N N . VAL A 312 ? 0.0811 0.0690 0.0666 0.0028 -0.0050 -0.0054 398 VAL A N 2505 C CA . VAL A 312 ? 0.0841 0.0772 0.0693 0.0049 -0.0050 -0.0091 398 VAL A CA 2506 C C . VAL A 312 ? 0.0791 0.0735 0.0603 0.0038 0.0016 0.0041 398 VAL A C 2507 O O . VAL A 312 ? 0.0807 0.0777 0.0772 0.0000 -0.0022 -0.0011 398 VAL A O 2508 C CB . VAL A 312 ? 0.0820 0.0784 0.0716 0.0039 -0.0010 -0.0007 398 VAL A CB 2509 C CG1 . VAL A 312 ? 0.0781 0.0813 0.0813 0.0057 0.0011 0.0082 398 VAL A CG1 2510 C CG2 . VAL A 312 ? 0.0912 0.0815 0.0846 0.0030 0.0009 -0.0017 398 VAL A CG2 2511 N N . LYS A 313 ? 0.0807 0.0781 0.0837 0.0004 -0.0022 -0.0046 399 LYS A N 2512 C CA . LYS A 313 ? 0.0835 0.0809 0.0767 0.0031 0.0047 -0.0010 399 LYS A CA 2513 C C . LYS A 313 ? 0.0841 0.0860 0.0844 0.0011 -0.0001 -0.0096 399 LYS A C 2514 O O . LYS A 313 ? 0.1087 0.0961 0.0869 -0.0048 0.0005 -0.0016 399 LYS A O 2515 C CB . LYS A 313 ? 0.0923 0.0919 0.0974 -0.0021 0.0017 -0.0083 399 LYS A CB 2516 C CG . LYS A 313 ? 0.1116 0.1019 0.1367 0.0044 0.0006 0.0104 399 LYS A CG 2517 C CD . LYS A 313 ? 0.1292 0.1350 0.1410 0.0054 -0.0034 0.0000 399 LYS A CD 2518 C CE . LYS A 313 ? 0.1338 0.1596 0.1585 0.0067 0.0025 0.0057 399 LYS A CE 2519 N NZ . LYS A 313 ? 0.1503 0.1861 0.1986 -0.0005 -0.0073 -0.0054 399 LYS A NZ 2520 N N . PRO A 314 ? 0.0841 0.0817 0.0755 0.0023 0.0092 -0.0024 400 PRO A N 2521 C CA . PRO A 314 ? 0.0947 0.0906 0.0858 0.0051 0.0051 0.0053 400 PRO A CA 2522 C C . PRO A 314 ? 0.0817 0.0834 0.0830 -0.0006 -0.0014 -0.0008 400 PRO A C 2523 O O . PRO A 314 ? 0.1070 0.1195 0.0976 0.0032 0.0004 -0.0033 400 PRO A O 2524 C CB . PRO A 314 ? 0.1020 0.0945 0.1111 0.0050 0.0072 0.0071 400 PRO A CB 2525 C CG . PRO A 314 ? 0.1108 0.1148 0.1156 0.0019 -0.0012 -0.0057 400 PRO A CG 2526 C CD . PRO A 314 ? 0.1024 0.0896 0.0854 -0.0020 0.0102 -0.0084 400 PRO A CD 2527 N N . GLY A 315 ? 0.0884 0.1115 0.1010 0.0137 -0.0020 -0.0048 401 GLY A N 2528 C CA . GLY A 315 ? 0.1045 0.1095 0.0965 0.0142 0.0052 -0.0059 401 GLY A CA 2529 C C . GLY A 315 ? 0.1096 0.1029 0.0854 0.0143 0.0050 0.0059 401 GLY A C 2530 O O . GLY A 315 ? 0.1187 0.1114 0.1017 0.0165 0.0019 0.0073 401 GLY A O 2531 N N . GLY A 316 ? 0.0964 0.0973 0.1027 0.0021 0.0064 0.0035 402 GLY A N 2532 C CA . GLY A 316 ? 0.1123 0.1033 0.1087 0.0010 0.0053 0.0036 402 GLY A CA 2533 C C . GLY A 316 ? 0.1047 0.1018 0.1127 -0.0013 -0.0039 0.0050 402 GLY A C 2534 O O . GLY A 316 ? 0.1183 0.1170 0.1365 -0.0019 -0.0015 0.0049 402 GLY A O 2535 N N . GLU A 317 ? 0.1101 0.0994 0.0994 0.0016 -0.0019 -0.0026 403 GLU A N 2536 C CA . GLU A 317 ? 0.1180 0.1058 0.1069 0.0117 -0.0099 -0.0007 403 GLU A CA 2537 C C . GLU A 317 ? 0.1289 0.1138 0.1069 0.0011 0.0017 -0.0067 403 GLU A C 2538 O O . GLU A 317 ? 0.1473 0.1253 0.1578 -0.0004 0.0065 0.0074 403 GLU A O 2539 C CB . GLU A 317 ? 0.1263 0.1040 0.1013 0.0094 -0.0022 -0.0059 403 GLU A CB 2540 C CG . GLU A 317 ? 0.1210 0.1127 0.1129 0.0059 -0.0009 -0.0063 403 GLU A CG 2541 C CD . GLU A 317 ? 0.1292 0.1111 0.0980 0.0041 0.0098 0.0007 403 GLU A CD 2542 O OE1 . GLU A 317 ? 0.1524 0.1370 0.1548 0.0030 0.0075 0.0093 403 GLU A OE1 2543 O OE2 . GLU A 317 ? 0.1101 0.1052 0.1082 0.0017 -0.0011 -0.0042 403 GLU A OE2 2544 N N . CYS A 318 ? 0.1273 0.1059 0.1160 0.0164 -0.0061 0.0021 404 CYS A N 2545 C CA . CYS A 318 ? 0.1395 0.1039 0.1109 0.0253 -0.0055 -0.0076 404 CYS A CA 2546 C C . CYS A 318 ? 0.1468 0.1152 0.1108 0.0360 -0.0020 0.0047 404 CYS A C 2547 O O . CYS A 318 ? 0.2218 0.1302 0.1131 0.0494 0.0257 -0.0154 404 CYS A O 2548 C CB . CYS A 318 ? 0.1424 0.1048 0.0991 0.0210 0.0114 0.0007 404 CYS A CB 2549 S SG . CYS A 318 ? 0.1284 0.1114 0.1095 0.0143 -0.0034 -0.0007 404 CYS A SG 2550 N N . ASN A 319 ? 0.1075 0.1110 0.0974 0.0104 -0.0089 -0.0058 405 ASN A N 2551 C CA . ASN A 319 ? 0.1015 0.1068 0.0856 0.0048 -0.0103 -0.0032 405 ASN A CA 2552 C C . ASN A 319 ? 0.0962 0.1074 0.0916 0.0022 -0.0135 -0.0065 405 ASN A C 2553 O O . ASN A 319 ? 0.1088 0.1193 0.0995 -0.0013 -0.0090 0.0048 405 ASN A O 2554 C CB . ASN A 319 ? 0.1063 0.1030 0.0943 0.0076 -0.0217 0.0000 405 ASN A CB 2555 C CG . ASN A 319 ? 0.0985 0.1347 0.1101 0.0214 -0.0085 -0.0239 405 ASN A CG 2556 O OD1 . ASN A 319 ? 0.0927 0.1048 0.0985 0.0035 -0.0163 -0.0057 405 ASN A OD1 2557 N ND2 . ASN A 319 ? 0.1540 0.1791 0.1508 0.0435 -0.0036 -0.0265 405 ASN A ND2 2558 N N . GLY A 320 ? 0.1049 0.1024 0.0908 0.0073 -0.0084 -0.0012 406 GLY A N 2559 C CA . GLY A 320 ? 0.1010 0.1038 0.0914 -0.0003 -0.0107 -0.0121 406 GLY A CA 2560 C C . GLY A 320 ? 0.1010 0.0964 0.0904 -0.0015 -0.0092 0.0018 406 GLY A C 2561 O O . GLY A 320 ? 0.1032 0.1109 0.0988 0.0041 -0.0058 -0.0004 406 GLY A O 2562 N N . THR A 321 ? 0.1107 0.1118 0.0969 -0.0030 -0.0092 -0.0002 407 THR A N 2563 C CA . THR A 321 ? 0.1112 0.1147 0.1111 -0.0065 -0.0181 0.0046 407 THR A CA 2564 C C . THR A 321 ? 0.0975 0.1150 0.1077 -0.0112 -0.0181 0.0035 407 THR A C 2565 O O . THR A 321 ? 0.1086 0.1110 0.1120 -0.0019 -0.0028 -0.0008 407 THR A O 2566 C CB . THR A 321 ? 0.1211 0.1229 0.1219 -0.0056 -0.0167 -0.0106 407 THR A CB 2567 O OG1 . THR A 321 ? 0.1350 0.1412 0.1748 -0.0171 -0.0148 -0.0205 407 THR A OG1 2568 C CG2 . THR A 321 ? 0.1440 0.1369 0.1332 0.0006 -0.0268 -0.0174 407 THR A CG2 2569 N N . SER A 322 ? 0.1145 0.1132 0.1213 -0.0023 -0.0081 0.0085 408 SER A N 2570 C CA . SER A 322 ? 0.1183 0.1183 0.1151 -0.0070 -0.0027 -0.0001 408 SER A CA 2571 C C . SER A 322 ? 0.1197 0.1316 0.1267 -0.0057 0.0000 0.0073 408 SER A C 2572 O O . SER A 322 ? 0.1377 0.1646 0.1470 0.0054 0.0004 -0.0107 408 SER A O 2573 C CB . SER A 322 ? 0.1317 0.1417 0.1349 -0.0041 -0.0042 0.0094 408 SER A CB 2574 O OG . SER A 322 ? 0.1458 0.1502 0.1399 -0.0079 0.0023 0.0150 408 SER A OG 2575 N N . ASP A 323 ? 0.1105 0.1417 0.1304 -0.0094 -0.0146 -0.0008 409 ASP A N 2576 C CA . ASP A 323 ? 0.1124 0.1692 0.1500 -0.0078 -0.0133 0.0023 409 ASP A CA 2577 C C . ASP A 323 ? 0.1206 0.1533 0.1433 -0.0071 -0.0109 -0.0051 409 ASP A C 2578 O O . ASP A 323 ? 0.1141 0.1526 0.1294 -0.0019 -0.0164 0.0058 409 ASP A O 2579 C CB . ASP A 323 ? 0.1178 0.1640 0.1508 -0.0116 -0.0275 0.0063 409 ASP A CB 2580 C CG . ASP A 323 ? 0.1508 0.1631 0.1990 -0.0086 -0.0109 0.0026 409 ASP A CG 2581 O OD1 . ASP A 323 ? 0.1365 0.1820 0.1922 -0.0314 -0.0181 0.0018 409 ASP A OD1 2582 O OD2 . ASP A 323 ? 0.1779 0.2137 0.2543 -0.0263 -0.0510 -0.0212 409 ASP A OD2 2583 N N . THR A 324 ? 0.1170 0.1643 0.1556 -0.0028 -0.0035 0.0066 410 THR A N 2584 C CA . THR A 324 ? 0.1247 0.1788 0.1744 0.0057 0.0003 0.0079 410 THR A CA 2585 C C . THR A 324 ? 0.1537 0.2001 0.1851 0.0143 -0.0040 0.0192 410 THR A C 2586 O O . THR A 324 ? 0.1700 0.2342 0.1910 0.0019 -0.0138 0.0304 410 THR A O 2587 C CB . THR A 324 ? 0.1291 0.1935 0.1980 0.0142 0.0102 0.0228 410 THR A CB 2588 O OG1 . THR A 324 ? 0.1236 0.2562 0.2586 0.0226 -0.0070 0.0072 410 THR A OG1 2589 C CG2 . THR A 324 ? 0.1294 0.1997 0.2201 0.0135 0.0033 0.0092 410 THR A CG2 2590 N N . THR A 325 ? 0.1353 0.2029 0.1662 0.0045 -0.0219 0.0074 411 THR A N 2591 C CA . THR A 325 ? 0.1575 0.2301 0.1842 -0.0112 -0.0253 -0.0028 411 THR A CA 2592 C C . THR A 325 ? 0.1569 0.2111 0.1710 -0.0151 -0.0235 -0.0084 411 THR A C 2593 O O . THR A 325 ? 0.1764 0.2484 0.1934 -0.0126 -0.0386 -0.0126 411 THR A O 2594 C CB . THR A 325 ? 0.1725 0.2299 0.2044 -0.0233 -0.0273 -0.0182 411 THR A CB 2595 O OG1 . THR A 325 ? 0.1598 0.2683 0.2494 -0.0491 -0.0281 -0.0031 411 THR A OG1 2596 C CG2 . THR A 325 ? 0.1922 0.2684 0.2352 -0.0115 -0.0126 0.0097 411 THR A CG2 2597 N N . ALA A 326 ? 0.1358 0.1874 0.1747 -0.0218 -0.0307 -0.0031 412 ALA A N 2598 C CA . ALA A 326 ? 0.1636 0.1806 0.1565 -0.0201 -0.0320 -0.0117 412 ALA A CA 2599 C C . ALA A 326 ? 0.1355 0.1742 0.1561 0.0028 -0.0139 -0.0034 412 ALA A C 2600 O O . ALA A 326 ? 0.1516 0.1762 0.1623 -0.0086 -0.0163 -0.0192 412 ALA A O 2601 C CB . ALA A 326 ? 0.1745 0.1796 0.1592 0.0103 -0.0267 -0.0088 412 ALA A CB 2602 N N . ALA A 327 ? 0.1797 0.1956 0.1766 -0.0282 -0.0177 -0.0329 413 ALA A N 2603 C CA . ALA A 327 ? 0.1795 0.1918 0.1914 -0.0132 -0.0100 -0.0230 413 ALA A CA 2604 C C . ALA A 327 ? 0.2138 0.1915 0.2008 -0.0086 -0.0057 -0.0126 413 ALA A C 2605 O O . ALA A 327 ? 0.2426 0.2141 0.2311 -0.0071 -0.0008 -0.0025 413 ALA A O 2606 C CB . ALA A 327 ? 0.2151 0.2150 0.2106 -0.0032 -0.0080 -0.0277 413 ALA A CB 2607 N N . ARG A 328 ? 0.1642 0.1833 0.1825 0.0202 -0.0112 -0.0433 414 ARG A N 2608 C CA . ARG A 328 ? 0.1616 0.1889 0.1853 -0.0003 -0.0005 -0.0364 414 ARG A CA 2609 C C . ARG A 328 ? 0.1212 0.1387 0.1422 0.0035 -0.0068 -0.0170 414 ARG A C 2610 O O . ARG A 328 ? 0.1159 0.1303 0.1383 -0.0084 -0.0116 -0.0153 414 ARG A O 2611 C CB . ARG A 328 ? 0.1904 0.1763 0.2150 0.0130 -0.0056 -0.0376 414 ARG A CB 2612 C CG . ARG A 328 ? 0.2434 0.2254 0.2441 0.0090 0.0082 -0.0444 414 ARG A CG 2613 C CD . ARG A 328 ? 0.2283 0.2897 0.2840 0.0016 0.0168 -0.0136 414 ARG A CD 2614 N NE . ARG A 328 ? 0.3343 0.3435 0.3669 0.0067 -0.0005 0.0054 414 ARG A NE 2615 C CZ . ARG A 328 ? 0.4022 0.3809 0.3928 -0.0057 -0.0082 -0.0044 414 ARG A CZ 2616 N NH1 . ARG A 328 ? 0.3586 0.3497 0.3603 0.0127 -0.0068 -0.0143 414 ARG A NH1 2617 N NH2 . ARG A 328 ? 0.4362 0.4116 0.4175 -0.0038 -0.0013 0.0122 414 ARG A NH2 2618 N N . TYR A 329 ? 0.1169 0.1372 0.1407 0.0001 -0.0117 -0.0255 415 TYR A N 2619 C CA . TYR A 329 ? 0.1143 0.1226 0.1173 0.0051 -0.0116 -0.0016 415 TYR A CA 2620 C C . TYR A 329 ? 0.0998 0.1120 0.1032 -0.0024 -0.0068 0.0003 415 TYR A C 2621 O O . TYR A 329 ? 0.1121 0.1351 0.1079 -0.0025 -0.0173 -0.0020 415 TYR A O 2622 C CB . TYR A 329 ? 0.1075 0.1257 0.1333 -0.0124 -0.0080 -0.0030 415 TYR A CB 2623 C CG . TYR A 329 ? 0.0924 0.1269 0.1260 -0.0098 -0.0048 -0.0028 415 TYR A CG 2624 C CD1 . TYR A 329 ? 0.1027 0.1374 0.1453 -0.0024 -0.0093 0.0030 415 TYR A CD1 2625 C CD2 . TYR A 329 ? 0.1129 0.1255 0.1188 -0.0026 -0.0071 -0.0058 415 TYR A CD2 2626 C CE1 . TYR A 329 ? 0.1115 0.1365 0.1187 -0.0061 -0.0064 0.0019 415 TYR A CE1 2627 C CE2 . TYR A 329 ? 0.1059 0.1184 0.1154 0.0017 -0.0095 -0.0051 415 TYR A CE2 2628 C CZ . TYR A 329 ? 0.1031 0.1346 0.1234 0.0012 0.0011 -0.0141 415 TYR A CZ 2629 O OH . TYR A 329 ? 0.1292 0.1728 0.1335 0.0073 -0.0027 -0.0230 415 TYR A OH 2630 N N . ASP A 330 ? 0.0965 0.0992 0.0934 0.0009 -0.0070 -0.0032 416 ASP A N 2631 C CA . ASP A 330 ? 0.0858 0.0954 0.0976 0.0035 -0.0086 -0.0052 416 ASP A CA 2632 C C . ASP A 330 ? 0.0876 0.0977 0.0960 0.0004 -0.0055 -0.0042 416 ASP A C 2633 O O . ASP A 330 ? 0.0939 0.0996 0.0947 0.0012 -0.0023 -0.0007 416 ASP A O 2634 C CB . ASP A 330 ? 0.0879 0.0994 0.0892 0.0050 -0.0004 -0.0109 416 ASP A CB 2635 C CG . ASP A 330 ? 0.0865 0.1048 0.0795 0.0079 0.0055 -0.0032 416 ASP A CG 2636 O OD1 . ASP A 330 ? 0.0933 0.0972 0.1005 0.0037 -0.0024 -0.0006 416 ASP A OD1 2637 O OD2 . ASP A 330 ? 0.1051 0.1179 0.1051 -0.0047 0.0052 -0.0071 416 ASP A OD2 2638 N N . TYR A 331 ? 0.0942 0.1043 0.0933 0.0122 -0.0049 -0.0029 417 TYR A N 2639 C CA . TYR A 331 ? 0.0856 0.1142 0.1001 0.0112 -0.0038 -0.0026 417 TYR A CA 2640 C C . TYR A 331 ? 0.0820 0.0894 0.0885 0.0036 -0.0029 0.0063 417 TYR A C 2641 O O . TYR A 331 ? 0.0888 0.0977 0.0949 0.0091 -0.0004 0.0008 417 TYR A O 2642 C CB . TYR A 331 ? 0.1038 0.1227 0.1067 0.0259 -0.0098 0.0073 417 TYR A CB 2643 C CG . TYR A 331 ? 0.0992 0.1058 0.1010 0.0295 -0.0011 0.0107 417 TYR A CG 2644 C CD1 . TYR A 331 ? 0.1090 0.1047 0.1174 0.0275 0.0046 0.0169 417 TYR A CD1 2645 C CD2 . TYR A 331 ? 0.1422 0.1258 0.1219 0.0344 0.0007 0.0040 417 TYR A CD2 2646 C CE1 . TYR A 331 ? 0.1269 0.1255 0.1234 0.0149 0.0088 0.0185 417 TYR A CE1 2647 C CE2 . TYR A 331 ? 0.1256 0.1487 0.1389 0.0298 0.0131 0.0289 417 TYR A CE2 2648 C CZ . TYR A 331 ? 0.1285 0.1304 0.1537 0.0237 0.0121 0.0218 417 TYR A CZ 2649 O OH . TYR A 331 ? 0.1431 0.1474 0.1785 0.0190 0.0238 0.0251 417 TYR A OH 2650 N N . HIS A 332 ? 0.0812 0.0949 0.0872 0.0033 -0.0060 -0.0011 418 HIS A N 2651 C CA . HIS A 332 ? 0.0846 0.0886 0.0852 0.0025 -0.0112 -0.0035 418 HIS A CA 2652 C C . HIS A 332 ? 0.0682 0.0932 0.0909 0.0053 -0.0005 0.0037 418 HIS A C 2653 O O . HIS A 332 ? 0.0909 0.0927 0.0864 0.0033 -0.0040 0.0010 418 HIS A O 2654 C CB . HIS A 332 ? 0.0838 0.0956 0.0889 0.0058 -0.0105 0.0062 418 HIS A CB 2655 C CG . HIS A 332 ? 0.0914 0.0979 0.1044 -0.0023 0.0043 -0.0039 418 HIS A CG 2656 N ND1 . HIS A 332 ? 0.0975 0.0998 0.1012 0.0087 0.0060 0.0138 418 HIS A ND1 2657 C CD2 . HIS A 332 ? 0.1309 0.1222 0.1072 -0.0018 0.0115 0.0028 418 HIS A CD2 2658 C CE1 . HIS A 332 ? 0.1084 0.1229 0.1173 0.0006 0.0094 0.0197 418 HIS A CE1 2659 N NE2 . HIS A 332 ? 0.1212 0.1232 0.1433 -0.0106 0.0146 -0.0098 418 HIS A NE2 2660 N N . CYS A 333 ? 0.0780 0.0920 0.0858 0.0021 0.0003 0.0017 419 CYS A N 2661 C CA . CYS A 333 ? 0.0826 0.0860 0.0906 0.0098 -0.0015 0.0020 419 CYS A CA 2662 C C . CYS A 333 ? 0.0870 0.0937 0.0860 -0.0005 -0.0093 0.0018 419 CYS A C 2663 O O . CYS A 333 ? 0.0954 0.1087 0.1084 0.0051 0.0018 0.0053 419 CYS A O 2664 C CB . CYS A 333 ? 0.0963 0.0920 0.0946 0.0027 -0.0077 0.0033 419 CYS A CB 2665 S SG . CYS A 333 ? 0.0971 0.0985 0.0990 0.0030 -0.0008 -0.0030 419 CYS A SG 2666 N N . GLY A 334 ? 0.0822 0.1019 0.1049 0.0031 0.0031 -0.0024 420 GLY A N 2667 C CA . GLY A 334 ? 0.0977 0.1078 0.1061 0.0091 -0.0073 0.0015 420 GLY A CA 2668 C C . GLY A 334 ? 0.0815 0.1088 0.1100 0.0077 0.0055 -0.0020 420 GLY A C 2669 O O . GLY A 334 ? 0.1069 0.1353 0.1384 0.0124 0.0105 -0.0136 420 GLY A O 2670 N N . LEU A 335 ? 0.0872 0.0995 0.0986 -0.0010 -0.0016 -0.0009 421 LEU A N 2671 C CA . LEU A 335 ? 0.0940 0.0963 0.1044 0.0160 -0.0071 0.0018 421 LEU A CA 2672 C C . LEU A 335 ? 0.0865 0.1046 0.1130 0.0122 -0.0052 -0.0058 421 LEU A C 2673 O O . LEU A 335 ? 0.0987 0.1129 0.1161 0.0064 -0.0014 0.0022 421 LEU A O 2674 C CB . LEU A 335 ? 0.1020 0.1060 0.1029 0.0105 -0.0070 0.0017 421 LEU A CB 2675 C CG . LEU A 335 ? 0.0989 0.0962 0.1061 0.0051 -0.0091 -0.0076 421 LEU A CG 2676 C CD1 . LEU A 335 ? 0.1218 0.1258 0.1160 -0.0028 -0.0057 -0.0042 421 LEU A CD1 2677 C CD2 . LEU A 335 ? 0.1362 0.1341 0.1311 0.0281 -0.0083 0.0086 421 LEU A CD2 2678 N N . GLU A 336 ? 0.1130 0.1132 0.1052 0.0039 0.0072 0.0020 422 GLU A N 2679 C CA . GLU A 336 ? 0.1082 0.1329 0.1228 0.0139 0.0059 -0.0010 422 GLU A CA 2680 C C . GLU A 336 ? 0.1118 0.1259 0.0939 0.0047 0.0091 0.0067 422 GLU A C 2681 O O . GLU A 336 ? 0.1242 0.1633 0.1389 0.0201 0.0216 0.0219 422 GLU A O 2682 C CB . GLU A 336 ? 0.1380 0.1710 0.1428 0.0455 0.0134 -0.0025 422 GLU A CB 2683 C CG . GLU A 336 ? 0.2075 0.1830 0.1893 0.0345 -0.0011 -0.0155 422 GLU A CG 2684 C CD . GLU A 336 ? 0.2685 0.2284 0.2751 0.0133 0.0148 -0.0115 422 GLU A CD 2685 O OE1 . GLU A 336 ? 0.2998 0.2851 0.3032 0.0352 0.0157 -0.0288 422 GLU A OE1 2686 O OE2 . GLU A 336 ? 0.2777 0.2662 0.2510 0.0218 0.0134 -0.0019 422 GLU A OE2 2687 N N . ASP A 337 ? 0.0982 0.1020 0.1044 0.0059 0.0019 0.0050 423 ASP A N 2688 C CA . ASP A 337 ? 0.0846 0.1062 0.0898 0.0114 0.0014 0.0042 423 ASP A CA 2689 C C . ASP A 337 ? 0.0940 0.0954 0.0874 0.0067 0.0013 0.0073 423 ASP A C 2690 O O . ASP A 337 ? 0.1007 0.1039 0.1029 0.0107 -0.0041 0.0027 423 ASP A O 2691 C CB . ASP A 337 ? 0.1025 0.0971 0.0955 0.0173 0.0010 -0.0025 423 ASP A CB 2692 C CG . ASP A 337 ? 0.0974 0.0974 0.0882 0.0026 -0.0047 -0.0026 423 ASP A CG 2693 O OD1 . ASP A 337 ? 0.1084 0.1071 0.0992 0.0012 -0.0007 -0.0026 423 ASP A OD1 2694 O OD2 . ASP A 337 ? 0.1022 0.1048 0.0983 0.0018 0.0000 0.0024 423 ASP A OD2 2695 N N . ALA A 338 ? 0.0834 0.0901 0.0967 0.0098 -0.0006 0.0035 424 ALA A N 2696 C CA . ALA A 338 ? 0.0796 0.0865 0.0967 0.0082 -0.0005 0.0039 424 ALA A CA 2697 C C . ALA A 338 ? 0.0711 0.0999 0.1040 -0.0026 -0.0001 -0.0028 424 ALA A C 2698 O O . ALA A 338 ? 0.0954 0.1167 0.1349 0.0055 0.0048 0.0146 424 ALA A O 2699 C CB . ALA A 338 ? 0.0856 0.0956 0.0986 -0.0011 0.0025 -0.0014 424 ALA A CB 2700 N N . LEU A 339 ? 0.0892 0.0878 0.0981 -0.0034 0.0048 0.0014 425 LEU A N 2701 C CA . LEU A 339 ? 0.0886 0.0993 0.0941 -0.0046 0.0031 0.0053 425 LEU A CA 2702 C C . LEU A 339 ? 0.0853 0.0953 0.0982 -0.0053 0.0085 0.0053 425 LEU A C 2703 O O . LEU A 339 ? 0.0972 0.1058 0.1054 -0.0086 0.0035 0.0020 425 LEU A O 2704 C CB . LEU A 339 ? 0.0878 0.0991 0.0961 -0.0010 -0.0023 0.0020 425 LEU A CB 2705 C CG . LEU A 339 ? 0.0933 0.1138 0.1047 -0.0086 0.0043 0.0038 425 LEU A CG 2706 C CD1 . LEU A 339 ? 0.1340 0.1343 0.1333 0.0061 0.0138 0.0116 425 LEU A CD1 2707 C CD2 . LEU A 339 ? 0.1126 0.1253 0.1148 -0.0032 -0.0042 0.0060 425 LEU A CD2 2708 N N . LYS A 340 ? 0.0984 0.1236 0.1040 -0.0139 -0.0049 -0.0009 426 LYS A N 2709 C CA . LYS A 340 ? 0.1096 0.1395 0.1216 -0.0164 0.0044 -0.0004 426 LYS A CA 2710 C C . LYS A 340 ? 0.1342 0.1646 0.1497 -0.0267 0.0088 -0.0042 426 LYS A C 2711 O O . LYS A 340 ? 0.1380 0.1785 0.1574 -0.0346 0.0156 0.0010 426 LYS A O 2712 C CB . LYS A 340 ? 0.1346 0.1635 0.1601 -0.0085 -0.0024 0.0034 426 LYS A CB 2713 C CG . LYS A 340 ? 0.1450 0.1535 0.1523 0.0147 -0.0235 0.0098 426 LYS A CG 2714 C CD . LYS A 340 ? 0.1671 0.1851 0.1976 0.0064 -0.0281 0.0121 426 LYS A CD 2715 C CE . LYS A 340 ? 0.1593 0.1876 0.1850 0.0001 -0.0153 0.0125 426 LYS A CE 2716 N NZ . LYS A 340 ? 0.1795 0.2013 0.2452 0.0015 -0.0183 -0.0057 426 LYS A NZ 2717 N N . PRO A 341 ? 0.1403 0.1646 0.1527 -0.0386 0.0169 0.0087 427 PRO A N 2718 C CA . PRO A 341 ? 0.1246 0.1462 0.1459 -0.0274 -0.0018 0.0020 427 PRO A CA 2719 C C . PRO A 341 ? 0.1254 0.1519 0.1429 -0.0244 -0.0046 0.0127 427 PRO A C 2720 O O . PRO A 341 ? 0.1416 0.1714 0.1569 -0.0216 0.0087 0.0311 427 PRO A O 2721 C CB . PRO A 341 ? 0.1292 0.1598 0.1550 -0.0263 -0.0038 -0.0095 427 PRO A CB 2722 C CG . PRO A 341 ? 0.1376 0.1733 0.1955 -0.0374 0.0009 0.0070 427 PRO A CG 2723 C CD . PRO A 341 ? 0.1545 0.1845 0.1781 -0.0367 0.0138 0.0193 427 PRO A CD 2724 N N . ALA A 342 ? 0.1312 0.1265 0.1173 -0.0130 -0.0088 0.0063 428 ALA A N 2725 C CA . ALA A 342 ? 0.1272 0.1206 0.1176 -0.0083 -0.0084 -0.0005 428 ALA A CA 2726 C C . ALA A 342 ? 0.1267 0.1196 0.1147 -0.0100 -0.0126 0.0095 428 ALA A C 2727 O O . ALA A 342 ? 0.1378 0.1267 0.1285 -0.0098 -0.0196 0.0004 428 ALA A O 2728 C CB . ALA A 342 ? 0.1193 0.1093 0.1130 -0.0041 -0.0062 0.0022 428 ALA A CB 2729 N N . PRO A 343 ? 0.1381 0.1246 0.1122 -0.0077 -0.0211 -0.0080 429 PRO A N 2730 C CA . PRO A 343 ? 0.1468 0.1238 0.1373 -0.0011 -0.0241 -0.0098 429 PRO A CA 2731 C C . PRO A 343 ? 0.1533 0.1344 0.1273 0.0027 -0.0268 -0.0180 429 PRO A C 2732 O O . PRO A 343 ? 0.1537 0.1270 0.1229 0.0064 -0.0167 -0.0020 429 PRO A O 2733 C CB . PRO A 343 ? 0.1791 0.1357 0.1505 -0.0095 -0.0263 -0.0081 429 PRO A CB 2734 C CG . PRO A 343 ? 0.1668 0.1405 0.1280 0.0032 -0.0188 0.0033 429 PRO A CG 2735 C CD . PRO A 343 ? 0.1413 0.1227 0.1251 -0.0017 -0.0231 0.0078 429 PRO A CD 2736 N N . GLU A 344 ? 0.1985 0.1420 0.1459 0.0023 -0.0177 -0.0184 430 GLU A N 2737 C CA . GLU A 344 ? 0.1966 0.1529 0.1523 0.0153 -0.0095 -0.0203 430 GLU A CA 2738 C C . GLU A 344 ? 0.1840 0.1454 0.1362 0.0267 -0.0069 -0.0178 430 GLU A C 2739 O O . GLU A 344 ? 0.1926 0.1337 0.1322 0.0258 -0.0064 -0.0019 430 GLU A O 2740 C CB . GLU A 344 ? 0.2381 0.1848 0.1677 0.0098 -0.0080 -0.0252 430 GLU A CB 2741 C CG . GLU A 344 ? 0.2752 0.2536 0.2474 -0.0066 -0.0114 -0.0019 430 GLU A CG 2742 C CD . GLU A 344 ? 0.3322 0.2943 0.2688 0.0009 -0.0091 -0.0083 430 GLU A CD 2743 O OE1 . GLU A 344 ? 0.3426 0.3276 0.2916 -0.0357 -0.0043 -0.0621 430 GLU A OE1 2744 O OE2 . GLU A 344 ? 0.3397 0.3731 0.3562 0.0189 -0.0185 -0.0125 430 GLU A OE2 2745 N N . ALA A 345 ? 0.1998 0.1542 0.1265 0.0241 -0.0018 -0.0012 431 ALA A N 2746 C CA . ALA A 345 ? 0.2014 0.1612 0.1318 0.0283 0.0205 0.0000 431 ALA A CA 2747 C C . ALA A 345 ? 0.2075 0.1676 0.1378 0.0330 0.0059 -0.0126 431 ALA A C 2748 O O . ALA A 345 ? 0.2438 0.1839 0.1584 0.0420 0.0059 -0.0309 431 ALA A O 2749 C CB . ALA A 345 ? 0.2043 0.1798 0.1571 0.0316 0.0221 0.0108 431 ALA A CB 2750 N N . GLY A 346 ? 0.1839 0.1481 0.1389 0.0402 0.0066 -0.0171 432 GLY A N 2751 C CA . GLY A 346 ? 0.1887 0.1613 0.1532 0.0404 -0.0008 -0.0079 432 GLY A CA 2752 C C . GLY A 346 ? 0.2103 0.1649 0.1565 0.0333 -0.0121 -0.0031 432 GLY A C 2753 O O . GLY A 346 ? 0.2383 0.1941 0.2358 0.0731 -0.0081 0.0199 432 GLY A O 2754 N N . GLN A 347 ? 0.1982 0.1608 0.1458 0.0293 -0.0119 -0.0075 433 GLN A N 2755 C CA . GLN A 347 ? 0.1996 0.1498 0.1397 0.0186 -0.0077 -0.0232 433 GLN A CA 2756 C C . GLN A 347 ? 0.1689 0.1267 0.1075 0.0019 -0.0175 -0.0095 433 GLN A C 2757 O O . GLN A 347 ? 0.1773 0.1185 0.1228 0.0070 -0.0147 -0.0104 433 GLN A O 2758 C CB . GLN A 347 ? 0.2164 0.1435 0.1366 0.0147 -0.0206 -0.0115 433 GLN A CB 2759 C CG . GLN A 347 ? 0.2532 0.1722 0.1781 0.0207 -0.0258 -0.0251 433 GLN A CG 2760 C CD . GLN A 347 ? 0.2631 0.1747 0.2310 0.0033 -0.0289 -0.0140 433 GLN A CD 2761 O OE1 . GLN A 347 ? 0.2699 0.2161 0.2608 0.0229 -0.0169 -0.0523 433 GLN A OE1 2762 N NE2 . GLN A 347 ? 0.3123 0.2229 0.2457 0.0126 -0.0483 0.0093 433 GLN A NE2 2763 N N . TRP A 348 ? 0.1610 0.1165 0.1131 0.0045 -0.0173 -0.0119 434 TRP A N 2764 C CA . TRP A 348 ? 0.1367 0.1136 0.1000 0.0000 -0.0228 -0.0130 434 TRP A CA 2765 C C . TRP A 348 ? 0.1255 0.1024 0.1207 -0.0042 -0.0173 -0.0049 434 TRP A C 2766 O O . TRP A 348 ? 0.1489 0.1273 0.1571 -0.0010 -0.0237 -0.0266 434 TRP A O 2767 C CB . TRP A 348 ? 0.1378 0.1169 0.1271 0.0019 -0.0182 -0.0050 434 TRP A CB 2768 C CG . TRP A 348 ? 0.1214 0.1022 0.1134 0.0042 -0.0164 0.0056 434 TRP A CG 2769 C CD1 . TRP A 348 ? 0.1233 0.1143 0.1318 -0.0123 -0.0134 0.0000 434 TRP A CD1 2770 C CD2 . TRP A 348 ? 0.1240 0.1036 0.1111 0.0042 -0.0050 -0.0107 434 TRP A CD2 2771 N NE1 . TRP A 348 ? 0.1226 0.1101 0.1078 -0.0047 -0.0082 0.0102 434 TRP A NE1 2772 C CE2 . TRP A 348 ? 0.1148 0.1031 0.1022 -0.0096 0.0029 0.0024 434 TRP A CE2 2773 C CE3 . TRP A 348 ? 0.1353 0.1076 0.1095 0.0085 -0.0003 -0.0004 434 TRP A CE3 2774 C CZ2 . TRP A 348 ? 0.1187 0.0961 0.0986 -0.0061 -0.0040 0.0006 434 TRP A CZ2 2775 C CZ3 . TRP A 348 ? 0.1087 0.1048 0.1092 -0.0012 -0.0016 0.0063 434 TRP A CZ3 2776 C CH2 . TRP A 348 ? 0.1122 0.0970 0.1015 -0.0029 -0.0023 0.0014 434 TRP A CH2 2777 N N . PHE A 349 ? 0.1209 0.0992 0.1072 -0.0068 -0.0105 -0.0143 435 PHE A N 2778 C CA . PHE A 349 ? 0.0968 0.1030 0.1085 -0.0108 -0.0057 -0.0037 435 PHE A CA 2779 C C . PHE A 349 ? 0.0990 0.0975 0.1035 -0.0089 0.0034 -0.0071 435 PHE A C 2780 O O . PHE A 349 ? 0.1003 0.0936 0.1048 -0.0090 -0.0080 -0.0001 435 PHE A O 2781 C CB . PHE A 349 ? 0.1134 0.1070 0.1015 -0.0085 -0.0084 -0.0057 435 PHE A CB 2782 C CG . PHE A 349 ? 0.1084 0.1049 0.1056 -0.0049 -0.0059 -0.0021 435 PHE A CG 2783 C CD1 . PHE A 349 ? 0.1215 0.1040 0.1140 -0.0015 -0.0103 0.0039 435 PHE A CD1 2784 C CD2 . PHE A 349 ? 0.1090 0.0959 0.0921 -0.0112 -0.0105 -0.0065 435 PHE A CD2 2785 C CE1 . PHE A 349 ? 0.1198 0.1266 0.1209 0.0005 0.0112 0.0061 435 PHE A CE1 2786 C CE2 . PHE A 349 ? 0.1234 0.1132 0.1048 -0.0062 -0.0185 -0.0035 435 PHE A CE2 2787 C CZ . PHE A 349 ? 0.1293 0.1178 0.1166 0.0025 -0.0259 0.0025 435 PHE A CZ 2788 N N . ASN A 350 ? 0.1114 0.1065 0.1126 -0.0167 -0.0028 -0.0033 436 ASN A N 2789 C CA . ASN A 350 ? 0.1084 0.0994 0.1177 -0.0049 -0.0029 -0.0031 436 ASN A CA 2790 C C . ASN A 350 ? 0.1064 0.0968 0.1084 -0.0132 0.0002 0.0030 436 ASN A C 2791 O O . ASN A 350 ? 0.1155 0.1119 0.1153 -0.0138 -0.0026 0.0097 436 ASN A O 2792 C CB . ASN A 350 ? 0.1361 0.1115 0.1411 -0.0143 0.0083 0.0041 436 ASN A CB 2793 C CG . ASN A 350 ? 0.1396 0.1151 0.1480 -0.0212 0.0140 0.0122 436 ASN A CG 2794 O OD1 . ASN A 350 ? 0.1532 0.1354 0.1414 0.0031 0.0104 0.0234 436 ASN A OD1 2795 N ND2 . ASN A 350 ? 0.1776 0.1567 0.1608 -0.0119 0.0136 0.0252 436 ASN A ND2 2796 N N . GLU A 351 ? 0.1047 0.1050 0.1088 -0.0116 0.0035 0.0084 437 GLU A N 2797 C CA . GLU A 351 ? 0.0960 0.1144 0.1080 -0.0072 0.0061 0.0055 437 GLU A CA 2798 C C . GLU A 351 ? 0.0834 0.0898 0.0922 0.0005 0.0027 0.0042 437 GLU A C 2799 O O . GLU A 351 ? 0.1027 0.1115 0.1034 -0.0035 0.0059 -0.0024 437 GLU A O 2800 C CB . GLU A 351 ? 0.0986 0.1205 0.1230 -0.0134 0.0160 0.0009 437 GLU A CB 2801 C CG . GLU A 351 ? 0.1375 0.1675 0.1793 -0.0161 0.0072 0.0123 437 GLU A CG 2802 C CD . GLU A 351 ? 0.2144 0.2014 0.2155 -0.0262 0.0268 0.0228 437 GLU A CD 2803 O OE1 . GLU A 351 ? 0.2578 0.2852 0.2073 0.0131 0.0409 0.0111 437 GLU A OE1 2804 O OE2 . GLU A 351 ? 0.2981 0.2762 0.2737 0.0088 0.0181 0.0321 437 GLU A OE2 2805 N N . TYR A 352 ? 0.0939 0.0914 0.0933 -0.0070 -0.0038 0.0002 438 TYR A N 2806 C CA . TYR A 352 ? 0.0922 0.0865 0.0920 -0.0049 -0.0009 -0.0003 438 TYR A CA 2807 C C . TYR A 352 ? 0.0926 0.0849 0.0877 -0.0042 0.0056 0.0033 438 TYR A C 2808 O O . TYR A 352 ? 0.0862 0.0862 0.0853 -0.0067 0.0012 0.0020 438 TYR A O 2809 C CB . TYR A 352 ? 0.0869 0.0924 0.0902 -0.0044 -0.0093 0.0043 438 TYR A CB 2810 C CG . TYR A 352 ? 0.0923 0.0980 0.0894 -0.0033 0.0034 0.0012 438 TYR A CG 2811 C CD1 . TYR A 352 ? 0.0879 0.0852 0.0868 0.0000 -0.0002 0.0028 438 TYR A CD1 2812 C CD2 . TYR A 352 ? 0.0790 0.0894 0.0892 0.0019 0.0002 0.0077 438 TYR A CD2 2813 C CE1 . TYR A 352 ? 0.0810 0.0959 0.0883 -0.0020 0.0090 -0.0025 438 TYR A CE1 2814 C CE2 . TYR A 352 ? 0.0836 0.0910 0.0876 0.0019 0.0036 0.0079 438 TYR A CE2 2815 C CZ . TYR A 352 ? 0.0722 0.0810 0.0771 -0.0058 0.0029 0.0006 438 TYR A CZ 2816 O OH . TYR A 352 ? 0.0856 0.0836 0.0863 -0.0007 0.0037 0.0019 438 TYR A OH 2817 N N . PHE A 353 ? 0.0935 0.0895 0.0949 -0.0040 -0.0038 -0.0049 439 PHE A N 2818 C CA . PHE A 353 ? 0.0893 0.0892 0.0868 -0.0023 0.0026 -0.0001 439 PHE A CA 2819 C C . PHE A 353 ? 0.0948 0.0897 0.0974 -0.0028 -0.0030 0.0046 439 PHE A C 2820 O O . PHE A 353 ? 0.0968 0.0944 0.0955 -0.0074 0.0016 0.0032 439 PHE A O 2821 C CB . PHE A 353 ? 0.1019 0.0896 0.0916 -0.0065 0.0030 -0.0091 439 PHE A CB 2822 C CG . PHE A 353 ? 0.1000 0.0866 0.0888 -0.0119 0.0013 -0.0024 439 PHE A CG 2823 C CD1 . PHE A 353 ? 0.0984 0.0867 0.0872 -0.0065 0.0001 0.0055 439 PHE A CD1 2824 C CD2 . PHE A 353 ? 0.1066 0.1157 0.1136 -0.0032 0.0054 0.0189 439 PHE A CD2 2825 C CE1 . PHE A 353 ? 0.0924 0.0951 0.1068 -0.0057 -0.0032 -0.0021 439 PHE A CE1 2826 C CE2 . PHE A 353 ? 0.1197 0.1198 0.1356 -0.0019 0.0057 0.0183 439 PHE A CE2 2827 C CZ . PHE A 353 ? 0.1136 0.1278 0.1232 -0.0088 0.0027 0.0093 439 PHE A CZ 2828 N N . ILE A 354 ? 0.0998 0.0880 0.0896 0.0001 -0.0013 0.0059 440 ILE A N 2829 C CA . ILE A 354 ? 0.1030 0.1020 0.1042 -0.0088 0.0073 0.0039 440 ILE A CA 2830 C C . ILE A 354 ? 0.0933 0.0950 0.0885 -0.0074 0.0047 -0.0001 440 ILE A C 2831 O O . ILE A 354 ? 0.1076 0.1016 0.0912 -0.0041 0.0088 0.0050 440 ILE A O 2832 C CB . ILE A 354 ? 0.1123 0.1073 0.1100 -0.0198 0.0097 0.0047 440 ILE A CB 2833 C CG1 . ILE A 354 ? 0.1443 0.1253 0.1365 -0.0222 0.0052 0.0081 440 ILE A CG1 2834 C CG2 . ILE A 354 ? 0.1310 0.1345 0.1208 -0.0276 0.0186 0.0076 440 ILE A CG2 2835 C CD1 . ILE A 354 ? 0.2010 0.1715 0.1778 -0.0325 0.0102 0.0049 440 ILE A CD1 2836 N N . GLN A 355 ? 0.0909 0.1018 0.0987 -0.0056 0.0043 0.0006 441 GLN A N 2837 C CA . GLN A 355 ? 0.0968 0.0940 0.0946 -0.0029 0.0086 -0.0010 441 GLN A CA 2838 C C . GLN A 355 ? 0.0946 0.0840 0.0883 0.0014 0.0000 0.0053 441 GLN A C 2839 O O . GLN A 355 ? 0.0958 0.0904 0.0822 -0.0023 0.0011 0.0072 441 GLN A O 2840 C CB . GLN A 355 ? 0.0862 0.0992 0.1002 -0.0083 0.0103 0.0008 441 GLN A CB 2841 C CG . GLN A 355 ? 0.0941 0.1011 0.0968 0.0011 0.0038 0.0027 441 GLN A CG 2842 C CD . GLN A 355 ? 0.0953 0.0978 0.0886 0.0023 -0.0017 0.0006 441 GLN A CD 2843 O OE1 . GLN A 355 ? 0.1016 0.1157 0.1040 0.0003 0.0032 0.0118 441 GLN A OE1 2844 N NE2 . GLN A 355 ? 0.0961 0.0958 0.0990 -0.0077 0.0128 -0.0076 441 GLN A NE2 2845 N N . LEU A 356 ? 0.0888 0.0918 0.0896 -0.0034 0.0035 -0.0040 442 LEU A N 2846 C CA . LEU A 356 ? 0.0886 0.0933 0.0855 -0.0018 0.0040 -0.0016 442 LEU A CA 2847 C C . LEU A 356 ? 0.0888 0.0831 0.0796 -0.0027 0.0065 -0.0008 442 LEU A C 2848 O O . LEU A 356 ? 0.0951 0.0953 0.0874 -0.0015 -0.0051 -0.0019 442 LEU A O 2849 C CB . LEU A 356 ? 0.0922 0.0932 0.0806 0.0010 -0.0001 -0.0081 442 LEU A CB 2850 C CG . LEU A 356 ? 0.0860 0.0865 0.0827 0.0001 0.0045 -0.0035 442 LEU A CG 2851 C CD1 . LEU A 356 ? 0.0927 0.0919 0.0841 0.0025 -0.0011 0.0003 442 LEU A CD1 2852 C CD2 . LEU A 356 ? 0.1110 0.0956 0.0819 -0.0013 0.0044 -0.0038 442 LEU A CD2 2853 N N . LEU A 357 ? 0.1009 0.1002 0.0962 -0.0059 -0.0009 0.0000 443 LEU A N 2854 C CA . LEU A 357 ? 0.0999 0.0916 0.1100 -0.0032 -0.0015 0.0091 443 LEU A CA 2855 C C . LEU A 357 ? 0.1101 0.0952 0.0962 -0.0051 -0.0014 0.0160 443 LEU A C 2856 O O . LEU A 357 ? 0.1197 0.1176 0.1091 -0.0037 -0.0041 0.0169 443 LEU A O 2857 C CB . LEU A 357 ? 0.1257 0.1269 0.1502 -0.0099 0.0086 0.0043 443 LEU A CB 2858 C CG . LEU A 357 ? 0.1717 0.1579 0.1461 -0.0171 0.0057 0.0029 443 LEU A CG 2859 C CD1 . LEU A 357 ? 0.1929 0.1542 0.2348 -0.0209 0.0036 0.0048 443 LEU A CD1 2860 C CD2 . LEU A 357 ? 0.1730 0.1642 0.2060 0.0124 0.0107 0.0130 443 LEU A CD2 2861 N N . ARG A 358 ? 0.1089 0.1084 0.0861 -0.0022 0.0009 0.0063 444 ARG A N 2862 C CA . ARG A 358 ? 0.1235 0.1182 0.0883 -0.0068 0.0010 0.0080 444 ARG A CA 2863 C C . ARG A 358 ? 0.1014 0.1135 0.0805 -0.0056 0.0025 -0.0001 444 ARG A C 2864 O O . ARG A 358 ? 0.1348 0.1259 0.0909 -0.0170 0.0077 0.0040 444 ARG A O 2865 C CB . ARG A 358 ? 0.1302 0.1323 0.1104 -0.0160 0.0214 -0.0150 444 ARG A CB 2866 C CG . ARG A 358 ? 0.1548 0.1600 0.1378 -0.0204 0.0079 -0.0111 444 ARG A CG 2867 C CD . ARG A 358 ? 0.1936 0.2178 0.2129 -0.0278 0.0105 0.0057 444 ARG A CD 2868 N NE . ARG A 358 ? 0.2471 0.2792 0.2805 -0.0431 0.0036 -0.0228 444 ARG A NE 2869 C CZ . ARG A 358 ? 0.3460 0.3540 0.3371 -0.0150 0.0106 -0.0055 444 ARG A CZ 2870 N NH1 . ARG A 358 ? 0.3418 0.3943 0.3446 -0.0029 0.0106 -0.0089 444 ARG A NH1 2871 N NH2 . ARG A 358 ? 0.3522 0.3845 0.4042 -0.0187 0.0073 0.0034 444 ARG A NH2 2872 N N . ASN A 359 ? 0.1065 0.1054 0.0789 -0.0055 0.0081 0.0034 445 ASN A N 2873 C CA . ASN A 359 ? 0.1131 0.1006 0.0895 -0.0049 0.0066 0.0046 445 ASN A CA 2874 C C . ASN A 359 ? 0.1096 0.0968 0.0784 -0.0047 -0.0031 0.0007 445 ASN A C 2875 O O . ASN A 359 ? 0.1141 0.1096 0.1018 -0.0112 -0.0074 0.0030 445 ASN A O 2876 C CB . ASN A 359 ? 0.1097 0.0986 0.0883 0.0049 0.0120 -0.0033 445 ASN A CB 2877 C CG . ASN A 359 ? 0.1204 0.1074 0.0998 0.0121 0.0167 -0.0119 445 ASN A CG 2878 O OD1 . ASN A 359 ? 0.1511 0.1286 0.1104 0.0176 0.0169 -0.0090 445 ASN A OD1 2879 N ND2 . ASN A 359 ? 0.1234 0.1398 0.1313 0.0058 0.0164 -0.0284 445 ASN A ND2 2880 N N . ALA A 360 ? 0.1131 0.1002 0.0859 -0.0033 0.0065 0.0025 446 ALA A N 2881 C CA . ALA A 360 ? 0.1001 0.0932 0.0838 -0.0056 0.0001 0.0035 446 ALA A CA 2882 C C . ALA A 360 ? 0.1134 0.1020 0.0788 0.0036 -0.0013 0.0070 446 ALA A C 2883 O O . ALA A 360 ? 0.1167 0.1142 0.0816 -0.0080 -0.0028 0.0052 446 ALA A O 2884 C CB . ALA A 360 ? 0.1050 0.1063 0.1007 -0.0057 -0.0022 -0.0005 446 ALA A CB 2885 N N . ASN A 361 ? 0.1097 0.1063 0.0801 -0.0061 -0.0079 -0.0009 447 ASN A N 2886 C CA . ASN A 361 ? 0.1275 0.1062 0.1018 -0.0133 -0.0153 0.0058 447 ASN A CA 2887 C C . ASN A 361 ? 0.1244 0.1114 0.0957 -0.0105 -0.0063 0.0058 447 ASN A C 2888 O O . ASN A 361 ? 0.1343 0.1306 0.0980 -0.0217 -0.0088 0.0055 447 ASN A O 2889 C CB . ASN A 361 ? 0.1377 0.1160 0.1301 -0.0150 -0.0120 -0.0008 447 ASN A CB 2890 C CG . ASN A 361 ? 0.1906 0.1393 0.1701 -0.0173 -0.0154 -0.0054 447 ASN A CG 2891 O OD1 . ASN A 361 ? 0.2428 0.1858 0.1706 -0.0335 -0.0503 -0.0100 447 ASN A OD1 2892 N ND2 . ASN A 361 ? 0.2220 0.1667 0.2005 -0.0234 -0.0042 0.0077 447 ASN A ND2 2893 N N . PRO A 362 ? 0.1214 0.1384 0.1138 -0.0092 -0.0070 0.0055 448 PRO A N 2894 C CA . PRO A 362 ? 0.1223 0.1323 0.1178 0.0005 -0.0129 0.0172 448 PRO A CA 2895 C C . PRO A 362 ? 0.1258 0.1267 0.1071 -0.0046 -0.0064 0.0102 448 PRO A C 2896 O O . PRO A 362 ? 0.1266 0.1246 0.1089 -0.0050 -0.0064 0.0106 448 PRO A O 2897 C CB . PRO A 362 ? 0.1368 0.1597 0.1626 0.0001 -0.0128 0.0171 448 PRO A CB 2898 C CG . PRO A 362 ? 0.1771 0.2157 0.1931 0.0003 -0.0145 0.0133 448 PRO A CG 2899 C CD . PRO A 362 ? 0.1437 0.1601 0.1377 -0.0012 -0.0065 0.0132 448 PRO A CD 2900 N N . PRO A 363 ? 0.1327 0.1247 0.1102 -0.0090 -0.0101 0.0062 449 PRO A N 2901 C CA . PRO A 363 ? 0.1354 0.1306 0.1017 -0.0025 -0.0073 0.0119 449 PRO A CA 2902 C C . PRO A 363 ? 0.1260 0.1343 0.1188 0.0011 -0.0039 0.0131 449 PRO A C 2903 O O . PRO A 363 ? 0.1437 0.1410 0.1311 0.0057 -0.0027 0.0171 449 PRO A O 2904 C CB . PRO A 363 ? 0.1469 0.1534 0.1242 0.0056 0.0056 0.0126 449 PRO A CB 2905 C CG . PRO A 363 ? 0.2078 0.1904 0.1633 -0.0204 0.0101 0.0017 449 PRO A CG 2906 C CD . PRO A 363 ? 0.1640 0.1577 0.1201 -0.0102 -0.0040 0.0100 449 PRO A CD 2907 N N . PHE A 364 ? 0.1441 0.1342 0.1305 0.0030 -0.0017 0.0162 450 PHE A N 2908 C CA . PHE A 364 ? 0.1757 0.1453 0.1485 0.0002 0.0008 0.0262 450 PHE A CA 2909 C C . PHE A 364 ? 0.2384 0.1932 0.2075 0.0232 0.0029 0.0390 450 PHE A C 2910 O O . PHE A 364 ? 0.2573 0.2178 0.1954 0.0131 0.0246 0.0681 450 PHE A O 2911 C CB . PHE A 364 ? 0.1565 0.1366 0.1770 -0.0107 -0.0024 0.0060 450 PHE A CB 2912 C CG . PHE A 364 ? 0.1474 0.1310 0.1414 -0.0105 -0.0150 0.0056 450 PHE A CG 2913 C CD1 . PHE A 364 ? 0.1591 0.1094 0.1338 -0.0058 -0.0173 -0.0012 450 PHE A CD1 2914 C CD2 . PHE A 364 ? 0.1483 0.1215 0.1374 0.0129 -0.0151 -0.0084 450 PHE A CD2 2915 C CE1 . PHE A 364 ? 0.1514 0.1207 0.1374 0.0192 -0.0194 -0.0061 450 PHE A CE1 2916 C CE2 . PHE A 364 ? 0.1490 0.1295 0.1166 0.0166 -0.0246 -0.0013 450 PHE A CE2 2917 C CZ . PHE A 364 ? 0.1537 0.1326 0.1089 0.0104 -0.0093 -0.0004 450 PHE A CZ 2918 O OXT . PHE A 364 ? 0.2901 0.2174 0.3030 0.0272 0.0277 0.0669 450 PHE A OXT 2919 C C1 . NAG B . ? 0.0975 0.0795 0.0931 -0.0005 -0.0112 -0.0136 500 NAG A C1 2920 C C2 . NAG B . ? 0.0916 0.0930 0.0912 -0.0085 -0.0014 -0.0014 500 NAG A C2 2921 C C3 . NAG B . ? 0.0960 0.1003 0.0973 -0.0144 -0.0121 -0.0168 500 NAG A C3 2922 C C4 . NAG B . ? 0.0989 0.1029 0.1049 -0.0024 0.0028 -0.0172 500 NAG A C4 2923 C C5 . NAG B . ? 0.1013 0.0982 0.1065 -0.0086 0.0009 -0.0125 500 NAG A C5 2924 C C6 . NAG B . ? 0.1102 0.1101 0.1058 -0.0045 0.0020 -0.0122 500 NAG A C6 2925 C C7 . NAG B . ? 0.1006 0.1108 0.1115 -0.0034 0.0029 -0.0082 500 NAG A C7 2926 C C8 . NAG B . ? 0.1244 0.1212 0.1028 -0.0053 -0.0104 -0.0057 500 NAG A C8 2927 N N2 . NAG B . ? 0.0930 0.0962 0.1078 -0.0052 -0.0148 -0.0129 500 NAG A N2 2928 O O3 . NAG B . ? 0.1136 0.1051 0.1081 -0.0184 -0.0096 -0.0211 500 NAG A O3 2929 O O4 . NAG B . ? 0.1230 0.1224 0.1318 -0.0002 0.0002 -0.0194 500 NAG A O4 2930 O O5 . NAG B . ? 0.0932 0.0951 0.1022 -0.0038 -0.0033 -0.0066 500 NAG A O5 2931 O O6 . NAG B . ? 0.1003 0.1021 0.1077 0.0022 -0.0002 -0.0063 500 NAG A O6 2932 O O7 . NAG B . ? 0.1124 0.1207 0.1301 -0.0109 -0.0064 -0.0085 500 NAG A O7 2933 MG MG . MG C . ? 0.1515 0.1310 0.1382 0.0075 -0.0040 0.0130 501 MG A MG 2934 C C . ACT D . ? 0.1601 0.1453 0.1438 0.0050 0.0018 0.0048 502 ACT A C 2935 O O . ACT D . ? 0.1725 0.1621 0.1389 0.0017 0.0050 -0.0006 502 ACT A O 2936 O OXT . ACT D . ? 0.1818 0.1676 0.2115 -0.0003 0.0136 -0.0127 502 ACT A OXT 2937 C CH3 . ACT D . ? 0.1869 0.1783 0.1832 -0.0072 0.0098 0.0003 502 ACT A CH3 2938 C C1 . DMF E . ? 0.1847 0.1559 0.1648 0.0037 -0.0027 0.0142 503 DMF A C1 2939 C C2 . DMF E . ? 0.1939 0.1614 0.1764 -0.0044 0.0013 0.0013 503 DMF A C2 2940 C C . DMF E . ? 0.1457 0.1267 0.1213 0.0026 0.0047 0.0134 503 DMF A C 2941 O O . DMF E . ? 0.1399 0.1198 0.1232 0.0070 -0.0077 0.0123 503 DMF A O 2942 N N . DMF E . ? 0.1533 0.1357 0.1449 -0.0050 -0.0005 0.0101 503 DMF A N 2943 C C1 . DMF F . ? 0.1957 0.2024 0.2324 -0.0190 0.0033 0.0124 504 DMF A C1 2944 C C2 . DMF F . ? 0.1762 0.1790 0.1574 -0.0137 -0.0186 -0.0154 504 DMF A C2 2945 C C . DMF F . ? 0.2277 0.2039 0.1891 0.0062 -0.0010 -0.0015 504 DMF A C 2946 O O . DMF F . ? 0.2180 0.2191 0.1847 -0.0077 -0.0178 0.0064 504 DMF A O 2947 N N . DMF F . ? 0.2041 0.2001 0.1800 -0.0087 -0.0209 -0.0043 504 DMF A N 2948 C C1 . GOL G . ? 0.2255 0.2396 0.2469 -0.0050 -0.0121 0.0045 505 GOL A C1 2949 O O1 . GOL G . ? 0.2593 0.2795 0.2610 0.0002 -0.0120 -0.0104 505 GOL A O1 2950 C C2 . GOL G . ? 0.1661 0.2447 0.1919 0.0143 0.0030 -0.0262 505 GOL A C2 2951 O O2 . GOL G . ? 0.2732 0.2832 0.2285 0.0256 -0.0114 -0.0173 505 GOL A O2 2952 C C3 . GOL G . ? 0.1828 0.1931 0.1709 -0.0070 0.0211 -0.0003 505 GOL A C3 2953 O O3 . GOL G . ? 0.3493 0.2886 0.3268 -0.0109 -0.0049 0.0078 505 GOL A O3 2954 C C1 . GOL H . ? 0.2191 0.2233 0.2408 -0.0093 0.0102 -0.0146 506 GOL A C1 2955 O O1 . GOL H . ? 0.2539 0.1994 0.1927 -0.0210 0.0447 0.0205 506 GOL A O1 2956 C C2 . GOL H . ? 0.2124 0.1756 0.1883 -0.0071 0.0000 0.0114 506 GOL A C2 2957 O O2 . GOL H . ? 0.2012 0.1617 0.1734 -0.0011 0.0016 0.0245 506 GOL A O2 2958 C C3 . GOL H . ? 0.2114 0.2086 0.1997 0.0254 -0.0039 0.0036 506 GOL A C3 2959 O O3 . GOL H . ? 0.2623 0.2376 0.2234 0.0046 -0.0103 0.0092 506 GOL A O3 2960 C C2 . BGC I . ? 0.1670 0.1766 0.1391 0.0364 -0.0089 0.0074 601 BGC A C2 2961 C C3 . BGC I . ? 0.1970 0.2012 0.1756 0.0295 0.0104 -0.0146 601 BGC A C3 2962 C C4 . BGC I . ? 0.1989 0.1770 0.2044 0.0444 0.0027 -0.0112 601 BGC A C4 2963 C C5 . BGC I . ? 0.1656 0.1905 0.1910 0.0386 -0.0108 -0.0125 601 BGC A C5 2964 C C6 . BGC I . ? 0.1503 0.1669 0.1636 0.0099 -0.0152 0.0002 601 BGC A C6 2965 C C1 . BGC I . ? 0.1594 0.1890 0.1756 0.0409 -0.0135 -0.0178 601 BGC A C1 2966 O O2 . BGC I . ? 0.1672 0.1833 0.1539 0.0261 -0.0380 -0.0011 601 BGC A O2 2967 O O3 . BGC I . ? 0.1967 0.2029 0.1496 0.0168 0.0156 0.0107 601 BGC A O3 2968 O O4 . BGC I . ? 0.1978 0.2035 0.1864 0.0665 0.0100 -0.0105 601 BGC A O4 2969 O O5 . BGC I . ? 0.1983 0.2050 0.1770 0.0472 -0.0220 -0.0299 601 BGC A O5 2970 O O6 . BGC I . ? 0.1999 0.1912 0.1825 0.0187 -0.0276 0.0019 601 BGC A O6 2971 C C1 . SGC J . ? 0.1261 0.1895 0.1168 -0.0112 0.0050 -0.0306 602 SGC A C1 2972 C C2 . SGC J . ? 0.1583 0.1496 0.0933 -0.0071 0.0076 -0.0251 602 SGC A C2 2973 O O2 . SGC J . ? 0.1479 0.2435 0.1427 -0.0286 -0.0156 0.0006 602 SGC A O2 2974 C C3 . SGC J . ? 0.1608 0.1753 0.1382 0.0105 -0.0259 -0.0066 602 SGC A C3 2975 O O3 . SGC J . ? 0.1691 0.2168 0.2028 0.0192 -0.0412 -0.0145 602 SGC A O3 2976 C C4 . SGC J . ? 0.1453 0.1855 0.1243 0.0143 -0.0165 -0.0173 602 SGC A C4 2977 C C5 . SGC J . ? 0.1435 0.1819 0.1372 0.0007 0.0063 -0.0087 602 SGC A C5 2978 O O5 . SGC J . ? 0.1328 0.2081 0.1585 -0.0159 -0.0241 -0.0233 602 SGC A O5 2979 C C6 . SGC J . ? 0.1344 0.1855 0.1194 0.0011 -0.0080 -0.0186 602 SGC A C6 2980 O O6 . SGC J . ? 0.1481 0.1600 0.1509 -0.0096 -0.0194 0.0052 602 SGC A O6 2981 S S4 . SGC J . ? 0.1464 0.1835 0.1451 0.0365 -0.0049 -0.0246 602 SGC A S4 2982 C C1 . SGC K . ? 0.1479 0.1817 0.1704 0.0091 0.0056 -0.0035 603 SGC A C1 2983 C C2 . SGC K . ? 0.1765 0.1995 0.1476 -0.0084 -0.0023 0.0085 603 SGC A C2 2984 O O2 . SGC K . ? 0.2470 0.2357 0.1764 0.0101 0.0229 0.0236 603 SGC A O2 2985 C C3 . SGC K . ? 0.1830 0.1933 0.1397 -0.0176 -0.0083 -0.0124 603 SGC A C3 2986 O O3 . SGC K . ? 0.2336 0.2263 0.1839 -0.0257 -0.0206 -0.0269 603 SGC A O3 2987 C C4 . SGC K . ? 0.1384 0.1901 0.1560 -0.0213 0.0064 -0.0038 603 SGC A C4 2988 C C5 . SGC K . ? 0.1323 0.1771 0.1430 -0.0067 0.0012 0.0131 603 SGC A C5 2989 O O5 . SGC K . ? 0.1498 0.1997 0.1675 0.0138 0.0064 0.0200 603 SGC A O5 2990 C C6 . SGC K . ? 0.1493 0.1500 0.1411 -0.0103 0.0078 0.0027 603 SGC A C6 2991 O O6 . SGC K . ? 0.1161 0.1558 0.1425 0.0070 -0.0043 -0.0085 603 SGC A O6 2992 S S4 . SGC K . ? 0.1404 0.2300 0.1500 -0.0242 0.0077 -0.0281 603 SGC A S4 2993 C C1 . SGC L . ? 0.1617 0.1710 0.1631 0.0225 0.0180 0.0145 604 SGC A C1 2994 C C2 . SGC L . ? 0.1649 0.2012 0.1675 0.0160 0.0107 -0.0055 604 SGC A C2 2995 O O2 . SGC L . ? 0.1868 0.2067 0.2058 0.0064 0.0229 -0.0101 604 SGC A O2 2996 C C3 . SGC L . ? 0.1883 0.1712 0.2061 0.0046 0.0056 0.0121 604 SGC A C3 2997 O O3 . SGC L . ? 0.1547 0.1625 0.1783 0.0138 0.0206 0.0260 604 SGC A O3 2998 C C4 . SGC L . ? 0.1833 0.1688 0.1541 0.0228 -0.0032 0.0180 604 SGC A C4 2999 C C5 . SGC L . ? 0.1763 0.1929 0.1760 0.0284 0.0092 0.0034 604 SGC A C5 3000 O O5 . SGC L . ? 0.2048 0.2000 0.1904 0.0174 0.0131 0.0146 604 SGC A O5 3001 C C6 . SGC L . ? 0.1883 0.1951 0.1909 0.0293 0.0189 0.0124 604 SGC A C6 3002 O O6 . SGC L . ? 0.1996 0.2265 0.2166 0.0173 0.0254 0.0088 604 SGC A O6 3003 S S4 . SGC L . ? 0.2069 0.2266 0.2013 0.0464 -0.0123 0.0136 604 SGC A S4 3004 C C1 . MA3 M . ? 0.2935 0.3074 0.2966 0.0033 -0.0011 0.0043 605 MA3 A C1 3005 C C2 . MA3 M . ? 0.2847 0.2831 0.2855 -0.0020 -0.0005 0.0130 605 MA3 A C2 3006 C C3 . MA3 M . ? 0.2440 0.2625 0.2334 0.0029 -0.0051 0.0148 605 MA3 A C3 3007 C C4 . MA3 M . ? 0.2194 0.2082 0.2287 -0.0048 -0.0034 0.0150 605 MA3 A C4 3008 C C5 . MA3 M . ? 0.2509 0.2484 0.2372 0.0010 -0.0035 0.0052 605 MA3 A C5 3009 C C6 . MA3 M . ? 0.2530 0.2574 0.2544 0.0022 -0.0113 -0.0048 605 MA3 A C6 3010 C C7 . MA3 M . ? 0.3042 0.3055 0.3113 0.0104 0.0074 -0.0080 605 MA3 A C7 3011 O O1 . MA3 M . ? 0.2972 0.2799 0.2764 -0.0050 -0.0093 0.0024 605 MA3 A O1 3012 O O2 . MA3 M . ? 0.2993 0.3231 0.2965 -0.0017 0.0089 0.0211 605 MA3 A O2 3013 O O3 . MA3 M . ? 0.2661 0.2404 0.2629 -0.0158 0.0120 0.0214 605 MA3 A O3 3014 S S4 . MA3 M . ? 0.1797 0.2121 0.2038 0.0185 -0.0091 0.0176 605 MA3 A S4 3015 O O5 . MA3 M . ? 0.2731 0.2694 0.2660 0.0032 -0.0069 0.0148 605 MA3 A O5 3016 O O6 . MA3 M . ? 0.2212 0.2290 0.2823 0.0305 -0.0380 -0.0027 605 MA3 A O6 3017 O O . HOH N . ? 0.1336 0.1612 0.1575 0.0145 -0.0020 0.0025 2001 HOH A O 3018 O O . HOH N . ? 0.1708 0.1535 0.2314 0.0242 0.0378 -0.0056 2002 HOH A O 3019 O O . HOH N . ? 0.1416 0.1449 0.1430 0.0113 -0.0115 -0.0020 2003 HOH A O 3020 O O . HOH N . ? 0.3356 0.2920 0.3092 0.0584 0.0433 0.0091 2004 HOH A O 3021 O O . HOH N . ? 0.3261 0.3551 0.3353 0.0223 -0.0076 0.0071 2005 HOH A O 3022 O O . HOH N . ? 0.1721 0.1650 0.1350 -0.0276 -0.0041 -0.0110 2006 HOH A O 3023 O O . HOH N . ? 0.2060 0.1993 0.2032 0.0124 0.0177 -0.0184 2007 HOH A O 3024 O O . HOH N . ? 0.2330 0.2306 0.1897 0.0157 -0.0372 0.0018 2008 HOH A O 3025 O O . HOH N . ? 0.2154 0.2492 0.3094 0.0680 0.0227 0.0404 2009 HOH A O 3026 O O . HOH N . ? 0.4136 0.4101 0.4530 -0.0043 -0.0320 -0.0309 2010 HOH A O 3027 O O . HOH N . ? 0.1843 0.2454 0.1993 -0.0325 -0.0201 0.0102 2011 HOH A O 3028 O O . HOH N . ? 0.1503 0.1400 0.1903 0.0155 0.0019 -0.0180 2012 HOH A O 3029 O O . HOH N . ? 0.2596 0.2089 0.1593 -0.0014 -0.0162 0.0081 2013 HOH A O 3030 O O . HOH N . ? 0.2034 0.2347 0.2291 -0.0025 -0.0344 -0.0246 2014 HOH A O 3031 O O . HOH N . ? 0.1851 0.3402 0.2464 -0.0342 -0.0306 -0.0406 2015 HOH A O 3032 O O . HOH N . ? 0.2674 0.3010 0.2963 0.0060 -0.0006 -0.0135 2016 HOH A O 3033 O O . HOH N . ? 0.3560 0.3235 0.3492 0.0123 0.0011 -0.0081 2017 HOH A O 3034 O O . HOH N . ? 0.4071 0.4332 0.4700 0.0185 -0.0330 0.0060 2018 HOH A O 3035 O O . HOH N . ? 0.1518 0.1518 0.1667 0.0071 0.0036 0.0083 2019 HOH A O 3036 O O . HOH N . ? 0.4183 0.2736 0.2946 0.0033 0.0383 0.0137 2020 HOH A O 3037 O O . HOH N . ? 0.3668 0.3833 0.3380 0.0257 0.0106 0.0489 2021 HOH A O 3038 O O . HOH N . ? 0.1119 0.0939 0.0974 0.0055 0.0024 0.0062 2022 HOH A O 3039 O O . HOH N . ? 0.2666 0.2425 0.2674 0.0009 0.0013 0.0019 2023 HOH A O 3040 O O . HOH N . ? 0.2714 0.2432 0.2944 0.0151 -0.0087 0.0386 2024 HOH A O 3041 O O . HOH N . ? 0.4011 0.4058 0.4161 -0.0001 -0.0082 0.0022 2025 HOH A O 3042 O O . HOH N . ? 0.2738 0.2458 0.1997 -0.0100 0.0165 -0.0308 2026 HOH A O 3043 O O . HOH N . ? 0.3011 0.2478 0.2680 -0.0236 -0.0064 0.0106 2027 HOH A O 3044 O O . HOH N . ? 0.3523 0.3915 0.3770 -0.0052 0.0054 -0.0137 2028 HOH A O 3045 O O . HOH N . ? 0.4036 0.3442 0.4047 0.0019 0.0124 0.0095 2029 HOH A O 3046 O O . HOH N . ? 0.2669 0.2620 0.2395 -0.0095 0.0171 0.0361 2030 HOH A O 3047 O O . HOH N . ? 0.2884 0.2695 0.2851 -0.0395 0.0196 0.0436 2031 HOH A O 3048 O O . HOH N . ? 0.2568 0.2145 0.1627 0.0120 -0.0328 0.0140 2032 HOH A O 3049 O O . HOH N . ? 0.2981 0.2369 0.2465 -0.0672 -0.0059 -0.0049 2033 HOH A O 3050 O O . HOH N . ? 0.3470 0.3453 0.3493 0.0158 0.0073 -0.0014 2034 HOH A O 3051 O O . HOH N . ? 0.2071 0.2808 0.2698 -0.0136 0.0048 -0.0233 2035 HOH A O 3052 O O . HOH N . ? 0.2688 0.2597 0.2699 -0.0409 0.0027 0.0152 2036 HOH A O 3053 O O . HOH N . ? 0.2624 0.2540 0.2700 -0.0139 -0.0269 -0.0104 2037 HOH A O 3054 O O . HOH N . ? 0.3858 0.3778 0.3788 0.0151 0.0051 0.0021 2038 HOH A O 3055 O O . HOH N . ? 0.3983 0.3891 0.4020 -0.0211 0.0183 -0.0023 2039 HOH A O 3056 O O . HOH N . ? 0.2696 0.2484 0.2450 0.0189 0.0127 0.0440 2040 HOH A O 3057 O O . HOH N . ? 0.2891 0.2722 0.2975 0.0150 0.0236 0.0180 2041 HOH A O 3058 O O . HOH N . ? 0.2686 0.2897 0.2606 0.0129 -0.0203 -0.0138 2042 HOH A O 3059 O O . HOH N . ? 0.3076 0.3665 0.3263 -0.0211 0.0250 -0.0155 2043 HOH A O 3060 O O . HOH N . ? 0.5098 0.4841 0.4885 -0.0237 -0.0059 -0.0068 2044 HOH A O 3061 O O . HOH N . ? 0.3037 0.3208 0.2915 -0.0453 0.0455 -0.0154 2045 HOH A O 3062 O O . HOH N . ? 0.3078 0.3239 0.3306 0.0112 0.0048 0.0044 2046 HOH A O 3063 O O . HOH N . ? 0.5152 0.5249 0.5136 0.0100 -0.0089 -0.0011 2047 HOH A O 3064 O O . HOH N . ? 0.1893 0.1649 0.1550 0.0115 -0.0119 0.0097 2048 HOH A O 3065 O O . HOH N . ? 0.3860 0.3488 0.3578 -0.0049 0.0300 -0.0079 2049 HOH A O 3066 O O . HOH N . ? 0.2262 0.2171 0.2447 -0.0338 0.0092 0.0396 2050 HOH A O 3067 O O . HOH N . ? 0.2495 0.2418 0.2243 -0.0141 -0.0001 0.0005 2051 HOH A O 3068 O O . HOH N . ? 0.2995 0.2676 0.3112 0.0010 0.0060 0.0059 2052 HOH A O 3069 O O . HOH N . ? 0.2743 0.2486 0.2281 -0.0186 0.0059 0.0149 2053 HOH A O 3070 O O . HOH N . ? 0.3712 0.4279 0.4461 0.0088 0.0000 -0.0075 2054 HOH A O 3071 O O . HOH N . ? 0.3775 0.3429 0.3982 0.0034 0.0080 -0.0228 2055 HOH A O 3072 O O . HOH N . ? 0.2984 0.2730 0.2961 0.0353 -0.0129 0.0030 2056 HOH A O 3073 O O . HOH N . ? 0.2471 0.2273 0.2392 0.0229 -0.0120 0.0194 2057 HOH A O 3074 O O . HOH N . ? 0.4168 0.4681 0.4654 0.0065 0.0051 0.0091 2058 HOH A O 3075 O O . HOH N . ? 0.3465 0.2814 0.3178 -0.0079 -0.0095 0.0179 2059 HOH A O 3076 O O . HOH N . ? 0.3187 0.3470 0.3536 0.0019 -0.0091 -0.0002 2060 HOH A O 3077 O O . HOH N . ? 0.4101 0.3714 0.3705 0.0004 -0.0045 0.0272 2061 HOH A O 3078 O O . HOH N . ? 0.4182 0.3811 0.3529 0.0432 -0.0266 0.0367 2062 HOH A O 3079 O O . HOH N . ? 0.4360 0.4200 0.3831 -0.0110 0.0206 -0.0097 2063 HOH A O 3080 O O . HOH N . ? 0.4450 0.4372 0.3920 -0.0114 -0.0038 -0.0036 2064 HOH A O 3081 O O . HOH N . ? 0.3738 0.3454 0.4271 -0.0106 0.0064 -0.0140 2065 HOH A O 3082 O O . HOH N . ? 0.2294 0.3237 0.3111 -0.0066 -0.0553 -0.0312 2066 HOH A O 3083 O O . HOH N . ? 0.4564 0.4468 0.4457 0.0194 0.0114 0.0103 2067 HOH A O 3084 O O . HOH N . ? 0.4241 0.4041 0.3913 0.0093 -0.0159 0.0076 2068 HOH A O 3085 O O . HOH N . ? 0.1221 0.1032 0.1049 0.0013 0.0001 -0.0057 2069 HOH A O 3086 O O . HOH N . ? 0.2647 0.1943 0.2810 0.0102 0.0202 0.0134 2070 HOH A O 3087 O O . HOH N . ? 0.1454 0.1256 0.1430 -0.0100 -0.0012 0.0025 2071 HOH A O 3088 O O . HOH N . ? 0.1756 0.1677 0.1830 0.0158 -0.0097 0.0093 2072 HOH A O 3089 O O . HOH N . ? 0.1603 0.1496 0.1497 0.0070 0.0049 0.0163 2073 HOH A O 3090 O O . HOH N . ? 0.1921 0.1655 0.1833 -0.0009 -0.0122 -0.0008 2074 HOH A O 3091 O O . HOH N . ? 0.4565 0.4565 0.3978 0.0190 -0.0078 -0.0043 2075 HOH A O 3092 O O . HOH N . ? 0.5388 0.5388 0.5399 0.0079 0.0048 -0.0029 2076 HOH A O 3093 O O . HOH N . ? 0.2994 0.2690 0.2414 0.0225 0.0059 0.0513 2077 HOH A O 3094 O O . HOH N . ? 0.3602 0.4099 0.3273 0.0262 -0.0172 -0.0127 2078 HOH A O 3095 O O . HOH N . ? 0.1677 0.1620 0.2092 0.0126 0.0123 0.0041 2079 HOH A O 3096 O O . HOH N . ? 0.3688 0.3368 0.4070 0.0109 -0.0063 0.0257 2080 HOH A O 3097 O O . HOH N . ? 0.5301 0.5461 0.5260 0.0081 -0.0001 -0.0021 2081 HOH A O 3098 O O . HOH N . ? 0.1127 0.0990 0.1110 -0.0042 -0.0048 -0.0071 2082 HOH A O 3099 O O . HOH N . ? 0.1043 0.0959 0.1034 0.0066 0.0021 -0.0025 2083 HOH A O 3100 O O . HOH N . ? 0.1092 0.1087 0.1049 -0.0021 0.0020 0.0041 2084 HOH A O 3101 O O . HOH N . ? 0.0967 0.0912 0.0982 0.0006 0.0005 -0.0006 2085 HOH A O 3102 O O . HOH N . ? 0.2122 0.1769 0.2277 0.0135 0.0255 -0.0023 2086 HOH A O 3103 O O . HOH N . ? 0.2723 0.3701 0.3575 0.0111 -0.0330 0.0117 2087 HOH A O 3104 O O . HOH N . ? 0.2713 0.2849 0.3109 -0.0218 0.0280 -0.0259 2088 HOH A O 3105 O O . HOH N . ? 0.3989 0.3932 0.4259 0.0174 0.0128 -0.0114 2089 HOH A O 3106 O O . HOH N . ? 0.4842 0.5019 0.4826 0.0011 -0.0020 0.0179 2090 HOH A O 3107 O O . HOH N . ? 0.2776 0.1916 0.2593 -0.0038 0.0341 0.0342 2091 HOH A O 3108 O O . HOH N . ? 0.0824 0.1804 0.1242 -0.0533 0.0309 0.0038 2092 HOH A O 3109 O O . HOH N . ? 0.4908 0.4552 0.4394 0.0011 -0.0173 0.0042 2093 HOH A O 3110 O O . HOH N . ? 0.1943 0.2014 0.2623 -0.0375 0.0182 0.0245 2094 HOH A O 3111 O O . HOH N . ? 0.2338 0.3002 0.3189 0.0094 0.0541 -0.0163 2095 HOH A O 3112 O O . HOH N . ? 0.1830 0.1950 0.2371 0.0134 0.0243 0.0403 2096 HOH A O 3113 O O . HOH N . ? 0.2539 0.2142 0.2349 0.0100 -0.0099 0.0007 2097 HOH A O 3114 O O . HOH N . ? 0.2206 0.2370 0.2573 0.0000 0.0123 -0.0253 2098 HOH A O 3115 O O . HOH N . ? 0.3114 0.2989 0.2705 0.0225 0.0156 0.0031 2099 HOH A O 3116 O O . HOH N . ? 0.3535 0.4047 0.2993 0.0130 -0.0027 0.0036 2100 HOH A O 3117 O O . HOH N . ? 0.3889 0.3328 0.3110 -0.0354 -0.0121 0.0517 2101 HOH A O 3118 O O . HOH N . ? 0.3003 0.3278 0.3339 0.0070 -0.0019 0.0260 2102 HOH A O 3119 O O . HOH N . ? 0.4557 0.3966 0.4258 -0.0107 -0.0179 -0.0063 2103 HOH A O 3120 O O . HOH N . ? 0.1576 0.2010 0.2081 -0.0147 -0.0047 -0.0153 2104 HOH A O 3121 O O . HOH N . ? 0.1038 0.1066 0.1134 -0.0125 -0.0053 -0.0150 2105 HOH A O 3122 O O . HOH N . ? 0.1002 0.1107 0.1189 -0.0067 -0.0080 -0.0085 2106 HOH A O 3123 O O . HOH N . ? 0.4514 0.4737 0.4689 -0.0048 0.0155 -0.0125 2107 HOH A O 3124 O O . HOH N . ? 0.4433 0.4151 0.4215 0.0040 -0.0243 -0.0012 2108 HOH A O 3125 O O . HOH N . ? 0.3254 0.2593 0.2982 0.0400 0.0084 0.0370 2109 HOH A O 3126 O O . HOH N . ? 0.4758 0.4365 0.4474 0.0354 -0.0116 0.0122 2110 HOH A O 3127 O O . HOH N . ? 0.4572 0.4068 0.4278 -0.0278 -0.0062 0.0263 2111 HOH A O 3128 O O . HOH N . ? 0.1750 0.1512 0.1780 0.0053 -0.0097 0.0096 2112 HOH A O 3129 O O . HOH N . ? 0.1584 0.1752 0.1658 -0.0086 -0.0119 -0.0236 2113 HOH A O 3130 O O . HOH N . ? 0.2499 0.2092 0.2591 -0.0120 0.0086 0.0025 2114 HOH A O 3131 O O . HOH N . ? 0.1722 0.1461 0.1728 -0.0126 0.0068 -0.0161 2115 HOH A O 3132 O O . HOH N . ? 0.1395 0.1371 0.1687 0.0013 0.0071 0.0283 2116 HOH A O 3133 O O . HOH N . ? 0.2664 0.2855 0.2401 0.0071 -0.0166 0.0012 2117 HOH A O 3134 O O . HOH N . ? 0.2909 0.2791 0.2851 -0.0002 -0.0204 -0.0081 2118 HOH A O 3135 O O . HOH N . ? 0.3780 0.3148 0.2814 -0.0175 -0.0349 0.0088 2119 HOH A O 3136 O O . HOH N . ? 0.2624 0.3570 0.3311 0.0134 -0.0315 -0.0089 2120 HOH A O 3137 O O . HOH N . ? 0.2232 0.2489 0.2071 -0.0301 -0.0066 -0.0245 2121 HOH A O 3138 O O . HOH N . ? 0.3628 0.3377 0.4091 -0.0151 -0.0128 -0.0356 2122 HOH A O 3139 O O . HOH N . ? 0.3448 0.3335 0.3822 -0.0149 -0.0141 0.0261 2123 HOH A O 3140 O O . HOH N . ? 0.5202 0.5119 0.5205 -0.0056 0.0029 -0.0001 2124 HOH A O 3141 O O . HOH N . ? 0.5568 0.5280 0.5587 0.0001 0.0086 -0.0055 2125 HOH A O 3142 O O . HOH N . ? 0.1528 0.1501 0.1333 0.0189 -0.0133 0.0027 2126 HOH A O 3143 O O . HOH N . ? 0.1559 0.2169 0.3345 -0.0433 -0.0192 0.0258 2127 HOH A O 3144 O O . HOH N . ? 0.3239 0.2174 0.2676 -0.0225 -0.0032 0.0063 2128 HOH A O 3145 O O . HOH N . ? 0.2683 0.2383 0.1988 -0.0073 0.0139 0.0539 2129 HOH A O 3146 O O . HOH N . ? 0.3300 0.3407 0.3320 -0.0614 -0.0031 0.0081 2130 HOH A O 3147 O O . HOH N . ? 0.4853 0.4385 0.4602 -0.0039 0.0342 -0.0139 2131 HOH A O 3148 O O . HOH N . ? 0.2001 0.1584 0.1757 0.0109 0.0057 -0.0187 2132 HOH A O 3149 O O . HOH N . ? 0.5718 0.5622 0.5569 -0.0037 -0.0023 -0.0105 2133 HOH A O 3150 O O . HOH N . ? 0.3049 0.3071 0.3441 0.0090 -0.0149 -0.0054 2134 HOH A O 3151 O O . HOH N . ? 0.1349 0.1230 0.1223 0.0001 0.0007 -0.0241 2135 HOH A O 3152 O O . HOH N . ? 0.3018 0.3896 0.2734 0.0163 0.0270 -0.0188 2136 HOH A O 3153 O O . HOH N . ? 0.5477 0.5297 0.5280 0.0004 0.0141 0.0095 2137 HOH A O 3154 O O . HOH N . ? 0.1339 0.1557 0.1590 -0.0226 -0.0073 -0.0236 2138 HOH A O 3155 O O . HOH N . ? 0.2701 0.2208 0.2265 -0.0631 0.0020 0.0043 2139 HOH A O 3156 O O . HOH N . ? 0.4802 0.4814 0.4933 -0.0142 0.0041 -0.0069 2140 HOH A O 3157 O O . HOH N . ? 0.2925 0.2947 0.2830 0.0384 0.0669 0.0000 2141 HOH A O 3158 O O . HOH N . ? 0.3642 0.3667 0.4288 0.0043 -0.0152 -0.0312 2142 HOH A O 3159 O O . HOH N . ? 0.3586 0.3451 0.3092 0.0275 0.0255 0.0074 2143 HOH A O 3160 O O . HOH N . ? 0.4593 0.4984 0.4705 -0.0002 0.0125 0.0003 2144 HOH A O 3161 O O . HOH N . ? 0.1909 0.1423 0.1784 0.0199 -0.0089 0.0067 2145 HOH A O 3162 O O . HOH N . ? 0.1885 0.1693 0.1835 -0.0169 0.0254 0.0341 2146 HOH A O 3163 O O . HOH N . ? 0.2662 0.2309 0.1907 0.0086 0.0198 0.0289 2147 HOH A O 3164 O O . HOH N . ? 0.2813 0.2348 0.1877 0.0579 0.0699 0.0296 2148 HOH A O 3165 O O . HOH N . ? 0.3677 0.4289 0.3648 -0.0006 -0.0258 0.0094 2149 HOH A O 3166 O O . HOH N . ? 0.2777 0.2607 0.3076 0.0013 -0.0061 -0.0134 2150 HOH A O 3167 O O . HOH N . ? 0.3291 0.2951 0.2628 -0.0121 0.0099 -0.0428 2151 HOH A O 3168 O O . HOH N . ? 0.3621 0.3368 0.3794 0.0263 0.0133 0.0198 2152 HOH A O 3169 O O . HOH N . ? 0.2267 0.2426 0.2337 0.0348 -0.0147 0.0325 2153 HOH A O 3170 O O . HOH N . ? 0.3395 0.2995 0.3502 0.0064 -0.0089 -0.0078 2154 HOH A O 3171 O O . HOH N . ? 0.4655 0.4730 0.4968 -0.0298 -0.0192 0.0063 2155 HOH A O 3172 O O . HOH N . ? 0.3723 0.3245 0.3495 0.0255 -0.0668 0.0286 2156 HOH A O 3173 O O . HOH N . ? 0.5804 0.5532 0.5739 -0.0124 -0.0011 -0.0076 2157 HOH A O 3174 O O . HOH N . ? 0.2537 0.2841 0.2612 -0.0489 0.0164 -0.0435 2158 HOH A O 3175 O O . HOH N . ? 0.6314 0.6334 0.6209 -0.0024 -0.0058 -0.0045 2159 HOH A O 3176 O O . HOH N . ? 0.3785 0.3335 0.3176 0.0091 -0.0006 0.0369 2160 HOH A O 3177 O O . HOH N . ? 0.4689 0.4239 0.4311 -0.0117 0.0048 0.0452 2161 HOH A O 3178 O O . HOH N . ? 0.7198 0.7166 0.7171 -0.0044 0.0057 0.0035 2162 HOH A O 3179 O O . HOH N . ? 0.4000 0.4516 0.3837 -0.0004 -0.0086 0.0038 2163 HOH A O 3180 O O . HOH N . ? 0.2790 0.3108 0.2654 0.0268 -0.0018 0.0564 2164 HOH A O 3181 O O . HOH N . ? 0.3758 0.4050 0.3705 -0.0053 0.0263 -0.0108 2165 HOH A O 3182 O O . HOH N . ? 0.2026 0.3327 0.3519 -0.0276 0.0011 -0.0014 2166 HOH A O 3183 O O . HOH N . ? 0.1437 0.1389 0.1192 0.0227 -0.0028 0.0123 2167 HOH A O 3184 O O . HOH N . ? 0.1604 0.1512 0.1465 0.0126 -0.0014 0.0134 2168 HOH A O 3185 O O . HOH N . ? 0.3474 0.2334 0.3164 0.0086 0.0445 0.0447 2169 HOH A O 3186 O O . HOH N . ? 0.2304 0.2451 0.3061 0.0442 0.0685 0.0333 2170 HOH A O 3187 O O . HOH N . ? 0.1891 0.2610 0.2378 0.0094 -0.0157 0.0042 2171 HOH A O 3188 O O . HOH N . ? 0.4395 0.4421 0.4955 0.0055 -0.0128 0.0056 2172 HOH A O 3189 O O . HOH N . ? 0.2808 0.2522 0.3076 -0.0042 0.0097 0.0358 2173 HOH A O 3190 O O . HOH N . ? 0.4318 0.3636 0.3381 0.0043 0.0033 0.0188 2174 HOH A O 3191 O O . HOH N . ? 0.0955 0.0849 0.0960 0.0077 -0.0020 -0.0080 2175 HOH A O 3192 O O . HOH N . ? 0.1199 0.1131 0.1201 -0.0029 -0.0007 0.0045 2176 HOH A O 3193 O O . HOH N . ? 0.4751 0.5219 0.4971 -0.0193 0.0113 0.0068 2177 HOH A O 3194 O O . HOH N . ? 0.1870 0.2452 0.2029 0.0022 0.0049 -0.0235 2178 HOH A O 3195 O O . HOH N . ? 0.4410 0.4470 0.4099 -0.0121 0.0105 0.0045 2179 HOH A O 3196 O O . HOH N . ? 0.3102 0.3244 0.2611 -0.0169 0.0236 0.0060 2180 HOH A O 3197 O O . HOH N . ? 0.4080 0.3950 0.3361 0.0336 -0.0118 0.0050 2181 HOH A O 3198 O O . HOH N . ? 0.5318 0.5078 0.5323 0.0086 0.0152 -0.0019 2182 HOH A O 3199 O O . HOH N . ? 0.3365 0.3403 0.3331 -0.0017 0.0187 -0.0115 2183 HOH A O 3200 O O . HOH N . ? 0.2447 0.2529 0.1888 -0.0016 -0.0053 -0.0081 2184 HOH A O 3201 O O . HOH N . ? 0.4144 0.4070 0.4101 0.0073 0.0352 0.0101 2185 HOH A O 3202 O O . HOH N . ? 0.2252 0.2723 0.3274 0.0528 0.0228 -0.0121 2186 HOH A O 3203 O O . HOH N . ? 0.2011 0.2671 0.2655 0.0224 0.0221 0.0012 2187 HOH A O 3204 O O . HOH N . ? 0.1126 0.1272 0.1315 -0.0025 -0.0214 0.0005 2188 HOH A O 3205 O O . HOH N . ? 0.1481 0.1471 0.1520 0.0056 -0.0101 -0.0063 2189 HOH A O 3206 O O . HOH N . ? 0.2396 0.3061 0.2713 -0.0294 0.0340 -0.0170 2190 HOH A O 3207 O O . HOH N . ? 0.1678 0.1922 0.1475 0.0284 -0.0259 -0.0052 2191 HOH A O 3208 O O . HOH N . ? 0.2872 0.3155 0.2936 0.0142 -0.0459 -0.0108 2192 HOH A O 3209 O O . HOH N . ? 0.0948 0.1008 0.0908 -0.0042 -0.0023 -0.0032 2193 HOH A O 3210 O O . HOH N . ? 0.2375 0.2542 0.2603 -0.0474 -0.0563 0.0453 2194 HOH A O 3211 O O . HOH N . ? 0.3690 0.3452 0.3864 0.0024 0.0140 0.0057 2195 HOH A O 3212 O O . HOH N . ? 0.4944 0.4199 0.5090 -0.0037 -0.0137 -0.0049 2196 HOH A O 3213 O O . HOH N . ? 0.1183 0.1645 0.1583 0.0120 -0.0054 0.0274 2197 HOH A O 3214 O O . HOH N . ? 0.1931 0.1896 0.1806 -0.0133 0.0069 -0.0073 2198 HOH A O 3215 O O . HOH N . ? 0.1943 0.1788 0.1427 0.0158 -0.0234 0.0130 2199 HOH A O 3216 O O . HOH N . ? 0.2598 0.3418 0.3354 0.0482 0.0129 -0.0089 2200 HOH A O 3217 O O . HOH N . ? 0.1457 0.1928 0.1997 0.0045 -0.0017 0.0094 2201 HOH A O 3218 O O . HOH N . ? 0.3005 0.3249 0.2558 -0.0253 -0.0196 0.0024 2202 HOH A O 3219 O O . HOH N . ? 0.6369 0.6310 0.6156 -0.0038 0.0147 0.0065 2203 HOH A O 3220 O O . HOH N . ? 0.3344 0.3520 0.3193 0.0055 0.0022 -0.0104 2204 HOH A O 3221 O O . HOH N . ? 0.1779 0.1788 0.1326 0.0343 -0.0145 -0.0112 2205 HOH A O 3222 O O . HOH N . ? 0.3709 0.4076 0.3388 0.0354 -0.0193 -0.0110 2206 HOH A O 3223 O O . HOH N . ? 0.4080 0.4160 0.4247 -0.0141 -0.0053 0.0115 2207 HOH A O 3224 O O . HOH N . ? 0.3552 0.3517 0.3549 -0.0025 -0.0251 0.0296 2208 HOH A O 3225 O O . HOH N . ? 0.3273 0.3216 0.3150 -0.0177 -0.0160 -0.0045 2209 HOH A O 3226 O O . HOH N . ? 0.2882 0.2964 0.3240 0.0423 0.0088 0.0262 2210 HOH A O 3227 O O . HOH N . ? 0.3885 0.4212 0.3999 -0.0268 0.0159 -0.0215 2211 HOH A O 3228 O O . HOH N . ? 0.4623 0.4872 0.4655 0.0092 -0.0040 -0.0133 2212 HOH A O 3229 O O . HOH N . ? 0.2843 0.3129 0.2829 -0.0172 0.0078 0.0080 2213 HOH A O 3230 O O . HOH N . ? 0.3066 0.3300 0.3178 0.0019 -0.0135 -0.0401 2214 HOH A O 3231 O O . HOH N . ? 0.1570 0.1588 0.1357 0.0002 -0.0240 -0.0009 2215 HOH A O 3232 O O . HOH N . ? 0.5211 0.5345 0.5021 -0.0043 0.0074 0.0117 2216 HOH A O 3233 O O . HOH N . ? 0.3703 0.4308 0.4874 -0.0135 0.0142 0.0046 2217 HOH A O 3234 O O . HOH N . ? 0.1138 0.1437 0.2013 -0.0043 -0.0220 -0.0045 2218 HOH A O 3235 O O . HOH N . ? 0.2153 0.1761 0.1652 -0.0411 0.0065 -0.0073 2219 HOH A O 3236 O O . HOH N . ? 0.1855 0.1872 0.2230 -0.0224 0.0055 -0.0051 2220 HOH A O 3237 O O . HOH N . ? 0.1505 0.1543 0.1151 0.0051 -0.0125 0.0072 2221 HOH A O 3238 O O . HOH N . ? 0.4662 0.4288 0.3717 0.0000 -0.0165 -0.0005 2222 HOH A O 3239 O O . HOH N . ? 0.5043 0.4886 0.5166 0.0018 -0.0070 0.0116 2223 HOH A O 3240 O O . HOH N . ? 0.3960 0.4126 0.3838 -0.0100 -0.0283 -0.0081 2224 HOH A O 3241 O O . HOH N . ? 0.3900 0.4542 0.4412 0.0179 -0.0075 0.0129 2225 HOH A O 3242 O O . HOH N . ? 0.2270 0.1664 0.1631 0.0014 0.0009 -0.0187 2226 HOH A O 3243 O O . HOH N . ? 0.3538 0.3463 0.3587 -0.0040 -0.0003 -0.0056 2227 HOH A O 3244 O O . HOH N . ? 0.3091 0.2105 0.2832 0.0109 -0.0073 0.0453 2228 HOH A O 3245 O O . HOH N . ? 0.1419 0.1472 0.1099 -0.0028 -0.0168 0.0112 2229 HOH A O 3246 O O . HOH N . ? 0.3583 0.3705 0.3646 0.0017 0.0301 -0.0178 2230 HOH A O 3247 O O . HOH N . ? 0.3062 0.2950 0.2605 0.0128 -0.0019 0.0775 2231 HOH A O 3248 O O . HOH N . ? 0.2912 0.2951 0.1914 -0.0060 0.0078 -0.0013 2232 HOH A O 3249 O O . HOH N . ? 0.3141 0.3331 0.3257 -0.0151 -0.0037 0.0318 2233 HOH A O 3250 O O . HOH N . ? 0.3961 0.3067 0.3240 0.0319 0.0103 -0.0131 2234 HOH A O 3251 O O . HOH N . ? 0.2615 0.2527 0.1890 0.0403 0.0564 0.0017 2235 HOH A O 3252 O O . HOH N . ? 0.4107 0.3524 0.3495 0.0012 0.0106 0.0019 2236 HOH A O 3253 O O . HOH N . ? 0.3798 0.3650 0.3453 0.0017 -0.0072 -0.0352 2237 HOH A O 3254 O O . HOH N . ? 0.0986 0.1056 0.1075 -0.0104 -0.0049 -0.0078 2238 HOH A O 3255 O O . HOH N . ? 0.1877 0.1950 0.1601 -0.0132 -0.0010 -0.0140 2239 HOH A O 3256 O O . HOH N . ? 0.2106 0.3404 0.2641 -0.0172 -0.0282 0.0087 2240 HOH A O 3257 O O . HOH N . ? 0.4215 0.3648 0.3775 -0.0217 -0.0125 0.0100 2241 HOH A O 3258 O O . HOH N . ? 0.4098 0.3810 0.4326 0.0067 0.0099 -0.0141 2242 HOH A O 3259 O O . HOH N . ? 0.2960 0.3098 0.2357 0.0128 0.0092 -0.0179 2243 HOH A O 3260 O O . HOH N . ? 0.2760 0.2768 0.2620 0.0046 0.0329 0.0062 2244 HOH A O 3261 O O . HOH N . ? 0.5188 0.5055 0.4957 -0.0045 -0.0167 -0.0008 2245 HOH A O 3262 O O . HOH N . ? 0.4502 0.4350 0.3795 0.0081 0.0000 -0.0153 2246 HOH A O 3263 O O . HOH N . ? 0.3609 0.3160 0.3730 -0.0497 0.0048 0.0060 2247 HOH A O 3264 O O . HOH N . ? 0.3767 0.2571 0.3304 -0.0278 0.0155 -0.0292 2248 HOH A O 3265 O O . HOH N . ? 0.1055 0.1104 0.1217 -0.0069 0.0049 -0.0061 2249 HOH A O 3266 O O . HOH N . ? 0.1740 0.1544 0.1429 0.0019 0.0054 -0.0150 2250 HOH A O 3267 O O . HOH N . ? 0.2829 0.3047 0.3172 -0.0102 -0.0144 0.0047 2251 HOH A O 3268 O O . HOH N . ? 0.2762 0.3179 0.2991 -0.0042 -0.0084 0.0124 2252 HOH A O 3269 O O . HOH N . ? 0.1890 0.1786 0.1645 -0.0037 0.0255 -0.0325 2253 HOH A O 3270 O O . HOH N . ? 0.1520 0.1706 0.1651 -0.0076 0.0061 -0.0141 2254 HOH A O 3271 O O . HOH N . ? 0.3978 0.3346 0.2567 -0.0304 0.0123 0.0193 2255 HOH A O 3272 O O . HOH N . ? 0.3548 0.3411 0.3834 0.0271 -0.0229 0.0114 2256 HOH A O 3273 O O . HOH N . ? 0.2367 0.2631 0.3061 0.0245 -0.0126 0.0108 2257 HOH A O 3274 O O . HOH N . ? 0.2870 0.2707 0.3305 -0.0037 0.0151 0.0057 2258 HOH A O 3275 O O . HOH N . ? 0.1881 0.2557 0.2760 0.0087 -0.0159 -0.0184 2259 HOH A O 3276 O O . HOH N . ? 0.4788 0.4613 0.4469 -0.0065 0.0178 0.0209 2260 HOH A O 3277 O O . HOH N . ? 0.3044 0.2999 0.3037 0.0182 -0.0307 -0.0138 2261 HOH A O 3278 O O . HOH N . ? 0.4575 0.4151 0.4451 0.0083 -0.0076 -0.0076 2262 HOH A O 3279 O O . HOH N . ? 0.2267 0.2930 0.2458 0.0282 -0.0039 -0.0091 2263 HOH A O 3280 O O . HOH N . ? 0.3872 0.3971 0.3683 -0.0112 0.0362 -0.0333 2264 HOH A O 3281 O O . HOH N . ? 0.3634 0.3962 0.4637 0.0393 -0.0130 -0.0105 2265 HOH A O 3282 O O . HOH N . ? 0.2690 0.2996 0.2440 -0.0619 -0.0144 -0.0466 2266 HOH A O 3283 O O . HOH N . ? 0.5227 0.4894 0.4495 -0.0133 0.0081 -0.0111 2267 HOH A O 3284 O O . HOH N . ? 0.1522 0.1685 0.1745 0.0243 0.0077 -0.0310 2268 HOH A O 3285 O O . HOH N . ? 0.3305 0.3127 0.2739 -0.0158 0.0007 -0.0337 2269 HOH A O 3286 O O . HOH N . ? 0.2256 0.2085 0.2070 0.0255 -0.0112 -0.0139 2270 HOH A O 3287 O O . HOH N . ? 0.2749 0.1971 0.1681 0.0123 -0.0077 -0.0140 2271 HOH A O 3288 O O . HOH N . ? 0.4116 0.4045 0.4243 0.0069 0.0164 -0.0133 2272 HOH A O 3289 O O . HOH N . ? 0.2338 0.2288 0.2405 0.0402 -0.0097 -0.0290 2273 HOH A O 3290 O O . HOH N . ? 0.2932 0.3013 0.3144 0.0064 -0.0100 -0.0065 2274 HOH A O 3291 O O . HOH N . ? 0.2717 0.3165 0.3388 0.0034 0.0025 -0.0185 2275 HOH A O 3292 O O . HOH N . ? 0.1628 0.1563 0.1515 0.0004 -0.0005 -0.0067 2276 HOH A O 3293 O O . HOH N . ? 0.2280 0.1973 0.1943 -0.0127 -0.0299 -0.0277 2277 HOH A O 3294 O O . HOH N . ? 0.3518 0.2335 0.2956 0.0334 -0.0534 0.0303 2278 HOH A O 3295 O O . HOH N . ? 0.3225 0.4155 0.3447 0.0322 -0.0328 0.0177 2279 HOH A O 3296 O O . HOH N . ? 0.2762 0.2273 0.1972 -0.0112 -0.0054 0.0093 2280 HOH A O 3297 O O . HOH N . ? 0.2118 0.2104 0.2241 -0.0366 0.0048 0.0230 2281 HOH A O 3298 O O . HOH N . ? 0.3065 0.3304 0.3250 0.0320 -0.0434 -0.0059 2282 HOH A O 3299 O O . HOH N . ? 0.2204 0.2924 0.2330 -0.0148 -0.0118 0.0149 2283 HOH A O 3300 O O . HOH N . ? 0.2208 0.2975 0.2190 -0.0310 -0.0001 0.0027 2284 HOH A O 3301 O O . HOH N . ? 0.1959 0.2317 0.2396 -0.0016 -0.0311 -0.0179 2285 HOH A O 3302 O O . HOH N . ? 0.4658 0.4881 0.4765 -0.0100 -0.0078 -0.0003 2286 HOH A O 3303 O O . HOH N . ? 0.4272 0.4437 0.4191 0.0026 0.0007 0.0048 2287 HOH A O 3304 O O . HOH N . ? 0.1060 0.0975 0.1043 -0.0055 0.0049 -0.0003 2288 HOH A O 3305 O O . HOH N . ? 0.0902 0.0926 0.0915 0.0012 -0.0029 0.0008 2289 HOH A O 3306 O O . HOH N . ? 0.2909 0.3473 0.3267 -0.0098 -0.0296 -0.0391 2290 HOH A O 3307 O O . HOH N . ? 0.1918 0.1780 0.2051 0.0064 -0.0083 0.0169 2291 HOH A O 3308 O O . HOH N . ? 0.3237 0.3490 0.3279 0.0145 -0.0077 0.0231 2292 HOH A O 3309 O O . HOH N . ? 0.4195 0.4048 0.4132 -0.0213 0.0067 0.0185 2293 HOH A O 3310 O O . HOH N . ? 0.3546 0.3428 0.3455 0.0153 -0.0003 -0.0012 2294 HOH A O 3311 O O . HOH N . ? 0.5848 0.5506 0.5692 -0.0015 0.0056 0.0006 2295 HOH A O 3312 O O . HOH N . ? 0.4706 0.4663 0.4927 -0.0075 0.0030 -0.0021 2296 HOH A O 3313 O O . HOH N . ? 0.3623 0.3812 0.3372 -0.0279 -0.0089 0.0405 2297 HOH A O 3314 O O . HOH N . ? 0.4567 0.4669 0.4462 -0.0153 -0.0173 0.0137 2298 HOH A O 3315 O O . HOH N . ? 0.2465 0.3510 0.2645 -0.0013 0.0156 0.0090 2299 HOH A O 3316 O O . HOH N . ? 0.1322 0.1782 0.1635 0.0201 -0.0132 0.0164 2300 HOH A O 3317 O O . HOH N . ? 0.3715 0.3551 0.3797 -0.0239 -0.0122 0.0065 2301 HOH A O 3318 O O . HOH N . ? 0.2423 0.2309 0.2361 -0.0182 -0.0018 0.0042 2302 HOH A O 3319 O O . HOH N . ? 0.2665 0.3191 0.3218 -0.0264 0.0214 0.0434 2303 HOH A O 3320 O O . HOH N . ? 0.2583 0.2539 0.2401 -0.0048 0.0365 0.0339 2304 HOH A O 3321 O O . HOH N . ? 0.4098 0.3926 0.4214 -0.0317 0.0020 0.0099 2305 HOH A O 3322 O O . HOH N . ? 0.4224 0.3991 0.4322 -0.0289 0.0034 -0.0196 2306 HOH A O 3323 O O . HOH N . ? 0.4955 0.4548 0.4626 0.0240 -0.0143 -0.0115 2307 HOH A O 3324 O O . HOH N . ? 0.4080 0.3296 0.2719 0.0051 -0.0598 -0.0065 2308 HOH A O 3325 O O . HOH N . ? 0.1988 0.2460 0.2140 0.0013 0.0144 0.0081 2309 HOH A O 3326 O O . HOH N . ? 0.2490 0.2072 0.1475 -0.0530 -0.0259 0.0361 2310 HOH A O 3327 O O . HOH N . ? 0.1465 0.1219 0.1179 0.0029 -0.0088 0.0172 2311 HOH A O 3328 O O . HOH N . ? 0.1907 0.2575 0.2364 0.0191 0.0043 0.0094 2312 HOH A O 3329 O O . HOH N . ? 0.3407 0.4481 0.3546 0.0363 0.0338 0.0202 2313 HOH A O 3330 O O . HOH N . ? 0.3838 0.4052 0.3595 0.0077 -0.0193 -0.0057 2314 HOH A O 3331 O O . HOH N . ? 0.1449 0.1379 0.1357 0.0005 -0.0239 0.0012 2315 HOH A O 3332 O O . HOH N . ? 0.3549 0.3805 0.3826 -0.0007 0.0076 0.0018 2316 HOH A O 3333 O O . HOH N . ? 0.4060 0.3878 0.3910 -0.0009 -0.0165 -0.0126 2317 HOH A O 3334 O O . HOH N . ? 0.3610 0.3611 0.3297 -0.0088 -0.0020 0.0354 2318 HOH A O 3335 O O . HOH N . ? 0.2469 0.2830 0.2988 -0.0073 -0.0213 -0.0159 2319 HOH A O 3336 O O . HOH N . ? 0.1318 0.1785 0.1872 0.0227 0.0060 -0.0063 2320 HOH A O 3337 O O . HOH N . ? 0.2885 0.3452 0.3739 -0.0321 -0.0450 0.0028 2321 HOH A O 3338 O O . HOH N . ? 0.1489 0.1834 0.1643 -0.0011 -0.0015 -0.0113 2322 HOH A O 3339 O O . HOH N . ? 0.4058 0.4189 0.3946 0.0057 -0.0251 0.0153 2323 HOH A O 3340 O O . HOH N . ? 0.1389 0.1605 0.1257 0.0277 -0.0087 0.0331 2324 HOH A O 3341 O O . HOH N . ? 0.2256 0.1962 0.2039 0.0154 -0.0143 0.0257 2325 HOH A O 3342 O O . HOH N . ? 0.2790 0.2892 0.3076 0.0098 0.0250 0.0033 2326 HOH A O 3343 O O . HOH N . ? 0.3336 0.3040 0.2326 0.0119 -0.0378 -0.0077 2327 HOH A O 3344 O O . HOH N . ? 0.2932 0.3218 0.3290 0.0005 0.0137 -0.0409 2328 HOH A O 3345 O O . HOH N . ? 0.2693 0.2312 0.1746 0.0255 -0.0198 0.0020 2329 HOH A O 3346 O O . HOH N . ? 0.2624 0.2136 0.1802 -0.0063 -0.0073 0.0039 2330 HOH A O 3347 O O . HOH N . ? 0.1446 0.1448 0.1297 0.0181 -0.0027 0.0078 2331 HOH A O 3348 O O . HOH N . ? 0.1991 0.1916 0.1608 0.0050 0.0210 -0.0200 2332 HOH A O 3349 O O . HOH N . ? 0.3274 0.2927 0.2813 0.0000 0.0055 0.0173 2333 HOH A O 3350 O O . HOH N . ? 0.2495 0.2785 0.2653 -0.0015 0.0229 0.0097 2334 HOH A O 3351 O O . HOH N . ? 0.1417 0.1668 0.1233 0.0215 0.0031 0.0033 2335 HOH A O 3352 O O . HOH N . ? 0.3090 0.2701 0.3459 -0.0370 0.0393 0.0261 2336 HOH A O 3353 O O . HOH N . ? 0.1667 0.2588 0.1682 0.0056 0.0349 -0.0024 2337 HOH A O 3354 O O . HOH N . ? 0.2541 0.2354 0.1899 -0.0027 -0.0270 -0.0076 2338 HOH A O 3355 O O . HOH N . ? 0.1148 0.1467 0.1021 0.0126 -0.0042 0.0209 2339 HOH A O 3356 O O . HOH N . ? 0.3311 0.3057 0.3231 -0.0059 0.0065 -0.0193 2340 HOH A O 3357 O O . HOH N . ? 0.4658 0.3991 0.4178 -0.0140 0.0009 -0.0051 2341 HOH A O 3358 O O . HOH N . ? 0.5658 0.5723 0.5511 -0.0135 -0.0077 -0.0093 2342 HOH A O 3359 O O . HOH N . ? 0.2607 0.2974 0.3245 0.0136 -0.0067 -0.0039 2343 HOH A O 3360 O O . HOH N . ? 0.4330 0.4762 0.4057 -0.0088 0.0131 0.0001 2344 HOH A O 3361 O O . HOH N . ? 0.2327 0.2396 0.2025 0.0082 -0.0005 -0.0072 2345 HOH A O 3362 O O . HOH N . ? 0.1816 0.2377 0.2103 -0.0103 -0.0507 -0.0498 2346 HOH A O 3363 O O . HOH N . ? 0.3185 0.3494 0.3059 0.0420 0.0126 -0.0083 2347 HOH A O 3364 O O . HOH N . ? 0.3179 0.3237 0.3449 0.0228 0.0041 0.0044 2348 HOH A O 3365 O O . HOH N . ? 0.2691 0.2255 0.2528 -0.0168 -0.0187 0.0051 2349 HOH A O 3366 O O . HOH N . ? 0.1913 0.2095 0.2281 -0.0018 -0.0259 0.0230 2350 HOH A O 3367 O O . HOH N . ? 0.5004 0.4877 0.4935 -0.0084 0.0120 -0.0005 2351 HOH A O 3368 O O . HOH N . ? 0.1242 0.1655 0.1822 0.0156 -0.0015 0.0177 2352 HOH A O 3369 O O . HOH N . ? 0.1214 0.1277 0.1385 0.0029 0.0151 -0.0090 2353 HOH A O 3370 O O . HOH N . ? 0.3278 0.2904 0.2948 0.0179 0.0121 -0.0025 2354 HOH A O 3371 O O . HOH N . ? 0.3918 0.3673 0.3815 0.0115 0.0395 -0.0177 2355 HOH A O 3372 O O . HOH N . ? 0.2308 0.2130 0.1934 -0.0068 -0.0094 0.0132 2356 HOH A O 3373 O O . HOH N . ? 0.1147 0.1112 0.1469 0.0120 -0.0024 -0.0092 2357 HOH A O 3374 O O . HOH N . ? 0.1370 0.1511 0.1505 -0.0176 -0.0196 -0.0032 2358 HOH A O 3375 O O . HOH N . ? 0.1061 0.1274 0.1153 0.0099 0.0011 -0.0027 2359 HOH A O 3376 O O . HOH N . ? 0.0901 0.0847 0.0931 0.0038 0.0032 -0.0019 2360 HOH A O 3377 O O . HOH N . ? 0.1102 0.1766 0.1185 0.0040 0.0016 -0.0246 2361 HOH A O 3378 O O . HOH N . ? 0.0859 0.0860 0.0811 -0.0017 -0.0092 0.0031 2362 HOH A O 3379 O O . HOH N . ? 0.0859 0.0827 0.0819 0.0011 -0.0090 0.0027 2363 HOH A O 3380 O O . HOH N . ? 0.1036 0.0918 0.0859 -0.0125 0.0067 0.0030 2364 HOH A O 3381 O O . HOH N . ? 0.2280 0.2411 0.2608 -0.0092 -0.0126 -0.0022 2365 HOH A O 3382 O O . HOH N . ? 0.2438 0.1617 0.2157 0.0086 0.0868 -0.0023 2366 HOH A O 3383 O O . HOH N . ? 0.2096 0.1671 0.1964 0.0201 0.0403 0.0262 2367 HOH A O 3384 O O . HOH N . ? 0.3123 0.2171 0.2727 0.0522 0.0034 0.0352 2368 HOH A O 3385 O O . HOH N . ? 0.5379 0.5471 0.4901 0.0103 -0.0069 0.0238 2369 HOH A O 3386 O O . HOH N . ? 0.2867 0.2368 0.2926 0.0289 -0.0066 0.0154 2370 HOH A O 3387 O O . HOH N . ? 0.4339 0.4213 0.4272 0.0006 0.0001 0.0105 2371 HOH A O 3388 O O . HOH N . ? 0.3996 0.3852 0.4434 -0.0195 0.0114 -0.0016 2372 HOH A O 3389 O O . HOH N . ? 0.4600 0.3652 0.3903 -0.0208 0.0246 -0.0229 2373 HOH A O 3390 O O . HOH N . ? 0.3090 0.2833 0.2563 0.0257 -0.0118 0.0216 2374 HOH A O 3391 O O . HOH N . ? 0.1568 0.1998 0.1649 0.0150 -0.0047 0.0084 2375 HOH A O 3392 O O . HOH N . ? 0.1603 0.1439 0.1983 -0.0435 0.0252 0.0053 2376 HOH A O 3393 O O . HOH N . ? 0.2431 0.2473 0.3294 0.0200 -0.0238 0.0108 2377 HOH A O 3394 O O . HOH N . ? 0.3287 0.3108 0.2802 0.0000 -0.0157 0.0054 2378 HOH A O 3395 O O . HOH N . ? 0.5090 0.4489 0.4446 -0.0143 0.0052 0.0051 2379 HOH A O 3396 O O . HOH N . ? 0.1030 0.1082 0.1055 -0.0104 0.0048 0.0052 2380 HOH A O 3397 O O . HOH N . ? 0.1906 0.2251 0.2998 -0.0332 -0.0641 0.0262 2381 HOH A O 3398 O O . HOH N . ? 0.1037 0.1115 0.1171 0.0013 0.0032 0.0068 2382 HOH A O 3399 O O . HOH N . ? 0.1849 0.1779 0.1674 0.0087 0.0300 0.0038 2383 HOH A O 3400 O O . HOH N . ? 0.3083 0.2439 0.2144 -0.0210 -0.0184 0.0083 2384 HOH A O 3401 O O . HOH N . ? 0.3344 0.3901 0.3235 0.0276 0.0330 0.0050 2385 HOH A O 3402 O O . HOH N . ? 0.5123 0.4948 0.4504 0.0053 -0.0010 -0.0017 2386 HOH A O 3403 O O . HOH N . ? 0.1872 0.2017 0.2775 0.0089 0.0274 0.0224 2387 HOH A O 3404 O O . HOH N . ? 0.2749 0.2345 0.2654 -0.0192 0.0348 0.0478 2388 HOH A O 3405 O O . HOH N . ? 0.1945 0.2410 0.2008 0.0211 0.0207 0.0394 2389 HOH A O 3406 O O . HOH N . ? 0.2377 0.3098 0.3189 -0.0042 -0.0574 -0.0066 2390 HOH A O 3407 O O . HOH N . ? 0.1371 0.1750 0.1948 -0.0165 -0.0002 -0.0089 2391 HOH A O 3408 O O . HOH N . ? 0.1922 0.2027 0.2238 -0.0208 0.0091 -0.0105 2392 HOH A O 3409 O O . HOH N . ? 0.2113 0.2749 0.2794 0.0034 -0.0140 0.0043 2393 HOH A O 3410 O O . HOH N . ? 0.3021 0.3302 0.3931 -0.0452 -0.0504 -0.0100 2394 HOH A O 3411 O O . HOH N . ? 0.1111 0.1062 0.1041 0.0064 -0.0128 0.0051 2395 HOH A O 3412 O O . HOH N . ? 0.1540 0.1538 0.1205 0.0232 -0.0035 -0.0035 2396 HOH A O 3413 O O . HOH N . ? 0.1031 0.1271 0.1100 0.0087 -0.0128 -0.0139 2397 HOH A O 3414 O O . HOH N . ? 0.1132 0.0995 0.1016 0.0133 0.0131 0.0012 2398 HOH A O 3415 O O . HOH N . ? 0.1115 0.1292 0.0820 0.0203 -0.0372 -0.0112 2399 HOH A O 3416 O O . HOH N . ? 0.1930 0.2104 0.2055 0.0114 -0.0135 0.0462 2400 HOH A O 3417 O O . HOH N . ? 0.4036 0.4082 0.3317 -0.0086 -0.0074 0.0250 2401 HOH A O 3418 O O . HOH N . ? 0.4008 0.3534 0.3396 -0.0196 -0.0001 -0.0052 2402 HOH A O 3419 O O . HOH N . ? 0.4956 0.5335 0.5142 -0.0070 -0.0183 -0.0123 2403 HOH A O 3420 O O . HOH N . ? 0.4843 0.5021 0.4931 -0.0049 0.0035 -0.0090 2404 HOH A O 3421 O O . HOH N . ? 0.3163 0.3008 0.2321 0.0002 0.0271 0.0513 2405 HOH A O 3422 O O . HOH N . ? 0.3169 0.3917 0.2778 0.0014 0.0246 -0.0224 2406 HOH A O 3423 O O . HOH N . ? 0.6202 0.6408 0.6197 0.0039 0.0036 -0.0002 2407 HOH A O 3424 O O . HOH N . ? 0.2719 0.2370 0.2778 -0.0087 0.0542 0.0051 2408 HOH A O 3425 O O . HOH N . ? 0.2577 0.2724 0.2001 -0.0429 0.0137 -0.0399 2409 HOH A O 3426 O O . HOH N . ? 0.4962 0.4835 0.5005 0.0053 -0.0103 -0.0105 2410 HOH A O 3427 O O . HOH N . ? 0.3690 0.2992 0.3594 0.0399 0.0128 0.0075 2411 HOH A O 3428 O O . HOH N . ? 0.1974 0.3025 0.2872 0.0197 0.0175 0.0256 2412 HOH A O 3429 O O . HOH N . ? 0.3085 0.2995 0.2845 -0.0071 0.0095 0.0238 2413 HOH A O 3430 O O . HOH N . ? 0.0871 0.0878 0.0886 0.0008 0.0069 -0.0022 2414 HOH A O 3431 O O . HOH N . ? 0.1185 0.1060 0.1373 0.0141 0.0037 0.0062 2415 HOH A O 3432 O O . HOH N . ? 0.4549 0.3714 0.4016 0.0268 0.0078 -0.0482 2416 HOH A O 3433 O O . HOH N . ? 0.1296 0.1212 0.1415 0.0049 0.0071 -0.0141 2417 HOH A O 3434 O O . HOH N . ? 0.2791 0.2167 0.2207 -0.0282 -0.0497 -0.0403 2418 HOH A O 3435 O O . HOH N . ? 0.2030 0.2089 0.2629 -0.0319 -0.0037 0.0185 2419 HOH A O 3436 O O . HOH N . ? 0.2227 0.2070 0.3034 -0.0112 -0.0497 -0.0222 2420 HOH A O 3437 O O . HOH N . ? 0.5292 0.5285 0.4723 -0.0014 -0.0137 -0.0090 2421 HOH A O 3438 O O . HOH N . ? 0.1009 0.0957 0.1159 0.0070 0.0011 -0.0042 2422 HOH A O 3439 O O . HOH N . ? 0.1536 0.1375 0.1588 -0.0151 -0.0138 0.0035 2423 HOH A O 3440 O O . HOH N . ? 0.2088 0.1616 0.1694 -0.0097 -0.0259 -0.0187 2424 HOH A O 3441 O O . HOH N . ? 0.1416 0.1604 0.1262 0.0110 -0.0483 -0.0188 2425 HOH A O 3442 O O . HOH N . ? 0.1880 0.1992 0.3712 0.0165 0.0018 -0.0225 2426 HOH A O 3443 O O . HOH N . ? 0.1846 0.2106 0.2097 0.0100 0.0197 -0.0111 2427 HOH A O 3444 O O . HOH N . ? 0.1535 0.1282 0.1412 -0.0163 -0.0111 -0.0106 2428 HOH A O 3445 O O . HOH N . ? 0.2562 0.2783 0.2661 0.0167 0.0093 -0.0105 2429 HOH A O 3446 O O . HOH N . ? 0.4059 0.3080 0.3743 -0.0006 0.0109 -0.0833 2430 HOH A O 3447 O O . HOH N . ? 0.2319 0.2110 0.1850 -0.0132 -0.0745 -0.0026 2431 HOH A O 3448 O O . HOH N . ? 0.1832 0.1849 0.1650 0.0359 -0.0342 -0.0284 2432 HOH A O 3449 O O . HOH N . ? 0.2371 0.1566 0.2059 -0.0401 0.0197 0.0121 2433 HOH A O 3450 O O . HOH N . ? 0.2037 0.2574 0.2312 -0.0460 -0.0174 0.0034 2434 HOH A O 3451 O O . HOH N . ? 0.3785 0.3817 0.3887 -0.0235 -0.0290 0.0216 2435 HOH A O 3452 O O . HOH N . ? 0.4487 0.4865 0.5072 -0.0024 -0.0044 0.0209 2436 HOH A O 3453 O O . HOH N . ? 0.2114 0.2451 0.2788 -0.0184 -0.0017 0.0171 2437 HOH A O 3454 O O . HOH N . ? 0.3144 0.3455 0.3738 -0.0077 -0.0389 -0.0039 2438 HOH A O 3455 O O . HOH N . ? 0.2216 0.2447 0.2261 0.0102 0.0134 0.0253 2439 HOH A O 3456 O O . HOH N . ? 0.2573 0.2317 0.2546 -0.0427 -0.0211 -0.0372 2440 HOH A O 3457 O O . HOH N . ? 0.1495 0.1692 0.1714 0.0105 0.0104 0.0217 2441 HOH A O 3458 O O . HOH N . ? 0.2412 0.2573 0.2754 0.0122 -0.0705 0.0249 2442 HOH A O 3459 O O . HOH N . ? 0.2420 0.3350 0.3706 -0.0213 -0.0277 -0.0265 2443 HOH A O 3460 O O . HOH N . ? 0.1126 0.1112 0.1076 -0.0018 0.0021 -0.0069 2444 HOH A O 3461 O O . HOH N . ? 0.0832 0.0826 0.0793 0.0048 0.0017 -0.0039 2445 HOH A O 3462 O O . HOH N . ? 0.0823 0.0816 0.0813 -0.0001 0.0012 0.0062 2446 HOH A O 3463 O O . HOH N . ? 0.0813 0.0830 0.0806 0.0012 0.0003 -0.0001 2447 HOH A O 3464 O O . HOH N . ? 0.1549 0.1552 0.1885 0.0046 0.0151 -0.0220 2448 HOH A O 3465 O O . HOH N . ? 0.2718 0.2336 0.2048 -0.0057 -0.0585 0.0223 2449 HOH A O 3466 O O . HOH N . ? 0.1944 0.1933 0.2045 -0.0041 -0.0157 0.0169 2450 HOH A O 3467 O O . HOH N . ? 0.1943 0.1590 0.1688 0.0200 0.0076 -0.0181 2451 HOH A O 3468 O O . HOH N . ? 0.1609 0.1809 0.1708 -0.0047 0.0356 -0.0078 2452 HOH A O 3469 O O . HOH N . ? 0.1762 0.2045 0.1799 0.0106 0.0085 -0.0263 2453 HOH A O 3470 O O . HOH N . ? 0.1030 0.1086 0.0920 0.0007 0.0054 -0.0009 2454 HOH A O 3471 O O . HOH N . ? 0.1718 0.1663 0.1985 0.0252 -0.0238 -0.0003 2455 HOH A O 3472 O O . HOH N . ? 0.2462 0.2739 0.3128 0.0246 0.0102 -0.0085 2456 HOH A O 3473 O O . HOH N . ? 0.5944 0.5700 0.5741 -0.0096 0.0147 -0.0026 2457 HOH A O 3474 O O . HOH N . ? 0.1893 0.2282 0.2211 0.0055 -0.0026 -0.0066 2458 HOH A O 3475 O O . HOH N . ? 0.1688 0.1477 0.1377 0.0226 -0.0319 0.0046 2459 HOH A O 3476 O O . HOH N . ? 0.1283 0.1329 0.1369 0.0276 -0.0093 0.0032 2460 HOH A O 3477 O O . HOH N . ? 0.4071 0.3814 0.3691 0.0245 0.0469 0.0019 2461 HOH A O 3478 O O . HOH N . ? 0.1616 0.1486 0.1467 0.0338 0.0136 0.0237 2462 HOH A O 3479 O O . HOH N . ? 0.2171 0.2410 0.1587 -0.0285 0.0065 0.0258 2463 HOH A O 3480 O O . HOH N . ? 0.2891 0.2749 0.2479 0.0000 -0.0226 -0.0504 2464 HOH A O 3481 O O . HOH N . ? 0.2018 0.1865 0.1815 0.0149 0.0036 0.0185 2465 HOH A O 3482 O O . HOH N . ? 0.1061 0.1150 0.0991 0.0024 0.0096 -0.0026 2466 HOH A O 3483 O O . HOH N . ? 0.1657 0.1812 0.1447 0.0171 -0.0143 0.0140 2467 HOH A O 3484 O O . HOH N . ? 0.2157 0.2063 0.1806 -0.0219 0.0005 0.0311 2468 HOH A O 3485 O O . HOH N . ? 0.1542 0.2354 0.1620 -0.0115 -0.0090 -0.0452 2469 HOH A O 3486 O O . HOH N . ? 0.2313 0.1688 0.2287 0.0017 -0.0369 0.0159 2470 HOH A O 3487 O O . HOH N . ? 0.1367 0.1538 0.1194 0.0034 -0.0176 -0.0194 2471 HOH A O 3488 O O . HOH N . ? 0.1126 0.1050 0.1039 -0.0045 -0.0021 0.0076 2472 HOH A O 3489 O O . HOH N . ? 0.2600 0.2819 0.3518 0.0308 -0.0110 -0.0208 2473 HOH A O 3490 O O . HOH N . ? 0.3016 0.3292 0.2899 0.0202 0.0354 0.0064 2474 HOH A O 3491 O O . HOH N . ? 0.3452 0.3209 0.2780 -0.0487 -0.0648 0.0262 2475 HOH A O 3492 O O . HOH N . ? 0.3251 0.3041 0.3499 0.0073 -0.0150 0.0469 2476 HOH A O 3493 O O . HOH N . ? 0.1920 0.1866 0.2333 0.0005 0.0109 0.0018 2477 HOH A O 3494 O O . HOH N . ? 0.1781 0.1303 0.1837 0.0233 0.0082 0.0086 2478 HOH A O 3495 O O . HOH N . ? 0.2072 0.1887 0.1662 0.0188 -0.0157 -0.0242 2479 HOH A O 3496 O O . HOH N . ? 0.2233 0.2413 0.2600 -0.0162 -0.0234 -0.0197 2480 HOH A O 3497 O O . HOH N . ? 0.3453 0.3705 0.2922 -0.0313 0.0075 0.0228 2481 HOH A O 3498 O O . HOH N . ? 0.3876 0.2796 0.3931 0.0239 -0.0442 -0.0065 2482 HOH A O 3499 O O . HOH N . ? 0.5038 0.5106 0.4966 -0.0075 0.0235 0.0075 2483 HOH A O 3500 O O . HOH N . ? 0.1661 0.1711 0.1524 0.0142 -0.0171 -0.0193 2484 HOH A O 3501 O O . HOH N . ? 0.2509 0.3213 0.2367 -0.0080 0.0020 0.0194 2485 HOH A O 3502 O O . HOH N . ? 0.1769 0.1625 0.1913 0.0114 0.0214 -0.0273 2486 HOH A O 3503 O O . HOH N . ? 0.2001 0.1671 0.2007 -0.0129 0.0188 -0.0248 2487 HOH A O 3504 O O . HOH N . ? 0.1884 0.1701 0.3734 -0.0218 0.0399 -0.0496 2488 HOH A O 3505 O O . HOH N . ? 0.2519 0.2625 0.3017 0.0417 -0.0365 -0.0231 2489 HOH A O 3506 O O . HOH N . ? 0.3231 0.3176 0.2831 0.0019 -0.0312 -0.0098 2490 HOH A O 3507 O O . HOH N . ? 0.2290 0.3078 0.2784 -0.0482 -0.0229 0.0071 2491 HOH A O 3508 O O . HOH N . ? 0.1939 0.1938 0.1832 -0.0023 -0.0232 -0.0136 2492 HOH A O 3509 O O . HOH N . ? 0.0840 0.0869 0.0815 0.0032 -0.0010 0.0029 2493 HOH A O 3510 O O . HOH N . ? 0.3708 0.3921 0.3605 0.0107 0.0073 -0.0048 2494 HOH A O 3511 O O . HOH N . ? 0.1197 0.1002 0.1175 -0.0048 -0.0097 -0.0070 2495 HOH A O 3512 O O . HOH N . ? 0.1075 0.0997 0.1485 0.0150 -0.0128 0.0067 2496 HOH A O 3513 O O . HOH N . ? 0.1630 0.1229 0.1209 0.0186 0.0282 0.0108 2497 HOH A O 3514 O O . HOH N . ? 0.2318 0.2729 0.2379 0.0169 0.0321 0.0358 2498 HOH A O 3515 O O . HOH N . ? 0.2463 0.2499 0.2435 0.0236 0.0196 0.0109 2499 HOH A O 3516 O O . HOH N . ? 0.1330 0.1304 0.1499 0.0060 -0.0017 -0.0299 2500 HOH A O 3517 O O . HOH N . ? 0.1796 0.2233 0.1441 0.0019 -0.0095 -0.0025 2501 HOH A O 3518 O O . HOH N . ? 0.2499 0.2043 0.2632 -0.0291 -0.0165 -0.0151 2502 HOH A O 3519 O O . HOH N . ? 0.2364 0.2153 0.2653 0.0018 -0.0013 0.0106 2503 HOH A O 3520 O O . HOH N . ? 0.1244 0.1228 0.1205 0.0026 -0.0066 0.0056 2504 HOH A O 3521 O O . HOH N . ? 0.1761 0.2593 0.2621 -0.0126 0.0089 0.0165 2505 HOH A O 3522 O O . HOH N . ? 0.1998 0.2363 0.2625 -0.0103 -0.0231 -0.0202 2506 HOH A O 3523 O O . HOH N . ? 0.2777 0.3254 0.3645 -0.0101 0.0382 -0.0007 2507 HOH A O 3524 O O . HOH N . ? 0.1909 0.2018 0.2565 -0.0154 -0.0187 -0.0204 2508 HOH A O 3525 O O . HOH N . ? 0.2453 0.2707 0.2740 -0.0033 0.0245 0.0206 2509 HOH A O 3526 O O . HOH N . ? 0.2852 0.3536 0.3933 -0.0307 -0.0170 0.0174 2510 HOH A O 3527 O O . HOH N . ? 0.2194 0.2703 0.2381 0.0017 -0.0075 0.0222 2511 HOH A O 3528 O O . HOH N . ? 0.2796 0.3173 0.3164 0.0017 0.0696 0.0038 2512 HOH A O 3529 O O . HOH N . ? 0.3555 0.3452 0.3739 0.0056 -0.0125 0.0136 2513 HOH A O 3530 O O . HOH N . ? 0.4722 0.5160 0.5000 0.0148 -0.0219 0.0123 2514 HOH A O 3531 O O . HOH N . ? 0.3424 0.3702 0.4165 -0.0217 -0.0165 0.0076 2515 HOH A O 3532 O O . HOH N . ? 0.4562 0.4693 0.4602 0.0035 -0.0057 0.0006 2516 HOH A O 3533 O O . HOH N . ? 0.3438 0.3106 0.3733 -0.0367 -0.0291 -0.0333 2517 HOH A O 3534 O O . HOH N . ? 0.5157 0.5032 0.5048 0.0029 -0.0052 -0.0004 2518 HOH A O 3535 O O . HOH N . ? 0.1845 0.1755 0.1684 0.0151 -0.0238 -0.0060 2519 HOH A O 3536 O O . HOH N . ? 0.3172 0.3192 0.2902 -0.0031 0.0077 0.0182 2520 HOH A O 3537 O O . HOH N . ? 0.4019 0.4172 0.4278 -0.0189 -0.0081 0.0027 2521 HOH A O 3538 O O . HOH N . ? 0.2298 0.2225 0.1697 -0.0249 -0.0224 -0.0013 2522 HOH A O 3539 O O . HOH N . ? 0.2042 0.2173 0.2231 0.0541 -0.0189 -0.0275 2523 HOH A O 3540 O O . HOH N . ? 0.1642 0.1537 0.1376 0.0172 -0.0206 -0.0025 2524 HOH A O 3541 O O . HOH N . ? 0.1384 0.1432 0.1097 -0.0103 0.0154 -0.0066 2525 HOH A O 3542 O O . HOH N . ? 0.1391 0.1574 0.1831 0.0333 0.0083 -0.0160 2526 HOH A O 3543 O O . HOH N . ? 0.1437 0.1723 0.2164 0.0304 0.0278 0.0204 2527 HOH A O 3544 O O . HOH N . ? 0.2156 0.2504 0.2150 0.0024 0.0240 0.0695 2528 HOH A O 3545 O O . HOH N . ? 0.2166 0.1867 0.2610 -0.0193 -0.0129 0.0196 2529 HOH A O 3546 O O . HOH N . ? 0.0915 0.1004 0.0973 0.0032 -0.0018 0.0020 2530 HOH A O 3547 O O . HOH N . ? 0.2300 0.3004 0.3773 0.0091 0.0090 -0.0353 2531 HOH A O 3548 O O . HOH N . ? 0.3699 0.3357 0.3800 0.0571 -0.0051 0.0456 2532 HOH A O 3549 O O . HOH N . ? 0.1585 0.1426 0.1904 0.0185 0.0288 0.0125 2533 HOH A O 3550 O O . HOH N . ? 0.1724 0.1957 0.1639 0.0179 0.0037 0.0089 2534 HOH A O 3551 O O . HOH N . ? 0.2477 0.2784 0.2698 0.0040 0.0034 -0.0150 2535 HOH A O 3552 O O . HOH N . ? 0.3356 0.2737 0.2667 0.0382 0.0427 -0.0180 2536 HOH A O 3553 O O . HOH N . ? 0.3278 0.3331 0.3010 0.0184 0.0143 0.0090 2537 HOH A O 3554 O O . HOH N . ? 0.1031 0.1035 0.1070 0.0027 0.0045 0.0029 2538 HOH A O 3555 O O . HOH N . ? 0.2120 0.2134 0.2168 -0.0054 -0.0148 0.0088 2539 HOH A O 3556 O O . HOH N . ? 0.1894 0.2425 0.2381 0.0235 -0.0108 -0.0352 2540 HOH A O 3557 O O . HOH N . ? 0.1672 0.2066 0.1918 -0.0202 0.0034 0.0286 2541 HOH A O 3558 O O . HOH N . ? 0.2661 0.2833 0.3329 -0.0071 -0.0100 0.0024 2542 HOH A O 3559 O O . HOH N . ? 0.3290 0.3804 0.3780 -0.0026 0.0184 0.0021 2543 HOH A O 3560 O O . HOH N . ? 0.2063 0.2734 0.2868 -0.0639 -0.0338 -0.0038 2544 HOH A O 3561 O O . HOH N . ? 0.1821 0.1498 0.1302 0.0144 -0.0226 -0.0008 2545 HOH A O 3562 O O . HOH N . ? 0.2654 0.2254 0.2368 -0.0412 -0.0402 -0.0242 2546 HOH A O 3563 O O . HOH N . ? 0.3089 0.2813 0.2796 0.0372 -0.0087 0.0038 2547 HOH A O 3564 O O . HOH N . ? 0.2197 0.2371 0.2296 0.0161 0.0056 0.0177 2548 HOH A O 3565 O O . HOH N . ? 0.4278 0.4446 0.4710 -0.0083 -0.0099 -0.0216 2549 HOH A O 3566 O O . HOH N . ? 0.3371 0.3129 0.3215 -0.0084 -0.0141 0.0021 2550 HOH A O 3567 O O . HOH N . ? 0.2244 0.1953 0.2232 -0.0663 -0.0255 -0.0496 2551 HOH A O 3568 O O . HOH N . ? 0.1353 0.1656 0.1681 -0.0331 -0.0187 -0.0002 2552 HOH A O 3569 O O . HOH N . ? 0.2187 0.2201 0.2078 0.0102 0.0548 -0.0384 2553 HOH A O 3570 O O . HOH N . ? 0.1961 0.2730 0.2425 0.0038 0.0337 0.0205 2554 HOH A O 3571 O O . HOH N . ? 0.2386 0.2509 0.2194 -0.0005 -0.0188 -0.0215 2555 HOH A O 3572 O O . HOH N . ? 0.3172 0.3162 0.2669 0.0380 -0.0003 -0.0180 2556 HOH A O 3573 O O . HOH N . ? 0.1296 0.1905 0.1510 -0.0032 0.0096 -0.0061 2557 HOH A O 3574 O O . HOH N . ? 0.1716 0.2216 0.2074 -0.0007 -0.0063 0.0810 2558 HOH A O 3575 O O . HOH N . ? 0.1734 0.1910 0.1763 0.0421 -0.0137 -0.0322 2559 HOH A O 3576 O O . HOH N . ? 0.2900 0.2999 0.2087 0.0062 0.0193 0.0273 2560 HOH A O 3577 O O . HOH N . ? 0.1216 0.1115 0.1293 0.0058 0.0180 -0.0207 2561 HOH A O 3578 O O . HOH N . ? 0.1730 0.1880 0.2121 -0.0237 0.0411 -0.0399 2562 HOH A O 3579 O O . HOH N . ? 0.1303 0.1595 0.2558 -0.0132 0.0925 -0.0638 2563 HOH A O 3580 O O . HOH N . ? 0.3837 0.2757 0.2289 -0.0094 -0.0247 -0.0091 2564 HOH A O 3581 O O . HOH N . ? 0.1930 0.2865 0.1515 -0.0157 0.0143 0.0213 2565 HOH A O 3582 O O . HOH N . ? 0.4787 0.4230 0.3887 -0.0120 -0.0118 -0.0135 2566 HOH A O 3583 O O . HOH N . ? 0.4088 0.4103 0.3900 -0.0154 -0.0070 0.0015 2567 HOH A O 3584 O O . HOH N . ? 0.3954 0.3888 0.3929 -0.0171 -0.0108 -0.0222 2568 HOH A O 3585 O O . HOH N . ? 0.2244 0.2458 0.2592 0.0118 -0.0442 0.0296 2569 HOH A O 3586 O O . HOH N . ? 0.2802 0.2641 0.3133 -0.0117 -0.0200 -0.0066 2570 HOH A O 3587 O O . HOH N . ? 0.3237 0.2873 0.2775 0.0092 0.0132 0.0243 2571 HOH A O 3588 O O . HOH N . ? 0.3852 0.3460 0.3547 -0.0081 0.0075 -0.0196 2572 HOH A O 3589 O O . HOH N . ? 0.1591 0.1587 0.1764 -0.0173 -0.0081 -0.0055 2573 HOH A O 3590 O O . HOH N . ? 0.2210 0.1716 0.1761 -0.0113 0.0068 -0.0270 2574 HOH A O 3591 O O . HOH N . ? 0.2115 0.2266 0.1827 0.0236 0.0140 -0.0413 2575 HOH A O 3592 O O . HOH N . ? 0.2343 0.2184 0.2245 0.0282 0.0377 -0.0392 2576 HOH A O 3593 O O . HOH N . ? 0.2140 0.2548 0.2449 0.0032 0.0181 0.0136 2577 HOH A O 3594 O O . HOH N . ? 0.1501 0.1455 0.1631 0.0097 -0.0083 0.0054 2578 HOH A O 3595 O O . HOH N . ? 0.1576 0.1375 0.1953 0.0016 0.0073 0.0123 2579 HOH A O 3596 O O . HOH N . ? 0.3498 0.3707 0.3611 0.0109 0.0115 -0.0120 2580 HOH A O 3597 O O . HOH N . ? 0.1632 0.1538 0.1364 -0.0036 0.0042 0.0120 2581 HOH A O 3598 O O . HOH N . ? 0.2141 0.2988 0.3052 -0.0422 -0.0437 0.0443 2582 HOH A O 3599 O O . HOH N . ? 0.2360 0.2633 0.2231 -0.0822 -0.0043 -0.0229 2583 HOH A O 3600 O O . HOH N . ? 0.1610 0.1448 0.1331 -0.0065 0.0148 0.0063 2584 HOH A O 3601 O O . HOH N . ? 0.2576 0.2904 0.2163 -0.0023 0.0032 0.0233 2585 HOH A O 3602 O O . HOH N . ? 0.1253 0.1480 0.1718 0.0039 -0.0119 -0.0054 2586 HOH A O 3603 O O . HOH N . ? 0.2368 0.2320 0.2160 0.0212 -0.0390 -0.0365 2587 HOH A O 3604 O O . HOH N . ? 0.2701 0.2715 0.2566 -0.0055 0.0102 -0.0033 2588 HOH A O 3605 O O . HOH N . ? 0.2588 0.2868 0.2104 0.0372 -0.0190 -0.0207 2589 HOH A O 3606 O O . HOH N . ? 0.3072 0.3540 0.3425 0.0515 0.0424 0.0141 2590 HOH A O 3607 O O . HOH N . ? 0.1299 0.1249 0.1105 0.0009 -0.0021 0.0192 2591 HOH A O 3608 O O . HOH N . ? 0.2404 0.2758 0.2517 0.0102 0.0058 0.0057 2592 HOH A O 3609 O O . HOH N . ? 0.2787 0.2883 0.2623 0.0000 -0.0029 0.0275 2593 HOH A O 3610 O O . HOH N . ? 0.1415 0.1603 0.1640 0.0189 -0.0211 -0.0037 2594 HOH A O 3611 O O . HOH N . ? 0.0865 0.0712 0.0840 0.0239 0.0084 0.0045 2595 HOH A O 3612 O O . HOH N . ? 0.1434 0.1774 0.1803 0.0183 0.0056 0.0151 2596 HOH A O 3613 O O . HOH N . ? 0.1461 0.2094 0.1875 -0.0160 -0.0039 0.0203 2597 HOH A O 3614 O O . HOH N . ? 0.1061 0.1306 0.1154 -0.0014 -0.0075 0.0007 2598 HOH A O 3615 O O . HOH N . ? 0.1898 0.2534 0.2192 -0.0038 -0.0027 -0.0139 2599 HOH A O 3616 O O . HOH N . ? 0.2569 0.2882 0.2416 -0.0308 0.0292 0.0064 2600 HOH A O 3617 O O . HOH N . ? 0.3934 0.4199 0.4181 0.0187 -0.0001 -0.0081 2601 HOH A O 3618 O O . HOH N . ? 0.2693 0.2686 0.2944 0.0138 -0.0086 0.0007 2602 HOH A O 3619 O O . HOH N . ? 0.3065 0.2572 0.3473 -0.0101 0.0548 0.0026 2603 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 ALA 1 87 87 ALA ALA A . n A 1 2 PRO 2 88 88 PRO PRO A . n A 1 3 TYR 3 89 89 TYR TYR A . n A 1 4 ASN 4 90 90 ASN ASN A . n A 1 5 GLY 5 91 91 GLY GLY A . n A 1 6 ASN 6 92 92 ASN ASN A . n A 1 7 PRO 7 93 93 PRO PRO A . n A 1 8 PHE 8 94 94 PHE PHE A . n A 1 9 GLU 9 95 95 GLU GLU A . n A 1 10 GLY 10 96 96 GLY GLY A . n A 1 11 VAL 11 97 97 VAL VAL A . n A 1 12 GLN 12 98 98 GLN GLN A . n A 1 13 LEU 13 99 99 LEU LEU A . n A 1 14 TRP 14 100 100 TRP TRP A . n A 1 15 ALA 15 101 101 ALA ALA A . n A 1 16 ASN 16 102 102 ASN ASN A . n A 1 17 ASN 17 103 103 ASN ASN A . n A 1 18 TYR 18 104 104 TYR TYR A . n A 1 19 TYR 19 105 105 TYR TYR A . n A 1 20 ARG 20 106 106 ARG ARG A . n A 1 21 SER 21 107 107 SER SER A . n A 1 22 GLU 22 108 108 GLU GLU A . n A 1 23 VAL 23 109 109 VAL VAL A . n A 1 24 HIS 24 110 110 HIS HIS A . n A 1 25 THR 25 111 111 THR THR A . n A 1 26 LEU 26 112 112 LEU LEU A . n A 1 27 ALA 27 113 113 ALA ALA A . n A 1 28 ILE 28 114 114 ILE ILE A . n A 1 29 PRO 29 115 115 PRO PRO A . n A 1 30 GLN 30 116 116 GLN GLN A . n A 1 31 ILE 31 117 117 ILE ILE A . n A 1 32 THR 32 118 118 THR THR A . n A 1 33 ASP 33 119 119 ASP ASP A . n A 1 34 PRO 34 120 120 PRO PRO A . n A 1 35 ALA 35 121 121 ALA ALA A . n A 1 36 LEU 36 122 122 LEU LEU A . n A 1 37 ARG 37 123 123 ARG ARG A . n A 1 38 ALA 38 124 124 ALA ALA A . n A 1 39 ALA 39 125 125 ALA ALA A . n A 1 40 ALA 40 126 126 ALA ALA A . n A 1 41 SER 41 127 127 SER SER A . n A 1 42 ALA 42 128 128 ALA ALA A . n A 1 43 VAL 43 129 129 VAL VAL A . n A 1 44 ALA 44 130 130 ALA ALA A . n A 1 45 GLU 45 131 131 GLU GLU A . n A 1 46 VAL 46 132 132 VAL VAL A . n A 1 47 PRO 47 133 133 PRO PRO A . n A 1 48 SER 48 134 134 SER SER A . n A 1 49 PHE 49 135 135 PHE PHE A . n A 1 50 GLN 50 136 136 GLN GLN A . n A 1 51 TRP 51 137 137 TRP TRP A . n A 1 52 LEU 52 138 138 LEU LEU A . n A 1 53 ASP 53 139 139 ASP ASP A . n A 1 54 ARG 54 140 140 ARG ARG A . n A 1 55 ASN 55 141 141 ASN ASN A . n A 1 56 VAL 56 142 142 VAL VAL A . n A 1 57 THR 57 143 143 THR THR A . n A 1 58 VAL 58 144 144 VAL VAL A . n A 1 59 ASP 59 145 145 ASP ASP A . n A 1 60 THR 60 146 146 THR THR A . n A 1 61 LEU 61 147 147 LEU LEU A . n A 1 62 LEU 62 148 148 LEU LEU A . n A 1 63 VAL 63 149 149 VAL VAL A . n A 1 64 GLN 64 150 150 GLN GLN A . n A 1 65 THR 65 151 151 THR THR A . n A 1 66 LEU 66 152 152 LEU LEU A . n A 1 67 SER 67 153 153 SER SER A . n A 1 68 GLU 68 154 154 GLU GLU A . n A 1 69 ILE 69 155 155 ILE ILE A . n A 1 70 ARG 70 156 156 ARG ARG A . n A 1 71 GLU 71 157 157 GLU GLU A . n A 1 72 ALA 72 158 158 ALA ALA A . n A 1 73 ASN 73 159 159 ASN ASN A . n A 1 74 GLN 74 160 160 GLN GLN A . n A 1 75 ALA 75 161 161 ALA ALA A . n A 1 76 GLY 76 162 162 GLY GLY A . n A 1 77 ALA 77 163 163 ALA ALA A . n A 1 78 ASN 78 164 164 ASN ASN A . n A 1 79 PRO 79 165 165 PRO PRO A . n A 1 80 GLN 80 166 166 GLN GLN A . n A 1 81 TYR 81 167 167 TYR TYR A . n A 1 82 ALA 82 168 168 ALA ALA A . n A 1 83 ALA 83 169 169 ALA ALA A . n A 1 84 GLN 84 170 170 GLN GLN A . n A 1 85 ILE 85 171 171 ILE ILE A . n A 1 86 VAL 86 172 172 VAL VAL A . n A 1 87 VAL 87 173 173 VAL VAL A . n A 1 88 TYR 88 174 174 TYR TYR A . n A 1 89 ASP 89 175 175 ASP ASP A . n A 1 90 LEU 90 176 176 LEU LEU A . n A 1 91 PRO 91 177 177 PRO PRO A . n A 1 92 ASP 92 178 178 ASP ASP A . n A 1 93 ARG 93 179 179 ARG ARG A . n A 1 94 ASP 94 180 180 ASP ASP A . n A 1 95 CYS 95 181 181 CYS CYS A . n A 1 96 ALA 96 182 182 ALA ALA A . n A 1 97 ALA 97 183 183 ALA ALA A . n A 1 98 ALA 98 184 184 ALA ALA A . n A 1 99 ALA 99 185 185 ALA ALA A . n A 1 100 SER 100 186 186 SER SER A . n A 1 101 ASN 101 187 187 ASN ASN A . n A 1 102 GLY 102 188 188 GLY GLY A . n A 1 103 GLU 103 189 189 GLU GLU A . n A 1 104 TRP 104 190 190 TRP TRP A . n A 1 105 ALA 105 191 191 ALA ALA A . n A 1 106 ILE 106 192 192 ILE ILE A . n A 1 107 ALA 107 193 193 ALA ALA A . n A 1 108 ASN 108 194 194 ASN ASN A . n A 1 109 ASN 109 195 195 ASN ASN A . n A 1 110 GLY 110 196 196 GLY GLY A . n A 1 111 VAL 111 197 197 VAL VAL A . n A 1 112 ASN 112 198 198 ASN ASN A . n A 1 113 ASN 113 199 199 ASN ASN A . n A 1 114 TYR 114 200 200 TYR TYR A . n A 1 115 LYS 115 201 201 LYS LYS A . n A 1 116 ALA 116 202 202 ALA ALA A . n A 1 117 TYR 117 203 203 TYR TYR A . n A 1 118 ILE 118 204 204 ILE ILE A . n A 1 119 ASN 119 205 205 ASN ASN A . n A 1 120 ARG 120 206 206 ARG ARG A . n A 1 121 ILE 121 207 207 ILE ILE A . n A 1 122 ARG 122 208 208 ARG ARG A . n A 1 123 GLU 123 209 209 GLU GLU A . n A 1 124 ILE 124 210 210 ILE ILE A . n A 1 125 LEU 125 211 211 LEU LEU A . n A 1 126 ILE 126 212 212 ILE ILE A . n A 1 127 SER 127 213 213 SER SER A . n A 1 128 PHE 128 214 214 PHE PHE A . n A 1 129 SER 129 215 215 SER SER A . n A 1 130 ASP 130 216 216 ASP ASP A . n A 1 131 VAL 131 217 217 VAL VAL A . n A 1 132 ARG 132 218 218 ARG ARG A . n A 1 133 THR 133 219 219 THR THR A . n A 1 134 ILE 134 220 220 ILE ILE A . n A 1 135 LEU 135 221 221 LEU LEU A . n A 1 136 VAL 136 222 222 VAL VAL A . n A 1 137 ILE 137 223 223 ILE ILE A . n A 1 138 GLU 138 224 224 GLU GLU A . n A 1 139 PRO 139 225 225 PRO PRO A . n A 1 140 ASP 140 226 226 ASP ASP A . n A 1 141 SER 141 227 227 SER SER A . n A 1 142 LEU 142 228 228 LEU LEU A . n A 1 143 ALA 143 229 229 ALA ALA A . n A 1 144 ASN 144 230 230 ASN ASN A . n A 1 145 MET 145 231 231 MET MET A . n A 1 146 VAL 146 232 232 VAL VAL A . n A 1 147 THR 147 233 233 THR THR A . n A 1 148 ASN 148 234 234 ASN ASN A . n A 1 149 MET 149 235 235 MET MET A . n A 1 150 ASN 150 236 236 ASN ASN A . n A 1 151 VAL 151 237 237 VAL VAL A . n A 1 152 PRO 152 238 238 PRO PRO A . n A 1 153 LYS 153 239 239 LYS LYS A . n A 1 154 CYS 154 240 240 CYS CYS A . n A 1 155 SER 155 241 241 SER SER A . n A 1 156 GLY 156 242 242 GLY GLY A . n A 1 157 ALA 157 243 243 ALA ALA A . n A 1 158 ALA 158 244 244 ALA ALA A . n A 1 159 SER 159 245 245 SER SER A . n A 1 160 THR 160 246 246 THR THR A . n A 1 161 TYR 161 247 247 TYR TYR A . n A 1 162 ARG 162 248 248 ARG ARG A . n A 1 163 GLU 163 249 249 GLU GLU A . n A 1 164 LEU 164 250 250 LEU LEU A . n A 1 165 THR 165 251 251 THR THR A . n A 1 166 ILE 166 252 252 ILE ILE A . n A 1 167 TYR 167 253 253 TYR TYR A . n A 1 168 ALA 168 254 254 ALA ALA A . n A 1 169 LEU 169 255 255 LEU LEU A . n A 1 170 LYS 170 256 256 LYS LYS A . n A 1 171 GLN 171 257 257 GLN GLN A . n A 1 172 LEU 172 258 258 LEU LEU A . n A 1 173 ASP 173 259 259 ASP ASP A . n A 1 174 LEU 174 260 260 LEU LEU A . n A 1 175 PRO 175 261 261 PRO PRO A . n A 1 176 HIS 176 262 262 HIS HIS A . n A 1 177 VAL 177 263 263 VAL VAL A . n A 1 178 ALA 178 264 264 ALA ALA A . n A 1 179 MET 179 265 265 MET MET A . n A 1 180 TYR 180 266 266 TYR TYR A . n A 1 181 MET 181 267 267 MET MET A . n A 1 182 ASP 182 268 268 ASP ASP A . n A 1 183 ALA 183 269 269 ALA ALA A . n A 1 184 GLY 184 270 270 GLY GLY A . n A 1 185 HIS 185 271 271 HIS HIS A . n A 1 186 ALA 186 272 272 ALA ALA A . n A 1 187 GLY 187 273 273 GLY GLY A . n A 1 188 TRP 188 274 274 TRP TRP A . n A 1 189 LEU 189 275 275 LEU LEU A . n A 1 190 GLY 190 276 276 GLY GLY A . n A 1 191 TRP 191 277 277 TRP TRP A . n A 1 192 PRO 192 278 278 PRO PRO A . n A 1 193 ALA 193 279 279 ALA ALA A . n A 1 194 ASN 194 280 280 ASN ASN A . n A 1 195 ILE 195 281 281 ILE ILE A . n A 1 196 GLN 196 282 282 GLN GLN A . n A 1 197 PRO 197 283 283 PRO PRO A . n A 1 198 ALA 198 284 284 ALA ALA A . n A 1 199 ALA 199 285 285 ALA ALA A . n A 1 200 GLU 200 286 286 GLU GLU A . n A 1 201 LEU 201 287 287 LEU LEU A . n A 1 202 PHE 202 288 288 PHE PHE A . n A 1 203 ALA 203 289 289 ALA ALA A . n A 1 204 LYS 204 290 290 LYS LYS A . n A 1 205 ILE 205 291 291 ILE ILE A . n A 1 206 TYR 206 292 292 TYR TYR A . n A 1 207 GLU 207 293 293 GLU GLU A . n A 1 208 ASP 208 294 294 ASP ASP A . n A 1 209 ALA 209 295 295 ALA ALA A . n A 1 210 GLY 210 296 296 GLY GLY A . n A 1 211 LYS 211 297 297 LYS LYS A . n A 1 212 PRO 212 298 298 PRO PRO A . n A 1 213 ARG 213 299 299 ARG ARG A . n A 1 214 ALA 214 300 300 ALA ALA A . n A 1 215 VAL 215 301 301 VAL VAL A . n A 1 216 ARG 216 302 302 ARG ARG A . n A 1 217 GLY 217 303 303 GLY GLY A . n A 1 218 LEU 218 304 304 LEU LEU A . n A 1 219 ALA 219 305 305 ALA ALA A . n A 1 220 THR 220 306 306 THR THR A . n A 1 221 ASN 221 307 307 ASN ASN A . n A 1 222 VAL 222 308 308 VAL VAL A . n A 1 223 ALA 223 309 309 ALA ALA A . n A 1 224 ASN 224 310 310 ASN ASN A . n A 1 225 TYR 225 311 311 TYR TYR A . n A 1 226 ASN 226 312 312 ASN ASN A . n A 1 227 ALA 227 313 313 ALA ALA A . n A 1 228 TRP 228 314 314 TRP TRP A . n A 1 229 SER 229 315 315 SER SER A . n A 1 230 VAL 230 316 316 VAL VAL A . n A 1 231 SER 231 317 317 SER SER A . n A 1 232 SER 232 318 318 SER SER A . n A 1 233 PRO 233 319 319 PRO PRO A . n A 1 234 PRO 234 320 320 PRO PRO A . n A 1 235 PRO 235 321 321 PRO PRO A . n A 1 236 TYR 236 322 322 TYR TYR A . n A 1 237 THR 237 323 323 THR THR A . n A 1 238 SER 238 324 324 SER SER A . n A 1 239 PRO 239 325 325 PRO PRO A . n A 1 240 ASN 240 326 326 ASN ASN A . n A 1 241 PRO 241 327 327 PRO PRO A . n A 1 242 ASN 242 328 328 ASN ASN A . n A 1 243 TYR 243 329 329 TYR TYR A . n A 1 244 ASP 244 330 330 ASP ASP A . n A 1 245 GLU 245 331 331 GLU GLU A . n A 1 246 LYS 246 332 332 LYS LYS A . n A 1 247 HIS 247 333 333 HIS HIS A . n A 1 248 TYR 248 334 334 TYR TYR A . n A 1 249 ILE 249 335 335 ILE ILE A . n A 1 250 GLU 250 336 336 GLU GLU A . n A 1 251 ALA 251 337 337 ALA ALA A . n A 1 252 PHE 252 338 338 PHE PHE A . n A 1 253 ARG 253 339 339 ARG ARG A . n A 1 254 PRO 254 340 340 PRO PRO A . n A 1 255 LEU 255 341 341 LEU LEU A . n A 1 256 LEU 256 342 342 LEU LEU A . n A 1 257 GLU 257 343 343 GLU GLU A . n A 1 258 ALA 258 344 344 ALA ALA A . n A 1 259 ARG 259 345 345 ARG ARG A . n A 1 260 GLY 260 346 346 GLY GLY A . n A 1 261 PHE 261 347 347 PHE PHE A . n A 1 262 PRO 262 348 348 PRO PRO A . n A 1 263 ALA 263 349 349 ALA ALA A . n A 1 264 GLN 264 350 350 GLN GLN A . n A 1 265 PHE 265 351 351 PHE PHE A . n A 1 266 ILE 266 352 352 ILE ILE A . n A 1 267 VAL 267 353 353 VAL VAL A . n A 1 268 ASP 268 354 354 ASP ASP A . n A 1 269 GLN 269 355 355 GLN GLN A . n A 1 270 GLY 270 356 356 GLY GLY A . n A 1 271 ARG 271 357 357 ARG ARG A . n A 1 272 SER 272 358 358 SER SER A . n A 1 273 GLY 273 359 359 GLY GLY A . n A 1 274 LYS 274 360 360 LYS LYS A . n A 1 275 GLN 275 361 361 GLN GLN A . n A 1 276 PRO 276 362 362 PRO PRO A . n A 1 277 THR 277 363 363 THR THR A . n A 1 278 GLY 278 364 364 GLY GLY A . n A 1 279 GLN 279 365 365 GLN GLN A . n A 1 280 LYS 280 366 366 LYS LYS A . n A 1 281 GLU 281 367 367 GLU GLU A . n A 1 282 TRP 282 368 368 TRP TRP A . n A 1 283 GLY 283 369 369 GLY GLY A . n A 1 284 HIS 284 370 370 HIS HIS A . n A 1 285 TRP 285 371 371 TRP TRP A . n A 1 286 CYS 286 372 372 CYS CYS A . n A 1 287 ASN 287 373 373 ASN ASN A . n A 1 288 ALA 288 374 374 ALA ALA A . n A 1 289 ILE 289 375 375 ILE ILE A . n A 1 290 GLY 290 376 376 GLY GLY A . n A 1 291 THR 291 377 377 THR THR A . n A 1 292 GLY 292 378 378 GLY GLY A . n A 1 293 PHE 293 379 379 PHE PHE A . n A 1 294 GLY 294 380 380 GLY GLY A . n A 1 295 MET 295 381 381 MET MET A . n A 1 296 ARG 296 382 382 ARG ARG A . n A 1 297 PRO 297 383 383 PRO PRO A . n A 1 298 THR 298 384 384 THR THR A . n A 1 299 ALA 299 385 385 ALA ALA A . n A 1 300 ASN 300 386 386 ASN ASN A . n A 1 301 THR 301 387 387 THR THR A . n A 1 302 GLY 302 388 388 GLY GLY A . n A 1 303 HIS 303 389 389 HIS HIS A . n A 1 304 GLN 304 390 390 GLN GLN A . n A 1 305 TYR 305 391 391 TYR TYR A . n A 1 306 VAL 306 392 392 VAL VAL A . n A 1 307 ASP 307 393 393 ASP ASP A . n A 1 308 ALA 308 394 394 ALA ALA A . n A 1 309 PHE 309 395 395 PHE PHE A . n A 1 310 VAL 310 396 396 VAL VAL A . n A 1 311 TRP 311 397 397 TRP TRP A . n A 1 312 VAL 312 398 398 VAL VAL A . n A 1 313 LYS 313 399 399 LYS LYS A . n A 1 314 PRO 314 400 400 PRO PRO A . n A 1 315 GLY 315 401 401 GLY GLY A . n A 1 316 GLY 316 402 402 GLY GLY A . n A 1 317 GLU 317 403 403 GLU GLU A . n A 1 318 CYS 318 404 404 CYS CYS A . n A 1 319 ASN 319 405 405 ASN ASN A . n A 1 320 GLY 320 406 406 GLY GLY A . n A 1 321 THR 321 407 407 THR THR A . n A 1 322 SER 322 408 408 SER SER A . n A 1 323 ASP 323 409 409 ASP ASP A . n A 1 324 THR 324 410 410 THR THR A . n A 1 325 THR 325 411 411 THR THR A . n A 1 326 ALA 326 412 412 ALA ALA A . n A 1 327 ALA 327 413 413 ALA ALA A . n A 1 328 ARG 328 414 414 ARG ARG A . n A 1 329 TYR 329 415 415 TYR TYR A . n A 1 330 ASP 330 416 416 ASP ASP A . n A 1 331 TYR 331 417 417 TYR TYR A . n A 1 332 HIS 332 418 418 HIS HIS A . n A 1 333 CYS 333 419 419 CYS CYS A . n A 1 334 GLY 334 420 420 GLY GLY A . n A 1 335 LEU 335 421 421 LEU LEU A . n A 1 336 GLU 336 422 422 GLU GLU A . n A 1 337 ASP 337 423 423 ASP ASP A . n A 1 338 ALA 338 424 424 ALA ALA A . n A 1 339 LEU 339 425 425 LEU LEU A . n A 1 340 LYS 340 426 426 LYS LYS A . n A 1 341 PRO 341 427 427 PRO PRO A . n A 1 342 ALA 342 428 428 ALA ALA A . n A 1 343 PRO 343 429 429 PRO PRO A . n A 1 344 GLU 344 430 430 GLU GLU A . n A 1 345 ALA 345 431 431 ALA ALA A . n A 1 346 GLY 346 432 432 GLY GLY A . n A 1 347 GLN 347 433 433 GLN GLN A . n A 1 348 TRP 348 434 434 TRP TRP A . n A 1 349 PHE 349 435 435 PHE PHE A . n A 1 350 ASN 350 436 436 ASN ASN A . n A 1 351 GLU 351 437 437 GLU GLU A . n A 1 352 TYR 352 438 438 TYR TYR A . n A 1 353 PHE 353 439 439 PHE PHE A . n A 1 354 ILE 354 440 440 ILE ILE A . n A 1 355 GLN 355 441 441 GLN GLN A . n A 1 356 LEU 356 442 442 LEU LEU A . n A 1 357 LEU 357 443 443 LEU LEU A . n A 1 358 ARG 358 444 444 ARG ARG A . n A 1 359 ASN 359 445 445 ASN ASN A . n A 1 360 ALA 360 446 446 ALA ALA A . n A 1 361 ASN 361 447 447 ASN ASN A . n A 1 362 PRO 362 448 448 PRO PRO A . n A 1 363 PRO 363 449 449 PRO PRO A . n A 1 364 PHE 364 450 450 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 MG 1 501 501 MG MG A . D 4 ACT 1 502 502 ACT ACT A . E 5 DMF 1 503 503 DMF DMF A . F 5 DMF 1 504 504 DMF DMF A . G 6 GOL 1 505 505 GOL GOL A . H 6 GOL 1 506 506 GOL GOL A . I 7 BGC 1 601 601 BGC BGC A . J 8 SGC 2 602 602 SGC SGC A . K 8 SGC 3 603 603 SGC SGC A . L 8 SGC 4 604 604 SGC SGC A . M 9 MA3 5 605 605 MA3 MA3 A . N 10 HOH 1 2001 2001 HOH HOH A . N 10 HOH 2 2002 2002 HOH HOH A . N 10 HOH 3 2003 2003 HOH HOH A . N 10 HOH 4 2004 2004 HOH HOH A . N 10 HOH 5 2005 2005 HOH HOH A . N 10 HOH 6 2006 2006 HOH HOH A . N 10 HOH 7 2007 2007 HOH HOH A . N 10 HOH 8 2008 2008 HOH HOH A . N 10 HOH 9 2009 2009 HOH HOH A . N 10 HOH 10 2010 2010 HOH HOH A . N 10 HOH 11 2011 2011 HOH HOH A . N 10 HOH 12 2012 2012 HOH HOH A . N 10 HOH 13 2013 2013 HOH HOH A . N 10 HOH 14 2014 2014 HOH HOH A . N 10 HOH 15 2015 2015 HOH HOH A . N 10 HOH 16 2016 2016 HOH HOH A . N 10 HOH 17 2017 2017 HOH HOH A . N 10 HOH 18 2018 2018 HOH HOH A . N 10 HOH 19 2019 2019 HOH HOH A . N 10 HOH 20 2020 2020 HOH HOH A . N 10 HOH 21 2021 2021 HOH HOH A . N 10 HOH 22 2022 2022 HOH HOH A . N 10 HOH 23 2023 2023 HOH HOH A . N 10 HOH 24 2024 2024 HOH HOH A . N 10 HOH 25 2025 2025 HOH HOH A . N 10 HOH 26 2026 2026 HOH HOH A . N 10 HOH 27 2027 2027 HOH HOH A . N 10 HOH 28 2028 2028 HOH HOH A . N 10 HOH 29 2029 2029 HOH HOH A . N 10 HOH 30 2030 2030 HOH HOH A . N 10 HOH 31 2031 2031 HOH HOH A . N 10 HOH 32 2032 2032 HOH HOH A . N 10 HOH 33 2033 2033 HOH HOH A . N 10 HOH 34 2034 2034 HOH HOH A . N 10 HOH 35 2035 2035 HOH HOH A . N 10 HOH 36 2036 2036 HOH HOH A . N 10 HOH 37 2037 2037 HOH HOH A . N 10 HOH 38 2038 2038 HOH HOH A . N 10 HOH 39 2039 2039 HOH HOH A . N 10 HOH 40 2040 2040 HOH HOH A . N 10 HOH 41 2041 2041 HOH HOH A . N 10 HOH 42 2042 2042 HOH HOH A . N 10 HOH 43 2043 2043 HOH HOH A . N 10 HOH 44 2044 2044 HOH HOH A . N 10 HOH 45 2045 2045 HOH HOH A . N 10 HOH 46 2046 2046 HOH HOH A . N 10 HOH 47 2047 2047 HOH HOH A . N 10 HOH 48 2048 2048 HOH HOH A . N 10 HOH 49 2049 2049 HOH HOH A . N 10 HOH 50 2050 2050 HOH HOH A . N 10 HOH 51 2051 2051 HOH HOH A . N 10 HOH 52 2052 2052 HOH HOH A . N 10 HOH 53 2053 2053 HOH HOH A . N 10 HOH 54 2054 2054 HOH HOH A . N 10 HOH 55 2055 2055 HOH HOH A . N 10 HOH 56 2056 2056 HOH HOH A . N 10 HOH 57 2057 2057 HOH HOH A . N 10 HOH 58 2058 2058 HOH HOH A . N 10 HOH 59 2059 2059 HOH HOH A . N 10 HOH 60 2060 2060 HOH HOH A . N 10 HOH 61 2061 2061 HOH HOH A . N 10 HOH 62 2062 2062 HOH HOH A . N 10 HOH 63 2063 2063 HOH HOH A . N 10 HOH 64 2064 2064 HOH HOH A . N 10 HOH 65 2065 2065 HOH HOH A . N 10 HOH 66 2066 2066 HOH HOH A . N 10 HOH 67 2067 2067 HOH HOH A . N 10 HOH 68 2068 2068 HOH HOH A . N 10 HOH 69 2069 2069 HOH HOH A . N 10 HOH 70 2070 2070 HOH HOH A . N 10 HOH 71 2071 2071 HOH HOH A . N 10 HOH 72 2072 2072 HOH HOH A . N 10 HOH 73 2073 2073 HOH HOH A . N 10 HOH 74 2074 2074 HOH HOH A . N 10 HOH 75 2075 2075 HOH HOH A . N 10 HOH 76 2076 2076 HOH HOH A . N 10 HOH 77 2077 2077 HOH HOH A . N 10 HOH 78 2078 2078 HOH HOH A . N 10 HOH 79 2079 2079 HOH HOH A . N 10 HOH 80 2080 2080 HOH HOH A . N 10 HOH 81 2081 2081 HOH HOH A . N 10 HOH 82 2082 2082 HOH HOH A . N 10 HOH 83 2083 2083 HOH HOH A . N 10 HOH 84 2084 2084 HOH HOH A . N 10 HOH 85 2085 2085 HOH HOH A . N 10 HOH 86 2086 2086 HOH HOH A . N 10 HOH 87 2087 2087 HOH HOH A . N 10 HOH 88 2088 2088 HOH HOH A . N 10 HOH 89 2089 2089 HOH HOH A . N 10 HOH 90 2090 2090 HOH HOH A . N 10 HOH 91 2091 2091 HOH HOH A . N 10 HOH 92 2092 2092 HOH HOH A . N 10 HOH 93 2093 2093 HOH HOH A . N 10 HOH 94 2094 2094 HOH HOH A . N 10 HOH 95 2095 2095 HOH HOH A . N 10 HOH 96 2096 2096 HOH HOH A . N 10 HOH 97 2097 2097 HOH HOH A . N 10 HOH 98 2098 2098 HOH HOH A . N 10 HOH 99 2099 2099 HOH HOH A . N 10 HOH 100 2100 2100 HOH HOH A . N 10 HOH 101 2101 2101 HOH HOH A . N 10 HOH 102 2102 2102 HOH HOH A . N 10 HOH 103 2103 2103 HOH HOH A . N 10 HOH 104 2104 2104 HOH HOH A . N 10 HOH 105 2105 2105 HOH HOH A . N 10 HOH 106 2106 2106 HOH HOH A . N 10 HOH 107 2107 2107 HOH HOH A . N 10 HOH 108 2108 2108 HOH HOH A . N 10 HOH 109 2109 2109 HOH HOH A . N 10 HOH 110 2110 2110 HOH HOH A . N 10 HOH 111 2111 2111 HOH HOH A . N 10 HOH 112 2112 2112 HOH HOH A . N 10 HOH 113 2113 2113 HOH HOH A . N 10 HOH 114 2114 2114 HOH HOH A . N 10 HOH 115 2115 2115 HOH HOH A . N 10 HOH 116 2116 2116 HOH HOH A . N 10 HOH 117 2117 2117 HOH HOH A . N 10 HOH 118 2118 2118 HOH HOH A . N 10 HOH 119 2119 2119 HOH HOH A . N 10 HOH 120 2120 2120 HOH HOH A . N 10 HOH 121 2121 2121 HOH HOH A . N 10 HOH 122 2122 2122 HOH HOH A . N 10 HOH 123 2123 2123 HOH HOH A . N 10 HOH 124 2124 2124 HOH HOH A . N 10 HOH 125 2125 2125 HOH HOH A . N 10 HOH 126 2126 2126 HOH HOH A . N 10 HOH 127 2127 2127 HOH HOH A . N 10 HOH 128 2128 2128 HOH HOH A . N 10 HOH 129 2129 2129 HOH HOH A . N 10 HOH 130 2130 2130 HOH HOH A . N 10 HOH 131 2131 2131 HOH HOH A . N 10 HOH 132 2132 2132 HOH HOH A . N 10 HOH 133 2133 2133 HOH HOH A . N 10 HOH 134 2134 2134 HOH HOH A . N 10 HOH 135 2135 2135 HOH HOH A . N 10 HOH 136 2136 2136 HOH HOH A . N 10 HOH 137 2137 2137 HOH HOH A . N 10 HOH 138 2138 2138 HOH HOH A . N 10 HOH 139 2139 2139 HOH HOH A . N 10 HOH 140 2140 2140 HOH HOH A . N 10 HOH 141 2141 2141 HOH HOH A . N 10 HOH 142 2142 2142 HOH HOH A . N 10 HOH 143 2143 2143 HOH HOH A . N 10 HOH 144 2144 2144 HOH HOH A . N 10 HOH 145 2145 2145 HOH HOH A . N 10 HOH 146 2146 2146 HOH HOH A . N 10 HOH 147 2147 2147 HOH HOH A . N 10 HOH 148 2148 2148 HOH HOH A . N 10 HOH 149 2149 2149 HOH HOH A . N 10 HOH 150 2150 2150 HOH HOH A . N 10 HOH 151 2151 2151 HOH HOH A . N 10 HOH 152 2152 2152 HOH HOH A . N 10 HOH 153 2153 2153 HOH HOH A . N 10 HOH 154 2154 2154 HOH HOH A . N 10 HOH 155 2155 2155 HOH HOH A . N 10 HOH 156 2156 2156 HOH HOH A . N 10 HOH 157 2157 2157 HOH HOH A . N 10 HOH 158 2158 2158 HOH HOH A . N 10 HOH 159 2159 2159 HOH HOH A . N 10 HOH 160 2160 2160 HOH HOH A . N 10 HOH 161 2161 2161 HOH HOH A . N 10 HOH 162 2162 2162 HOH HOH A . N 10 HOH 163 2163 2163 HOH HOH A . N 10 HOH 164 2164 2164 HOH HOH A . N 10 HOH 165 2165 2165 HOH HOH A . N 10 HOH 166 2166 2166 HOH HOH A . N 10 HOH 167 2167 2167 HOH HOH A . N 10 HOH 168 2168 2168 HOH HOH A . N 10 HOH 169 2169 2169 HOH HOH A . N 10 HOH 170 2170 2170 HOH HOH A . N 10 HOH 171 2171 2171 HOH HOH A . N 10 HOH 172 2172 2172 HOH HOH A . N 10 HOH 173 2173 2173 HOH HOH A . N 10 HOH 174 2174 2174 HOH HOH A . N 10 HOH 175 2175 2175 HOH HOH A . N 10 HOH 176 2176 2176 HOH HOH A . N 10 HOH 177 2177 2177 HOH HOH A . N 10 HOH 178 2178 2178 HOH HOH A . N 10 HOH 179 2179 2179 HOH HOH A . N 10 HOH 180 2180 2180 HOH HOH A . N 10 HOH 181 2181 2181 HOH HOH A . N 10 HOH 182 2182 2182 HOH HOH A . N 10 HOH 183 2183 2183 HOH HOH A . N 10 HOH 184 2184 2184 HOH HOH A . N 10 HOH 185 2185 2185 HOH HOH A . N 10 HOH 186 2186 2186 HOH HOH A . N 10 HOH 187 2187 2187 HOH HOH A . N 10 HOH 188 2188 2188 HOH HOH A . N 10 HOH 189 2189 2189 HOH HOH A . N 10 HOH 190 2190 2190 HOH HOH A . N 10 HOH 191 2191 2191 HOH HOH A . N 10 HOH 192 2192 2192 HOH HOH A . N 10 HOH 193 2193 2193 HOH HOH A . N 10 HOH 194 2194 2194 HOH HOH A . N 10 HOH 195 2195 2195 HOH HOH A . N 10 HOH 196 2196 2196 HOH HOH A . N 10 HOH 197 2197 2197 HOH HOH A . N 10 HOH 198 2198 2198 HOH HOH A . N 10 HOH 199 2199 2199 HOH HOH A . N 10 HOH 200 2200 2200 HOH HOH A . N 10 HOH 201 2201 2201 HOH HOH A . N 10 HOH 202 2202 2202 HOH HOH A . N 10 HOH 203 2203 2203 HOH HOH A . N 10 HOH 204 2204 2204 HOH HOH A . N 10 HOH 205 2205 2205 HOH HOH A . N 10 HOH 206 2206 2206 HOH HOH A . N 10 HOH 207 2207 2207 HOH HOH A . N 10 HOH 208 2208 2208 HOH HOH A . N 10 HOH 209 2209 2209 HOH HOH A . N 10 HOH 210 2210 2210 HOH HOH A . N 10 HOH 211 2211 2211 HOH HOH A . N 10 HOH 212 2212 2212 HOH HOH A . N 10 HOH 213 2213 2213 HOH HOH A . N 10 HOH 214 2214 2214 HOH HOH A . N 10 HOH 215 2215 2215 HOH HOH A . N 10 HOH 216 2216 2216 HOH HOH A . N 10 HOH 217 2217 2217 HOH HOH A . N 10 HOH 218 2218 2218 HOH HOH A . N 10 HOH 219 2219 2219 HOH HOH A . N 10 HOH 220 2220 2220 HOH HOH A . N 10 HOH 221 2221 2221 HOH HOH A . N 10 HOH 222 2222 2222 HOH HOH A . N 10 HOH 223 2223 2223 HOH HOH A . N 10 HOH 224 2224 2224 HOH HOH A . N 10 HOH 225 2225 2225 HOH HOH A . N 10 HOH 226 2226 2226 HOH HOH A . N 10 HOH 227 2227 2227 HOH HOH A . N 10 HOH 228 2228 2228 HOH HOH A . N 10 HOH 229 2229 2229 HOH HOH A . N 10 HOH 230 2230 2230 HOH HOH A . N 10 HOH 231 2231 2231 HOH HOH A . N 10 HOH 232 2232 2232 HOH HOH A . N 10 HOH 233 2233 2233 HOH HOH A . N 10 HOH 234 2234 2234 HOH HOH A . N 10 HOH 235 2235 2235 HOH HOH A . N 10 HOH 236 2236 2236 HOH HOH A . N 10 HOH 237 2237 2237 HOH HOH A . N 10 HOH 238 2238 2238 HOH HOH A . N 10 HOH 239 2239 2239 HOH HOH A . N 10 HOH 240 2240 2240 HOH HOH A . N 10 HOH 241 2241 2241 HOH HOH A . N 10 HOH 242 2242 2242 HOH HOH A . N 10 HOH 243 2243 2243 HOH HOH A . N 10 HOH 244 2244 2244 HOH HOH A . N 10 HOH 245 2245 2245 HOH HOH A . N 10 HOH 246 2246 2246 HOH HOH A . N 10 HOH 247 2247 2247 HOH HOH A . N 10 HOH 248 2248 2248 HOH HOH A . N 10 HOH 249 2249 2249 HOH HOH A . N 10 HOH 250 2250 2250 HOH HOH A . N 10 HOH 251 2251 2251 HOH HOH A . N 10 HOH 252 2252 2252 HOH HOH A . N 10 HOH 253 2253 2253 HOH HOH A . N 10 HOH 254 2254 2254 HOH HOH A . N 10 HOH 255 2255 2255 HOH HOH A . N 10 HOH 256 2256 2256 HOH HOH A . N 10 HOH 257 2257 2257 HOH HOH A . N 10 HOH 258 2258 2258 HOH HOH A . N 10 HOH 259 2259 2259 HOH HOH A . N 10 HOH 260 2260 2260 HOH HOH A . N 10 HOH 261 2261 2261 HOH HOH A . N 10 HOH 262 2262 2262 HOH HOH A . N 10 HOH 263 2263 2263 HOH HOH A . N 10 HOH 264 2264 2264 HOH HOH A . N 10 HOH 265 2265 2265 HOH HOH A . N 10 HOH 266 2266 2266 HOH HOH A . N 10 HOH 267 2267 2267 HOH HOH A . N 10 HOH 268 2268 2268 HOH HOH A . N 10 HOH 269 2269 2269 HOH HOH A . N 10 HOH 270 2270 2270 HOH HOH A . N 10 HOH 271 2271 2271 HOH HOH A . N 10 HOH 272 2272 2272 HOH HOH A . N 10 HOH 273 2273 2273 HOH HOH A . N 10 HOH 274 2274 2274 HOH HOH A . N 10 HOH 275 2275 2275 HOH HOH A . N 10 HOH 276 2276 2276 HOH HOH A . N 10 HOH 277 2277 2277 HOH HOH A . N 10 HOH 278 2278 2278 HOH HOH A . N 10 HOH 279 2279 2279 HOH HOH A . N 10 HOH 280 2280 2280 HOH HOH A . N 10 HOH 281 2281 2281 HOH HOH A . N 10 HOH 282 2282 2282 HOH HOH A . N 10 HOH 283 2283 2283 HOH HOH A . N 10 HOH 284 2284 2284 HOH HOH A . N 10 HOH 285 2285 2285 HOH HOH A . N 10 HOH 286 2286 2286 HOH HOH A . N 10 HOH 287 2287 2287 HOH HOH A . N 10 HOH 288 2288 2288 HOH HOH A . N 10 HOH 289 2289 2289 HOH HOH A . N 10 HOH 290 2290 2290 HOH HOH A . N 10 HOH 291 2291 2291 HOH HOH A . N 10 HOH 292 2292 2292 HOH HOH A . N 10 HOH 293 2293 2293 HOH HOH A . N 10 HOH 294 2294 2294 HOH HOH A . N 10 HOH 295 2295 2295 HOH HOH A . N 10 HOH 296 2296 2296 HOH HOH A . N 10 HOH 297 2297 2297 HOH HOH A . N 10 HOH 298 2298 2298 HOH HOH A . N 10 HOH 299 2299 2299 HOH HOH A . N 10 HOH 300 2300 2300 HOH HOH A . N 10 HOH 301 2301 2301 HOH HOH A . N 10 HOH 302 2302 2302 HOH HOH A . N 10 HOH 303 2303 2303 HOH HOH A . N 10 HOH 304 2304 2304 HOH HOH A . N 10 HOH 305 2305 2305 HOH HOH A . N 10 HOH 306 2306 2306 HOH HOH A . N 10 HOH 307 2307 2307 HOH HOH A . N 10 HOH 308 2308 2308 HOH HOH A . N 10 HOH 309 2309 2309 HOH HOH A . N 10 HOH 310 2310 2310 HOH HOH A . N 10 HOH 311 2311 2311 HOH HOH A . N 10 HOH 312 2312 2312 HOH HOH A . N 10 HOH 313 2313 2313 HOH HOH A . N 10 HOH 314 2314 2314 HOH HOH A . N 10 HOH 315 2315 2315 HOH HOH A . N 10 HOH 316 2316 2316 HOH HOH A . N 10 HOH 317 2317 2317 HOH HOH A . N 10 HOH 318 2318 2318 HOH HOH A . N 10 HOH 319 2319 2319 HOH HOH A . N 10 HOH 320 2320 2320 HOH HOH A . N 10 HOH 321 2321 2321 HOH HOH A . N 10 HOH 322 2322 2322 HOH HOH A . N 10 HOH 323 2323 2323 HOH HOH A . N 10 HOH 324 2324 2324 HOH HOH A . N 10 HOH 325 2325 2325 HOH HOH A . N 10 HOH 326 2326 2326 HOH HOH A . N 10 HOH 327 2327 2327 HOH HOH A . N 10 HOH 328 2328 2328 HOH HOH A . N 10 HOH 329 2329 2329 HOH HOH A . N 10 HOH 330 2330 2330 HOH HOH A . N 10 HOH 331 2331 2331 HOH HOH A . N 10 HOH 332 2332 2332 HOH HOH A . N 10 HOH 333 2333 2333 HOH HOH A . N 10 HOH 334 2334 2334 HOH HOH A . N 10 HOH 335 2335 2335 HOH HOH A . N 10 HOH 336 2336 2336 HOH HOH A . N 10 HOH 337 2337 2337 HOH HOH A . N 10 HOH 338 2338 2338 HOH HOH A . N 10 HOH 339 2339 2339 HOH HOH A . N 10 HOH 340 2340 2340 HOH HOH A . N 10 HOH 341 2341 2341 HOH HOH A . N 10 HOH 342 2342 2342 HOH HOH A . N 10 HOH 343 2343 2343 HOH HOH A . N 10 HOH 344 2344 2344 HOH HOH A . N 10 HOH 345 2345 2345 HOH HOH A . N 10 HOH 346 2346 2346 HOH HOH A . N 10 HOH 347 2347 2347 HOH HOH A . N 10 HOH 348 2348 2348 HOH HOH A . N 10 HOH 349 2349 2349 HOH HOH A . N 10 HOH 350 2350 2350 HOH HOH A . N 10 HOH 351 2351 2351 HOH HOH A . N 10 HOH 352 2352 2352 HOH HOH A . N 10 HOH 353 2353 2353 HOH HOH A . N 10 HOH 354 2354 2354 HOH HOH A . N 10 HOH 355 2355 2355 HOH HOH A . N 10 HOH 356 2356 2356 HOH HOH A . N 10 HOH 357 2357 2357 HOH HOH A . N 10 HOH 358 2358 2358 HOH HOH A . N 10 HOH 359 2359 2359 HOH HOH A . N 10 HOH 360 2360 2360 HOH HOH A . N 10 HOH 361 2361 2361 HOH HOH A . N 10 HOH 362 2362 2362 HOH HOH A . N 10 HOH 363 2363 2363 HOH HOH A . N 10 HOH 364 2364 2364 HOH HOH A . N 10 HOH 365 2365 2365 HOH HOH A . N 10 HOH 366 2366 2366 HOH HOH A . N 10 HOH 367 2367 2367 HOH HOH A . N 10 HOH 368 2368 2368 HOH HOH A . N 10 HOH 369 2369 2369 HOH HOH A . N 10 HOH 370 2370 2370 HOH HOH A . N 10 HOH 371 2371 2371 HOH HOH A . N 10 HOH 372 2372 2372 HOH HOH A . N 10 HOH 373 2373 2373 HOH HOH A . N 10 HOH 374 2374 2374 HOH HOH A . N 10 HOH 375 2375 2375 HOH HOH A . N 10 HOH 376 2376 2376 HOH HOH A . N 10 HOH 377 2377 2377 HOH HOH A . N 10 HOH 378 2378 2378 HOH HOH A . N 10 HOH 379 2379 2379 HOH HOH A . N 10 HOH 380 2380 2380 HOH HOH A . N 10 HOH 381 2381 2381 HOH HOH A . N 10 HOH 382 2382 2382 HOH HOH A . N 10 HOH 383 2383 2383 HOH HOH A . N 10 HOH 384 2384 2384 HOH HOH A . N 10 HOH 385 2385 2385 HOH HOH A . N 10 HOH 386 2386 2386 HOH HOH A . N 10 HOH 387 2387 2387 HOH HOH A . N 10 HOH 388 2388 2388 HOH HOH A . N 10 HOH 389 2389 2389 HOH HOH A . N 10 HOH 390 2390 2390 HOH HOH A . N 10 HOH 391 2391 2391 HOH HOH A . N 10 HOH 392 2392 2392 HOH HOH A . N 10 HOH 393 2393 2393 HOH HOH A . N 10 HOH 394 2394 2394 HOH HOH A . N 10 HOH 395 2395 2395 HOH HOH A . N 10 HOH 396 2396 2396 HOH HOH A . N 10 HOH 397 2397 2397 HOH HOH A . N 10 HOH 398 2398 2398 HOH HOH A . N 10 HOH 399 2399 2399 HOH HOH A . N 10 HOH 400 2400 2400 HOH HOH A . N 10 HOH 401 2401 2401 HOH HOH A . N 10 HOH 402 2402 2402 HOH HOH A . N 10 HOH 403 2403 2403 HOH HOH A . N 10 HOH 404 2404 2404 HOH HOH A . N 10 HOH 405 2405 2405 HOH HOH A . N 10 HOH 406 2406 2406 HOH HOH A . N 10 HOH 407 2407 2407 HOH HOH A . N 10 HOH 408 2408 2408 HOH HOH A . N 10 HOH 409 2409 2409 HOH HOH A . N 10 HOH 410 2410 2410 HOH HOH A . N 10 HOH 411 2411 2411 HOH HOH A . N 10 HOH 412 2412 2412 HOH HOH A . N 10 HOH 413 2413 2413 HOH HOH A . N 10 HOH 414 2414 2414 HOH HOH A . N 10 HOH 415 2415 2415 HOH HOH A . N 10 HOH 416 2416 2416 HOH HOH A . N 10 HOH 417 2417 2417 HOH HOH A . N 10 HOH 418 2418 2418 HOH HOH A . N 10 HOH 419 2419 2419 HOH HOH A . N 10 HOH 420 2420 2420 HOH HOH A . N 10 HOH 421 2421 2421 HOH HOH A . N 10 HOH 422 2422 2422 HOH HOH A . N 10 HOH 423 2423 2423 HOH HOH A . N 10 HOH 424 2424 2424 HOH HOH A . N 10 HOH 425 2425 2425 HOH HOH A . N 10 HOH 426 2426 2426 HOH HOH A . N 10 HOH 427 2427 2427 HOH HOH A . N 10 HOH 428 2428 2428 HOH HOH A . N 10 HOH 429 2429 2429 HOH HOH A . N 10 HOH 430 2430 2430 HOH HOH A . N 10 HOH 431 2431 2431 HOH HOH A . N 10 HOH 432 2432 2432 HOH HOH A . N 10 HOH 433 2433 2433 HOH HOH A . N 10 HOH 434 2434 2434 HOH HOH A . N 10 HOH 435 2435 2435 HOH HOH A . N 10 HOH 436 2436 2436 HOH HOH A . N 10 HOH 437 2437 2437 HOH HOH A . N 10 HOH 438 2438 2438 HOH HOH A . N 10 HOH 439 2439 2439 HOH HOH A . N 10 HOH 440 2440 2440 HOH HOH A . N 10 HOH 441 2441 2441 HOH HOH A . N 10 HOH 442 2442 2442 HOH HOH A . N 10 HOH 443 2443 2443 HOH HOH A . N 10 HOH 444 2444 2444 HOH HOH A . N 10 HOH 445 2445 2445 HOH HOH A . N 10 HOH 446 2446 2446 HOH HOH A . N 10 HOH 447 2447 2447 HOH HOH A . N 10 HOH 448 2448 2448 HOH HOH A . N 10 HOH 449 2449 2449 HOH HOH A . N 10 HOH 450 2450 2450 HOH HOH A . N 10 HOH 451 2451 2451 HOH HOH A . N 10 HOH 452 2452 2452 HOH HOH A . N 10 HOH 453 2453 2453 HOH HOH A . N 10 HOH 454 2454 2454 HOH HOH A . N 10 HOH 455 2455 2455 HOH HOH A . N 10 HOH 456 2456 2456 HOH HOH A . N 10 HOH 457 2457 2457 HOH HOH A . N 10 HOH 458 2458 2458 HOH HOH A . N 10 HOH 459 2459 2459 HOH HOH A . N 10 HOH 460 2460 2460 HOH HOH A . N 10 HOH 461 2461 2461 HOH HOH A . N 10 HOH 462 2462 2462 HOH HOH A . N 10 HOH 463 2463 2463 HOH HOH A . N 10 HOH 464 2464 2464 HOH HOH A . N 10 HOH 465 2465 2465 HOH HOH A . N 10 HOH 466 2466 2466 HOH HOH A . N 10 HOH 467 2467 2467 HOH HOH A . N 10 HOH 468 2468 2468 HOH HOH A . N 10 HOH 469 2469 2469 HOH HOH A . N 10 HOH 470 2470 2470 HOH HOH A . N 10 HOH 471 2471 2471 HOH HOH A . N 10 HOH 472 2472 2472 HOH HOH A . N 10 HOH 473 2473 2473 HOH HOH A . N 10 HOH 474 2474 2474 HOH HOH A . N 10 HOH 475 2475 2475 HOH HOH A . N 10 HOH 476 2476 2476 HOH HOH A . N 10 HOH 477 2477 2477 HOH HOH A . N 10 HOH 478 2478 2478 HOH HOH A . N 10 HOH 479 2479 2479 HOH HOH A . N 10 HOH 480 2480 2480 HOH HOH A . N 10 HOH 481 2481 2481 HOH HOH A . N 10 HOH 482 2482 2482 HOH HOH A . N 10 HOH 483 2483 2483 HOH HOH A . N 10 HOH 484 2484 2484 HOH HOH A . N 10 HOH 485 2485 2485 HOH HOH A . N 10 HOH 486 2486 2486 HOH HOH A . N 10 HOH 487 2487 2487 HOH HOH A . N 10 HOH 488 2488 2488 HOH HOH A . N 10 HOH 489 2489 2489 HOH HOH A . N 10 HOH 490 2490 2490 HOH HOH A . N 10 HOH 491 2491 2491 HOH HOH A . N 10 HOH 492 2492 2492 HOH HOH A . N 10 HOH 493 2493 2493 HOH HOH A . N 10 HOH 494 2494 2494 HOH HOH A . N 10 HOH 495 2495 2495 HOH HOH A . N 10 HOH 496 2496 2496 HOH HOH A . N 10 HOH 497 2497 2497 HOH HOH A . N 10 HOH 498 2498 2498 HOH HOH A . N 10 HOH 499 2499 2499 HOH HOH A . N 10 HOH 500 2500 2500 HOH HOH A . N 10 HOH 501 2501 2501 HOH HOH A . N 10 HOH 502 2502 2502 HOH HOH A . N 10 HOH 503 2503 2503 HOH HOH A . N 10 HOH 504 2504 2504 HOH HOH A . N 10 HOH 505 2505 2505 HOH HOH A . N 10 HOH 506 2506 2506 HOH HOH A . N 10 HOH 507 2507 2507 HOH HOH A . N 10 HOH 508 2508 2508 HOH HOH A . N 10 HOH 509 2509 2509 HOH HOH A . N 10 HOH 510 2510 2510 HOH HOH A . N 10 HOH 511 2511 2511 HOH HOH A . N 10 HOH 512 2512 2512 HOH HOH A . N 10 HOH 513 2513 2513 HOH HOH A . N 10 HOH 514 2514 2514 HOH HOH A . N 10 HOH 515 2515 2515 HOH HOH A . N 10 HOH 516 2516 2516 HOH HOH A . N 10 HOH 517 2517 2517 HOH HOH A . N 10 HOH 518 2518 2518 HOH HOH A . N 10 HOH 519 2519 2519 HOH HOH A . N 10 HOH 520 2520 2520 HOH HOH A . N 10 HOH 521 2521 2521 HOH HOH A . N 10 HOH 522 2522 2522 HOH HOH A . N 10 HOH 523 2523 2523 HOH HOH A . N 10 HOH 524 2524 2524 HOH HOH A . N 10 HOH 525 2525 2525 HOH HOH A . N 10 HOH 526 2526 2526 HOH HOH A . N 10 HOH 527 2527 2527 HOH HOH A . N 10 HOH 528 2528 2528 HOH HOH A . N 10 HOH 529 2529 2529 HOH HOH A . N 10 HOH 530 2530 2530 HOH HOH A . N 10 HOH 531 2531 2531 HOH HOH A . N 10 HOH 532 2532 2532 HOH HOH A . N 10 HOH 533 2533 2533 HOH HOH A . N 10 HOH 534 2534 2534 HOH HOH A . N 10 HOH 535 2535 2535 HOH HOH A . N 10 HOH 536 2536 2536 HOH HOH A . N 10 HOH 537 2537 2537 HOH HOH A . N 10 HOH 538 2538 2538 HOH HOH A . N 10 HOH 539 2539 2539 HOH HOH A . N 10 HOH 540 2540 2540 HOH HOH A . N 10 HOH 541 2541 2541 HOH HOH A . N 10 HOH 542 2542 2542 HOH HOH A . N 10 HOH 543 2543 2543 HOH HOH A . N 10 HOH 544 2544 2544 HOH HOH A . N 10 HOH 545 2545 2545 HOH HOH A . N 10 HOH 546 2546 2546 HOH HOH A . N 10 HOH 547 2547 2547 HOH HOH A . N 10 HOH 548 2548 2548 HOH HOH A . N 10 HOH 549 2549 2549 HOH HOH A . N 10 HOH 550 2550 2550 HOH HOH A . N 10 HOH 551 2551 2551 HOH HOH A . N 10 HOH 552 2552 2552 HOH HOH A . N 10 HOH 553 2553 2553 HOH HOH A . N 10 HOH 554 2554 2554 HOH HOH A . N 10 HOH 555 2555 2555 HOH HOH A . N 10 HOH 556 2556 2556 HOH HOH A . N 10 HOH 557 2557 2557 HOH HOH A . N 10 HOH 558 2558 2558 HOH HOH A . N 10 HOH 559 2559 2559 HOH HOH A . N 10 HOH 560 2560 2560 HOH HOH A . N 10 HOH 561 2561 2561 HOH HOH A . N 10 HOH 562 2562 2562 HOH HOH A . N 10 HOH 563 2563 2563 HOH HOH A . N 10 HOH 564 2564 2564 HOH HOH A . N 10 HOH 565 2565 2565 HOH HOH A . N 10 HOH 566 2566 2566 HOH HOH A . N 10 HOH 567 2567 2567 HOH HOH A . N 10 HOH 568 2568 2568 HOH HOH A . N 10 HOH 569 2569 2569 HOH HOH A . N 10 HOH 570 2570 2570 HOH HOH A . N 10 HOH 571 2571 2571 HOH HOH A . N 10 HOH 572 2572 2572 HOH HOH A . N 10 HOH 573 2573 2573 HOH HOH A . N 10 HOH 574 2574 2574 HOH HOH A . N 10 HOH 575 2575 2575 HOH HOH A . N 10 HOH 576 2576 2576 HOH HOH A . N 10 HOH 577 2577 2577 HOH HOH A . N 10 HOH 578 2578 2578 HOH HOH A . N 10 HOH 579 2579 2579 HOH HOH A . N 10 HOH 580 2580 2580 HOH HOH A . N 10 HOH 581 2581 2581 HOH HOH A . N 10 HOH 582 2582 2582 HOH HOH A . N 10 HOH 583 2583 2583 HOH HOH A . N 10 HOH 584 2584 2584 HOH HOH A . N 10 HOH 585 2585 2585 HOH HOH A . N 10 HOH 586 2586 2586 HOH HOH A . N 10 HOH 587 2587 2587 HOH HOH A . N 10 HOH 588 2588 2588 HOH HOH A . N 10 HOH 589 2589 2589 HOH HOH A . N 10 HOH 590 2590 2590 HOH HOH A . N 10 HOH 591 2591 2591 HOH HOH A . N 10 HOH 592 2592 2592 HOH HOH A . N 10 HOH 593 2593 2593 HOH HOH A . N 10 HOH 594 2594 2594 HOH HOH A . N 10 HOH 595 2595 2595 HOH HOH A . N 10 HOH 596 2596 2596 HOH HOH A . N 10 HOH 597 2597 2597 HOH HOH A . N 10 HOH 598 2598 2598 HOH HOH A . N 10 HOH 599 2599 2599 HOH HOH A . N 10 HOH 600 2600 2600 HOH HOH A . N 10 HOH 601 2601 2601 HOH HOH A . N 10 HOH 602 2602 2602 HOH HOH A . N 10 HOH 603 2603 2603 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 55 _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 PQS _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,K,L,M,N # _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 ? N HOH . ? A HOH 2073 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2581 ? 1_555 88.0 ? 2 O ? N HOH . ? A HOH 2073 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2168 ? 1_555 92.8 ? 3 O ? N HOH . ? A HOH 2581 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2168 ? 1_555 89.9 ? 4 O ? N HOH . ? A HOH 2073 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2048 ? 1_555 88.7 ? 5 O ? N HOH . ? A HOH 2581 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2048 ? 1_555 175.1 ? 6 O ? N HOH . ? A HOH 2168 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2048 ? 1_555 86.6 ? 7 O ? N HOH . ? A HOH 2073 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2578 ? 1_555 89.5 ? 8 O ? N HOH . ? A HOH 2581 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2578 ? 1_555 92.5 ? 9 O ? N HOH . ? A HOH 2168 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2578 ? 1_555 176.6 ? 10 O ? N HOH . ? A HOH 2048 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2578 ? 1_555 91.0 ? 11 O ? N HOH . ? A HOH 2073 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2019 ? 1_555 177.1 ? 12 O ? N HOH . ? A HOH 2581 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2019 ? 1_555 91.3 ? 13 O ? N HOH . ? A HOH 2168 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2019 ? 1_555 90.0 ? 14 O ? N HOH . ? A HOH 2048 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2019 ? 1_555 92.1 ? 15 O ? N HOH . ? A HOH 2578 ? 1_555 MG ? C MG . ? A MG 501 ? 1_555 O ? N HOH . ? A HOH 2019 ? 1_555 87.7 ? # 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 2011-05-08 3 'Structure model' 1 2 2011-07-13 # _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' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.1.06 ? 1 DENZO 'data reduction' . ? 2 SCALEPACK 'data scaling' . ? 3 # _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 1OC7 _pdbx_entry_details.compound_details 'ENGINEERED MUTATION ASP 405 ASN 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 AS ONLY THE SIGNAL PEPTIDE AND THE CATALYTIC DOMAIN WERE EXPRESSED. THE CATALYTIC DOMAIN SHOULD BEGIN AT PHE 89. OUR NUMBERING BEGIN AT THE FIRST RESIDUE OF THE MATURE PROTEIN WHICH EXPLAIN A DIFFERENCE WITH THE DATABASE SEQUENCE WHICH INCLUDE THE PROSEQUENCE. HERE,DUE TO THE INCORRECT PROCESSING OF THE SIGNAL PEPTIDE ALA 87 AND PRO 88 ARE ALSO PRESENT IN THE MATURE PROTEIN. THIS PROTEIN IS CLOSELY RELATED TO AVICELASE 2 (SWISS-PROT ACCESSION ID:Q9C1S9) WITH WHICH IT HAS 96% SEQUENCE IDENTITY. ; # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 CD _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 GLU _pdbx_validate_rmsd_bond.auth_seq_id_1 293 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 OE2 _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 GLU _pdbx_validate_rmsd_bond.auth_seq_id_2 293 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.150 _pdbx_validate_rmsd_bond.bond_target_value 1.252 _pdbx_validate_rmsd_bond.bond_deviation -0.102 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.011 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 139 ? ? CG A ASP 139 ? ? OD1 A ASP 139 ? ? 124.95 118.30 6.65 0.90 N 2 1 NE A ARG 444 ? ? CZ A ARG 444 ? ? NH2 A ARG 444 ? ? 116.98 120.30 -3.32 0.50 N # 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 ? ? -113.37 -87.21 2 1 TYR A 174 ? ? -151.15 72.04 3 1 ASP A 175 ? ? -151.20 31.19 4 1 ASN A 194 ? ? -119.32 56.98 5 1 PHE A 214 ? ? -102.05 40.41 6 1 GLU A 224 ? ? 53.61 74.31 7 1 SER A 227 ? ? -118.47 -92.97 8 1 TRP A 274 ? ? -116.68 -77.99 # _pdbx_validate_planes.id 1 _pdbx_validate_planes.PDB_model_num 1 _pdbx_validate_planes.auth_comp_id ARG _pdbx_validate_planes.auth_asym_id A _pdbx_validate_planes.auth_seq_id 339 _pdbx_validate_planes.PDB_ins_code ? _pdbx_validate_planes.label_alt_id ? _pdbx_validate_planes.rmsd 0.089 _pdbx_validate_planes.type 'SIDE CHAIN' # 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 2081 ? 6.21 . 2 1 O ? A HOH 2103 ? 6.44 . # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 'MAGNESIUM ION' MG 4 'ACETATE ION' ACT 5 DIMETHYLFORMAMIDE DMF 6 GLYCEROL GOL 7 BETA-D-GLUCOSE BGC 8 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE SGC 9 O1-METHYL-4-DEOXY-4-THIO-ALPHA-D-GLUCOSE MA3 10 water HOH #