data_1OC5 # _entry.id 1OC5 # _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 1OC5 PDBE EBI-9306 WWPDB D_1290009306 # 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 1OC6 unspecified 'STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION' PDB 1OC7 unspecified ;D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-TETRATHIO-ALPHA-D-CELLOPENTOSIDE AT 1 .1 ANGSTROM RESOLUTION ; PDB 1OCB unspecified 'STRUCTURE OF THE WILD-TYPE CELLOBIOHYDROLASE CEL6A FROM HUMICOLAS INSOLENS IN COMPLEX WITH A FLUORESCENT SUBSTRATE' PDB 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 1OC5 _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 1OC5 _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 1OC5 _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 GLYCEROL 92.094 6 ? ? ? ? 4 non-polymer man O1-METHYL-GLUCOSE 194.182 1 ? ? ? ? 5 non-polymer man 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE 196.221 1 ? ? ? ? 6 non-polymer man BETA-D-GLUCOSE 180.156 2 ? ? ? ? 7 water nat water 18.015 471 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'CELLULASE, CEL6A' # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;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 1OC5 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession 1OC5 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1OC5 _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 1OC5 _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 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BGC saccharide . BETA-D-GLUCOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MGL saccharide . O1-METHYL-GLUCOSE ? 'C7 H14 O6' 194.182 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 1OC5 _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 'NATIVE WILD-TYPE STRUCTURE OF CEL6A FROM HUMICOLA INSOLENS' # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 7.50 _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 IN 100MM HEPES BUFFER AT PH 7.5. PRECIPITANT WAS 16% POLYETHYLENE GLYCOL 5000MME. THE PROTEIN WAS INCUBATED WITH 1MM OF THE INHIBITOR PRIOR CRYSTALLISATION. ; # _diffrn.id 1 _diffrn.ambient_temp 100.0 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date 1999-09-15 _diffrn_detector.details 'TOROIDAL MIRROR' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator SILICON _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.9393 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-4' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-4 _diffrn_source.pdbx_wavelength 0.9393 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1OC5 _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 50.000 _reflns.d_resolution_high 1.700 _reflns.number_obs 33830 _reflns.number_all ? _reflns.percent_possible_obs 93.9 _reflns.pdbx_Rmerge_I_obs 0.05500 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 17.0000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 2.900 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.70 _reflns_shell.d_res_low 1.76 _reflns_shell.percent_possible_all 88.7 _reflns_shell.Rmerge_I_obs 0.15700 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 5.800 _reflns_shell.pdbx_redundancy 2.70 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1OC5 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 33830 _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 50.00 _refine.ls_d_res_high 1.70 _refine.ls_percent_reflns_obs 94.1 _refine.ls_R_factor_obs 0.129 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.127 _refine.ls_R_factor_R_free 0.168 _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 1773 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.971 _refine.correlation_coeff_Fo_to_Fc_free 0.951 _refine.B_iso_mean 9.09 _refine.aniso_B[1][1] -0.43000 _refine.aniso_B[2][2] 0.21000 _refine.aniso_B[3][3] 0.22000 _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 1BVW' _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 0.094 _refine.pdbx_overall_ESU_R_Free 0.095 _refine.overall_SU_ML 0.054 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 1.609 _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 95 _refine_hist.number_atoms_solvent 471 _refine_hist.number_atoms_total 3405 _refine_hist.d_res_high 1.70 _refine_hist.d_res_low 50.00 # 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 0.014 0.021 ? 3096 'X-RAY DIFFRACTION' ? r_bond_other_d 0.002 0.020 ? 2691 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.653 1.959 ? 4224 'X-RAY DIFFRACTION' ? r_angle_other_deg 2.143 3.000 ? 6283 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.279 5.000 ? 363 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 39.021 24.305 ? 151 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 11.374 15.000 ? 450 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 17.508 15.000 ? 19 'X-RAY DIFFRACTION' ? r_chiral_restr 0.103 0.200 ? 461 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.008 0.020 ? 3385 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.005 0.020 ? 612 'X-RAY DIFFRACTION' ? r_nbd_refined 0.225 0.200 ? 595 'X-RAY DIFFRACTION' ? r_nbd_other 0.285 0.200 ? 3036 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other 0.088 0.200 ? 1564 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.100 0.200 ? 311 '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 0.167 0.200 ? 11 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.236 0.200 ? 48 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.146 0.200 ? 27 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it 0.934 1.500 ? 1838 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.535 2.000 ? 2975 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.372 3.000 ? 1258 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.600 4.500 ? 1249 '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 1.70 _refine_ls_shell.d_res_low 1.74 _refine_ls_shell.number_reflns_R_work 2288 _refine_ls_shell.R_factor_R_work 0.1460 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.2080 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 126 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 1OC5 _struct.title ;D405N mutant of the CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS in complex with methyl-cellobiosyl-4-deoxy-4-thio-beta-D-cellobioside ; _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 1OC5 _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 3 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 3 ? I N N 4 ? J N N 5 ? K N N 6 ? L N N 6 ? M N N 7 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 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 ? ? ? ? ? ? ? 2.066 ? disulf2 disulf ? ? A CYS 286 SG ? ? ? 1_555 A CYS 333 SG ? ? A CYS 372 A CYS 419 1_555 ? ? ? ? ? ? ? 2.082 ? covale1 covale ? ? A ASN 55 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 141 A NAG 500 1_555 ? ? ? ? ? ? ? 1.460 ? covale2 covale ? ? I MGL . O4 ? ? ? 1_555 J SGC . C1 ? ? A MGL 507 A SGC 508 1_555 ? ? ? ? ? ? ? 1.330 ? covale3 covale ? ? J SGC . S4 ? ? ? 1_555 K BGC . C1 ? ? A SGC 508 A BGC 509 1_555 ? ? ? ? ? ? ? 1.807 ? covale4 covale ? ? K BGC . O4 ? ? ? 1_555 L BGC . C1 ? ? A BGC 509 A BGC 510 1_555 ? ? ? ? ? ? ? 1.416 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # 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 -0.90 2 SER 238 A . ? SER 324 A PRO 239 A ? PRO 325 A 1 1.06 3 GLN 275 A . ? GLN 361 A PRO 276 A ? PRO 362 A 1 -6.71 4 LYS 340 A . ? LYS 426 A PRO 341 A ? PRO 427 A 1 -2.18 5 ASN 361 A . ? ASN 447 A PRO 362 A ? PRO 448 A 1 2.03 # 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 ? ? ? ? 10 'BINDING SITE FOR RESIDUE MGL A 507' AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SGC A 508' AC4 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE BGC A 509' AC5 Software ? ? ? ? 11 'BINDING SITE FOR RESIDUE BGC A 510' AC6 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE GOL A 501' AC7 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL A 502' AC8 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL A 503' AC9 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE GOL A 504' BC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE GOL A 505' BC2 Software ? ? ? ? 6 '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 M . ? HOH A 2074 . ? 1_555 ? 8 AC1 15 HOH M . ? HOH A 2075 . ? 1_555 ? 9 AC1 15 HOH M . ? HOH A 2180 . ? 1_555 ? 10 AC1 15 HOH M . ? HOH A 2351 . ? 1_555 ? 11 AC1 15 HOH M . ? HOH A 2411 . ? 1_555 ? 12 AC1 15 HOH M . ? HOH A 2449 . ? 1_555 ? 13 AC1 15 HOH M . ? HOH A 2450 . ? 1_555 ? 14 AC1 15 HOH M . ? HOH A 2452 . ? 1_555 ? 15 AC1 15 HOH M . ? HOH A 2453 . ? 1_555 ? 16 AC2 10 GLU A 103 ? GLU A 189 . ? 1_555 ? 17 AC2 10 TRP A 191 ? TRP A 277 . ? 1_555 ? 18 AC2 10 ARG A 328 ? ARG A 414 . ? 1_555 ? 19 AC2 10 SGC J . ? SGC A 508 . ? 1_555 ? 20 AC2 10 HOH M . ? HOH A 2279 . ? 1_555 ? 21 AC2 10 HOH M . ? HOH A 2280 . ? 1_555 ? 22 AC2 10 HOH M . ? HOH A 2459 . ? 1_555 ? 23 AC2 10 HOH M . ? HOH A 2460 . ? 1_555 ? 24 AC2 10 HOH M . ? HOH A 2461 . ? 1_555 ? 25 AC2 10 HOH M . ? HOH A 2464 . ? 1_555 ? 26 AC3 10 TRP A 188 ? TRP A 274 . ? 1_555 ? 27 AC3 10 ASN A 194 ? ASN A 280 . ? 1_555 ? 28 AC3 10 GLY A 283 ? GLY A 369 . ? 1_555 ? 29 AC3 10 MGL I . ? MGL A 507 . ? 1_555 ? 30 AC3 10 BGC K . ? BGC A 509 . ? 1_555 ? 31 AC3 10 HOH M . ? HOH A 2462 . ? 1_555 ? 32 AC3 10 HOH M . ? HOH A 2463 . ? 1_555 ? 33 AC3 10 HOH M . ? HOH A 2464 . ? 1_555 ? 34 AC3 10 HOH M . ? HOH A 2465 . ? 1_555 ? 35 AC3 10 HOH M . ? HOH A 2466 . ? 1_555 ? 36 AC4 10 ASN A 148 ? ASN A 234 . ? 1_555 ? 37 AC4 10 HIS A 185 ? HIS A 271 . ? 1_555 ? 38 AC4 10 TRP A 188 ? TRP A 274 . ? 1_555 ? 39 AC4 10 SGC J . ? SGC A 508 . ? 1_555 ? 40 AC4 10 BGC L . ? BGC A 510 . ? 1_555 ? 41 AC4 10 HOH M . ? HOH A 2229 . ? 1_555 ? 42 AC4 10 HOH M . ? HOH A 2354 . ? 1_555 ? 43 AC4 10 HOH M . ? HOH A 2465 . ? 1_555 ? 44 AC4 10 HOH M . ? HOH A 2468 . ? 1_555 ? 45 AC4 10 HOH M . ? HOH A 2470 . ? 1_555 ? 46 AC5 11 ALA A 97 ? ALA A 183 . ? 1_555 ? 47 AC5 11 ASN A 224 ? ASN A 310 . ? 1_555 ? 48 AC5 11 TRP A 285 ? TRP A 371 . ? 1_555 ? 49 AC5 11 GOL E . ? GOL A 503 . ? 1_555 ? 50 AC5 11 BGC K . ? BGC A 509 . ? 1_555 ? 51 AC5 11 HOH M . ? HOH A 2303 . ? 1_555 ? 52 AC5 11 HOH M . ? HOH A 2357 . ? 1_555 ? 53 AC5 11 HOH M . ? HOH A 2408 . ? 1_555 ? 54 AC5 11 HOH M . ? HOH A 2469 . ? 1_555 ? 55 AC5 11 HOH M . ? HOH A 2470 . ? 1_555 ? 56 AC5 11 HOH M . ? HOH A 2471 . ? 1_555 ? 57 AC6 7 TYR A 206 ? TYR A 292 . ? 1_555 ? 58 AC6 7 ARG A 216 ? ARG A 302 . ? 1_555 ? 59 AC6 7 PHE A 261 ? PHE A 347 . ? 1_555 ? 60 AC6 7 PRO A 262 ? PRO A 348 . ? 1_555 ? 61 AC6 7 GLN A 264 ? GLN A 350 . ? 1_555 ? 62 AC6 7 HOH M . ? HOH A 2296 . ? 1_555 ? 63 AC6 7 HOH M . ? HOH A 2454 . ? 1_555 ? 64 AC7 9 ALA A 227 ? ALA A 313 . ? 1_555 ? 65 AC7 9 TRP A 228 ? TRP A 314 . ? 1_555 ? 66 AC7 9 SER A 229 ? SER A 315 . ? 1_555 ? 67 AC7 9 GLN A 269 ? GLN A 355 . ? 1_555 ? 68 AC7 9 SER A 272 ? SER A 358 . ? 1_555 ? 69 AC7 9 GLY A 273 ? GLY A 359 . ? 1_555 ? 70 AC7 9 GLN A 275 ? GLN A 361 . ? 1_555 ? 71 AC7 9 HOH M . ? HOH A 2444 . ? 1_555 ? 72 AC7 9 HOH M . ? HOH A 2456 . ? 1_555 ? 73 AC8 8 ALA A 223 ? ALA A 309 . ? 1_555 ? 74 AC8 8 TRP A 285 ? TRP A 371 . ? 1_555 ? 75 AC8 8 LYS A 313 ? LYS A 399 . ? 1_555 ? 76 AC8 8 CYS A 318 ? CYS A 404 . ? 1_555 ? 77 AC8 8 ASN A 319 ? ASN A 405 . ? 1_555 ? 78 AC8 8 GOL H . ? GOL A 506 . ? 1_555 ? 79 AC8 8 BGC L . ? BGC A 510 . ? 1_555 ? 80 AC8 8 HOH M . ? HOH A 2356 . ? 1_555 ? 81 AC9 9 TYR A 18 ? TYR A 104 . ? 1_555 ? 82 AC9 9 GLN A 50 ? GLN A 136 . ? 1_555 ? 83 AC9 9 TRP A 51 ? TRP A 137 . ? 1_555 ? 84 AC9 9 ASP A 53 ? ASP A 139 . ? 1_555 ? 85 AC9 9 LEU A 61 ? LEU A 147 . ? 1_555 ? 86 AC9 9 GLU A 317 ? GLU A 403 . ? 1_555 ? 87 AC9 9 GOL H . ? GOL A 506 . ? 1_555 ? 88 AC9 9 HOH M . ? HOH A 2386 . ? 1_555 ? 89 AC9 9 HOH M . ? HOH A 2457 . ? 1_555 ? 90 BC1 3 ARG A 120 ? ARG A 206 . ? 1_555 ? 91 BC1 3 SER A 127 ? SER A 213 . ? 1_555 ? 92 BC1 3 HOH M . ? HOH A 2458 . ? 1_555 ? 93 BC2 6 ASP A 53 ? ASP A 139 . ? 1_555 ? 94 BC2 6 TYR A 88 ? TYR A 174 . ? 1_555 ? 95 BC2 6 LYS A 313 ? LYS A 399 . ? 1_555 ? 96 BC2 6 GLU A 317 ? GLU A 403 . ? 1_555 ? 97 BC2 6 GOL E . ? GOL A 503 . ? 1_555 ? 98 BC2 6 GOL F . ? GOL A 504 . ? 1_555 ? # _database_PDB_matrix.entry_id 1OC5 _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 1OC5 _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 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 ? -1.707 36.256 18.899 1.00 11.98 ? 87 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? -2.905 35.610 18.336 1.00 12.53 ? 87 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? -2.744 34.099 18.283 1.00 11.95 ? 87 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? -1.639 33.565 18.166 1.00 12.05 ? 87 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? -3.156 36.152 16.943 1.00 11.99 ? 87 ALA A CB 1 ATOM 6 N N . PRO A 1 2 ? -3.885 33.425 18.350 1.00 12.07 ? 88 PRO A N 1 ATOM 7 C CA . PRO A 1 2 ? -3.916 31.970 18.284 1.00 11.94 ? 88 PRO A CA 1 ATOM 8 C C . PRO A 1 2 ? -3.781 31.482 16.873 1.00 12.00 ? 88 PRO A C 1 ATOM 9 O O . PRO A 1 2 ? -3.974 32.216 15.907 1.00 11.79 ? 88 PRO A O 1 ATOM 10 C CB . PRO A 1 2 ? -5.310 31.594 18.787 1.00 13.65 ? 88 PRO A CB 1 ATOM 11 C CG . PRO A 1 2 ? -6.199 32.777 18.492 1.00 13.64 ? 88 PRO A CG 1 ATOM 12 C CD . PRO A 1 2 ? -5.233 33.975 18.483 1.00 11.68 ? 88 PRO A CD 1 ATOM 13 N N . TYR A 1 3 ? -3.435 30.206 16.761 1.00 11.80 ? 89 TYR A N 1 ATOM 14 C CA . TYR A 1 3 ? -3.425 29.552 15.471 1.00 11.26 ? 89 TYR A CA 1 ATOM 15 C C . TYR A 1 3 ? -3.945 28.128 15.639 1.00 12.04 ? 89 TYR A C 1 ATOM 16 O O . TYR A 1 3 ? -3.931 27.567 16.727 1.00 11.93 ? 89 TYR A O 1 ATOM 17 C CB . TYR A 1 3 ? -2.008 29.580 14.876 1.00 10.97 ? 89 TYR A CB 1 ATOM 18 C CG . TYR A 1 3 ? -1.056 28.718 15.641 1.00 10.32 ? 89 TYR A CG 1 ATOM 19 C CD1 . TYR A 1 3 ? -0.398 29.224 16.764 1.00 10.17 ? 89 TYR A CD1 1 ATOM 20 C CD2 . TYR A 1 3 ? -0.843 27.389 15.284 1.00 9.96 ? 89 TYR A CD2 1 ATOM 21 C CE1 . TYR A 1 3 ? 0.413 28.417 17.529 1.00 9.01 ? 89 TYR A CE1 1 ATOM 22 C CE2 . TYR A 1 3 ? -0.014 26.580 16.032 1.00 9.01 ? 89 TYR A CE2 1 ATOM 23 C CZ . TYR A 1 3 ? 0.610 27.078 17.155 1.00 8.57 ? 89 TYR A CZ 1 ATOM 24 O OH . TYR A 1 3 ? 1.413 26.281 17.951 1.00 9.57 ? 89 TYR A OH 1 ATOM 25 N N . ASN A 1 4 ? -4.375 27.555 14.538 1.00 13.50 ? 90 ASN A N 1 ATOM 26 C CA . ASN A 1 4 ? -4.806 26.166 14.531 1.00 15.44 ? 90 ASN A CA 1 ATOM 27 C C . ASN A 1 4 ? -3.870 25.395 13.602 1.00 13.45 ? 90 ASN A C 1 ATOM 28 O O . ASN A 1 4 ? -3.418 25.946 12.610 1.00 14.17 ? 90 ASN A O 1 ATOM 29 C CB . ASN A 1 4 ? -6.222 26.035 14.001 1.00 16.51 ? 90 ASN A CB 1 ATOM 30 C CG . ASN A 1 4 ? -7.240 26.808 14.821 1.00 20.84 ? 90 ASN A CG 1 ATOM 31 O OD1 . ASN A 1 4 ? -7.251 26.758 16.063 1.00 26.20 ? 90 ASN A OD1 1 ATOM 32 N ND2 . ASN A 1 4 ? -8.130 27.477 14.129 1.00 27.82 ? 90 ASN A ND2 1 ATOM 33 N N . GLY A 1 5 ? -3.560 24.150 13.951 1.00 12.29 ? 91 GLY A N 1 ATOM 34 C CA . GLY A 1 5 ? -2.823 23.295 13.042 1.00 11.14 ? 91 GLY A CA 1 ATOM 35 C C . GLY A 1 5 ? -1.353 23.668 12.910 1.00 8.62 ? 91 GLY A C 1 ATOM 36 O O . GLY A 1 5 ? -0.719 24.065 13.881 1.00 10.91 ? 91 GLY A O 1 ATOM 37 N N . ASN A 1 6 ? -0.835 23.506 11.707 1.00 9.17 ? 92 ASN A N 1 ATOM 38 C CA . ASN A 1 6 ? 0.591 23.649 11.419 1.00 7.10 ? 92 ASN A CA 1 ATOM 39 C C . ASN A 1 6 ? 0.977 25.108 11.550 1.00 7.18 ? 92 ASN A C 1 ATOM 40 O O . ASN A 1 6 ? 0.472 25.945 10.801 1.00 8.13 ? 92 ASN A O 1 ATOM 41 C CB . ASN A 1 6 ? 0.844 23.111 10.015 1.00 7.33 ? 92 ASN A CB 1 ATOM 42 C CG . ASN A 1 6 ? 2.269 23.270 9.568 1.00 8.88 ? 92 ASN A CG 1 ATOM 43 O OD1 . ASN A 1 6 ? 3.125 23.724 10.344 1.00 7.77 ? 92 ASN A OD1 1 ATOM 44 N ND2 . ASN A 1 6 ? 2.553 22.817 8.337 1.00 10.77 ? 92 ASN A ND2 1 ATOM 45 N N . PRO A 1 7 ? 1.839 25.456 12.494 1.00 7.20 ? 93 PRO A N 1 ATOM 46 C CA . PRO A 1 7 ? 2.229 26.863 12.706 1.00 7.63 ? 93 PRO A CA 1 ATOM 47 C C . PRO A 1 7 ? 2.953 27.479 11.542 1.00 8.29 ? 93 PRO A C 1 ATOM 48 O O . PRO A 1 7 ? 3.069 28.696 11.498 1.00 8.27 ? 93 PRO A O 1 ATOM 49 C CB . PRO A 1 7 ? 3.137 26.777 13.923 1.00 8.05 ? 93 PRO A CB 1 ATOM 50 C CG . PRO A 1 7 ? 3.705 25.407 13.889 1.00 7.28 ? 93 PRO A CG 1 ATOM 51 C CD . PRO A 1 7 ? 2.564 24.550 13.401 1.00 6.34 ? 93 PRO A CD 1 ATOM 52 N N . PHE A 1 8 ? 3.479 26.674 10.615 1.00 8.54 ? 94 PHE A N 1 ATOM 53 C CA . PHE A 1 8 ? 4.149 27.175 9.409 1.00 7.44 ? 94 PHE A CA 1 ATOM 54 C C . PHE A 1 8 ? 3.194 27.572 8.288 1.00 9.34 ? 94 PHE A C 1 ATOM 55 O O . PHE A 1 8 ? 3.599 28.177 7.276 1.00 9.23 ? 94 PHE A O 1 ATOM 56 C CB . PHE A 1 8 ? 5.162 26.178 8.855 1.00 8.21 ? 94 PHE A CB 1 ATOM 57 C CG . PHE A 1 8 ? 6.351 25.971 9.748 1.00 5.71 ? 94 PHE A CG 1 ATOM 58 C CD1 . PHE A 1 8 ? 6.293 25.095 10.805 1.00 6.37 ? 94 PHE A CD1 1 ATOM 59 C CD2 . PHE A 1 8 ? 7.525 26.673 9.536 1.00 7.32 ? 94 PHE A CD2 1 ATOM 60 C CE1 . PHE A 1 8 ? 7.390 24.865 11.624 1.00 7.01 ? 94 PHE A CE1 1 ATOM 61 C CE2 . PHE A 1 8 ? 8.622 26.470 10.359 1.00 7.78 ? 94 PHE A CE2 1 ATOM 62 C CZ . PHE A 1 8 ? 8.558 25.569 11.397 1.00 6.49 ? 94 PHE A CZ 1 ATOM 63 N N . GLU A 1 9 ? 1.937 27.202 8.474 1.00 9.51 ? 95 GLU A N 1 ATOM 64 C CA . GLU A 1 9 ? 0.909 27.556 7.478 1.00 11.55 ? 95 GLU A CA 1 ATOM 65 C C . GLU A 1 9 ? 0.373 28.954 7.760 1.00 10.87 ? 95 GLU A C 1 ATOM 66 O O . GLU A 1 9 ? 0.107 29.298 8.898 1.00 12.57 ? 95 GLU A O 1 ATOM 67 C CB A GLU A 1 9 ? -0.283 26.612 7.500 0.50 11.65 ? 95 GLU A CB 1 ATOM 68 C CB B GLU A 1 9 ? -0.183 26.512 7.569 0.50 11.92 ? 95 GLU A CB 1 ATOM 69 C CG A GLU A 1 9 ? -0.046 25.308 6.786 0.50 14.59 ? 95 GLU A CG 1 ATOM 70 C CG B GLU A 1 9 ? -1.274 26.668 6.548 0.50 15.15 ? 95 GLU A CG 1 ATOM 71 C CD A GLU A 1 9 ? -1.228 24.362 6.862 0.50 21.24 ? 95 GLU A CD 1 ATOM 72 C CD B GLU A 1 9 ? -2.228 25.494 6.558 0.50 21.80 ? 95 GLU A CD 1 ATOM 73 O OE1 A GLU A 1 9 ? -2.411 24.807 6.808 0.50 26.58 ? 95 GLU A OE1 1 ATOM 74 O OE1 B GLU A 1 9 ? -1.793 24.345 6.858 0.50 26.11 ? 95 GLU A OE1 1 ATOM 75 O OE2 A GLU A 1 9 ? -0.968 23.143 6.967 0.50 24.57 ? 95 GLU A OE2 1 ATOM 76 O OE2 B GLU A 1 9 ? -3.421 25.725 6.288 0.50 22.13 ? 95 GLU A OE2 1 ATOM 77 N N . GLY A 1 10 ? 0.197 29.699 6.668 1.00 12.14 ? 96 GLY A N 1 ATOM 78 C CA . GLY A 1 10 ? -0.405 31.007 6.737 1.00 13.71 ? 96 GLY A CA 1 ATOM 79 C C . GLY A 1 10 ? 0.524 32.128 7.172 1.00 13.13 ? 96 GLY A C 1 ATOM 80 O O . GLY A 1 10 ? 0.063 33.248 7.438 1.00 14.01 ? 96 GLY A O 1 ATOM 81 N N . VAL A 1 11 ? 1.817 31.828 7.268 1.00 11.87 ? 97 VAL A N 1 ATOM 82 C CA . VAL A 1 11 ? 2.844 32.822 7.604 1.00 10.81 ? 97 VAL A CA 1 ATOM 83 C C . VAL A 1 11 ? 4.019 32.656 6.652 1.00 10.56 ? 97 VAL A C 1 ATOM 84 O O . VAL A 1 11 ? 4.197 31.606 6.042 1.00 12.83 ? 97 VAL A O 1 ATOM 85 C CB . VAL A 1 11 ? 3.344 32.689 9.067 1.00 9.94 ? 97 VAL A CB 1 ATOM 86 C CG1 . VAL A 1 11 ? 2.282 33.067 10.066 1.00 11.18 ? 97 VAL A CG1 1 ATOM 87 C CG2 . VAL A 1 11 ? 3.797 31.276 9.298 1.00 10.33 ? 97 VAL A CG2 1 ATOM 88 N N . GLN A 1 12 ? 4.830 33.700 6.535 1.00 10.03 ? 98 GLN A N 1 ATOM 89 C CA . GLN A 1 12 ? 6.137 33.694 5.891 1.00 11.04 ? 98 GLN A CA 1 ATOM 90 C C . GLN A 1 12 ? 7.170 33.566 6.995 1.00 9.92 ? 98 GLN A C 1 ATOM 91 O O . GLN A 1 12 ? 6.895 33.942 8.126 1.00 10.29 ? 98 GLN A O 1 ATOM 92 C CB . GLN A 1 12 ? 6.452 35.064 5.226 1.00 12.88 ? 98 GLN A CB 1 ATOM 93 C CG . GLN A 1 12 ? 5.540 35.538 4.207 1.00 17.62 ? 98 GLN A CG 1 ATOM 94 C CD . GLN A 1 12 ? 6.165 36.738 3.526 1.00 20.77 ? 98 GLN A CD 1 ATOM 95 O OE1 . GLN A 1 12 ? 7.248 36.623 2.933 1.00 20.47 ? 98 GLN A OE1 1 ATOM 96 N NE2 . GLN A 1 12 ? 5.528 37.900 3.680 1.00 17.34 ? 98 GLN A NE2 1 ATOM 97 N N . LEU A 1 13 ? 8.339 33.029 6.682 1.00 9.26 ? 99 LEU A N 1 ATOM 98 C CA . LEU A 1 13 ? 9.383 32.907 7.680 1.00 7.70 ? 99 LEU A CA 1 ATOM 99 C C . LEU A 1 13 ? 10.377 34.073 7.610 1.00 6.62 ? 99 LEU A C 1 ATOM 100 O O . LEU A 1 13 ? 10.912 34.386 6.557 1.00 8.17 ? 99 LEU A O 1 ATOM 101 C CB . LEU A 1 13 ? 10.097 31.547 7.607 1.00 7.19 ? 99 LEU A CB 1 ATOM 102 C CG . LEU A 1 13 ? 9.140 30.370 7.764 1.00 6.95 ? 99 LEU A CG 1 ATOM 103 C CD1 . LEU A 1 13 ? 9.851 29.081 7.436 1.00 8.80 ? 99 LEU A CD1 1 ATOM 104 C CD2 . LEU A 1 13 ? 8.593 30.323 9.179 1.00 8.00 ? 99 LEU A CD2 1 ATOM 105 N N . TRP A 1 14 ? 10.639 34.713 8.735 1.00 6.74 ? 100 TRP A N 1 ATOM 106 C CA . TRP A 1 14 ? 11.555 35.876 8.759 1.00 7.33 ? 100 TRP A CA 1 ATOM 107 C C . TRP A 1 14 ? 13.005 35.454 8.664 1.00 8.36 ? 100 TRP A C 1 ATOM 108 O O . TRP A 1 14 ? 13.412 34.557 9.415 1.00 9.93 ? 100 TRP A O 1 ATOM 109 C CB . TRP A 1 14 ? 11.390 36.569 10.102 1.00 8.30 ? 100 TRP A CB 1 ATOM 110 C CG . TRP A 1 14 ? 12.255 37.756 10.362 1.00 8.04 ? 100 TRP A CG 1 ATOM 111 C CD1 . TRP A 1 14 ? 13.270 37.828 11.251 1.00 7.98 ? 100 TRP A CD1 1 ATOM 112 C CD2 . TRP A 1 14 ? 12.130 39.057 9.784 1.00 10.11 ? 100 TRP A CD2 1 ATOM 113 N NE1 . TRP A 1 14 ? 13.811 39.091 11.262 1.00 9.02 ? 100 TRP A NE1 1 ATOM 114 C CE2 . TRP A 1 14 ? 13.127 39.860 10.364 1.00 10.81 ? 100 TRP A CE2 1 ATOM 115 C CE3 . TRP A 1 14 ? 11.266 39.634 8.834 1.00 12.15 ? 100 TRP A CE3 1 ATOM 116 C CZ2 . TRP A 1 14 ? 13.293 41.198 10.038 1.00 12.75 ? 100 TRP A CZ2 1 ATOM 117 C CZ3 . TRP A 1 14 ? 11.432 40.969 8.508 1.00 13.11 ? 100 TRP A CZ3 1 ATOM 118 C CH2 . TRP A 1 14 ? 12.453 41.732 9.119 1.00 10.38 ? 100 TRP A CH2 1 ATOM 119 N N . ALA A 1 15 ? 13.782 36.092 7.788 1.00 8.31 ? 101 ALA A N 1 ATOM 120 C CA . ALA A 1 15 ? 15.232 35.867 7.758 1.00 9.18 ? 101 ALA A CA 1 ATOM 121 C C . ALA A 1 15 ? 15.842 36.931 8.647 1.00 9.49 ? 101 ALA A C 1 ATOM 122 O O . ALA A 1 15 ? 15.639 38.116 8.402 1.00 9.25 ? 101 ALA A O 1 ATOM 123 C CB . ALA A 1 15 ? 15.772 35.945 6.320 1.00 9.53 ? 101 ALA A CB 1 ATOM 124 N N . ASN A 1 16 ? 16.541 36.535 9.703 1.00 8.16 ? 102 ASN A N 1 ATOM 125 C CA . ASN A 1 16 ? 16.952 37.475 10.735 1.00 8.33 ? 102 ASN A CA 1 ATOM 126 C C . ASN A 1 16 ? 18.197 38.255 10.345 1.00 8.40 ? 102 ASN A C 1 ATOM 127 O O . ASN A 1 16 ? 18.975 37.874 9.473 1.00 7.60 ? 102 ASN A O 1 ATOM 128 C CB . ASN A 1 16 ? 17.080 36.736 12.083 1.00 7.80 ? 102 ASN A CB 1 ATOM 129 C CG . ASN A 1 16 ? 18.276 35.811 12.099 1.00 8.15 ? 102 ASN A CG 1 ATOM 130 O OD1 . ASN A 1 16 ? 19.423 36.276 12.164 1.00 8.63 ? 102 ASN A OD1 1 ATOM 131 N ND2 . ASN A 1 16 ? 18.036 34.495 11.976 1.00 9.01 ? 102 ASN A ND2 1 ATOM 132 N N . ASN A 1 17 ? 18.316 39.415 10.970 1.00 8.47 ? 103 ASN A N 1 ATOM 133 C CA . ASN A 1 17 ? 19.416 40.343 10.693 1.00 9.88 ? 103 ASN A CA 1 ATOM 134 C C . ASN A 1 17 ? 20.767 39.971 11.264 1.00 8.87 ? 103 ASN A C 1 ATOM 135 O O . ASN A 1 17 ? 21.768 40.456 10.829 1.00 9.71 ? 103 ASN A O 1 ATOM 136 C CB . ASN A 1 17 ? 18.974 41.729 11.103 1.00 10.22 ? 103 ASN A CB 1 ATOM 137 C CG . ASN A 1 17 ? 18.152 42.373 10.033 1.00 13.53 ? 103 ASN A CG 1 ATOM 138 O OD1 . ASN A 1 17 ? 18.563 42.385 8.873 1.00 15.87 ? 103 ASN A OD1 1 ATOM 139 N ND2 . ASN A 1 17 ? 16.994 42.905 10.389 1.00 17.75 ? 103 ASN A ND2 1 ATOM 140 N N . TYR A 1 18 ? 20.781 39.042 12.214 1.00 9.70 ? 104 TYR A N 1 ATOM 141 C CA . TYR A 1 18 ? 22.033 38.494 12.749 1.00 8.90 ? 104 TYR A CA 1 ATOM 142 C C . TYR A 1 18 ? 22.736 37.687 11.642 1.00 8.55 ? 104 TYR A C 1 ATOM 143 O O . TYR A 1 18 ? 23.866 37.980 11.263 1.00 7.71 ? 104 TYR A O 1 ATOM 144 C CB . TYR A 1 18 ? 21.754 37.629 13.954 1.00 10.24 ? 104 TYR A CB 1 ATOM 145 C CG . TYR A 1 18 ? 22.963 37.040 14.619 1.00 9.11 ? 104 TYR A CG 1 ATOM 146 C CD1 . TYR A 1 18 ? 23.549 35.864 14.149 1.00 13.27 ? 104 TYR A CD1 1 ATOM 147 C CD2 . TYR A 1 18 ? 23.524 37.658 15.744 1.00 10.04 ? 104 TYR A CD2 1 ATOM 148 C CE1 . TYR A 1 18 ? 24.673 35.346 14.771 1.00 12.23 ? 104 TYR A CE1 1 ATOM 149 C CE2 . TYR A 1 18 ? 24.616 37.135 16.362 1.00 11.60 ? 104 TYR A CE2 1 ATOM 150 C CZ . TYR A 1 18 ? 25.176 35.972 15.890 1.00 13.04 ? 104 TYR A CZ 1 ATOM 151 O OH . TYR A 1 18 ? 26.286 35.412 16.530 1.00 14.56 ? 104 TYR A OH 1 ATOM 152 N N . TYR A 1 19 ? 22.023 36.739 11.075 1.00 6.97 ? 105 TYR A N 1 ATOM 153 C CA . TYR A 1 19 ? 22.631 35.923 10.015 1.00 7.14 ? 105 TYR A CA 1 ATOM 154 C C . TYR A 1 19 ? 22.945 36.808 8.792 1.00 6.97 ? 105 TYR A C 1 ATOM 155 O O . TYR A 1 19 ? 24.007 36.746 8.183 1.00 8.05 ? 105 TYR A O 1 ATOM 156 C CB . TYR A 1 19 ? 21.732 34.754 9.638 1.00 7.01 ? 105 TYR A CB 1 ATOM 157 C CG . TYR A 1 19 ? 22.398 33.827 8.654 1.00 6.08 ? 105 TYR A CG 1 ATOM 158 C CD1 . TYR A 1 19 ? 23.303 32.867 9.069 1.00 8.36 ? 105 TYR A CD1 1 ATOM 159 C CD2 . TYR A 1 19 ? 22.143 33.904 7.295 1.00 6.88 ? 105 TYR A CD2 1 ATOM 160 C CE1 . TYR A 1 19 ? 23.929 32.018 8.164 1.00 8.95 ? 105 TYR A CE1 1 ATOM 161 C CE2 . TYR A 1 19 ? 22.729 33.042 6.399 1.00 7.43 ? 105 TYR A CE2 1 ATOM 162 C CZ . TYR A 1 19 ? 23.630 32.099 6.837 1.00 9.38 ? 105 TYR A CZ 1 ATOM 163 O OH . TYR A 1 19 ? 24.235 31.236 5.932 1.00 8.44 ? 105 TYR A OH 1 ATOM 164 N N . ARG A 1 20 ? 22.017 37.701 8.461 1.00 7.58 ? 106 ARG A N 1 ATOM 165 C CA . ARG A 1 20 ? 22.183 38.608 7.316 1.00 7.56 ? 106 ARG A CA 1 ATOM 166 C C . ARG A 1 20 ? 23.441 39.449 7.499 1.00 8.08 ? 106 ARG A C 1 ATOM 167 O O . ARG A 1 20 ? 24.222 39.659 6.575 1.00 7.48 ? 106 ARG A O 1 ATOM 168 C CB . ARG A 1 20 ? 20.959 39.529 7.147 1.00 8.35 ? 106 ARG A CB 1 ATOM 169 C CG . ARG A 1 20 ? 21.018 40.372 5.857 1.00 9.82 ? 106 ARG A CG 1 ATOM 170 C CD . ARG A 1 20 ? 19.798 41.281 5.680 1.00 10.59 ? 106 ARG A CD 1 ATOM 171 N NE . ARG A 1 20 ? 18.628 40.498 5.264 1.00 9.91 ? 106 ARG A NE 1 ATOM 172 C CZ . ARG A 1 20 ? 17.630 40.068 6.033 1.00 13.67 ? 106 ARG A CZ 1 ATOM 173 N NH1 . ARG A 1 20 ? 17.553 40.333 7.332 1.00 15.51 ? 106 ARG A NH1 1 ATOM 174 N NH2 . ARG A 1 20 ? 16.692 39.333 5.496 1.00 15.24 ? 106 ARG A NH2 1 ATOM 175 N N . SER A 1 21 ? 23.645 39.903 8.731 1.00 8.83 ? 107 SER A N 1 ATOM 176 C CA . SER A 1 21 ? 24.839 40.708 9.060 1.00 8.15 ? 107 SER A CA 1 ATOM 177 C C . SER A 1 21 ? 26.103 39.868 8.996 1.00 7.72 ? 107 SER A C 1 ATOM 178 O O . SER A 1 21 ? 27.118 40.347 8.522 1.00 8.97 ? 107 SER A O 1 ATOM 179 C CB A SER A 1 21 ? 24.768 41.282 10.473 0.50 9.10 ? 107 SER A CB 1 ATOM 180 C CB B SER A 1 21 ? 24.750 41.433 10.410 0.50 9.21 ? 107 SER A CB 1 ATOM 181 O OG A SER A 1 21 ? 23.809 42.319 10.540 0.50 10.70 ? 107 SER A OG 1 ATOM 182 O OG B SER A 1 21 ? 24.851 40.588 11.531 0.50 8.60 ? 107 SER A OG 1 ATOM 183 N N . GLU A 1 22 ? 26.065 38.620 9.413 1.00 7.27 ? 108 GLU A N 1 ATOM 184 C CA . GLU A 1 22 ? 27.243 37.780 9.195 1.00 7.39 ? 108 GLU A CA 1 ATOM 185 C C . GLU A 1 22 ? 27.593 37.680 7.710 1.00 7.32 ? 108 GLU A C 1 ATOM 186 O O . GLU A 1 22 ? 28.748 37.810 7.312 1.00 7.84 ? 108 GLU A O 1 ATOM 187 C CB . GLU A 1 22 ? 27.036 36.390 9.793 1.00 7.55 ? 108 GLU A CB 1 ATOM 188 C CG . GLU A 1 22 ? 26.893 36.403 11.304 1.00 8.56 ? 108 GLU A CG 1 ATOM 189 C CD . GLU A 1 22 ? 26.633 35.009 11.840 1.00 9.30 ? 108 GLU A CD 1 ATOM 190 O OE1 . GLU A 1 22 ? 25.595 34.422 11.447 1.00 9.50 ? 108 GLU A OE1 1 ATOM 191 O OE2 . GLU A 1 22 ? 27.443 34.495 12.641 1.00 9.19 ? 108 GLU A OE2 1 ATOM 192 N N . VAL A 1 23 ? 26.591 37.460 6.852 1.00 7.36 ? 109 VAL A N 1 ATOM 193 C CA . VAL A 1 23 ? 26.907 37.291 5.449 1.00 7.41 ? 109 VAL A CA 1 ATOM 194 C C . VAL A 1 23 ? 27.436 38.585 4.864 1.00 8.19 ? 109 VAL A C 1 ATOM 195 O O . VAL A 1 23 ? 28.466 38.553 4.204 1.00 10.53 ? 109 VAL A O 1 ATOM 196 C CB . VAL A 1 23 ? 25.723 36.749 4.666 1.00 7.58 ? 109 VAL A CB 1 ATOM 197 C CG1 . VAL A 1 23 ? 26.021 36.679 3.209 1.00 8.60 ? 109 VAL A CG1 1 ATOM 198 C CG2 . VAL A 1 23 ? 25.341 35.350 5.205 1.00 8.43 ? 109 VAL A CG2 1 ATOM 199 N N . HIS A 1 24 ? 26.743 39.690 5.104 1.00 8.86 ? 110 HIS A N 1 ATOM 200 C CA . HIS A 1 24 ? 27.151 40.972 4.518 1.00 9.45 ? 110 HIS A CA 1 ATOM 201 C C . HIS A 1 24 ? 28.388 41.584 5.083 1.00 10.55 ? 110 HIS A C 1 ATOM 202 O O . HIS A 1 24 ? 29.163 42.191 4.323 1.00 10.68 ? 110 HIS A O 1 ATOM 203 C CB . HIS A 1 24 ? 26.004 41.955 4.520 1.00 9.87 ? 110 HIS A CB 1 ATOM 204 C CG . HIS A 1 24 ? 24.957 41.582 3.528 1.00 10.40 ? 110 HIS A CG 1 ATOM 205 N ND1 . HIS A 1 24 ? 25.050 41.946 2.200 1.00 14.65 ? 110 HIS A ND1 1 ATOM 206 C CD2 . HIS A 1 24 ? 23.861 40.784 3.634 1.00 9.95 ? 110 HIS A CD2 1 ATOM 207 C CE1 . HIS A 1 24 ? 24.011 41.432 1.553 1.00 15.62 ? 110 HIS A CE1 1 ATOM 208 N NE2 . HIS A 1 24 ? 23.277 40.730 2.405 1.00 10.66 ? 110 HIS A NE2 1 ATOM 209 N N . THR A 1 25 ? 28.632 41.440 6.375 1.00 10.94 ? 111 THR A N 1 ATOM 210 C CA . THR A 1 25 ? 29.780 42.136 6.953 1.00 11.86 ? 111 THR A CA 1 ATOM 211 C C . THR A 1 25 ? 30.989 41.230 7.105 1.00 11.51 ? 111 THR A C 1 ATOM 212 O O . THR A 1 25 ? 32.129 41.734 7.124 1.00 11.50 ? 111 THR A O 1 ATOM 213 C CB . THR A 1 25 ? 29.454 42.797 8.286 1.00 13.84 ? 111 THR A CB 1 ATOM 214 O OG1 . THR A 1 25 ? 29.201 41.814 9.280 1.00 15.43 ? 111 THR A OG1 1 ATOM 215 C CG2 . THR A 1 25 ? 28.190 43.617 8.214 1.00 14.18 ? 111 THR A CG2 1 ATOM 216 N N . LEU A 1 26 ? 30.763 39.910 7.243 1.00 9.45 ? 112 LEU A N 1 ATOM 217 C CA . LEU A 1 26 ? 31.892 38.987 7.406 1.00 10.08 ? 112 LEU A CA 1 ATOM 218 C C . LEU A 1 26 ? 32.249 38.143 6.169 1.00 11.13 ? 112 LEU A C 1 ATOM 219 O O . LEU A 1 26 ? 33.429 37.947 5.865 1.00 13.97 ? 112 LEU A O 1 ATOM 220 C CB . LEU A 1 26 ? 31.700 38.075 8.611 1.00 10.32 ? 112 LEU A CB 1 ATOM 221 C CG . LEU A 1 26 ? 31.218 38.738 9.890 1.00 8.91 ? 112 LEU A CG 1 ATOM 222 C CD1 . LEU A 1 26 ? 30.938 37.742 11.004 1.00 9.01 ? 112 LEU A CD1 1 ATOM 223 C CD2 . LEU A 1 26 ? 32.267 39.775 10.342 1.00 12.41 ? 112 LEU A CD2 1 ATOM 224 N N . ALA A 1 27 ? 31.243 37.679 5.440 1.00 8.28 ? 113 ALA A N 1 ATOM 225 C CA . ALA A 1 27 ? 31.437 36.737 4.322 1.00 9.86 ? 113 ALA A CA 1 ATOM 226 C C . ALA A 1 27 ? 31.735 37.458 3.002 1.00 10.56 ? 113 ALA A C 1 ATOM 227 O O . ALA A 1 27 ? 32.767 37.246 2.403 1.00 10.28 ? 113 ALA A O 1 ATOM 228 C CB . ALA A 1 27 ? 30.278 35.823 4.184 1.00 9.99 ? 113 ALA A CB 1 ATOM 229 N N . ILE A 1 28 ? 30.817 38.329 2.609 1.00 10.46 ? 114 ILE A N 1 ATOM 230 C CA . ILE A 1 28 ? 30.843 38.924 1.267 1.00 9.75 ? 114 ILE A CA 1 ATOM 231 C C . ILE A 1 28 ? 32.151 39.711 1.041 1.00 11.01 ? 114 ILE A C 1 ATOM 232 O O . ILE A 1 28 ? 32.762 39.593 -0.037 1.00 12.77 ? 114 ILE A O 1 ATOM 233 C CB . ILE A 1 28 ? 29.562 39.687 0.939 1.00 10.84 ? 114 ILE A CB 1 ATOM 234 C CG1 . ILE A 1 28 ? 28.447 38.661 0.696 1.00 8.75 ? 114 ILE A CG1 1 ATOM 235 C CG2 . ILE A 1 28 ? 29.725 40.515 -0.327 1.00 10.68 ? 114 ILE A CG2 1 ATOM 236 C CD1 . ILE A 1 28 ? 27.025 39.264 0.643 1.00 12.74 ? 114 ILE A CD1 1 ATOM 237 N N . PRO A 1 29 ? 32.614 40.472 2.036 1.00 12.08 ? 115 PRO A N 1 ATOM 238 C CA . PRO A 1 29 ? 33.853 41.221 1.832 1.00 14.42 ? 115 PRO A CA 1 ATOM 239 C C . PRO A 1 29 ? 35.057 40.372 1.560 1.00 15.79 ? 115 PRO A C 1 ATOM 240 O O . PRO A 1 29 ? 36.047 40.907 1.066 1.00 18.17 ? 115 PRO A O 1 ATOM 241 C CB . PRO A 1 29 ? 33.999 42.019 3.139 1.00 13.46 ? 115 PRO A CB 1 ATOM 242 C CG . PRO A 1 29 ? 32.602 42.207 3.590 1.00 14.14 ? 115 PRO A CG 1 ATOM 243 C CD . PRO A 1 29 ? 32.003 40.857 3.318 1.00 12.28 ? 115 PRO A CD 1 ATOM 244 N N . GLN A 1 30 ? 35.012 39.089 1.886 1.00 16.96 ? 116 GLN A N 1 ATOM 245 C CA . GLN A 1 30 ? 36.123 38.151 1.613 1.00 18.10 ? 116 GLN A CA 1 ATOM 246 C C . GLN A 1 30 ? 35.945 37.422 0.289 1.00 19.18 ? 116 GLN A C 1 ATOM 247 O O . GLN A 1 30 ? 36.764 36.590 -0.050 1.00 20.13 ? 116 GLN A O 1 ATOM 248 C CB . GLN A 1 30 ? 36.227 37.078 2.707 1.00 18.24 ? 116 GLN A CB 1 ATOM 249 C CG . GLN A 1 30 ? 36.460 37.615 4.087 1.00 21.55 ? 116 GLN A CG 1 ATOM 250 C CD . GLN A 1 30 ? 36.725 36.519 5.128 1.00 28.09 ? 116 GLN A CD 1 ATOM 251 O OE1 . GLN A 1 30 ? 37.812 35.923 5.147 1.00 32.73 ? 116 GLN A OE1 1 ATOM 252 N NE2 . GLN A 1 30 ? 35.738 36.270 6.029 1.00 28.67 ? 116 GLN A NE2 1 ATOM 253 N N . ILE A 1 31 ? 34.856 37.704 -0.416 1.00 18.70 ? 117 ILE A N 1 ATOM 254 C CA . ILE A 1 31 ? 34.522 37.013 -1.662 1.00 18.45 ? 117 ILE A CA 1 ATOM 255 C C . ILE A 1 31 ? 34.649 37.999 -2.807 1.00 19.09 ? 117 ILE A C 1 ATOM 256 O O . ILE A 1 31 ? 34.025 39.051 -2.787 1.00 18.82 ? 117 ILE A O 1 ATOM 257 C CB . ILE A 1 31 ? 33.090 36.449 -1.625 1.00 18.57 ? 117 ILE A CB 1 ATOM 258 C CG1 . ILE A 1 31 ? 32.948 35.454 -0.468 1.00 19.67 ? 117 ILE A CG1 1 ATOM 259 C CG2 . ILE A 1 31 ? 32.715 35.756 -2.955 1.00 18.92 ? 117 ILE A CG2 1 ATOM 260 C CD1 . ILE A 1 31 ? 31.500 35.082 -0.129 1.00 19.75 ? 117 ILE A CD1 1 ATOM 261 N N . THR A 1 32 ? 35.439 37.640 -3.809 1.00 19.88 ? 118 THR A N 1 ATOM 262 C CA . THR A 1 32 ? 35.649 38.521 -4.975 1.00 20.09 ? 118 THR A CA 1 ATOM 263 C C . THR A 1 32 ? 34.909 38.097 -6.225 1.00 20.64 ? 118 THR A C 1 ATOM 264 O O . THR A 1 32 ? 34.628 38.916 -7.066 1.00 20.59 ? 118 THR A O 1 ATOM 265 C CB . THR A 1 32 ? 37.135 38.672 -5.312 1.00 20.52 ? 118 THR A CB 1 ATOM 266 O OG1 . THR A 1 32 ? 37.744 37.376 -5.453 1.00 22.23 ? 118 THR A OG1 1 ATOM 267 C CG2 . THR A 1 32 ? 37.851 39.442 -4.168 1.00 21.69 ? 118 THR A CG2 1 ATOM 268 N N . ASP A 1 33 ? 34.585 36.817 -6.316 1.00 19.78 ? 119 ASP A N 1 ATOM 269 C CA . ASP A 1 33 ? 33.876 36.279 -7.481 1.00 20.82 ? 119 ASP A CA 1 ATOM 270 C C . ASP A 1 33 ? 32.424 36.785 -7.554 1.00 19.89 ? 119 ASP A C 1 ATOM 271 O O . ASP A 1 33 ? 31.646 36.563 -6.602 1.00 18.32 ? 119 ASP A O 1 ATOM 272 C CB A ASP A 1 33 ? 33.938 34.763 -7.489 0.55 20.84 ? 119 ASP A CB 1 ATOM 273 C CB B ASP A 1 33 ? 33.875 34.758 -7.398 0.45 20.90 ? 119 ASP A CB 1 ATOM 274 C CG A ASP A 1 33 ? 33.105 34.154 -8.593 0.55 22.09 ? 119 ASP A CG 1 ATOM 275 C CG B ASP A 1 33 ? 33.290 34.095 -8.621 0.45 22.31 ? 119 ASP A CG 1 ATOM 276 O OD1 A ASP A 1 33 ? 33.333 34.463 -9.801 0.55 22.09 ? 119 ASP A OD1 1 ATOM 277 O OD1 B ASP A 1 33 ? 32.078 34.276 -8.931 0.45 23.19 ? 119 ASP A OD1 1 ATOM 278 O OD2 A ASP A 1 33 ? 32.184 33.356 -8.329 0.55 22.58 ? 119 ASP A OD2 1 ATOM 279 O OD2 B ASP A 1 33 ? 34.001 33.339 -9.315 0.45 24.17 ? 119 ASP A OD2 1 ATOM 280 N N . PRO A 1 34 ? 32.061 37.483 -8.624 1.00 18.65 ? 120 PRO A N 1 ATOM 281 C CA . PRO A 1 34 ? 30.716 38.058 -8.744 1.00 18.57 ? 120 PRO A CA 1 ATOM 282 C C . PRO A 1 34 ? 29.589 37.060 -8.489 1.00 19.90 ? 120 PRO A C 1 ATOM 283 O O . PRO A 1 34 ? 28.623 37.392 -7.814 1.00 19.10 ? 120 PRO A O 1 ATOM 284 C CB . PRO A 1 34 ? 30.700 38.573 -10.188 1.00 19.09 ? 120 PRO A CB 1 ATOM 285 C CG . PRO A 1 34 ? 32.136 39.065 -10.329 1.00 18.69 ? 120 PRO A CG 1 ATOM 286 C CD . PRO A 1 34 ? 32.912 37.892 -9.767 1.00 19.90 ? 120 PRO A CD 1 ATOM 287 N N . ALA A 1 35 ? 29.711 35.880 -9.073 1.00 20.45 ? 121 ALA A N 1 ATOM 288 C CA . ALA A 1 35 ? 28.649 34.863 -8.952 1.00 20.72 ? 121 ALA A CA 1 ATOM 289 C C . ALA A 1 35 ? 28.501 34.394 -7.499 1.00 19.31 ? 121 ALA A C 1 ATOM 290 O O . ALA A 1 35 ? 27.382 34.295 -6.995 1.00 19.75 ? 121 ALA A O 1 ATOM 291 C CB . ALA A 1 35 ? 28.883 33.682 -9.874 1.00 21.08 ? 121 ALA A CB 1 ATOM 292 N N . LEU A 1 36 ? 29.612 34.125 -6.841 1.00 18.00 ? 122 LEU A N 1 ATOM 293 C CA . LEU A 1 36 ? 29.571 33.704 -5.415 1.00 18.46 ? 122 LEU A CA 1 ATOM 294 C C . LEU A 1 36 ? 29.079 34.823 -4.494 1.00 16.78 ? 122 LEU A C 1 ATOM 295 O O . LEU A 1 36 ? 28.412 34.553 -3.523 1.00 15.75 ? 122 LEU A O 1 ATOM 296 C CB . LEU A 1 36 ? 30.907 33.188 -4.899 1.00 19.69 ? 122 LEU A CB 1 ATOM 297 C CG . LEU A 1 36 ? 31.359 31.773 -5.283 1.00 23.27 ? 122 LEU A CG 1 ATOM 298 C CD1 . LEU A 1 36 ? 32.732 31.533 -4.695 1.00 26.13 ? 122 LEU A CD1 1 ATOM 299 C CD2 . LEU A 1 36 ? 30.385 30.722 -4.816 1.00 25.39 ? 122 LEU A CD2 1 ATOM 300 N N . ARG A 1 37 ? 29.419 36.081 -4.797 1.00 15.36 ? 123 ARG A N 1 ATOM 301 C CA . ARG A 1 37 ? 28.898 37.184 -3.997 1.00 14.56 ? 123 ARG A CA 1 ATOM 302 C C . ARG A 1 37 ? 27.381 37.258 -4.137 1.00 13.73 ? 123 ARG A C 1 ATOM 303 O O . ARG A 1 37 ? 26.689 37.502 -3.171 1.00 12.74 ? 123 ARG A O 1 ATOM 304 C CB . ARG A 1 37 ? 29.492 38.541 -4.404 1.00 15.12 ? 123 ARG A CB 1 ATOM 305 C CG . ARG A 1 37 ? 30.962 38.681 -4.218 1.00 16.42 ? 123 ARG A CG 1 ATOM 306 C CD . ARG A 1 37 ? 31.478 39.982 -4.854 1.00 14.76 ? 123 ARG A CD 1 ATOM 307 N NE . ARG A 1 37 ? 30.782 41.118 -4.263 1.00 15.30 ? 123 ARG A NE 1 ATOM 308 C CZ . ARG A 1 37 ? 31.142 41.728 -3.140 1.00 13.41 ? 123 ARG A CZ 1 ATOM 309 N NH1 . ARG A 1 37 ? 32.219 41.371 -2.461 1.00 15.39 ? 123 ARG A NH1 1 ATOM 310 N NH2 . ARG A 1 37 ? 30.425 42.734 -2.694 1.00 16.79 ? 123 ARG A NH2 1 ATOM 311 N N . ALA A 1 38 ? 26.872 37.069 -5.358 1.00 13.60 ? 124 ALA A N 1 ATOM 312 C CA . ALA A 1 38 ? 25.421 37.164 -5.580 1.00 13.57 ? 124 ALA A CA 1 ATOM 313 C C . ALA A 1 38 ? 24.723 35.977 -4.899 1.00 13.00 ? 124 ALA A C 1 ATOM 314 O O . ALA A 1 38 ? 23.628 36.121 -4.346 1.00 13.91 ? 124 ALA A O 1 ATOM 315 C CB . ALA A 1 38 ? 25.064 37.185 -7.051 1.00 15.24 ? 124 ALA A CB 1 ATOM 316 N N . ALA A 1 39 ? 25.375 34.835 -4.949 1.00 12.15 ? 125 ALA A N 1 ATOM 317 C CA . ALA A 1 39 ? 24.853 33.621 -4.285 1.00 12.15 ? 125 ALA A CA 1 ATOM 318 C C . ALA A 1 39 ? 24.826 33.831 -2.771 1.00 11.54 ? 125 ALA A C 1 ATOM 319 O O . ALA A 1 39 ? 23.863 33.496 -2.077 1.00 12.54 ? 125 ALA A O 1 ATOM 320 C CB . ALA A 1 39 ? 25.707 32.434 -4.644 1.00 13.40 ? 125 ALA A CB 1 ATOM 321 N N . ALA A 1 40 ? 25.890 34.419 -2.246 1.00 10.70 ? 126 ALA A N 1 ATOM 322 C CA . ALA A 1 40 ? 25.950 34.721 -0.823 1.00 10.15 ? 126 ALA A CA 1 ATOM 323 C C . ALA A 1 40 ? 24.814 35.679 -0.405 1.00 9.90 ? 126 ALA A C 1 ATOM 324 O O . ALA A 1 40 ? 24.167 35.509 0.632 1.00 8.90 ? 126 ALA A O 1 ATOM 325 C CB . ALA A 1 40 ? 27.331 35.323 -0.468 1.00 9.90 ? 126 ALA A CB 1 ATOM 326 N N . SER A 1 41 ? 24.637 36.745 -1.187 1.00 9.82 ? 127 SER A N 1 ATOM 327 C CA . SER A 1 41 ? 23.567 37.689 -0.915 1.00 10.41 ? 127 SER A CA 1 ATOM 328 C C . SER A 1 41 ? 22.218 36.997 -0.855 1.00 9.19 ? 127 SER A C 1 ATOM 329 O O . SER A 1 41 ? 21.365 37.320 -0.015 1.00 10.07 ? 127 SER A O 1 ATOM 330 C CB A SER A 1 41 ? 23.579 38.821 -1.946 0.60 11.51 ? 127 SER A CB 1 ATOM 331 C CB B SER A 1 41 ? 23.522 38.796 -1.968 0.40 11.13 ? 127 SER A CB 1 ATOM 332 O OG A SER A 1 41 ? 22.673 39.818 -1.546 0.60 9.98 ? 127 SER A OG 1 ATOM 333 O OG B SER A 1 41 ? 24.596 39.677 -1.768 0.40 10.67 ? 127 SER A OG 1 ATOM 334 N N . ALA A 1 42 ? 22.027 36.019 -1.728 1.00 9.04 ? 128 ALA A N 1 ATOM 335 C CA . ALA A 1 42 ? 20.753 35.286 -1.788 1.00 8.96 ? 128 ALA A CA 1 ATOM 336 C C . ALA A 1 42 ? 20.562 34.392 -0.560 1.00 8.64 ? 128 ALA A C 1 ATOM 337 O O . ALA A 1 42 ? 19.459 34.269 -0.035 1.00 8.80 ? 128 ALA A O 1 ATOM 338 C CB . ALA A 1 42 ? 20.643 34.480 -3.063 1.00 9.58 ? 128 ALA A CB 1 ATOM 339 N N . VAL A 1 43 ? 21.629 33.745 -0.126 1.00 8.48 ? 129 VAL A N 1 ATOM 340 C CA . VAL A 1 43 ? 21.559 32.849 1.049 1.00 9.58 ? 129 VAL A CA 1 ATOM 341 C C . VAL A 1 43 ? 21.254 33.650 2.337 1.00 8.71 ? 129 VAL A C 1 ATOM 342 O O . VAL A 1 43 ? 20.512 33.203 3.207 1.00 8.18 ? 129 VAL A O 1 ATOM 343 C CB . VAL A 1 43 ? 22.708 31.848 1.180 1.00 10.55 ? 129 VAL A CB 1 ATOM 344 C CG1 . VAL A 1 43 ? 23.921 32.507 1.629 1.00 13.59 ? 129 VAL A CG1 1 ATOM 345 C CG2 . VAL A 1 43 ? 22.345 30.735 2.178 1.00 13.98 ? 129 VAL A CG2 1 ATOM 346 N N . ALA A 1 44 ? 21.695 34.907 2.384 1.00 8.53 ? 130 ALA A N 1 ATOM 347 C CA . ALA A 1 44 ? 21.380 35.763 3.519 1.00 7.86 ? 130 ALA A CA 1 ATOM 348 C C . ALA A 1 44 ? 19.884 36.000 3.737 1.00 8.93 ? 130 ALA A C 1 ATOM 349 O O . ALA A 1 44 ? 19.463 36.431 4.822 1.00 8.78 ? 130 ALA A O 1 ATOM 350 C CB . ALA A 1 44 ? 22.064 37.110 3.371 1.00 8.72 ? 130 ALA A CB 1 ATOM 351 N N . GLU A 1 45 ? 19.113 35.837 2.664 1.00 9.25 ? 131 GLU A N 1 ATOM 352 C CA . GLU A 1 45 ? 17.647 36.002 2.717 1.00 8.80 ? 131 GLU A CA 1 ATOM 353 C C . GLU A 1 45 ? 16.893 34.709 2.994 1.00 8.49 ? 131 GLU A C 1 ATOM 354 O O . GLU A 1 45 ? 15.655 34.719 3.036 1.00 9.32 ? 131 GLU A O 1 ATOM 355 C CB . GLU A 1 45 ? 17.149 36.603 1.402 1.00 10.47 ? 131 GLU A CB 1 ATOM 356 C CG . GLU A 1 45 ? 17.897 37.887 1.051 1.00 10.32 ? 131 GLU A CG 1 ATOM 357 C CD . GLU A 1 45 ? 17.709 38.937 2.125 1.00 13.69 ? 131 GLU A CD 1 ATOM 358 O OE1 . GLU A 1 45 ? 16.564 39.116 2.573 1.00 17.98 ? 131 GLU A OE1 1 ATOM 359 O OE2 . GLU A 1 45 ? 18.702 39.548 2.567 1.00 13.82 ? 131 GLU A OE2 1 ATOM 360 N N . VAL A 1 46 ? 17.621 33.602 3.166 1.00 6.95 ? 132 VAL A N 1 ATOM 361 C CA . VAL A 1 46 ? 16.953 32.339 3.498 1.00 6.98 ? 132 VAL A CA 1 ATOM 362 C C . VAL A 1 46 ? 16.678 32.301 5.024 1.00 6.97 ? 132 VAL A C 1 ATOM 363 O O . VAL A 1 46 ? 17.585 32.561 5.824 1.00 7.76 ? 132 VAL A O 1 ATOM 364 C CB . VAL A 1 46 ? 17.744 31.127 3.054 1.00 7.00 ? 132 VAL A CB 1 ATOM 365 C CG1 . VAL A 1 46 ? 16.997 29.832 3.444 1.00 6.42 ? 132 VAL A CG1 1 ATOM 366 C CG2 . VAL A 1 46 ? 18.002 31.132 1.566 1.00 7.51 ? 132 VAL A CG2 1 ATOM 367 N N . PRO A 1 47 ? 15.438 32.072 5.439 1.00 7.35 ? 133 PRO A N 1 ATOM 368 C CA . PRO A 1 47 ? 15.078 32.193 6.857 1.00 7.70 ? 133 PRO A CA 1 ATOM 369 C C . PRO A 1 47 ? 15.472 30.982 7.712 1.00 9.00 ? 133 PRO A C 1 ATOM 370 O O . PRO A 1 47 ? 14.761 29.970 7.734 1.00 9.32 ? 133 PRO A O 1 ATOM 371 C CB . PRO A 1 47 ? 13.589 32.391 6.818 1.00 8.95 ? 133 PRO A CB 1 ATOM 372 C CG . PRO A 1 47 ? 13.161 31.726 5.602 1.00 7.60 ? 133 PRO A CG 1 ATOM 373 C CD . PRO A 1 47 ? 14.256 31.839 4.600 1.00 7.15 ? 133 PRO A CD 1 ATOM 374 N N . SER A 1 48 ? 16.559 31.137 8.446 1.00 8.44 ? 134 SER A N 1 ATOM 375 C CA . SER A 1 48 ? 17.069 30.100 9.347 1.00 6.59 ? 134 SER A CA 1 ATOM 376 C C . SER A 1 48 ? 16.705 30.461 10.798 1.00 6.53 ? 134 SER A C 1 ATOM 377 O O . SER A 1 48 ? 16.481 31.627 11.129 1.00 6.31 ? 134 SER A O 1 ATOM 378 C CB . SER A 1 48 ? 18.589 29.936 9.219 1.00 7.18 ? 134 SER A CB 1 ATOM 379 O OG . SER A 1 48 ? 19.310 31.161 9.238 1.00 7.48 ? 134 SER A OG 1 ATOM 380 N N . PHE A 1 49 ? 16.748 29.447 11.664 1.00 7.06 ? 135 PHE A N 1 ATOM 381 C CA . PHE A 1 49 ? 16.503 29.663 13.080 1.00 6.91 ? 135 PHE A CA 1 ATOM 382 C C . PHE A 1 49 ? 17.601 30.542 13.682 1.00 6.57 ? 135 PHE A C 1 ATOM 383 O O . PHE A 1 49 ? 18.758 30.446 13.336 1.00 5.81 ? 135 PHE A O 1 ATOM 384 C CB . PHE A 1 49 ? 16.438 28.329 13.860 1.00 6.04 ? 135 PHE A CB 1 ATOM 385 C CG . PHE A 1 49 ? 15.092 27.637 13.816 1.00 5.57 ? 135 PHE A CG 1 ATOM 386 C CD1 . PHE A 1 49 ? 14.591 27.102 12.619 1.00 5.02 ? 135 PHE A CD1 1 ATOM 387 C CD2 . PHE A 1 49 ? 14.338 27.528 14.959 1.00 6.01 ? 135 PHE A CD2 1 ATOM 388 C CE1 . PHE A 1 49 ? 13.353 26.486 12.582 1.00 5.10 ? 135 PHE A CE1 1 ATOM 389 C CE2 . PHE A 1 49 ? 13.101 26.967 14.943 1.00 6.65 ? 135 PHE A CE2 1 ATOM 390 C CZ . PHE A 1 49 ? 12.610 26.427 13.747 1.00 4.26 ? 135 PHE A CZ 1 ATOM 391 N N . GLN A 1 50 ? 17.197 31.312 14.682 1.00 6.99 ? 136 GLN A N 1 ATOM 392 C CA . GLN A 1 50 ? 18.076 32.128 15.502 1.00 6.76 ? 136 GLN A CA 1 ATOM 393 C C . GLN A 1 50 ? 18.191 31.423 16.858 1.00 8.13 ? 136 GLN A C 1 ATOM 394 O O . GLN A 1 50 ? 17.187 31.048 17.443 1.00 8.27 ? 136 GLN A O 1 ATOM 395 C CB . GLN A 1 50 ? 17.505 33.537 15.665 1.00 7.71 ? 136 GLN A CB 1 ATOM 396 C CG . GLN A 1 50 ? 18.417 34.325 16.531 1.00 12.87 ? 136 GLN A CG 1 ATOM 397 C CD . GLN A 1 50 ? 18.154 35.787 16.469 1.00 16.98 ? 136 GLN A CD 1 ATOM 398 O OE1 . GLN A 1 50 ? 17.233 36.274 17.106 1.00 20.52 ? 136 GLN A OE1 1 ATOM 399 N NE2 . GLN A 1 50 ? 18.980 36.488 15.741 1.00 20.75 ? 136 GLN A NE2 1 ATOM 400 N N . TRP A 1 51 ? 19.424 31.211 17.322 1.00 8.12 ? 137 TRP A N 1 ATOM 401 C CA . TRP A 1 51 ? 19.671 30.381 18.509 1.00 6.76 ? 137 TRP A CA 1 ATOM 402 C C . TRP A 1 51 ? 19.891 31.214 19.756 1.00 6.71 ? 137 TRP A C 1 ATOM 403 O O . TRP A 1 51 ? 20.737 32.108 19.757 1.00 7.88 ? 137 TRP A O 1 ATOM 404 C CB . TRP A 1 51 ? 20.882 29.486 18.308 1.00 6.77 ? 137 TRP A CB 1 ATOM 405 C CG . TRP A 1 51 ? 20.711 28.418 17.278 1.00 6.91 ? 137 TRP A CG 1 ATOM 406 C CD1 . TRP A 1 51 ? 20.316 28.573 15.990 1.00 7.94 ? 137 TRP A CD1 1 ATOM 407 C CD2 . TRP A 1 51 ? 20.994 27.028 17.448 1.00 7.15 ? 137 TRP A CD2 1 ATOM 408 N NE1 . TRP A 1 51 ? 20.305 27.355 15.347 1.00 7.41 ? 137 TRP A NE1 1 ATOM 409 C CE2 . TRP A 1 51 ? 20.743 26.390 16.205 1.00 7.27 ? 137 TRP A CE2 1 ATOM 410 C CE3 . TRP A 1 51 ? 21.464 26.267 18.505 1.00 8.65 ? 137 TRP A CE3 1 ATOM 411 C CZ2 . TRP A 1 51 ? 20.919 25.019 16.017 1.00 9.03 ? 137 TRP A CZ2 1 ATOM 412 C CZ3 . TRP A 1 51 ? 21.637 24.894 18.332 1.00 7.83 ? 137 TRP A CZ3 1 ATOM 413 C CH2 . TRP A 1 51 ? 21.357 24.281 17.086 1.00 9.24 ? 137 TRP A CH2 1 ATOM 414 N N . LEU A 1 52 ? 19.186 30.873 20.835 1.00 6.25 ? 138 LEU A N 1 ATOM 415 C CA . LEU A 1 52 ? 19.455 31.474 22.137 1.00 7.00 ? 138 LEU A CA 1 ATOM 416 C C . LEU A 1 52 ? 20.370 30.510 22.907 1.00 6.79 ? 138 LEU A C 1 ATOM 417 O O . LEU A 1 52 ? 20.000 29.915 23.924 1.00 8.86 ? 138 LEU A O 1 ATOM 418 C CB . LEU A 1 52 ? 18.164 31.738 22.913 1.00 6.19 ? 138 LEU A CB 1 ATOM 419 C CG . LEU A 1 52 ? 17.067 32.487 22.116 1.00 6.78 ? 138 LEU A CG 1 ATOM 420 C CD1 . LEU A 1 52 ? 15.857 32.667 23.016 1.00 6.93 ? 138 LEU A CD1 1 ATOM 421 C CD2 . LEU A 1 52 ? 17.548 33.813 21.531 1.00 7.54 ? 138 LEU A CD2 1 ATOM 422 N N . ASP A 1 53 ? 21.588 30.402 22.404 1.00 6.50 ? 139 ASP A N 1 ATOM 423 C CA . ASP A 1 53 ? 22.561 29.447 22.937 1.00 7.31 ? 139 ASP A CA 1 ATOM 424 C C . ASP A 1 53 ? 23.423 30.031 24.051 1.00 8.02 ? 139 ASP A C 1 ATOM 425 O O . ASP A 1 53 ? 24.257 29.340 24.640 1.00 9.26 ? 139 ASP A O 1 ATOM 426 C CB . ASP A 1 53 ? 23.450 28.933 21.811 1.00 8.50 ? 139 ASP A CB 1 ATOM 427 C CG . ASP A 1 53 ? 24.275 30.010 21.187 1.00 13.24 ? 139 ASP A CG 1 ATOM 428 O OD1 . ASP A 1 53 ? 23.877 31.197 21.120 1.00 15.78 ? 139 ASP A OD1 1 ATOM 429 O OD2 . ASP A 1 53 ? 25.407 29.747 20.781 1.00 21.89 ? 139 ASP A OD2 1 ATOM 430 N N . ARG A 1 54 ? 23.208 31.312 24.338 1.00 8.60 ? 140 ARG A N 1 ATOM 431 C CA . ARG A 1 54 ? 23.857 31.961 25.477 1.00 8.89 ? 140 ARG A CA 1 ATOM 432 C C . ARG A 1 54 ? 22.846 32.915 26.079 1.00 8.59 ? 140 ARG A C 1 ATOM 433 O O . ARG A 1 54 ? 22.113 33.555 25.355 1.00 8.08 ? 140 ARG A O 1 ATOM 434 C CB . ARG A 1 54 ? 25.052 32.829 25.045 1.00 11.73 ? 140 ARG A CB 1 ATOM 435 C CG . ARG A 1 54 ? 25.992 32.138 24.053 1.00 20.65 ? 140 ARG A CG 1 ATOM 436 C CD . ARG A 1 54 ? 26.879 33.085 23.325 1.00 27.97 ? 140 ARG A CD 1 ATOM 437 N NE . ARG A 1 54 ? 28.121 33.240 24.069 1.00 36.96 ? 140 ARG A NE 1 ATOM 438 C CZ . ARG A 1 54 ? 29.280 32.697 23.685 1.00 38.96 ? 140 ARG A CZ 1 ATOM 439 N NH1 . ARG A 1 54 ? 29.341 32.031 22.545 1.00 38.75 ? 140 ARG A NH1 1 ATOM 440 N NH2 . ARG A 1 54 ? 30.380 32.845 24.420 1.00 39.22 ? 140 ARG A NH2 1 ATOM 441 N N . ASN A 1 55 ? 22.867 33.056 27.379 1.00 8.04 ? 141 ASN A N 1 ATOM 442 C CA . ASN A 1 55 ? 21.885 33.883 28.090 1.00 7.49 ? 141 ASN A CA 1 ATOM 443 C C . ASN A 1 55 ? 21.788 35.320 27.569 1.00 8.20 ? 141 ASN A C 1 ATOM 444 O O . ASN A 1 55 ? 20.677 35.919 27.530 1.00 7.12 ? 141 ASN A O 1 ATOM 445 C CB . ASN A 1 55 ? 22.157 33.821 29.590 1.00 6.43 ? 141 ASN A CB 1 ATOM 446 C CG . ASN A 1 55 ? 21.117 34.536 30.400 1.00 6.89 ? 141 ASN A CG 1 ATOM 447 O OD1 . ASN A 1 55 ? 19.920 34.268 30.249 1.00 7.34 ? 141 ASN A OD1 1 ATOM 448 N ND2 . ASN A 1 55 ? 21.567 35.449 31.286 1.00 8.08 ? 141 ASN A ND2 1 ATOM 449 N N . VAL A 1 56 ? 22.925 35.907 27.194 1.00 7.49 ? 142 VAL A N 1 ATOM 450 C CA . VAL A 1 56 ? 22.978 37.290 26.674 1.00 7.55 ? 142 VAL A CA 1 ATOM 451 C C . VAL A 1 56 ? 22.097 37.528 25.422 1.00 7.37 ? 142 VAL A C 1 ATOM 452 O O . VAL A 1 56 ? 21.708 38.684 25.162 1.00 8.91 ? 142 VAL A O 1 ATOM 453 C CB A VAL A 1 56 ? 24.436 37.745 26.376 0.50 8.48 ? 142 VAL A CB 1 ATOM 454 C CB B VAL A 1 56 ? 24.430 37.784 26.429 0.50 8.50 ? 142 VAL A CB 1 ATOM 455 C CG1 A VAL A 1 56 ? 25.052 37.030 25.177 0.50 8.20 ? 142 VAL A CG1 1 ATOM 456 C CG1 B VAL A 1 56 ? 25.113 38.047 27.773 0.50 7.72 ? 142 VAL A CG1 1 ATOM 457 C CG2 A VAL A 1 56 ? 24.467 39.214 26.127 0.50 9.22 ? 142 VAL A CG2 1 ATOM 458 C CG2 B VAL A 1 56 ? 25.248 36.810 25.584 0.50 9.23 ? 142 VAL A CG2 1 ATOM 459 N N . THR A 1 57 ? 21.737 36.456 24.719 1.00 7.22 ? 143 THR A N 1 ATOM 460 C CA . THR A 1 57 ? 20.932 36.543 23.488 1.00 7.28 ? 143 THR A CA 1 ATOM 461 C C . THR A 1 57 ? 19.472 36.908 23.809 1.00 7.82 ? 143 THR A C 1 ATOM 462 O O . THR A 1 57 ? 18.767 37.415 22.964 1.00 8.58 ? 143 THR A O 1 ATOM 463 C CB . THR A 1 57 ? 20.976 35.299 22.628 1.00 7.18 ? 143 THR A CB 1 ATOM 464 O OG1 . THR A 1 57 ? 20.407 34.229 23.374 1.00 6.45 ? 143 THR A OG1 1 ATOM 465 C CG2 . THR A 1 57 ? 22.422 34.939 22.281 1.00 9.36 ? 143 THR A CG2 1 ATOM 466 N N . VAL A 1 58 ? 19.036 36.639 25.033 1.00 6.11 ? 144 VAL A N 1 ATOM 467 C CA . VAL A 1 58 ? 17.618 36.798 25.387 1.00 6.73 ? 144 VAL A CA 1 ATOM 468 C C . VAL A 1 58 ? 17.190 38.250 25.324 1.00 8.36 ? 144 VAL A C 1 ATOM 469 O O . VAL A 1 58 ? 16.244 38.605 24.610 1.00 8.31 ? 144 VAL A O 1 ATOM 470 C CB . VAL A 1 58 ? 17.306 36.154 26.745 1.00 7.42 ? 144 VAL A CB 1 ATOM 471 C CG1 . VAL A 1 58 ? 15.865 36.414 27.177 1.00 7.62 ? 144 VAL A CG1 1 ATOM 472 C CG2 . VAL A 1 58 ? 17.536 34.661 26.680 1.00 7.20 ? 144 VAL A CG2 1 ATOM 473 N N . ASP A 1 59 ? 17.904 39.117 26.045 1.00 8.60 ? 145 ASP A N 1 ATOM 474 C CA . ASP A 1 59 ? 17.568 40.529 26.082 1.00 8.71 ? 145 ASP A CA 1 ATOM 475 C C . ASP A 1 59 ? 18.202 41.362 24.950 1.00 9.16 ? 145 ASP A C 1 ATOM 476 O O . ASP A 1 59 ? 18.014 42.584 24.881 1.00 11.73 ? 145 ASP A O 1 ATOM 477 C CB . ASP A 1 59 ? 17.831 41.115 27.479 1.00 8.08 ? 145 ASP A CB 1 ATOM 478 C CG . ASP A 1 59 ? 16.598 41.139 28.316 1.00 9.78 ? 145 ASP A CG 1 ATOM 479 O OD1 . ASP A 1 59 ? 15.631 41.876 27.948 1.00 11.39 ? 145 ASP A OD1 1 ATOM 480 O OD2 . ASP A 1 59 ? 16.482 40.450 29.352 1.00 9.95 ? 145 ASP A OD2 1 ATOM 481 N N . THR A 1 60 ? 18.923 40.700 24.065 1.00 9.24 ? 146 THR A N 1 ATOM 482 C CA . THR A 1 60 ? 19.472 41.360 22.873 1.00 9.28 ? 146 THR A CA 1 ATOM 483 C C . THR A 1 60 ? 18.782 40.817 21.611 1.00 9.62 ? 146 THR A C 1 ATOM 484 O O . THR A 1 60 ? 17.791 41.396 21.150 1.00 10.45 ? 146 THR A O 1 ATOM 485 C CB . THR A 1 60 ? 21.014 41.229 22.767 1.00 10.23 ? 146 THR A CB 1 ATOM 486 O OG1 . THR A 1 60 ? 21.440 39.847 22.859 1.00 9.77 ? 146 THR A OG1 1 ATOM 487 C CG2 . THR A 1 60 ? 21.708 41.980 23.904 1.00 10.43 ? 146 THR A CG2 1 ATOM 488 N N . LEU A 1 61 ? 19.323 39.729 21.075 1.00 9.32 ? 147 LEU A N 1 ATOM 489 C CA . LEU A 1 61 ? 18.868 39.115 19.830 1.00 9.09 ? 147 LEU A CA 1 ATOM 490 C C . LEU A 1 61 ? 17.387 38.797 19.808 1.00 9.08 ? 147 LEU A C 1 ATOM 491 O O . LEU A 1 61 ? 16.717 39.094 18.809 1.00 10.34 ? 147 LEU A O 1 ATOM 492 C CB . LEU A 1 61 ? 19.635 37.824 19.550 1.00 9.59 ? 147 LEU A CB 1 ATOM 493 C CG . LEU A 1 61 ? 21.143 37.937 19.420 1.00 14.67 ? 147 LEU A CG 1 ATOM 494 C CD1 . LEU A 1 61 ? 21.684 36.606 18.935 1.00 14.59 ? 147 LEU A CD1 1 ATOM 495 C CD2 . LEU A 1 61 ? 21.511 39.079 18.475 1.00 17.94 ? 147 LEU A CD2 1 ATOM 496 N N . LEU A 1 62 ? 16.856 38.185 20.867 1.00 7.79 ? 148 LEU A N 1 ATOM 497 C CA . LEU A 1 62 ? 15.444 37.781 20.852 1.00 7.38 ? 148 LEU A CA 1 ATOM 498 C C . LEU A 1 62 ? 14.536 39.012 20.739 1.00 7.16 ? 148 LEU A C 1 ATOM 499 O O . LEU A 1 62 ? 13.663 39.101 19.863 1.00 7.91 ? 148 LEU A O 1 ATOM 500 C CB . LEU A 1 62 ? 15.038 36.911 22.053 1.00 7.42 ? 148 LEU A CB 1 ATOM 501 C CG . LEU A 1 62 ? 13.562 36.471 22.087 1.00 5.03 ? 148 LEU A CG 1 ATOM 502 C CD1 . LEU A 1 62 ? 13.217 35.596 20.919 1.00 6.39 ? 148 LEU A CD1 1 ATOM 503 C CD2 . LEU A 1 62 ? 13.257 35.858 23.434 1.00 7.14 ? 148 LEU A CD2 1 ATOM 504 N N . VAL A 1 63 ? 14.796 40.003 21.549 1.00 7.96 ? 149 VAL A N 1 ATOM 505 C CA . VAL A 1 63 ? 14.018 41.238 21.528 1.00 8.24 ? 149 VAL A CA 1 ATOM 506 C C . VAL A 1 63 ? 14.146 41.942 20.162 1.00 8.19 ? 149 VAL A C 1 ATOM 507 O O . VAL A 1 63 ? 13.167 42.429 19.612 1.00 7.97 ? 149 VAL A O 1 ATOM 508 C CB . VAL A 1 63 ? 14.431 42.154 22.678 1.00 8.87 ? 149 VAL A CB 1 ATOM 509 C CG1 . VAL A 1 63 ? 13.739 43.540 22.591 1.00 10.68 ? 149 VAL A CG1 1 ATOM 510 C CG2 . VAL A 1 63 ? 14.112 41.506 24.000 1.00 8.41 ? 149 VAL A CG2 1 ATOM 511 N N . GLN A 1 64 ? 15.361 42.018 19.657 1.00 8.93 ? 150 GLN A N 1 ATOM 512 C CA . GLN A 1 64 ? 15.646 42.652 18.362 1.00 10.43 ? 150 GLN A CA 1 ATOM 513 C C . GLN A 1 64 ? 14.879 42.002 17.220 1.00 8.97 ? 150 GLN A C 1 ATOM 514 O O . GLN A 1 64 ? 14.185 42.668 16.457 1.00 10.36 ? 150 GLN A O 1 ATOM 515 C CB . GLN A 1 64 ? 17.144 42.628 18.054 1.00 11.17 ? 150 GLN A CB 1 ATOM 516 C CG . GLN A 1 64 ? 17.943 43.461 19.000 1.00 17.26 ? 150 GLN A CG 1 ATOM 517 C CD . GLN A 1 64 ? 19.468 43.268 18.981 1.00 24.50 ? 150 GLN A CD 1 ATOM 518 O OE1 . GLN A 1 64 ? 20.159 43.982 19.720 1.00 28.90 ? 150 GLN A OE1 1 ATOM 519 N NE2 . GLN A 1 64 ? 19.987 42.323 18.204 1.00 24.19 ? 150 GLN A NE2 1 ATOM 520 N N . THR A 1 65 ? 14.967 40.690 17.126 1.00 8.16 ? 151 THR A N 1 ATOM 521 C CA . THR A 1 65 ? 14.293 39.946 16.053 1.00 9.11 ? 151 THR A CA 1 ATOM 522 C C . THR A 1 65 ? 12.793 40.093 16.136 1.00 8.41 ? 151 THR A C 1 ATOM 523 O O . THR A 1 65 ? 12.151 40.364 15.118 1.00 8.99 ? 151 THR A O 1 ATOM 524 C CB . THR A 1 65 ? 14.697 38.482 16.071 1.00 9.68 ? 151 THR A CB 1 ATOM 525 O OG1 . THR A 1 65 ? 16.097 38.432 15.678 1.00 10.94 ? 151 THR A OG1 1 ATOM 526 C CG2 . THR A 1 65 ? 13.893 37.673 15.036 1.00 9.97 ? 151 THR A CG2 1 ATOM 527 N N . LEU A 1 66 ? 12.221 39.915 17.312 1.00 7.55 ? 152 LEU A N 1 ATOM 528 C CA . LEU A 1 66 ? 10.769 40.049 17.460 1.00 7.09 ? 152 LEU A CA 1 ATOM 529 C C . LEU A 1 66 ? 10.332 41.486 17.166 1.00 7.69 ? 152 LEU A C 1 ATOM 530 O O . LEU A 1 66 ? 9.276 41.688 16.569 1.00 8.75 ? 152 LEU A O 1 ATOM 531 C CB . LEU A 1 66 ? 10.285 39.629 18.838 1.00 7.20 ? 152 LEU A CB 1 ATOM 532 C CG . LEU A 1 66 ? 10.553 38.160 19.171 1.00 7.22 ? 152 LEU A CG 1 ATOM 533 C CD1 . LEU A 1 66 ? 10.241 37.793 20.598 1.00 8.22 ? 152 LEU A CD1 1 ATOM 534 C CD2 . LEU A 1 66 ? 9.773 37.252 18.153 1.00 12.06 ? 152 LEU A CD2 1 ATOM 535 N N . SER A 1 67 ? 11.145 42.452 17.565 1.00 8.63 ? 153 SER A N 1 ATOM 536 C CA . SER A 1 67 ? 10.808 43.867 17.295 1.00 9.08 ? 153 SER A CA 1 ATOM 537 C C . SER A 1 67 ? 10.813 44.135 15.799 1.00 8.66 ? 153 SER A C 1 ATOM 538 O O . SER A 1 67 ? 9.933 44.853 15.274 1.00 9.01 ? 153 SER A O 1 ATOM 539 C CB . SER A 1 67 ? 11.853 44.773 17.959 1.00 9.18 ? 153 SER A CB 1 ATOM 540 O OG . SER A 1 67 ? 11.716 44.764 19.358 1.00 13.70 ? 153 SER A OG 1 ATOM 541 N N . GLU A 1 68 ? 11.817 43.596 15.115 1.00 6.90 ? 154 GLU A N 1 ATOM 542 C CA . GLU A 1 68 ? 11.959 43.748 13.674 1.00 8.74 ? 154 GLU A CA 1 ATOM 543 C C . GLU A 1 68 ? 10.822 43.079 12.900 1.00 8.98 ? 154 GLU A C 1 ATOM 544 O O . GLU A 1 68 ? 10.316 43.647 11.906 1.00 9.07 ? 154 GLU A O 1 ATOM 545 C CB . GLU A 1 68 ? 13.315 43.302 13.159 1.00 9.67 ? 154 GLU A CB 1 ATOM 546 C CG . GLU A 1 68 ? 14.413 44.212 13.717 1.00 11.29 ? 154 GLU A CG 1 ATOM 547 C CD . GLU A 1 68 ? 15.831 43.716 13.471 1.00 17.59 ? 154 GLU A CD 1 ATOM 548 O OE1 . GLU A 1 68 ? 15.989 42.582 12.999 1.00 16.34 ? 154 GLU A OE1 1 ATOM 549 O OE2 . GLU A 1 68 ? 16.810 44.472 13.743 1.00 17.86 ? 154 GLU A OE2 1 ATOM 550 N N . ILE A 1 69 ? 10.393 41.918 13.395 1.00 8.86 ? 155 ILE A N 1 ATOM 551 C CA . ILE A 1 69 ? 9.260 41.208 12.776 1.00 8.94 ? 155 ILE A CA 1 ATOM 552 C C . ILE A 1 69 ? 7.954 42.000 12.967 1.00 8.51 ? 155 ILE A C 1 ATOM 553 O O . ILE A 1 69 ? 7.184 42.198 11.982 1.00 8.73 ? 155 ILE A O 1 ATOM 554 C CB . ILE A 1 69 ? 9.093 39.800 13.288 1.00 8.27 ? 155 ILE A CB 1 ATOM 555 C CG1 . ILE A 1 69 ? 10.285 38.952 12.852 1.00 9.09 ? 155 ILE A CG1 1 ATOM 556 C CG2 . ILE A 1 69 ? 7.813 39.196 12.754 1.00 8.35 ? 155 ILE A CG2 1 ATOM 557 C CD1 . ILE A 1 69 ? 10.424 37.629 13.589 1.00 6.67 ? 155 ILE A CD1 1 ATOM 558 N N . ARG A 1 70 ? 7.749 42.511 14.166 1.00 8.48 ? 156 ARG A N 1 ATOM 559 C CA . ARG A 1 70 ? 6.552 43.321 14.431 1.00 8.94 ? 156 ARG A CA 1 ATOM 560 C C . ARG A 1 70 ? 6.541 44.514 13.454 1.00 10.06 ? 156 ARG A C 1 ATOM 561 O O . ARG A 1 70 ? 5.530 44.785 12.857 1.00 9.94 ? 156 ARG A O 1 ATOM 562 C CB . ARG A 1 70 ? 6.475 43.812 15.861 1.00 8.97 ? 156 ARG A CB 1 ATOM 563 C CG . ARG A 1 70 ? 5.458 44.877 16.092 1.00 6.08 ? 156 ARG A CG 1 ATOM 564 C CD . ARG A 1 70 ? 5.494 45.404 17.491 1.00 11.28 ? 156 ARG A CD 1 ATOM 565 N NE . ARG A 1 70 ? 4.937 44.433 18.422 1.00 10.59 ? 156 ARG A NE 1 ATOM 566 C CZ . ARG A 1 70 ? 5.069 44.502 19.735 1.00 11.42 ? 156 ARG A CZ 1 ATOM 567 N NH1 . ARG A 1 70 ? 5.775 45.471 20.296 1.00 14.53 ? 156 ARG A NH1 1 ATOM 568 N NH2 . ARG A 1 70 ? 4.490 43.592 20.496 1.00 12.52 ? 156 ARG A NH2 1 ATOM 569 N N . GLU A 1 71 ? 7.679 45.189 13.330 1.00 9.88 ? 157 GLU A N 1 ATOM 570 C CA . GLU A 1 71 ? 7.795 46.350 12.424 1.00 11.72 ? 157 GLU A CA 1 ATOM 571 C C . GLU A 1 71 ? 7.449 45.955 11.002 1.00 13.09 ? 157 GLU A C 1 ATOM 572 O O . GLU A 1 71 ? 6.717 46.649 10.295 1.00 12.55 ? 157 GLU A O 1 ATOM 573 C CB . GLU A 1 71 ? 9.191 46.983 12.503 1.00 13.21 ? 157 GLU A CB 1 ATOM 574 C CG . GLU A 1 71 ? 9.486 48.058 11.479 1.00 14.92 ? 157 GLU A CG 1 ATOM 575 C CD . GLU A 1 71 ? 10.911 48.569 11.569 1.00 20.35 ? 157 GLU A CD 1 ATOM 576 O OE1 . GLU A 1 71 ? 11.859 47.755 11.554 1.00 23.41 ? 157 GLU A OE1 1 ATOM 577 O OE2 . GLU A 1 71 ? 11.085 49.791 11.666 1.00 26.90 ? 157 GLU A OE2 1 ATOM 578 N N . ALA A 1 72 ? 7.999 44.838 10.539 1.00 10.41 ? 158 ALA A N 1 ATOM 579 C CA . ALA A 1 72 ? 7.736 44.402 9.162 1.00 10.92 ? 158 ALA A CA 1 ATOM 580 C C . ALA A 1 72 ? 6.265 44.033 8.933 1.00 10.71 ? 158 ALA A C 1 ATOM 581 O O . ALA A 1 72 ? 5.697 44.225 7.846 1.00 11.38 ? 158 ALA A O 1 ATOM 582 C CB . ALA A 1 72 ? 8.637 43.229 8.820 1.00 12.02 ? 158 ALA A CB 1 ATOM 583 N N . ASN A 1 73 ? 5.665 43.443 9.945 1.00 8.52 ? 159 ASN A N 1 ATOM 584 C CA . ASN A 1 73 ? 4.265 43.022 9.888 1.00 8.67 ? 159 ASN A CA 1 ATOM 585 C C . ASN A 1 73 ? 3.340 44.241 9.899 1.00 11.02 ? 159 ASN A C 1 ATOM 586 O O . ASN A 1 73 ? 2.332 44.294 9.183 1.00 11.44 ? 159 ASN A O 1 ATOM 587 C CB . ASN A 1 73 ? 3.903 42.041 10.983 1.00 8.72 ? 159 ASN A CB 1 ATOM 588 C CG . ASN A 1 73 ? 4.448 40.645 10.695 1.00 9.10 ? 159 ASN A CG 1 ATOM 589 O OD1 . ASN A 1 73 ? 4.880 40.371 9.566 1.00 10.25 ? 159 ASN A OD1 1 ATOM 590 N ND2 . ASN A 1 73 ? 4.439 39.775 11.725 1.00 9.08 ? 159 ASN A ND2 1 ATOM 591 N N . GLN A 1 74 ? 3.685 45.214 10.699 1.00 11.69 ? 160 GLN A N 1 ATOM 592 C CA . GLN A 1 74 ? 2.881 46.447 10.769 1.00 12.82 ? 160 GLN A CA 1 ATOM 593 C C . GLN A 1 74 ? 3.047 47.272 9.496 1.00 14.10 ? 160 GLN A C 1 ATOM 594 O O . GLN A 1 74 ? 2.156 48.081 9.156 1.00 16.92 ? 160 GLN A O 1 ATOM 595 C CB . GLN A 1 74 ? 3.278 47.242 12.000 1.00 12.12 ? 160 GLN A CB 1 ATOM 596 C CG . GLN A 1 74 ? 2.730 46.618 13.296 1.00 12.70 ? 160 GLN A CG 1 ATOM 597 C CD . GLN A 1 74 ? 3.111 47.360 14.589 1.00 12.38 ? 160 GLN A CD 1 ATOM 598 O OE1 . GLN A 1 74 ? 2.600 47.010 15.696 1.00 17.80 ? 160 GLN A OE1 1 ATOM 599 N NE2 . GLN A 1 74 ? 3.998 48.285 14.496 1.00 15.99 ? 160 GLN A NE2 1 ATOM 600 N N . ALA A 1 75 ? 4.156 47.059 8.796 1.00 13.59 ? 161 ALA A N 1 ATOM 601 C CA . ALA A 1 75 ? 4.450 47.711 7.493 1.00 14.25 ? 161 ALA A CA 1 ATOM 602 C C . ALA A 1 75 ? 3.871 46.926 6.294 1.00 15.02 ? 161 ALA A C 1 ATOM 603 O O . ALA A 1 75 ? 4.179 47.237 5.156 1.00 18.23 ? 161 ALA A O 1 ATOM 604 C CB . ALA A 1 75 ? 5.928 47.939 7.296 1.00 15.20 ? 161 ALA A CB 1 ATOM 605 N N . GLY A 1 76 ? 3.028 45.949 6.575 1.00 16.16 ? 162 GLY A N 1 ATOM 606 C CA . GLY A 1 76 ? 2.181 45.270 5.596 1.00 16.13 ? 162 GLY A CA 1 ATOM 607 C C . GLY A 1 76 ? 2.584 43.934 5.039 1.00 16.98 ? 162 GLY A C 1 ATOM 608 O O . GLY A 1 76 ? 2.018 43.465 4.042 1.00 18.21 ? 162 GLY A O 1 ATOM 609 N N . ALA A 1 77 ? 3.563 43.296 5.664 1.00 15.76 ? 163 ALA A N 1 ATOM 610 C CA . ALA A 1 77 ? 4.035 41.996 5.196 1.00 15.62 ? 163 ALA A CA 1 ATOM 611 C C . ALA A 1 77 ? 2.830 41.103 5.000 1.00 15.13 ? 163 ALA A C 1 ATOM 612 O O . ALA A 1 77 ? 1.937 41.015 5.854 1.00 13.66 ? 163 ALA A O 1 ATOM 613 C CB . ALA A 1 77 ? 5.008 41.358 6.176 1.00 16.04 ? 163 ALA A CB 1 ATOM 614 N N . ASN A 1 78 ? 2.800 40.387 3.884 1.00 16.49 ? 164 ASN A N 1 ATOM 615 C CA . ASN A 1 78 ? 1.651 39.530 3.629 1.00 18.57 ? 164 ASN A CA 1 ATOM 616 C C . ASN A 1 78 ? 2.062 38.298 2.853 1.00 18.38 ? 164 ASN A C 1 ATOM 617 O O . ASN A 1 78 ? 2.598 38.414 1.748 1.00 19.81 ? 164 ASN A O 1 ATOM 618 C CB . ASN A 1 78 ? 0.577 40.335 2.887 1.00 20.43 ? 164 ASN A CB 1 ATOM 619 C CG . ASN A 1 78 ? -0.594 39.498 2.453 1.00 24.96 ? 164 ASN A CG 1 ATOM 620 O OD1 . ASN A 1 78 ? -1.117 38.683 3.208 1.00 28.99 ? 164 ASN A OD1 1 ATOM 621 N ND2 . ASN A 1 78 ? -1.017 39.697 1.211 1.00 32.98 ? 164 ASN A ND2 1 ATOM 622 N N . PRO A 1 79 ? 1.889 37.124 3.461 1.00 18.23 ? 165 PRO A N 1 ATOM 623 C CA . PRO A 1 79 ? 1.355 36.983 4.808 1.00 17.17 ? 165 PRO A CA 1 ATOM 624 C C . PRO A 1 79 ? 2.348 37.474 5.881 1.00 14.69 ? 165 PRO A C 1 ATOM 625 O O . PRO A 1 79 ? 3.505 37.776 5.572 1.00 14.28 ? 165 PRO A O 1 ATOM 626 C CB . PRO A 1 79 ? 1.147 35.464 4.957 1.00 18.02 ? 165 PRO A CB 1 ATOM 627 C CG . PRO A 1 79 ? 1.992 34.850 3.977 1.00 19.31 ? 165 PRO A CG 1 ATOM 628 C CD . PRO A 1 79 ? 2.206 35.822 2.852 1.00 20.19 ? 165 PRO A CD 1 ATOM 629 N N . GLN A 1 80 ? 1.867 37.553 7.098 1.00 14.44 ? 166 GLN A N 1 ATOM 630 C CA . GLN A 1 80 ? 2.684 38.034 8.225 1.00 14.58 ? 166 GLN A CA 1 ATOM 631 C C . GLN A 1 80 ? 3.886 37.109 8.410 1.00 12.35 ? 166 GLN A C 1 ATOM 632 O O . GLN A 1 80 ? 3.812 35.919 8.131 1.00 11.84 ? 166 GLN A O 1 ATOM 633 C CB . GLN A 1 80 ? 1.920 38.125 9.563 1.00 15.79 ? 166 GLN A CB 1 ATOM 634 C CG . GLN A 1 80 ? 1.284 36.798 10.044 1.00 23.21 ? 166 GLN A CG 1 ATOM 635 C CD . GLN A 1 80 ? 0.710 36.806 11.500 1.00 28.22 ? 166 GLN A CD 1 ATOM 636 O OE1 . GLN A 1 80 ? 0.860 37.788 12.253 1.00 31.32 ? 166 GLN A OE1 1 ATOM 637 N NE2 . GLN A 1 80 ? 0.082 35.689 11.890 1.00 33.90 ? 166 GLN A NE2 1 ATOM 638 N N . TYR A 1 81 ? 4.961 37.686 8.910 1.00 10.05 ? 167 TYR A N 1 ATOM 639 C CA . TYR A 1 81 ? 6.176 36.951 9.218 1.00 7.97 ? 167 TYR A CA 1 ATOM 640 C C . TYR A 1 81 ? 6.051 36.294 10.584 1.00 8.84 ? 167 TYR A C 1 ATOM 641 O O . TYR A 1 81 ? 5.441 36.844 11.523 1.00 8.82 ? 167 TYR A O 1 ATOM 642 C CB . TYR A 1 81 ? 7.377 37.876 9.235 1.00 8.48 ? 167 TYR A CB 1 ATOM 643 C CG . TYR A 1 81 ? 7.924 38.239 7.870 1.00 7.60 ? 167 TYR A CG 1 ATOM 644 C CD1 . TYR A 1 81 ? 8.629 37.313 7.122 1.00 9.60 ? 167 TYR A CD1 1 ATOM 645 C CD2 . TYR A 1 81 ? 7.776 39.499 7.380 1.00 12.08 ? 167 TYR A CD2 1 ATOM 646 C CE1 . TYR A 1 81 ? 9.166 37.651 5.893 1.00 12.03 ? 167 TYR A CE1 1 ATOM 647 C CE2 . TYR A 1 81 ? 8.319 39.854 6.185 1.00 13.89 ? 167 TYR A CE2 1 ATOM 648 C CZ . TYR A 1 81 ? 8.990 38.937 5.431 1.00 17.02 ? 167 TYR A CZ 1 ATOM 649 O OH . TYR A 1 81 ? 9.518 39.325 4.210 1.00 21.25 ? 167 TYR A OH 1 ATOM 650 N N . ALA A 1 82 ? 6.681 35.121 10.698 1.00 7.67 ? 168 ALA A N 1 ATOM 651 C CA . ALA A 1 82 ? 6.824 34.371 11.950 1.00 7.61 ? 168 ALA A CA 1 ATOM 652 C C . ALA A 1 82 ? 8.290 34.205 12.315 1.00 6.89 ? 168 ALA A C 1 ATOM 653 O O . ALA A 1 82 ? 9.148 34.184 11.435 1.00 6.62 ? 168 ALA A O 1 ATOM 654 C CB . ALA A 1 82 ? 6.168 32.993 11.863 1.00 7.54 ? 168 ALA A CB 1 ATOM 655 N N . ALA A 1 83 ? 8.551 34.078 13.619 1.00 5.51 ? 169 ALA A N 1 ATOM 656 C CA . ALA A 1 83 ? 9.910 33.891 14.131 1.00 5.75 ? 169 ALA A CA 1 ATOM 657 C C . ALA A 1 83 ? 10.228 32.404 14.324 1.00 5.27 ? 169 ALA A C 1 ATOM 658 O O . ALA A 1 83 ? 9.361 31.611 14.610 1.00 5.13 ? 169 ALA A O 1 ATOM 659 C CB . ALA A 1 83 ? 10.077 34.581 15.463 1.00 5.42 ? 169 ALA A CB 1 ATOM 660 N N . GLN A 1 84 ? 11.493 32.087 14.199 1.00 6.14 ? 170 GLN A N 1 ATOM 661 C CA . GLN A 1 84 ? 12.044 30.747 14.385 1.00 5.66 ? 170 GLN A CA 1 ATOM 662 C C . GLN A 1 84 ? 13.222 30.836 15.336 1.00 6.83 ? 170 GLN A C 1 ATOM 663 O O . GLN A 1 84 ? 14.263 31.450 15.012 1.00 6.96 ? 170 GLN A O 1 ATOM 664 C CB . GLN A 1 84 ? 12.527 30.186 13.055 1.00 6.96 ? 170 GLN A CB 1 ATOM 665 C CG . GLN A 1 84 ? 11.420 29.754 12.069 1.00 5.36 ? 170 GLN A CG 1 ATOM 666 C CD . GLN A 1 84 ? 11.993 29.400 10.711 1.00 10.56 ? 170 GLN A CD 1 ATOM 667 O OE1 . GLN A 1 84 ? 11.962 28.221 10.347 1.00 8.59 ? 170 GLN A OE1 1 ATOM 668 N NE2 . GLN A 1 84 ? 12.571 30.394 9.977 1.00 6.28 ? 170 GLN A NE2 1 ATOM 669 N N . ILE A 1 85 ? 13.063 30.277 16.517 1.00 5.64 ? 171 ILE A N 1 ATOM 670 C CA . ILE A 1 85 ? 14.009 30.443 17.636 1.00 5.56 ? 171 ILE A CA 1 ATOM 671 C C . ILE A 1 85 ? 14.378 29.087 18.243 1.00 5.77 ? 171 ILE A C 1 ATOM 672 O O . ILE A 1 85 ? 13.524 28.208 18.415 1.00 5.83 ? 171 ILE A O 1 ATOM 673 C CB . ILE A 1 85 ? 13.380 31.351 18.744 1.00 5.85 ? 171 ILE A CB 1 ATOM 674 C CG1 . ILE A 1 85 ? 12.993 32.726 18.223 1.00 8.23 ? 171 ILE A CG1 1 ATOM 675 C CG2 . ILE A 1 85 ? 14.284 31.454 19.978 1.00 7.76 ? 171 ILE A CG2 1 ATOM 676 C CD1 . ILE A 1 85 ? 14.187 33.575 17.744 1.00 9.77 ? 171 ILE A CD1 1 ATOM 677 N N . VAL A 1 86 ? 15.646 28.909 18.583 1.00 4.52 ? 172 VAL A N 1 ATOM 678 C CA . VAL A 1 86 ? 16.101 27.703 19.302 1.00 5.83 ? 172 VAL A CA 1 ATOM 679 C C . VAL A 1 86 ? 16.402 28.055 20.780 1.00 5.99 ? 172 VAL A C 1 ATOM 680 O O . VAL A 1 86 ? 17.152 28.996 21.057 1.00 6.39 ? 172 VAL A O 1 ATOM 681 C CB . VAL A 1 86 ? 17.338 27.100 18.708 1.00 4.60 ? 172 VAL A CB 1 ATOM 682 C CG1 . VAL A 1 86 ? 17.638 25.744 19.346 1.00 6.92 ? 172 VAL A CG1 1 ATOM 683 C CG2 . VAL A 1 86 ? 17.236 26.913 17.183 1.00 5.73 ? 172 VAL A CG2 1 ATOM 684 N N . VAL A 1 87 ? 15.874 27.262 21.700 1.00 5.63 ? 173 VAL A N 1 ATOM 685 C CA . VAL A 1 87 ? 16.176 27.401 23.119 1.00 6.16 ? 173 VAL A CA 1 ATOM 686 C C . VAL A 1 87 ? 17.282 26.380 23.400 1.00 5.83 ? 173 VAL A C 1 ATOM 687 O O . VAL A 1 87 ? 17.091 25.211 23.172 1.00 6.89 ? 173 VAL A O 1 ATOM 688 C CB . VAL A 1 87 ? 14.925 27.136 23.953 1.00 5.87 ? 173 VAL A CB 1 ATOM 689 C CG1 . VAL A 1 87 ? 15.215 27.231 25.447 1.00 5.95 ? 173 VAL A CG1 1 ATOM 690 C CG2 . VAL A 1 87 ? 13.807 28.100 23.564 1.00 5.83 ? 173 VAL A CG2 1 ATOM 691 N N . TYR A 1 88 ? 18.453 26.868 23.814 1.00 6.30 ? 174 TYR A N 1 ATOM 692 C CA . TYR A 1 88 ? 19.612 25.956 23.929 1.00 5.43 ? 174 TYR A CA 1 ATOM 693 C C . TYR A 1 88 ? 20.571 26.398 25.033 1.00 5.96 ? 174 TYR A C 1 ATOM 694 O O . TYR A 1 88 ? 21.666 26.886 24.762 1.00 8.33 ? 174 TYR A O 1 ATOM 695 C CB . TYR A 1 88 ? 20.321 25.861 22.561 1.00 4.89 ? 174 TYR A CB 1 ATOM 696 C CG . TYR A 1 88 ? 21.479 24.914 22.439 1.00 5.85 ? 174 TYR A CG 1 ATOM 697 C CD1 . TYR A 1 88 ? 21.399 23.616 22.902 1.00 7.97 ? 174 TYR A CD1 1 ATOM 698 C CD2 . TYR A 1 88 ? 22.638 25.312 21.771 1.00 5.57 ? 174 TYR A CD2 1 ATOM 699 C CE1 . TYR A 1 88 ? 22.461 22.740 22.755 1.00 6.89 ? 174 TYR A CE1 1 ATOM 700 C CE2 . TYR A 1 88 ? 23.689 24.443 21.597 1.00 9.62 ? 174 TYR A CE2 1 ATOM 701 C CZ . TYR A 1 88 ? 23.592 23.148 22.080 1.00 9.92 ? 174 TYR A CZ 1 ATOM 702 O OH . TYR A 1 88 ? 24.641 22.259 21.909 1.00 10.99 ? 174 TYR A OH 1 ATOM 703 N N . ASP A 1 89 ? 20.148 26.251 26.281 1.00 6.63 ? 175 ASP A N 1 ATOM 704 C CA . ASP A 1 89 ? 21.050 26.632 27.366 1.00 5.89 ? 175 ASP A CA 1 ATOM 705 C C . ASP A 1 89 ? 20.849 25.805 28.617 1.00 6.88 ? 175 ASP A C 1 ATOM 706 O O . ASP A 1 89 ? 21.064 26.298 29.716 1.00 7.11 ? 175 ASP A O 1 ATOM 707 C CB . ASP A 1 89 ? 20.903 28.117 27.659 1.00 5.41 ? 175 ASP A CB 1 ATOM 708 C CG . ASP A 1 89 ? 22.170 28.750 28.179 1.00 8.18 ? 175 ASP A CG 1 ATOM 709 O OD1 . ASP A 1 89 ? 23.235 28.090 28.206 1.00 6.39 ? 175 ASP A OD1 1 ATOM 710 O OD2 . ASP A 1 89 ? 22.161 29.936 28.607 1.00 8.25 ? 175 ASP A OD2 1 ATOM 711 N N . LEU A 1 90 ? 20.458 24.533 28.479 1.00 5.35 ? 176 LEU A N 1 ATOM 712 C CA . LEU A 1 90 ? 20.363 23.683 29.683 1.00 6.11 ? 176 LEU A CA 1 ATOM 713 C C . LEU A 1 90 ? 21.699 23.676 30.449 1.00 5.21 ? 176 LEU A C 1 ATOM 714 O O . LEU A 1 90 ? 22.768 23.709 29.844 1.00 6.74 ? 176 LEU A O 1 ATOM 715 C CB . LEU A 1 90 ? 19.997 22.248 29.354 1.00 5.44 ? 176 LEU A CB 1 ATOM 716 C CG . LEU A 1 90 ? 18.510 22.017 29.037 1.00 5.54 ? 176 LEU A CG 1 ATOM 717 C CD1 . LEU A 1 90 ? 18.423 20.651 28.342 1.00 5.86 ? 176 LEU A CD1 1 ATOM 718 C CD2 . LEU A 1 90 ? 17.687 22.053 30.297 1.00 6.50 ? 176 LEU A CD2 1 ATOM 719 N N . PRO A 1 91 ? 21.614 23.634 31.777 1.00 6.65 ? 177 PRO A N 1 ATOM 720 C CA . PRO A 1 91 ? 22.800 23.448 32.607 1.00 7.21 ? 177 PRO A CA 1 ATOM 721 C C . PRO A 1 91 ? 23.341 22.036 32.357 1.00 7.58 ? 177 PRO A C 1 ATOM 722 O O . PRO A 1 91 ? 22.584 21.119 32.100 1.00 6.13 ? 177 PRO A O 1 ATOM 723 C CB . PRO A 1 91 ? 22.261 23.591 34.034 1.00 8.12 ? 177 PRO A CB 1 ATOM 724 C CG . PRO A 1 91 ? 20.804 23.127 33.978 1.00 6.69 ? 177 PRO A CG 1 ATOM 725 C CD . PRO A 1 91 ? 20.382 23.615 32.575 1.00 5.60 ? 177 PRO A CD 1 ATOM 726 N N . ASP A 1 92 ? 24.652 21.869 32.534 1.00 7.00 ? 178 ASP A N 1 ATOM 727 C CA . ASP A 1 92 ? 25.378 20.647 32.168 1.00 7.92 ? 178 ASP A CA 1 ATOM 728 C C . ASP A 1 92 ? 25.010 20.230 30.730 1.00 8.49 ? 178 ASP A C 1 ATOM 729 O O . ASP A 1 92 ? 24.740 19.068 30.418 1.00 7.15 ? 178 ASP A O 1 ATOM 730 C CB . ASP A 1 92 ? 25.117 19.504 33.148 1.00 8.36 ? 178 ASP A CB 1 ATOM 731 C CG . ASP A 1 92 ? 25.941 19.606 34.407 1.00 13.29 ? 178 ASP A CG 1 ATOM 732 O OD1 . ASP A 1 92 ? 26.345 20.724 34.794 1.00 10.54 ? 178 ASP A OD1 1 ATOM 733 O OD2 . ASP A 1 92 ? 26.193 18.578 35.076 1.00 13.97 ? 178 ASP A OD2 1 ATOM 734 N N . ARG A 1 93 ? 24.999 21.224 29.855 1.00 7.92 ? 179 ARG A N 1 ATOM 735 C CA . ARG A 1 93 ? 24.589 21.071 28.459 1.00 7.23 ? 179 ARG A CA 1 ATOM 736 C C . ARG A 1 93 ? 25.498 20.089 27.720 1.00 7.85 ? 179 ARG A C 1 ATOM 737 O O . ARG A 1 93 ? 26.687 19.986 28.006 1.00 8.20 ? 179 ARG A O 1 ATOM 738 C CB . ARG A 1 93 ? 24.617 22.435 27.771 1.00 8.46 ? 179 ARG A CB 1 ATOM 739 C CG . ARG A 1 93 ? 23.580 22.561 26.664 1.00 6.79 ? 179 ARG A CG 1 ATOM 740 C CD . ARG A 1 93 ? 23.652 23.910 25.936 1.00 7.14 ? 179 ARG A CD 1 ATOM 741 N NE . ARG A 1 93 ? 24.844 24.003 25.110 1.00 8.52 ? 179 ARG A NE 1 ATOM 742 C CZ . ARG A 1 93 ? 25.208 25.152 24.572 1.00 9.28 ? 179 ARG A CZ 1 ATOM 743 N NH1 . ARG A 1 93 ? 24.465 26.232 24.782 1.00 7.77 ? 179 ARG A NH1 1 ATOM 744 N NH2 . ARG A 1 93 ? 26.297 25.221 23.818 1.00 9.76 ? 179 ARG A NH2 1 ATOM 745 N N . ASP A 1 94 ? 24.895 19.364 26.777 1.00 6.96 ? 180 ASP A N 1 ATOM 746 C CA . ASP A 1 94 ? 25.645 18.431 25.922 1.00 8.03 ? 180 ASP A CA 1 ATOM 747 C C . ASP A 1 94 ? 26.407 17.412 26.762 1.00 8.65 ? 180 ASP A C 1 ATOM 748 O O . ASP A 1 94 ? 27.628 17.259 26.645 1.00 8.13 ? 180 ASP A O 1 ATOM 749 C CB . ASP A 1 94 ? 26.621 19.212 25.030 1.00 8.28 ? 180 ASP A CB 1 ATOM 750 C CG . ASP A 1 94 ? 25.942 20.397 24.393 1.00 9.77 ? 180 ASP A CG 1 ATOM 751 O OD1 . ASP A 1 94 ? 25.028 20.156 23.590 1.00 10.71 ? 180 ASP A OD1 1 ATOM 752 O OD2 . ASP A 1 94 ? 26.282 21.549 24.691 1.00 10.14 ? 180 ASP A OD2 1 ATOM 753 N N . CYS A 1 95 ? 25.669 16.705 27.614 1.00 8.09 ? 181 CYS A N 1 ATOM 754 C CA . CYS A 1 95 ? 26.292 15.880 28.659 1.00 8.49 ? 181 CYS A CA 1 ATOM 755 C C . CYS A 1 95 ? 27.261 14.805 28.151 1.00 8.95 ? 181 CYS A C 1 ATOM 756 O O . CYS A 1 95 ? 28.190 14.455 28.861 1.00 8.63 ? 181 CYS A O 1 ATOM 757 C CB . CYS A 1 95 ? 25.232 15.256 29.554 1.00 9.46 ? 181 CYS A CB 1 ATOM 758 S SG . CYS A 1 95 ? 24.115 14.139 28.692 1.00 9.18 ? 181 CYS A SG 1 ATOM 759 N N . ALA A 1 96 ? 27.073 14.268 26.943 1.00 7.45 ? 182 ALA A N 1 ATOM 760 C CA . ALA A 1 96 ? 27.939 13.219 26.458 1.00 9.04 ? 182 ALA A CA 1 ATOM 761 C C . ALA A 1 96 ? 29.056 13.730 25.563 1.00 9.16 ? 182 ALA A C 1 ATOM 762 O O . ALA A 1 96 ? 29.855 12.919 25.045 1.00 9.73 ? 182 ALA A O 1 ATOM 763 C CB . ALA A 1 96 ? 27.080 12.229 25.679 1.00 9.68 ? 182 ALA A CB 1 ATOM 764 N N . ALA A 1 97 ? 29.114 15.043 25.327 1.00 8.57 ? 183 ALA A N 1 ATOM 765 C CA . ALA A 1 97 ? 30.090 15.619 24.412 1.00 8.77 ? 183 ALA A CA 1 ATOM 766 C C . ALA A 1 97 ? 31.492 15.594 24.987 1.00 8.80 ? 183 ALA A C 1 ATOM 767 O O . ALA A 1 97 ? 31.680 15.631 26.212 1.00 9.42 ? 183 ALA A O 1 ATOM 768 C CB . ALA A 1 97 ? 29.733 17.069 24.040 1.00 9.46 ? 183 ALA A CB 1 ATOM 769 N N . ALA A 1 98 ? 32.466 15.582 24.095 1.00 8.96 ? 184 ALA A N 1 ATOM 770 C CA . ALA A 1 98 ? 33.865 15.602 24.514 1.00 10.09 ? 184 ALA A CA 1 ATOM 771 C C . ALA A 1 98 ? 34.181 16.901 25.185 1.00 11.30 ? 184 ALA A C 1 ATOM 772 O O . ALA A 1 98 ? 34.994 16.956 26.098 1.00 12.92 ? 184 ALA A O 1 ATOM 773 C CB . ALA A 1 98 ? 34.812 15.324 23.344 1.00 9.22 ? 184 ALA A CB 1 ATOM 774 N N . ALA A 1 99 ? 33.516 17.962 24.728 1.00 11.34 ? 185 ALA A N 1 ATOM 775 C CA . ALA A 1 99 ? 33.654 19.298 25.292 1.00 11.97 ? 185 ALA A CA 1 ATOM 776 C C . ALA A 1 99 ? 32.318 19.988 25.053 1.00 13.38 ? 185 ALA A C 1 ATOM 777 O O . ALA A 1 99 ? 31.620 19.670 24.091 1.00 15.94 ? 185 ALA A O 1 ATOM 778 C CB . ALA A 1 99 ? 34.786 20.040 24.602 1.00 12.14 ? 185 ALA A CB 1 ATOM 779 N N . SER A 1 100 ? 31.921 20.833 25.981 1.00 13.21 ? 186 SER A N 1 ATOM 780 C CA . SER A 1 100 ? 30.720 21.640 25.826 1.00 12.62 ? 186 SER A CA 1 ATOM 781 C C . SER A 1 100 ? 31.041 23.108 25.950 1.00 13.40 ? 186 SER A C 1 ATOM 782 O O . SER A 1 100 ? 31.844 23.508 26.780 1.00 14.85 ? 186 SER A O 1 ATOM 783 C CB . SER A 1 100 ? 29.679 21.312 26.893 1.00 13.94 ? 186 SER A CB 1 ATOM 784 O OG . SER A 1 100 ? 28.481 22.061 26.695 1.00 11.36 ? 186 SER A OG 1 ATOM 785 N N . ASN A 1 101 ? 30.321 23.893 25.155 1.00 13.41 ? 187 ASN A N 1 ATOM 786 C CA . ASN A 1 101 ? 30.331 25.335 25.225 1.00 14.15 ? 187 ASN A CA 1 ATOM 787 C C . ASN A 1 101 ? 29.186 25.879 26.061 1.00 11.94 ? 187 ASN A C 1 ATOM 788 O O . ASN A 1 101 ? 29.071 27.094 26.192 1.00 14.14 ? 187 ASN A O 1 ATOM 789 C CB . ASN A 1 101 ? 30.293 25.896 23.801 1.00 15.24 ? 187 ASN A CB 1 ATOM 790 C CG . ASN A 1 101 ? 31.472 25.396 22.980 1.00 19.14 ? 187 ASN A CG 1 ATOM 791 O OD1 . ASN A 1 101 ? 31.327 24.676 22.000 1.00 21.74 ? 187 ASN A OD1 1 ATOM 792 N ND2 . ASN A 1 101 ? 32.664 25.794 23.404 1.00 22.54 ? 187 ASN A ND2 1 ATOM 793 N N . GLY A 1 102 ? 28.362 25.005 26.665 1.00 10.65 ? 188 GLY A N 1 ATOM 794 C CA . GLY A 1 102 ? 27.234 25.433 27.502 1.00 9.99 ? 188 GLY A CA 1 ATOM 795 C C . GLY A 1 102 ? 27.766 26.205 28.708 1.00 10.44 ? 188 GLY A C 1 ATOM 796 O O . GLY A 1 102 ? 28.735 25.828 29.346 1.00 10.68 ? 188 GLY A O 1 ATOM 797 N N . GLU A 1 103 ? 27.199 27.364 28.982 1.00 9.16 ? 189 GLU A N 1 ATOM 798 C CA . GLU A 1 103 ? 27.760 28.215 30.027 1.00 8.87 ? 189 GLU A CA 1 ATOM 799 C C . GLU A 1 103 ? 27.430 27.855 31.468 1.00 9.31 ? 189 GLU A C 1 ATOM 800 O O . GLU A 1 103 ? 28.150 28.291 32.377 1.00 10.26 ? 189 GLU A O 1 ATOM 801 C CB . GLU A 1 103 ? 27.374 29.668 29.782 1.00 9.76 ? 189 GLU A CB 1 ATOM 802 C CG . GLU A 1 103 ? 25.897 29.941 29.893 1.00 7.40 ? 189 GLU A CG 1 ATOM 803 C CD . GLU A 1 103 ? 25.438 31.240 29.245 1.00 10.31 ? 189 GLU A CD 1 ATOM 804 O OE1 . GLU A 1 103 ? 26.268 32.163 29.002 1.00 14.09 ? 189 GLU A OE1 1 ATOM 805 O OE2 . GLU A 1 103 ? 24.213 31.353 29.012 1.00 8.68 ? 189 GLU A OE2 1 ATOM 806 N N . TRP A 1 104 ? 26.371 27.075 31.684 1.00 6.71 ? 190 TRP A N 1 ATOM 807 C CA . TRP A 1 104 ? 25.884 26.849 33.035 1.00 6.92 ? 190 TRP A CA 1 ATOM 808 C C . TRP A 1 104 ? 26.096 25.413 33.499 1.00 8.79 ? 190 TRP A C 1 ATOM 809 O O . TRP A 1 104 ? 26.018 24.478 32.697 1.00 8.28 ? 190 TRP A O 1 ATOM 810 C CB . TRP A 1 104 ? 24.414 27.204 33.187 1.00 8.41 ? 190 TRP A CB 1 ATOM 811 C CG . TRP A 1 104 ? 24.151 28.667 33.102 1.00 7.16 ? 190 TRP A CG 1 ATOM 812 C CD1 . TRP A 1 104 ? 25.014 29.678 33.430 1.00 8.06 ? 190 TRP A CD1 1 ATOM 813 C CD2 . TRP A 1 104 ? 22.963 29.315 32.610 1.00 5.72 ? 190 TRP A CD2 1 ATOM 814 N NE1 . TRP A 1 104 ? 24.432 30.895 33.185 1.00 6.91 ? 190 TRP A NE1 1 ATOM 815 C CE2 . TRP A 1 104 ? 23.175 30.696 32.672 1.00 6.44 ? 190 TRP A CE2 1 ATOM 816 C CE3 . TRP A 1 104 ? 21.749 28.857 32.094 1.00 5.13 ? 190 TRP A CE3 1 ATOM 817 C CZ2 . TRP A 1 104 ? 22.215 31.608 32.273 1.00 6.99 ? 190 TRP A CZ2 1 ATOM 818 C CZ3 . TRP A 1 104 ? 20.814 29.762 31.668 1.00 7.02 ? 190 TRP A CZ3 1 ATOM 819 C CH2 . TRP A 1 104 ? 21.044 31.121 31.765 1.00 7.09 ? 190 TRP A CH2 1 ATOM 820 N N . ALA A 1 105 ? 26.355 25.284 34.800 1.00 9.34 ? 191 ALA A N 1 ATOM 821 C CA . ALA A 1 105 ? 26.578 23.994 35.436 1.00 9.26 ? 191 ALA A CA 1 ATOM 822 C C . ALA A 1 105 ? 25.534 23.770 36.511 1.00 8.60 ? 191 ALA A C 1 ATOM 823 O O . ALA A 1 105 ? 25.234 24.656 37.295 1.00 8.70 ? 191 ALA A O 1 ATOM 824 C CB . ALA A 1 105 ? 27.933 23.942 36.058 1.00 9.78 ? 191 ALA A CB 1 ATOM 825 N N . ILE A 1 106 ? 25.029 22.545 36.601 1.00 9.24 ? 192 ILE A N 1 ATOM 826 C CA . ILE A 1 106 ? 24.128 22.172 37.707 1.00 9.65 ? 192 ILE A CA 1 ATOM 827 C C . ILE A 1 106 ? 24.755 22.516 39.059 1.00 10.82 ? 192 ILE A C 1 ATOM 828 O O . ILE A 1 106 ? 24.096 23.070 39.939 1.00 11.34 ? 192 ILE A O 1 ATOM 829 C CB . ILE A 1 106 ? 23.709 20.683 37.601 1.00 10.57 ? 192 ILE A CB 1 ATOM 830 C CG1 . ILE A 1 106 ? 22.903 20.510 36.295 1.00 9.66 ? 192 ILE A CG1 1 ATOM 831 C CG2 . ILE A 1 106 ? 22.877 20.287 38.801 1.00 12.50 ? 192 ILE A CG2 1 ATOM 832 C CD1 . ILE A 1 106 ? 22.624 19.045 35.915 1.00 11.48 ? 192 ILE A CD1 1 ATOM 833 N N . ALA A 1 107 ? 26.038 22.221 39.196 1.00 12.01 ? 193 ALA A N 1 ATOM 834 C CA . ALA A 1 107 ? 26.752 22.492 40.469 1.00 13.34 ? 193 ALA A CA 1 ATOM 835 C C . ALA A 1 107 ? 26.892 23.989 40.790 1.00 13.18 ? 193 ALA A C 1 ATOM 836 O O . ALA A 1 107 ? 27.252 24.366 41.903 1.00 13.22 ? 193 ALA A O 1 ATOM 837 C CB . ALA A 1 107 ? 28.146 21.875 40.422 1.00 14.50 ? 193 ALA A CB 1 ATOM 838 N N . ASN A 1 108 ? 26.663 24.856 39.796 1.00 11.86 ? 194 ASN A N 1 ATOM 839 C CA . ASN A 1 108 ? 26.849 26.287 39.996 1.00 12.56 ? 194 ASN A CA 1 ATOM 840 C C . ASN A 1 108 ? 25.557 27.076 39.749 1.00 10.66 ? 194 ASN A C 1 ATOM 841 O O . ASN A 1 108 ? 25.515 27.999 38.931 1.00 11.18 ? 194 ASN A O 1 ATOM 842 C CB . ASN A 1 108 ? 27.957 26.825 39.069 1.00 14.63 ? 194 ASN A CB 1 ATOM 843 C CG . ASN A 1 108 ? 29.305 26.178 39.336 1.00 18.97 ? 194 ASN A CG 1 ATOM 844 O OD1 . ASN A 1 108 ? 29.799 26.141 40.478 1.00 23.42 ? 194 ASN A OD1 1 ATOM 845 N ND2 . ASN A 1 108 ? 29.926 25.680 38.269 1.00 22.44 ? 194 ASN A ND2 1 ATOM 846 N N . ASN A 1 109 ? 24.494 26.656 40.445 1.00 10.41 ? 195 ASN A N 1 ATOM 847 C CA . ASN A 1 109 ? 23.193 27.312 40.374 1.00 9.74 ? 195 ASN A CA 1 ATOM 848 C C . ASN A 1 109 ? 22.548 27.205 38.985 1.00 8.54 ? 195 ASN A C 1 ATOM 849 O O . ASN A 1 109 ? 21.683 27.996 38.627 1.00 7.70 ? 195 ASN A O 1 ATOM 850 C CB . ASN A 1 109 ? 23.310 28.775 40.798 1.00 10.66 ? 195 ASN A CB 1 ATOM 851 C CG . ASN A 1 109 ? 22.021 29.276 41.408 1.00 12.99 ? 195 ASN A CG 1 ATOM 852 O OD1 . ASN A 1 109 ? 21.243 28.514 41.973 1.00 14.24 ? 195 ASN A OD1 1 ATOM 853 N ND2 . ASN A 1 109 ? 21.787 30.592 41.297 1.00 15.12 ? 195 ASN A ND2 1 ATOM 854 N N . GLY A 1 110 ? 22.894 26.158 38.235 1.00 7.99 ? 196 GLY A N 1 ATOM 855 C CA . GLY A 1 110 ? 22.456 26.065 36.842 1.00 7.06 ? 196 GLY A CA 1 ATOM 856 C C . GLY A 1 110 ? 20.957 25.901 36.709 1.00 7.21 ? 196 GLY A C 1 ATOM 857 O O . GLY A 1 110 ? 20.395 26.455 35.772 1.00 7.16 ? 196 GLY A O 1 ATOM 858 N N . VAL A 1 111 ? 20.314 25.141 37.600 1.00 6.82 ? 197 VAL A N 1 ATOM 859 C CA . VAL A 1 111 ? 18.858 24.959 37.578 1.00 7.34 ? 197 VAL A CA 1 ATOM 860 C C . VAL A 1 111 ? 18.138 26.317 37.712 1.00 6.72 ? 197 VAL A C 1 ATOM 861 O O . VAL A 1 111 ? 17.281 26.667 36.898 1.00 7.48 ? 197 VAL A O 1 ATOM 862 C CB . VAL A 1 111 ? 18.370 23.899 38.595 1.00 8.41 ? 197 VAL A CB 1 ATOM 863 C CG1 . VAL A 1 111 ? 16.847 23.890 38.687 1.00 9.82 ? 197 VAL A CG1 1 ATOM 864 C CG2 . VAL A 1 111 ? 18.918 22.539 38.235 1.00 10.00 ? 197 VAL A CG2 1 ATOM 865 N N . ASN A 1 112 ? 18.472 27.073 38.743 1.00 7.43 ? 198 ASN A N 1 ATOM 866 C CA . ASN A 1 112 ? 17.861 28.402 38.912 1.00 8.15 ? 198 ASN A CA 1 ATOM 867 C C . ASN A 1 112 ? 18.164 29.327 37.738 1.00 7.73 ? 198 ASN A C 1 ATOM 868 O O . ASN A 1 112 ? 17.285 30.084 37.318 1.00 7.95 ? 198 ASN A O 1 ATOM 869 C CB . ASN A 1 112 ? 18.319 29.026 40.235 1.00 10.12 ? 198 ASN A CB 1 ATOM 870 C CG . ASN A 1 112 ? 17.694 28.329 41.421 1.00 14.29 ? 198 ASN A CG 1 ATOM 871 O OD1 . ASN A 1 112 ? 16.600 27.759 41.290 1.00 16.91 ? 198 ASN A OD1 1 ATOM 872 N ND2 . ASN A 1 112 ? 18.383 28.357 42.577 1.00 19.11 ? 198 ASN A ND2 1 ATOM 873 N N . ASN A 1 113 ? 19.385 29.271 37.232 1.00 7.58 ? 199 ASN A N 1 ATOM 874 C CA . ASN A 1 113 ? 19.789 30.084 36.080 1.00 6.80 ? 199 ASN A CA 1 ATOM 875 C C . ASN A 1 113 ? 18.871 29.774 34.898 1.00 5.54 ? 199 ASN A C 1 ATOM 876 O O . ASN A 1 113 ? 18.409 30.686 34.234 1.00 5.38 ? 199 ASN A O 1 ATOM 877 C CB . ASN A 1 113 ? 21.220 29.846 35.642 1.00 6.73 ? 199 ASN A CB 1 ATOM 878 C CG . ASN A 1 113 ? 22.245 30.392 36.657 1.00 6.93 ? 199 ASN A CG 1 ATOM 879 O OD1 . ASN A 1 113 ? 21.896 31.158 37.567 1.00 7.75 ? 199 ASN A OD1 1 ATOM 880 N ND2 . ASN A 1 113 ? 23.522 30.052 36.450 1.00 7.68 ? 199 ASN A ND2 1 ATOM 881 N N . TYR A 1 114 ? 18.612 28.477 34.691 1.00 5.71 ? 200 TYR A N 1 ATOM 882 C CA . TYR A 1 114 ? 17.842 28.082 33.512 1.00 4.88 ? 200 TYR A CA 1 ATOM 883 C C . TYR A 1 114 ? 16.357 28.462 33.659 1.00 5.65 ? 200 TYR A C 1 ATOM 884 O O . TYR A 1 114 ? 15.700 28.911 32.726 1.00 5.18 ? 200 TYR A O 1 ATOM 885 C CB . TYR A 1 114 ? 17.957 26.572 33.286 1.00 4.57 ? 200 TYR A CB 1 ATOM 886 C CG . TYR A 1 114 ? 17.341 26.159 31.964 1.00 4.95 ? 200 TYR A CG 1 ATOM 887 C CD1 . TYR A 1 114 ? 18.032 26.328 30.781 1.00 7.64 ? 200 TYR A CD1 1 ATOM 888 C CD2 . TYR A 1 114 ? 16.062 25.613 31.914 1.00 6.76 ? 200 TYR A CD2 1 ATOM 889 C CE1 . TYR A 1 114 ? 17.478 25.953 29.560 1.00 7.73 ? 200 TYR A CE1 1 ATOM 890 C CE2 . TYR A 1 114 ? 15.492 25.225 30.721 1.00 8.06 ? 200 TYR A CE2 1 ATOM 891 C CZ . TYR A 1 114 ? 16.190 25.407 29.534 1.00 6.02 ? 200 TYR A CZ 1 ATOM 892 O OH . TYR A 1 114 ? 15.638 25.004 28.345 1.00 7.10 ? 200 TYR A OH 1 ATOM 893 N N . LYS A 1 115 ? 15.822 28.255 34.859 1.00 5.74 ? 201 LYS A N 1 ATOM 894 C CA . LYS A 1 115 ? 14.440 28.631 35.079 1.00 5.57 ? 201 LYS A CA 1 ATOM 895 C C . LYS A 1 115 ? 14.237 30.131 34.843 1.00 5.55 ? 201 LYS A C 1 ATOM 896 O O . LYS A 1 115 ? 13.245 30.551 34.271 1.00 6.91 ? 201 LYS A O 1 ATOM 897 C CB . LYS A 1 115 ? 14.022 28.236 36.494 1.00 6.88 ? 201 LYS A CB 1 ATOM 898 C CG A LYS A 1 115 ? 13.868 26.752 36.681 0.55 7.85 ? 201 LYS A CG 1 ATOM 899 C CG B LYS A 1 115 ? 13.772 26.733 36.608 0.45 7.69 ? 201 LYS A CG 1 ATOM 900 C CD A LYS A 1 115 ? 13.392 26.384 38.074 0.55 9.97 ? 201 LYS A CD 1 ATOM 901 C CD B LYS A 1 115 ? 13.011 26.377 37.862 0.45 9.74 ? 201 LYS A CD 1 ATOM 902 C CE A LYS A 1 115 ? 11.898 26.642 38.237 0.55 12.52 ? 201 LYS A CE 1 ATOM 903 C CE B LYS A 1 115 ? 12.848 24.878 38.045 0.45 10.81 ? 201 LYS A CE 1 ATOM 904 N NZ A LYS A 1 115 ? 11.461 26.336 39.626 0.55 17.07 ? 201 LYS A NZ 1 ATOM 905 N NZ B LYS A 1 115 ? 12.352 24.621 39.420 0.45 11.77 ? 201 LYS A NZ 1 ATOM 906 N N . ALA A 1 116 ? 15.209 30.940 35.294 1.00 5.60 ? 202 ALA A N 1 ATOM 907 C CA . ALA A 1 116 ? 15.107 32.384 35.069 1.00 5.84 ? 202 ALA A CA 1 ATOM 908 C C . ALA A 1 116 ? 15.100 32.772 33.567 1.00 6.77 ? 202 ALA A C 1 ATOM 909 O O . ALA A 1 116 ? 14.313 33.618 33.122 1.00 6.84 ? 202 ALA A O 1 ATOM 910 C CB . ALA A 1 116 ? 16.219 33.107 35.826 1.00 5.44 ? 202 ALA A CB 1 ATOM 911 N N . TYR A 1 117 ? 16.084 32.213 32.848 1.00 6.83 ? 203 TYR A N 1 ATOM 912 C CA . TYR A 1 117 ? 16.157 32.107 31.402 1.00 6.06 ? 203 TYR A CA 1 ATOM 913 C C . TYR A 1 117 ? 14.771 31.843 30.754 1.00 6.46 ? 203 TYR A C 1 ATOM 914 O O . TYR A 1 117 ? 14.261 32.635 29.944 1.00 5.40 ? 203 TYR A O 1 ATOM 915 C CB . TYR A 1 117 ? 17.070 30.925 31.145 1.00 7.78 ? 203 TYR A CB 1 ATOM 916 C CG . TYR A 1 117 ? 17.318 30.614 29.704 1.00 7.74 ? 203 TYR A CG 1 ATOM 917 C CD1 . TYR A 1 117 ? 18.060 31.478 28.934 1.00 5.93 ? 203 TYR A CD1 1 ATOM 918 C CD2 . TYR A 1 117 ? 16.868 29.446 29.149 1.00 5.97 ? 203 TYR A CD2 1 ATOM 919 C CE1 . TYR A 1 117 ? 18.330 31.220 27.616 1.00 6.89 ? 203 TYR A CE1 1 ATOM 920 C CE2 . TYR A 1 117 ? 17.124 29.163 27.841 1.00 5.22 ? 203 TYR A CE2 1 ATOM 921 C CZ . TYR A 1 117 ? 17.851 30.026 27.062 1.00 5.44 ? 203 TYR A CZ 1 ATOM 922 O OH . TYR A 1 117 ? 18.099 29.664 25.734 1.00 6.21 ? 203 TYR A OH 1 ATOM 923 N N . ILE A 1 118 ? 14.178 30.710 31.085 1.00 5.51 ? 204 ILE A N 1 ATOM 924 C CA . ILE A 1 118 ? 12.860 30.385 30.514 1.00 5.73 ? 204 ILE A CA 1 ATOM 925 C C . ILE A 1 118 ? 11.815 31.452 30.902 1.00 5.76 ? 204 ILE A C 1 ATOM 926 O O . ILE A 1 118 ? 10.983 31.855 30.081 1.00 6.86 ? 204 ILE A O 1 ATOM 927 C CB . ILE A 1 118 ? 12.420 29.010 31.029 1.00 6.40 ? 204 ILE A CB 1 ATOM 928 C CG1 . ILE A 1 118 ? 13.312 27.901 30.445 1.00 5.93 ? 204 ILE A CG1 1 ATOM 929 C CG2 . ILE A 1 118 ? 10.970 28.737 30.645 1.00 7.15 ? 204 ILE A CG2 1 ATOM 930 C CD1 . ILE A 1 118 ? 13.356 27.901 28.918 1.00 6.63 ? 204 ILE A CD1 1 ATOM 931 N N . ASN A 1 119 ? 11.834 31.872 32.175 1.00 7.00 ? 205 ASN A N 1 ATOM 932 C CA . ASN A 1 119 ? 10.873 32.881 32.649 1.00 7.38 ? 205 ASN A CA 1 ATOM 933 C C . ASN A 1 119 ? 11.037 34.210 31.880 1.00 7.31 ? 205 ASN A C 1 ATOM 934 O O . ASN A 1 119 ? 10.062 34.885 31.548 1.00 6.67 ? 205 ASN A O 1 ATOM 935 C CB . ASN A 1 119 ? 11.062 33.137 34.145 1.00 8.35 ? 205 ASN A CB 1 ATOM 936 C CG . ASN A 1 119 ? 10.637 31.970 35.026 1.00 10.06 ? 205 ASN A CG 1 ATOM 937 O OD1 . ASN A 1 119 ? 9.950 31.040 34.612 1.00 10.74 ? 205 ASN A OD1 1 ATOM 938 N ND2 . ASN A 1 119 ? 11.018 32.072 36.306 1.00 14.67 ? 205 ASN A ND2 1 ATOM 939 N N . ARG A 1 120 ? 12.259 34.631 31.589 1.00 7.53 ? 206 ARG A N 1 ATOM 940 C CA . ARG A 1 120 ? 12.471 35.891 30.842 1.00 7.43 ? 206 ARG A CA 1 ATOM 941 C C . ARG A 1 120 ? 12.046 35.733 29.396 1.00 7.29 ? 206 ARG A C 1 ATOM 942 O O . ARG A 1 120 ? 11.448 36.627 28.805 1.00 6.68 ? 206 ARG A O 1 ATOM 943 C CB . ARG A 1 120 ? 13.947 36.291 30.939 1.00 7.34 ? 206 ARG A CB 1 ATOM 944 C CG . ARG A 1 120 ? 14.251 37.631 30.319 1.00 6.71 ? 206 ARG A CG 1 ATOM 945 C CD . ARG A 1 120 ? 13.499 38.781 30.938 1.00 10.12 ? 206 ARG A CD 1 ATOM 946 N NE . ARG A 1 120 ? 13.688 39.949 30.092 1.00 8.99 ? 206 ARG A NE 1 ATOM 947 C CZ . ARG A 1 120 ? 12.761 40.836 29.786 1.00 11.06 ? 206 ARG A CZ 1 ATOM 948 N NH1 . ARG A 1 120 ? 11.541 40.758 30.285 1.00 12.04 ? 206 ARG A NH1 1 ATOM 949 N NH2 . ARG A 1 120 ? 13.072 41.824 28.967 1.00 12.32 ? 206 ARG A NH2 1 ATOM 950 N N . ILE A 1 121 ? 12.356 34.582 28.808 1.00 7.22 ? 207 ILE A N 1 ATOM 951 C CA . ILE A 1 121 ? 11.865 34.293 27.442 1.00 7.02 ? 207 ILE A CA 1 ATOM 952 C C . ILE A 1 121 ? 10.340 34.338 27.443 1.00 6.56 ? 207 ILE A C 1 ATOM 953 O O . ILE A 1 121 ? 9.762 34.961 26.550 1.00 7.46 ? 207 ILE A O 1 ATOM 954 C CB . ILE A 1 121 ? 12.390 32.925 26.917 1.00 5.76 ? 207 ILE A CB 1 ATOM 955 C CG1 . ILE A 1 121 ? 13.886 33.042 26.735 1.00 5.79 ? 207 ILE A CG1 1 ATOM 956 C CG2 . ILE A 1 121 ? 11.716 32.514 25.610 1.00 6.34 ? 207 ILE A CG2 1 ATOM 957 C CD1 . ILE A 1 121 ? 14.569 31.720 26.575 1.00 6.32 ? 207 ILE A CD1 1 ATOM 958 N N . ARG A 1 122 ? 9.688 33.766 28.432 1.00 6.51 ? 208 ARG A N 1 ATOM 959 C CA . ARG A 1 122 ? 8.217 33.804 28.505 1.00 6.43 ? 208 ARG A CA 1 ATOM 960 C C . ARG A 1 122 ? 7.719 35.260 28.486 1.00 6.76 ? 208 ARG A C 1 ATOM 961 O O . ARG A 1 122 ? 6.796 35.608 27.765 1.00 6.25 ? 208 ARG A O 1 ATOM 962 C CB . ARG A 1 122 ? 7.670 33.098 29.735 1.00 7.64 ? 208 ARG A CB 1 ATOM 963 C CG . ARG A 1 122 ? 6.161 33.170 29.829 1.00 6.52 ? 208 ARG A CG 1 ATOM 964 C CD . ARG A 1 122 ? 5.644 32.523 31.094 1.00 7.77 ? 208 ARG A CD 1 ATOM 965 N NE . ARG A 1 122 ? 4.224 32.837 31.330 1.00 13.07 ? 208 ARG A NE 1 ATOM 966 C CZ . ARG A 1 122 ? 3.211 32.031 31.060 1.00 13.64 ? 208 ARG A CZ 1 ATOM 967 N NH1 . ARG A 1 122 ? 3.430 30.842 30.519 1.00 13.05 ? 208 ARG A NH1 1 ATOM 968 N NH2 . ARG A 1 122 ? 1.937 32.404 31.268 1.00 13.57 ? 208 ARG A NH2 1 ATOM 969 N N . GLU A 1 123 ? 8.328 36.097 29.326 1.00 5.77 ? 209 GLU A N 1 ATOM 970 C CA . GLU A 1 123 ? 7.923 37.508 29.378 1.00 6.03 ? 209 GLU A CA 1 ATOM 971 C C . GLU A 1 123 ? 8.061 38.171 28.016 1.00 6.82 ? 209 GLU A C 1 ATOM 972 O O . GLU A 1 123 ? 7.192 38.962 27.611 1.00 7.11 ? 209 GLU A O 1 ATOM 973 C CB . GLU A 1 123 ? 8.800 38.270 30.366 1.00 7.07 ? 209 GLU A CB 1 ATOM 974 C CG . GLU A 1 123 ? 8.614 37.822 31.792 1.00 10.40 ? 209 GLU A CG 1 ATOM 975 C CD . GLU A 1 123 ? 9.453 38.618 32.789 1.00 17.87 ? 209 GLU A CD 1 ATOM 976 O OE1 . GLU A 1 123 ? 10.494 39.202 32.428 1.00 15.59 ? 209 GLU A OE1 1 ATOM 977 O OE2 . GLU A 1 123 ? 9.066 38.634 33.976 1.00 18.60 ? 209 GLU A OE2 1 ATOM 978 N N . ILE A 1 124 ? 9.188 37.933 27.354 1.00 5.66 ? 210 ILE A N 1 ATOM 979 C CA . ILE A 1 124 ? 9.397 38.544 26.033 1.00 4.85 ? 210 ILE A CA 1 ATOM 980 C C . ILE A 1 124 ? 8.405 38.046 24.989 1.00 5.19 ? 210 ILE A C 1 ATOM 981 O O . ILE A 1 124 ? 7.840 38.817 24.212 1.00 6.34 ? 210 ILE A O 1 ATOM 982 C CB . ILE A 1 124 ? 10.864 38.375 25.598 1.00 5.93 ? 210 ILE A CB 1 ATOM 983 C CG1 . ILE A 1 124 ? 11.754 39.215 26.527 1.00 5.82 ? 210 ILE A CG1 1 ATOM 984 C CG2 . ILE A 1 124 ? 11.080 38.738 24.109 1.00 5.56 ? 210 ILE A CG2 1 ATOM 985 C CD1 . ILE A 1 124 ? 13.165 38.695 26.524 1.00 7.36 ? 210 ILE A CD1 1 ATOM 986 N N . LEU A 1 125 ? 8.183 36.733 24.981 1.00 4.60 ? 211 LEU A N 1 ATOM 987 C CA . LEU A 1 125 ? 7.186 36.170 24.067 1.00 5.38 ? 211 LEU A CA 1 ATOM 988 C C . LEU A 1 125 ? 5.775 36.771 24.290 1.00 6.86 ? 211 LEU A C 1 ATOM 989 O O . LEU A 1 125 ? 5.108 37.064 23.344 1.00 6.25 ? 211 LEU A O 1 ATOM 990 C CB . LEU A 1 125 ? 7.173 34.653 24.138 1.00 5.53 ? 211 LEU A CB 1 ATOM 991 C CG . LEU A 1 125 ? 8.485 33.952 23.769 1.00 8.14 ? 211 LEU A CG 1 ATOM 992 C CD1 . LEU A 1 125 ? 8.265 32.474 23.821 1.00 9.26 ? 211 LEU A CD1 1 ATOM 993 C CD2 . LEU A 1 125 ? 9.007 34.313 22.382 1.00 9.52 ? 211 LEU A CD2 1 ATOM 994 N N . ILE A 1 126 ? 5.350 36.917 25.535 1.00 5.21 ? 212 ILE A N 1 ATOM 995 C CA . ILE A 1 126 ? 4.085 37.571 25.864 1.00 6.70 ? 212 ILE A CA 1 ATOM 996 C C . ILE A 1 126 ? 4.044 38.979 25.317 1.00 6.48 ? 212 ILE A C 1 ATOM 997 O O . ILE A 1 126 ? 3.068 39.390 24.672 1.00 6.58 ? 212 ILE A O 1 ATOM 998 C CB . ILE A 1 126 ? 3.877 37.523 27.392 1.00 6.66 ? 212 ILE A CB 1 ATOM 999 C CG1 . ILE A 1 126 ? 3.424 36.107 27.785 1.00 8.57 ? 212 ILE A CG1 1 ATOM 1000 C CG2 . ILE A 1 126 ? 2.871 38.594 27.824 1.00 8.96 ? 212 ILE A CG2 1 ATOM 1001 C CD1 . ILE A 1 126 ? 3.298 35.937 29.286 1.00 9.98 ? 212 ILE A CD1 1 ATOM 1002 N N . SER A 1 127 ? 5.135 39.696 25.495 1.00 7.04 ? 213 SER A N 1 ATOM 1003 C CA . SER A 1 127 ? 5.202 41.084 25.033 1.00 7.39 ? 213 SER A CA 1 ATOM 1004 C C . SER A 1 127 ? 5.023 41.140 23.508 1.00 7.52 ? 213 SER A C 1 ATOM 1005 O O . SER A 1 127 ? 4.350 42.000 22.961 1.00 8.32 ? 213 SER A O 1 ATOM 1006 C CB A SER A 1 127 ? 6.541 41.709 25.458 0.65 8.08 ? 213 SER A CB 1 ATOM 1007 C CB B SER A 1 127 ? 6.473 41.801 25.513 0.35 7.88 ? 213 SER A CB 1 ATOM 1008 O OG A SER A 1 127 ? 6.649 43.039 25.019 0.65 11.00 ? 213 SER A OG 1 ATOM 1009 O OG B SER A 1 127 ? 7.599 41.479 24.739 0.35 9.00 ? 213 SER A OG 1 ATOM 1010 N N . PHE A 1 128 ? 5.593 40.165 22.839 1.00 6.81 ? 214 PHE A N 1 ATOM 1011 C CA . PHE A 1 128 ? 5.457 39.964 21.387 1.00 6.35 ? 214 PHE A CA 1 ATOM 1012 C C . PHE A 1 128 ? 4.455 38.886 20.923 1.00 4.25 ? 214 PHE A C 1 ATOM 1013 O O . PHE A 1 128 ? 4.702 38.207 19.934 1.00 7.44 ? 214 PHE A O 1 ATOM 1014 C CB . PHE A 1 128 ? 6.828 39.730 20.775 1.00 6.64 ? 214 PHE A CB 1 ATOM 1015 C CG . PHE A 1 128 ? 7.692 40.942 20.837 1.00 5.85 ? 214 PHE A CG 1 ATOM 1016 C CD1 . PHE A 1 128 ? 7.533 41.924 19.852 1.00 9.01 ? 214 PHE A CD1 1 ATOM 1017 C CD2 . PHE A 1 128 ? 8.611 41.136 21.853 1.00 8.91 ? 214 PHE A CD2 1 ATOM 1018 C CE1 . PHE A 1 128 ? 8.284 43.071 19.891 1.00 10.90 ? 214 PHE A CE1 1 ATOM 1019 C CE2 . PHE A 1 128 ? 9.390 42.307 21.905 1.00 10.23 ? 214 PHE A CE2 1 ATOM 1020 C CZ . PHE A 1 128 ? 9.224 43.256 20.879 1.00 10.63 ? 214 PHE A CZ 1 ATOM 1021 N N . SER A 1 129 ? 3.334 38.766 21.600 1.00 6.16 ? 215 SER A N 1 ATOM 1022 C CA . SER A 1 129 ? 2.276 37.808 21.242 1.00 5.59 ? 215 SER A CA 1 ATOM 1023 C C . SER A 1 129 ? 1.747 37.953 19.840 1.00 6.42 ? 215 SER A C 1 ATOM 1024 O O . SER A 1 129 ? 1.183 37.013 19.302 1.00 7.31 ? 215 SER A O 1 ATOM 1025 C CB . SER A 1 129 ? 1.104 37.870 22.235 1.00 6.90 ? 215 SER A CB 1 ATOM 1026 O OG . SER A 1 129 ? 0.504 39.196 22.198 1.00 6.85 ? 215 SER A OG 1 ATOM 1027 N N . ASP A 1 130 ? 1.896 39.133 19.246 1.00 6.50 ? 216 ASP A N 1 ATOM 1028 C CA . ASP A 1 130 ? 1.487 39.390 17.884 1.00 7.48 ? 216 ASP A CA 1 ATOM 1029 C C . ASP A 1 130 ? 2.390 38.769 16.811 1.00 7.81 ? 216 ASP A C 1 ATOM 1030 O O . ASP A 1 130 ? 2.054 38.783 15.625 1.00 10.36 ? 216 ASP A O 1 ATOM 1031 C CB . ASP A 1 130 ? 1.361 40.902 17.635 1.00 7.65 ? 216 ASP A CB 1 ATOM 1032 C CG . ASP A 1 130 ? 2.570 41.725 18.060 1.00 10.13 ? 216 ASP A CG 1 ATOM 1033 O OD1 . ASP A 1 130 ? 3.201 41.502 19.129 1.00 9.17 ? 216 ASP A OD1 1 ATOM 1034 O OD2 . ASP A 1 130 ? 2.887 42.725 17.400 1.00 12.95 ? 216 ASP A OD2 1 ATOM 1035 N N . VAL A 1 131 ? 3.539 38.239 17.216 1.00 6.76 ? 217 VAL A N 1 ATOM 1036 C CA . VAL A 1 131 ? 4.472 37.571 16.301 1.00 6.59 ? 217 VAL A CA 1 ATOM 1037 C C . VAL A 1 131 ? 4.460 36.075 16.571 1.00 7.08 ? 217 VAL A C 1 ATOM 1038 O O . VAL A 1 131 ? 4.970 35.659 17.598 1.00 6.98 ? 217 VAL A O 1 ATOM 1039 C CB . VAL A 1 131 ? 5.915 38.092 16.486 1.00 7.66 ? 217 VAL A CB 1 ATOM 1040 C CG1 . VAL A 1 131 ? 6.924 37.326 15.600 1.00 8.31 ? 217 VAL A CG1 1 ATOM 1041 C CG2 . VAL A 1 131 ? 6.030 39.588 16.217 1.00 8.35 ? 217 VAL A CG2 1 ATOM 1042 N N . ARG A 1 132 ? 3.866 35.296 15.679 1.00 6.26 ? 218 ARG A N 1 ATOM 1043 C CA . ARG A 1 132 ? 3.828 33.843 15.875 1.00 5.94 ? 218 ARG A CA 1 ATOM 1044 C C . ARG A 1 132 ? 5.283 33.380 15.965 1.00 6.49 ? 218 ARG A C 1 ATOM 1045 O O . ARG A 1 132 ? 6.120 33.823 15.187 1.00 7.53 ? 218 ARG A O 1 ATOM 1046 C CB . ARG A 1 132 ? 3.106 33.173 14.722 1.00 7.06 ? 218 ARG A CB 1 ATOM 1047 C CG . ARG A 1 132 ? 2.886 31.690 14.946 1.00 7.87 ? 218 ARG A CG 1 ATOM 1048 C CD . ARG A 1 132 ? 2.216 30.990 13.796 1.00 9.75 ? 218 ARG A CD 1 ATOM 1049 N NE . ARG A 1 132 ? 0.893 31.552 13.472 1.00 9.77 ? 218 ARG A NE 1 ATOM 1050 C CZ . ARG A 1 132 ? 0.194 31.151 12.423 1.00 10.65 ? 218 ARG A CZ 1 ATOM 1051 N NH1 . ARG A 1 132 ? 0.703 30.220 11.621 1.00 9.79 ? 218 ARG A NH1 1 ATOM 1052 N NH2 . ARG A 1 132 ? -0.991 31.691 12.160 1.00 11.66 ? 218 ARG A NH2 1 ATOM 1053 N N . THR A 1 133 ? 5.563 32.530 16.934 1.00 6.11 ? 219 THR A N 1 ATOM 1054 C CA . THR A 1 133 ? 6.925 32.114 17.275 1.00 6.45 ? 219 THR A CA 1 ATOM 1055 C C . THR A 1 133 ? 7.045 30.615 17.385 1.00 6.13 ? 219 THR A C 1 ATOM 1056 O O . THR A 1 133 ? 6.303 29.999 18.142 1.00 7.01 ? 219 THR A O 1 ATOM 1057 C CB . THR A 1 133 ? 7.307 32.788 18.582 1.00 6.13 ? 219 THR A CB 1 ATOM 1058 O OG1 . THR A 1 133 ? 7.264 34.201 18.340 1.00 5.96 ? 219 THR A OG1 1 ATOM 1059 C CG2 . THR A 1 133 ? 8.754 32.461 18.983 1.00 6.95 ? 219 THR A CG2 1 ATOM 1060 N N . ILE A 1 134 ? 7.911 30.074 16.551 1.00 5.75 ? 220 ILE A N 1 ATOM 1061 C CA . ILE A 1 134 ? 8.163 28.651 16.452 1.00 5.86 ? 220 ILE A CA 1 ATOM 1062 C C . ILE A 1 134 ? 9.483 28.354 17.123 1.00 5.16 ? 220 ILE A C 1 ATOM 1063 O O . ILE A 1 134 ? 10.513 28.951 16.783 1.00 6.43 ? 220 ILE A O 1 ATOM 1064 C CB . ILE A 1 134 ? 8.157 28.210 14.948 1.00 6.07 ? 220 ILE A CB 1 ATOM 1065 C CG1 . ILE A 1 134 ? 6.775 28.469 14.338 1.00 9.18 ? 220 ILE A CG1 1 ATOM 1066 C CG2 . ILE A 1 134 ? 8.475 26.724 14.819 1.00 8.41 ? 220 ILE A CG2 1 ATOM 1067 C CD1 . ILE A 1 134 ? 6.740 28.622 12.832 1.00 8.99 ? 220 ILE A CD1 1 ATOM 1068 N N . LEU A 1 135 ? 9.436 27.451 18.098 1.00 4.68 ? 221 LEU A N 1 ATOM 1069 C CA . LEU A 1 135 ? 10.634 27.071 18.873 1.00 5.29 ? 221 LEU A CA 1 ATOM 1070 C C . LEU A 1 135 ? 11.069 25.650 18.690 1.00 4.60 ? 221 LEU A C 1 ATOM 1071 O O . LEU A 1 135 ? 10.265 24.742 18.611 1.00 5.46 ? 221 LEU A O 1 ATOM 1072 C CB . LEU A 1 135 ? 10.386 27.226 20.373 1.00 5.41 ? 221 LEU A CB 1 ATOM 1073 C CG . LEU A 1 135 ? 9.800 28.551 20.869 1.00 5.43 ? 221 LEU A CG 1 ATOM 1074 C CD1 . LEU A 1 135 ? 9.505 28.522 22.391 1.00 7.60 ? 221 LEU A CD1 1 ATOM 1075 C CD2 . LEU A 1 135 ? 10.703 29.660 20.551 1.00 8.20 ? 221 LEU A CD2 1 ATOM 1076 N N . VAL A 1 136 ? 12.383 25.502 18.613 1.00 4.11 ? 222 VAL A N 1 ATOM 1077 C CA . VAL A 1 136 ? 13.030 24.224 18.765 1.00 5.16 ? 222 VAL A CA 1 ATOM 1078 C C . VAL A 1 136 ? 13.559 24.184 20.220 1.00 5.80 ? 222 VAL A C 1 ATOM 1079 O O . VAL A 1 136 ? 14.326 25.061 20.599 1.00 6.34 ? 222 VAL A O 1 ATOM 1080 C CB . VAL A 1 136 ? 14.164 23.996 17.754 1.00 5.92 ? 222 VAL A CB 1 ATOM 1081 C CG1 . VAL A 1 136 ? 15.049 22.810 18.196 1.00 6.80 ? 222 VAL A CG1 1 ATOM 1082 C CG2 . VAL A 1 136 ? 13.610 23.731 16.365 1.00 5.68 ? 222 VAL A CG2 1 ATOM 1083 N N . ILE A 1 137 ? 13.206 23.146 20.960 1.00 5.25 ? 223 ILE A N 1 ATOM 1084 C CA . ILE A 1 137 ? 13.610 23.020 22.359 1.00 4.96 ? 223 ILE A CA 1 ATOM 1085 C C . ILE A 1 137 ? 14.819 22.107 22.547 1.00 6.54 ? 223 ILE A C 1 ATOM 1086 O O . ILE A 1 137 ? 14.730 20.922 22.294 1.00 6.51 ? 223 ILE A O 1 ATOM 1087 C CB . ILE A 1 137 ? 12.461 22.548 23.264 1.00 5.43 ? 223 ILE A CB 1 ATOM 1088 C CG1 . ILE A 1 137 ? 11.248 23.482 23.144 1.00 5.52 ? 223 ILE A CG1 1 ATOM 1089 C CG2 . ILE A 1 137 ? 12.920 22.467 24.745 1.00 6.35 ? 223 ILE A CG2 1 ATOM 1090 C CD1 . ILE A 1 137 ? 11.475 24.953 23.485 1.00 7.57 ? 223 ILE A CD1 1 ATOM 1091 N N . GLU A 1 138 ? 15.927 22.713 22.951 1.00 6.05 ? 224 GLU A N 1 ATOM 1092 C CA . GLU A 1 138 ? 17.137 22.008 23.436 1.00 6.47 ? 224 GLU A CA 1 ATOM 1093 C C . GLU A 1 138 ? 17.715 20.860 22.610 1.00 6.74 ? 224 GLU A C 1 ATOM 1094 O O . GLU A 1 138 ? 17.655 19.708 23.005 1.00 6.85 ? 224 GLU A O 1 ATOM 1095 C CB . GLU A 1 138 ? 16.920 21.652 24.901 1.00 6.79 ? 224 GLU A CB 1 ATOM 1096 C CG . GLU A 1 138 ? 16.633 22.867 25.789 1.00 6.52 ? 224 GLU A CG 1 ATOM 1097 C CD . GLU A 1 138 ? 17.842 23.733 26.066 1.00 7.44 ? 224 GLU A CD 1 ATOM 1098 O OE1 . GLU A 1 138 ? 18.996 23.300 25.805 1.00 6.85 ? 224 GLU A OE1 1 ATOM 1099 O OE2 . GLU A 1 138 ? 17.637 24.861 26.579 1.00 5.58 ? 224 GLU A OE2 1 ATOM 1100 N N . PRO A 1 139 ? 18.360 21.193 21.489 1.00 6.74 ? 225 PRO A N 1 ATOM 1101 C CA . PRO A 1 139 ? 19.136 20.190 20.763 1.00 6.20 ? 225 PRO A CA 1 ATOM 1102 C C . PRO A 1 139 ? 20.132 19.485 21.692 1.00 6.59 ? 225 PRO A C 1 ATOM 1103 O O . PRO A 1 139 ? 20.633 20.041 22.675 1.00 5.75 ? 225 PRO A O 1 ATOM 1104 C CB . PRO A 1 139 ? 19.880 21.015 19.725 1.00 7.01 ? 225 PRO A CB 1 ATOM 1105 C CG . PRO A 1 139 ? 18.967 22.215 19.541 1.00 7.96 ? 225 PRO A CG 1 ATOM 1106 C CD . PRO A 1 139 ? 18.521 22.524 20.908 1.00 7.11 ? 225 PRO A CD 1 ATOM 1107 N N . ASP A 1 140 ? 20.378 18.222 21.382 1.00 6.17 ? 226 ASP A N 1 ATOM 1108 C CA . ASP A 1 140 ? 21.388 17.447 22.074 1.00 6.38 ? 226 ASP A CA 1 ATOM 1109 C C . ASP A 1 140 ? 21.141 17.355 23.571 1.00 6.45 ? 226 ASP A C 1 ATOM 1110 O O . ASP A 1 140 ? 22.088 17.466 24.344 1.00 5.60 ? 226 ASP A O 1 ATOM 1111 C CB . ASP A 1 140 ? 22.777 18.025 21.804 1.00 7.90 ? 226 ASP A CB 1 ATOM 1112 C CG . ASP A 1 140 ? 23.889 17.127 22.265 1.00 9.43 ? 226 ASP A CG 1 ATOM 1113 O OD1 . ASP A 1 140 ? 23.733 15.890 22.215 1.00 9.30 ? 226 ASP A OD1 1 ATOM 1114 O OD2 . ASP A 1 140 ? 24.964 17.623 22.689 1.00 9.71 ? 226 ASP A OD2 1 ATOM 1115 N N . SER A 1 141 ? 19.874 17.182 23.951 1.00 5.85 ? 227 SER A N 1 ATOM 1116 C CA . SER A 1 141 ? 19.494 17.083 25.368 1.00 6.36 ? 227 SER A CA 1 ATOM 1117 C C . SER A 1 141 ? 18.923 15.715 25.672 1.00 6.59 ? 227 SER A C 1 ATOM 1118 O O . SER A 1 141 ? 19.669 14.764 25.886 1.00 5.73 ? 227 SER A O 1 ATOM 1119 C CB . SER A 1 141 ? 18.575 18.241 25.821 1.00 6.89 ? 227 SER A CB 1 ATOM 1120 O OG . SER A 1 141 ? 17.311 18.250 25.168 1.00 6.97 ? 227 SER A OG 1 ATOM 1121 N N . LEU A 1 142 ? 17.624 15.565 25.612 1.00 6.38 ? 228 LEU A N 1 ATOM 1122 C CA . LEU A 1 142 ? 16.963 14.289 25.923 1.00 6.15 ? 228 LEU A CA 1 ATOM 1123 C C . LEU A 1 142 ? 17.353 13.101 25.053 1.00 6.83 ? 228 LEU A C 1 ATOM 1124 O O . LEU A 1 142 ? 17.273 11.968 25.508 1.00 6.54 ? 228 LEU A O 1 ATOM 1125 C CB . LEU A 1 142 ? 15.449 14.481 25.924 1.00 8.10 ? 228 LEU A CB 1 ATOM 1126 C CG . LEU A 1 142 ? 14.869 15.397 27.003 1.00 8.10 ? 228 LEU A CG 1 ATOM 1127 C CD1 . LEU A 1 142 ? 13.399 15.673 26.746 1.00 10.52 ? 228 LEU A CD1 1 ATOM 1128 C CD2 . LEU A 1 142 ? 15.076 14.901 28.391 1.00 10.06 ? 228 LEU A CD2 1 ATOM 1129 N N . ALA A 1 143 ? 17.886 13.321 23.855 1.00 6.78 ? 229 ALA A N 1 ATOM 1130 C CA . ALA A 1 143 ? 18.377 12.204 23.052 1.00 7.14 ? 229 ALA A CA 1 ATOM 1131 C C . ALA A 1 143 ? 19.489 11.459 23.815 1.00 7.19 ? 229 ALA A C 1 ATOM 1132 O O . ALA A 1 143 ? 19.643 10.241 23.667 1.00 8.04 ? 229 ALA A O 1 ATOM 1133 C CB . ALA A 1 143 ? 18.845 12.645 21.681 1.00 7.52 ? 229 ALA A CB 1 ATOM 1134 N N . ASN A 1 144 ? 20.229 12.164 24.662 1.00 7.80 ? 230 ASN A N 1 ATOM 1135 C CA . ASN A 1 144 ? 21.259 11.539 25.506 1.00 7.17 ? 230 ASN A CA 1 ATOM 1136 C C . ASN A 1 144 ? 20.706 10.587 26.568 1.00 7.43 ? 230 ASN A C 1 ATOM 1137 O O . ASN A 1 144 ? 21.400 9.662 26.983 1.00 7.06 ? 230 ASN A O 1 ATOM 1138 C CB . ASN A 1 144 ? 22.151 12.581 26.193 1.00 6.20 ? 230 ASN A CB 1 ATOM 1139 C CG . ASN A 1 144 ? 22.966 13.370 25.202 1.00 7.98 ? 230 ASN A CG 1 ATOM 1140 O OD1 . ASN A 1 144 ? 23.921 12.844 24.622 1.00 8.60 ? 230 ASN A OD1 1 ATOM 1141 N ND2 . ASN A 1 144 ? 22.621 14.678 25.026 1.00 6.51 ? 230 ASN A ND2 1 ATOM 1142 N N . MET A 1 145 ? 19.472 10.803 27.003 1.00 7.56 ? 231 MET A N 1 ATOM 1143 C CA . MET A 1 145 ? 18.853 9.889 27.968 1.00 8.41 ? 231 MET A CA 1 ATOM 1144 C C . MET A 1 145 ? 18.509 8.574 27.289 1.00 7.98 ? 231 MET A C 1 ATOM 1145 O O . MET A 1 145 ? 18.397 7.568 27.975 1.00 9.59 ? 231 MET A O 1 ATOM 1146 C CB . MET A 1 145 ? 17.639 10.459 28.653 1.00 8.74 ? 231 MET A CB 1 ATOM 1147 C CG . MET A 1 145 ? 17.925 11.365 29.883 1.00 7.66 ? 231 MET A CG 1 ATOM 1148 S SD . MET A 1 145 ? 18.672 12.966 29.497 1.00 8.80 ? 231 MET A SD 1 ATOM 1149 C CE . MET A 1 145 ? 20.371 12.578 29.748 1.00 7.19 ? 231 MET A CE 1 ATOM 1150 N N . VAL A 1 146 ? 18.396 8.554 25.963 1.00 6.61 ? 232 VAL A N 1 ATOM 1151 C CA . VAL A 1 146 ? 18.095 7.283 25.268 1.00 7.88 ? 232 VAL A CA 1 ATOM 1152 C C . VAL A 1 146 ? 19.325 6.379 25.155 1.00 8.64 ? 232 VAL A C 1 ATOM 1153 O O . VAL A 1 146 ? 19.234 5.183 25.425 1.00 9.71 ? 232 VAL A O 1 ATOM 1154 C CB . VAL A 1 146 ? 17.497 7.491 23.871 1.00 7.12 ? 232 VAL A CB 1 ATOM 1155 C CG1 . VAL A 1 146 ? 17.197 6.168 23.193 1.00 8.02 ? 232 VAL A CG1 1 ATOM 1156 C CG2 . VAL A 1 146 ? 16.252 8.427 23.964 1.00 8.75 ? 232 VAL A CG2 1 ATOM 1157 N N . THR A 1 147 ? 20.470 6.935 24.794 1.00 8.20 ? 233 THR A N 1 ATOM 1158 C CA . THR A 1 147 ? 21.634 6.110 24.475 1.00 8.57 ? 233 THR A CA 1 ATOM 1159 C C . THR A 1 147 ? 22.881 6.312 25.316 1.00 8.26 ? 233 THR A C 1 ATOM 1160 O O . THR A 1 147 ? 23.751 5.485 25.272 1.00 9.17 ? 233 THR A O 1 ATOM 1161 C CB . THR A 1 147 ? 22.038 6.245 23.004 1.00 8.97 ? 233 THR A CB 1 ATOM 1162 O OG1 . THR A 1 147 ? 22.538 7.588 22.780 1.00 7.27 ? 233 THR A OG1 1 ATOM 1163 C CG2 . THR A 1 147 ? 20.828 6.068 22.077 1.00 10.80 ? 233 THR A CG2 1 ATOM 1164 N N . ASN A 1 148 ? 22.965 7.406 26.067 1.00 7.13 ? 234 ASN A N 1 ATOM 1165 C CA . ASN A 1 148 ? 24.208 7.814 26.721 1.00 7.81 ? 234 ASN A CA 1 ATOM 1166 C C . ASN A 1 148 ? 24.131 7.847 28.240 1.00 8.24 ? 234 ASN A C 1 ATOM 1167 O O . ASN A 1 148 ? 24.947 8.517 28.899 1.00 8.30 ? 234 ASN A O 1 ATOM 1168 C CB . ASN A 1 148 ? 24.690 9.172 26.172 1.00 8.25 ? 234 ASN A CB 1 ATOM 1169 C CG . ASN A 1 148 ? 25.013 9.108 24.697 1.00 12.87 ? 234 ASN A CG 1 ATOM 1170 O OD1 . ASN A 1 148 ? 25.500 8.085 24.203 1.00 13.76 ? 234 ASN A OD1 1 ATOM 1171 N ND2 . ASN A 1 148 ? 24.798 10.221 23.986 1.00 8.48 ? 234 ASN A ND2 1 ATOM 1172 N N . MET A 1 149 ? 23.229 7.065 28.813 1.00 7.83 ? 235 MET A N 1 ATOM 1173 C CA . MET A 1 149 ? 23.104 7.048 30.274 1.00 8.33 ? 235 MET A CA 1 ATOM 1174 C C . MET A 1 149 ? 24.285 6.355 30.962 1.00 8.07 ? 235 MET A C 1 ATOM 1175 O O . MET A 1 149 ? 24.418 6.444 32.180 1.00 8.43 ? 235 MET A O 1 ATOM 1176 C CB . MET A 1 149 ? 21.766 6.467 30.735 1.00 9.34 ? 235 MET A CB 1 ATOM 1177 C CG . MET A 1 149 ? 20.571 7.349 30.419 1.00 9.89 ? 235 MET A CG 1 ATOM 1178 S SD . MET A 1 149 ? 20.523 8.801 31.477 1.00 11.07 ? 235 MET A SD 1 ATOM 1179 C CE . MET A 1 149 ? 20.080 8.064 33.025 1.00 11.78 ? 235 MET A CE 1 ATOM 1180 N N . ASN A 1 150 ? 25.152 5.711 30.184 1.00 9.59 ? 236 ASN A N 1 ATOM 1181 C CA . ASN A 1 150 ? 26.405 5.170 30.706 1.00 10.60 ? 236 ASN A CA 1 ATOM 1182 C C . ASN A 1 150 ? 27.420 6.294 31.010 1.00 10.40 ? 236 ASN A C 1 ATOM 1183 O O . ASN A 1 150 ? 28.323 6.130 31.799 1.00 10.86 ? 236 ASN A O 1 ATOM 1184 C CB . ASN A 1 150 ? 26.995 4.171 29.740 1.00 12.51 ? 236 ASN A CB 1 ATOM 1185 C CG . ASN A 1 150 ? 27.308 4.822 28.407 1.00 15.35 ? 236 ASN A CG 1 ATOM 1186 O OD1 . ASN A 1 150 ? 26.405 5.190 27.672 1.00 18.47 ? 236 ASN A OD1 1 ATOM 1187 N ND2 . ASN A 1 150 ? 28.578 5.008 28.123 1.00 20.54 ? 236 ASN A ND2 1 ATOM 1188 N N . VAL A 1 151 ? 27.249 7.466 30.409 1.00 8.93 ? 237 VAL A N 1 ATOM 1189 C CA . VAL A 1 151 ? 28.128 8.592 30.672 1.00 9.45 ? 237 VAL A CA 1 ATOM 1190 C C . VAL A 1 151 ? 27.764 9.249 32.022 1.00 9.28 ? 237 VAL A C 1 ATOM 1191 O O . VAL A 1 151 ? 26.642 9.721 32.181 1.00 9.22 ? 237 VAL A O 1 ATOM 1192 C CB . VAL A 1 151 ? 28.028 9.693 29.583 1.00 9.51 ? 237 VAL A CB 1 ATOM 1193 C CG1 . VAL A 1 151 ? 29.006 10.869 29.899 1.00 9.73 ? 237 VAL A CG1 1 ATOM 1194 C CG2 . VAL A 1 151 ? 28.330 9.170 28.216 1.00 10.86 ? 237 VAL A CG2 1 ATOM 1195 N N . PRO A 1 152 ? 28.687 9.306 32.977 1.00 9.68 ? 238 PRO A N 1 ATOM 1196 C CA . PRO A 1 152 ? 28.354 9.851 34.276 1.00 8.95 ? 238 PRO A CA 1 ATOM 1197 C C . PRO A 1 152 ? 27.645 11.207 34.254 1.00 8.43 ? 238 PRO A C 1 ATOM 1198 O O . PRO A 1 152 ? 26.660 11.416 34.989 1.00 8.29 ? 238 PRO A O 1 ATOM 1199 C CB . PRO A 1 152 ? 29.704 9.854 35.019 1.00 10.54 ? 238 PRO A CB 1 ATOM 1200 C CG . PRO A 1 152 ? 30.436 8.688 34.420 1.00 10.34 ? 238 PRO A CG 1 ATOM 1201 C CD . PRO A 1 152 ? 30.048 8.727 32.938 1.00 10.93 ? 238 PRO A CD 1 ATOM 1202 N N . LYS A 1 153 ? 28.149 12.133 33.463 1.00 8.07 ? 239 LYS A N 1 ATOM 1203 C CA . LYS A 1 153 ? 27.533 13.464 33.385 1.00 7.77 ? 239 LYS A CA 1 ATOM 1204 C C . LYS A 1 153 ? 26.092 13.385 32.898 1.00 8.28 ? 239 LYS A C 1 ATOM 1205 O O . LYS A 1 153 ? 25.223 14.141 33.387 1.00 6.85 ? 239 LYS A O 1 ATOM 1206 C CB . LYS A 1 153 ? 28.380 14.407 32.529 1.00 9.61 ? 239 LYS A CB 1 ATOM 1207 C CG . LYS A 1 153 ? 27.887 15.829 32.513 1.00 9.10 ? 239 LYS A CG 1 ATOM 1208 C CD . LYS A 1 153 ? 28.909 16.730 31.821 1.00 11.74 ? 239 LYS A CD 1 ATOM 1209 C CE . LYS A 1 153 ? 28.438 18.173 31.768 1.00 11.37 ? 239 LYS A CE 1 ATOM 1210 N NZ . LYS A 1 153 ? 29.413 19.027 31.022 1.00 14.95 ? 239 LYS A NZ 1 ATOM 1211 N N . CYS A 1 154 ? 25.815 12.459 31.971 1.00 8.37 ? 240 CYS A N 1 ATOM 1212 C CA . CYS A 1 154 ? 24.432 12.330 31.497 1.00 8.99 ? 240 CYS A CA 1 ATOM 1213 C C . CYS A 1 154 ? 23.532 11.721 32.562 1.00 9.22 ? 240 CYS A C 1 ATOM 1214 O O . CYS A 1 154 ? 22.420 12.196 32.803 1.00 7.80 ? 240 CYS A O 1 ATOM 1215 C CB . CYS A 1 154 ? 24.356 11.503 30.221 1.00 8.27 ? 240 CYS A CB 1 ATOM 1216 S SG . CYS A 1 154 ? 25.064 12.305 28.763 1.00 9.46 ? 240 CYS A SG 1 ATOM 1217 N N . SER A 1 155 ? 23.995 10.662 33.208 1.00 8.60 ? 241 SER A N 1 ATOM 1218 C CA . SER A 1 155 ? 23.187 10.055 34.254 1.00 9.16 ? 241 SER A CA 1 ATOM 1219 C C . SER A 1 155 ? 22.897 11.060 35.367 1.00 9.25 ? 241 SER A C 1 ATOM 1220 O O . SER A 1 155 ? 21.799 11.083 35.906 1.00 10.04 ? 241 SER A O 1 ATOM 1221 C CB . SER A 1 155 ? 23.822 8.775 34.788 1.00 9.68 ? 241 SER A CB 1 ATOM 1222 O OG . SER A 1 155 ? 22.999 8.217 35.812 1.00 14.66 ? 241 SER A OG 1 ATOM 1223 N N . GLY A 1 156 ? 23.885 11.887 35.699 1.00 8.89 ? 242 GLY A N 1 ATOM 1224 C CA . GLY A 1 156 ? 23.742 12.860 36.793 1.00 9.18 ? 242 GLY A CA 1 ATOM 1225 C C . GLY A 1 156 ? 22.852 14.029 36.398 1.00 8.31 ? 242 GLY A C 1 ATOM 1226 O O . GLY A 1 156 ? 22.235 14.627 37.288 1.00 10.24 ? 242 GLY A O 1 ATOM 1227 N N . ALA A 1 157 ? 22.747 14.266 35.091 1.00 7.75 ? 243 ALA A N 1 ATOM 1228 C CA . ALA A 1 157 ? 21.961 15.367 34.540 1.00 7.52 ? 243 ALA A CA 1 ATOM 1229 C C . ALA A 1 157 ? 20.544 14.975 34.120 1.00 7.27 ? 243 ALA A C 1 ATOM 1230 O O . ALA A 1 157 ? 19.694 15.838 33.927 1.00 7.22 ? 243 ALA A O 1 ATOM 1231 C CB . ALA A 1 157 ? 22.688 16.009 33.382 1.00 8.36 ? 243 ALA A CB 1 ATOM 1232 N N . ALA A 1 158 ? 20.248 13.694 34.073 1.00 7.75 ? 244 ALA A N 1 ATOM 1233 C CA . ALA A 1 158 ? 19.006 13.218 33.441 1.00 8.16 ? 244 ALA A CA 1 ATOM 1234 C C . ALA A 1 158 ? 17.751 13.789 34.079 1.00 8.14 ? 244 ALA A C 1 ATOM 1235 O O . ALA A 1 158 ? 16.830 14.245 33.369 1.00 7.54 ? 244 ALA A O 1 ATOM 1236 C CB . ALA A 1 158 ? 18.952 11.703 33.392 1.00 8.85 ? 244 ALA A CB 1 ATOM 1237 N N . SER A 1 159 ? 17.696 13.779 35.403 1.00 7.43 ? 245 SER A N 1 ATOM 1238 C CA . SER A 1 159 ? 16.481 14.256 36.060 1.00 8.84 ? 245 SER A CA 1 ATOM 1239 C C . SER A 1 159 ? 16.324 15.751 35.844 1.00 9.12 ? 245 SER A C 1 ATOM 1240 O O . SER A 1 159 ? 15.202 16.248 35.779 1.00 8.67 ? 245 SER A O 1 ATOM 1241 C CB A SER A 1 159 ? 16.437 13.964 37.577 0.75 9.84 ? 245 SER A CB 1 ATOM 1242 C CB B SER A 1 159 ? 16.475 13.877 37.545 0.25 9.16 ? 245 SER A CB 1 ATOM 1243 O OG A SER A 1 159 ? 17.484 14.613 38.274 0.75 8.17 ? 245 SER A OG 1 ATOM 1244 O OG B SER A 1 159 ? 16.499 12.459 37.681 0.25 9.51 ? 245 SER A OG 1 ATOM 1245 N N . THR A 1 160 ? 17.444 16.442 35.739 1.00 8.34 ? 246 THR A N 1 ATOM 1246 C CA . THR A 1 160 ? 17.457 17.872 35.484 1.00 8.48 ? 246 THR A CA 1 ATOM 1247 C C . THR A 1 160 ? 17.008 18.166 34.048 1.00 7.53 ? 246 THR A C 1 ATOM 1248 O O . THR A 1 160 ? 16.164 19.033 33.823 1.00 7.88 ? 246 THR A O 1 ATOM 1249 C CB . THR A 1 160 ? 18.858 18.475 35.782 1.00 8.88 ? 246 THR A CB 1 ATOM 1250 O OG1 . THR A 1 160 ? 19.132 18.319 37.183 1.00 10.13 ? 246 THR A OG1 1 ATOM 1251 C CG2 . THR A 1 160 ? 18.896 19.972 35.483 1.00 10.51 ? 246 THR A CG2 1 ATOM 1252 N N . TYR A 1 161 ? 17.541 17.449 33.071 1.00 6.91 ? 247 TYR A N 1 ATOM 1253 C CA . TYR A 1 161 ? 17.085 17.610 31.701 1.00 7.24 ? 247 TYR A CA 1 ATOM 1254 C C . TYR A 1 161 ? 15.585 17.381 31.608 1.00 7.07 ? 247 TYR A C 1 ATOM 1255 O O . TYR A 1 161 ? 14.863 18.156 30.997 1.00 7.45 ? 247 TYR A O 1 ATOM 1256 C CB . TYR A 1 161 ? 17.785 16.684 30.714 1.00 7.40 ? 247 TYR A CB 1 ATOM 1257 C CG . TYR A 1 161 ? 19.190 16.985 30.285 1.00 6.78 ? 247 TYR A CG 1 ATOM 1258 C CD1 . TYR A 1 161 ? 19.994 17.966 30.908 1.00 5.70 ? 247 TYR A CD1 1 ATOM 1259 C CD2 . TYR A 1 161 ? 19.727 16.277 29.238 1.00 7.69 ? 247 TYR A CD2 1 ATOM 1260 C CE1 . TYR A 1 161 ? 21.291 18.184 30.478 1.00 6.59 ? 247 TYR A CE1 1 ATOM 1261 C CE2 . TYR A 1 161 ? 21.004 16.494 28.799 1.00 8.06 ? 247 TYR A CE2 1 ATOM 1262 C CZ . TYR A 1 161 ? 21.792 17.445 29.406 1.00 8.46 ? 247 TYR A CZ 1 ATOM 1263 O OH . TYR A 1 161 ? 23.109 17.594 28.943 1.00 7.28 ? 247 TYR A OH 1 ATOM 1264 N N . ARG A 1 162 ? 15.102 16.314 32.224 1.00 7.18 ? 248 ARG A N 1 ATOM 1265 C CA . ARG A 1 162 ? 13.676 16.048 32.179 1.00 8.07 ? 248 ARG A CA 1 ATOM 1266 C C . ARG A 1 162 ? 12.850 17.146 32.830 1.00 7.75 ? 248 ARG A C 1 ATOM 1267 O O . ARG A 1 162 ? 11.889 17.646 32.248 1.00 9.84 ? 248 ARG A O 1 ATOM 1268 C CB A ARG A 1 162 ? 13.353 14.725 32.862 0.50 8.87 ? 248 ARG A CB 1 ATOM 1269 C CB B ARG A 1 162 ? 13.361 14.691 32.814 0.50 8.04 ? 248 ARG A CB 1 ATOM 1270 C CG A ARG A 1 162 ? 11.933 14.278 32.600 0.50 11.33 ? 248 ARG A CG 1 ATOM 1271 C CG B ARG A 1 162 ? 13.935 13.541 31.988 0.50 6.91 ? 248 ARG A CG 1 ATOM 1272 C CD A ARG A 1 162 ? 11.559 12.966 33.266 0.50 14.30 ? 248 ARG A CD 1 ATOM 1273 C CD B ARG A 1 162 ? 13.630 12.136 32.465 0.50 10.62 ? 248 ARG A CD 1 ATOM 1274 N NE A ARG A 1 162 ? 10.132 12.961 33.584 0.50 13.21 ? 248 ARG A NE 1 ATOM 1275 N NE B ARG A 1 162 ? 12.244 11.707 32.420 0.50 14.06 ? 248 ARG A NE 1 ATOM 1276 C CZ A ARG A 1 162 ? 9.595 13.439 34.706 0.50 15.13 ? 248 ARG A CZ 1 ATOM 1277 C CZ B ARG A 1 162 ? 11.870 10.450 32.180 0.50 16.81 ? 248 ARG A CZ 1 ATOM 1278 N NH1 A ARG A 1 162 ? 10.333 13.961 35.683 0.50 17.16 ? 248 ARG A NH1 1 ATOM 1279 N NH1 B ARG A 1 162 ? 12.786 9.513 31.933 0.50 16.53 ? 248 ARG A NH1 1 ATOM 1280 N NH2 A ARG A 1 162 ? 8.284 13.415 34.864 0.50 15.53 ? 248 ARG A NH2 1 ATOM 1281 N NH2 B ARG A 1 162 ? 10.578 10.113 32.197 0.50 17.08 ? 248 ARG A NH2 1 ATOM 1282 N N . GLU A 1 163 ? 13.181 17.480 34.073 1.00 8.65 ? 249 GLU A N 1 ATOM 1283 C CA . GLU A 1 163 ? 12.401 18.465 34.824 1.00 9.08 ? 249 GLU A CA 1 ATOM 1284 C C . GLU A 1 163 ? 12.401 19.819 34.124 1.00 8.48 ? 249 GLU A C 1 ATOM 1285 O O . GLU A 1 163 ? 11.370 20.486 34.025 1.00 7.36 ? 249 GLU A O 1 ATOM 1286 C CB A GLU A 1 163 ? 12.854 18.586 36.268 0.55 9.86 ? 249 GLU A CB 1 ATOM 1287 C CB B GLU A 1 163 ? 13.003 18.603 36.244 0.45 10.22 ? 249 GLU A CB 1 ATOM 1288 C CG A GLU A 1 163 ? 12.420 17.388 37.093 0.55 12.43 ? 249 GLU A CG 1 ATOM 1289 C CG B GLU A 1 163 ? 12.536 19.813 37.054 0.45 13.40 ? 249 GLU A CG 1 ATOM 1290 C CD A GLU A 1 163 ? 13.233 17.229 38.365 0.55 16.20 ? 249 GLU A CD 1 ATOM 1291 C CD B GLU A 1 163 ? 13.588 20.464 37.978 0.45 18.47 ? 249 GLU A CD 1 ATOM 1292 O OE1 A GLU A 1 163 ? 13.882 18.215 38.802 0.55 17.89 ? 249 GLU A OE1 1 ATOM 1293 O OE1 B GLU A 1 163 ? 14.809 20.115 37.988 0.45 17.59 ? 249 GLU A OE1 1 ATOM 1294 O OE2 A GLU A 1 163 ? 13.208 16.110 38.923 0.55 17.22 ? 249 GLU A OE2 1 ATOM 1295 O OE2 B GLU A 1 163 ? 13.172 21.378 38.733 0.45 19.31 ? 249 GLU A OE2 1 ATOM 1296 N N . LEU A 1 164 ? 13.572 20.226 33.669 1.00 6.23 ? 250 LEU A N 1 ATOM 1297 C CA . LEU A 1 164 ? 13.698 21.528 33.022 1.00 6.96 ? 250 LEU A CA 1 ATOM 1298 C C . LEU A 1 164 ? 13.052 21.542 31.633 1.00 7.55 ? 250 LEU A C 1 ATOM 1299 O O . LEU A 1 164 ? 12.537 22.584 31.213 1.00 8.07 ? 250 LEU A O 1 ATOM 1300 C CB . LEU A 1 164 ? 15.145 22.003 32.969 1.00 7.55 ? 250 LEU A CB 1 ATOM 1301 C CG . LEU A 1 164 ? 15.752 22.293 34.338 1.00 7.46 ? 250 LEU A CG 1 ATOM 1302 C CD1 . LEU A 1 164 ? 17.140 22.829 34.154 1.00 7.97 ? 250 LEU A CD1 1 ATOM 1303 C CD2 . LEU A 1 164 ? 14.850 23.310 35.116 1.00 9.16 ? 250 LEU A CD2 1 ATOM 1304 N N . THR A 1 165 ? 13.032 20.411 30.932 1.00 7.73 ? 251 THR A N 1 ATOM 1305 C CA . THR A 1 165 ? 12.310 20.372 29.639 1.00 8.24 ? 251 THR A CA 1 ATOM 1306 C C . THR A 1 165 ? 10.818 20.562 29.937 1.00 7.64 ? 251 THR A C 1 ATOM 1307 O O . THR A 1 165 ? 10.143 21.378 29.310 1.00 8.70 ? 251 THR A O 1 ATOM 1308 C CB . THR A 1 165 ? 12.542 19.076 28.907 1.00 9.15 ? 251 THR A CB 1 ATOM 1309 O OG1 . THR A 1 165 ? 13.945 18.949 28.667 1.00 11.24 ? 251 THR A OG1 1 ATOM 1310 C CG2 . THR A 1 165 ? 11.832 19.077 27.563 1.00 7.41 ? 251 THR A CG2 1 ATOM 1311 N N . ILE A 1 166 ? 10.293 19.819 30.921 1.00 7.68 ? 252 ILE A N 1 ATOM 1312 C CA . ILE A 1 166 ? 8.883 19.947 31.278 1.00 8.24 ? 252 ILE A CA 1 ATOM 1313 C C . ILE A 1 166 ? 8.572 21.419 31.663 1.00 7.90 ? 252 ILE A C 1 ATOM 1314 O O . ILE A 1 166 ? 7.538 22.007 31.270 1.00 8.42 ? 252 ILE A O 1 ATOM 1315 C CB . ILE A 1 166 ? 8.522 18.954 32.362 1.00 8.53 ? 252 ILE A CB 1 ATOM 1316 C CG1 . ILE A 1 166 ? 8.513 17.542 31.775 1.00 9.56 ? 252 ILE A CG1 1 ATOM 1317 C CG2 . ILE A 1 166 ? 7.136 19.287 32.976 1.00 10.24 ? 252 ILE A CG2 1 ATOM 1318 C CD1 . ILE A 1 166 ? 8.569 16.435 32.854 1.00 10.97 ? 252 ILE A CD1 1 ATOM 1319 N N . TYR A 1 167 ? 9.479 22.012 32.424 1.00 9.18 ? 253 TYR A N 1 ATOM 1320 C CA . TYR A 1 167 ? 9.332 23.409 32.841 1.00 8.98 ? 253 TYR A CA 1 ATOM 1321 C C . TYR A 1 167 ? 9.194 24.313 31.606 1.00 8.21 ? 253 TYR A C 1 ATOM 1322 O O . TYR A 1 167 ? 8.259 25.135 31.525 1.00 8.51 ? 253 TYR A O 1 ATOM 1323 C CB . TYR A 1 167 ? 10.529 23.861 33.669 1.00 8.44 ? 253 TYR A CB 1 ATOM 1324 C CG . TYR A 1 167 ? 10.323 25.216 34.322 1.00 7.28 ? 253 TYR A CG 1 ATOM 1325 C CD1 . TYR A 1 167 ? 9.518 25.336 35.454 1.00 10.43 ? 253 TYR A CD1 1 ATOM 1326 C CD2 . TYR A 1 167 ? 10.904 26.344 33.813 1.00 7.91 ? 253 TYR A CD2 1 ATOM 1327 C CE1 . TYR A 1 167 ? 9.331 26.562 36.050 1.00 12.12 ? 253 TYR A CE1 1 ATOM 1328 C CE2 . TYR A 1 167 ? 10.703 27.582 34.422 1.00 8.20 ? 253 TYR A CE2 1 ATOM 1329 C CZ . TYR A 1 167 ? 9.950 27.668 35.547 1.00 9.92 ? 253 TYR A CZ 1 ATOM 1330 O OH . TYR A 1 167 ? 9.733 28.912 36.149 1.00 11.42 ? 253 TYR A OH 1 ATOM 1331 N N . ALA A 1 168 ? 10.103 24.188 30.646 1.00 7.19 ? 254 ALA A N 1 ATOM 1332 C CA . ALA A 1 168 ? 10.041 24.994 29.427 1.00 6.61 ? 254 ALA A CA 1 ATOM 1333 C C . ALA A 1 168 ? 8.748 24.721 28.634 1.00 6.57 ? 254 ALA A C 1 ATOM 1334 O O . ALA A 1 168 ? 8.101 25.652 28.144 1.00 6.79 ? 254 ALA A O 1 ATOM 1335 C CB . ALA A 1 168 ? 11.231 24.771 28.543 1.00 7.10 ? 254 ALA A CB 1 ATOM 1336 N N . LEU A 1 169 ? 8.364 23.460 28.508 1.00 6.74 ? 255 LEU A N 1 ATOM 1337 C CA . LEU A 1 169 ? 7.146 23.159 27.731 1.00 6.68 ? 255 LEU A CA 1 ATOM 1338 C C . LEU A 1 169 ? 5.917 23.791 28.366 1.00 7.19 ? 255 LEU A C 1 ATOM 1339 O O . LEU A 1 169 ? 5.000 24.202 27.651 1.00 8.91 ? 255 LEU A O 1 ATOM 1340 C CB . LEU A 1 169 ? 6.891 21.655 27.596 1.00 7.06 ? 255 LEU A CB 1 ATOM 1341 C CG . LEU A 1 169 ? 7.978 20.878 26.879 1.00 6.79 ? 255 LEU A CG 1 ATOM 1342 C CD1 . LEU A 1 169 ? 7.591 19.392 26.865 1.00 8.65 ? 255 LEU A CD1 1 ATOM 1343 C CD2 . LEU A 1 169 ? 8.256 21.337 25.498 1.00 7.99 ? 255 LEU A CD2 1 ATOM 1344 N N . LYS A 1 170 ? 5.842 23.798 29.675 1.00 6.55 ? 256 LYS A N 1 ATOM 1345 C CA . LYS A 1 170 ? 4.665 24.428 30.326 1.00 7.30 ? 256 LYS A CA 1 ATOM 1346 C C . LYS A 1 170 ? 4.774 25.939 30.316 1.00 7.16 ? 256 LYS A C 1 ATOM 1347 O O . LYS A 1 170 ? 3.773 26.644 30.109 1.00 7.80 ? 256 LYS A O 1 ATOM 1348 C CB . LYS A 1 170 ? 4.524 23.947 31.762 1.00 8.01 ? 256 LYS A CB 1 ATOM 1349 C CG . LYS A 1 170 ? 4.141 22.465 31.854 1.00 12.14 ? 256 LYS A CG 1 ATOM 1350 C CD . LYS A 1 170 ? 3.991 22.118 33.332 1.00 14.65 ? 256 LYS A CD 1 ATOM 1351 C CE . LYS A 1 170 ? 3.202 20.875 33.541 1.00 22.80 ? 256 LYS A CE 1 ATOM 1352 N NZ . LYS A 1 170 ? 2.532 20.854 34.865 1.00 24.69 ? 256 LYS A NZ 1 ATOM 1353 N N . GLN A 1 171 ? 5.957 26.474 30.586 1.00 5.87 ? 257 GLN A N 1 ATOM 1354 C CA . GLN A 1 171 ? 6.084 27.943 30.687 1.00 7.43 ? 257 GLN A CA 1 ATOM 1355 C C . GLN A 1 171 ? 5.972 28.648 29.336 1.00 6.98 ? 257 GLN A C 1 ATOM 1356 O O . GLN A 1 171 ? 5.513 29.787 29.272 1.00 7.86 ? 257 GLN A O 1 ATOM 1357 C CB . GLN A 1 171 ? 7.391 28.352 31.361 1.00 7.28 ? 257 GLN A CB 1 ATOM 1358 C CG . GLN A 1 171 ? 7.482 27.937 32.833 1.00 9.83 ? 257 GLN A CG 1 ATOM 1359 C CD . GLN A 1 171 ? 6.348 28.523 33.627 1.00 16.56 ? 257 GLN A CD 1 ATOM 1360 O OE1 . GLN A 1 171 ? 6.154 29.726 33.610 1.00 18.22 ? 257 GLN A OE1 1 ATOM 1361 N NE2 . GLN A 1 171 ? 5.555 27.668 34.272 1.00 20.25 ? 257 GLN A NE2 1 ATOM 1362 N N . LEU A 1 172 ? 6.317 27.963 28.255 1.00 6.23 ? 258 LEU A N 1 ATOM 1363 C CA . LEU A 1 172 ? 6.295 28.550 26.910 1.00 6.37 ? 258 LEU A CA 1 ATOM 1364 C C . LEU A 1 172 ? 5.038 28.096 26.143 1.00 5.51 ? 258 LEU A C 1 ATOM 1365 O O . LEU A 1 172 ? 4.894 28.350 24.956 1.00 7.83 ? 258 LEU A O 1 ATOM 1366 C CB . LEU A 1 172 ? 7.604 28.307 26.202 1.00 5.37 ? 258 LEU A CB 1 ATOM 1367 C CG . LEU A 1 172 ? 8.866 28.761 26.944 1.00 6.36 ? 258 LEU A CG 1 ATOM 1368 C CD1 . LEU A 1 172 ? 10.144 28.521 26.170 1.00 10.29 ? 258 LEU A CD1 1 ATOM 1369 C CD2 . LEU A 1 172 ? 8.763 30.265 27.299 1.00 6.89 ? 258 LEU A CD2 1 ATOM 1370 N N . ASP A 1 173 ? 4.139 27.453 26.861 1.00 5.99 ? 259 ASP A N 1 ATOM 1371 C CA . ASP A 1 173 ? 2.889 26.979 26.258 1.00 6.70 ? 259 ASP A CA 1 ATOM 1372 C C . ASP A 1 173 ? 1.945 28.177 26.145 1.00 7.19 ? 259 ASP A C 1 ATOM 1373 O O . ASP A 1 173 ? 1.082 28.400 27.000 1.00 7.82 ? 259 ASP A O 1 ATOM 1374 C CB . ASP A 1 173 ? 2.267 25.873 27.073 1.00 7.10 ? 259 ASP A CB 1 ATOM 1375 C CG . ASP A 1 173 ? 0.944 25.417 26.549 1.00 8.70 ? 259 ASP A CG 1 ATOM 1376 O OD1 . ASP A 1 173 ? 0.673 25.450 25.315 1.00 8.25 ? 259 ASP A OD1 1 ATOM 1377 O OD2 . ASP A 1 173 ? 0.090 25.000 27.368 1.00 8.02 ? 259 ASP A OD2 1 ATOM 1378 N N . LEU A 1 174 ? 2.143 28.946 25.091 1.00 6.76 ? 260 LEU A N 1 ATOM 1379 C CA . LEU A 1 174 ? 1.375 30.200 24.881 1.00 6.87 ? 260 LEU A CA 1 ATOM 1380 C C . LEU A 1 174 ? 0.668 30.077 23.539 1.00 6.62 ? 260 LEU A C 1 ATOM 1381 O O . LEU A 1 174 ? 1.185 29.423 22.626 1.00 6.90 ? 260 LEU A O 1 ATOM 1382 C CB . LEU A 1 174 ? 2.312 31.411 24.840 1.00 7.74 ? 260 LEU A CB 1 ATOM 1383 C CG . LEU A 1 174 ? 3.151 31.637 26.116 1.00 5.68 ? 260 LEU A CG 1 ATOM 1384 C CD1 . LEU A 1 174 ? 4.216 32.676 25.843 1.00 8.47 ? 260 LEU A CD1 1 ATOM 1385 C CD2 . LEU A 1 174 ? 2.305 32.016 27.326 1.00 6.84 ? 260 LEU A CD2 1 ATOM 1386 N N . PRO A 1 175 ? -0.514 30.673 23.399 1.00 6.99 ? 261 PRO A N 1 ATOM 1387 C CA . PRO A 1 175 ? -1.272 30.509 22.147 1.00 7.54 ? 261 PRO A CA 1 ATOM 1388 C C . PRO A 1 175 ? -0.602 30.922 20.847 1.00 7.99 ? 261 PRO A C 1 ATOM 1389 O O . PRO A 1 175 ? -0.979 30.385 19.834 1.00 9.18 ? 261 PRO A O 1 ATOM 1390 C CB . PRO A 1 175 ? -2.534 31.347 22.397 1.00 8.45 ? 261 PRO A CB 1 ATOM 1391 C CG . PRO A 1 175 ? -2.708 31.325 23.862 1.00 8.49 ? 261 PRO A CG 1 ATOM 1392 C CD . PRO A 1 175 ? -1.302 31.352 24.447 1.00 7.94 ? 261 PRO A CD 1 ATOM 1393 N N . HIS A 1 176 ? 0.366 31.834 20.864 1.00 6.24 ? 262 HIS A N 1 ATOM 1394 C CA . HIS A 1 176 ? 1.028 32.237 19.647 1.00 6.15 ? 262 HIS A CA 1 ATOM 1395 C C . HIS A 1 176 ? 2.315 31.442 19.384 1.00 6.02 ? 262 HIS A C 1 ATOM 1396 O O . HIS A 1 176 ? 3.034 31.728 18.433 1.00 6.37 ? 262 HIS A O 1 ATOM 1397 C CB . HIS A 1 176 ? 1.324 33.721 19.654 1.00 7.53 ? 262 HIS A CB 1 ATOM 1398 C CG . HIS A 1 176 ? 2.420 34.131 20.588 1.00 6.35 ? 262 HIS A CG 1 ATOM 1399 N ND1 . HIS A 1 176 ? 2.262 34.170 21.959 1.00 6.90 ? 262 HIS A ND1 1 ATOM 1400 C CD2 . HIS A 1 176 ? 3.678 34.572 20.336 1.00 5.63 ? 262 HIS A CD2 1 ATOM 1401 C CE1 . HIS A 1 176 ? 3.378 34.621 22.507 1.00 6.55 ? 262 HIS A CE1 1 ATOM 1402 N NE2 . HIS A 1 176 ? 4.260 34.845 21.548 1.00 6.75 ? 262 HIS A NE2 1 ATOM 1403 N N . VAL A 1 177 ? 2.567 30.482 20.250 1.00 5.25 ? 263 VAL A N 1 ATOM 1404 C CA . VAL A 1 177 ? 3.813 29.709 20.195 1.00 4.62 ? 263 VAL A CA 1 ATOM 1405 C C . VAL A 1 177 ? 3.572 28.288 19.708 1.00 5.22 ? 263 VAL A C 1 ATOM 1406 O O . VAL A 1 177 ? 2.549 27.678 20.034 1.00 4.91 ? 263 VAL A O 1 ATOM 1407 C CB . VAL A 1 177 ? 4.490 29.705 21.594 1.00 5.18 ? 263 VAL A CB 1 ATOM 1408 C CG1 . VAL A 1 177 ? 5.691 28.728 21.662 1.00 5.50 ? 263 VAL A CG1 1 ATOM 1409 C CG2 . VAL A 1 177 ? 4.934 31.105 21.992 1.00 7.03 ? 263 VAL A CG2 1 ATOM 1410 N N . ALA A 1 178 ? 4.582 27.749 19.004 1.00 5.34 ? 264 ALA A N 1 ATOM 1411 C CA . ALA A 1 178 ? 4.654 26.330 18.707 1.00 5.10 ? 264 ALA A CA 1 ATOM 1412 C C . ALA A 1 178 ? 5.972 25.799 19.169 1.00 5.70 ? 264 ALA A C 1 ATOM 1413 O O . ALA A 1 178 ? 6.982 26.495 19.013 1.00 6.60 ? 264 ALA A O 1 ATOM 1414 C CB . ALA A 1 178 ? 4.537 26.065 17.199 1.00 7.26 ? 264 ALA A CB 1 ATOM 1415 N N . MET A 1 179 ? 6.000 24.576 19.696 1.00 5.53 ? 265 MET A N 1 ATOM 1416 C CA . MET A 1 179 ? 7.279 23.968 20.119 1.00 4.63 ? 265 MET A CA 1 ATOM 1417 C C . MET A 1 179 ? 7.507 22.590 19.535 1.00 6.10 ? 265 MET A C 1 ATOM 1418 O O . MET A 1 179 ? 6.575 21.794 19.432 1.00 7.04 ? 265 MET A O 1 ATOM 1419 C CB . MET A 1 179 ? 7.337 23.800 21.632 1.00 5.31 ? 265 MET A CB 1 ATOM 1420 C CG . MET A 1 179 ? 7.630 25.102 22.387 1.00 5.10 ? 265 MET A CG 1 ATOM 1421 S SD . MET A 1 179 ? 7.525 24.905 24.179 1.00 6.93 ? 265 MET A SD 1 ATOM 1422 C CE . MET A 1 179 ? 5.746 24.974 24.347 1.00 7.17 ? 265 MET A CE 1 ATOM 1423 N N . TYR A 1 180 ? 8.766 22.344 19.174 1.00 5.45 ? 266 TYR A N 1 ATOM 1424 C CA . TYR A 1 180 ? 9.201 21.046 18.663 1.00 4.95 ? 266 TYR A CA 1 ATOM 1425 C C . TYR A 1 180 ? 10.372 20.625 19.530 1.00 5.33 ? 266 TYR A C 1 ATOM 1426 O O . TYR A 1 180 ? 11.368 21.368 19.572 1.00 5.81 ? 266 TYR A O 1 ATOM 1427 C CB . TYR A 1 180 ? 9.630 21.132 17.188 1.00 4.63 ? 266 TYR A CB 1 ATOM 1428 C CG . TYR A 1 180 ? 8.518 21.507 16.244 1.00 7.57 ? 266 TYR A CG 1 ATOM 1429 C CD1 . TYR A 1 180 ? 8.186 22.864 16.009 1.00 6.03 ? 266 TYR A CD1 1 ATOM 1430 C CD2 . TYR A 1 180 ? 7.778 20.530 15.579 1.00 6.70 ? 266 TYR A CD2 1 ATOM 1431 C CE1 . TYR A 1 180 ? 7.174 23.210 15.173 1.00 5.56 ? 266 TYR A CE1 1 ATOM 1432 C CE2 . TYR A 1 180 ? 6.766 20.907 14.694 1.00 4.07 ? 266 TYR A CE2 1 ATOM 1433 C CZ . TYR A 1 180 ? 6.456 22.245 14.504 1.00 5.95 ? 266 TYR A CZ 1 ATOM 1434 O OH . TYR A 1 180 ? 5.483 22.596 13.606 1.00 6.92 ? 266 TYR A OH 1 ATOM 1435 N N . MET A 1 181 ? 10.290 19.519 20.252 1.00 4.88 ? 267 MET A N 1 ATOM 1436 C CA . MET A 1 181 ? 11.468 19.086 21.028 1.00 5.61 ? 267 MET A CA 1 ATOM 1437 C C . MET A 1 181 ? 12.488 18.424 20.096 1.00 6.06 ? 267 MET A C 1 ATOM 1438 O O . MET A 1 181 ? 12.109 17.682 19.191 1.00 5.33 ? 267 MET A O 1 ATOM 1439 C CB . MET A 1 181 ? 11.110 18.054 22.115 1.00 6.53 ? 267 MET A CB 1 ATOM 1440 C CG . MET A 1 181 ? 10.346 18.607 23.286 1.00 5.07 ? 267 MET A CG 1 ATOM 1441 S SD . MET A 1 181 ? 9.924 17.341 24.482 1.00 8.02 ? 267 MET A SD 1 ATOM 1442 C CE . MET A 1 181 ? 8.513 16.557 23.711 1.00 8.98 ? 267 MET A CE 1 ATOM 1443 N N . ASP A 1 182 ? 13.773 18.673 20.327 1.00 4.88 ? 268 ASP A N 1 ATOM 1444 C CA . ASP A 1 182 ? 14.816 17.988 19.570 1.00 6.09 ? 268 ASP A CA 1 ATOM 1445 C C . ASP A 1 182 ? 14.694 16.472 19.735 1.00 5.55 ? 268 ASP A C 1 ATOM 1446 O O . ASP A 1 182 ? 14.513 15.966 20.817 1.00 6.68 ? 268 ASP A O 1 ATOM 1447 C CB . ASP A 1 182 ? 16.193 18.409 20.008 1.00 6.32 ? 268 ASP A CB 1 ATOM 1448 C CG . ASP A 1 182 ? 17.243 17.752 19.204 1.00 8.04 ? 268 ASP A CG 1 ATOM 1449 O OD1 . ASP A 1 182 ? 17.579 18.317 18.129 1.00 7.99 ? 268 ASP A OD1 1 ATOM 1450 O OD2 . ASP A 1 182 ? 17.725 16.665 19.578 1.00 7.77 ? 268 ASP A OD2 1 ATOM 1451 N N . ALA A 1 183 ? 14.848 15.748 18.653 1.00 5.48 ? 269 ALA A N 1 ATOM 1452 C CA . ALA A 1 183 ? 14.823 14.282 18.704 1.00 4.65 ? 269 ALA A CA 1 ATOM 1453 C C . ALA A 1 183 ? 15.933 13.667 17.869 1.00 5.28 ? 269 ALA A C 1 ATOM 1454 O O . ALA A 1 183 ? 15.696 12.667 17.141 1.00 6.18 ? 269 ALA A O 1 ATOM 1455 C CB . ALA A 1 183 ? 13.463 13.694 18.324 1.00 6.31 ? 269 ALA A CB 1 ATOM 1456 N N . GLY A 1 184 ? 17.139 14.236 17.991 1.00 4.62 ? 270 GLY A N 1 ATOM 1457 C CA . GLY A 1 184 ? 18.303 13.641 17.326 1.00 5.02 ? 270 GLY A CA 1 ATOM 1458 C C . GLY A 1 184 ? 18.097 13.502 15.822 1.00 5.78 ? 270 GLY A C 1 ATOM 1459 O O . GLY A 1 184 ? 17.497 14.378 15.184 1.00 7.22 ? 270 GLY A O 1 ATOM 1460 N N . HIS A 1 185 ? 18.551 12.397 15.256 1.00 5.83 ? 271 HIS A N 1 ATOM 1461 C CA . HIS A 1 185 ? 18.504 12.190 13.787 1.00 4.95 ? 271 HIS A CA 1 ATOM 1462 C C . HIS A 1 185 ? 18.467 10.707 13.476 1.00 5.83 ? 271 HIS A C 1 ATOM 1463 O O . HIS A 1 185 ? 18.581 9.895 14.420 1.00 5.54 ? 271 HIS A O 1 ATOM 1464 C CB . HIS A 1 185 ? 19.640 12.944 13.078 1.00 5.72 ? 271 HIS A CB 1 ATOM 1465 C CG . HIS A 1 185 ? 21.007 12.421 13.330 1.00 6.21 ? 271 HIS A CG 1 ATOM 1466 N ND1 . HIS A 1 185 ? 21.606 11.473 12.523 1.00 6.07 ? 271 HIS A ND1 1 ATOM 1467 C CD2 . HIS A 1 185 ? 21.906 12.721 14.301 1.00 6.30 ? 271 HIS A CD2 1 ATOM 1468 C CE1 . HIS A 1 185 ? 22.827 11.254 12.961 1.00 6.77 ? 271 HIS A CE1 1 ATOM 1469 N NE2 . HIS A 1 185 ? 23.024 11.967 14.052 1.00 6.09 ? 271 HIS A NE2 1 ATOM 1470 N N . ALA A 1 186 ? 18.306 10.346 12.213 1.00 5.08 ? 272 ALA A N 1 ATOM 1471 C CA . ALA A 1 186 ? 18.157 8.933 11.828 1.00 5.21 ? 272 ALA A CA 1 ATOM 1472 C C . ALA A 1 186 ? 19.321 8.060 12.288 1.00 6.42 ? 272 ALA A C 1 ATOM 1473 O O . ALA A 1 186 ? 19.158 6.891 12.649 1.00 6.50 ? 272 ALA A O 1 ATOM 1474 C CB . ALA A 1 186 ? 18.023 8.796 10.334 1.00 5.83 ? 272 ALA A CB 1 ATOM 1475 N N . GLY A 1 187 ? 20.495 8.658 12.297 1.00 5.71 ? 273 GLY A N 1 ATOM 1476 C CA . GLY A 1 187 ? 21.730 7.957 12.663 1.00 6.11 ? 273 GLY A CA 1 ATOM 1477 C C . GLY A 1 187 ? 22.055 8.032 14.144 1.00 5.72 ? 273 GLY A C 1 ATOM 1478 O O . GLY A 1 187 ? 23.125 7.575 14.596 1.00 6.46 ? 273 GLY A O 1 ATOM 1479 N N . TRP A 1 188 ? 21.159 8.591 14.938 1.00 5.45 ? 274 TRP A N 1 ATOM 1480 C CA . TRP A 1 188 ? 21.265 8.542 16.400 1.00 5.77 ? 274 TRP A CA 1 ATOM 1481 C C . TRP A 1 188 ? 20.111 7.692 16.954 1.00 6.54 ? 274 TRP A C 1 ATOM 1482 O O . TRP A 1 188 ? 20.308 6.519 17.285 1.00 7.05 ? 274 TRP A O 1 ATOM 1483 C CB . TRP A 1 188 ? 21.275 9.929 17.013 1.00 6.32 ? 274 TRP A CB 1 ATOM 1484 C CG . TRP A 1 188 ? 21.595 9.941 18.522 1.00 4.99 ? 274 TRP A CG 1 ATOM 1485 C CD1 . TRP A 1 188 ? 21.686 8.880 19.370 1.00 4.53 ? 274 TRP A CD1 1 ATOM 1486 C CD2 . TRP A 1 188 ? 21.762 11.110 19.327 1.00 6.71 ? 274 TRP A CD2 1 ATOM 1487 N NE1 . TRP A 1 188 ? 21.949 9.306 20.646 1.00 5.79 ? 274 TRP A NE1 1 ATOM 1488 C CE2 . TRP A 1 188 ? 22.004 10.680 20.653 1.00 6.48 ? 274 TRP A CE2 1 ATOM 1489 C CE3 . TRP A 1 188 ? 21.746 12.481 19.053 1.00 6.11 ? 274 TRP A CE3 1 ATOM 1490 C CZ2 . TRP A 1 188 ? 22.254 11.565 21.681 1.00 6.06 ? 274 TRP A CZ2 1 ATOM 1491 C CZ3 . TRP A 1 188 ? 22.000 13.354 20.061 1.00 5.80 ? 274 TRP A CZ3 1 ATOM 1492 C CH2 . TRP A 1 188 ? 22.244 12.901 21.373 1.00 6.79 ? 274 TRP A CH2 1 ATOM 1493 N N . LEU A 1 189 ? 18.923 8.274 16.981 1.00 5.82 ? 275 LEU A N 1 ATOM 1494 C CA . LEU A 1 189 ? 17.748 7.590 17.531 1.00 5.99 ? 275 LEU A CA 1 ATOM 1495 C C . LEU A 1 189 ? 17.003 6.718 16.551 1.00 6.93 ? 275 LEU A C 1 ATOM 1496 O O . LEU A 1 189 ? 16.174 5.920 16.981 1.00 7.42 ? 275 LEU A O 1 ATOM 1497 C CB . LEU A 1 189 ? 16.798 8.615 18.171 1.00 5.54 ? 275 LEU A CB 1 ATOM 1498 C CG . LEU A 1 189 ? 17.393 9.501 19.293 1.00 5.78 ? 275 LEU A CG 1 ATOM 1499 C CD1 . LEU A 1 189 ? 16.358 10.433 19.900 1.00 5.65 ? 275 LEU A CD1 1 ATOM 1500 C CD2 . LEU A 1 189 ? 18.117 8.687 20.366 1.00 7.21 ? 275 LEU A CD2 1 ATOM 1501 N N . GLY A 1 190 ? 17.303 6.831 15.272 1.00 6.74 ? 276 GLY A N 1 ATOM 1502 C CA . GLY A 1 190 ? 16.635 6.003 14.263 1.00 7.16 ? 276 GLY A CA 1 ATOM 1503 C C . GLY A 1 190 ? 17.105 4.586 14.149 1.00 6.72 ? 276 GLY A C 1 ATOM 1504 O O . GLY A 1 190 ? 16.446 3.779 13.474 1.00 8.12 ? 276 GLY A O 1 ATOM 1505 N N . TRP A 1 191 ? 18.264 4.269 14.711 1.00 6.75 ? 277 TRP A N 1 ATOM 1506 C CA . TRP A 1 191 ? 18.738 2.878 14.681 1.00 7.34 ? 277 TRP A CA 1 ATOM 1507 C C . TRP A 1 191 ? 17.674 2.005 15.300 1.00 7.83 ? 277 TRP A C 1 ATOM 1508 O O . TRP A 1 191 ? 17.065 2.361 16.309 1.00 8.06 ? 277 TRP A O 1 ATOM 1509 C CB . TRP A 1 191 ? 20.023 2.710 15.493 1.00 6.39 ? 277 TRP A CB 1 ATOM 1510 C CG . TRP A 1 191 ? 21.170 3.280 14.766 1.00 8.27 ? 277 TRP A CG 1 ATOM 1511 C CD1 . TRP A 1 191 ? 21.696 4.523 14.908 1.00 6.59 ? 277 TRP A CD1 1 ATOM 1512 C CD2 . TRP A 1 191 ? 21.937 2.639 13.742 1.00 6.88 ? 277 TRP A CD2 1 ATOM 1513 N NE1 . TRP A 1 191 ? 22.745 4.699 14.044 1.00 7.12 ? 277 TRP A NE1 1 ATOM 1514 C CE2 . TRP A 1 191 ? 22.942 3.546 13.341 1.00 7.74 ? 277 TRP A CE2 1 ATOM 1515 C CE3 . TRP A 1 191 ? 21.931 1.371 13.180 1.00 10.81 ? 277 TRP A CE3 1 ATOM 1516 C CZ2 . TRP A 1 191 ? 23.895 3.247 12.370 1.00 9.26 ? 277 TRP A CZ2 1 ATOM 1517 C CZ3 . TRP A 1 191 ? 22.909 1.076 12.206 1.00 7.60 ? 277 TRP A CZ3 1 ATOM 1518 C CH2 . TRP A 1 191 ? 23.845 2.008 11.814 1.00 9.83 ? 277 TRP A CH2 1 ATOM 1519 N N . PRO A 1 192 ? 17.434 0.816 14.747 1.00 7.84 ? 278 PRO A N 1 ATOM 1520 C CA . PRO A 1 192 ? 16.404 -0.046 15.326 1.00 9.10 ? 278 PRO A CA 1 ATOM 1521 C C . PRO A 1 192 ? 16.449 -0.273 16.819 1.00 9.10 ? 278 PRO A C 1 ATOM 1522 O O . PRO A 1 192 ? 15.388 -0.365 17.428 1.00 9.05 ? 278 PRO A O 1 ATOM 1523 C CB . PRO A 1 192 ? 16.630 -1.362 14.578 1.00 9.80 ? 278 PRO A CB 1 ATOM 1524 C CG . PRO A 1 192 ? 16.960 -0.854 13.173 1.00 9.24 ? 278 PRO A CG 1 ATOM 1525 C CD . PRO A 1 192 ? 18.016 0.253 13.517 1.00 9.55 ? 278 PRO A CD 1 ATOM 1526 N N . ALA A 1 193 ? 17.628 -0.377 17.415 1.00 7.65 ? 279 ALA A N 1 ATOM 1527 C CA . ALA A 1 193 ? 17.715 -0.651 18.849 1.00 8.93 ? 279 ALA A CA 1 ATOM 1528 C C . ALA A 1 193 ? 17.347 0.544 19.699 1.00 8.25 ? 279 ALA A C 1 ATOM 1529 O O . ALA A 1 193 ? 17.074 0.404 20.889 1.00 9.54 ? 279 ALA A O 1 ATOM 1530 C CB . ALA A 1 193 ? 19.118 -1.143 19.244 1.00 10.21 ? 279 ALA A CB 1 ATOM 1531 N N . ASN A 1 194 ? 17.406 1.729 19.101 1.00 6.99 ? 280 ASN A N 1 ATOM 1532 C CA . ASN A 1 194 ? 17.169 2.986 19.802 1.00 7.42 ? 280 ASN A CA 1 ATOM 1533 C C . ASN A 1 194 ? 15.806 3.584 19.653 1.00 8.32 ? 280 ASN A C 1 ATOM 1534 O O . ASN A 1 194 ? 15.395 4.383 20.507 1.00 8.45 ? 280 ASN A O 1 ATOM 1535 C CB . ASN A 1 194 ? 18.186 4.034 19.344 1.00 7.08 ? 280 ASN A CB 1 ATOM 1536 C CG . ASN A 1 194 ? 19.617 3.664 19.695 1.00 7.71 ? 280 ASN A CG 1 ATOM 1537 O OD1 . ASN A 1 194 ? 19.878 2.804 20.568 1.00 7.73 ? 280 ASN A OD1 1 ATOM 1538 N ND2 . ASN A 1 194 ? 20.585 4.310 19.017 1.00 6.54 ? 280 ASN A ND2 1 ATOM 1539 N N . ILE A 1 195 ? 15.113 3.229 18.574 1.00 8.29 ? 281 ILE A N 1 ATOM 1540 C CA . ILE A 1 195 ? 13.892 3.944 18.183 1.00 7.86 ? 281 ILE A CA 1 ATOM 1541 C C . ILE A 1 195 ? 12.687 3.756 19.141 1.00 7.76 ? 281 ILE A C 1 ATOM 1542 O O . ILE A 1 195 ? 11.989 4.722 19.457 1.00 7.13 ? 281 ILE A O 1 ATOM 1543 C CB . ILE A 1 195 ? 13.591 3.671 16.703 1.00 7.08 ? 281 ILE A CB 1 ATOM 1544 C CG1 . ILE A 1 195 ? 12.631 4.731 16.152 1.00 7.25 ? 281 ILE A CG1 1 ATOM 1545 C CG2 . ILE A 1 195 ? 13.056 2.280 16.535 1.00 9.27 ? 281 ILE A CG2 1 ATOM 1546 C CD1 . ILE A 1 195 ? 12.374 4.614 14.653 1.00 9.25 ? 281 ILE A CD1 1 ATOM 1547 N N . GLN A 1 196 ? 12.461 2.550 19.670 1.00 8.46 ? 282 GLN A N 1 ATOM 1548 C CA . GLN A 1 196 ? 11.356 2.359 20.639 1.00 9.46 ? 282 GLN A CA 1 ATOM 1549 C C . GLN A 1 196 ? 11.629 3.053 21.998 1.00 8.81 ? 282 GLN A C 1 ATOM 1550 O O . GLN A 1 196 ? 10.762 3.759 22.523 1.00 7.80 ? 282 GLN A O 1 ATOM 1551 C CB . GLN A 1 196 ? 11.007 0.889 20.830 1.00 10.55 ? 282 GLN A CB 1 ATOM 1552 C CG . GLN A 1 196 ? 9.738 0.770 21.694 1.00 15.07 ? 282 GLN A CG 1 ATOM 1553 C CD . GLN A 1 196 ? 9.256 -0.662 21.830 1.00 23.33 ? 282 GLN A CD 1 ATOM 1554 O OE1 . GLN A 1 196 ? 9.018 -1.339 20.822 1.00 28.07 ? 282 GLN A OE1 1 ATOM 1555 N NE2 . GLN A 1 196 ? 9.103 -1.125 23.071 1.00 25.38 ? 282 GLN A NE2 1 ATOM 1556 N N . PRO A 1 197 ? 12.822 2.934 22.553 1.00 8.33 ? 283 PRO A N 1 ATOM 1557 C CA . PRO A 1 197 ? 13.111 3.652 23.796 1.00 8.39 ? 283 PRO A CA 1 ATOM 1558 C C . PRO A 1 197 ? 13.044 5.190 23.624 1.00 6.77 ? 283 PRO A C 1 ATOM 1559 O O . PRO A 1 197 ? 12.682 5.906 24.546 1.00 7.76 ? 283 PRO A O 1 ATOM 1560 C CB . PRO A 1 197 ? 14.530 3.221 24.134 1.00 10.11 ? 283 PRO A CB 1 ATOM 1561 C CG . PRO A 1 197 ? 14.743 1.942 23.412 1.00 11.27 ? 283 PRO A CG 1 ATOM 1562 C CD . PRO A 1 197 ? 13.905 1.989 22.204 1.00 9.62 ? 283 PRO A CD 1 ATOM 1563 N N . ALA A 1 198 ? 13.402 5.657 22.442 1.00 6.05 ? 284 ALA A N 1 ATOM 1564 C CA . ALA A 1 198 ? 13.298 7.089 22.130 1.00 6.30 ? 284 ALA A CA 1 ATOM 1565 C C . ALA A 1 198 ? 11.830 7.483 22.133 1.00 6.91 ? 284 ALA A C 1 ATOM 1566 O O . ALA A 1 198 ? 11.445 8.501 22.727 1.00 6.18 ? 284 ALA A O 1 ATOM 1567 C CB . ALA A 1 198 ? 13.920 7.416 20.772 1.00 7.31 ? 284 ALA A CB 1 ATOM 1568 N N . ALA A 1 199 ? 10.988 6.671 21.502 1.00 6.43 ? 285 ALA A N 1 ATOM 1569 C CA . ALA A 1 199 ? 9.532 6.985 21.484 1.00 7.02 ? 285 ALA A CA 1 ATOM 1570 C C . ALA A 1 199 ? 8.940 6.962 22.874 1.00 7.06 ? 285 ALA A C 1 ATOM 1571 O O . ALA A 1 199 ? 8.137 7.839 23.218 1.00 6.57 ? 285 ALA A O 1 ATOM 1572 C CB . ALA A 1 199 ? 8.758 5.998 20.580 1.00 9.17 ? 285 ALA A CB 1 ATOM 1573 N N . GLU A 1 200 ? 9.354 5.992 23.680 1.00 7.08 ? 286 GLU A N 1 ATOM 1574 C CA . GLU A 1 200 ? 8.892 5.909 25.071 1.00 7.31 ? 286 GLU A CA 1 ATOM 1575 C C . GLU A 1 200 ? 9.248 7.167 25.867 1.00 6.72 ? 286 GLU A C 1 ATOM 1576 O O . GLU A 1 200 ? 8.416 7.727 26.551 1.00 8.00 ? 286 GLU A O 1 ATOM 1577 C CB A GLU A 1 200 ? 9.422 4.645 25.735 0.65 8.15 ? 286 GLU A CB 1 ATOM 1578 C CB B GLU A 1 200 ? 9.442 4.670 25.782 0.35 8.12 ? 286 GLU A CB 1 ATOM 1579 C CG A GLU A 1 200 ? 8.897 4.487 27.147 0.65 9.95 ? 286 GLU A CG 1 ATOM 1580 C CG B GLU A 1 200 ? 8.814 3.376 25.304 0.35 9.88 ? 286 GLU A CG 1 ATOM 1581 C CD A GLU A 1 200 ? 9.153 3.122 27.757 0.65 16.31 ? 286 GLU A CD 1 ATOM 1582 C CD B GLU A 1 200 ? 8.866 2.230 26.307 0.35 14.70 ? 286 GLU A CD 1 ATOM 1583 O OE1 A GLU A 1 200 ? 8.689 2.083 27.181 0.65 20.28 ? 286 GLU A OE1 1 ATOM 1584 O OE1 B GLU A 1 200 ? 8.805 2.466 27.537 0.35 20.32 ? 286 GLU A OE1 1 ATOM 1585 O OE2 A GLU A 1 200 ? 9.777 3.095 28.841 0.65 15.47 ? 286 GLU A OE2 1 ATOM 1586 O OE2 B GLU A 1 200 ? 8.903 1.076 25.841 0.35 15.79 ? 286 GLU A OE2 1 ATOM 1587 N N . LEU A 1 201 ? 10.466 7.656 25.678 1.00 7.07 ? 287 LEU A N 1 ATOM 1588 C CA . LEU A 1 201 ? 10.944 8.826 26.415 1.00 6.84 ? 287 LEU A CA 1 ATOM 1589 C C . LEU A 1 201 ? 10.173 10.074 26.031 1.00 6.42 ? 287 LEU A C 1 ATOM 1590 O O . LEU A 1 201 ? 9.657 10.767 26.918 1.00 7.37 ? 287 LEU A O 1 ATOM 1591 C CB A LEU A 1 201 ? 12.445 9.044 26.196 0.55 6.39 ? 287 LEU A CB 1 ATOM 1592 C CB B LEU A 1 201 ? 12.454 9.025 26.215 0.45 6.53 ? 287 LEU A CB 1 ATOM 1593 C CG A LEU A 1 201 ? 13.016 10.277 26.902 0.55 6.43 ? 287 LEU A CG 1 ATOM 1594 C CG B LEU A 1 201 ? 13.125 10.109 27.069 0.45 6.88 ? 287 LEU A CG 1 ATOM 1595 C CD1 A LEU A 1 201 ? 12.915 10.085 28.418 0.55 9.45 ? 287 LEU A CD1 1 ATOM 1596 C CD1 B LEU A 1 201 ? 14.595 9.783 27.320 0.45 8.93 ? 287 LEU A CD1 1 ATOM 1597 C CD2 A LEU A 1 201 ? 14.434 10.576 26.453 0.55 6.42 ? 287 LEU A CD2 1 ATOM 1598 C CD2 B LEU A 1 201 ? 12.974 11.490 26.450 0.45 6.57 ? 287 LEU A CD2 1 ATOM 1599 N N . PHE A 1 202 ? 10.103 10.342 24.726 1.00 6.33 ? 288 PHE A N 1 ATOM 1600 C CA . PHE A 1 202 ? 9.453 11.578 24.260 1.00 5.63 ? 288 PHE A CA 1 ATOM 1601 C C . PHE A 1 202 ? 7.974 11.585 24.585 1.00 6.58 ? 288 PHE A C 1 ATOM 1602 O O . PHE A 1 202 ? 7.437 12.593 25.019 1.00 6.99 ? 288 PHE A O 1 ATOM 1603 C CB . PHE A 1 202 ? 9.763 11.884 22.798 1.00 6.33 ? 288 PHE A CB 1 ATOM 1604 C CG . PHE A 1 202 ? 11.170 12.384 22.625 1.00 5.40 ? 288 PHE A CG 1 ATOM 1605 C CD1 . PHE A 1 202 ? 11.516 13.655 23.036 1.00 8.21 ? 288 PHE A CD1 1 ATOM 1606 C CD2 . PHE A 1 202 ? 12.174 11.544 22.181 1.00 8.07 ? 288 PHE A CD2 1 ATOM 1607 C CE1 . PHE A 1 202 ? 12.826 14.077 22.934 1.00 8.57 ? 288 PHE A CE1 1 ATOM 1608 C CE2 . PHE A 1 202 ? 13.480 11.965 22.059 1.00 9.68 ? 288 PHE A CE2 1 ATOM 1609 C CZ . PHE A 1 202 ? 13.815 13.249 22.439 1.00 9.18 ? 288 PHE A CZ 1 ATOM 1610 N N . ALA A 1 203 ? 7.318 10.448 24.429 1.00 6.53 ? 289 ALA A N 1 ATOM 1611 C CA . ALA A 1 203 ? 5.888 10.408 24.743 1.00 6.49 ? 289 ALA A CA 1 ATOM 1612 C C . ALA A 1 203 ? 5.658 10.559 26.246 1.00 6.80 ? 289 ALA A C 1 ATOM 1613 O O . ALA A 1 203 ? 4.707 11.198 26.644 1.00 6.09 ? 289 ALA A O 1 ATOM 1614 C CB . ALA A 1 203 ? 5.263 9.142 24.226 1.00 8.15 ? 289 ALA A CB 1 ATOM 1615 N N . LYS A 1 204 ? 6.565 10.046 27.061 1.00 7.40 ? 290 LYS A N 1 ATOM 1616 C CA . LYS A 1 204 ? 6.404 10.245 28.510 1.00 8.47 ? 290 LYS A CA 1 ATOM 1617 C C . LYS A 1 204 ? 6.571 11.720 28.896 1.00 7.73 ? 290 LYS A C 1 ATOM 1618 O O . LYS A 1 204 ? 5.863 12.246 29.758 1.00 7.66 ? 290 LYS A O 1 ATOM 1619 C CB . LYS A 1 204 ? 7.332 9.325 29.323 1.00 10.55 ? 290 LYS A CB 1 ATOM 1620 C CG . LYS A 1 204 ? 7.238 9.462 30.829 1.00 16.83 ? 290 LYS A CG 1 ATOM 1621 C CD . LYS A 1 204 ? 5.952 8.892 31.416 1.00 24.49 ? 290 LYS A CD 1 ATOM 1622 C CE . LYS A 1 204 ? 6.159 8.353 32.865 1.00 25.47 ? 290 LYS A CE 1 ATOM 1623 N NZ . LYS A 1 204 ? 6.871 9.309 33.781 1.00 27.01 ? 290 LYS A NZ 1 ATOM 1624 N N . ILE A 1 205 ? 7.563 12.374 28.316 1.00 7.23 ? 291 ILE A N 1 ATOM 1625 C CA . ILE A 1 205 ? 7.800 13.790 28.593 1.00 6.84 ? 291 ILE A CA 1 ATOM 1626 C C . ILE A 1 205 ? 6.553 14.563 28.227 1.00 7.43 ? 291 ILE A C 1 ATOM 1627 O O . ILE A 1 205 ? 6.108 15.434 28.952 1.00 7.15 ? 291 ILE A O 1 ATOM 1628 C CB . ILE A 1 205 ? 9.015 14.319 27.838 1.00 6.84 ? 291 ILE A CB 1 ATOM 1629 C CG1 . ILE A 1 205 ? 10.307 13.717 28.374 1.00 9.56 ? 291 ILE A CG1 1 ATOM 1630 C CG2 . ILE A 1 205 ? 9.138 15.862 27.947 1.00 9.13 ? 291 ILE A CG2 1 ATOM 1631 C CD1 . ILE A 1 205 ? 10.722 14.118 29.783 1.00 14.25 ? 291 ILE A CD1 1 ATOM 1632 N N . TYR A 1 206 ? 6.036 14.269 27.046 1.00 6.33 ? 292 TYR A N 1 ATOM 1633 C CA . TYR A 1 206 ? 4.832 14.944 26.547 1.00 7.57 ? 292 TYR A CA 1 ATOM 1634 C C . TYR A 1 206 ? 3.670 14.784 27.543 1.00 7.92 ? 292 TYR A C 1 ATOM 1635 O O . TYR A 1 206 ? 3.039 15.767 27.917 1.00 6.70 ? 292 TYR A O 1 ATOM 1636 C CB . TYR A 1 206 ? 4.477 14.365 25.193 1.00 8.04 ? 292 TYR A CB 1 ATOM 1637 C CG . TYR A 1 206 ? 3.308 15.003 24.466 1.00 7.24 ? 292 TYR A CG 1 ATOM 1638 C CD1 . TYR A 1 206 ? 3.275 16.348 24.187 1.00 7.12 ? 292 TYR A CD1 1 ATOM 1639 C CD2 . TYR A 1 206 ? 2.261 14.225 24.033 1.00 6.70 ? 292 TYR A CD2 1 ATOM 1640 C CE1 . TYR A 1 206 ? 2.203 16.892 23.487 1.00 6.72 ? 292 TYR A CE1 1 ATOM 1641 C CE2 . TYR A 1 206 ? 1.193 14.745 23.331 1.00 6.88 ? 292 TYR A CE2 1 ATOM 1642 C CZ . TYR A 1 206 ? 1.164 16.091 23.066 1.00 7.40 ? 292 TYR A CZ 1 ATOM 1643 O OH . TYR A 1 206 ? 0.103 16.631 22.360 1.00 7.89 ? 292 TYR A OH 1 ATOM 1644 N N . GLU A 1 207 ? 3.403 13.544 27.978 1.00 8.26 ? 293 GLU A N 1 ATOM 1645 C CA . GLU A 1 207 ? 2.392 13.281 29.020 1.00 10.54 ? 293 GLU A CA 1 ATOM 1646 C C . GLU A 1 207 ? 2.639 14.025 30.316 1.00 9.68 ? 293 GLU A C 1 ATOM 1647 O O . GLU A 1 207 ? 1.719 14.605 30.909 1.00 9.55 ? 293 GLU A O 1 ATOM 1648 C CB . GLU A 1 207 ? 2.351 11.789 29.471 1.00 11.85 ? 293 GLU A CB 1 ATOM 1649 C CG . GLU A 1 207 ? 1.860 10.894 28.444 1.00 15.82 ? 293 GLU A CG 1 ATOM 1650 C CD . GLU A 1 207 ? 1.823 9.450 28.880 1.00 12.31 ? 293 GLU A CD 1 ATOM 1651 O OE1 . GLU A 1 207 ? 2.274 8.989 30.013 1.00 13.51 ? 293 GLU A OE1 1 ATOM 1652 O OE2 . GLU A 1 207 ? 1.343 8.758 28.035 1.00 14.38 ? 293 GLU A OE2 1 ATOM 1653 N N . ASP A 1 208 ? 3.870 13.971 30.768 1.00 9.44 ? 294 ASP A N 1 ATOM 1654 C CA . ASP A 1 208 ? 4.234 14.525 32.083 1.00 10.54 ? 294 ASP A CA 1 ATOM 1655 C C . ASP A 1 208 ? 4.080 16.060 32.075 1.00 9.87 ? 294 ASP A C 1 ATOM 1656 O O . ASP A 1 208 ? 3.846 16.681 33.124 1.00 11.19 ? 294 ASP A O 1 ATOM 1657 C CB . ASP A 1 208 ? 5.618 14.069 32.523 1.00 10.72 ? 294 ASP A CB 1 ATOM 1658 C CG . ASP A 1 208 ? 5.650 12.603 32.917 1.00 14.86 ? 294 ASP A CG 1 ATOM 1659 O OD1 . ASP A 1 208 ? 4.571 11.994 33.072 1.00 17.40 ? 294 ASP A OD1 1 ATOM 1660 O OD2 . ASP A 1 208 ? 6.729 12.016 33.081 1.00 15.77 ? 294 ASP A OD2 1 ATOM 1661 N N . ALA A 1 209 ? 4.194 16.666 30.900 1.00 8.45 ? 295 ALA A N 1 ATOM 1662 C CA . ALA A 1 209 ? 3.997 18.119 30.699 1.00 8.36 ? 295 ALA A CA 1 ATOM 1663 C C . ALA A 1 209 ? 2.538 18.478 30.513 1.00 8.15 ? 295 ALA A C 1 ATOM 1664 O O . ALA A 1 209 ? 2.192 19.641 30.283 1.00 9.09 ? 295 ALA A O 1 ATOM 1665 C CB . ALA A 1 209 ? 4.808 18.623 29.510 1.00 7.66 ? 295 ALA A CB 1 ATOM 1666 N N . GLY A 1 210 ? 1.673 17.484 30.571 1.00 8.53 ? 296 GLY A N 1 ATOM 1667 C CA . GLY A 1 210 ? 0.221 17.707 30.367 1.00 9.24 ? 296 GLY A CA 1 ATOM 1668 C C . GLY A 1 210 ? -0.227 17.922 28.928 1.00 7.34 ? 296 GLY A C 1 ATOM 1669 O O . GLY A 1 210 ? -1.275 18.537 28.662 1.00 8.45 ? 296 GLY A O 1 ATOM 1670 N N . LYS A 1 211 ? 0.542 17.408 27.974 1.00 7.60 ? 297 LYS A N 1 ATOM 1671 C CA . LYS A 1 211 ? 0.291 17.505 26.545 1.00 7.44 ? 297 LYS A CA 1 ATOM 1672 C C . LYS A 1 211 ? -0.058 18.938 26.148 1.00 7.91 ? 297 LYS A C 1 ATOM 1673 O O . LYS A 1 211 ? -1.165 19.252 25.670 1.00 8.17 ? 297 LYS A O 1 ATOM 1674 C CB . LYS A 1 211 ? -0.804 16.515 26.093 1.00 6.02 ? 297 LYS A CB 1 ATOM 1675 C CG . LYS A 1 211 ? -0.441 15.104 26.488 1.00 6.79 ? 297 LYS A CG 1 ATOM 1676 C CD . LYS A 1 211 ? -1.293 14.051 25.837 1.00 5.94 ? 297 LYS A CD 1 ATOM 1677 C CE . LYS A 1 211 ? -0.851 12.656 26.218 1.00 8.24 ? 297 LYS A CE 1 ATOM 1678 N NZ . LYS A 1 211 ? -1.485 11.588 25.331 1.00 7.99 ? 297 LYS A NZ 1 ATOM 1679 N N . PRO A 1 212 ? 0.886 19.838 26.357 1.00 7.77 ? 298 PRO A N 1 ATOM 1680 C CA . PRO A 1 212 ? 0.588 21.257 26.160 1.00 7.72 ? 298 PRO A CA 1 ATOM 1681 C C . PRO A 1 212 ? 0.208 21.489 24.725 1.00 8.04 ? 298 PRO A C 1 ATOM 1682 O O . PRO A 1 212 ? 0.827 20.983 23.795 1.00 8.29 ? 298 PRO A O 1 ATOM 1683 C CB . PRO A 1 212 ? 1.913 21.986 26.509 1.00 8.24 ? 298 PRO A CB 1 ATOM 1684 C CG . PRO A 1 212 ? 2.761 20.979 27.188 1.00 8.56 ? 298 PRO A CG 1 ATOM 1685 C CD . PRO A 1 212 ? 2.260 19.622 26.796 1.00 9.00 ? 298 PRO A CD 1 ATOM 1686 N N . ARG A 1 213 ? -0.794 22.321 24.532 1.00 7.87 ? 299 ARG A N 1 ATOM 1687 C CA . ARG A 1 213 ? -1.259 22.606 23.167 1.00 8.84 ? 299 ARG A CA 1 ATOM 1688 C C . ARG A 1 213 ? -0.161 23.127 22.202 1.00 7.78 ? 299 ARG A C 1 ATOM 1689 O O . ARG A 1 213 ? -0.155 22.855 21.001 1.00 8.37 ? 299 ARG A O 1 ATOM 1690 C CB . ARG A 1 213 ? -2.399 23.615 23.233 1.00 9.85 ? 299 ARG A CB 1 ATOM 1691 C CG . ARG A 1 213 ? -2.850 24.042 21.879 1.00 14.79 ? 299 ARG A CG 1 ATOM 1692 C CD . ARG A 1 213 ? -3.880 25.127 21.950 1.00 21.26 ? 299 ARG A CD 1 ATOM 1693 N NE . ARG A 1 213 ? -4.285 25.632 20.645 1.00 24.98 ? 299 ARG A NE 1 ATOM 1694 C CZ . ARG A 1 213 ? -5.524 26.042 20.351 1.00 28.53 ? 299 ARG A CZ 1 ATOM 1695 N NH1 . ARG A 1 213 ? -6.489 25.959 21.265 1.00 28.38 ? 299 ARG A NH1 1 ATOM 1696 N NH2 . ARG A 1 213 ? -5.822 26.524 19.133 1.00 27.70 ? 299 ARG A NH2 1 ATOM 1697 N N . ALA A 1 214 ? 0.752 23.914 22.719 1.00 7.18 ? 300 ALA A N 1 ATOM 1698 C CA . ALA A 1 214 ? 1.806 24.520 21.878 1.00 8.53 ? 300 ALA A CA 1 ATOM 1699 C C . ALA A 1 214 ? 2.787 23.479 21.311 1.00 7.61 ? 300 ALA A C 1 ATOM 1700 O O . ALA A 1 214 ? 3.465 23.747 20.327 1.00 9.05 ? 300 ALA A O 1 ATOM 1701 C CB . ALA A 1 214 ? 2.551 25.547 22.647 1.00 8.10 ? 300 ALA A CB 1 ATOM 1702 N N . VAL A 1 215 ? 2.865 22.315 21.944 1.00 7.96 ? 301 VAL A N 1 ATOM 1703 C CA . VAL A 1 215 ? 3.826 21.316 21.473 1.00 8.13 ? 301 VAL A CA 1 ATOM 1704 C C . VAL A 1 215 ? 3.267 20.628 20.244 1.00 9.14 ? 301 VAL A C 1 ATOM 1705 O O . VAL A 1 215 ? 2.246 19.947 20.341 1.00 10.31 ? 301 VAL A O 1 ATOM 1706 C CB . VAL A 1 215 ? 4.150 20.308 22.574 1.00 8.06 ? 301 VAL A CB 1 ATOM 1707 C CG1 . VAL A 1 215 ? 5.050 19.205 22.014 1.00 10.51 ? 301 VAL A CG1 1 ATOM 1708 C CG2 . VAL A 1 215 ? 4.804 20.997 23.778 1.00 11.08 ? 301 VAL A CG2 1 ATOM 1709 N N . ARG A 1 216 ? 3.902 20.815 19.093 1.00 8.03 ? 302 ARG A N 1 ATOM 1710 C CA . ARG A 1 216 ? 3.451 20.260 17.819 1.00 8.54 ? 302 ARG A CA 1 ATOM 1711 C C . ARG A 1 216 ? 4.091 18.915 17.601 1.00 8.29 ? 302 ARG A C 1 ATOM 1712 O O . ARG A 1 216 ? 3.523 18.087 16.925 1.00 7.83 ? 302 ARG A O 1 ATOM 1713 C CB . ARG A 1 216 ? 3.802 21.107 16.597 1.00 11.20 ? 302 ARG A CB 1 ATOM 1714 C CG . ARG A 1 216 ? 2.834 22.180 16.210 1.00 13.53 ? 302 ARG A CG 1 ATOM 1715 C CD . ARG A 1 216 ? 1.484 21.608 15.722 1.00 12.85 ? 302 ARG A CD 1 ATOM 1716 N NE . ARG A 1 216 ? 1.494 21.095 14.371 1.00 10.66 ? 302 ARG A NE 1 ATOM 1717 C CZ . ARG A 1 216 ? 0.408 20.636 13.738 1.00 9.43 ? 302 ARG A CZ 1 ATOM 1718 N NH1 . ARG A 1 216 ? -0.757 20.670 14.373 1.00 11.24 ? 302 ARG A NH1 1 ATOM 1719 N NH2 . ARG A 1 216 ? 0.455 20.209 12.488 1.00 10.36 ? 302 ARG A NH2 1 ATOM 1720 N N . GLY A 1 217 ? 5.290 18.729 18.150 1.00 7.64 ? 303 GLY A N 1 ATOM 1721 C CA . GLY A 1 217 ? 5.983 17.477 17.900 1.00 6.76 ? 303 GLY A CA 1 ATOM 1722 C C . GLY A 1 217 ? 7.481 17.603 18.137 1.00 6.21 ? 303 GLY A C 1 ATOM 1723 O O . GLY A 1 217 ? 7.901 18.064 19.197 1.00 4.35 ? 303 GLY A O 1 ATOM 1724 N N . LEU A 1 218 ? 8.251 17.131 17.159 1.00 5.69 ? 304 LEU A N 1 ATOM 1725 C CA . LEU A 1 218 ? 9.699 16.959 17.292 1.00 4.87 ? 304 LEU A CA 1 ATOM 1726 C C . LEU A 1 218 ? 10.471 17.559 16.130 1.00 5.28 ? 304 LEU A C 1 ATOM 1727 O O . LEU A 1 218 ? 9.964 17.659 15.009 1.00 6.20 ? 304 LEU A O 1 ATOM 1728 C CB . LEU A 1 218 ? 10.039 15.455 17.419 1.00 6.54 ? 304 LEU A CB 1 ATOM 1729 C CG . LEU A 1 218 ? 9.358 14.705 18.542 1.00 5.36 ? 304 LEU A CG 1 ATOM 1730 C CD1 . LEU A 1 218 ? 9.629 13.224 18.452 1.00 5.60 ? 304 LEU A CD1 1 ATOM 1731 C CD2 . LEU A 1 218 ? 9.745 15.246 19.910 1.00 6.67 ? 304 LEU A CD2 1 ATOM 1732 N N . ALA A 1 219 ? 11.733 17.908 16.388 1.00 5.25 ? 305 ALA A N 1 ATOM 1733 C CA . ALA A 1 219 ? 12.648 18.401 15.357 1.00 5.24 ? 305 ALA A CA 1 ATOM 1734 C C . ALA A 1 219 ? 13.735 17.394 15.133 1.00 6.11 ? 305 ALA A C 1 ATOM 1735 O O . ALA A 1 219 ? 14.295 16.851 16.118 1.00 6.77 ? 305 ALA A O 1 ATOM 1736 C CB . ALA A 1 219 ? 13.302 19.744 15.781 1.00 6.47 ? 305 ALA A CB 1 ATOM 1737 N N . THR A 1 220 ? 14.061 17.091 13.875 1.00 4.89 ? 306 THR A N 1 ATOM 1738 C CA . THR A 1 220 ? 15.119 16.106 13.629 1.00 5.98 ? 306 THR A CA 1 ATOM 1739 C C . THR A 1 220 ? 16.183 16.651 12.723 1.00 5.83 ? 306 THR A C 1 ATOM 1740 O O . THR A 1 220 ? 15.976 17.615 12.002 1.00 5.93 ? 306 THR A O 1 ATOM 1741 C CB . THR A 1 220 ? 14.616 14.755 13.050 1.00 6.86 ? 306 THR A CB 1 ATOM 1742 O OG1 . THR A 1 220 ? 14.153 14.920 11.695 1.00 9.45 ? 306 THR A OG1 1 ATOM 1743 C CG2 . THR A 1 220 ? 13.437 14.260 13.883 1.00 8.56 ? 306 THR A CG2 1 ATOM 1744 N N . ASN A 1 221 ? 17.335 16.011 12.795 1.00 5.75 ? 307 ASN A N 1 ATOM 1745 C CA . ASN A 1 221 ? 18.500 16.365 11.996 1.00 6.02 ? 307 ASN A CA 1 ATOM 1746 C C . ASN A 1 221 ? 19.106 17.727 12.336 1.00 4.80 ? 307 ASN A C 1 ATOM 1747 O O . ASN A 1 221 ? 19.918 18.224 11.565 1.00 4.18 ? 307 ASN A O 1 ATOM 1748 C CB . ASN A 1 221 ? 18.198 16.307 10.484 1.00 5.67 ? 307 ASN A CB 1 ATOM 1749 C CG . ASN A 1 221 ? 19.461 16.197 9.621 1.00 8.14 ? 307 ASN A CG 1 ATOM 1750 O OD1 . ASN A 1 221 ? 20.353 15.410 9.962 1.00 5.79 ? 307 ASN A OD1 1 ATOM 1751 N ND2 . ASN A 1 221 ? 19.545 16.955 8.496 1.00 5.08 ? 307 ASN A ND2 1 ATOM 1752 N N . VAL A 1 222 ? 18.737 18.325 13.476 1.00 4.92 ? 308 VAL A N 1 ATOM 1753 C CA . VAL A 1 222 ? 19.303 19.638 13.851 1.00 5.29 ? 308 VAL A CA 1 ATOM 1754 C C . VAL A 1 222 ? 20.834 19.572 13.885 1.00 5.57 ? 308 VAL A C 1 ATOM 1755 O O . VAL A 1 222 ? 21.422 18.717 14.563 1.00 6.80 ? 308 VAL A O 1 ATOM 1756 C CB . VAL A 1 222 ? 18.767 20.092 15.215 1.00 4.28 ? 308 VAL A CB 1 ATOM 1757 C CG1 . VAL A 1 222 ? 19.440 21.401 15.644 1.00 4.82 ? 308 VAL A CG1 1 ATOM 1758 C CG2 . VAL A 1 222 ? 17.266 20.299 15.175 1.00 6.19 ? 308 VAL A CG2 1 ATOM 1759 N N . ALA A 1 223 ? 21.466 20.486 13.136 1.00 5.66 ? 309 ALA A N 1 ATOM 1760 C CA . ALA A 1 223 ? 22.910 20.608 13.051 1.00 5.71 ? 309 ALA A CA 1 ATOM 1761 C C . ALA A 1 223 ? 23.609 19.394 12.403 1.00 6.01 ? 309 ALA A C 1 ATOM 1762 O O . ALA A 1 223 ? 24.824 19.271 12.415 1.00 6.71 ? 309 ALA A O 1 ATOM 1763 C CB . ALA A 1 223 ? 23.506 20.872 14.450 1.00 7.56 ? 309 ALA A CB 1 ATOM 1764 N N . ASN A 1 224 ? 22.809 18.497 11.845 1.00 5.60 ? 310 ASN A N 1 ATOM 1765 C CA . ASN A 1 224 ? 23.376 17.380 11.126 1.00 5.01 ? 310 ASN A CA 1 ATOM 1766 C C . ASN A 1 224 ? 23.150 17.516 9.618 1.00 6.03 ? 310 ASN A C 1 ATOM 1767 O O . ASN A 1 224 ? 22.657 18.538 9.139 1.00 5.42 ? 310 ASN A O 1 ATOM 1768 C CB . ASN A 1 224 ? 22.848 16.078 11.707 1.00 4.89 ? 310 ASN A CB 1 ATOM 1769 C CG . ASN A 1 224 ? 23.715 15.627 12.854 1.00 6.43 ? 310 ASN A CG 1 ATOM 1770 O OD1 . ASN A 1 224 ? 24.595 14.779 12.697 1.00 10.78 ? 310 ASN A OD1 1 ATOM 1771 N ND2 . ASN A 1 224 ? 23.514 16.246 14.021 1.00 10.96 ? 310 ASN A ND2 1 ATOM 1772 N N . TYR A 1 225 ? 23.519 16.471 8.869 1.00 5.29 ? 311 TYR A N 1 ATOM 1773 C CA . TYR A 1 225 ? 23.635 16.613 7.410 1.00 4.94 ? 311 TYR A CA 1 ATOM 1774 C C . TYR A 1 225 ? 22.791 15.617 6.645 1.00 5.16 ? 311 TYR A C 1 ATOM 1775 O O . TYR A 1 225 ? 22.951 15.452 5.432 1.00 5.59 ? 311 TYR A O 1 ATOM 1776 C CB . TYR A 1 225 ? 25.098 16.459 7.017 1.00 4.77 ? 311 TYR A CB 1 ATOM 1777 C CG . TYR A 1 225 ? 26.022 17.238 7.877 1.00 5.52 ? 311 TYR A CG 1 ATOM 1778 C CD1 . TYR A 1 225 ? 26.379 18.534 7.529 1.00 5.22 ? 311 TYR A CD1 1 ATOM 1779 C CD2 . TYR A 1 225 ? 26.606 16.663 9.018 1.00 6.79 ? 311 TYR A CD2 1 ATOM 1780 C CE1 . TYR A 1 225 ? 27.282 19.247 8.301 1.00 5.93 ? 311 TYR A CE1 1 ATOM 1781 C CE2 . TYR A 1 225 ? 27.512 17.371 9.780 1.00 5.61 ? 311 TYR A CE2 1 ATOM 1782 C CZ . TYR A 1 225 ? 27.852 18.665 9.430 1.00 5.67 ? 311 TYR A CZ 1 ATOM 1783 O OH . TYR A 1 225 ? 28.780 19.374 10.174 1.00 7.51 ? 311 TYR A OH 1 ATOM 1784 N N . ASN A 1 226 ? 21.878 14.939 7.314 1.00 5.58 ? 312 ASN A N 1 ATOM 1785 C CA . ASN A 1 226 ? 21.173 13.823 6.692 1.00 6.00 ? 312 ASN A CA 1 ATOM 1786 C C . ASN A 1 226 ? 20.273 14.221 5.538 1.00 6.12 ? 312 ASN A C 1 ATOM 1787 O O . ASN A 1 226 ? 19.707 15.336 5.489 1.00 5.07 ? 312 ASN A O 1 ATOM 1788 C CB . ASN A 1 226 ? 20.321 13.070 7.713 1.00 4.94 ? 312 ASN A CB 1 ATOM 1789 C CG . ASN A 1 226 ? 21.143 12.429 8.829 1.00 4.92 ? 312 ASN A CG 1 ATOM 1790 O OD1 . ASN A 1 226 ? 22.386 12.460 8.819 1.00 7.12 ? 312 ASN A OD1 1 ATOM 1791 N ND2 . ASN A 1 226 ? 20.457 11.868 9.791 1.00 6.11 ? 312 ASN A ND2 1 ATOM 1792 N N . ALA A 1 227 ? 20.065 13.240 4.658 1.00 6.17 ? 313 ALA A N 1 ATOM 1793 C CA . ALA A 1 227 ? 19.085 13.409 3.596 1.00 6.49 ? 313 ALA A CA 1 ATOM 1794 C C . ALA A 1 227 ? 17.691 13.365 4.138 1.00 6.48 ? 313 ALA A C 1 ATOM 1795 O O . ALA A 1 227 ? 17.430 12.660 5.115 1.00 6.69 ? 313 ALA A O 1 ATOM 1796 C CB . ALA A 1 227 ? 19.214 12.301 2.589 1.00 7.78 ? 313 ALA A CB 1 ATOM 1797 N N . TRP A 1 228 ? 16.780 14.085 3.489 1.00 7.38 ? 314 TRP A N 1 ATOM 1798 C CA . TRP A 1 228 ? 15.355 13.854 3.783 1.00 7.37 ? 314 TRP A CA 1 ATOM 1799 C C . TRP A 1 228 ? 14.980 12.527 3.142 1.00 8.14 ? 314 TRP A C 1 ATOM 1800 O O . TRP A 1 228 ? 14.512 11.614 3.793 1.00 7.41 ? 314 TRP A O 1 ATOM 1801 C CB . TRP A 1 228 ? 14.475 15.021 3.292 1.00 7.70 ? 314 TRP A CB 1 ATOM 1802 C CG . TRP A 1 228 ? 13.038 14.625 2.984 1.00 6.22 ? 314 TRP A CG 1 ATOM 1803 C CD1 . TRP A 1 228 ? 12.461 14.581 1.760 1.00 8.54 ? 314 TRP A CD1 1 ATOM 1804 C CD2 . TRP A 1 228 ? 12.056 14.141 3.917 1.00 6.34 ? 314 TRP A CD2 1 ATOM 1805 N NE1 . TRP A 1 228 ? 11.168 14.128 1.872 1.00 6.98 ? 314 TRP A NE1 1 ATOM 1806 C CE2 . TRP A 1 228 ? 10.900 13.830 3.184 1.00 5.99 ? 314 TRP A CE2 1 ATOM 1807 C CE3 . TRP A 1 228 ? 12.036 13.939 5.298 1.00 6.43 ? 314 TRP A CE3 1 ATOM 1808 C CZ2 . TRP A 1 228 ? 9.742 13.351 3.786 1.00 8.94 ? 314 TRP A CZ2 1 ATOM 1809 C CZ3 . TRP A 1 228 ? 10.922 13.460 5.892 1.00 7.00 ? 314 TRP A CZ3 1 ATOM 1810 C CH2 . TRP A 1 228 ? 9.768 13.152 5.138 1.00 5.35 ? 314 TRP A CH2 1 ATOM 1811 N N . SER A 1 229 ? 15.186 12.427 1.823 1.00 7.87 ? 315 SER A N 1 ATOM 1812 C CA . SER A 1 229 ? 14.829 11.200 1.104 1.00 9.67 ? 315 SER A CA 1 ATOM 1813 C C . SER A 1 229 ? 15.779 10.988 -0.055 1.00 10.73 ? 315 SER A C 1 ATOM 1814 O O . SER A 1 229 ? 15.825 11.824 -0.974 1.00 13.65 ? 315 SER A O 1 ATOM 1815 C CB . SER A 1 229 ? 13.416 11.294 0.557 1.00 11.70 ? 315 SER A CB 1 ATOM 1816 O OG . SER A 1 229 ? 12.970 10.084 -0.053 1.00 9.94 ? 315 SER A OG 1 ATOM 1817 N N . VAL A 1 230 ? 16.523 9.895 0.001 1.00 9.67 ? 316 VAL A N 1 ATOM 1818 C CA . VAL A 1 230 ? 17.429 9.510 -1.094 1.00 12.69 ? 316 VAL A CA 1 ATOM 1819 C C . VAL A 1 230 ? 17.181 8.065 -1.433 1.00 12.28 ? 316 VAL A C 1 ATOM 1820 O O . VAL A 1 230 ? 16.779 7.292 -0.576 1.00 10.49 ? 316 VAL A O 1 ATOM 1821 C CB . VAL A 1 230 ? 18.927 9.770 -0.838 1.00 13.10 ? 316 VAL A CB 1 ATOM 1822 C CG1 . VAL A 1 230 ? 19.207 11.230 -1.007 1.00 17.88 ? 316 VAL A CG1 1 ATOM 1823 C CG2 . VAL A 1 230 ? 19.369 9.223 0.521 1.00 14.40 ? 316 VAL A CG2 1 ATOM 1824 N N . SER A 1 231 ? 17.423 7.713 -2.700 1.00 14.43 ? 317 SER A N 1 ATOM 1825 C CA . SER A 1 231 ? 17.165 6.379 -3.205 1.00 16.84 ? 317 SER A CA 1 ATOM 1826 C C . SER A 1 231 ? 18.166 5.336 -2.722 1.00 17.17 ? 317 SER A C 1 ATOM 1827 O O . SER A 1 231 ? 17.826 4.174 -2.610 1.00 18.07 ? 317 SER A O 1 ATOM 1828 C CB . SER A 1 231 ? 17.187 6.385 -4.746 1.00 17.67 ? 317 SER A CB 1 ATOM 1829 O OG . SER A 1 231 ? 18.481 6.758 -5.168 1.00 23.87 ? 317 SER A OG 1 ATOM 1830 N N . SER A 1 232 ? 19.390 5.738 -2.445 1.00 16.35 ? 318 SER A N 1 ATOM 1831 C CA . SER A 1 232 ? 20.394 4.757 -2.026 1.00 16.57 ? 318 SER A CA 1 ATOM 1832 C C . SER A 1 232 ? 21.042 5.201 -0.705 1.00 14.92 ? 318 SER A C 1 ATOM 1833 O O . SER A 1 232 ? 21.307 6.401 -0.525 1.00 14.05 ? 318 SER A O 1 ATOM 1834 C CB A SER A 1 232 ? 21.457 4.546 -3.083 0.50 16.89 ? 318 SER A CB 1 ATOM 1835 C CB B SER A 1 232 ? 21.438 4.574 -3.118 0.50 16.83 ? 318 SER A CB 1 ATOM 1836 O OG A SER A 1 232 ? 22.234 3.402 -2.753 0.50 19.50 ? 318 SER A OG 1 ATOM 1837 O OG B SER A 1 232 ? 22.449 5.560 -3.068 0.50 19.54 ? 318 SER A OG 1 ATOM 1838 N N . PRO A 1 233 ? 21.236 4.261 0.213 1.00 13.39 ? 319 PRO A N 1 ATOM 1839 C CA . PRO A 1 233 ? 21.776 4.606 1.527 1.00 12.18 ? 319 PRO A CA 1 ATOM 1840 C C . PRO A 1 233 ? 23.190 5.065 1.407 1.00 10.72 ? 319 PRO A C 1 ATOM 1841 O O . PRO A 1 233 ? 24.062 4.370 0.834 1.00 10.25 ? 319 PRO A O 1 ATOM 1842 C CB . PRO A 1 233 ? 21.648 3.314 2.354 1.00 13.50 ? 319 PRO A CB 1 ATOM 1843 C CG . PRO A 1 233 ? 20.838 2.373 1.529 1.00 15.48 ? 319 PRO A CG 1 ATOM 1844 C CD . PRO A 1 233 ? 20.832 2.851 0.126 1.00 14.37 ? 319 PRO A CD 1 ATOM 1845 N N . PRO A 1 234 ? 23.499 6.245 1.937 1.00 9.23 ? 320 PRO A N 1 ATOM 1846 C CA . PRO A 1 234 ? 24.885 6.675 1.993 1.00 8.70 ? 320 PRO A CA 1 ATOM 1847 C C . PRO A 1 234 ? 25.732 5.606 2.706 1.00 9.58 ? 320 PRO A C 1 ATOM 1848 O O . PRO A 1 234 ? 25.275 4.909 3.602 1.00 7.72 ? 320 PRO A O 1 ATOM 1849 C CB . PRO A 1 234 ? 24.860 8.013 2.757 1.00 8.91 ? 320 PRO A CB 1 ATOM 1850 C CG . PRO A 1 234 ? 23.464 8.571 2.558 1.00 9.09 ? 320 PRO A CG 1 ATOM 1851 C CD . PRO A 1 234 ? 22.612 7.277 2.466 1.00 8.84 ? 320 PRO A CD 1 ATOM 1852 N N . PRO A 1 235 ? 26.987 5.447 2.268 1.00 11.65 ? 321 PRO A N 1 ATOM 1853 C CA . PRO A 1 235 ? 27.835 4.365 2.787 1.00 10.84 ? 321 PRO A CA 1 ATOM 1854 C C . PRO A 1 235 ? 28.020 4.379 4.303 1.00 11.46 ? 321 PRO A C 1 ATOM 1855 O O . PRO A 1 235 ? 28.068 3.319 4.937 1.00 10.85 ? 321 PRO A O 1 ATOM 1856 C CB . PRO A 1 235 ? 29.210 4.546 2.118 1.00 12.75 ? 321 PRO A CB 1 ATOM 1857 C CG . PRO A 1 235 ? 29.056 5.494 0.977 1.00 16.03 ? 321 PRO A CG 1 ATOM 1858 C CD . PRO A 1 235 ? 27.707 6.244 1.273 1.00 11.43 ? 321 PRO A CD 1 ATOM 1859 N N . TYR A 1 236 ? 28.131 5.573 4.885 1.00 8.71 ? 322 TYR A N 1 ATOM 1860 C CA . TYR A 1 236 ? 28.354 5.643 6.317 1.00 7.99 ? 322 TYR A CA 1 ATOM 1861 C C . TYR A 1 236 ? 27.074 5.346 7.118 1.00 7.33 ? 322 TYR A C 1 ATOM 1862 O O . TYR A 1 236 ? 27.100 5.273 8.335 1.00 7.15 ? 322 TYR A O 1 ATOM 1863 C CB . TYR A 1 236 ? 28.900 7.025 6.685 1.00 8.14 ? 322 TYR A CB 1 ATOM 1864 C CG . TYR A 1 236 ? 28.173 8.097 5.941 1.00 7.38 ? 322 TYR A CG 1 ATOM 1865 C CD1 . TYR A 1 236 ? 26.939 8.540 6.390 1.00 7.71 ? 322 TYR A CD1 1 ATOM 1866 C CD2 . TYR A 1 236 ? 28.702 8.626 4.774 1.00 7.69 ? 322 TYR A CD2 1 ATOM 1867 C CE1 . TYR A 1 236 ? 26.247 9.518 5.690 1.00 5.85 ? 322 TYR A CE1 1 ATOM 1868 C CE2 . TYR A 1 236 ? 28.014 9.614 4.063 1.00 6.89 ? 322 TYR A CE2 1 ATOM 1869 C CZ . TYR A 1 236 ? 26.779 10.040 4.517 1.00 8.52 ? 322 TYR A CZ 1 ATOM 1870 O OH . TYR A 1 236 ? 26.083 10.997 3.790 1.00 7.33 ? 322 TYR A OH 1 ATOM 1871 N N . THR A 1 237 ? 25.946 5.145 6.453 1.00 7.87 ? 323 THR A N 1 ATOM 1872 C CA . THR A 1 237 ? 24.723 4.775 7.173 1.00 7.15 ? 323 THR A CA 1 ATOM 1873 C C . THR A 1 237 ? 24.555 3.311 7.430 1.00 8.11 ? 323 THR A C 1 ATOM 1874 O O . THR A 1 237 ? 23.697 2.944 8.231 1.00 7.82 ? 323 THR A O 1 ATOM 1875 C CB . THR A 1 237 ? 23.438 5.311 6.498 1.00 7.29 ? 323 THR A CB 1 ATOM 1876 O OG1 . THR A 1 237 ? 23.200 4.636 5.246 1.00 7.74 ? 323 THR A OG1 1 ATOM 1877 C CG2 . THR A 1 237 ? 23.535 6.826 6.260 1.00 5.24 ? 323 THR A CG2 1 ATOM 1878 N N . SER A 1 238 ? 25.308 2.471 6.726 1.00 9.12 ? 324 SER A N 1 ATOM 1879 C CA . SER A 1 238 ? 25.102 1.019 6.841 1.00 10.47 ? 324 SER A CA 1 ATOM 1880 C C . SER A 1 238 ? 25.444 0.537 8.247 1.00 10.69 ? 324 SER A C 1 ATOM 1881 O O . SER A 1 238 ? 26.440 0.989 8.811 1.00 9.78 ? 324 SER A O 1 ATOM 1882 C CB . SER A 1 238 ? 25.997 0.310 5.824 1.00 11.32 ? 324 SER A CB 1 ATOM 1883 O OG . SER A 1 238 ? 25.914 -1.095 5.973 1.00 15.97 ? 324 SER A OG 1 ATOM 1884 N N . PRO A 1 239 ? 24.697 -0.397 8.830 1.00 9.97 ? 325 PRO A N 1 ATOM 1885 C CA . PRO A 1 239 ? 23.546 -1.056 8.237 1.00 9.71 ? 325 PRO A CA 1 ATOM 1886 C C . PRO A 1 239 ? 22.194 -0.588 8.749 1.00 9.15 ? 325 PRO A C 1 ATOM 1887 O O . PRO A 1 239 ? 21.277 -1.394 8.889 1.00 10.85 ? 325 PRO A O 1 ATOM 1888 C CB . PRO A 1 239 ? 23.760 -2.498 8.714 1.00 11.74 ? 325 PRO A CB 1 ATOM 1889 C CG . PRO A 1 239 ? 24.295 -2.335 10.077 1.00 12.67 ? 325 PRO A CG 1 ATOM 1890 C CD . PRO A 1 239 ? 25.026 -1.039 10.130 1.00 12.13 ? 325 PRO A CD 1 ATOM 1891 N N . ASN A 1 240 ? 22.026 0.708 8.958 1.00 7.10 ? 326 ASN A N 1 ATOM 1892 C CA . ASN A 1 240 ? 20.741 1.212 9.448 1.00 8.18 ? 326 ASN A CA 1 ATOM 1893 C C . ASN A 1 240 ? 19.665 1.205 8.336 1.00 8.34 ? 326 ASN A C 1 ATOM 1894 O O . ASN A 1 240 ? 19.829 1.845 7.303 1.00 8.29 ? 326 ASN A O 1 ATOM 1895 C CB . ASN A 1 240 ? 20.945 2.653 9.959 1.00 6.53 ? 326 ASN A CB 1 ATOM 1896 C CG . ASN A 1 240 ? 19.805 3.170 10.811 1.00 9.75 ? 326 ASN A CG 1 ATOM 1897 O OD1 . ASN A 1 240 ? 18.716 2.580 10.890 1.00 8.31 ? 326 ASN A OD1 1 ATOM 1898 N ND2 . ASN A 1 240 ? 20.049 4.317 11.458 1.00 6.35 ? 326 ASN A ND2 1 ATOM 1899 N N . PRO A 1 241 ? 18.535 0.524 8.545 1.00 9.07 ? 327 PRO A N 1 ATOM 1900 C CA . PRO A 1 241 ? 17.443 0.588 7.555 1.00 9.45 ? 327 PRO A CA 1 ATOM 1901 C C . PRO A 1 241 ? 16.864 1.981 7.455 1.00 8.26 ? 327 PRO A C 1 ATOM 1902 O O . PRO A 1 241 ? 16.332 2.371 6.423 1.00 8.74 ? 327 PRO A O 1 ATOM 1903 C CB . PRO A 1 241 ? 16.389 -0.360 8.111 1.00 9.68 ? 327 PRO A CB 1 ATOM 1904 C CG . PRO A 1 241 ? 16.703 -0.527 9.530 1.00 11.28 ? 327 PRO A CG 1 ATOM 1905 C CD . PRO A 1 241 ? 18.191 -0.302 9.698 1.00 9.48 ? 327 PRO A CD 1 ATOM 1906 N N . ASN A 1 242 ? 16.975 2.722 8.545 1.00 8.16 ? 328 ASN A N 1 ATOM 1907 C CA . ASN A 1 242 ? 16.540 4.141 8.588 1.00 7.73 ? 328 ASN A CA 1 ATOM 1908 C C . ASN A 1 242 ? 17.680 5.068 8.229 1.00 7.04 ? 328 ASN A C 1 ATOM 1909 O O . ASN A 1 242 ? 18.273 5.712 9.095 1.00 7.87 ? 328 ASN A O 1 ATOM 1910 C CB . ASN A 1 242 ? 15.944 4.414 9.924 1.00 7.03 ? 328 ASN A CB 1 ATOM 1911 C CG . ASN A 1 242 ? 14.712 3.533 10.170 1.00 9.48 ? 328 ASN A CG 1 ATOM 1912 O OD1 . ASN A 1 242 ? 13.935 3.293 9.248 1.00 9.40 ? 328 ASN A OD1 1 ATOM 1913 N ND2 . ASN A 1 242 ? 14.557 3.023 11.378 1.00 9.92 ? 328 ASN A ND2 1 ATOM 1914 N N . TYR A 1 243 ? 17.968 5.130 6.931 1.00 6.43 ? 329 TYR A N 1 ATOM 1915 C CA . TYR A 1 243 ? 19.198 5.786 6.466 1.00 7.49 ? 329 TYR A CA 1 ATOM 1916 C C . TYR A 1 243 ? 18.998 7.244 6.044 1.00 6.92 ? 329 TYR A C 1 ATOM 1917 O O . TYR A 1 243 ? 19.959 7.937 5.723 1.00 7.27 ? 329 TYR A O 1 ATOM 1918 C CB . TYR A 1 243 ? 19.821 4.953 5.342 1.00 6.65 ? 329 TYR A CB 1 ATOM 1919 C CG . TYR A 1 243 ? 18.932 4.792 4.136 1.00 9.56 ? 329 TYR A CG 1 ATOM 1920 C CD1 . TYR A 1 243 ? 18.813 5.829 3.228 1.00 10.40 ? 329 TYR A CD1 1 ATOM 1921 C CD2 . TYR A 1 243 ? 18.194 3.635 3.918 1.00 12.33 ? 329 TYR A CD2 1 ATOM 1922 C CE1 . TYR A 1 243 ? 18.004 5.749 2.131 1.00 13.01 ? 329 TYR A CE1 1 ATOM 1923 C CE2 . TYR A 1 243 ? 17.369 3.535 2.796 1.00 14.31 ? 329 TYR A CE2 1 ATOM 1924 C CZ . TYR A 1 243 ? 17.279 4.598 1.921 1.00 13.96 ? 329 TYR A CZ 1 ATOM 1925 O OH . TYR A 1 243 ? 16.493 4.557 0.797 1.00 19.51 ? 329 TYR A OH 1 ATOM 1926 N N . ASP A 1 244 ? 17.761 7.699 6.107 1.00 6.86 ? 330 ASP A N 1 ATOM 1927 C CA . ASP A 1 244 ? 17.426 9.097 5.835 1.00 6.24 ? 330 ASP A CA 1 ATOM 1928 C C . ASP A 1 244 ? 16.296 9.526 6.762 1.00 6.16 ? 330 ASP A C 1 ATOM 1929 O O . ASP A 1 244 ? 15.729 8.689 7.504 1.00 6.27 ? 330 ASP A O 1 ATOM 1930 C CB . ASP A 1 244 ? 17.174 9.318 4.342 1.00 6.90 ? 330 ASP A CB 1 ATOM 1931 C CG . ASP A 1 244 ? 15.975 8.567 3.788 1.00 6.23 ? 330 ASP A CG 1 ATOM 1932 O OD1 . ASP A 1 244 ? 15.130 8.111 4.595 1.00 7.85 ? 330 ASP A OD1 1 ATOM 1933 O OD2 . ASP A 1 244 ? 15.824 8.463 2.544 1.00 8.67 ? 330 ASP A OD2 1 ATOM 1934 N N . GLU A 1 245 ? 16.005 10.815 6.796 1.00 4.88 ? 331 GLU A N 1 ATOM 1935 C CA . GLU A 1 245 ? 15.035 11.339 7.765 1.00 5.88 ? 331 GLU A CA 1 ATOM 1936 C C . GLU A 1 245 ? 13.613 10.855 7.497 1.00 5.49 ? 331 GLU A C 1 ATOM 1937 O O . GLU A 1 245 ? 12.833 10.612 8.432 1.00 5.16 ? 331 GLU A O 1 ATOM 1938 C CB . GLU A 1 245 ? 15.133 12.856 7.880 1.00 6.88 ? 331 GLU A CB 1 ATOM 1939 C CG . GLU A 1 245 ? 16.472 13.284 8.486 1.00 5.64 ? 331 GLU A CG 1 ATOM 1940 C CD . GLU A 1 245 ? 16.699 12.780 9.914 1.00 8.01 ? 331 GLU A CD 1 ATOM 1941 O OE1 . GLU A 1 245 ? 15.841 12.986 10.781 1.00 7.45 ? 331 GLU A OE1 1 ATOM 1942 O OE2 . GLU A 1 245 ? 17.732 12.142 10.148 1.00 10.21 ? 331 GLU A OE2 1 ATOM 1943 N N . LYS A 1 246 ? 13.291 10.664 6.233 1.00 6.00 ? 332 LYS A N 1 ATOM 1944 C CA . LYS A 1 246 ? 11.946 10.126 5.896 1.00 5.74 ? 332 LYS A CA 1 ATOM 1945 C C . LYS A 1 246 ? 11.759 8.724 6.473 1.00 5.89 ? 332 LYS A C 1 ATOM 1946 O O . LYS A 1 246 ? 10.724 8.435 7.063 1.00 6.01 ? 332 LYS A O 1 ATOM 1947 C CB A LYS A 1 246 ? 11.732 10.127 4.387 0.65 5.81 ? 332 LYS A CB 1 ATOM 1948 C CB B LYS A 1 246 ? 11.703 10.131 4.389 0.35 6.01 ? 332 LYS A CB 1 ATOM 1949 C CG A LYS A 1 246 ? 10.349 9.568 3.949 0.65 6.84 ? 332 LYS A CG 1 ATOM 1950 C CG B LYS A 1 246 ? 10.287 9.660 4.009 0.35 6.87 ? 332 LYS A CG 1 ATOM 1951 C CD A LYS A 1 246 ? 10.207 9.639 2.445 0.65 8.16 ? 332 LYS A CD 1 ATOM 1952 C CD B LYS A 1 246 ? 10.122 9.521 2.519 0.35 8.55 ? 332 LYS A CD 1 ATOM 1953 C CE A LYS A 1 246 ? 8.871 9.092 1.974 0.65 7.16 ? 332 LYS A CE 1 ATOM 1954 C CE B LYS A 1 246 ? 8.676 9.256 2.148 0.35 8.96 ? 332 LYS A CE 1 ATOM 1955 N NZ A LYS A 1 246 ? 8.783 7.605 2.152 0.65 4.63 ? 332 LYS A NZ 1 ATOM 1956 N NZ B LYS A 1 246 ? 8.464 9.132 0.686 0.35 10.73 ? 332 LYS A NZ 1 ATOM 1957 N N . HIS A 1 247 ? 12.734 7.849 6.313 1.00 6.06 ? 333 HIS A N 1 ATOM 1958 C CA . HIS A 1 247 ? 12.616 6.501 6.877 1.00 6.34 ? 333 HIS A CA 1 ATOM 1959 C C . HIS A 1 247 ? 12.480 6.575 8.404 1.00 5.67 ? 333 HIS A C 1 ATOM 1960 O O . HIS A 1 247 ? 11.681 5.867 9.010 1.00 6.27 ? 333 HIS A O 1 ATOM 1961 C CB . HIS A 1 247 ? 13.797 5.593 6.554 1.00 6.39 ? 333 HIS A CB 1 ATOM 1962 C CG . HIS A 1 247 ? 13.763 4.983 5.186 1.00 7.94 ? 333 HIS A CG 1 ATOM 1963 N ND1 . HIS A 1 247 ? 14.096 5.680 4.047 1.00 11.39 ? 333 HIS A ND1 1 ATOM 1964 C CD2 . HIS A 1 247 ? 13.497 3.714 4.797 1.00 9.94 ? 333 HIS A CD2 1 ATOM 1965 C CE1 . HIS A 1 247 ? 14.034 4.856 3.003 1.00 11.01 ? 333 HIS A CE1 1 ATOM 1966 N NE2 . HIS A 1 247 ? 13.662 3.660 3.435 1.00 10.63 ? 333 HIS A NE2 1 ATOM 1967 N N . TYR A 1 248 ? 13.328 7.373 9.026 1.00 5.58 ? 334 TYR A N 1 ATOM 1968 C CA . TYR A 1 248 ? 13.294 7.564 10.497 1.00 4.65 ? 334 TYR A CA 1 ATOM 1969 C C . TYR A 1 248 ? 11.912 8.029 10.955 1.00 5.02 ? 334 TYR A C 1 ATOM 1970 O O . TYR A 1 248 ? 11.330 7.422 11.825 1.00 5.60 ? 334 TYR A O 1 ATOM 1971 C CB . TYR A 1 248 ? 14.349 8.585 10.918 1.00 4.51 ? 334 TYR A CB 1 ATOM 1972 C CG . TYR A 1 248 ? 14.378 9.045 12.355 1.00 4.62 ? 334 TYR A CG 1 ATOM 1973 C CD1 . TYR A 1 248 ? 14.061 8.194 13.413 1.00 6.96 ? 334 TYR A CD1 1 ATOM 1974 C CD2 . TYR A 1 248 ? 14.800 10.352 12.671 1.00 5.24 ? 334 TYR A CD2 1 ATOM 1975 C CE1 . TYR A 1 248 ? 14.140 8.620 14.728 1.00 5.74 ? 334 TYR A CE1 1 ATOM 1976 C CE2 . TYR A 1 248 ? 14.899 10.774 14.000 1.00 5.69 ? 334 TYR A CE2 1 ATOM 1977 C CZ . TYR A 1 248 ? 14.554 9.893 15.010 1.00 6.39 ? 334 TYR A CZ 1 ATOM 1978 O OH . TYR A 1 248 ? 14.624 10.293 16.329 1.00 6.23 ? 334 TYR A OH 1 ATOM 1979 N N . ILE A 1 249 ? 11.411 9.104 10.375 1.00 6.05 ? 335 ILE A N 1 ATOM 1980 C CA . ILE A 1 249 ? 10.125 9.680 10.791 1.00 6.12 ? 335 ILE A CA 1 ATOM 1981 C C . ILE A 1 249 ? 8.955 8.719 10.573 1.00 6.82 ? 335 ILE A C 1 ATOM 1982 O O . ILE A 1 249 ? 8.109 8.552 11.449 1.00 7.05 ? 335 ILE A O 1 ATOM 1983 C CB . ILE A 1 249 ? 9.913 11.023 10.147 1.00 8.41 ? 335 ILE A CB 1 ATOM 1984 C CG1 . ILE A 1 249 ? 10.825 12.032 10.860 1.00 6.88 ? 335 ILE A CG1 1 ATOM 1985 C CG2 . ILE A 1 249 ? 8.472 11.471 10.262 1.00 12.40 ? 335 ILE A CG2 1 ATOM 1986 C CD1 . ILE A 1 249 ? 11.057 13.332 10.112 1.00 9.92 ? 335 ILE A CD1 1 ATOM 1987 N N . GLU A 1 250 ? 8.954 8.029 9.439 1.00 7.19 ? 336 GLU A N 1 ATOM 1988 C CA . GLU A 1 250 ? 7.897 7.035 9.162 1.00 8.10 ? 336 GLU A CA 1 ATOM 1989 C C . GLU A 1 250 ? 7.930 5.873 10.112 1.00 8.05 ? 336 GLU A C 1 ATOM 1990 O O . GLU A 1 250 ? 6.880 5.320 10.405 1.00 9.66 ? 336 GLU A O 1 ATOM 1991 C CB . GLU A 1 250 ? 7.951 6.552 7.709 1.00 8.08 ? 336 GLU A CB 1 ATOM 1992 C CG . GLU A 1 250 ? 7.508 7.698 6.791 1.00 9.50 ? 336 GLU A CG 1 ATOM 1993 C CD . GLU A 1 250 ? 7.453 7.396 5.282 1.00 13.00 ? 336 GLU A CD 1 ATOM 1994 O OE1 . GLU A 1 250 ? 8.071 6.425 4.814 1.00 11.37 ? 336 GLU A OE1 1 ATOM 1995 O OE2 . GLU A 1 250 ? 6.758 8.174 4.571 1.00 11.44 ? 336 GLU A OE2 1 ATOM 1996 N N . ALA A 1 251 ? 9.104 5.474 10.589 1.00 7.53 ? 337 ALA A N 1 ATOM 1997 C CA . ALA A 1 251 ? 9.179 4.437 11.597 1.00 7.31 ? 337 ALA A CA 1 ATOM 1998 C C . ALA A 1 251 ? 8.842 4.929 13.011 1.00 7.38 ? 337 ALA A C 1 ATOM 1999 O O . ALA A 1 251 ? 8.346 4.181 13.868 1.00 7.50 ? 337 ALA A O 1 ATOM 2000 C CB . ALA A 1 251 ? 10.598 3.825 11.605 1.00 7.63 ? 337 ALA A CB 1 ATOM 2001 N N . PHE A 1 252 ? 9.238 6.167 13.281 1.00 6.75 ? 338 PHE A N 1 ATOM 2002 C CA . PHE A 1 252 ? 9.178 6.745 14.627 1.00 6.66 ? 338 PHE A CA 1 ATOM 2003 C C . PHE A 1 252 ? 7.754 7.181 15.002 1.00 7.31 ? 338 PHE A C 1 ATOM 2004 O O . PHE A 1 252 ? 7.280 6.967 16.120 1.00 6.80 ? 338 PHE A O 1 ATOM 2005 C CB . PHE A 1 252 ? 10.143 7.956 14.616 1.00 6.68 ? 338 PHE A CB 1 ATOM 2006 C CG . PHE A 1 252 ? 10.518 8.524 15.960 1.00 7.10 ? 338 PHE A CG 1 ATOM 2007 C CD1 . PHE A 1 252 ? 10.483 7.783 17.147 1.00 6.65 ? 338 PHE A CD1 1 ATOM 2008 C CD2 . PHE A 1 252 ? 11.038 9.815 15.996 1.00 8.82 ? 338 PHE A CD2 1 ATOM 2009 C CE1 . PHE A 1 252 ? 10.911 8.346 18.342 1.00 5.90 ? 338 PHE A CE1 1 ATOM 2010 C CE2 . PHE A 1 252 ? 11.478 10.379 17.189 1.00 8.42 ? 338 PHE A CE2 1 ATOM 2011 C CZ . PHE A 1 252 ? 11.422 9.663 18.363 1.00 6.13 ? 338 PHE A CZ 1 ATOM 2012 N N . ARG A 1 253 ? 7.041 7.772 14.014 1.00 8.22 ? 339 ARG A N 1 ATOM 2013 C CA . ARG A 1 253 ? 5.767 8.374 14.411 1.00 8.51 ? 339 ARG A CA 1 ATOM 2014 C C . ARG A 1 253 ? 4.712 7.353 14.896 1.00 7.98 ? 339 ARG A C 1 ATOM 2015 O O . ARG A 1 253 ? 4.028 7.589 15.878 1.00 7.10 ? 339 ARG A O 1 ATOM 2016 C CB . ARG A 1 253 ? 5.206 9.217 13.286 1.00 9.90 ? 339 ARG A CB 1 ATOM 2017 C CG . ARG A 1 253 ? 3.687 9.334 13.318 1.00 10.15 ? 339 ARG A CG 1 ATOM 2018 C CD . ARG A 1 253 ? 3.179 10.388 14.297 1.00 11.19 ? 339 ARG A CD 1 ATOM 2019 N NE . ARG A 1 253 ? 1.743 10.558 14.154 1.00 9.59 ? 339 ARG A NE 1 ATOM 2020 C CZ . ARG A 1 253 ? 1.232 11.608 13.534 1.00 10.99 ? 339 ARG A CZ 1 ATOM 2021 N NH1 . ARG A 1 253 ? 2.030 12.605 13.186 1.00 11.44 ? 339 ARG A NH1 1 ATOM 2022 N NH2 . ARG A 1 253 ? -0.068 11.672 13.252 1.00 11.79 ? 339 ARG A NH2 1 ATOM 2023 N N . PRO A 1 254 ? 4.590 6.186 14.287 1.00 7.80 ? 340 PRO A N 1 ATOM 2024 C CA . PRO A 1 254 ? 3.638 5.194 14.794 1.00 9.36 ? 340 PRO A CA 1 ATOM 2025 C C . PRO A 1 254 ? 3.947 4.766 16.232 1.00 8.98 ? 340 PRO A C 1 ATOM 2026 O O . PRO A 1 254 ? 3.038 4.525 17.031 1.00 9.21 ? 340 PRO A O 1 ATOM 2027 C CB . PRO A 1 254 ? 3.718 4.010 13.824 1.00 10.31 ? 340 PRO A CB 1 ATOM 2028 C CG . PRO A 1 254 ? 4.908 4.200 12.955 1.00 13.09 ? 340 PRO A CG 1 ATOM 2029 C CD . PRO A 1 254 ? 5.236 5.723 13.066 1.00 8.35 ? 340 PRO A CD 1 ATOM 2030 N N . LEU A 1 255 ? 5.236 4.695 16.566 1.00 8.70 ? 341 LEU A N 1 ATOM 2031 C CA . LEU A 1 255 ? 5.674 4.329 17.928 1.00 7.05 ? 341 LEU A CA 1 ATOM 2032 C C . LEU A 1 255 ? 5.307 5.414 18.932 1.00 8.43 ? 341 LEU A C 1 ATOM 2033 O O . LEU A 1 255 ? 4.839 5.144 20.027 1.00 7.83 ? 341 LEU A O 1 ATOM 2034 C CB . LEU A 1 255 ? 7.193 4.055 17.967 1.00 7.33 ? 341 LEU A CB 1 ATOM 2035 C CG . LEU A 1 255 ? 7.698 2.884 17.103 1.00 8.71 ? 341 LEU A CG 1 ATOM 2036 C CD1 . LEU A 1 255 ? 9.227 2.813 17.036 1.00 9.95 ? 341 LEU A CD1 1 ATOM 2037 C CD2 . LEU A 1 255 ? 7.187 1.575 17.671 1.00 12.24 ? 341 LEU A CD2 1 ATOM 2038 N N . LEU A 1 256 ? 5.554 6.649 18.544 1.00 7.52 ? 342 LEU A N 1 ATOM 2039 C CA . LEU A 1 256 ? 5.168 7.790 19.371 1.00 7.10 ? 342 LEU A CA 1 ATOM 2040 C C . LEU A 1 256 ? 3.655 7.877 19.548 1.00 7.64 ? 342 LEU A C 1 ATOM 2041 O O . LEU A 1 256 ? 3.151 8.156 20.650 1.00 7.89 ? 342 LEU A O 1 ATOM 2042 C CB . LEU A 1 256 ? 5.704 9.079 18.721 1.00 5.19 ? 342 LEU A CB 1 ATOM 2043 C CG . LEU A 1 256 ? 7.226 9.302 18.763 1.00 7.15 ? 342 LEU A CG 1 ATOM 2044 C CD1 . LEU A 1 256 ? 7.702 10.173 17.629 1.00 4.71 ? 342 LEU A CD1 1 ATOM 2045 C CD2 . LEU A 1 256 ? 7.664 9.873 20.091 1.00 7.28 ? 342 LEU A CD2 1 ATOM 2046 N N . GLU A 1 257 ? 2.946 7.698 18.436 1.00 8.16 ? 343 GLU A N 1 ATOM 2047 C CA . GLU A 1 257 ? 1.482 7.851 18.411 1.00 8.68 ? 343 GLU A CA 1 ATOM 2048 C C . GLU A 1 257 ? 0.774 6.800 19.283 1.00 8.79 ? 343 GLU A C 1 ATOM 2049 O O . GLU A 1 257 ? -0.122 7.129 20.045 1.00 7.39 ? 343 GLU A O 1 ATOM 2050 C CB . GLU A 1 257 ? 0.958 7.859 16.985 1.00 10.38 ? 343 GLU A CB 1 ATOM 2051 C CG . GLU A 1 257 ? -0.553 8.039 16.968 1.00 13.54 ? 343 GLU A CG 1 ATOM 2052 C CD . GLU A 1 257 ? -1.074 8.629 15.690 1.00 18.86 ? 343 GLU A CD 1 ATOM 2053 O OE1 . GLU A 1 257 ? -0.292 8.774 14.726 1.00 14.80 ? 343 GLU A OE1 1 ATOM 2054 O OE2 . GLU A 1 257 ? -2.295 8.966 15.697 1.00 23.81 ? 343 GLU A OE2 1 ATOM 2055 N N . ALA A 1 258 ? 1.262 5.572 19.264 1.00 8.05 ? 344 ALA A N 1 ATOM 2056 C CA . ALA A 1 258 ? 0.727 4.511 20.119 1.00 7.47 ? 344 ALA A CA 1 ATOM 2057 C C . ALA A 1 258 ? 0.932 4.850 21.596 1.00 8.75 ? 344 ALA A C 1 ATOM 2058 O O . ALA A 1 258 ? 0.237 4.342 22.473 1.00 9.53 ? 344 ALA A O 1 ATOM 2059 C CB . ALA A 1 258 ? 1.341 3.144 19.788 1.00 7.87 ? 344 ALA A CB 1 ATOM 2060 N N . ARG A 1 259 ? 1.896 5.721 21.861 1.00 7.11 ? 345 ARG A N 1 ATOM 2061 C CA . ARG A 1 259 ? 2.252 6.098 23.205 1.00 8.52 ? 345 ARG A CA 1 ATOM 2062 C C . ARG A 1 259 ? 1.711 7.460 23.593 1.00 7.84 ? 345 ARG A C 1 ATOM 2063 O O . ARG A 1 259 ? 2.092 7.963 24.635 1.00 9.18 ? 345 ARG A O 1 ATOM 2064 C CB . ARG A 1 259 ? 3.758 5.950 23.390 1.00 7.96 ? 345 ARG A CB 1 ATOM 2065 C CG . ARG A 1 259 ? 4.188 4.520 23.296 1.00 7.91 ? 345 ARG A CG 1 ATOM 2066 C CD . ARG A 1 259 ? 5.683 4.327 23.205 1.00 9.25 ? 345 ARG A CD 1 ATOM 2067 N NE . ARG A 1 259 ? 5.952 2.878 23.191 1.00 12.21 ? 345 ARG A NE 1 ATOM 2068 C CZ . ARG A 1 259 ? 5.770 2.071 22.149 1.00 12.51 ? 345 ARG A CZ 1 ATOM 2069 N NH1 . ARG A 1 259 ? 5.366 2.524 20.967 1.00 11.18 ? 345 ARG A NH1 1 ATOM 2070 N NH2 . ARG A 1 259 ? 6.015 0.754 22.282 1.00 14.60 ? 345 ARG A NH2 1 ATOM 2071 N N . GLY A 1 260 ? 0.774 7.970 22.795 1.00 6.81 ? 346 GLY A N 1 ATOM 2072 C CA . GLY A 1 260 ? 0.001 9.139 23.147 1.00 6.87 ? 346 GLY A CA 1 ATOM 2073 C C . GLY A 1 260 ? 0.479 10.449 22.546 1.00 6.51 ? 346 GLY A C 1 ATOM 2074 O O . GLY A 1 260 ? -0.125 11.481 22.797 1.00 8.31 ? 346 GLY A O 1 ATOM 2075 N N . PHE A 1 261 ? 1.515 10.393 21.711 1.00 7.07 ? 347 PHE A N 1 ATOM 2076 C CA . PHE A 1 261 ? 2.125 11.604 21.151 1.00 6.61 ? 347 PHE A CA 1 ATOM 2077 C C . PHE A 1 261 ? 2.174 11.520 19.624 1.00 7.06 ? 347 PHE A C 1 ATOM 2078 O O . PHE A 1 261 ? 3.155 11.041 19.063 1.00 7.48 ? 347 PHE A O 1 ATOM 2079 C CB . PHE A 1 261 ? 3.529 11.728 21.745 1.00 6.88 ? 347 PHE A CB 1 ATOM 2080 C CG . PHE A 1 261 ? 4.262 13.008 21.430 1.00 6.53 ? 347 PHE A CG 1 ATOM 2081 C CD1 . PHE A 1 261 ? 3.647 14.142 20.900 1.00 6.10 ? 347 PHE A CD1 1 ATOM 2082 C CD2 . PHE A 1 261 ? 5.605 13.075 21.769 1.00 5.92 ? 347 PHE A CD2 1 ATOM 2083 C CE1 . PHE A 1 261 ? 4.388 15.284 20.682 1.00 7.01 ? 347 PHE A CE1 1 ATOM 2084 C CE2 . PHE A 1 261 ? 6.334 14.192 21.529 1.00 7.21 ? 347 PHE A CE2 1 ATOM 2085 C CZ . PHE A 1 261 ? 5.736 15.309 21.000 1.00 6.73 ? 347 PHE A CZ 1 ATOM 2086 N N . PRO A 1 262 ? 1.138 11.996 18.948 1.00 6.88 ? 348 PRO A N 1 ATOM 2087 C CA . PRO A 1 262 ? 1.097 11.985 17.482 1.00 7.21 ? 348 PRO A CA 1 ATOM 2088 C C . PRO A 1 262 ? 1.892 13.143 16.884 1.00 6.96 ? 348 PRO A C 1 ATOM 2089 O O . PRO A 1 262 ? 1.393 14.051 16.192 1.00 8.49 ? 348 PRO A O 1 ATOM 2090 C CB . PRO A 1 262 ? -0.407 12.132 17.187 1.00 8.33 ? 348 PRO A CB 1 ATOM 2091 C CG . PRO A 1 262 ? -0.938 12.915 18.289 1.00 9.15 ? 348 PRO A CG 1 ATOM 2092 C CD . PRO A 1 262 ? -0.129 12.503 19.509 1.00 8.83 ? 348 PRO A CD 1 ATOM 2093 N N . ALA A 1 263 ? 3.183 13.096 17.142 1.00 6.55 ? 349 ALA A N 1 ATOM 2094 C CA . ALA A 1 263 ? 4.086 14.207 16.823 1.00 6.19 ? 349 ALA A CA 1 ATOM 2095 C C . ALA A 1 263 ? 4.183 14.479 15.351 1.00 6.01 ? 349 ALA A C 1 ATOM 2096 O O . ALA A 1 263 ? 4.399 13.584 14.521 1.00 7.25 ? 349 ALA A O 1 ATOM 2097 C CB . ALA A 1 263 ? 5.501 13.903 17.339 1.00 7.08 ? 349 ALA A CB 1 ATOM 2098 N N . GLN A 1 264 ? 4.072 15.760 15.031 1.00 6.30 ? 350 GLN A N 1 ATOM 2099 C CA . GLN A 1 264 ? 4.448 16.274 13.740 1.00 6.92 ? 350 GLN A CA 1 ATOM 2100 C C . GLN A 1 264 ? 5.907 16.674 13.790 1.00 6.72 ? 350 GLN A C 1 ATOM 2101 O O . GLN A 1 264 ? 6.430 16.940 14.844 1.00 8.86 ? 350 GLN A O 1 ATOM 2102 C CB . GLN A 1 264 ? 3.581 17.494 13.386 1.00 6.14 ? 350 GLN A CB 1 ATOM 2103 C CG . GLN A 1 264 ? 2.155 17.116 13.052 1.00 8.11 ? 350 GLN A CG 1 ATOM 2104 C CD . GLN A 1 264 ? 1.985 16.341 11.740 1.00 9.19 ? 350 GLN A CD 1 ATOM 2105 O OE1 . GLN A 1 264 ? 1.598 15.155 11.755 1.00 10.48 ? 350 GLN A OE1 1 ATOM 2106 N NE2 . GLN A 1 264 ? 2.209 16.995 10.624 1.00 9.79 ? 350 GLN A NE2 1 ATOM 2107 N N . PHE A 1 265 ? 6.564 16.736 12.639 1.00 6.54 ? 351 PHE A N 1 ATOM 2108 C CA . PHE A 1 265 ? 8.019 16.946 12.576 1.00 6.92 ? 351 PHE A CA 1 ATOM 2109 C C . PHE A 1 265 ? 8.436 18.159 11.799 1.00 6.66 ? 351 PHE A C 1 ATOM 2110 O O . PHE A 1 265 ? 7.747 18.584 10.864 1.00 7.30 ? 351 PHE A O 1 ATOM 2111 C CB . PHE A 1 265 ? 8.683 15.734 11.965 1.00 6.90 ? 351 PHE A CB 1 ATOM 2112 C CG . PHE A 1 265 ? 8.642 14.514 12.858 1.00 7.96 ? 351 PHE A CG 1 ATOM 2113 C CD1 . PHE A 1 265 ? 7.530 13.706 12.930 1.00 7.60 ? 351 PHE A CD1 1 ATOM 2114 C CD2 . PHE A 1 265 ? 9.752 14.198 13.632 1.00 7.04 ? 351 PHE A CD2 1 ATOM 2115 C CE1 . PHE A 1 265 ? 7.530 12.591 13.779 1.00 8.33 ? 351 PHE A CE1 1 ATOM 2116 C CE2 . PHE A 1 265 ? 9.768 13.112 14.456 1.00 7.98 ? 351 PHE A CE2 1 ATOM 2117 C CZ . PHE A 1 265 ? 8.624 12.285 14.532 1.00 7.03 ? 351 PHE A CZ 1 ATOM 2118 N N . ILE A 1 266 ? 9.565 18.729 12.209 1.00 5.41 ? 352 ILE A N 1 ATOM 2119 C CA . ILE A 1 266 ? 10.295 19.670 11.364 1.00 5.65 ? 352 ILE A CA 1 ATOM 2120 C C . ILE A 1 266 ? 11.672 19.078 11.177 1.00 5.86 ? 352 ILE A C 1 ATOM 2121 O O . ILE A 1 266 ? 12.186 18.425 12.098 1.00 6.40 ? 352 ILE A O 1 ATOM 2122 C CB . ILE A 1 266 ? 10.356 21.095 11.848 1.00 6.68 ? 352 ILE A CB 1 ATOM 2123 C CG1 . ILE A 1 266 ? 11.007 21.203 13.219 1.00 7.90 ? 352 ILE A CG1 1 ATOM 2124 C CG2 . ILE A 1 266 ? 8.936 21.683 11.864 1.00 5.93 ? 352 ILE A CG2 1 ATOM 2125 C CD1 . ILE A 1 266 ? 11.174 22.695 13.602 1.00 7.77 ? 352 ILE A CD1 1 ATOM 2126 N N . VAL A 1 267 ? 12.211 19.199 9.983 1.00 5.76 ? 353 VAL A N 1 ATOM 2127 C CA . VAL A 1 267 ? 13.459 18.503 9.642 1.00 5.88 ? 353 VAL A CA 1 ATOM 2128 C C . VAL A 1 267 ? 14.489 19.513 9.135 1.00 6.58 ? 353 VAL A C 1 ATOM 2129 O O . VAL A 1 267 ? 14.227 20.232 8.157 1.00 5.97 ? 353 VAL A O 1 ATOM 2130 C CB . VAL A 1 267 ? 13.255 17.432 8.545 1.00 6.72 ? 353 VAL A CB 1 ATOM 2131 C CG1 . VAL A 1 267 ? 14.575 16.734 8.215 1.00 7.25 ? 353 VAL A CG1 1 ATOM 2132 C CG2 . VAL A 1 267 ? 12.222 16.423 8.914 1.00 8.82 ? 353 VAL A CG2 1 ATOM 2133 N N . ASP A 1 268 ? 15.636 19.594 9.818 1.00 6.00 ? 354 ASP A N 1 ATOM 2134 C CA . ASP A 1 268 ? 16.722 20.480 9.364 1.00 5.59 ? 354 ASP A CA 1 ATOM 2135 C C . ASP A 1 268 ? 17.256 19.966 8.028 1.00 5.72 ? 354 ASP A C 1 ATOM 2136 O O . ASP A 1 268 ? 17.587 18.773 7.871 1.00 4.62 ? 354 ASP A O 1 ATOM 2137 C CB . ASP A 1 268 ? 17.831 20.492 10.400 1.00 5.99 ? 354 ASP A CB 1 ATOM 2138 C CG . ASP A 1 268 ? 18.766 21.677 10.324 1.00 6.48 ? 354 ASP A CG 1 ATOM 2139 O OD1 . ASP A 1 268 ? 18.743 22.449 9.325 1.00 8.25 ? 354 ASP A OD1 1 ATOM 2140 O OD2 . ASP A 1 268 ? 19.539 21.927 11.298 1.00 5.30 ? 354 ASP A OD2 1 ATOM 2141 N N . GLN A 1 269 ? 17.332 20.877 7.067 1.00 4.61 ? 355 GLN A N 1 ATOM 2142 C CA . GLN A 1 269 ? 17.949 20.598 5.758 1.00 6.12 ? 355 GLN A CA 1 ATOM 2143 C C . GLN A 1 269 ? 19.007 21.658 5.381 1.00 5.14 ? 355 GLN A C 1 ATOM 2144 O O . GLN A 1 269 ? 19.520 21.683 4.258 1.00 6.02 ? 355 GLN A O 1 ATOM 2145 C CB . GLN A 1 269 ? 16.914 20.443 4.649 1.00 6.04 ? 355 GLN A CB 1 ATOM 2146 C CG . GLN A 1 269 ? 16.090 19.159 4.768 1.00 6.88 ? 355 GLN A CG 1 ATOM 2147 C CD . GLN A 1 269 ? 16.854 17.894 4.459 1.00 7.12 ? 355 GLN A CD 1 ATOM 2148 O OE1 . GLN A 1 269 ? 17.080 17.622 3.285 1.00 7.36 ? 355 GLN A OE1 1 ATOM 2149 N NE2 . GLN A 1 269 ? 17.276 17.143 5.487 1.00 6.64 ? 355 GLN A NE2 1 ATOM 2150 N N . GLY A 1 270 ? 19.351 22.501 6.338 1.00 5.79 ? 356 GLY A N 1 ATOM 2151 C CA . GLY A 1 270 ? 20.275 23.575 6.077 1.00 5.54 ? 356 GLY A CA 1 ATOM 2152 C C . GLY A 1 270 ? 21.647 23.203 5.541 1.00 6.79 ? 356 GLY A C 1 ATOM 2153 O O . GLY A 1 270 ? 22.298 24.023 4.887 1.00 6.16 ? 356 GLY A O 1 ATOM 2154 N N . ARG A 1 271 ? 22.138 22.006 5.859 1.00 5.19 ? 357 ARG A N 1 ATOM 2155 C CA . ARG A 1 271 ? 23.431 21.529 5.345 1.00 5.92 ? 357 ARG A CA 1 ATOM 2156 C C . ARG A 1 271 ? 23.267 20.146 4.730 1.00 6.53 ? 357 ARG A C 1 ATOM 2157 O O . ARG A 1 271 ? 24.163 19.315 4.771 1.00 5.28 ? 357 ARG A O 1 ATOM 2158 C CB . ARG A 1 271 ? 24.475 21.546 6.456 1.00 6.21 ? 357 ARG A CB 1 ATOM 2159 C CG . ARG A 1 271 ? 24.700 22.953 7.046 1.00 6.33 ? 357 ARG A CG 1 ATOM 2160 C CD . ARG A 1 271 ? 25.856 23.065 8.001 1.00 5.56 ? 357 ARG A CD 1 ATOM 2161 N NE . ARG A 1 271 ? 25.703 22.275 9.231 1.00 6.07 ? 357 ARG A NE 1 ATOM 2162 C CZ . ARG A 1 271 ? 26.675 22.099 10.110 1.00 4.97 ? 357 ARG A CZ 1 ATOM 2163 N NH1 . ARG A 1 271 ? 27.854 22.700 9.916 1.00 7.59 ? 357 ARG A NH1 1 ATOM 2164 N NH2 . ARG A 1 271 ? 26.468 21.384 11.192 1.00 5.37 ? 357 ARG A NH2 1 ATOM 2165 N N . SER A 1 272 ? 22.115 19.911 4.111 1.00 5.36 ? 358 SER A N 1 ATOM 2166 C CA . SER A 1 272 ? 21.776 18.582 3.572 1.00 5.68 ? 358 SER A CA 1 ATOM 2167 C C . SER A 1 272 ? 21.692 18.522 2.050 1.00 5.83 ? 358 SER A C 1 ATOM 2168 O O . SER A 1 272 ? 21.260 17.510 1.492 1.00 5.88 ? 358 SER A O 1 ATOM 2169 C CB . SER A 1 272 ? 20.427 18.146 4.124 1.00 5.33 ? 358 SER A CB 1 ATOM 2170 O OG . SER A 1 272 ? 20.483 17.864 5.521 1.00 6.66 ? 358 SER A OG 1 ATOM 2171 N N . GLY A 1 273 ? 22.070 19.593 1.372 1.00 5.30 ? 359 GLY A N 1 ATOM 2172 C CA . GLY A 1 273 ? 21.853 19.656 -0.070 1.00 6.43 ? 359 GLY A CA 1 ATOM 2173 C C . GLY A 1 273 ? 22.657 18.622 -0.832 1.00 7.02 ? 359 GLY A C 1 ATOM 2174 O O . GLY A 1 273 ? 22.183 18.119 -1.874 1.00 8.86 ? 359 GLY A O 1 ATOM 2175 N N . LYS A 1 274 ? 23.871 18.326 -0.382 1.00 7.53 ? 360 LYS A N 1 ATOM 2176 C CA . LYS A 1 274 ? 24.695 17.329 -1.073 1.00 8.51 ? 360 LYS A CA 1 ATOM 2177 C C . LYS A 1 274 ? 24.605 15.955 -0.400 1.00 8.97 ? 360 LYS A C 1 ATOM 2178 O O . LYS A 1 274 ? 24.855 15.828 0.800 1.00 6.34 ? 360 LYS A O 1 ATOM 2179 C CB . LYS A 1 274 ? 26.142 17.786 -1.125 1.00 9.74 ? 360 LYS A CB 1 ATOM 2180 C CG . LYS A 1 274 ? 27.071 16.774 -1.786 1.00 9.23 ? 360 LYS A CG 1 ATOM 2181 C CD . LYS A 1 274 ? 28.443 17.345 -1.903 1.00 11.27 ? 360 LYS A CD 1 ATOM 2182 C CE . LYS A 1 274 ? 29.467 16.249 -2.155 1.00 9.68 ? 360 LYS A CE 1 ATOM 2183 N NZ . LYS A 1 274 ? 29.583 15.275 -1.045 1.00 12.72 ? 360 LYS A NZ 1 ATOM 2184 N N . GLN A 1 275 ? 24.249 14.946 -1.171 1.00 8.21 ? 361 GLN A N 1 ATOM 2185 C CA . GLN A 1 275 ? 24.128 13.591 -0.659 1.00 7.75 ? 361 GLN A CA 1 ATOM 2186 C C . GLN A 1 275 ? 24.761 12.625 -1.644 1.00 8.95 ? 361 GLN A C 1 ATOM 2187 O O . GLN A 1 275 ? 24.505 12.748 -2.846 1.00 9.38 ? 361 GLN A O 1 ATOM 2188 C CB . GLN A 1 275 ? 22.676 13.172 -0.476 1.00 7.53 ? 361 GLN A CB 1 ATOM 2189 C CG . GLN A 1 275 ? 21.920 13.988 0.513 1.00 7.18 ? 361 GLN A CG 1 ATOM 2190 C CD . GLN A 1 275 ? 22.424 13.878 1.919 1.00 6.61 ? 361 GLN A CD 1 ATOM 2191 O OE1 . GLN A 1 275 ? 22.971 12.850 2.317 1.00 8.03 ? 361 GLN A OE1 1 ATOM 2192 N NE2 . GLN A 1 275 ? 22.224 14.948 2.707 1.00 4.90 ? 361 GLN A NE2 1 ATOM 2193 N N . PRO A 1 276 ? 25.589 11.705 -1.164 1.00 8.18 ? 362 PRO A N 1 ATOM 2194 C CA . PRO A 1 276 ? 26.040 11.647 0.223 1.00 8.42 ? 362 PRO A CA 1 ATOM 2195 C C . PRO A 1 276 ? 26.972 12.779 0.562 1.00 8.16 ? 362 PRO A C 1 ATOM 2196 O O . PRO A 1 276 ? 27.465 13.485 -0.313 1.00 8.29 ? 362 PRO A O 1 ATOM 2197 C CB . PRO A 1 276 ? 26.759 10.298 0.310 1.00 10.00 ? 362 PRO A CB 1 ATOM 2198 C CG . PRO A 1 276 ? 27.199 10.020 -1.023 1.00 12.78 ? 362 PRO A CG 1 ATOM 2199 C CD . PRO A 1 276 ? 26.273 10.691 -2.001 1.00 11.37 ? 362 PRO A CD 1 ATOM 2200 N N . THR A 1 277 ? 27.221 12.959 1.844 1.00 6.70 ? 363 THR A N 1 ATOM 2201 C CA . THR A 1 277 ? 28.161 13.997 2.277 1.00 6.79 ? 363 THR A CA 1 ATOM 2202 C C . THR A 1 277 ? 29.615 13.521 2.156 1.00 7.65 ? 363 THR A C 1 ATOM 2203 O O . THR A 1 277 ? 29.887 12.407 1.714 1.00 8.00 ? 363 THR A O 1 ATOM 2204 C CB . THR A 1 277 ? 27.903 14.372 3.720 1.00 7.47 ? 363 THR A CB 1 ATOM 2205 O OG1 . THR A 1 277 ? 28.241 13.278 4.589 1.00 7.15 ? 363 THR A OG1 1 ATOM 2206 C CG2 . THR A 1 277 ? 26.443 14.703 3.959 1.00 7.24 ? 363 THR A CG2 1 ATOM 2207 N N . GLY A 1 278 ? 30.523 14.329 2.678 1.00 7.24 ? 364 GLY A N 1 ATOM 2208 C CA . GLY A 1 278 ? 31.916 13.963 2.858 1.00 7.96 ? 364 GLY A CA 1 ATOM 2209 C C . GLY A 1 278 ? 32.228 13.330 4.209 1.00 7.61 ? 364 GLY A C 1 ATOM 2210 O O . GLY A 1 278 ? 33.410 13.088 4.536 1.00 8.69 ? 364 GLY A O 1 ATOM 2211 N N . GLN A 1 279 ? 31.204 12.996 4.980 1.00 6.83 ? 365 GLN A N 1 ATOM 2212 C CA . GLN A 1 279 ? 31.460 12.354 6.272 1.00 6.80 ? 365 GLN A CA 1 ATOM 2213 C C . GLN A 1 279 ? 32.019 10.950 6.039 1.00 7.67 ? 365 GLN A C 1 ATOM 2214 O O . GLN A 1 279 ? 31.506 10.212 5.188 1.00 8.22 ? 365 GLN A O 1 ATOM 2215 C CB . GLN A 1 279 ? 30.170 12.212 7.059 1.00 6.61 ? 365 GLN A CB 1 ATOM 2216 C CG . GLN A 1 279 ? 29.566 13.517 7.563 1.00 6.87 ? 365 GLN A CG 1 ATOM 2217 C CD . GLN A 1 279 ? 28.121 13.322 7.972 1.00 5.50 ? 365 GLN A CD 1 ATOM 2218 O OE1 . GLN A 1 279 ? 27.289 13.189 7.078 1.00 7.32 ? 365 GLN A OE1 1 ATOM 2219 N NE2 . GLN A 1 279 ? 27.801 13.318 9.304 1.00 6.08 ? 365 GLN A NE2 1 ATOM 2220 N N . LYS A 1 280 ? 33.059 10.590 6.772 1.00 7.09 ? 366 LYS A N 1 ATOM 2221 C CA . LYS A 1 280 ? 33.601 9.226 6.720 1.00 8.03 ? 366 LYS A CA 1 ATOM 2222 C C . LYS A 1 280 ? 32.838 8.285 7.657 1.00 6.95 ? 366 LYS A C 1 ATOM 2223 O O . LYS A 1 280 ? 32.797 7.050 7.452 1.00 8.74 ? 366 LYS A O 1 ATOM 2224 C CB . LYS A 1 280 ? 35.094 9.258 7.088 1.00 9.48 ? 366 LYS A CB 1 ATOM 2225 C CG . LYS A 1 280 ? 35.954 9.953 6.080 1.00 14.94 ? 366 LYS A CG 1 ATOM 2226 C CD . LYS A 1 280 ? 36.028 9.209 4.776 1.00 23.17 ? 366 LYS A CD 1 ATOM 2227 C CE . LYS A 1 280 ? 37.200 8.235 4.762 1.00 29.27 ? 366 LYS A CE 1 ATOM 2228 N NZ . LYS A 1 280 ? 38.457 9.006 4.555 1.00 34.68 ? 366 LYS A NZ 1 ATOM 2229 N N . GLU A 1 281 ? 32.256 8.853 8.697 1.00 6.72 ? 367 GLU A N 1 ATOM 2230 C CA . GLU A 1 281 ? 31.380 8.132 9.642 1.00 7.01 ? 367 GLU A CA 1 ATOM 2231 C C . GLU A 1 281 ? 30.169 9.012 9.974 1.00 6.25 ? 367 GLU A C 1 ATOM 2232 O O . GLU A 1 281 ? 30.232 10.245 9.887 1.00 5.84 ? 367 GLU A O 1 ATOM 2233 C CB . GLU A 1 281 ? 32.083 7.736 10.939 1.00 7.92 ? 367 GLU A CB 1 ATOM 2234 C CG . GLU A 1 281 ? 33.337 6.904 10.793 1.00 7.78 ? 367 GLU A CG 1 ATOM 2235 C CD . GLU A 1 281 ? 33.124 5.524 10.202 1.00 10.32 ? 367 GLU A CD 1 ATOM 2236 O OE1 . GLU A 1 281 ? 31.978 4.998 10.113 1.00 10.73 ? 367 GLU A OE1 1 ATOM 2237 O OE2 . GLU A 1 281 ? 34.163 4.954 9.802 1.00 8.98 ? 367 GLU A OE2 1 ATOM 2238 N N . TRP A 1 282 ? 29.048 8.367 10.232 1.00 6.34 ? 368 TRP A N 1 ATOM 2239 C CA . TRP A 1 282 ? 27.785 9.099 10.453 1.00 6.37 ? 368 TRP A CA 1 ATOM 2240 C C . TRP A 1 282 ? 27.867 10.046 11.632 1.00 6.60 ? 368 TRP A C 1 ATOM 2241 O O . TRP A 1 282 ? 27.328 11.139 11.617 1.00 6.14 ? 368 TRP A O 1 ATOM 2242 C CB . TRP A 1 282 ? 26.632 8.122 10.655 1.00 6.00 ? 368 TRP A CB 1 ATOM 2243 C CG . TRP A 1 282 ? 25.291 8.610 10.178 1.00 6.56 ? 368 TRP A CG 1 ATOM 2244 C CD1 . TRP A 1 282 ? 24.905 9.899 9.890 1.00 8.63 ? 368 TRP A CD1 1 ATOM 2245 C CD2 . TRP A 1 282 ? 24.141 7.808 9.994 1.00 4.96 ? 368 TRP A CD2 1 ATOM 2246 N NE1 . TRP A 1 282 ? 23.601 9.921 9.482 1.00 6.18 ? 368 TRP A NE1 1 ATOM 2247 C CE2 . TRP A 1 282 ? 23.093 8.656 9.575 1.00 5.45 ? 368 TRP A CE2 1 ATOM 2248 C CE3 . TRP A 1 282 ? 23.871 6.443 10.158 1.00 7.92 ? 368 TRP A CE3 1 ATOM 2249 C CZ2 . TRP A 1 282 ? 21.817 8.191 9.280 1.00 6.12 ? 368 TRP A CZ2 1 ATOM 2250 C CZ3 . TRP A 1 282 ? 22.610 5.992 9.859 1.00 6.01 ? 368 TRP A CZ3 1 ATOM 2251 C CH2 . TRP A 1 282 ? 21.600 6.858 9.446 1.00 8.05 ? 368 TRP A CH2 1 ATOM 2252 N N . GLY A 1 283 ? 28.600 9.610 12.651 1.00 5.78 ? 369 GLY A N 1 ATOM 2253 C CA . GLY A 1 283 ? 28.814 10.344 13.871 1.00 6.91 ? 369 GLY A CA 1 ATOM 2254 C C . GLY A 1 283 ? 29.781 11.517 13.871 1.00 6.37 ? 369 GLY A C 1 ATOM 2255 O O . GLY A 1 283 ? 29.985 12.152 14.923 1.00 7.02 ? 369 GLY A O 1 ATOM 2256 N N . HIS A 1 284 ? 30.349 11.804 12.727 1.00 7.02 ? 370 HIS A N 1 ATOM 2257 C CA . HIS A 1 284 ? 31.266 12.924 12.533 1.00 6.26 ? 370 HIS A CA 1 ATOM 2258 C C . HIS A 1 284 ? 30.390 14.109 12.220 1.00 6.30 ? 370 HIS A C 1 ATOM 2259 O O . HIS A 1 284 ? 29.959 14.293 11.081 1.00 7.43 ? 370 HIS A O 1 ATOM 2260 C CB . HIS A 1 284 ? 32.231 12.587 11.421 1.00 6.43 ? 370 HIS A CB 1 ATOM 2261 C CG . HIS A 1 284 ? 33.177 11.466 11.769 1.00 6.54 ? 370 HIS A CG 1 ATOM 2262 N ND1 . HIS A 1 284 ? 34.155 11.072 10.890 1.00 6.86 ? 370 HIS A ND1 1 ATOM 2263 C CD2 . HIS A 1 284 ? 33.312 10.674 12.869 1.00 10.30 ? 370 HIS A CD2 1 ATOM 2264 C CE1 . HIS A 1 284 ? 34.868 10.089 11.433 1.00 7.87 ? 370 HIS A CE1 1 ATOM 2265 N NE2 . HIS A 1 284 ? 34.358 9.803 12.620 1.00 7.08 ? 370 HIS A NE2 1 ATOM 2266 N N . TRP A 1 285 ? 30.126 14.916 13.239 1.00 6.24 ? 371 TRP A N 1 ATOM 2267 C CA . TRP A 1 285 ? 29.151 15.997 13.157 1.00 6.64 ? 371 TRP A CA 1 ATOM 2268 C C . TRP A 1 285 ? 29.796 17.352 12.948 1.00 6.42 ? 371 TRP A C 1 ATOM 2269 O O . TRP A 1 285 ? 29.097 18.323 12.655 1.00 7.25 ? 371 TRP A O 1 ATOM 2270 C CB . TRP A 1 285 ? 28.253 16.084 14.426 1.00 5.71 ? 371 TRP A CB 1 ATOM 2271 C CG . TRP A 1 285 ? 29.019 16.060 15.699 1.00 6.76 ? 371 TRP A CG 1 ATOM 2272 C CD1 . TRP A 1 285 ? 29.316 14.953 16.453 1.00 7.14 ? 371 TRP A CD1 1 ATOM 2273 C CD2 . TRP A 1 285 ? 29.675 17.160 16.331 1.00 5.52 ? 371 TRP A CD2 1 ATOM 2274 N NE1 . TRP A 1 285 ? 30.084 15.315 17.538 1.00 7.03 ? 371 TRP A NE1 1 ATOM 2275 C CE2 . TRP A 1 285 ? 30.309 16.664 17.493 1.00 6.60 ? 371 TRP A CE2 1 ATOM 2276 C CE3 . TRP A 1 285 ? 29.742 18.543 16.067 1.00 6.59 ? 371 TRP A CE3 1 ATOM 2277 C CZ2 . TRP A 1 285 ? 31.045 17.493 18.356 1.00 7.95 ? 371 TRP A CZ2 1 ATOM 2278 C CZ3 . TRP A 1 285 ? 30.486 19.360 16.901 1.00 7.80 ? 371 TRP A CZ3 1 ATOM 2279 C CH2 . TRP A 1 285 ? 31.096 18.823 18.068 1.00 8.20 ? 371 TRP A CH2 1 ATOM 2280 N N . CYS A 1 286 ? 31.105 17.453 13.194 1.00 5.50 ? 372 CYS A N 1 ATOM 2281 C CA . CYS A 1 286 ? 31.741 18.740 13.286 1.00 6.46 ? 372 CYS A CA 1 ATOM 2282 C C . CYS A 1 286 ? 32.284 19.258 11.969 1.00 5.58 ? 372 CYS A C 1 ATOM 2283 O O . CYS A 1 286 ? 33.213 18.676 11.395 1.00 7.29 ? 372 CYS A O 1 ATOM 2284 C CB . CYS A 1 286 ? 32.836 18.736 14.349 1.00 6.53 ? 372 CYS A CB 1 ATOM 2285 S SG . CYS A 1 286 ? 33.483 20.423 14.540 1.00 8.21 ? 372 CYS A SG 1 ATOM 2286 N N . ASN A 1 287 ? 31.693 20.354 11.487 1.00 6.84 ? 373 ASN A N 1 ATOM 2287 C CA . ASN A 1 287 ? 32.175 21.019 10.306 1.00 6.80 ? 373 ASN A CA 1 ATOM 2288 C C . ASN A 1 287 ? 32.480 20.055 9.138 1.00 7.31 ? 373 ASN A C 1 ATOM 2289 O O . ASN A 1 287 ? 33.538 20.097 8.523 1.00 6.35 ? 373 ASN A O 1 ATOM 2290 C CB . ASN A 1 287 ? 33.466 21.798 10.644 1.00 7.26 ? 373 ASN A CB 1 ATOM 2291 C CG . ASN A 1 287 ? 33.306 22.832 11.726 1.00 8.31 ? 373 ASN A CG 1 ATOM 2292 O OD1 . ASN A 1 287 ? 32.264 23.492 11.829 1.00 7.59 ? 373 ASN A OD1 1 ATOM 2293 N ND2 . ASN A 1 287 ? 34.364 23.001 12.544 1.00 7.75 ? 373 ASN A ND2 1 ATOM 2294 N N . ALA A 1 288 ? 31.537 19.163 8.832 1.00 6.51 ? 374 ALA A N 1 ATOM 2295 C CA . ALA A 1 288 ? 31.797 18.101 7.869 1.00 6.03 ? 374 ALA A CA 1 ATOM 2296 C C . ALA A 1 288 ? 32.031 18.601 6.455 1.00 6.55 ? 374 ALA A C 1 ATOM 2297 O O . ALA A 1 288 ? 31.318 19.464 5.966 1.00 6.66 ? 374 ALA A O 1 ATOM 2298 C CB . ALA A 1 288 ? 30.650 17.145 7.884 1.00 5.24 ? 374 ALA A CB 1 ATOM 2299 N N . ILE A 1 289 ? 33.043 18.050 5.816 1.00 6.26 ? 375 ILE A N 1 ATOM 2300 C CA . ILE A 1 289 ? 33.332 18.438 4.442 1.00 6.52 ? 375 ILE A CA 1 ATOM 2301 C C . ILE A 1 289 ? 32.329 17.787 3.495 1.00 6.14 ? 375 ILE A C 1 ATOM 2302 O O . ILE A 1 289 ? 31.601 16.870 3.856 1.00 6.24 ? 375 ILE A O 1 ATOM 2303 C CB . ILE A 1 289 ? 34.804 18.077 4.073 1.00 6.11 ? 375 ILE A CB 1 ATOM 2304 C CG1 . ILE A 1 289 ? 35.021 16.573 4.084 1.00 9.24 ? 375 ILE A CG1 1 ATOM 2305 C CG2 . ILE A 1 289 ? 35.729 18.853 4.954 1.00 9.48 ? 375 ILE A CG2 1 ATOM 2306 C CD1 . ILE A 1 289 ? 36.463 16.159 3.739 1.00 10.42 ? 375 ILE A CD1 1 ATOM 2307 N N . GLY A 1 290 ? 32.265 18.290 2.259 1.00 7.49 ? 376 GLY A N 1 ATOM 2308 C CA . GLY A 1 290 ? 31.417 17.671 1.246 1.00 7.35 ? 376 GLY A CA 1 ATOM 2309 C C . GLY A 1 290 ? 29.952 17.851 1.512 1.00 7.50 ? 376 GLY A C 1 ATOM 2310 O O . GLY A 1 290 ? 29.155 16.987 1.175 1.00 7.38 ? 376 GLY A O 1 ATOM 2311 N N . THR A 1 291 ? 29.587 18.964 2.123 1.00 6.66 ? 377 THR A N 1 ATOM 2312 C CA . THR A 1 291 ? 28.178 19.275 2.395 1.00 6.49 ? 377 THR A CA 1 ATOM 2313 C C . THR A 1 291 ? 27.767 20.551 1.692 1.00 6.40 ? 377 THR A C 1 ATOM 2314 O O . THR A 1 291 ? 28.629 21.374 1.336 1.00 6.97 ? 377 THR A O 1 ATOM 2315 C CB . THR A 1 291 ? 27.924 19.439 3.914 1.00 7.25 ? 377 THR A CB 1 ATOM 2316 O OG1 . THR A 1 291 ? 28.627 20.604 4.385 1.00 7.85 ? 377 THR A OG1 1 ATOM 2317 C CG2 . THR A 1 291 ? 28.392 18.194 4.664 1.00 9.15 ? 377 THR A CG2 1 ATOM 2318 N N . GLY A 1 292 ? 26.449 20.709 1.491 1.00 6.46 ? 378 GLY A N 1 ATOM 2319 C CA . GLY A 1 292 ? 25.953 21.895 0.802 1.00 7.19 ? 378 GLY A CA 1 ATOM 2320 C C . GLY A 1 292 ? 24.673 22.403 1.403 1.00 6.88 ? 378 GLY A C 1 ATOM 2321 O O . GLY A 1 292 ? 23.927 21.656 2.051 1.00 5.66 ? 378 GLY A O 1 ATOM 2322 N N . PHE A 1 293 ? 24.377 23.680 1.197 1.00 5.81 ? 379 PHE A N 1 ATOM 2323 C CA . PHE A 1 293 ? 23.075 24.238 1.581 1.00 6.77 ? 379 PHE A CA 1 ATOM 2324 C C . PHE A 1 293 ? 21.994 23.371 0.927 1.00 6.11 ? 379 PHE A C 1 ATOM 2325 O O . PHE A 1 293 ? 22.168 22.965 -0.219 1.00 6.89 ? 379 PHE A O 1 ATOM 2326 C CB . PHE A 1 293 ? 22.931 25.675 1.080 1.00 7.65 ? 379 PHE A CB 1 ATOM 2327 C CG . PHE A 1 293 ? 23.650 26.689 1.895 1.00 7.03 ? 379 PHE A CG 1 ATOM 2328 C CD1 . PHE A 1 293 ? 23.434 26.821 3.268 1.00 8.27 ? 379 PHE A CD1 1 ATOM 2329 C CD2 . PHE A 1 293 ? 24.583 27.520 1.266 1.00 6.37 ? 379 PHE A CD2 1 ATOM 2330 C CE1 . PHE A 1 293 ? 24.115 27.795 3.984 1.00 8.09 ? 379 PHE A CE1 1 ATOM 2331 C CE2 . PHE A 1 293 ? 25.324 28.462 1.994 1.00 7.00 ? 379 PHE A CE2 1 ATOM 2332 C CZ . PHE A 1 293 ? 25.054 28.620 3.334 1.00 6.71 ? 379 PHE A CZ 1 ATOM 2333 N N . GLY A 1 294 ? 20.944 23.066 1.660 1.00 5.64 ? 380 GLY A N 1 ATOM 2334 C CA . GLY A 1 294 ? 19.887 22.200 1.138 1.00 5.69 ? 380 GLY A CA 1 ATOM 2335 C C . GLY A 1 294 ? 18.541 22.868 0.793 1.00 7.38 ? 380 GLY A C 1 ATOM 2336 O O . GLY A 1 294 ? 18.434 24.076 0.522 1.00 7.54 ? 380 GLY A O 1 ATOM 2337 N N . MET A 1 295 ? 17.505 22.044 0.748 1.00 8.49 ? 381 MET A N 1 ATOM 2338 C CA . MET A 1 295 ? 16.203 22.545 0.316 1.00 10.15 ? 381 MET A CA 1 ATOM 2339 C C . MET A 1 295 ? 15.764 23.720 1.184 1.00 9.95 ? 381 MET A C 1 ATOM 2340 O O . MET A 1 295 ? 15.960 23.727 2.418 1.00 10.26 ? 381 MET A O 1 ATOM 2341 C CB A MET A 1 295 ? 15.162 21.434 0.323 0.55 11.37 ? 381 MET A CB 1 ATOM 2342 C CB B MET A 1 295 ? 15.144 21.451 0.388 0.45 10.88 ? 381 MET A CB 1 ATOM 2343 C CG A MET A 1 295 ? 14.928 20.859 1.685 0.55 13.85 ? 381 MET A CG 1 ATOM 2344 C CG B MET A 1 295 ? 15.032 20.709 1.701 0.45 13.37 ? 381 MET A CG 1 ATOM 2345 S SD A MET A 1 295 ? 13.637 19.586 1.688 0.55 21.55 ? 381 MET A SD 1 ATOM 2346 S SD B MET A 1 295 ? 13.557 19.604 1.687 0.45 19.89 ? 381 MET A SD 1 ATOM 2347 C CE A MET A 1 295 ? 14.574 18.212 1.005 0.55 11.61 ? 381 MET A CE 1 ATOM 2348 C CE B MET A 1 295 ? 13.608 19.017 -0.005 0.45 9.74 ? 381 MET A CE 1 ATOM 2349 N N . ARG A 1 296 ? 15.143 24.683 0.521 1.00 10.52 ? 382 ARG A N 1 ATOM 2350 C CA . ARG A 1 296 ? 14.743 25.932 1.179 1.00 10.18 ? 382 ARG A CA 1 ATOM 2351 C C . ARG A 1 296 ? 13.606 25.700 2.147 1.00 8.78 ? 382 ARG A C 1 ATOM 2352 O O . ARG A 1 296 ? 12.754 24.834 1.915 1.00 8.68 ? 382 ARG A O 1 ATOM 2353 C CB A ARG A 1 296 ? 14.379 26.992 0.146 0.55 10.71 ? 382 ARG A CB 1 ATOM 2354 C CB B ARG A 1 296 ? 14.373 26.996 0.147 0.45 10.64 ? 382 ARG A CB 1 ATOM 2355 C CG A ARG A 1 296 ? 15.408 27.104 -0.983 0.55 12.30 ? 382 ARG A CG 1 ATOM 2356 C CG B ARG A 1 296 ? 15.378 27.106 -1.005 0.45 12.18 ? 382 ARG A CG 1 ATOM 2357 C CD A ARG A 1 296 ? 16.796 27.540 -0.510 0.55 11.57 ? 382 ARG A CD 1 ATOM 2358 C CD B ARG A 1 296 ? 16.800 27.446 -0.545 0.45 11.85 ? 382 ARG A CD 1 ATOM 2359 N NE A ARG A 1 296 ? 17.616 27.819 -1.678 0.55 11.57 ? 382 ARG A NE 1 ATOM 2360 N NE B ARG A 1 296 ? 17.759 27.311 -1.637 0.45 12.50 ? 382 ARG A NE 1 ATOM 2361 C CZ A ARG A 1 296 ? 18.553 27.044 -2.217 0.55 13.52 ? 382 ARG A CZ 1 ATOM 2362 C CZ B ARG A 1 296 ? 17.835 28.128 -2.688 0.45 12.36 ? 382 ARG A CZ 1 ATOM 2363 N NH1 A ARG A 1 296 ? 18.969 25.906 -1.663 0.55 13.44 ? 382 ARG A NH1 1 ATOM 2364 N NH1 B ARG A 1 296 ? 17.037 29.192 -2.787 0.45 11.70 ? 382 ARG A NH1 1 ATOM 2365 N NH2 A ARG A 1 296 ? 19.125 27.497 -3.323 0.55 15.81 ? 382 ARG A NH2 1 ATOM 2366 N NH2 B ARG A 1 296 ? 18.730 27.909 -3.638 0.45 8.42 ? 382 ARG A NH2 1 ATOM 2367 N N . PRO A 1 297 ? 13.584 26.440 3.249 1.00 7.39 ? 383 PRO A N 1 ATOM 2368 C CA . PRO A 1 297 ? 12.512 26.326 4.239 1.00 7.91 ? 383 PRO A CA 1 ATOM 2369 C C . PRO A 1 297 ? 11.122 26.467 3.611 1.00 7.49 ? 383 PRO A C 1 ATOM 2370 O O . PRO A 1 297 ? 10.895 27.336 2.750 1.00 9.10 ? 383 PRO A O 1 ATOM 2371 C CB . PRO A 1 297 ? 12.799 27.426 5.260 1.00 7.34 ? 383 PRO A CB 1 ATOM 2372 C CG . PRO A 1 297 ? 14.281 27.667 5.203 1.00 7.16 ? 383 PRO A CG 1 ATOM 2373 C CD . PRO A 1 297 ? 14.572 27.437 3.682 1.00 7.98 ? 383 PRO A CD 1 ATOM 2374 N N . THR A 1 298 ? 10.205 25.572 3.990 1.00 7.87 ? 384 THR A N 1 ATOM 2375 C CA . THR A 1 298 ? 8.849 25.619 3.429 1.00 8.38 ? 384 THR A CA 1 ATOM 2376 C C . THR A 1 298 ? 7.849 24.840 4.268 1.00 9.30 ? 384 THR A C 1 ATOM 2377 O O . THR A 1 298 ? 8.212 23.826 4.907 1.00 8.78 ? 384 THR A O 1 ATOM 2378 C CB . THR A 1 298 ? 8.864 25.039 2.011 1.00 9.05 ? 384 THR A CB 1 ATOM 2379 O OG1 . THR A 1 298 ? 7.503 25.015 1.493 1.00 9.50 ? 384 THR A OG1 1 ATOM 2380 C CG2 . THR A 1 298 ? 9.326 23.596 2.073 1.00 8.08 ? 384 THR A CG2 1 ATOM 2381 N N . ALA A 1 299 ? 6.596 25.286 4.273 1.00 8.99 ? 385 ALA A N 1 ATOM 2382 C CA . ALA A 1 299 ? 5.563 24.514 4.921 1.00 9.64 ? 385 ALA A CA 1 ATOM 2383 C C . ALA A 1 299 ? 5.047 23.421 3.963 1.00 10.53 ? 385 ALA A C 1 ATOM 2384 O O . ALA A 1 299 ? 4.369 22.474 4.354 1.00 11.71 ? 385 ALA A O 1 ATOM 2385 C CB . ALA A 1 299 ? 4.426 25.424 5.357 1.00 10.83 ? 385 ALA A CB 1 ATOM 2386 N N . ASN A 1 300 ? 5.372 23.574 2.686 1.00 9.59 ? 386 ASN A N 1 ATOM 2387 C CA . ASN A 1 300 ? 4.833 22.661 1.679 1.00 10.95 ? 386 ASN A CA 1 ATOM 2388 C C . ASN A 1 300 ? 5.723 21.431 1.489 1.00 9.54 ? 386 ASN A C 1 ATOM 2389 O O . ASN A 1 300 ? 6.425 21.278 0.496 1.00 10.83 ? 386 ASN A O 1 ATOM 2390 C CB . ASN A 1 300 ? 4.621 23.409 0.366 1.00 11.19 ? 386 ASN A CB 1 ATOM 2391 C CG . ASN A 1 300 ? 3.639 24.558 0.531 1.00 12.73 ? 386 ASN A CG 1 ATOM 2392 O OD1 . ASN A 1 300 ? 3.834 25.659 -0.008 1.00 16.29 ? 386 ASN A OD1 1 ATOM 2393 N ND2 . ASN A 1 300 ? 2.568 24.297 1.277 1.00 13.01 ? 386 ASN A ND2 1 ATOM 2394 N N . THR A 1 301 ? 5.706 20.569 2.487 1.00 8.37 ? 387 THR A N 1 ATOM 2395 C CA . THR A 1 301 ? 6.629 19.433 2.509 1.00 8.73 ? 387 THR A CA 1 ATOM 2396 C C . THR A 1 301 ? 6.135 18.289 1.653 1.00 8.08 ? 387 THR A C 1 ATOM 2397 O O . THR A 1 301 ? 6.960 17.458 1.234 1.00 9.41 ? 387 THR A O 1 ATOM 2398 C CB . THR A 1 301 ? 6.782 18.872 3.909 1.00 7.39 ? 387 THR A CB 1 ATOM 2399 O OG1 . THR A 1 301 ? 5.508 18.383 4.362 1.00 8.04 ? 387 THR A OG1 1 ATOM 2400 C CG2 . THR A 1 301 ? 7.221 19.976 4.901 1.00 8.83 ? 387 THR A CG2 1 ATOM 2401 N N . GLY A 1 302 ? 4.811 18.201 1.472 1.00 8.15 ? 388 GLY A N 1 ATOM 2402 C CA . GLY A 1 302 ? 4.268 17.064 0.761 1.00 8.83 ? 388 GLY A CA 1 ATOM 2403 C C . GLY A 1 302 ? 4.137 15.789 1.573 1.00 9.21 ? 388 GLY A C 1 ATOM 2404 O O . GLY A 1 302 ? 3.722 14.771 1.033 1.00 10.96 ? 388 GLY A O 1 ATOM 2405 N N . HIS A 1 303 ? 4.505 15.840 2.853 1.00 8.67 ? 389 HIS A N 1 ATOM 2406 C CA . HIS A 1 303 ? 4.501 14.653 3.710 1.00 8.89 ? 389 HIS A CA 1 ATOM 2407 C C . HIS A 1 303 ? 3.564 14.879 4.894 1.00 9.12 ? 389 HIS A C 1 ATOM 2408 O O . HIS A 1 303 ? 3.619 15.928 5.565 1.00 9.18 ? 389 HIS A O 1 ATOM 2409 C CB . HIS A 1 303 ? 5.890 14.279 4.218 1.00 8.52 ? 389 HIS A CB 1 ATOM 2410 C CG . HIS A 1 303 ? 5.931 12.919 4.805 1.00 6.82 ? 389 HIS A CG 1 ATOM 2411 N ND1 . HIS A 1 303 ? 5.410 12.627 6.054 1.00 7.17 ? 389 HIS A ND1 1 ATOM 2412 C CD2 . HIS A 1 303 ? 6.410 11.759 4.309 1.00 9.33 ? 389 HIS A CD2 1 ATOM 2413 C CE1 . HIS A 1 303 ? 5.541 11.337 6.280 1.00 9.72 ? 389 HIS A CE1 1 ATOM 2414 N NE2 . HIS A 1 303 ? 6.151 10.789 5.241 1.00 9.40 ? 389 HIS A NE2 1 ATOM 2415 N N . GLN A 1 304 ? 2.682 13.921 5.124 1.00 8.38 ? 390 GLN A N 1 ATOM 2416 C CA . GLN A 1 304 ? 1.655 14.051 6.149 1.00 9.05 ? 390 GLN A CA 1 ATOM 2417 C C . GLN A 1 304 ? 2.193 14.281 7.571 1.00 8.57 ? 390 GLN A C 1 ATOM 2418 O O . GLN A 1 304 ? 1.484 14.839 8.413 1.00 9.41 ? 390 GLN A O 1 ATOM 2419 C CB . GLN A 1 304 ? 0.716 12.810 6.175 1.00 9.09 ? 390 GLN A CB 1 ATOM 2420 C CG . GLN A 1 304 ? 1.416 11.516 6.516 1.00 10.84 ? 390 GLN A CG 1 ATOM 2421 C CD . GLN A 1 304 ? 0.525 10.268 6.330 1.00 16.57 ? 390 GLN A CD 1 ATOM 2422 O OE1 . GLN A 1 304 ? -0.708 10.373 6.321 1.00 20.22 ? 390 GLN A OE1 1 ATOM 2423 N NE2 . GLN A 1 304 ? 1.160 9.090 6.174 1.00 16.91 ? 390 GLN A NE2 1 ATOM 2424 N N . TYR A 1 305 ? 3.401 13.814 7.876 1.00 7.77 ? 391 TYR A N 1 ATOM 2425 C CA . TYR A 1 305 ? 3.911 13.960 9.236 1.00 7.19 ? 391 TYR A CA 1 ATOM 2426 C C . TYR A 1 305 ? 4.902 15.106 9.410 1.00 7.78 ? 391 TYR A C 1 ATOM 2427 O O . TYR A 1 305 ? 5.460 15.266 10.495 1.00 8.59 ? 391 TYR A O 1 ATOM 2428 C CB . TYR A 1 305 ? 4.612 12.669 9.674 1.00 7.44 ? 391 TYR A CB 1 ATOM 2429 C CG . TYR A 1 305 ? 3.746 11.436 9.708 1.00 9.43 ? 391 TYR A CG 1 ATOM 2430 C CD1 . TYR A 1 305 ? 2.413 11.525 9.992 1.00 9.62 ? 391 TYR A CD1 1 ATOM 2431 C CD2 . TYR A 1 305 ? 4.304 10.173 9.497 1.00 13.54 ? 391 TYR A CD2 1 ATOM 2432 C CE1 . TYR A 1 305 ? 1.616 10.365 10.043 1.00 12.41 ? 391 TYR A CE1 1 ATOM 2433 C CE2 . TYR A 1 305 ? 3.522 9.044 9.548 1.00 14.59 ? 391 TYR A CE2 1 ATOM 2434 C CZ . TYR A 1 305 ? 2.184 9.162 9.808 1.00 14.58 ? 391 TYR A CZ 1 ATOM 2435 O OH . TYR A 1 305 ? 1.378 8.031 9.834 1.00 18.87 ? 391 TYR A OH 1 ATOM 2436 N N . VAL A 1 306 ? 5.173 15.841 8.346 1.00 6.29 ? 392 VAL A N 1 ATOM 2437 C CA . VAL A 1 306 ? 6.231 16.867 8.383 1.00 6.83 ? 392 VAL A CA 1 ATOM 2438 C C . VAL A 1 306 ? 5.574 18.223 8.157 1.00 6.46 ? 392 VAL A C 1 ATOM 2439 O O . VAL A 1 306 ? 5.029 18.520 7.059 1.00 7.93 ? 392 VAL A O 1 ATOM 2440 C CB . VAL A 1 306 ? 7.361 16.635 7.372 1.00 6.68 ? 392 VAL A CB 1 ATOM 2441 C CG1 . VAL A 1 306 ? 8.498 17.640 7.613 1.00 7.25 ? 392 VAL A CG1 1 ATOM 2442 C CG2 . VAL A 1 306 ? 7.911 15.243 7.432 1.00 6.23 ? 392 VAL A CG2 1 ATOM 2443 N N . ASP A 1 307 ? 5.562 19.021 9.208 1.00 6.03 ? 393 ASP A N 1 ATOM 2444 C CA . ASP A 1 307 ? 4.989 20.373 9.170 1.00 5.59 ? 393 ASP A CA 1 ATOM 2445 C C . ASP A 1 307 ? 5.870 21.316 8.323 1.00 7.70 ? 393 ASP A C 1 ATOM 2446 O O . ASP A 1 307 ? 5.379 22.258 7.708 1.00 7.24 ? 393 ASP A O 1 ATOM 2447 C CB . ASP A 1 307 ? 4.941 20.974 10.581 1.00 5.15 ? 393 ASP A CB 1 ATOM 2448 C CG . ASP A 1 307 ? 3.775 20.545 11.418 1.00 5.87 ? 393 ASP A CG 1 ATOM 2449 O OD1 . ASP A 1 307 ? 2.815 19.917 10.862 1.00 7.74 ? 393 ASP A OD1 1 ATOM 2450 O OD2 . ASP A 1 307 ? 3.791 20.831 12.668 1.00 7.40 ? 393 ASP A OD2 1 ATOM 2451 N N . ALA A 1 308 ? 7.185 21.124 8.360 1.00 7.27 ? 394 ALA A N 1 ATOM 2452 C CA . ALA A 1 308 ? 8.075 21.983 7.560 1.00 7.44 ? 394 ALA A CA 1 ATOM 2453 C C . ALA A 1 308 ? 9.471 21.422 7.392 1.00 6.70 ? 394 ALA A C 1 ATOM 2454 O O . ALA A 1 308 ? 9.975 20.711 8.250 1.00 5.91 ? 394 ALA A O 1 ATOM 2455 C CB . ALA A 1 308 ? 8.156 23.386 8.171 1.00 8.22 ? 394 ALA A CB 1 ATOM 2456 N N . PHE A 1 309 ? 10.082 21.716 6.257 1.00 6.35 ? 395 PHE A N 1 ATOM 2457 C CA . PHE A 1 309 ? 11.523 21.632 6.126 1.00 6.14 ? 395 PHE A CA 1 ATOM 2458 C C . PHE A 1 309 ? 12.107 22.974 6.535 1.00 6.15 ? 395 PHE A C 1 ATOM 2459 O O . PHE A 1 309 ? 11.583 24.014 6.183 1.00 7.85 ? 395 PHE A O 1 ATOM 2460 C CB . PHE A 1 309 ? 11.868 21.312 4.682 1.00 7.70 ? 395 PHE A CB 1 ATOM 2461 C CG . PHE A 1 309 ? 11.408 19.944 4.297 1.00 8.23 ? 395 PHE A CG 1 ATOM 2462 C CD1 . PHE A 1 309 ? 11.871 18.842 4.997 1.00 9.40 ? 395 PHE A CD1 1 ATOM 2463 C CD2 . PHE A 1 309 ? 10.555 19.767 3.226 1.00 9.66 ? 395 PHE A CD2 1 ATOM 2464 C CE1 . PHE A 1 309 ? 11.471 17.568 4.647 1.00 10.29 ? 395 PHE A CE1 1 ATOM 2465 C CE2 . PHE A 1 309 ? 10.162 18.467 2.863 1.00 10.36 ? 395 PHE A CE2 1 ATOM 2466 C CZ . PHE A 1 309 ? 10.613 17.384 3.574 1.00 9.92 ? 395 PHE A CZ 1 ATOM 2467 N N . VAL A 1 310 ? 13.135 22.953 7.350 1.00 4.75 ? 396 VAL A N 1 ATOM 2468 C CA . VAL A 1 310 ? 13.692 24.151 7.930 1.00 5.18 ? 396 VAL A CA 1 ATOM 2469 C C . VAL A 1 310 ? 15.183 24.188 7.845 1.00 5.19 ? 396 VAL A C 1 ATOM 2470 O O . VAL A 1 310 ? 15.819 23.177 7.540 1.00 6.47 ? 396 VAL A O 1 ATOM 2471 C CB . VAL A 1 310 ? 13.236 24.271 9.413 1.00 5.02 ? 396 VAL A CB 1 ATOM 2472 C CG1 . VAL A 1 310 ? 11.761 24.675 9.481 1.00 8.09 ? 396 VAL A CG1 1 ATOM 2473 C CG2 . VAL A 1 310 ? 13.515 23.009 10.140 1.00 6.38 ? 396 VAL A CG2 1 ATOM 2474 N N . TRP A 1 311 ? 15.733 25.359 8.107 1.00 4.59 ? 397 TRP A N 1 ATOM 2475 C CA . TRP A 1 311 ? 17.194 25.484 8.298 1.00 5.00 ? 397 TRP A CA 1 ATOM 2476 C C . TRP A 1 311 ? 17.365 25.834 9.764 1.00 6.17 ? 397 TRP A C 1 ATOM 2477 O O . TRP A 1 311 ? 17.102 26.972 10.157 1.00 6.45 ? 397 TRP A O 1 ATOM 2478 C CB . TRP A 1 311 ? 17.790 26.589 7.417 1.00 6.02 ? 397 TRP A CB 1 ATOM 2479 C CG . TRP A 1 311 ? 17.937 26.244 5.986 1.00 6.13 ? 397 TRP A CG 1 ATOM 2480 C CD1 . TRP A 1 311 ? 17.334 25.210 5.285 1.00 6.71 ? 397 TRP A CD1 1 ATOM 2481 C CD2 . TRP A 1 311 ? 18.768 26.921 5.060 1.00 5.44 ? 397 TRP A CD2 1 ATOM 2482 N NE1 . TRP A 1 311 ? 17.759 25.233 3.979 1.00 6.07 ? 397 TRP A NE1 1 ATOM 2483 C CE2 . TRP A 1 311 ? 18.648 26.253 3.811 1.00 5.24 ? 397 TRP A CE2 1 ATOM 2484 C CE3 . TRP A 1 311 ? 19.612 28.027 5.150 1.00 6.87 ? 397 TRP A CE3 1 ATOM 2485 C CZ2 . TRP A 1 311 ? 19.342 26.668 2.678 1.00 8.24 ? 397 TRP A CZ2 1 ATOM 2486 C CZ3 . TRP A 1 311 ? 20.301 28.435 4.040 1.00 8.59 ? 397 TRP A CZ3 1 ATOM 2487 C CH2 . TRP A 1 311 ? 20.164 27.754 2.818 1.00 8.85 ? 397 TRP A CH2 1 ATOM 2488 N N . VAL A 1 312 ? 17.758 24.872 10.594 1.00 5.33 ? 398 VAL A N 1 ATOM 2489 C CA . VAL A 1 312 ? 17.870 25.137 12.032 1.00 4.86 ? 398 VAL A CA 1 ATOM 2490 C C . VAL A 1 312 ? 19.292 25.637 12.328 1.00 5.97 ? 398 VAL A C 1 ATOM 2491 O O . VAL A 1 312 ? 19.503 26.788 12.712 1.00 6.37 ? 398 VAL A O 1 ATOM 2492 C CB . VAL A 1 312 ? 17.451 23.952 12.924 1.00 5.78 ? 398 VAL A CB 1 ATOM 2493 C CG1 . VAL A 1 312 ? 17.358 24.399 14.381 1.00 5.64 ? 398 VAL A CG1 1 ATOM 2494 C CG2 . VAL A 1 312 ? 16.133 23.335 12.515 1.00 6.02 ? 398 VAL A CG2 1 ATOM 2495 N N . LYS A 1 313 ? 20.285 24.785 12.133 1.00 5.01 ? 399 LYS A N 1 ATOM 2496 C CA . LYS A 1 313 ? 21.676 25.236 12.294 1.00 6.16 ? 399 LYS A CA 1 ATOM 2497 C C . LYS A 1 313 ? 22.076 26.118 11.090 1.00 5.63 ? 399 LYS A C 1 ATOM 2498 O O . LYS A 1 313 ? 21.935 25.690 9.945 1.00 6.13 ? 399 LYS A O 1 ATOM 2499 C CB A LYS A 1 313 ? 22.591 24.029 12.447 0.55 6.01 ? 399 LYS A CB 1 ATOM 2500 C CB B LYS A 1 313 ? 22.602 24.034 12.468 0.45 6.91 ? 399 LYS A CB 1 ATOM 2501 C CG A LYS A 1 313 ? 24.063 24.339 12.394 0.55 8.11 ? 399 LYS A CG 1 ATOM 2502 C CG B LYS A 1 313 ? 24.088 24.321 12.390 0.45 8.21 ? 399 LYS A CG 1 ATOM 2503 C CD A LYS A 1 313 ? 24.575 24.962 13.655 0.55 8.38 ? 399 LYS A CD 1 ATOM 2504 C CD B LYS A 1 313 ? 24.552 25.329 13.396 0.45 9.04 ? 399 LYS A CD 1 ATOM 2505 C CE A LYS A 1 313 ? 25.945 25.613 13.337 0.55 9.75 ? 399 LYS A CE 1 ATOM 2506 C CE B LYS A 1 313 ? 26.052 25.628 13.229 0.45 9.81 ? 399 LYS A CE 1 ATOM 2507 N NZ A LYS A 1 313 ? 26.578 26.251 14.510 0.55 5.89 ? 399 LYS A NZ 1 ATOM 2508 N NZ B LYS A 1 313 ? 26.519 25.731 11.789 0.45 6.12 ? 399 LYS A NZ 1 ATOM 2509 N N . PRO A 1 314 ? 22.461 27.386 11.305 1.00 6.72 ? 400 PRO A N 1 ATOM 2510 C CA . PRO A 1 314 ? 22.723 28.274 10.171 1.00 6.22 ? 400 PRO A CA 1 ATOM 2511 C C . PRO A 1 314 ? 24.089 28.004 9.554 1.00 6.21 ? 400 PRO A C 1 ATOM 2512 O O . PRO A 1 314 ? 25.111 28.013 10.218 1.00 8.31 ? 400 PRO A O 1 ATOM 2513 C CB . PRO A 1 314 ? 22.635 29.700 10.723 1.00 6.62 ? 400 PRO A CB 1 ATOM 2514 C CG . PRO A 1 314 ? 22.264 29.616 12.147 1.00 7.44 ? 400 PRO A CG 1 ATOM 2515 C CD . PRO A 1 314 ? 22.558 28.142 12.551 1.00 7.66 ? 400 PRO A CD 1 ATOM 2516 N N . GLY A 1 315 ? 24.090 27.622 8.281 1.00 6.33 ? 401 GLY A N 1 ATOM 2517 C CA . GLY A 1 315 ? 25.343 27.244 7.641 1.00 6.83 ? 401 GLY A CA 1 ATOM 2518 C C . GLY A 1 315 ? 26.361 28.382 7.573 1.00 7.10 ? 401 GLY A C 1 ATOM 2519 O O . GLY A 1 315 ? 26.043 29.499 7.132 1.00 8.57 ? 401 GLY A O 1 ATOM 2520 N N . GLY A 1 316 ? 27.598 28.115 7.962 1.00 5.99 ? 402 GLY A N 1 ATOM 2521 C CA . GLY A 1 316 ? 28.626 29.142 8.000 1.00 7.49 ? 402 GLY A CA 1 ATOM 2522 C C . GLY A 1 316 ? 29.083 29.452 9.418 1.00 8.12 ? 402 GLY A C 1 ATOM 2523 O O . GLY A 1 316 ? 30.206 29.927 9.641 1.00 9.43 ? 402 GLY A O 1 ATOM 2524 N N . GLU A 1 317 ? 28.200 29.187 10.373 1.00 7.53 ? 403 GLU A N 1 ATOM 2525 C CA . GLU A 1 317 ? 28.490 29.319 11.808 1.00 7.81 ? 403 GLU A CA 1 ATOM 2526 C C . GLU A 1 317 ? 29.175 28.043 12.272 1.00 9.46 ? 403 GLU A C 1 ATOM 2527 O O . GLU A 1 317 ? 28.636 26.938 12.129 1.00 10.72 ? 403 GLU A O 1 ATOM 2528 C CB . GLU A 1 317 ? 27.233 29.610 12.629 1.00 8.88 ? 403 GLU A CB 1 ATOM 2529 C CG . GLU A 1 317 ? 26.647 30.988 12.293 1.00 10.59 ? 403 GLU A CG 1 ATOM 2530 C CD . GLU A 1 317 ? 25.349 31.346 12.965 1.00 10.67 ? 403 GLU A CD 1 ATOM 2531 O OE1 . GLU A 1 317 ? 24.905 30.595 13.861 1.00 11.83 ? 403 GLU A OE1 1 ATOM 2532 O OE2 . GLU A 1 317 ? 24.739 32.393 12.612 1.00 7.47 ? 403 GLU A OE2 1 ATOM 2533 N N . CYS A 1 318 ? 30.380 28.203 12.767 1.00 8.39 ? 404 CYS A N 1 ATOM 2534 C CA . CYS A 1 318 ? 31.248 27.059 13.095 1.00 8.48 ? 404 CYS A CA 1 ATOM 2535 C C . CYS A 1 318 ? 30.679 26.138 14.167 1.00 9.37 ? 404 CYS A C 1 ATOM 2536 O O . CYS A 1 318 ? 30.052 26.563 15.125 1.00 10.82 ? 404 CYS A O 1 ATOM 2537 C CB . CYS A 1 318 ? 32.608 27.602 13.510 1.00 7.75 ? 404 CYS A CB 1 ATOM 2538 S SG . CYS A 1 318 ? 33.877 26.323 13.553 1.00 9.16 ? 404 CYS A SG 1 ATOM 2539 N N . ASN A 1 319 ? 30.948 24.840 14.019 1.00 7.91 ? 405 ASN A N 1 ATOM 2540 C CA . ASN A 1 319 ? 30.532 23.852 15.009 1.00 9.09 ? 405 ASN A CA 1 ATOM 2541 C C . ASN A 1 319 ? 31.567 23.657 16.130 1.00 8.91 ? 405 ASN A C 1 ATOM 2542 O O . ASN A 1 319 ? 31.253 23.056 17.159 1.00 8.72 ? 405 ASN A O 1 ATOM 2543 C CB . ASN A 1 319 ? 30.292 22.475 14.399 1.00 8.55 ? 405 ASN A CB 1 ATOM 2544 C CG . ASN A 1 319 ? 29.197 22.466 13.366 1.00 11.75 ? 405 ASN A CG 1 ATOM 2545 O OD1 . ASN A 1 319 ? 29.336 21.859 12.313 1.00 7.47 ? 405 ASN A OD1 1 ATOM 2546 N ND2 . ASN A 1 319 ? 28.081 23.097 13.682 1.00 14.17 ? 405 ASN A ND2 1 ATOM 2547 N N . GLY A 1 320 ? 32.779 24.133 15.905 1.00 8.16 ? 406 GLY A N 1 ATOM 2548 C CA . GLY A 1 320 ? 33.817 23.991 16.901 1.00 9.65 ? 406 GLY A CA 1 ATOM 2549 C C . GLY A 1 320 ? 35.200 24.186 16.329 1.00 8.99 ? 406 GLY A C 1 ATOM 2550 O O . GLY A 1 320 ? 35.441 23.984 15.137 1.00 9.05 ? 406 GLY A O 1 ATOM 2551 N N . THR A 1 321 ? 36.121 24.622 17.187 1.00 9.21 ? 407 THR A N 1 ATOM 2552 C CA . THR A 1 321 ? 37.462 24.924 16.752 1.00 9.87 ? 407 THR A CA 1 ATOM 2553 C C . THR A 1 321 ? 38.271 23.655 16.437 1.00 10.03 ? 407 THR A C 1 ATOM 2554 O O . THR A 1 321 ? 38.055 22.601 17.017 1.00 9.62 ? 407 THR A O 1 ATOM 2555 C CB . THR A 1 321 ? 38.211 25.781 17.801 1.00 9.79 ? 407 THR A CB 1 ATOM 2556 O OG1 . THR A 1 321 ? 39.506 26.118 17.300 1.00 11.48 ? 407 THR A OG1 1 ATOM 2557 C CG2 . THR A 1 321 ? 38.439 25.015 19.107 1.00 10.28 ? 407 THR A CG2 1 ATOM 2558 N N . SER A 1 322 ? 39.166 23.786 15.488 1.00 10.59 ? 408 SER A N 1 ATOM 2559 C CA . SER A 1 322 ? 40.101 22.701 15.120 1.00 10.71 ? 408 SER A CA 1 ATOM 2560 C C . SER A 1 322 ? 41.464 22.867 15.839 1.00 11.74 ? 408 SER A C 1 ATOM 2561 O O . SER A 1 322 ? 42.380 22.050 15.690 1.00 10.81 ? 408 SER A O 1 ATOM 2562 C CB . SER A 1 322 ? 40.308 22.633 13.610 1.00 11.83 ? 408 SER A CB 1 ATOM 2563 O OG . SER A 1 322 ? 40.900 23.810 13.122 1.00 12.45 ? 408 SER A OG 1 ATOM 2564 N N . ASP A 1 323 ? 41.551 23.899 16.663 1.00 11.68 ? 409 ASP A N 1 ATOM 2565 C CA . ASP A 1 323 ? 42.780 24.159 17.438 1.00 12.98 ? 409 ASP A CA 1 ATOM 2566 C C . ASP A 1 323 ? 42.794 23.210 18.637 1.00 12.31 ? 409 ASP A C 1 ATOM 2567 O O . ASP A 1 323 ? 42.032 23.392 19.580 1.00 10.65 ? 409 ASP A O 1 ATOM 2568 C CB . ASP A 1 323 ? 42.810 25.604 17.877 1.00 13.01 ? 409 ASP A CB 1 ATOM 2569 C CG . ASP A 1 323 ? 43.996 25.953 18.787 1.00 16.73 ? 409 ASP A CG 1 ATOM 2570 O OD1 . ASP A 1 323 ? 44.854 25.093 19.068 1.00 15.55 ? 409 ASP A OD1 1 ATOM 2571 O OD2 . ASP A 1 323 ? 44.076 27.114 19.255 1.00 18.04 ? 409 ASP A OD2 1 ATOM 2572 N N . THR A 1 324 ? 43.675 22.215 18.560 1.00 12.57 ? 410 THR A N 1 ATOM 2573 C CA . THR A 1 324 ? 43.759 21.159 19.566 1.00 13.24 ? 410 THR A CA 1 ATOM 2574 C C . THR A 1 324 ? 44.164 21.619 20.949 1.00 13.12 ? 410 THR A C 1 ATOM 2575 O O . THR A 1 324 ? 44.003 20.846 21.888 1.00 14.12 ? 410 THR A O 1 ATOM 2576 C CB . THR A 1 324 ? 44.748 20.050 19.183 1.00 13.85 ? 410 THR A CB 1 ATOM 2577 O OG1 . THR A 1 324 ? 46.076 20.592 19.114 1.00 15.58 ? 410 THR A OG1 1 ATOM 2578 C CG2 . THR A 1 324 ? 44.426 19.427 17.847 1.00 14.40 ? 410 THR A CG2 1 ATOM 2579 N N . THR A 1 325 ? 44.675 22.849 21.060 1.00 12.43 ? 411 THR A N 1 ATOM 2580 C CA . THR A 1 325 ? 45.106 23.415 22.326 1.00 14.15 ? 411 THR A CA 1 ATOM 2581 C C . THR A 1 325 ? 44.053 24.276 22.982 1.00 14.56 ? 411 THR A C 1 ATOM 2582 O O . THR A 1 325 ? 44.239 24.768 24.092 1.00 14.70 ? 411 THR A O 1 ATOM 2583 C CB . THR A 1 325 ? 46.414 24.231 22.164 1.00 15.45 ? 411 THR A CB 1 ATOM 2584 O OG1 . THR A 1 325 ? 46.178 25.500 21.538 1.00 18.09 ? 411 THR A OG1 1 ATOM 2585 C CG2 . THR A 1 325 ? 47.403 23.526 21.315 1.00 17.49 ? 411 THR A CG2 1 ATOM 2586 N N . ALA A 1 326 ? 42.963 24.508 22.273 1.00 13.90 ? 412 ALA A N 1 ATOM 2587 C CA . ALA A 1 326 ? 41.920 25.413 22.757 1.00 13.15 ? 412 ALA A CA 1 ATOM 2588 C C . ALA A 1 326 ? 41.229 24.799 23.979 1.00 13.59 ? 412 ALA A C 1 ATOM 2589 O O . ALA A 1 326 ? 41.114 23.564 24.109 1.00 13.25 ? 412 ALA A O 1 ATOM 2590 C CB . ALA A 1 326 ? 40.917 25.715 21.671 1.00 13.56 ? 412 ALA A CB 1 ATOM 2591 N N . ALA A 1 327 ? 40.763 25.674 24.873 1.00 13.78 ? 413 ALA A N 1 ATOM 2592 C CA . ALA A 1 327 ? 40.145 25.213 26.122 1.00 15.21 ? 413 ALA A CA 1 ATOM 2593 C C . ALA A 1 327 ? 39.012 24.209 25.918 1.00 15.64 ? 413 ALA A C 1 ATOM 2594 O O . ALA A 1 327 ? 38.885 23.251 26.687 1.00 16.99 ? 413 ALA A O 1 ATOM 2595 C CB . ALA A 1 327 ? 39.610 26.380 26.916 1.00 16.33 ? 413 ALA A CB 1 ATOM 2596 N N . ARG A 1 328 ? 38.154 24.487 24.950 1.00 13.79 ? 414 ARG A N 1 ATOM 2597 C CA . ARG A 1 328 ? 36.957 23.660 24.749 1.00 12.96 ? 414 ARG A CA 1 ATOM 2598 C C . ARG A 1 328 ? 37.011 22.886 23.432 1.00 11.26 ? 414 ARG A C 1 ATOM 2599 O O . ARG A 1 328 ? 36.010 22.701 22.744 1.00 9.59 ? 414 ARG A O 1 ATOM 2600 C CB . ARG A 1 328 ? 35.682 24.500 24.890 1.00 14.28 ? 414 ARG A CB 1 ATOM 2601 C CG . ARG A 1 328 ? 35.534 25.051 26.318 1.00 15.71 ? 414 ARG A CG 1 ATOM 2602 C CD . ARG A 1 328 ? 34.302 25.821 26.582 1.00 19.70 ? 414 ARG A CD 1 ATOM 2603 N NE . ARG A 1 328 ? 34.322 26.288 27.972 1.00 22.53 ? 414 ARG A NE 1 ATOM 2604 C CZ . ARG A 1 328 ? 34.827 27.470 28.372 1.00 24.42 ? 414 ARG A CZ 1 ATOM 2605 N NH1 . ARG A 1 328 ? 35.346 28.345 27.494 1.00 19.71 ? 414 ARG A NH1 1 ATOM 2606 N NH2 . ARG A 1 328 ? 34.800 27.769 29.662 1.00 25.73 ? 414 ARG A NH2 1 ATOM 2607 N N . TYR A 1 329 ? 38.212 22.448 23.097 1.00 9.57 ? 415 TYR A N 1 ATOM 2608 C CA . TYR A 1 329 ? 38.450 21.689 21.879 1.00 9.71 ? 415 TYR A CA 1 ATOM 2609 C C . TYR A 1 329 ? 37.740 20.352 21.958 1.00 8.78 ? 415 TYR A C 1 ATOM 2610 O O . TYR A 1 329 ? 37.838 19.619 22.945 1.00 8.69 ? 415 TYR A O 1 ATOM 2611 C CB . TYR A 1 329 ? 39.940 21.429 21.691 1.00 9.39 ? 415 TYR A CB 1 ATOM 2612 C CG . TYR A 1 329 ? 40.268 20.454 20.579 1.00 9.50 ? 415 TYR A CG 1 ATOM 2613 C CD1 . TYR A 1 329 ? 40.049 20.803 19.248 1.00 7.94 ? 415 TYR A CD1 1 ATOM 2614 C CD2 . TYR A 1 329 ? 40.813 19.196 20.836 1.00 7.74 ? 415 TYR A CD2 1 ATOM 2615 C CE1 . TYR A 1 329 ? 40.317 19.939 18.227 1.00 8.30 ? 415 TYR A CE1 1 ATOM 2616 C CE2 . TYR A 1 329 ? 41.075 18.338 19.830 1.00 9.21 ? 415 TYR A CE2 1 ATOM 2617 C CZ . TYR A 1 329 ? 40.855 18.696 18.515 1.00 9.72 ? 415 TYR A CZ 1 ATOM 2618 O OH . TYR A 1 329 ? 41.150 17.804 17.496 1.00 10.41 ? 415 TYR A OH 1 ATOM 2619 N N . ASP A 1 330 ? 37.040 20.024 20.893 1.00 7.81 ? 416 ASP A N 1 ATOM 2620 C CA . ASP A 1 330 ? 36.331 18.751 20.760 1.00 7.94 ? 416 ASP A CA 1 ATOM 2621 C C . ASP A 1 330 ? 37.022 18.007 19.635 1.00 7.40 ? 416 ASP A C 1 ATOM 2622 O O . ASP A 1 330 ? 37.087 18.526 18.522 1.00 7.08 ? 416 ASP A O 1 ATOM 2623 C CB . ASP A 1 330 ? 34.869 18.987 20.445 1.00 7.65 ? 416 ASP A CB 1 ATOM 2624 C CG . ASP A 1 330 ? 34.029 17.736 20.468 1.00 8.23 ? 416 ASP A CG 1 ATOM 2625 O OD1 . ASP A 1 330 ? 34.376 16.721 19.783 1.00 8.00 ? 416 ASP A OD1 1 ATOM 2626 O OD2 . ASP A 1 330 ? 32.930 17.716 21.099 1.00 6.69 ? 416 ASP A OD2 1 ATOM 2627 N N . TYR A 1 331 ? 37.570 16.810 19.920 1.00 7.37 ? 417 TYR A N 1 ATOM 2628 C CA . TYR A 1 331 ? 38.318 16.015 18.940 1.00 7.86 ? 417 TYR A CA 1 ATOM 2629 C C . TYR A 1 331 ? 37.546 15.724 17.633 1.00 7.56 ? 417 TYR A C 1 ATOM 2630 O O . TYR A 1 331 ? 38.157 15.475 16.580 1.00 7.19 ? 417 TYR A O 1 ATOM 2631 C CB . TYR A 1 331 ? 38.820 14.686 19.518 1.00 7.65 ? 417 TYR A CB 1 ATOM 2632 C CG . TYR A 1 331 ? 37.742 13.661 19.717 1.00 7.60 ? 417 TYR A CG 1 ATOM 2633 C CD1 . TYR A 1 331 ? 37.022 13.581 20.899 1.00 8.36 ? 417 TYR A CD1 1 ATOM 2634 C CD2 . TYR A 1 331 ? 37.432 12.764 18.690 1.00 8.26 ? 417 TYR A CD2 1 ATOM 2635 C CE1 . TYR A 1 331 ? 36.007 12.624 21.049 1.00 10.72 ? 417 TYR A CE1 1 ATOM 2636 C CE2 . TYR A 1 331 ? 36.449 11.826 18.827 1.00 7.37 ? 417 TYR A CE2 1 ATOM 2637 C CZ . TYR A 1 331 ? 35.741 11.747 20.028 1.00 10.48 ? 417 TYR A CZ 1 ATOM 2638 O OH . TYR A 1 331 ? 34.759 10.792 20.165 1.00 12.09 ? 417 TYR A OH 1 ATOM 2639 N N . HIS A 1 332 ? 36.227 15.787 17.678 1.00 8.27 ? 418 HIS A N 1 ATOM 2640 C CA . HIS A 1 332 ? 35.451 15.557 16.448 1.00 7.17 ? 418 HIS A CA 1 ATOM 2641 C C . HIS A 1 332 ? 35.798 16.641 15.401 1.00 8.04 ? 418 HIS A C 1 ATOM 2642 O O . HIS A 1 332 ? 35.741 16.415 14.207 1.00 8.45 ? 418 HIS A O 1 ATOM 2643 C CB . HIS A 1 332 ? 33.965 15.591 16.739 1.00 8.65 ? 418 HIS A CB 1 ATOM 2644 C CG . HIS A 1 332 ? 33.475 14.393 17.488 1.00 7.92 ? 418 HIS A CG 1 ATOM 2645 N ND1 . HIS A 1 332 ? 33.366 14.376 18.866 1.00 8.47 ? 418 HIS A ND1 1 ATOM 2646 C CD2 . HIS A 1 332 ? 33.011 13.192 17.051 1.00 10.10 ? 418 HIS A CD2 1 ATOM 2647 C CE1 . HIS A 1 332 ? 32.870 13.203 19.229 1.00 10.66 ? 418 HIS A CE1 1 ATOM 2648 N NE2 . HIS A 1 332 ? 32.682 12.456 18.156 1.00 11.40 ? 418 HIS A NE2 1 ATOM 2649 N N . CYS A 1 333 ? 36.168 17.812 15.890 1.00 7.31 ? 419 CYS A N 1 ATOM 2650 C CA . CYS A 1 333 ? 36.502 18.952 15.050 1.00 7.53 ? 419 CYS A CA 1 ATOM 2651 C C . CYS A 1 333 ? 37.915 18.872 14.471 1.00 7.10 ? 419 CYS A C 1 ATOM 2652 O O . CYS A 1 333 ? 38.305 19.714 13.669 1.00 8.78 ? 419 CYS A O 1 ATOM 2653 C CB . CYS A 1 333 ? 36.278 20.263 15.829 1.00 7.95 ? 419 CYS A CB 1 ATOM 2654 S SG . CYS A 1 333 ? 34.557 20.411 16.324 1.00 9.40 ? 419 CYS A SG 1 ATOM 2655 N N . GLY A 1 334 ? 38.660 17.866 14.881 1.00 8.36 ? 420 GLY A N 1 ATOM 2656 C CA . GLY A 1 334 ? 40.017 17.654 14.417 1.00 7.82 ? 420 GLY A CA 1 ATOM 2657 C C . GLY A 1 334 ? 40.116 16.477 13.475 1.00 7.88 ? 420 GLY A C 1 ATOM 2658 O O . GLY A 1 334 ? 41.232 16.139 13.043 1.00 8.23 ? 420 GLY A O 1 ATOM 2659 N N . LEU A 1 335 ? 38.994 15.835 13.177 1.00 8.10 ? 421 LEU A N 1 ATOM 2660 C CA . LEU A 1 335 ? 38.976 14.656 12.303 1.00 7.48 ? 421 LEU A CA 1 ATOM 2661 C C . LEU A 1 335 ? 39.290 15.001 10.833 1.00 8.57 ? 421 LEU A C 1 ATOM 2662 O O . LEU A 1 335 ? 39.180 16.148 10.404 1.00 8.35 ? 421 LEU A O 1 ATOM 2663 C CB . LEU A 1 335 ? 37.666 13.896 12.434 1.00 7.87 ? 421 LEU A CB 1 ATOM 2664 C CG . LEU A 1 335 ? 37.356 13.399 13.857 1.00 7.37 ? 421 LEU A CG 1 ATOM 2665 C CD1 . LEU A 1 335 ? 35.967 12.721 13.846 1.00 8.14 ? 421 LEU A CD1 1 ATOM 2666 C CD2 . LEU A 1 335 ? 38.432 12.452 14.380 1.00 9.84 ? 421 LEU A CD2 1 ATOM 2667 N N . GLU A 1 336 ? 39.636 13.961 10.070 1.00 9.06 ? 422 GLU A N 1 ATOM 2668 C CA . GLU A 1 336 ? 40.073 14.125 8.671 1.00 11.11 ? 422 GLU A CA 1 ATOM 2669 C C . GLU A 1 336 ? 38.978 14.717 7.792 1.00 9.98 ? 422 GLU A C 1 ATOM 2670 O O . GLU A 1 336 ? 39.279 15.351 6.795 1.00 11.54 ? 422 GLU A O 1 ATOM 2671 C CB . GLU A 1 336 ? 40.586 12.809 8.081 1.00 12.49 ? 422 GLU A CB 1 ATOM 2672 C CG . GLU A 1 336 ? 39.485 11.739 8.041 1.00 17.75 ? 422 GLU A CG 1 ATOM 2673 C CD . GLU A 1 336 ? 39.914 10.402 7.472 1.00 25.17 ? 422 GLU A CD 1 ATOM 2674 O OE1 . GLU A 1 336 ? 40.864 10.390 6.667 1.00 26.43 ? 422 GLU A OE1 1 ATOM 2675 O OE2 . GLU A 1 336 ? 39.256 9.362 7.819 1.00 26.96 ? 422 GLU A OE2 1 ATOM 2676 N N . ASP A 1 337 ? 37.722 14.494 8.156 1.00 7.98 ? 423 ASP A N 1 ATOM 2677 C CA . ASP A 1 337 ? 36.575 15.009 7.392 1.00 7.09 ? 423 ASP A CA 1 ATOM 2678 C C . ASP A 1 337 ? 35.971 16.271 7.975 1.00 8.57 ? 423 ASP A C 1 ATOM 2679 O O . ASP A 1 337 ? 34.870 16.628 7.608 1.00 8.49 ? 423 ASP A O 1 ATOM 2680 C CB . ASP A 1 337 ? 35.516 13.901 7.222 1.00 7.89 ? 423 ASP A CB 1 ATOM 2681 C CG . ASP A 1 337 ? 35.053 13.338 8.526 1.00 7.91 ? 423 ASP A CG 1 ATOM 2682 O OD1 . ASP A 1 337 ? 35.311 13.945 9.599 1.00 9.18 ? 423 ASP A OD1 1 ATOM 2683 O OD2 . ASP A 1 337 ? 34.339 12.321 8.519 1.00 7.99 ? 423 ASP A OD2 1 ATOM 2684 N N . ALA A 1 338 ? 36.691 16.927 8.881 1.00 7.75 ? 424 ALA A N 1 ATOM 2685 C CA . ALA A 1 338 ? 36.287 18.197 9.467 1.00 7.19 ? 424 ALA A CA 1 ATOM 2686 C C . ALA A 1 338 ? 37.104 19.306 8.798 1.00 8.76 ? 424 ALA A C 1 ATOM 2687 O O . ALA A 1 338 ? 38.325 19.203 8.673 1.00 11.16 ? 424 ALA A O 1 ATOM 2688 C CB . ALA A 1 338 ? 36.481 18.200 11.020 1.00 7.18 ? 424 ALA A CB 1 ATOM 2689 N N . LEU A 1 339 ? 36.441 20.327 8.298 1.00 7.36 ? 425 LEU A N 1 ATOM 2690 C CA . LEU A 1 339 ? 37.169 21.369 7.584 1.00 8.28 ? 425 LEU A CA 1 ATOM 2691 C C . LEU A 1 339 ? 38.018 22.205 8.552 1.00 8.19 ? 425 LEU A C 1 ATOM 2692 O O . LEU A 1 339 ? 37.604 22.561 9.630 1.00 8.61 ? 425 LEU A O 1 ATOM 2693 C CB . LEU A 1 339 ? 36.214 22.313 6.852 1.00 7.42 ? 425 LEU A CB 1 ATOM 2694 C CG . LEU A 1 339 ? 36.848 23.271 5.824 1.00 8.32 ? 425 LEU A CG 1 ATOM 2695 C CD1 . LEU A 1 339 ? 37.500 22.513 4.681 1.00 11.58 ? 425 LEU A CD1 1 ATOM 2696 C CD2 . LEU A 1 339 ? 35.770 24.203 5.266 1.00 9.73 ? 425 LEU A CD2 1 ATOM 2697 N N . LYS A 1 340 ? 39.228 22.524 8.110 1.00 9.80 ? 426 LYS A N 1 ATOM 2698 C CA . LYS A 1 340 ? 40.215 23.233 8.953 1.00 12.00 ? 426 LYS A CA 1 ATOM 2699 C C . LYS A 1 340 ? 40.969 24.245 8.140 1.00 13.14 ? 426 LYS A C 1 ATOM 2700 O O . LYS A 1 340 ? 41.106 24.070 6.916 1.00 13.99 ? 426 LYS A O 1 ATOM 2701 C CB . LYS A 1 340 ? 41.270 22.240 9.468 1.00 13.09 ? 426 LYS A CB 1 ATOM 2702 C CG . LYS A 1 340 ? 40.730 21.158 10.294 1.00 15.82 ? 426 LYS A CG 1 ATOM 2703 C CD . LYS A 1 340 ? 41.835 20.174 10.681 1.00 18.50 ? 426 LYS A CD 1 ATOM 2704 C CE . LYS A 1 340 ? 41.197 18.864 10.949 1.00 18.53 ? 426 LYS A CE 1 ATOM 2705 N NZ . LYS A 1 340 ? 40.889 18.148 9.681 1.00 21.11 ? 426 LYS A NZ 1 ATOM 2706 N N . PRO A 1 341 ? 41.498 25.285 8.765 1.00 14.39 ? 427 PRO A N 1 ATOM 2707 C CA . PRO A 1 341 ? 41.359 25.538 10.186 1.00 13.78 ? 427 PRO A CA 1 ATOM 2708 C C . PRO A 1 341 ? 40.005 26.129 10.473 1.00 13.30 ? 427 PRO A C 1 ATOM 2709 O O . PRO A 1 341 ? 39.494 26.966 9.707 1.00 16.37 ? 427 PRO A O 1 ATOM 2710 C CB . PRO A 1 341 ? 42.438 26.579 10.458 1.00 14.94 ? 427 PRO A CB 1 ATOM 2711 C CG . PRO A 1 341 ? 42.521 27.358 9.155 1.00 15.39 ? 427 PRO A CG 1 ATOM 2712 C CD . PRO A 1 341 ? 42.256 26.356 8.082 1.00 14.71 ? 427 PRO A CD 1 ATOM 2713 N N . ALA A 1 342 ? 39.431 25.741 11.596 1.00 10.71 ? 428 ALA A N 1 ATOM 2714 C CA . ALA A 1 342 ? 38.135 26.209 12.049 1.00 9.59 ? 428 ALA A CA 1 ATOM 2715 C C . ALA A 1 342 ? 38.236 27.056 13.321 1.00 11.08 ? 428 ALA A C 1 ATOM 2716 O O . ALA A 1 342 ? 38.982 26.676 14.251 1.00 10.71 ? 428 ALA A O 1 ATOM 2717 C CB . ALA A 1 342 ? 37.249 25.005 12.299 1.00 8.84 ? 428 ALA A CB 1 ATOM 2718 N N . PRO A 1 343 ? 37.469 28.138 13.411 1.00 11.81 ? 429 PRO A N 1 ATOM 2719 C CA . PRO A 1 343 ? 37.480 28.997 14.583 1.00 13.44 ? 429 PRO A CA 1 ATOM 2720 C C . PRO A 1 343 ? 36.571 28.436 15.688 1.00 14.65 ? 429 PRO A C 1 ATOM 2721 O O . PRO A 1 343 ? 35.973 27.370 15.536 1.00 14.41 ? 429 PRO A O 1 ATOM 2722 C CB . PRO A 1 343 ? 36.939 30.310 13.987 1.00 14.34 ? 429 PRO A CB 1 ATOM 2723 C CG . PRO A 1 343 ? 35.859 29.818 13.059 1.00 12.91 ? 429 PRO A CG 1 ATOM 2724 C CD . PRO A 1 343 ? 36.477 28.601 12.428 1.00 11.41 ? 429 PRO A CD 1 ATOM 2725 N N . GLU A 1 344 ? 36.422 29.151 16.799 1.00 15.34 ? 430 GLU A N 1 ATOM 2726 C CA . GLU A 1 344 ? 35.557 28.685 17.892 1.00 15.40 ? 430 GLU A CA 1 ATOM 2727 C C . GLU A 1 344 ? 34.082 28.521 17.501 1.00 15.18 ? 430 GLU A C 1 ATOM 2728 O O . GLU A 1 344 ? 33.563 29.161 16.584 1.00 14.10 ? 430 GLU A O 1 ATOM 2729 C CB . GLU A 1 344 ? 35.658 29.568 19.153 1.00 17.08 ? 430 GLU A CB 1 ATOM 2730 C CG . GLU A 1 344 ? 37.068 29.671 19.699 1.00 20.96 ? 430 GLU A CG 1 ATOM 2731 C CD . GLU A 1 344 ? 37.501 28.531 20.619 1.00 27.78 ? 430 GLU A CD 1 ATOM 2732 O OE1 . GLU A 1 344 ? 36.641 27.742 21.102 1.00 29.70 ? 430 GLU A OE1 1 ATOM 2733 O OE2 . GLU A 1 344 ? 38.737 28.436 20.876 1.00 32.34 ? 430 GLU A OE2 1 ATOM 2734 N N . ALA A 1 345 ? 33.430 27.630 18.210 1.00 13.39 ? 431 ALA A N 1 ATOM 2735 C CA . ALA A 1 345 ? 32.032 27.318 17.988 1.00 13.27 ? 431 ALA A CA 1 ATOM 2736 C C . ALA A 1 345 ? 31.243 28.639 17.970 1.00 14.87 ? 431 ALA A C 1 ATOM 2737 O O . ALA A 1 345 ? 31.470 29.525 18.819 1.00 14.02 ? 431 ALA A O 1 ATOM 2738 C CB . ALA A 1 345 ? 31.503 26.383 19.020 1.00 14.81 ? 431 ALA A CB 1 ATOM 2739 N N . GLY A 1 346 ? 30.373 28.779 16.979 1.00 15.21 ? 432 GLY A N 1 ATOM 2740 C CA . GLY A 1 346 ? 29.524 29.958 16.857 1.00 16.24 ? 432 GLY A CA 1 ATOM 2741 C C . GLY A 1 346 ? 30.158 31.113 16.099 1.00 15.62 ? 432 GLY A C 1 ATOM 2742 O O . GLY A 1 346 ? 29.450 32.072 15.753 1.00 16.96 ? 432 GLY A O 1 ATOM 2743 N N . GLN A 1 347 ? 31.456 31.061 15.838 1.00 14.22 ? 433 GLN A N 1 ATOM 2744 C CA . GLN A 1 347 ? 32.091 32.127 15.093 1.00 13.39 ? 433 GLN A CA 1 ATOM 2745 C C . GLN A 1 347 ? 31.914 31.842 13.610 1.00 13.04 ? 433 GLN A C 1 ATOM 2746 O O . GLN A 1 347 ? 31.806 30.677 13.194 1.00 11.61 ? 433 GLN A O 1 ATOM 2747 C CB . GLN A 1 347 ? 33.555 32.281 15.416 1.00 14.32 ? 433 GLN A CB 1 ATOM 2748 C CG . GLN A 1 347 ? 33.749 32.705 16.873 1.00 13.19 ? 433 GLN A CG 1 ATOM 2749 C CD . GLN A 1 347 ? 35.221 32.948 17.227 1.00 15.77 ? 433 GLN A CD 1 ATOM 2750 O OE1 . GLN A 1 347 ? 36.051 33.095 16.340 1.00 17.91 ? 433 GLN A OE1 1 ATOM 2751 N NE2 . GLN A 1 347 ? 35.530 33.026 18.530 1.00 15.36 ? 433 GLN A NE2 1 ATOM 2752 N N . TRP A 1 348 ? 31.887 32.897 12.822 1.00 11.50 ? 434 TRP A N 1 ATOM 2753 C CA . TRP A 1 348 ? 31.790 32.731 11.367 1.00 10.97 ? 434 TRP A CA 1 ATOM 2754 C C . TRP A 1 348 ? 32.992 31.970 10.807 1.00 10.78 ? 434 TRP A C 1 ATOM 2755 O O . TRP A 1 348 ? 34.160 32.296 11.090 1.00 10.96 ? 434 TRP A O 1 ATOM 2756 C CB . TRP A 1 348 ? 31.641 34.097 10.671 1.00 10.17 ? 434 TRP A CB 1 ATOM 2757 C CG . TRP A 1 348 ? 31.221 33.977 9.242 1.00 8.64 ? 434 TRP A CG 1 ATOM 2758 C CD1 . TRP A 1 348 ? 31.984 34.149 8.123 1.00 8.69 ? 434 TRP A CD1 1 ATOM 2759 C CD2 . TRP A 1 348 ? 29.923 33.582 8.783 1.00 7.92 ? 434 TRP A CD2 1 ATOM 2760 N NE1 . TRP A 1 348 ? 31.239 33.888 6.986 1.00 9.76 ? 434 TRP A NE1 1 ATOM 2761 C CE2 . TRP A 1 348 ? 29.964 33.560 7.365 1.00 8.27 ? 434 TRP A CE2 1 ATOM 2762 C CE3 . TRP A 1 348 ? 28.738 33.229 9.434 1.00 10.22 ? 434 TRP A CE3 1 ATOM 2763 C CZ2 . TRP A 1 348 ? 28.856 33.217 6.592 1.00 9.73 ? 434 TRP A CZ2 1 ATOM 2764 C CZ3 . TRP A 1 348 ? 27.639 32.909 8.672 1.00 7.65 ? 434 TRP A CZ3 1 ATOM 2765 C CH2 . TRP A 1 348 ? 27.709 32.886 7.267 1.00 7.05 ? 434 TRP A CH2 1 ATOM 2766 N N . PHE A 1 349 ? 32.710 31.002 9.929 1.00 8.65 ? 435 PHE A N 1 ATOM 2767 C CA . PHE A 1 349 ? 33.717 30.167 9.314 1.00 9.07 ? 435 PHE A CA 1 ATOM 2768 C C . PHE A 1 349 ? 33.591 30.295 7.795 1.00 9.26 ? 435 PHE A C 1 ATOM 2769 O O . PHE A 1 349 ? 32.847 29.561 7.133 1.00 8.45 ? 435 PHE A O 1 ATOM 2770 C CB . PHE A 1 349 ? 33.480 28.717 9.783 1.00 9.05 ? 435 PHE A CB 1 ATOM 2771 C CG . PHE A 1 349 ? 34.521 27.717 9.376 1.00 7.18 ? 435 PHE A CG 1 ATOM 2772 C CD1 . PHE A 1 349 ? 35.639 28.006 8.595 1.00 9.64 ? 435 PHE A CD1 1 ATOM 2773 C CD2 . PHE A 1 349 ? 34.353 26.401 9.810 1.00 9.79 ? 435 PHE A CD2 1 ATOM 2774 C CE1 . PHE A 1 349 ? 36.564 26.997 8.270 1.00 10.51 ? 435 PHE A CE1 1 ATOM 2775 C CE2 . PHE A 1 349 ? 35.248 25.418 9.501 1.00 7.64 ? 435 PHE A CE2 1 ATOM 2776 C CZ . PHE A 1 349 ? 36.366 25.693 8.710 1.00 10.73 ? 435 PHE A CZ 1 ATOM 2777 N N . ASN A 1 350 ? 34.276 31.272 7.230 1.00 8.99 ? 436 ASN A N 1 ATOM 2778 C CA . ASN A 1 350 ? 34.001 31.608 5.834 1.00 9.33 ? 436 ASN A CA 1 ATOM 2779 C C . ASN A 1 350 ? 34.268 30.518 4.795 1.00 9.34 ? 436 ASN A C 1 ATOM 2780 O O . ASN A 1 350 ? 33.494 30.348 3.863 1.00 9.80 ? 436 ASN A O 1 ATOM 2781 C CB . ASN A 1 350 ? 34.662 32.905 5.400 1.00 9.94 ? 436 ASN A CB 1 ATOM 2782 C CG . ASN A 1 350 ? 33.896 33.540 4.262 1.00 12.40 ? 436 ASN A CG 1 ATOM 2783 O OD1 . ASN A 1 350 ? 32.683 33.803 4.399 1.00 12.21 ? 436 ASN A OD1 1 ATOM 2784 N ND2 . ASN A 1 350 ? 34.573 33.793 3.136 1.00 17.12 ? 436 ASN A ND2 1 ATOM 2785 N N . GLU A 1 351 ? 35.337 29.741 4.974 1.00 8.07 ? 437 GLU A N 1 ATOM 2786 C CA . GLU A 1 351 ? 35.649 28.688 4.052 1.00 9.03 ? 437 GLU A CA 1 ATOM 2787 C C . GLU A 1 351 ? 34.550 27.649 4.052 1.00 8.01 ? 437 GLU A C 1 ATOM 2788 O O . GLU A 1 351 ? 34.290 27.028 3.007 1.00 8.27 ? 437 GLU A O 1 ATOM 2789 C CB . GLU A 1 351 ? 37.015 28.056 4.315 1.00 9.39 ? 437 GLU A CB 1 ATOM 2790 C CG . GLU A 1 351 ? 38.164 29.030 4.083 1.00 16.41 ? 437 GLU A CG 1 ATOM 2791 C CD . GLU A 1 351 ? 38.298 29.473 2.629 1.00 25.58 ? 437 GLU A CD 1 ATOM 2792 O OE1 . GLU A 1 351 ? 38.097 28.653 1.719 1.00 29.64 ? 437 GLU A OE1 1 ATOM 2793 O OE2 . GLU A 1 351 ? 38.618 30.653 2.391 1.00 32.65 ? 437 GLU A OE2 1 ATOM 2794 N N . TYR A 1 352 ? 33.952 27.450 5.219 1.00 7.15 ? 438 TYR A N 1 ATOM 2795 C CA . TYR A 1 352 ? 32.820 26.506 5.341 1.00 7.20 ? 438 TYR A CA 1 ATOM 2796 C C . TYR A 1 352 ? 31.578 27.064 4.610 1.00 8.46 ? 438 TYR A C 1 ATOM 2797 O O . TYR A 1 352 ? 30.878 26.369 3.897 1.00 7.54 ? 438 TYR A O 1 ATOM 2798 C CB . TYR A 1 352 ? 32.485 26.188 6.785 1.00 7.61 ? 438 TYR A CB 1 ATOM 2799 C CG . TYR A 1 352 ? 31.720 24.893 6.858 1.00 6.61 ? 438 TYR A CG 1 ATOM 2800 C CD1 . TYR A 1 352 ? 32.400 23.686 6.949 1.00 8.29 ? 438 TYR A CD1 1 ATOM 2801 C CD2 . TYR A 1 352 ? 30.347 24.862 6.812 1.00 5.88 ? 438 TYR A CD2 1 ATOM 2802 C CE1 . TYR A 1 352 ? 31.716 22.495 6.975 1.00 7.65 ? 438 TYR A CE1 1 ATOM 2803 C CE2 . TYR A 1 352 ? 29.662 23.688 6.810 1.00 6.55 ? 438 TYR A CE2 1 ATOM 2804 C CZ . TYR A 1 352 ? 30.345 22.496 6.920 1.00 4.94 ? 438 TYR A CZ 1 ATOM 2805 O OH . TYR A 1 352 ? 29.659 21.300 6.946 1.00 7.45 ? 438 TYR A OH 1 ATOM 2806 N N . PHE A 1 353 ? 31.329 28.344 4.770 1.00 7.59 ? 439 PHE A N 1 ATOM 2807 C CA . PHE A 1 353 ? 30.246 28.993 4.036 1.00 8.47 ? 439 PHE A CA 1 ATOM 2808 C C . PHE A 1 353 ? 30.425 28.837 2.543 1.00 8.93 ? 439 PHE A C 1 ATOM 2809 O O . PHE A 1 353 ? 29.469 28.527 1.842 1.00 8.65 ? 439 PHE A O 1 ATOM 2810 C CB . PHE A 1 353 ? 30.227 30.465 4.399 1.00 8.04 ? 439 PHE A CB 1 ATOM 2811 C CG . PHE A 1 353 ? 29.140 31.279 3.732 1.00 6.68 ? 439 PHE A CG 1 ATOM 2812 C CD1 . PHE A 1 353 ? 27.800 31.116 4.060 1.00 5.05 ? 439 PHE A CD1 1 ATOM 2813 C CD2 . PHE A 1 353 ? 29.488 32.234 2.779 1.00 9.29 ? 439 PHE A CD2 1 ATOM 2814 C CE1 . PHE A 1 353 ? 26.821 31.928 3.513 1.00 7.78 ? 439 PHE A CE1 1 ATOM 2815 C CE2 . PHE A 1 353 ? 28.531 33.022 2.199 1.00 10.25 ? 439 PHE A CE2 1 ATOM 2816 C CZ . PHE A 1 353 ? 27.185 32.873 2.545 1.00 9.03 ? 439 PHE A CZ 1 ATOM 2817 N N . ILE A 1 354 ? 31.647 29.057 2.043 1.00 9.24 ? 440 ILE A N 1 ATOM 2818 C CA . ILE A 1 354 ? 31.867 28.894 0.605 1.00 9.91 ? 440 ILE A CA 1 ATOM 2819 C C . ILE A 1 354 ? 31.617 27.450 0.161 1.00 9.63 ? 440 ILE A C 1 ATOM 2820 O O . ILE A 1 354 ? 31.012 27.201 -0.880 1.00 9.49 ? 440 ILE A O 1 ATOM 2821 C CB . ILE A 1 354 ? 33.269 29.384 0.221 1.00 11.66 ? 440 ILE A CB 1 ATOM 2822 C CG1 . ILE A 1 354 ? 33.373 30.870 0.572 1.00 12.22 ? 440 ILE A CG1 1 ATOM 2823 C CG2 . ILE A 1 354 ? 33.491 29.086 -1.255 1.00 12.98 ? 440 ILE A CG2 1 ATOM 2824 C CD1 . ILE A 1 354 ? 34.728 31.470 0.443 1.00 16.88 ? 440 ILE A CD1 1 ATOM 2825 N N . GLN A 1 355 ? 32.076 26.492 0.962 1.00 7.49 ? 441 GLN A N 1 ATOM 2826 C CA . GLN A 1 355 ? 31.845 25.076 0.672 1.00 7.40 ? 441 GLN A CA 1 ATOM 2827 C C . GLN A 1 355 ? 30.320 24.839 0.484 1.00 6.52 ? 441 GLN A C 1 ATOM 2828 O O . GLN A 1 355 ? 29.880 24.154 -0.432 1.00 7.17 ? 441 GLN A O 1 ATOM 2829 C CB . GLN A 1 355 ? 32.363 24.195 1.815 1.00 6.50 ? 441 GLN A CB 1 ATOM 2830 C CG . GLN A 1 355 ? 31.979 22.731 1.645 1.00 8.88 ? 441 GLN A CG 1 ATOM 2831 C CD . GLN A 1 355 ? 32.258 21.932 2.894 1.00 10.92 ? 441 GLN A CD 1 ATOM 2832 O OE1 . GLN A 1 355 ? 33.446 21.744 3.235 1.00 9.45 ? 441 GLN A OE1 1 ATOM 2833 N NE2 . GLN A 1 355 ? 31.190 21.395 3.543 1.00 6.30 ? 441 GLN A NE2 1 ATOM 2834 N N . LEU A 1 356 ? 29.548 25.358 1.430 1.00 6.38 ? 442 LEU A N 1 ATOM 2835 C CA . LEU A 1 356 ? 28.077 25.167 1.429 1.00 7.84 ? 442 LEU A CA 1 ATOM 2836 C C . LEU A 1 356 ? 27.439 25.786 0.196 1.00 8.61 ? 442 LEU A C 1 ATOM 2837 O O . LEU A 1 356 ? 26.552 25.223 -0.361 1.00 6.81 ? 442 LEU A O 1 ATOM 2838 C CB . LEU A 1 356 ? 27.420 25.727 2.679 1.00 7.32 ? 442 LEU A CB 1 ATOM 2839 C CG . LEU A 1 356 ? 27.707 24.999 3.993 1.00 5.49 ? 442 LEU A CG 1 ATOM 2840 C CD1 . LEU A 1 356 ? 27.199 25.829 5.155 1.00 7.48 ? 442 LEU A CD1 1 ATOM 2841 C CD2 . LEU A 1 356 ? 27.023 23.600 4.007 1.00 6.40 ? 442 LEU A CD2 1 ATOM 2842 N N . LEU A 1 357 ? 27.967 26.933 -0.219 1.00 9.25 ? 443 LEU A N 1 ATOM 2843 C CA . LEU A 1 357 ? 27.528 27.578 -1.445 1.00 11.18 ? 443 LEU A CA 1 ATOM 2844 C C . LEU A 1 357 ? 27.854 26.756 -2.692 1.00 10.59 ? 443 LEU A C 1 ATOM 2845 O O . LEU A 1 357 ? 27.007 26.575 -3.561 1.00 11.67 ? 443 LEU A O 1 ATOM 2846 C CB . LEU A 1 357 ? 28.207 28.947 -1.617 1.00 11.91 ? 443 LEU A CB 1 ATOM 2847 C CG . LEU A 1 357 ? 27.640 30.106 -0.843 1.00 15.52 ? 443 LEU A CG 1 ATOM 2848 C CD1 . LEU A 1 357 ? 28.444 31.351 -1.214 1.00 15.48 ? 443 LEU A CD1 1 ATOM 2849 C CD2 . LEU A 1 357 ? 26.159 30.316 -1.181 1.00 15.58 ? 443 LEU A CD2 1 ATOM 2850 N N . ARG A 1 358 ? 29.095 26.298 -2.807 1.00 10.72 ? 444 ARG A N 1 ATOM 2851 C CA . ARG A 1 358 ? 29.502 25.529 -3.985 1.00 10.16 ? 444 ARG A CA 1 ATOM 2852 C C . ARG A 1 358 ? 28.724 24.236 -4.164 1.00 9.57 ? 444 ARG A C 1 ATOM 2853 O O . ARG A 1 358 ? 28.481 23.805 -5.284 1.00 9.94 ? 444 ARG A O 1 ATOM 2854 C CB . ARG A 1 358 ? 30.966 25.137 -3.919 1.00 12.08 ? 444 ARG A CB 1 ATOM 2855 C CG . ARG A 1 358 ? 31.917 26.277 -4.028 1.00 15.95 ? 444 ARG A CG 1 ATOM 2856 C CD . ARG A 1 358 ? 33.353 25.684 -3.901 1.00 23.02 ? 444 ARG A CD 1 ATOM 2857 N NE . ARG A 1 358 ? 34.425 26.650 -4.063 1.00 25.71 ? 444 ARG A NE 1 ATOM 2858 C CZ . ARG A 1 358 ? 34.908 27.042 -5.221 1.00 29.66 ? 444 ARG A CZ 1 ATOM 2859 N NH1 . ARG A 1 358 ? 34.401 26.572 -6.367 1.00 30.15 ? 444 ARG A NH1 1 ATOM 2860 N NH2 . ARG A 1 358 ? 35.906 27.914 -5.234 1.00 30.18 ? 444 ARG A NH2 1 ATOM 2861 N N . ASN A 1 359 ? 28.365 23.619 -3.047 1.00 8.94 ? 445 ASN A N 1 ATOM 2862 C CA . ASN A 1 359 ? 27.637 22.364 -3.018 1.00 8.82 ? 445 ASN A CA 1 ATOM 2863 C C . ASN A 1 359 ? 26.121 22.526 -2.855 1.00 8.64 ? 445 ASN A C 1 ATOM 2864 O O . ASN A 1 359 ? 25.403 21.541 -2.705 1.00 10.05 ? 445 ASN A O 1 ATOM 2865 C CB . ASN A 1 359 ? 28.152 21.475 -1.875 1.00 9.34 ? 445 ASN A CB 1 ATOM 2866 C CG . ASN A 1 359 ? 29.533 20.910 -2.131 1.00 14.51 ? 445 ASN A CG 1 ATOM 2867 O OD1 . ASN A 1 359 ? 29.818 20.467 -3.259 1.00 20.02 ? 445 ASN A OD1 1 ATOM 2868 N ND2 . ASN A 1 359 ? 30.372 20.827 -1.071 1.00 11.58 ? 445 ASN A ND2 1 ATOM 2869 N N . ALA A 1 360 ? 25.638 23.756 -2.918 1.00 8.77 ? 446 ALA A N 1 ATOM 2870 C CA . ALA A 1 360 ? 24.225 24.012 -2.671 1.00 8.48 ? 446 ALA A CA 1 ATOM 2871 C C . ALA A 1 360 ? 23.329 23.253 -3.633 1.00 9.65 ? 446 ALA A C 1 ATOM 2872 O O . ALA A 1 360 ? 23.594 23.156 -4.840 1.00 8.55 ? 446 ALA A O 1 ATOM 2873 C CB . ALA A 1 360 ? 23.924 25.495 -2.685 1.00 10.01 ? 446 ALA A CB 1 ATOM 2874 N N . ASN A 1 361 ? 22.244 22.763 -3.093 1.00 7.94 ? 447 ASN A N 1 ATOM 2875 C CA . ASN A 1 361 ? 21.252 22.022 -3.882 1.00 10.68 ? 447 ASN A CA 1 ATOM 2876 C C . ASN A 1 361 ? 19.895 22.126 -3.235 1.00 10.19 ? 447 ASN A C 1 ATOM 2877 O O . ASN A 1 361 ? 19.658 21.547 -2.163 1.00 9.38 ? 447 ASN A O 1 ATOM 2878 C CB . ASN A 1 361 ? 21.685 20.578 -4.108 1.00 11.33 ? 447 ASN A CB 1 ATOM 2879 C CG . ASN A 1 361 ? 20.663 19.799 -4.858 1.00 16.42 ? 447 ASN A CG 1 ATOM 2880 O OD1 . ASN A 1 361 ? 20.018 20.331 -5.755 1.00 16.21 ? 447 ASN A OD1 1 ATOM 2881 N ND2 . ASN A 1 361 ? 20.463 18.544 -4.459 1.00 22.72 ? 447 ASN A ND2 1 ATOM 2882 N N . PRO A 1 362 ? 18.997 22.913 -3.833 1.00 11.33 ? 448 PRO A N 1 ATOM 2883 C CA . PRO A 1 362 ? 19.238 23.635 -5.085 1.00 10.98 ? 448 PRO A CA 1 ATOM 2884 C C . PRO A 1 362 ? 20.247 24.764 -5.015 1.00 10.93 ? 448 PRO A C 1 ATOM 2885 O O . PRO A 1 362 ? 20.440 25.358 -3.982 1.00 10.94 ? 448 PRO A O 1 ATOM 2886 C CB . PRO A 1 362 ? 17.881 24.295 -5.395 1.00 12.11 ? 448 PRO A CB 1 ATOM 2887 C CG . PRO A 1 362 ? 16.959 23.937 -4.350 1.00 14.84 ? 448 PRO A CG 1 ATOM 2888 C CD . PRO A 1 362 ? 17.620 23.106 -3.339 1.00 12.62 ? 448 PRO A CD 1 ATOM 2889 N N . PRO A 1 363 ? 20.898 25.036 -6.125 1.00 11.84 ? 449 PRO A N 1 ATOM 2890 C CA . PRO A 1 363 ? 21.935 26.063 -6.167 1.00 11.54 ? 449 PRO A CA 1 ATOM 2891 C C . PRO A 1 363 ? 21.381 27.448 -6.016 1.00 11.39 ? 449 PRO A C 1 ATOM 2892 O O . PRO A 1 363 ? 20.213 27.687 -6.268 1.00 10.97 ? 449 PRO A O 1 ATOM 2893 C CB . PRO A 1 363 ? 22.589 25.872 -7.552 1.00 13.26 ? 449 PRO A CB 1 ATOM 2894 C CG . PRO A 1 363 ? 21.698 25.012 -8.309 1.00 14.51 ? 449 PRO A CG 1 ATOM 2895 C CD . PRO A 1 363 ? 20.754 24.313 -7.405 1.00 13.27 ? 449 PRO A CD 1 ATOM 2896 N N . PHE A 1 364 ? 22.257 28.345 -5.602 1.00 12.90 ? 450 PHE A N 1 ATOM 2897 C CA . PHE A 1 364 ? 21.966 29.770 -5.477 1.00 14.73 ? 450 PHE A CA 1 ATOM 2898 C C . PHE A 1 364 ? 22.392 30.512 -6.725 1.00 18.33 ? 450 PHE A C 1 ATOM 2899 O O . PHE A 1 364 ? 23.193 29.992 -7.487 1.00 20.16 ? 450 PHE A O 1 ATOM 2900 C CB . PHE A 1 364 ? 22.630 30.376 -4.251 1.00 13.59 ? 450 PHE A CB 1 ATOM 2901 C CG . PHE A 1 364 ? 21.911 30.018 -2.996 1.00 10.89 ? 450 PHE A CG 1 ATOM 2902 C CD1 . PHE A 1 364 ? 20.800 30.746 -2.585 1.00 10.40 ? 450 PHE A CD1 1 ATOM 2903 C CD2 . PHE A 1 364 ? 22.264 28.892 -2.279 1.00 12.23 ? 450 PHE A CD2 1 ATOM 2904 C CE1 . PHE A 1 364 ? 20.072 30.385 -1.479 1.00 13.09 ? 450 PHE A CE1 1 ATOM 2905 C CE2 . PHE A 1 364 ? 21.558 28.526 -1.162 1.00 10.15 ? 450 PHE A CE2 1 ATOM 2906 C CZ . PHE A 1 364 ? 20.450 29.276 -0.756 1.00 13.14 ? 450 PHE A CZ 1 ATOM 2907 O OXT . PHE A 1 364 ? 21.867 31.611 -6.940 1.00 23.04 ? 450 PHE A OXT 1 HETATM 2908 C C1 . NAG B 2 . ? 20.653 36.123 32.204 1.00 6.16 ? 500 NAG A C1 1 HETATM 2909 C C2 . NAG B 2 . ? 21.380 36.410 33.499 1.00 6.66 ? 500 NAG A C2 1 HETATM 2910 C C3 . NAG B 2 . ? 20.513 37.266 34.379 1.00 6.89 ? 500 NAG A C3 1 HETATM 2911 C C4 . NAG B 2 . ? 19.990 38.477 33.623 1.00 7.44 ? 500 NAG A C4 1 HETATM 2912 C C5 . NAG B 2 . ? 19.390 38.043 32.291 1.00 6.58 ? 500 NAG A C5 1 HETATM 2913 C C6 . NAG B 2 . ? 18.849 39.164 31.458 1.00 6.39 ? 500 NAG A C6 1 HETATM 2914 C C7 . NAG B 2 . ? 22.838 34.871 34.803 1.00 8.36 ? 500 NAG A C7 1 HETATM 2915 C C8 . NAG B 2 . ? 22.899 33.558 35.519 1.00 8.20 ? 500 NAG A C8 1 HETATM 2916 N N2 . NAG B 2 . ? 21.686 35.153 34.189 1.00 7.47 ? 500 NAG A N2 1 HETATM 2917 O O3 . NAG B 2 . ? 21.284 37.728 35.482 1.00 10.83 ? 500 NAG A O3 1 HETATM 2918 O O4 . NAG B 2 . ? 18.998 39.132 34.414 1.00 8.01 ? 500 NAG A O4 1 HETATM 2919 O O5 . NAG B 2 . ? 20.287 37.299 31.509 1.00 7.94 ? 500 NAG A O5 1 HETATM 2920 O O6 . NAG B 2 . ? 18.082 38.687 30.375 1.00 8.98 ? 500 NAG A O6 1 HETATM 2921 O O7 . NAG B 2 . ? 23.801 35.630 34.805 1.00 9.00 ? 500 NAG A O7 1 HETATM 2922 C C1 . GOL C 3 . ? 0.246 18.406 17.264 1.00 29.52 ? 501 GOL A C1 1 HETATM 2923 O O1 . GOL C 3 . ? 0.941 17.993 16.105 1.00 28.45 ? 501 GOL A O1 1 HETATM 2924 C C2 . GOL C 3 . ? -0.068 17.246 18.186 1.00 27.88 ? 501 GOL A C2 1 HETATM 2925 O O2 . GOL C 3 . ? -0.845 17.754 19.251 1.00 30.48 ? 501 GOL A O2 1 HETATM 2926 C C3 . GOL C 3 . ? 1.198 16.607 18.752 1.00 25.36 ? 501 GOL A C3 1 HETATM 2927 O O3 . GOL C 3 . ? 0.842 15.664 19.736 1.00 25.50 ? 501 GOL A O3 1 HETATM 2928 C C1 . GOL D 3 . ? 16.910 15.259 -0.409 1.00 29.41 ? 502 GOL A C1 1 HETATM 2929 O O1 . GOL D 3 . ? 15.947 14.555 0.275 1.00 24.21 ? 502 GOL A O1 1 HETATM 2930 C C2 . GOL D 3 . ? 18.145 15.363 0.456 1.00 30.69 ? 502 GOL A C2 1 HETATM 2931 O O2 . GOL D 3 . ? 17.969 15.931 1.735 1.00 26.21 ? 502 GOL A O2 1 HETATM 2932 C C3 . GOL D 3 . ? 19.227 16.171 -0.262 1.00 29.74 ? 502 GOL A C3 1 HETATM 2933 O O3 . GOL D 3 . ? 18.891 16.553 -1.591 1.00 34.40 ? 502 GOL A O3 1 HETATM 2934 C C1 A GOL E 3 . ? 27.073 21.538 16.233 0.55 23.88 ? 503 GOL A C1 1 HETATM 2935 C C1 B GOL E 3 . ? 27.192 21.475 16.339 0.45 23.93 ? 503 GOL A C1 1 HETATM 2936 O O1 A GOL E 3 . ? 26.490 20.269 16.486 0.55 18.40 ? 503 GOL A O1 1 HETATM 2937 O O1 B GOL E 3 . ? 26.504 20.243 16.499 0.45 19.24 ? 503 GOL A O1 1 HETATM 2938 C C2 A GOL E 3 . ? 26.381 22.688 16.983 0.55 24.15 ? 503 GOL A C2 1 HETATM 2939 C C2 B GOL E 3 . ? 26.448 22.658 16.979 0.45 24.23 ? 503 GOL A C2 1 HETATM 2940 O O2 A GOL E 3 . ? 24.994 22.474 17.167 0.55 23.15 ? 503 GOL A O2 1 HETATM 2941 O O2 B GOL E 3 . ? 25.048 22.555 16.813 0.45 23.32 ? 503 GOL A O2 1 HETATM 2942 C C3 A GOL E 3 . ? 26.594 24.022 16.281 0.55 24.15 ? 503 GOL A C3 1 HETATM 2943 C C3 B GOL E 3 . ? 26.945 24.000 16.435 0.45 23.95 ? 503 GOL A C3 1 HETATM 2944 O O3 A GOL E 3 . ? 27.846 24.601 16.553 0.55 25.86 ? 503 GOL A O3 1 HETATM 2945 O O3 B GOL E 3 . ? 25.867 24.913 16.364 0.45 26.18 ? 503 GOL A O3 1 HETATM 2946 C C1 A GOL F 3 . ? 22.308 33.245 16.891 0.55 17.06 ? 504 GOL A C1 1 HETATM 2947 C C1 B GOL F 3 . ? 24.353 32.512 16.702 0.45 21.53 ? 504 GOL A C1 1 HETATM 2948 O O1 A GOL F 3 . ? 21.737 32.303 15.995 0.55 11.82 ? 504 GOL A O1 1 HETATM 2949 O O1 B GOL F 3 . ? 23.879 31.371 16.007 0.45 21.37 ? 504 GOL A O1 1 HETATM 2950 C C2 A GOL F 3 . ? 23.299 32.576 17.848 0.55 19.10 ? 504 GOL A C2 1 HETATM 2951 C C2 B GOL F 3 . ? 23.532 32.704 17.988 0.45 22.04 ? 504 GOL A C2 1 HETATM 2952 O O2 A GOL F 3 . ? 24.344 31.963 17.083 0.55 22.85 ? 504 GOL A O2 1 HETATM 2953 O O2 B GOL F 3 . ? 24.192 33.557 18.905 0.45 25.47 ? 504 GOL A O2 1 HETATM 2954 C C3 A GOL F 3 . ? 23.867 33.537 18.904 0.55 20.64 ? 504 GOL A C3 1 HETATM 2955 C C3 B GOL F 3 . ? 22.141 33.189 17.601 0.45 20.74 ? 504 GOL A C3 1 HETATM 2956 O O3 A GOL F 3 . ? 25.000 33.028 19.605 0.55 16.57 ? 504 GOL A O3 1 HETATM 2957 O O3 B GOL F 3 . ? 22.068 34.525 17.103 0.45 19.41 ? 504 GOL A O3 1 HETATM 2958 C C1 . GOL G 3 . ? 9.401 42.195 27.839 1.00 35.51 ? 505 GOL A C1 1 HETATM 2959 O O1 . GOL G 3 . ? 9.232 42.397 29.237 1.00 36.97 ? 505 GOL A O1 1 HETATM 2960 C C2 . GOL G 3 . ? 9.983 43.445 27.196 1.00 36.21 ? 505 GOL A C2 1 HETATM 2961 O O2 . GOL G 3 . ? 11.110 43.873 27.958 1.00 34.74 ? 505 GOL A O2 1 HETATM 2962 C C3 . GOL G 3 . ? 10.357 43.189 25.737 1.00 34.49 ? 505 GOL A C3 1 HETATM 2963 O O3 . GOL G 3 . ? 11.028 44.304 25.177 1.00 38.00 ? 505 GOL A O3 1 HETATM 2964 C C1 . GOL H 3 . ? 25.706 27.447 18.048 1.00 33.07 ? 506 GOL A C1 1 HETATM 2965 O O1 . GOL H 3 . ? 25.198 26.688 19.147 1.00 35.01 ? 506 GOL A O1 1 HETATM 2966 C C2 . GOL H 3 . ? 24.609 28.358 17.494 1.00 28.66 ? 506 GOL A C2 1 HETATM 2967 O O2 . GOL H 3 . ? 25.039 29.698 17.637 1.00 31.91 ? 506 GOL A O2 1 HETATM 2968 C C3 . GOL H 3 . ? 24.312 28.087 16.023 1.00 24.79 ? 506 GOL A C3 1 HETATM 2969 C C1 . MGL I 4 . ? 23.794 -0.302 15.867 1.00 15.32 ? 507 MGL A C1 1 HETATM 2970 C C2 . MGL I 4 . ? 23.664 0.477 17.149 1.00 14.88 ? 507 MGL A C2 1 HETATM 2971 C C3 . MGL I 4 . ? 23.955 1.958 16.870 1.00 12.20 ? 507 MGL A C3 1 HETATM 2972 C C4 . MGL I 4 . ? 25.278 2.113 16.099 1.00 13.84 ? 507 MGL A C4 1 HETATM 2973 C C5 . MGL I 4 . ? 25.327 1.177 14.907 1.00 13.31 ? 507 MGL A C5 1 HETATM 2974 C C6 . MGL I 4 . ? 26.666 1.205 14.175 1.00 17.47 ? 507 MGL A C6 1 HETATM 2975 C C7 . MGL I 4 . ? 23.430 -2.295 14.817 1.00 19.37 ? 507 MGL A C7 1 HETATM 2976 O O1 . MGL I 4 . ? 23.507 -1.670 16.114 1.00 18.44 ? 507 MGL A O1 1 HETATM 2977 O O2 . MGL I 4 . ? 22.340 0.378 17.662 1.00 13.50 ? 507 MGL A O2 1 HETATM 2978 O O3 . MGL I 4 . ? 23.952 2.616 18.135 1.00 13.10 ? 507 MGL A O3 1 HETATM 2979 O O4 . MGL I 4 . ? 25.512 3.450 15.624 1.00 12.65 ? 507 MGL A O4 1 HETATM 2980 O O5 . MGL I 4 . ? 25.121 -0.173 15.320 1.00 13.86 ? 507 MGL A O5 1 HETATM 2981 O O6 . MGL I 4 . ? 27.668 0.723 15.098 1.00 21.64 ? 507 MGL A O6 1 HETATM 2982 C C1 . SGC J 5 . ? 25.997 4.399 16.419 1.00 11.14 ? 508 SGC A C1 1 HETATM 2983 C C2 . SGC J 5 . ? 26.648 5.486 15.616 1.00 9.71 ? 508 SGC A C2 1 HETATM 2984 O O2 . SGC J 5 . ? 27.744 4.940 14.877 1.00 11.62 ? 508 SGC A O2 1 HETATM 2985 C C3 . SGC J 5 . ? 27.139 6.628 16.488 1.00 12.19 ? 508 SGC A C3 1 HETATM 2986 O O3 . SGC J 5 . ? 27.638 7.643 15.602 1.00 10.90 ? 508 SGC A O3 1 HETATM 2987 C C4 . SGC J 5 . ? 26.062 7.127 17.439 1.00 11.00 ? 508 SGC A C4 1 HETATM 2988 C C5 . SGC J 5 . ? 25.355 5.942 18.094 1.00 13.31 ? 508 SGC A C5 1 HETATM 2989 O O5 . SGC J 5 . ? 24.913 5.016 17.119 1.00 14.26 ? 508 SGC A O5 1 HETATM 2990 C C6 . SGC J 5 . ? 24.132 6.323 18.932 1.00 13.07 ? 508 SGC A C6 1 HETATM 2991 O O6 . SGC J 5 . ? 23.464 5.196 19.511 1.00 13.43 ? 508 SGC A O6 1 HETATM 2992 S S4 . SGC J 5 . ? 26.821 8.168 18.676 1.00 13.26 ? 508 SGC A S4 1 HETATM 2993 C C2 . BGC K 6 . ? 26.110 10.378 20.025 1.00 15.74 ? 509 BGC A C2 1 HETATM 2994 C C3 . BGC K 6 . ? 25.488 11.755 20.002 1.00 13.39 ? 509 BGC A C3 1 HETATM 2995 C C4 . BGC K 6 . ? 25.859 12.549 18.749 1.00 10.55 ? 509 BGC A C4 1 HETATM 2996 C C5 . BGC K 6 . ? 25.550 11.702 17.513 1.00 10.46 ? 509 BGC A C5 1 HETATM 2997 C C6 . BGC K 6 . ? 25.975 12.424 16.247 1.00 12.61 ? 509 BGC A C6 1 HETATM 2998 C C1 . BGC K 6 . ? 25.791 9.652 18.732 1.00 12.62 ? 509 BGC A C1 1 HETATM 2999 O O2 . BGC K 6 . ? 25.585 9.617 21.103 1.00 16.69 ? 509 BGC A O2 1 HETATM 3000 O O3 . BGC K 6 . ? 25.802 12.527 21.179 1.00 15.07 ? 509 BGC A O3 1 HETATM 3001 O O4 . BGC K 6 . ? 25.038 13.706 18.767 1.00 10.91 ? 509 BGC A O4 1 HETATM 3002 O O5 . BGC K 6 . ? 26.191 10.456 17.638 1.00 13.01 ? 509 BGC A O5 1 HETATM 3003 O O6 . BGC K 6 . ? 25.529 11.688 15.133 1.00 10.24 ? 509 BGC A O6 1 HETATM 3004 C C2 . BGC L 6 . ? 24.829 15.963 18.007 1.00 11.10 ? 510 BGC A C2 1 HETATM 3005 C C3 . BGC L 6 . ? 25.587 17.286 17.898 1.00 11.87 ? 510 BGC A C3 1 HETATM 3006 C C4 . BGC L 6 . ? 26.429 17.644 19.119 1.00 11.47 ? 510 BGC A C4 1 HETATM 3007 C C5 . BGC L 6 . ? 27.286 16.425 19.460 1.00 12.40 ? 510 BGC A C5 1 HETATM 3008 C C6 . BGC L 6 . ? 28.138 16.666 20.700 1.00 12.58 ? 510 BGC A C6 1 HETATM 3009 C C1 . BGC L 6 . ? 25.792 14.873 18.496 1.00 11.64 ? 510 BGC A C1 1 HETATM 3010 O O2 . BGC L 6 . ? 24.278 15.562 16.729 1.00 10.27 ? 510 BGC A O2 1 HETATM 3011 O O3 . BGC L 6 . ? 24.724 18.366 17.676 1.00 13.09 ? 510 BGC A O3 1 HETATM 3012 O O4 . BGC L 6 . ? 27.264 18.785 18.863 1.00 12.96 ? 510 BGC A O4 1 HETATM 3013 O O5 . BGC L 6 . ? 26.474 15.278 19.666 1.00 10.59 ? 510 BGC A O5 1 HETATM 3014 O O6 . BGC L 6 . ? 29.000 15.533 20.922 1.00 13.59 ? 510 BGC A O6 1 HETATM 3015 O O . HOH M 7 . ? -2.062 35.118 21.565 1.00 12.54 ? 2001 HOH A O 1 HETATM 3016 O O . HOH M 7 . ? -0.173 33.216 15.920 1.00 15.07 ? 2002 HOH A O 1 HETATM 3017 O O . HOH M 7 . ? -5.513 34.152 15.100 1.00 33.38 ? 2003 HOH A O 1 HETATM 3018 O O . HOH M 7 . ? 0.441 23.666 18.348 1.00 14.73 ? 2004 HOH A O 1 HETATM 3019 O O . HOH M 7 . ? -4.767 29.346 12.222 1.00 19.26 ? 2005 HOH A O 1 HETATM 3020 O O . HOH M 7 . ? -1.878 27.330 10.964 1.00 21.00 ? 2006 HOH A O 1 HETATM 3021 O O . HOH M 7 . ? -1.470 23.209 16.631 1.00 18.58 ? 2007 HOH A O 1 HETATM 3022 O O . HOH M 7 . ? -2.668 22.952 9.428 1.00 23.79 ? 2008 HOH A O 1 HETATM 3023 O O . HOH M 7 . ? 5.790 29.313 6.383 1.00 18.97 ? 2009 HOH A O 1 HETATM 3024 O O . HOH M 7 . ? 0.233 22.063 6.515 0.50 20.05 ? 2010 HOH A O 1 HETATM 3025 O O . HOH M 7 . ? 1.197 28.536 4.097 1.00 30.26 ? 2011 HOH A O 1 HETATM 3026 O O . HOH M 7 . ? 2.738 30.924 3.732 1.00 40.46 ? 2012 HOH A O 1 HETATM 3027 O O . HOH M 7 . ? 5.649 40.535 2.225 1.00 31.14 ? 2013 HOH A O 1 HETATM 3028 O O . HOH M 7 . ? 11.326 34.393 3.855 1.00 20.38 ? 2014 HOH A O 1 HETATM 3029 O O . HOH M 7 . ? 8.526 31.752 4.152 1.00 20.80 ? 2015 HOH A O 1 HETATM 3030 O O . HOH M 7 . ? 11.798 32.960 11.088 1.00 9.65 ? 2016 HOH A O 1 HETATM 3031 O O . HOH M 7 . ? 12.815 37.848 5.755 1.00 16.85 ? 2017 HOH A O 1 HETATM 3032 O O . HOH M 7 . ? 14.545 44.894 9.847 1.00 22.94 ? 2018 HOH A O 1 HETATM 3033 O O . HOH M 7 . ? 21.518 42.833 8.616 1.00 24.05 ? 2019 HOH A O 1 HETATM 3034 O O . HOH M 7 . ? 26.587 36.209 19.179 1.00 36.94 ? 2020 HOH A O 1 HETATM 3035 O O . HOH M 7 . ? 14.179 39.901 6.517 1.00 28.02 ? 2021 HOH A O 1 HETATM 3036 O O . HOH M 7 . ? 24.558 42.083 13.707 0.50 20.23 ? 2022 HOH A O 1 HETATM 3037 O O . HOH M 7 . ? 25.016 44.936 9.806 1.00 33.86 ? 2023 HOH A O 1 HETATM 3038 O O . HOH M 7 . ? 21.668 43.599 13.132 1.00 43.35 ? 2024 HOH A O 1 HETATM 3039 O O . HOH M 7 . ? 29.469 43.525 1.934 1.00 20.33 ? 2025 HOH A O 1 HETATM 3040 O O . HOH M 7 . ? 27.029 43.529 0.850 1.00 21.02 ? 2026 HOH A O 1 HETATM 3041 O O . HOH M 7 . ? 29.439 43.096 11.665 0.50 13.41 ? 2027 HOH A O 1 HETATM 3042 O O . HOH M 7 . ? 33.032 44.228 6.930 1.00 22.68 ? 2028 HOH A O 1 HETATM 3043 O O . HOH M 7 . ? 35.256 41.652 8.426 1.00 29.99 ? 2029 HOH A O 1 HETATM 3044 O O . HOH M 7 . ? 37.791 34.133 6.981 0.30 15.27 ? 2030 HOH A O 1 HETATM 3045 O O . HOH M 7 . ? 38.438 32.579 5.873 0.70 17.42 ? 2031 HOH A O 1 HETATM 3046 O O . HOH M 7 . ? 36.198 37.810 9.207 1.00 35.62 ? 2032 HOH A O 1 HETATM 3047 O O . HOH M 7 . ? -7.773 35.432 16.248 1.00 34.90 ? 2033 HOH A O 1 HETATM 3048 O O . HOH M 7 . ? 36.678 39.649 -8.939 1.00 23.06 ? 2034 HOH A O 1 HETATM 3049 O O . HOH M 7 . ? 35.878 34.582 -4.319 1.00 24.76 ? 2035 HOH A O 1 HETATM 3050 O O . HOH M 7 . ? 31.373 35.158 -11.466 1.00 30.62 ? 2036 HOH A O 1 HETATM 3051 O O . HOH M 7 . ? 36.083 35.015 -10.068 1.00 33.01 ? 2037 HOH A O 1 HETATM 3052 O O . HOH M 7 . ? 27.665 39.834 -7.746 1.00 22.61 ? 2038 HOH A O 1 HETATM 3053 O O . HOH M 7 . ? 23.400 43.514 6.940 1.00 27.69 ? 2039 HOH A O 1 HETATM 3054 O O . HOH M 7 . ? 25.034 34.018 -8.526 1.00 22.61 ? 2040 HOH A O 1 HETATM 3055 O O . HOH M 7 . ? 22.483 41.229 15.317 1.00 23.49 ? 2041 HOH A O 1 HETATM 3056 O O . HOH M 7 . ? 31.765 43.495 0.028 1.00 20.36 ? 2042 HOH A O 1 HETATM 3057 O O . HOH M 7 . ? 27.628 43.896 12.208 0.50 15.53 ? 2043 HOH A O 1 HETATM 3058 O O . HOH M 7 . ? 21.681 37.810 -5.008 1.00 22.75 ? 2044 HOH A O 1 HETATM 3059 O O . HOH M 7 . ? 21.010 39.718 1.118 1.00 12.49 ? 2045 HOH A O 1 HETATM 3060 O O . HOH M 7 . ? 26.628 42.623 -1.887 0.70 22.49 ? 2046 HOH A O 1 HETATM 3061 O O . HOH M 7 . ? 19.902 38.780 -3.034 1.00 25.66 ? 2047 HOH A O 1 HETATM 3062 O O . HOH M 7 . ? 26.433 41.116 -2.995 0.30 26.26 ? 2048 HOH A O 1 HETATM 3063 O O . HOH M 7 . ? 20.350 41.953 -0.205 1.00 35.76 ? 2049 HOH A O 1 HETATM 3064 O O . HOH M 7 . ? 27.032 40.112 -10.245 1.00 33.04 ? 2050 HOH A O 1 HETATM 3065 O O . HOH M 7 . ? 25.835 40.585 -5.670 1.00 32.74 ? 2051 HOH A O 1 HETATM 3066 O O . HOH M 7 . ? 30.105 33.218 -13.087 1.00 40.94 ? 2052 HOH A O 1 HETATM 3067 O O . HOH M 7 . ? 17.134 33.502 -1.297 1.00 17.68 ? 2053 HOH A O 1 HETATM 3068 O O . HOH M 7 . ? 22.774 40.085 -5.989 1.00 28.45 ? 2054 HOH A O 1 HETATM 3069 O O . HOH M 7 . ? 19.056 35.793 7.513 1.00 8.89 ? 2055 HOH A O 1 HETATM 3070 O O . HOH M 7 . ? 13.538 36.482 3.401 1.00 24.62 ? 2056 HOH A O 1 HETATM 3071 O O . HOH M 7 . ? 19.299 43.106 2.397 0.50 24.82 ? 2057 HOH A O 1 HETATM 3072 O O . HOH M 7 . ? 14.456 33.426 0.821 1.00 30.39 ? 2058 HOH A O 1 HETATM 3073 O O . HOH M 7 . ? 16.281 41.883 2.973 1.00 34.71 ? 2059 HOH A O 1 HETATM 3074 O O . HOH M 7 . ? 14.219 38.617 1.372 1.00 33.97 ? 2060 HOH A O 1 HETATM 3075 O O . HOH M 7 . ? 21.105 44.019 3.043 0.50 28.27 ? 2061 HOH A O 1 HETATM 3076 O O . HOH M 7 . ? 13.901 27.534 8.573 1.00 7.73 ? 2062 HOH A O 1 HETATM 3077 O O . HOH M 7 . ? 15.163 33.874 11.414 1.00 5.21 ? 2063 HOH A O 1 HETATM 3078 O O . HOH M 7 . ? 19.951 31.420 6.694 1.00 9.07 ? 2064 HOH A O 1 HETATM 3079 O O . HOH M 7 . ? 17.634 33.864 8.889 1.00 9.98 ? 2065 HOH A O 1 HETATM 3080 O O . HOH M 7 . ? 19.936 32.242 11.667 1.00 6.42 ? 2066 HOH A O 1 HETATM 3081 O O . HOH M 7 . ? 13.611 42.561 32.748 1.00 25.71 ? 2067 HOH A O 1 HETATM 3082 O O . HOH M 7 . ? 25.254 39.016 19.605 1.00 29.47 ? 2068 HOH A O 1 HETATM 3083 O O . HOH M 7 . ? 26.836 27.916 22.584 1.00 21.63 ? 2069 HOH A O 1 HETATM 3084 O O . HOH M 7 . ? 15.087 46.300 18.920 1.00 42.62 ? 2070 HOH A O 1 HETATM 3085 O O . HOH M 7 . ? 17.065 35.533 38.395 0.50 15.61 ? 2071 HOH A O 1 HETATM 3086 O O . HOH M 7 . ? 11.143 45.638 7.786 1.00 25.28 ? 2072 HOH A O 1 HETATM 3087 O O . HOH M 7 . ? 7.055 33.161 37.210 0.70 19.34 ? 2073 HOH A O 1 HETATM 3088 O O . HOH M 7 . ? 19.885 38.405 28.154 1.00 5.16 ? 2074 HOH A O 1 HETATM 3089 O O . HOH M 7 . ? 17.560 35.739 30.479 1.00 9.21 ? 2075 HOH A O 1 HETATM 3090 O O . HOH M 7 . ? 24.486 35.581 31.451 0.70 6.32 ? 2076 HOH A O 1 HETATM 3091 O O . HOH M 7 . ? 24.578 36.981 30.811 0.30 7.17 ? 2077 HOH A O 1 HETATM 3092 O O . HOH M 7 . ? 16.067 41.763 31.906 1.00 13.13 ? 2078 HOH A O 1 HETATM 3093 O O . HOH M 7 . ? 19.627 45.233 23.616 0.50 17.76 ? 2079 HOH A O 1 HETATM 3094 O O . HOH M 7 . ? 15.399 44.323 27.318 1.00 26.65 ? 2080 HOH A O 1 HETATM 3095 O O . HOH M 7 . ? 16.876 45.730 25.684 1.00 33.65 ? 2081 HOH A O 1 HETATM 3096 O O . HOH M 7 . ? 24.493 39.874 22.025 0.40 19.01 ? 2082 HOH A O 1 HETATM 3097 O O . HOH M 7 . ? 26.022 15.385 37.998 1.00 33.47 ? 2083 HOH A O 1 HETATM 3098 O O . HOH M 7 . ? 18.813 -4.589 17.771 1.00 36.97 ? 2084 HOH A O 1 HETATM 3099 O O . HOH M 7 . ? 20.849 44.973 21.824 0.50 17.94 ? 2085 HOH A O 1 HETATM 3100 O O . HOH M 7 . ? 19.776 41.422 15.805 1.00 28.18 ? 2086 HOH A O 1 HETATM 3101 O O . HOH M 7 . ? 18.412 39.359 14.709 1.00 28.77 ? 2087 HOH A O 1 HETATM 3102 O O . HOH M 7 . ? 27.889 35.730 27.382 1.00 28.70 ? 2088 HOH A O 1 HETATM 3103 O O . HOH M 7 . ? 30.753 30.478 29.498 1.00 25.59 ? 2089 HOH A O 1 HETATM 3104 O O . HOH M 7 . ? 30.457 25.611 33.870 0.50 19.48 ? 2090 HOH A O 1 HETATM 3105 O O . HOH M 7 . ? 20.283 21.627 41.359 1.00 15.65 ? 2091 HOH A O 1 HETATM 3106 O O . HOH M 7 . ? 8.672 47.022 16.539 1.00 14.09 ? 2092 HOH A O 1 HETATM 3107 O O . HOH M 7 . ? 30.218 21.264 37.309 1.00 25.62 ? 2093 HOH A O 1 HETATM 3108 O O . HOH M 7 . ? 19.044 45.108 12.014 1.00 42.02 ? 2094 HOH A O 1 HETATM 3109 O O . HOH M 7 . ? 19.159 43.517 14.384 1.00 26.71 ? 2095 HOH A O 1 HETATM 3110 O O . HOH M 7 . ? 16.566 46.187 16.018 1.00 32.43 ? 2096 HOH A O 1 HETATM 3111 O O . HOH M 7 . ? 16.118 40.003 12.918 1.00 10.73 ? 2097 HOH A O 1 HETATM 3112 O O . HOH M 7 . ? 19.160 34.189 37.052 1.00 9.93 ? 2098 HOH A O 1 HETATM 3113 O O . HOH M 7 . ? 13.652 29.716 40.316 1.00 33.90 ? 2099 HOH A O 1 HETATM 3114 O O . HOH M 7 . ? 14.437 -3.215 11.709 1.00 44.33 ? 2100 HOH A O 1 HETATM 3115 O O . HOH M 7 . ? 13.306 -2.604 9.275 1.00 46.91 ? 2101 HOH A O 1 HETATM 3116 O O . HOH M 7 . ? 7.967 47.159 19.234 1.00 21.32 ? 2102 HOH A O 1 HETATM 3117 O O . HOH M 7 . ? 6.006 48.672 19.172 1.00 38.58 ? 2103 HOH A O 1 HETATM 3118 O O . HOH M 7 . ? 10.623 35.175 38.684 1.00 28.91 ? 2104 HOH A O 1 HETATM 3119 O O . HOH M 7 . ? 7.475 31.390 38.156 0.30 17.62 ? 2105 HOH A O 1 HETATM 3120 O O . HOH M 7 . ? 9.357 -2.408 12.618 1.00 41.28 ? 2106 HOH A O 1 HETATM 3121 O O . HOH M 7 . ? 6.091 49.276 10.743 1.00 13.73 ? 2107 HOH A O 1 HETATM 3122 O O . HOH M 7 . ? 11.777 45.323 10.330 1.00 14.67 ? 2108 HOH A O 1 HETATM 3123 O O . HOH M 7 . ? 4.350 42.432 28.440 1.00 15.86 ? 2109 HOH A O 1 HETATM 3124 O O . HOH M 7 . ? -0.547 27.904 31.348 1.00 38.26 ? 2110 HOH A O 1 HETATM 3125 O O . HOH M 7 . ? 26.928 14.809 -4.956 1.00 32.60 ? 2111 HOH A O 1 HETATM 3126 O O . HOH M 7 . ? 7.062 44.556 5.452 1.00 21.79 ? 2112 HOH A O 1 HETATM 3127 O O . HOH M 7 . ? 3.201 40.817 14.033 1.00 21.13 ? 2113 HOH A O 1 HETATM 3128 O O . HOH M 7 . ? 3.908 46.235 24.907 1.00 35.95 ? 2114 HOH A O 1 HETATM 3129 O O . HOH M 7 . ? 8.086 46.318 23.313 1.00 44.70 ? 2115 HOH A O 1 HETATM 3130 O O . HOH M 7 . ? 0.572 48.309 6.842 1.00 21.34 ? 2116 HOH A O 1 HETATM 3131 O O . HOH M 7 . ? 5.931 49.904 13.276 1.00 28.64 ? 2117 HOH A O 1 HETATM 3132 O O . HOH M 7 . ? 6.671 48.474 15.513 1.00 28.59 ? 2118 HOH A O 1 HETATM 3133 O O . HOH M 7 . ? -0.097 48.260 10.802 1.00 29.83 ? 2119 HOH A O 1 HETATM 3134 O O . HOH M 7 . ? -3.759 30.945 8.212 1.00 31.04 ? 2120 HOH A O 1 HETATM 3135 O O . HOH M 7 . ? 1.465 42.012 8.165 1.00 25.16 ? 2121 HOH A O 1 HETATM 3136 O O . HOH M 7 . ? 41.342 26.128 30.821 1.00 42.50 ? 2122 HOH A O 1 HETATM 3137 O O . HOH M 7 . ? 17.599 5.034 31.608 1.00 31.34 ? 2123 HOH A O 1 HETATM 3138 O O . HOH M 7 . ? 0.120 40.095 11.703 1.00 37.47 ? 2124 HOH A O 1 HETATM 3139 O O . HOH M 7 . ? -0.190 37.214 14.517 1.00 32.06 ? 2125 HOH A O 1 HETATM 3140 O O . HOH M 7 . ? -0.836 36.668 7.425 1.00 31.95 ? 2126 HOH A O 1 HETATM 3141 O O . HOH M 7 . ? 31.498 8.719 26.285 0.60 18.53 ? 2127 HOH A O 1 HETATM 3142 O O . HOH M 7 . ? 3.217 36.375 13.062 1.00 11.35 ? 2128 HOH A O 1 HETATM 3143 O O . HOH M 7 . ? 31.676 13.694 34.535 0.50 19.73 ? 2129 HOH A O 1 HETATM 3144 O O . HOH M 7 . ? 32.885 10.651 31.053 1.00 20.05 ? 2130 HOH A O 1 HETATM 3145 O O . HOH M 7 . ? 21.824 17.214 40.826 1.00 26.36 ? 2131 HOH A O 1 HETATM 3146 O O . HOH M 7 . ? 13.685 34.065 13.842 1.00 7.73 ? 2132 HOH A O 1 HETATM 3147 O O . HOH M 7 . ? 6.983 22.222 35.508 1.00 19.97 ? 2133 HOH A O 1 HETATM 3148 O O . HOH M 7 . ? 8.474 17.792 36.657 1.00 32.83 ? 2134 HOH A O 1 HETATM 3149 O O . HOH M 7 . ? 5.935 17.844 36.589 1.00 32.70 ? 2135 HOH A O 1 HETATM 3150 O O . HOH M 7 . ? -4.324 25.122 26.127 1.00 24.67 ? 2136 HOH A O 1 HETATM 3151 O O . HOH M 7 . ? -3.349 27.495 25.192 1.00 27.58 ? 2137 HOH A O 1 HETATM 3152 O O . HOH M 7 . ? 24.377 25.988 29.763 1.00 9.22 ? 2138 HOH A O 1 HETATM 3153 O O . HOH M 7 . ? 28.737 21.252 33.624 1.00 22.60 ? 2139 HOH A O 1 HETATM 3154 O O . HOH M 7 . ? 25.535 16.033 35.493 1.00 10.71 ? 2140 HOH A O 1 HETATM 3155 O O . HOH M 7 . ? 29.081 17.870 35.524 1.00 25.83 ? 2141 HOH A O 1 HETATM 3156 O O . HOH M 7 . ? 28.097 21.217 29.979 1.00 13.99 ? 2142 HOH A O 1 HETATM 3157 O O . HOH M 7 . ? 29.998 17.708 28.066 1.00 26.80 ? 2143 HOH A O 1 HETATM 3158 O O . HOH M 7 . ? 30.717 13.919 29.659 1.00 27.46 ? 2144 HOH A O 1 HETATM 3159 O O . HOH M 7 . ? 20.104 -3.355 15.501 1.00 29.42 ? 2145 HOH A O 1 HETATM 3160 O O . HOH M 7 . ? 10.450 -0.927 15.965 1.00 37.95 ? 2146 HOH A O 1 HETATM 3161 O O . HOH M 7 . ? 30.015 11.954 21.817 1.00 33.27 ? 2147 HOH A O 1 HETATM 3162 O O . HOH M 7 . ? 32.410 12.085 24.943 1.00 28.32 ? 2148 HOH A O 1 HETATM 3163 O O . HOH M 7 . ? 36.918 18.528 27.048 1.00 32.19 ? 2149 HOH A O 1 HETATM 3164 O O . HOH M 7 . ? 31.530 20.132 21.364 1.00 12.82 ? 2150 HOH A O 1 HETATM 3165 O O . HOH M 7 . ? 4.674 4.176 26.703 1.00 14.18 ? 2151 HOH A O 1 HETATM 3166 O O . HOH M 7 . ? 33.414 20.968 28.412 1.00 33.34 ? 2152 HOH A O 1 HETATM 3167 O O . HOH M 7 . ? 31.333 25.346 28.685 1.00 31.37 ? 2153 HOH A O 1 HETATM 3168 O O . HOH M 7 . ? 28.327 23.010 23.348 1.00 15.06 ? 2154 HOH A O 1 HETATM 3169 O O . HOH M 7 . ? 28.923 24.360 20.949 1.00 27.42 ? 2155 HOH A O 1 HETATM 3170 O O . HOH M 7 . ? 31.389 28.681 27.522 1.00 39.43 ? 2156 HOH A O 1 HETATM 3171 O O . HOH M 7 . ? 28.019 29.256 25.071 1.00 29.52 ? 2157 HOH A O 1 HETATM 3172 O O . HOH M 7 . ? 25.842 28.712 26.929 1.00 13.89 ? 2158 HOH A O 1 HETATM 3173 O O . HOH M 7 . ? 28.718 32.877 29.830 1.00 17.29 ? 2159 HOH A O 1 HETATM 3174 O O . HOH M 7 . ? 25.458 34.696 28.356 1.00 12.57 ? 2160 HOH A O 1 HETATM 3175 O O . HOH M 7 . ? 25.663 33.585 33.064 1.00 19.39 ? 2161 HOH A O 1 HETATM 3176 O O . HOH M 7 . ? 29.579 24.025 32.415 0.50 18.59 ? 2162 HOH A O 1 HETATM 3177 O O . HOH M 7 . ? 26.614 23.722 30.322 1.00 18.51 ? 2163 HOH A O 1 HETATM 3178 O O . HOH M 7 . ? 21.490 23.750 40.017 1.00 10.55 ? 2164 HOH A O 1 HETATM 3179 O O . HOH M 7 . ? 25.130 19.541 41.607 1.00 32.86 ? 2165 HOH A O 1 HETATM 3180 O O . HOH M 7 . ? 27.437 20.375 37.474 1.00 12.02 ? 2166 HOH A O 1 HETATM 3181 O O . HOH M 7 . ? 31.849 24.584 41.529 1.00 37.27 ? 2167 HOH A O 1 HETATM 3182 O O . HOH M 7 . ? 25.992 27.800 36.182 1.00 14.26 ? 2168 HOH A O 1 HETATM 3183 O O . HOH M 7 . ? 20.152 25.989 40.922 1.00 9.35 ? 2169 HOH A O 1 HETATM 3184 O O . HOH M 7 . ? 23.964 24.925 42.743 1.00 22.34 ? 2170 HOH A O 1 HETATM 3185 O O . HOH M 7 . ? 11.412 13.925 -2.468 1.00 33.96 ? 2171 HOH A O 1 HETATM 3186 O O . HOH M 7 . ? 22.525 9.694 -3.387 1.00 37.30 ? 2172 HOH A O 1 HETATM 3187 O O . HOH M 7 . ? 15.332 31.135 39.098 1.00 16.46 ? 2173 HOH A O 1 HETATM 3188 O O . HOH M 7 . ? 18.013 24.800 42.416 1.00 26.39 ? 2174 HOH A O 1 HETATM 3189 O O . HOH M 7 . ? 17.305 27.385 45.014 1.00 40.95 ? 2175 HOH A O 1 HETATM 3190 O O . HOH M 7 . ? 14.810 25.639 41.672 1.00 46.88 ? 2176 HOH A O 1 HETATM 3191 O O . HOH M 7 . ? 25.707 31.036 38.321 0.70 19.28 ? 2177 HOH A O 1 HETATM 3192 O O . HOH M 7 . ? 19.616 32.200 38.843 1.00 15.36 ? 2178 HOH A O 1 HETATM 3193 O O . HOH M 7 . ? 23.443 32.330 39.459 1.00 11.60 ? 2179 HOH A O 1 HETATM 3194 O O . HOH M 7 . ? 19.241 33.431 34.227 1.00 7.54 ? 2180 HOH A O 1 HETATM 3195 O O . HOH M 7 . ? 22.594 -0.130 4.144 1.00 36.20 ? 2181 HOH A O 1 HETATM 3196 O O . HOH M 7 . ? 10.789 0.294 10.282 1.00 33.48 ? 2182 HOH A O 1 HETATM 3197 O O . HOH M 7 . ? 13.217 -1.440 13.347 1.00 50.07 ? 2183 HOH A O 1 HETATM 3198 O O . HOH M 7 . ? 13.005 0.149 6.007 1.00 25.95 ? 2184 HOH A O 1 HETATM 3199 O O . HOH M 7 . ? 10.290 25.258 42.745 1.00 36.98 ? 2185 HOH A O 1 HETATM 3200 O O . HOH M 7 . ? 13.530 35.693 34.883 1.00 12.64 ? 2186 HOH A O 1 HETATM 3201 O O . HOH M 7 . ? 5.585 0.483 14.313 1.00 23.48 ? 2187 HOH A O 1 HETATM 3202 O O . HOH M 7 . ? 10.265 0.506 13.950 0.50 19.26 ? 2188 HOH A O 1 HETATM 3203 O O . HOH M 7 . ? 17.411 35.158 33.181 1.00 10.12 ? 2189 HOH A O 1 HETATM 3204 O O . HOH M 7 . ? 12.774 34.526 37.181 1.00 16.43 ? 2190 HOH A O 1 HETATM 3205 O O . HOH M 7 . ? 7.749 34.699 33.189 1.00 12.65 ? 2191 HOH A O 1 HETATM 3206 O O . HOH M 7 . ? 10.724 30.671 38.961 1.00 28.42 ? 2192 HOH A O 1 HETATM 3207 O O . HOH M 7 . ? 5.243 35.798 32.427 1.00 22.32 ? 2193 HOH A O 1 HETATM 3208 O O . HOH M 7 . ? 2.821 34.881 32.893 1.00 28.51 ? 2194 HOH A O 1 HETATM 3209 O O . HOH M 7 . ? -0.117 30.456 30.906 1.00 25.67 ? 2195 HOH A O 1 HETATM 3210 O O . HOH M 7 . ? 5.714 40.384 29.442 1.00 11.37 ? 2196 HOH A O 1 HETATM 3211 O O . HOH M 7 . ? 9.363 40.090 36.216 1.00 38.45 ? 2197 HOH A O 1 HETATM 3212 O O . HOH M 7 . ? 12.046 40.848 33.906 1.00 23.06 ? 2198 HOH A O 1 HETATM 3213 O O . HOH M 7 . ? 11.121 36.668 34.594 1.00 34.44 ? 2199 HOH A O 1 HETATM 3214 O O . HOH M 7 . ? 24.487 17.409 -5.125 1.00 30.79 ? 2200 HOH A O 1 HETATM 3215 O O . HOH M 7 . ? 33.250 6.621 3.118 1.00 28.54 ? 2201 HOH A O 1 HETATM 3216 O O . HOH M 7 . ? 5.652 44.993 23.345 1.00 17.58 ? 2202 HOH A O 1 HETATM 3217 O O . HOH M 7 . ? 0.424 35.923 16.806 1.00 13.39 ? 2203 HOH A O 1 HETATM 3218 O O . HOH M 7 . ? 14.310 21.534 -3.396 1.00 18.16 ? 2204 HOH A O 1 HETATM 3219 O O . HOH M 7 . ? 13.614 25.826 -4.035 1.00 27.38 ? 2205 HOH A O 1 HETATM 3220 O O . HOH M 7 . ? 10.753 21.331 -0.880 0.50 19.49 ? 2206 HOH A O 1 HETATM 3221 O O . HOH M 7 . ? 10.372 25.507 -1.630 1.00 30.65 ? 2207 HOH A O 1 HETATM 3222 O O . HOH M 7 . ? 10.870 31.936 2.555 1.00 25.66 ? 2208 HOH A O 1 HETATM 3223 O O . HOH M 7 . ? 14.210 30.703 0.905 1.00 19.22 ? 2209 HOH A O 1 HETATM 3224 O O . HOH M 7 . ? -2.287 33.716 13.764 1.00 35.37 ? 2210 HOH A O 1 HETATM 3225 O O . HOH M 7 . ? -2.627 29.978 10.511 1.00 21.68 ? 2211 HOH A O 1 HETATM 3226 O O . HOH M 7 . ? 11.110 17.546 -1.050 1.00 44.62 ? 2212 HOH A O 1 HETATM 3227 O O . HOH M 7 . ? 3.331 28.572 2.730 1.00 31.55 ? 2213 HOH A O 1 HETATM 3228 O O . HOH M 7 . ? 0.054 17.436 4.761 1.00 35.12 ? 2214 HOH A O 1 HETATM 3229 O O . HOH M 7 . ? 13.726 18.950 24.057 1.00 8.58 ? 2215 HOH A O 1 HETATM 3230 O O . HOH M 7 . ? 20.541 21.144 25.139 1.00 7.76 ? 2216 HOH A O 1 HETATM 3231 O O . HOH M 7 . ? 22.098 19.365 26.397 1.00 8.84 ? 2217 HOH A O 1 HETATM 3232 O O . HOH M 7 . ? 43.834 26.046 13.991 1.00 35.08 ? 2218 HOH A O 1 HETATM 3233 O O . HOH M 7 . ? 41.404 19.371 25.805 1.00 29.70 ? 2219 HOH A O 1 HETATM 3234 O O . HOH M 7 . ? 42.862 26.067 28.409 1.00 33.33 ? 2220 HOH A O 1 HETATM 3235 O O . HOH M 7 . ? 25.790 15.123 24.269 1.00 11.94 ? 2221 HOH A O 1 HETATM 3236 O O . HOH M 7 . ? 16.762 7.365 30.271 1.00 22.23 ? 2222 HOH A O 1 HETATM 3237 O O . HOH M 7 . ? 43.333 8.463 10.063 1.00 39.67 ? 2223 HOH A O 1 HETATM 3238 O O . HOH M 7 . ? 24.278 3.258 23.770 1.00 32.71 ? 2224 HOH A O 1 HETATM 3239 O O . HOH M 7 . ? 41.587 29.634 6.269 1.00 27.35 ? 2225 HOH A O 1 HETATM 3240 O O . HOH M 7 . ? 41.050 29.717 12.738 1.00 31.38 ? 2226 HOH A O 1 HETATM 3241 O O . HOH M 7 . ? 42.371 22.761 3.153 1.00 41.73 ? 2227 HOH A O 1 HETATM 3242 O O . HOH M 7 . ? 28.886 8.585 24.707 1.00 28.63 ? 2228 HOH A O 1 HETATM 3243 O O . HOH M 7 . ? 25.733 7.113 22.017 1.00 31.40 ? 2229 HOH A O 1 HETATM 3244 O O . HOH M 7 . ? 21.219 5.234 27.721 1.00 11.68 ? 2230 HOH A O 1 HETATM 3245 O O . HOH M 7 . ? 25.483 5.471 34.598 1.00 11.86 ? 2231 HOH A O 1 HETATM 3246 O O . HOH M 7 . ? 26.702 5.620 25.046 1.00 26.04 ? 2232 HOH A O 1 HETATM 3247 O O . HOH M 7 . ? 24.163 3.435 27.955 1.00 25.84 ? 2233 HOH A O 1 HETATM 3248 O O . HOH M 7 . ? 28.174 5.918 34.548 1.00 10.31 ? 2234 HOH A O 1 HETATM 3249 O O . HOH M 7 . ? 37.419 31.084 9.543 1.00 20.09 ? 2235 HOH A O 1 HETATM 3250 O O . HOH M 7 . ? 34.621 35.762 9.738 1.00 24.74 ? 2236 HOH A O 1 HETATM 3251 O O . HOH M 7 . ? 30.960 12.154 32.364 1.00 12.08 ? 2237 HOH A O 1 HETATM 3252 O O . HOH M 7 . ? 26.576 26.955 -7.374 0.50 19.96 ? 2238 HOH A O 1 HETATM 3253 O O . HOH M 7 . ? 16.123 19.516 -3.103 1.00 29.95 ? 2239 HOH A O 1 HETATM 3254 O O . HOH M 7 . ? 19.614 12.233 37.094 1.00 11.38 ? 2240 HOH A O 1 HETATM 3255 O O . HOH M 7 . ? 23.345 5.615 36.058 0.60 11.82 ? 2241 HOH A O 1 HETATM 3256 O O . HOH M 7 . ? 20.202 8.497 36.748 1.00 23.88 ? 2242 HOH A O 1 HETATM 3257 O O . HOH M 7 . ? 19.858 15.694 37.395 1.00 9.46 ? 2243 HOH A O 1 HETATM 3258 O O . HOH M 7 . ? 23.497 15.439 39.701 1.00 28.90 ? 2244 HOH A O 1 HETATM 3259 O O . HOH M 7 . ? 16.310 16.626 39.546 1.00 25.79 ? 2245 HOH A O 1 HETATM 3260 O O . HOH M 7 . ? 14.678 11.150 35.842 1.00 33.98 ? 2246 HOH A O 1 HETATM 3261 O O . HOH M 7 . ? 20.229 13.043 39.711 1.00 25.15 ? 2247 HOH A O 1 HETATM 3262 O O . HOH M 7 . ? 17.849 9.972 36.867 1.00 26.38 ? 2248 HOH A O 1 HETATM 3263 O O . HOH M 7 . ? 17.454 19.222 39.188 1.00 31.09 ? 2249 HOH A O 1 HETATM 3264 O O . HOH M 7 . ? 15.826 9.367 31.909 1.00 32.54 ? 2250 HOH A O 1 HETATM 3265 O O . HOH M 7 . ? 9.711 9.252 33.526 0.50 24.45 ? 2251 HOH A O 1 HETATM 3266 O O . HOH M 7 . ? 9.419 12.283 32.059 0.50 20.06 ? 2252 HOH A O 1 HETATM 3267 O O . HOH M 7 . ? 10.802 7.088 30.031 1.00 40.23 ? 2253 HOH A O 1 HETATM 3268 O O . HOH M 7 . ? 9.357 20.811 35.864 1.00 15.40 ? 2254 HOH A O 1 HETATM 3269 O O . HOH M 7 . ? 14.979 19.323 26.289 1.00 11.11 ? 2255 HOH A O 1 HETATM 3270 O O . HOH M 7 . ? 1.819 28.616 29.783 1.00 26.72 ? 2256 HOH A O 1 HETATM 3271 O O . HOH M 7 . ? 5.122 20.458 36.320 1.00 36.78 ? 2257 HOH A O 1 HETATM 3272 O O . HOH M 7 . ? 0.796 18.494 34.410 1.00 39.51 ? 2258 HOH A O 1 HETATM 3273 O O . HOH M 7 . ? 1.315 25.898 31.469 1.00 32.94 ? 2259 HOH A O 1 HETATM 3274 O O . HOH M 7 . ? 3.494 30.713 34.557 1.00 36.10 ? 2260 HOH A O 1 HETATM 3275 O O . HOH M 7 . ? 6.084 25.054 35.558 1.00 28.65 ? 2261 HOH A O 1 HETATM 3276 O O . HOH M 7 . ? 17.221 36.738 37.187 0.50 14.84 ? 2262 HOH A O 1 HETATM 3277 O O . HOH M 7 . ? -5.171 18.138 19.820 1.00 47.33 ? 2263 HOH A O 1 HETATM 3278 O O . HOH M 7 . ? -0.997 27.203 24.039 1.00 11.78 ? 2264 HOH A O 1 HETATM 3279 O O . HOH M 7 . ? 0.942 23.939 29.815 1.00 17.92 ? 2265 HOH A O 1 HETATM 3280 O O . HOH M 7 . ? -2.155 23.610 26.657 1.00 9.67 ? 2266 HOH A O 1 HETATM 3281 O O . HOH M 7 . ? -3.226 28.888 19.493 1.00 12.88 ? 2267 HOH A O 1 HETATM 3282 O O . HOH M 7 . ? -0.141 34.294 23.311 1.00 7.19 ? 2268 HOH A O 1 HETATM 3283 O O . HOH M 7 . ? 6.662 36.113 20.524 1.00 6.58 ? 2269 HOH A O 1 HETATM 3284 O O . HOH M 7 . ? -0.207 27.042 21.179 1.00 12.98 ? 2270 HOH A O 1 HETATM 3285 O O . HOH M 7 . ? 17.769 15.957 22.371 1.00 6.36 ? 2271 HOH A O 1 HETATM 3286 O O . HOH M 7 . ? 17.779 16.988 15.886 1.00 5.99 ? 2272 HOH A O 1 HETATM 3287 O O . HOH M 7 . ? 20.371 16.776 18.835 1.00 10.21 ? 2273 HOH A O 1 HETATM 3288 O O . HOH M 7 . ? 15.271 16.749 23.335 1.00 8.19 ? 2274 HOH A O 1 HETATM 3289 O O . HOH M 7 . ? 13.709 -0.083 19.531 1.00 12.90 ? 2275 HOH A O 1 HETATM 3290 O O . HOH M 7 . ? 12.916 -1.502 16.337 1.00 29.42 ? 2276 HOH A O 1 HETATM 3291 O O . HOH M 7 . ? 18.693 -0.063 23.198 1.00 34.53 ? 2277 HOH A O 1 HETATM 3292 O O . HOH M 7 . ? 14.766 -1.573 21.846 1.00 18.91 ? 2278 HOH A O 1 HETATM 3293 O O . HOH M 7 . ? 20.116 -0.836 15.959 1.00 11.39 ? 2279 HOH A O 1 HETATM 3294 O O . HOH M 7 . ? 21.975 1.117 20.325 1.00 14.45 ? 2280 HOH A O 1 HETATM 3295 O O . HOH M 7 . ? 11.492 -2.035 19.488 1.00 32.19 ? 2281 HOH A O 1 HETATM 3296 O O . HOH M 7 . ? 13.062 5.424 27.196 1.00 23.46 ? 2282 HOH A O 1 HETATM 3297 O O . HOH M 7 . ? 6.098 1.862 25.957 1.00 18.47 ? 2283 HOH A O 1 HETATM 3298 O O . HOH M 7 . ? 6.146 6.402 27.434 1.00 16.59 ? 2284 HOH A O 1 HETATM 3299 O O . HOH M 7 . ? 8.284 -0.384 28.136 1.00 31.36 ? 2285 HOH A O 1 HETATM 3300 O O . HOH M 7 . ? 0.129 19.219 21.825 1.00 9.73 ? 2286 HOH A O 1 HETATM 3301 O O . HOH M 7 . ? -2.364 15.273 21.916 1.00 20.72 ? 2287 HOH A O 1 HETATM 3302 O O . HOH M 7 . ? 3.427 7.660 26.953 1.00 15.10 ? 2288 HOH A O 1 HETATM 3303 O O . HOH M 7 . ? -1.025 14.647 30.219 1.00 24.15 ? 2289 HOH A O 1 HETATM 3304 O O . HOH M 7 . ? 2.715 9.556 32.525 1.00 22.51 ? 2290 HOH A O 1 HETATM 3305 O O . HOH M 7 . ? 0.218 21.421 30.276 1.00 15.16 ? 2291 HOH A O 1 HETATM 3306 O O . HOH M 7 . ? -3.231 18.688 30.568 1.00 15.75 ? 2292 HOH A O 1 HETATM 3307 O O . HOH M 7 . ? -2.150 21.447 28.747 1.00 20.10 ? 2293 HOH A O 1 HETATM 3308 O O . HOH M 7 . ? -3.053 18.755 23.753 1.00 29.90 ? 2294 HOH A O 1 HETATM 3309 O O . HOH M 7 . ? -3.446 19.747 27.190 1.00 33.55 ? 2295 HOH A O 1 HETATM 3310 O O . HOH M 7 . ? -1.328 20.706 19.689 1.00 24.90 ? 2296 HOH A O 1 HETATM 3311 O O . HOH M 7 . ? -2.011 26.268 19.227 1.00 20.00 ? 2297 HOH A O 1 HETATM 3312 O O . HOH M 7 . ? -5.373 29.300 21.341 1.00 23.50 ? 2298 HOH A O 1 HETATM 3313 O O . HOH M 7 . ? -7.062 24.628 23.976 1.00 36.07 ? 2299 HOH A O 1 HETATM 3314 O O . HOH M 7 . ? -3.182 19.794 13.105 1.00 29.13 ? 2300 HOH A O 1 HETATM 3315 O O . HOH M 7 . ? -1.784 18.061 11.591 1.00 47.24 ? 2301 HOH A O 1 HETATM 3316 O O . HOH M 7 . ? 20.385 16.122 14.890 1.00 6.67 ? 2302 HOH A O 1 HETATM 3317 O O . HOH M 7 . ? 21.826 18.723 17.386 1.00 10.63 ? 2303 HOH A O 1 HETATM 3318 O O . HOH M 7 . ? 24.577 13.855 9.930 1.00 7.69 ? 2304 HOH A O 1 HETATM 3319 O O . HOH M 7 . ? 9.554 14.078 -0.407 1.00 17.33 ? 2305 HOH A O 1 HETATM 3320 O O . HOH M 7 . ? 10.316 10.626 -1.288 1.00 33.20 ? 2306 HOH A O 1 HETATM 3321 O O . HOH M 7 . ? 13.944 5.884 -0.539 1.00 39.89 ? 2307 HOH A O 1 HETATM 3322 O O . HOH M 7 . ? 18.214 10.192 -4.523 1.00 33.81 ? 2308 HOH A O 1 HETATM 3323 O O . HOH M 7 . ? 25.327 6.811 -1.854 1.00 28.36 ? 2309 HOH A O 1 HETATM 3324 O O . HOH M 7 . ? 23.072 8.368 -1.201 1.00 22.47 ? 2310 HOH A O 1 HETATM 3325 O O . HOH M 7 . ? 23.602 11.593 4.600 1.00 7.11 ? 2311 HOH A O 1 HETATM 3326 O O . HOH M 7 . ? 28.420 -2.232 6.037 1.00 39.49 ? 2312 HOH A O 1 HETATM 3327 O O . HOH M 7 . ? 23.661 -2.471 4.943 1.00 39.93 ? 2313 HOH A O 1 HETATM 3328 O O . HOH M 7 . ? 27.526 2.058 11.078 1.00 34.46 ? 2314 HOH A O 1 HETATM 3329 O O . HOH M 7 . ? 22.006 2.011 5.582 1.00 9.95 ? 2315 HOH A O 1 HETATM 3330 O O . HOH M 7 . ? 15.655 0.623 4.548 1.00 19.63 ? 2316 HOH A O 1 HETATM 3331 O O . HOH M 7 . ? 12.688 0.852 12.311 1.00 16.29 ? 2317 HOH A O 1 HETATM 3332 O O . HOH M 7 . ? 12.236 1.640 8.197 1.00 21.15 ? 2318 HOH A O 1 HETATM 3333 O O . HOH M 7 . ? 21.032 10.571 5.361 1.00 6.66 ? 2319 HOH A O 1 HETATM 3334 O O . HOH M 7 . ? 13.641 7.704 1.364 1.00 11.16 ? 2320 HOH A O 1 HETATM 3335 O O . HOH M 7 . ? 11.335 6.269 1.831 1.00 28.63 ? 2321 HOH A O 1 HETATM 3336 O O . HOH M 7 . ? 6.469 6.571 0.396 1.00 25.70 ? 2322 HOH A O 1 HETATM 3337 O O . HOH M 7 . ? 8.252 11.898 0.017 1.00 36.01 ? 2323 HOH A O 1 HETATM 3338 O O . HOH M 7 . ? 13.846 1.477 1.769 1.00 37.55 ? 2324 HOH A O 1 HETATM 3339 O O . HOH M 7 . ? 10.449 3.735 7.766 1.00 12.78 ? 2325 HOH A O 1 HETATM 3340 O O . HOH M 7 . ? 4.403 5.348 9.358 1.00 26.33 ? 2326 HOH A O 1 HETATM 3341 O O . HOH M 7 . ? 5.146 7.735 2.455 1.00 25.85 ? 2327 HOH A O 1 HETATM 3342 O O . HOH M 7 . ? 9.856 4.627 5.189 1.00 17.37 ? 2328 HOH A O 1 HETATM 3343 O O . HOH M 7 . ? 7.849 1.575 13.446 1.00 15.63 ? 2329 HOH A O 1 HETATM 3344 O O . HOH M 7 . ? 0.512 3.747 16.188 1.00 20.79 ? 2330 HOH A O 1 HETATM 3345 O O . HOH M 7 . ? 1.186 6.737 13.075 1.00 34.33 ? 2331 HOH A O 1 HETATM 3346 O O . HOH M 7 . ? -4.668 8.347 16.806 1.00 19.60 ? 2332 HOH A O 1 HETATM 3347 O O . HOH M 7 . ? 2.203 10.845 25.123 1.00 6.78 ? 2333 HOH A O 1 HETATM 3348 O O . HOH M 7 . ? 5.701 -1.408 24.716 1.00 27.79 ? 2334 HOH A O 1 HETATM 3349 O O . HOH M 7 . ? 4.222 0.570 19.071 1.00 19.07 ? 2335 HOH A O 1 HETATM 3350 O O . HOH M 7 . ? -2.456 12.784 22.160 1.00 13.78 ? 2336 HOH A O 1 HETATM 3351 O O . HOH M 7 . ? -0.753 15.140 15.064 1.00 22.64 ? 2337 HOH A O 1 HETATM 3352 O O . HOH M 7 . ? -0.692 13.812 11.091 1.00 26.35 ? 2338 HOH A O 1 HETATM 3353 O O . HOH M 7 . ? 18.235 19.280 1.351 1.00 7.63 ? 2339 HOH A O 1 HETATM 3354 O O . HOH M 7 . ? 23.098 21.300 9.935 1.00 4.56 ? 2340 HOH A O 1 HETATM 3355 O O . HOH M 7 . ? 20.945 19.889 7.351 1.00 5.69 ? 2341 HOH A O 1 HETATM 3356 O O . HOH M 7 . ? 25.027 18.156 2.330 1.00 5.71 ? 2342 HOH A O 1 HETATM 3357 O O . HOH M 7 . ? 30.224 12.712 -2.467 1.00 15.80 ? 2343 HOH A O 1 HETATM 3358 O O . HOH M 7 . ? 22.979 15.657 -3.728 1.00 22.75 ? 2344 HOH A O 1 HETATM 3359 O O . HOH M 7 . ? 30.268 9.629 1.052 1.00 23.81 ? 2345 HOH A O 1 HETATM 3360 O O . HOH M 7 . ? 35.489 12.609 2.943 1.00 16.29 ? 2346 HOH A O 1 HETATM 3361 O O . HOH M 7 . ? 32.229 9.047 2.767 1.00 23.52 ? 2347 HOH A O 1 HETATM 3362 O O . HOH M 7 . ? 24.536 12.754 6.860 1.00 6.97 ? 2348 HOH A O 1 HETATM 3363 O O . HOH M 7 . ? 34.956 5.544 6.535 1.00 40.20 ? 2349 HOH A O 1 HETATM 3364 O O . HOH M 7 . ? 31.682 4.706 5.118 1.00 35.62 ? 2350 HOH A O 1 HETATM 3365 O O . HOH M 7 . ? 36.470 5.912 10.970 1.00 11.08 ? 2351 HOH A O 1 HETATM 3366 O O . HOH M 7 . ? 30.175 2.178 11.375 0.30 11.32 ? 2352 HOH A O 1 HETATM 3367 O O . HOH M 7 . ? 29.148 5.555 10.268 1.00 9.45 ? 2353 HOH A O 1 HETATM 3368 O O . HOH M 7 . ? 29.195 11.143 17.363 1.00 16.22 ? 2354 HOH A O 1 HETATM 3369 O O . HOH M 7 . ? 34.156 9.610 15.804 1.00 24.27 ? 2355 HOH A O 1 HETATM 3370 O O . HOH M 7 . ? 27.154 19.755 13.876 1.00 6.81 ? 2356 HOH A O 1 HETATM 3371 O O . HOH M 7 . ? 29.605 13.033 19.340 1.00 16.68 ? 2357 HOH A O 1 HETATM 3372 O O . HOH M 7 . ? 33.353 15.908 10.559 1.00 8.87 ? 2358 HOH A O 1 HETATM 3373 O O . HOH M 7 . ? 30.574 24.493 9.994 1.00 13.83 ? 2359 HOH A O 1 HETATM 3374 O O . HOH M 7 . ? 34.507 19.338 0.582 1.00 19.84 ? 2360 HOH A O 1 HETATM 3375 O O . HOH M 7 . ? 16.763 30.520 -2.144 0.45 11.49 ? 2361 HOH A O 1 HETATM 3376 O O . HOH M 7 . ? 17.952 30.281 -4.985 1.00 25.55 ? 2362 HOH A O 1 HETATM 3377 O O . HOH M 7 . ? 14.120 23.937 -2.217 1.00 9.45 ? 2363 HOH A O 1 HETATM 3378 O O . HOH M 7 . ? 11.899 23.815 -0.373 1.00 12.75 ? 2364 HOH A O 1 HETATM 3379 O O . HOH M 7 . ? 19.943 25.545 -1.165 0.45 13.28 ? 2365 HOH A O 1 HETATM 3380 O O . HOH M 7 . ? 10.004 28.266 0.432 1.00 38.39 ? 2366 HOH A O 1 HETATM 3381 O O . HOH M 7 . ? 12.303 29.640 2.332 1.00 18.56 ? 2367 HOH A O 1 HETATM 3382 O O . HOH M 7 . ? 7.109 27.771 0.524 1.00 34.56 ? 2368 HOH A O 1 HETATM 3383 O O . HOH M 7 . ? 6.066 27.806 3.175 1.00 21.02 ? 2369 HOH A O 1 HETATM 3384 O O . HOH M 7 . ? 3.234 20.561 5.901 1.00 20.29 ? 2370 HOH A O 1 HETATM 3385 O O . HOH M 7 . ? 7.785 22.968 -1.774 1.00 37.83 ? 2371 HOH A O 1 HETATM 3386 O O . HOH M 7 . ? 2.269 28.061 0.179 1.00 30.73 ? 2372 HOH A O 1 HETATM 3387 O O . HOH M 7 . ? 6.188 26.197 -1.549 1.00 44.38 ? 2373 HOH A O 1 HETATM 3388 O O . HOH M 7 . ? 1.376 21.874 1.460 1.00 21.43 ? 2374 HOH A O 1 HETATM 3389 O O . HOH M 7 . ? 5.614 19.600 -1.733 1.00 21.02 ? 2375 HOH A O 1 HETATM 3390 O O . HOH M 7 . ? 9.028 19.865 -0.375 0.50 20.35 ? 2376 HOH A O 1 HETATM 3391 O O . HOH M 7 . ? 7.350 15.806 -0.809 1.00 17.41 ? 2377 HOH A O 1 HETATM 3392 O O . HOH M 7 . ? 2.614 19.711 2.454 1.00 20.67 ? 2378 HOH A O 1 HETATM 3393 O O . HOH M 7 . ? 1.953 17.991 6.378 1.00 26.64 ? 2379 HOH A O 1 HETATM 3394 O O . HOH M 7 . ? 3.753 8.094 5.881 1.00 27.36 ? 2380 HOH A O 1 HETATM 3395 O O . HOH M 7 . ? -2.671 10.773 4.408 1.00 24.67 ? 2381 HOH A O 1 HETATM 3396 O O . HOH M 7 . ? 1.292 19.505 8.586 1.00 13.18 ? 2382 HOH A O 1 HETATM 3397 O O . HOH M 7 . ? 21.412 23.166 8.926 1.00 4.95 ? 2383 HOH A O 1 HETATM 3398 O O . HOH M 7 . ? 22.165 26.450 6.507 1.00 8.85 ? 2384 HOH A O 1 HETATM 3399 O O . HOH M 7 . ? 28.223 25.675 9.307 1.00 7.99 ? 2385 HOH A O 1 HETATM 3400 O O . HOH M 7 . ? 22.159 32.948 13.280 1.00 7.35 ? 2386 HOH A O 1 HETATM 3401 O O . HOH M 7 . ? 32.220 22.300 19.911 1.00 19.64 ? 2387 HOH A O 1 HETATM 3402 O O . HOH M 7 . ? 40.358 28.568 17.579 1.00 28.40 ? 2388 HOH A O 1 HETATM 3403 O O . HOH M 7 . ? 36.319 21.932 18.995 1.00 8.46 ? 2389 HOH A O 1 HETATM 3404 O O . HOH M 7 . ? 42.735 19.735 14.223 1.00 19.64 ? 2390 HOH A O 1 HETATM 3405 O O . HOH M 7 . ? 43.503 23.699 12.653 1.00 19.63 ? 2391 HOH A O 1 HETATM 3406 O O . HOH M 7 . ? 42.346 29.089 19.075 1.00 37.48 ? 2392 HOH A O 1 HETATM 3407 O O . HOH M 7 . ? 46.495 28.324 19.401 1.00 33.23 ? 2393 HOH A O 1 HETATM 3408 O O . HOH M 7 . ? 45.762 22.393 16.236 1.00 26.69 ? 2394 HOH A O 1 HETATM 3409 O O . HOH M 7 . ? 43.697 18.219 22.539 1.00 23.21 ? 2395 HOH A O 1 HETATM 3410 O O . HOH M 7 . ? 44.966 27.888 24.971 1.00 46.88 ? 2396 HOH A O 1 HETATM 3411 O O . HOH M 7 . ? 44.631 28.337 22.331 1.00 37.98 ? 2397 HOH A O 1 HETATM 3412 O O . HOH M 7 . ? 43.691 23.721 26.575 1.00 37.75 ? 2398 HOH A O 1 HETATM 3413 O O . HOH M 7 . ? 48.218 27.266 21.894 1.00 35.69 ? 2399 HOH A O 1 HETATM 3414 O O . HOH M 7 . ? 42.753 21.443 24.276 1.00 17.27 ? 2400 HOH A O 1 HETATM 3415 O O . HOH M 7 . ? 36.672 21.309 27.814 1.00 36.35 ? 2401 HOH A O 1 HETATM 3416 O O . HOH M 7 . ? 41.168 28.566 24.714 1.00 23.33 ? 2402 HOH A O 1 HETATM 3417 O O . HOH M 7 . ? 37.832 26.853 23.572 1.00 27.89 ? 2403 HOH A O 1 HETATM 3418 O O . HOH M 7 . ? 34.404 23.395 20.724 1.00 14.90 ? 2404 HOH A O 1 HETATM 3419 O O . HOH M 7 . ? 38.684 20.090 25.612 1.00 18.11 ? 2405 HOH A O 1 HETATM 3420 O O . HOH M 7 . ? 42.428 15.622 18.128 1.00 17.48 ? 2406 HOH A O 1 HETATM 3421 O O . HOH M 7 . ? 38.245 16.727 22.870 1.00 11.78 ? 2407 HOH A O 1 HETATM 3422 O O . HOH M 7 . ? 31.752 15.375 21.294 1.00 9.11 ? 2408 HOH A O 1 HETATM 3423 O O . HOH M 7 . ? 32.744 11.993 22.296 1.00 20.15 ? 2409 HOH A O 1 HETATM 3424 O O . HOH M 7 . ? 40.693 14.378 16.278 1.00 12.25 ? 2410 HOH A O 1 HETATM 3425 O O . HOH M 7 . ? 35.028 8.719 18.413 1.00 11.32 ? 2411 HOH A O 1 HETATM 3426 O O . HOH M 7 . ? 33.308 15.368 13.325 1.00 7.83 ? 2412 HOH A O 1 HETATM 3427 O O . HOH M 7 . ? 31.655 9.923 18.281 1.00 21.35 ? 2413 HOH A O 1 HETATM 3428 O O . HOH M 7 . ? 42.471 13.669 13.778 1.00 28.47 ? 2414 HOH A O 1 HETATM 3429 O O . HOH M 7 . ? 43.459 17.114 14.376 1.00 27.89 ? 2415 HOH A O 1 HETATM 3430 O O . HOH M 7 . ? 42.542 8.418 5.992 1.00 33.85 ? 2416 HOH A O 1 HETATM 3431 O O . HOH M 7 . ? 39.220 18.061 6.093 1.00 32.41 ? 2417 HOH A O 1 HETATM 3432 O O . HOH M 7 . ? 37.239 8.364 9.655 1.00 18.19 ? 2418 HOH A O 1 HETATM 3433 O O . HOH M 7 . ? 40.388 11.449 11.256 1.00 12.18 ? 2419 HOH A O 1 HETATM 3434 O O . HOH M 7 . ? 36.763 21.534 12.093 1.00 10.10 ? 2420 HOH A O 1 HETATM 3435 O O . HOH M 7 . ? 43.107 24.417 5.155 1.00 32.55 ? 2421 HOH A O 1 HETATM 3436 O O . HOH M 7 . ? 39.371 25.980 5.448 1.00 24.47 ? 2422 HOH A O 1 HETATM 3437 O O . HOH M 7 . ? 40.468 20.720 6.016 1.00 21.07 ? 2423 HOH A O 1 HETATM 3438 O O . HOH M 7 . ? 39.421 29.647 10.536 1.00 25.94 ? 2424 HOH A O 1 HETATM 3439 O O . HOH M 7 . ? 39.570 28.048 7.219 1.00 18.11 ? 2425 HOH A O 1 HETATM 3440 O O . HOH M 7 . ? 41.509 27.624 14.487 1.00 25.01 ? 2426 HOH A O 1 HETATM 3441 O O . HOH M 7 . ? 34.495 27.471 22.542 1.00 35.48 ? 2427 HOH A O 1 HETATM 3442 O O . HOH M 7 . ? 38.708 31.099 16.957 1.00 21.30 ? 2428 HOH A O 1 HETATM 3443 O O . HOH M 7 . ? 34.993 25.799 19.765 1.00 11.44 ? 2429 HOH A O 1 HETATM 3444 O O . HOH M 7 . ? 27.130 33.121 15.254 1.00 21.78 ? 2430 HOH A O 1 HETATM 3445 O O . HOH M 7 . ? 35.521 33.843 12.904 0.40 14.06 ? 2431 HOH A O 1 HETATM 3446 O O . HOH M 7 . ? 35.959 33.122 8.735 1.00 15.72 ? 2432 HOH A O 1 HETATM 3447 O O . HOH M 7 . ? 37.296 32.664 2.926 1.00 27.19 ? 2433 HOH A O 1 HETATM 3448 O O . HOH M 7 . ? 36.008 26.350 0.823 1.00 26.50 ? 2434 HOH A O 1 HETATM 3449 O O . HOH M 7 . ? 37.543 30.324 6.932 1.00 12.54 ? 2435 HOH A O 1 HETATM 3450 O O . HOH M 7 . ? 35.606 21.728 1.556 1.00 16.23 ? 2436 HOH A O 1 HETATM 3451 O O . HOH M 7 . ? 25.069 27.756 -5.083 0.70 9.37 ? 2437 HOH A O 1 HETATM 3452 O O . HOH M 7 . ? 32.304 24.286 -7.058 1.00 29.10 ? 2438 HOH A O 1 HETATM 3453 O O . HOH M 7 . ? 29.509 25.099 -7.455 1.00 24.64 ? 2439 HOH A O 1 HETATM 3454 O O . HOH M 7 . ? 36.750 27.537 -8.436 1.00 22.62 ? 2440 HOH A O 1 HETATM 3455 O O . HOH M 7 . ? 33.122 20.000 -1.607 1.00 15.47 ? 2441 HOH A O 1 HETATM 3456 O O . HOH M 7 . ? 31.539 18.516 -3.332 1.00 14.40 ? 2442 HOH A O 1 HETATM 3457 O O . HOH M 7 . ? 25.660 24.112 -6.275 1.00 19.84 ? 2443 HOH A O 1 HETATM 3458 O O . HOH M 7 . ? 18.265 19.257 -1.577 1.00 14.44 ? 2444 HOH A O 1 HETATM 3459 O O . HOH M 7 . ? 18.143 27.018 -7.924 1.00 22.04 ? 2445 HOH A O 1 HETATM 3460 O O . HOH M 7 . ? 22.608 33.999 -7.235 1.00 31.42 ? 2446 HOH A O 1 HETATM 3461 O O . HOH M 7 . ? 19.307 32.281 -5.914 1.00 27.03 ? 2447 HOH A O 1 HETATM 3462 O O . HOH M 7 . ? 26.093 28.534 -6.368 0.30 18.29 ? 2448 HOH A O 1 HETATM 3463 O O . HOH M 7 . ? 16.361 39.671 33.860 1.00 22.23 ? 2449 HOH A O 1 HETATM 3464 O O . HOH M 7 . ? 19.198 39.839 37.052 1.00 18.69 ? 2450 HOH A O 1 HETATM 3465 O O . HOH M 7 . ? 16.051 37.044 34.677 1.00 16.77 ? 2451 HOH A O 1 HETATM 3466 O O . HOH M 7 . ? 25.060 37.992 34.156 1.00 14.60 ? 2452 HOH A O 1 HETATM 3467 O O . HOH M 7 . ? 26.451 34.797 35.529 1.00 11.74 ? 2453 HOH A O 1 HETATM 3468 O O . HOH M 7 . ? -3.100 16.512 19.351 1.00 35.61 ? 2454 HOH A O 1 HETATM 3469 O O . HOH M 7 . ? -3.055 19.424 21.121 1.00 32.66 ? 2455 HOH A O 1 HETATM 3470 O O . HOH M 7 . ? 14.037 14.805 -1.701 1.00 39.49 ? 2456 HOH A O 1 HETATM 3471 O O . HOH M 7 . ? 27.446 31.522 19.364 1.00 37.40 ? 2457 HOH A O 1 HETATM 3472 O O . HOH M 7 . ? 7.329 41.812 31.366 1.00 31.42 ? 2458 HOH A O 1 HETATM 3473 O O . HOH M 7 . ? 29.480 -0.546 13.031 1.00 28.67 ? 2459 HOH A O 1 HETATM 3474 O O . HOH M 7 . ? 25.207 -3.663 17.604 1.00 30.72 ? 2460 HOH A O 1 HETATM 3475 O O . HOH M 7 . ? 26.725 -1.591 16.703 1.00 23.76 ? 2461 HOH A O 1 HETATM 3476 O O . HOH M 7 . ? 25.208 4.578 21.503 1.00 18.84 ? 2462 HOH A O 1 HETATM 3477 O O . HOH M 7 . ? 27.408 4.597 12.263 1.00 15.70 ? 2463 HOH A O 1 HETATM 3478 O O . HOH M 7 . ? 29.163 2.998 16.155 1.00 15.10 ? 2464 HOH A O 1 HETATM 3479 O O . HOH M 7 . ? 25.642 9.014 14.414 1.00 10.29 ? 2465 HOH A O 1 HETATM 3480 O O . HOH M 7 . ? 29.704 7.195 13.715 1.00 10.27 ? 2466 HOH A O 1 HETATM 3481 O O . HOH M 7 . ? 28.752 8.177 21.979 1.00 33.90 ? 2467 HOH A O 1 HETATM 3482 O O . HOH M 7 . ? 26.748 13.118 13.282 1.00 16.11 ? 2468 HOH A O 1 HETATM 3483 O O . HOH M 7 . ? 28.872 20.012 20.613 1.00 25.94 ? 2469 HOH A O 1 HETATM 3484 O O . HOH M 7 . ? 27.862 13.688 22.437 1.00 24.05 ? 2470 HOH A O 1 HETATM 3485 O O . HOH M 7 . ? 21.641 15.040 16.993 1.00 8.89 ? 2471 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 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 GOL 1 501 501 GOL GOL A . D 3 GOL 1 502 502 GOL GOL A . E 3 GOL 1 503 503 GOL GOL A . F 3 GOL 1 504 504 GOL GOL A . G 3 GOL 1 505 505 GOL GOL A . H 3 GOL 1 506 506 GOL GOL A . I 4 MGL 1 507 507 MGL MGL A . J 5 SGC 2 508 508 SGC SGC A . K 6 BGC 3 509 509 BGC BGC A . L 6 BGC 4 510 510 BGC BGC A . M 7 HOH 1 2001 2001 HOH HOH A . M 7 HOH 2 2002 2002 HOH HOH A . M 7 HOH 3 2003 2003 HOH HOH A . M 7 HOH 4 2004 2004 HOH HOH A . M 7 HOH 5 2005 2005 HOH HOH A . M 7 HOH 6 2006 2006 HOH HOH A . M 7 HOH 7 2007 2007 HOH HOH A . M 7 HOH 8 2008 2008 HOH HOH A . M 7 HOH 9 2009 2009 HOH HOH A . M 7 HOH 10 2010 2010 HOH HOH A . M 7 HOH 11 2011 2011 HOH HOH A . M 7 HOH 12 2012 2012 HOH HOH A . M 7 HOH 13 2013 2013 HOH HOH A . M 7 HOH 14 2014 2014 HOH HOH A . M 7 HOH 15 2015 2015 HOH HOH A . M 7 HOH 16 2016 2016 HOH HOH A . M 7 HOH 17 2017 2017 HOH HOH A . M 7 HOH 18 2018 2018 HOH HOH A . M 7 HOH 19 2019 2019 HOH HOH A . M 7 HOH 20 2020 2020 HOH HOH A . M 7 HOH 21 2021 2021 HOH HOH A . M 7 HOH 22 2022 2022 HOH HOH A . M 7 HOH 23 2023 2023 HOH HOH A . M 7 HOH 24 2024 2024 HOH HOH A . M 7 HOH 25 2025 2025 HOH HOH A . M 7 HOH 26 2026 2026 HOH HOH A . M 7 HOH 27 2027 2027 HOH HOH A . M 7 HOH 28 2028 2028 HOH HOH A . M 7 HOH 29 2029 2029 HOH HOH A . M 7 HOH 30 2030 2030 HOH HOH A . M 7 HOH 31 2031 2031 HOH HOH A . M 7 HOH 32 2032 2032 HOH HOH A . M 7 HOH 33 2033 2033 HOH HOH A . M 7 HOH 34 2034 2034 HOH HOH A . M 7 HOH 35 2035 2035 HOH HOH A . M 7 HOH 36 2036 2036 HOH HOH A . M 7 HOH 37 2037 2037 HOH HOH A . M 7 HOH 38 2038 2038 HOH HOH A . M 7 HOH 39 2039 2039 HOH HOH A . M 7 HOH 40 2040 2040 HOH HOH A . M 7 HOH 41 2041 2041 HOH HOH A . M 7 HOH 42 2042 2042 HOH HOH A . M 7 HOH 43 2043 2043 HOH HOH A . M 7 HOH 44 2044 2044 HOH HOH A . M 7 HOH 45 2045 2045 HOH HOH A . M 7 HOH 46 2046 2046 HOH HOH A . M 7 HOH 47 2047 2047 HOH HOH A . M 7 HOH 48 2048 2048 HOH HOH A . M 7 HOH 49 2049 2049 HOH HOH A . M 7 HOH 50 2050 2050 HOH HOH A . M 7 HOH 51 2051 2051 HOH HOH A . M 7 HOH 52 2052 2052 HOH HOH A . M 7 HOH 53 2053 2053 HOH HOH A . M 7 HOH 54 2054 2054 HOH HOH A . M 7 HOH 55 2055 2055 HOH HOH A . M 7 HOH 56 2056 2056 HOH HOH A . M 7 HOH 57 2057 2057 HOH HOH A . M 7 HOH 58 2058 2058 HOH HOH A . M 7 HOH 59 2059 2059 HOH HOH A . M 7 HOH 60 2060 2060 HOH HOH A . M 7 HOH 61 2061 2061 HOH HOH A . M 7 HOH 62 2062 2062 HOH HOH A . M 7 HOH 63 2063 2063 HOH HOH A . M 7 HOH 64 2064 2064 HOH HOH A . M 7 HOH 65 2065 2065 HOH HOH A . M 7 HOH 66 2066 2066 HOH HOH A . M 7 HOH 67 2067 2067 HOH HOH A . M 7 HOH 68 2068 2068 HOH HOH A . M 7 HOH 69 2069 2069 HOH HOH A . M 7 HOH 70 2070 2070 HOH HOH A . M 7 HOH 71 2071 2071 HOH HOH A . M 7 HOH 72 2072 2072 HOH HOH A . M 7 HOH 73 2073 2073 HOH HOH A . M 7 HOH 74 2074 2074 HOH HOH A . M 7 HOH 75 2075 2075 HOH HOH A . M 7 HOH 76 2076 2076 HOH HOH A . M 7 HOH 77 2077 2077 HOH HOH A . M 7 HOH 78 2078 2078 HOH HOH A . M 7 HOH 79 2079 2079 HOH HOH A . M 7 HOH 80 2080 2080 HOH HOH A . M 7 HOH 81 2081 2081 HOH HOH A . M 7 HOH 82 2082 2082 HOH HOH A . M 7 HOH 83 2083 2083 HOH HOH A . M 7 HOH 84 2084 2084 HOH HOH A . M 7 HOH 85 2085 2085 HOH HOH A . M 7 HOH 86 2086 2086 HOH HOH A . M 7 HOH 87 2087 2087 HOH HOH A . M 7 HOH 88 2088 2088 HOH HOH A . M 7 HOH 89 2089 2089 HOH HOH A . M 7 HOH 90 2090 2090 HOH HOH A . M 7 HOH 91 2091 2091 HOH HOH A . M 7 HOH 92 2092 2092 HOH HOH A . M 7 HOH 93 2093 2093 HOH HOH A . M 7 HOH 94 2094 2094 HOH HOH A . M 7 HOH 95 2095 2095 HOH HOH A . M 7 HOH 96 2096 2096 HOH HOH A . M 7 HOH 97 2097 2097 HOH HOH A . M 7 HOH 98 2098 2098 HOH HOH A . M 7 HOH 99 2099 2099 HOH HOH A . M 7 HOH 100 2100 2100 HOH HOH A . M 7 HOH 101 2101 2101 HOH HOH A . M 7 HOH 102 2102 2102 HOH HOH A . M 7 HOH 103 2103 2103 HOH HOH A . M 7 HOH 104 2104 2104 HOH HOH A . M 7 HOH 105 2105 2105 HOH HOH A . M 7 HOH 106 2106 2106 HOH HOH A . M 7 HOH 107 2107 2107 HOH HOH A . M 7 HOH 108 2108 2108 HOH HOH A . M 7 HOH 109 2109 2109 HOH HOH A . M 7 HOH 110 2110 2110 HOH HOH A . M 7 HOH 111 2111 2111 HOH HOH A . M 7 HOH 112 2112 2112 HOH HOH A . M 7 HOH 113 2113 2113 HOH HOH A . M 7 HOH 114 2114 2114 HOH HOH A . M 7 HOH 115 2115 2115 HOH HOH A . M 7 HOH 116 2116 2116 HOH HOH A . M 7 HOH 117 2117 2117 HOH HOH A . M 7 HOH 118 2118 2118 HOH HOH A . M 7 HOH 119 2119 2119 HOH HOH A . M 7 HOH 120 2120 2120 HOH HOH A . M 7 HOH 121 2121 2121 HOH HOH A . M 7 HOH 122 2122 2122 HOH HOH A . M 7 HOH 123 2123 2123 HOH HOH A . M 7 HOH 124 2124 2124 HOH HOH A . M 7 HOH 125 2125 2125 HOH HOH A . M 7 HOH 126 2126 2126 HOH HOH A . M 7 HOH 127 2127 2127 HOH HOH A . M 7 HOH 128 2128 2128 HOH HOH A . M 7 HOH 129 2129 2129 HOH HOH A . M 7 HOH 130 2130 2130 HOH HOH A . M 7 HOH 131 2131 2131 HOH HOH A . M 7 HOH 132 2132 2132 HOH HOH A . M 7 HOH 133 2133 2133 HOH HOH A . M 7 HOH 134 2134 2134 HOH HOH A . M 7 HOH 135 2135 2135 HOH HOH A . M 7 HOH 136 2136 2136 HOH HOH A . M 7 HOH 137 2137 2137 HOH HOH A . M 7 HOH 138 2138 2138 HOH HOH A . M 7 HOH 139 2139 2139 HOH HOH A . M 7 HOH 140 2140 2140 HOH HOH A . M 7 HOH 141 2141 2141 HOH HOH A . M 7 HOH 142 2142 2142 HOH HOH A . M 7 HOH 143 2143 2143 HOH HOH A . M 7 HOH 144 2144 2144 HOH HOH A . M 7 HOH 145 2145 2145 HOH HOH A . M 7 HOH 146 2146 2146 HOH HOH A . M 7 HOH 147 2147 2147 HOH HOH A . M 7 HOH 148 2148 2148 HOH HOH A . M 7 HOH 149 2149 2149 HOH HOH A . M 7 HOH 150 2150 2150 HOH HOH A . M 7 HOH 151 2151 2151 HOH HOH A . M 7 HOH 152 2152 2152 HOH HOH A . M 7 HOH 153 2153 2153 HOH HOH A . M 7 HOH 154 2154 2154 HOH HOH A . M 7 HOH 155 2155 2155 HOH HOH A . M 7 HOH 156 2156 2156 HOH HOH A . M 7 HOH 157 2157 2157 HOH HOH A . M 7 HOH 158 2158 2158 HOH HOH A . M 7 HOH 159 2159 2159 HOH HOH A . M 7 HOH 160 2160 2160 HOH HOH A . M 7 HOH 161 2161 2161 HOH HOH A . M 7 HOH 162 2162 2162 HOH HOH A . M 7 HOH 163 2163 2163 HOH HOH A . M 7 HOH 164 2164 2164 HOH HOH A . M 7 HOH 165 2165 2165 HOH HOH A . M 7 HOH 166 2166 2166 HOH HOH A . M 7 HOH 167 2167 2167 HOH HOH A . M 7 HOH 168 2168 2168 HOH HOH A . M 7 HOH 169 2169 2169 HOH HOH A . M 7 HOH 170 2170 2170 HOH HOH A . M 7 HOH 171 2171 2171 HOH HOH A . M 7 HOH 172 2172 2172 HOH HOH A . M 7 HOH 173 2173 2173 HOH HOH A . M 7 HOH 174 2174 2174 HOH HOH A . M 7 HOH 175 2175 2175 HOH HOH A . M 7 HOH 176 2176 2176 HOH HOH A . M 7 HOH 177 2177 2177 HOH HOH A . M 7 HOH 178 2178 2178 HOH HOH A . M 7 HOH 179 2179 2179 HOH HOH A . M 7 HOH 180 2180 2180 HOH HOH A . M 7 HOH 181 2181 2181 HOH HOH A . M 7 HOH 182 2182 2182 HOH HOH A . M 7 HOH 183 2183 2183 HOH HOH A . M 7 HOH 184 2184 2184 HOH HOH A . M 7 HOH 185 2185 2185 HOH HOH A . M 7 HOH 186 2186 2186 HOH HOH A . M 7 HOH 187 2187 2187 HOH HOH A . M 7 HOH 188 2188 2188 HOH HOH A . M 7 HOH 189 2189 2189 HOH HOH A . M 7 HOH 190 2190 2190 HOH HOH A . M 7 HOH 191 2191 2191 HOH HOH A . M 7 HOH 192 2192 2192 HOH HOH A . M 7 HOH 193 2193 2193 HOH HOH A . M 7 HOH 194 2194 2194 HOH HOH A . M 7 HOH 195 2195 2195 HOH HOH A . M 7 HOH 196 2196 2196 HOH HOH A . M 7 HOH 197 2197 2197 HOH HOH A . M 7 HOH 198 2198 2198 HOH HOH A . M 7 HOH 199 2199 2199 HOH HOH A . M 7 HOH 200 2200 2200 HOH HOH A . M 7 HOH 201 2201 2201 HOH HOH A . M 7 HOH 202 2202 2202 HOH HOH A . M 7 HOH 203 2203 2203 HOH HOH A . M 7 HOH 204 2204 2204 HOH HOH A . M 7 HOH 205 2205 2205 HOH HOH A . M 7 HOH 206 2206 2206 HOH HOH A . M 7 HOH 207 2207 2207 HOH HOH A . M 7 HOH 208 2208 2208 HOH HOH A . M 7 HOH 209 2209 2209 HOH HOH A . M 7 HOH 210 2210 2210 HOH HOH A . M 7 HOH 211 2211 2211 HOH HOH A . M 7 HOH 212 2212 2212 HOH HOH A . M 7 HOH 213 2213 2213 HOH HOH A . M 7 HOH 214 2214 2214 HOH HOH A . M 7 HOH 215 2215 2215 HOH HOH A . M 7 HOH 216 2216 2216 HOH HOH A . M 7 HOH 217 2217 2217 HOH HOH A . M 7 HOH 218 2218 2218 HOH HOH A . M 7 HOH 219 2219 2219 HOH HOH A . M 7 HOH 220 2220 2220 HOH HOH A . M 7 HOH 221 2221 2221 HOH HOH A . M 7 HOH 222 2222 2222 HOH HOH A . M 7 HOH 223 2223 2223 HOH HOH A . M 7 HOH 224 2224 2224 HOH HOH A . M 7 HOH 225 2225 2225 HOH HOH A . M 7 HOH 226 2226 2226 HOH HOH A . M 7 HOH 227 2227 2227 HOH HOH A . M 7 HOH 228 2228 2228 HOH HOH A . M 7 HOH 229 2229 2229 HOH HOH A . M 7 HOH 230 2230 2230 HOH HOH A . M 7 HOH 231 2231 2231 HOH HOH A . M 7 HOH 232 2232 2232 HOH HOH A . M 7 HOH 233 2233 2233 HOH HOH A . M 7 HOH 234 2234 2234 HOH HOH A . M 7 HOH 235 2235 2235 HOH HOH A . M 7 HOH 236 2236 2236 HOH HOH A . M 7 HOH 237 2237 2237 HOH HOH A . M 7 HOH 238 2238 2238 HOH HOH A . M 7 HOH 239 2239 2239 HOH HOH A . M 7 HOH 240 2240 2240 HOH HOH A . M 7 HOH 241 2241 2241 HOH HOH A . M 7 HOH 242 2242 2242 HOH HOH A . M 7 HOH 243 2243 2243 HOH HOH A . M 7 HOH 244 2244 2244 HOH HOH A . M 7 HOH 245 2245 2245 HOH HOH A . M 7 HOH 246 2246 2246 HOH HOH A . M 7 HOH 247 2247 2247 HOH HOH A . M 7 HOH 248 2248 2248 HOH HOH A . M 7 HOH 249 2249 2249 HOH HOH A . M 7 HOH 250 2250 2250 HOH HOH A . M 7 HOH 251 2251 2251 HOH HOH A . M 7 HOH 252 2252 2252 HOH HOH A . M 7 HOH 253 2253 2253 HOH HOH A . M 7 HOH 254 2254 2254 HOH HOH A . M 7 HOH 255 2255 2255 HOH HOH A . M 7 HOH 256 2256 2256 HOH HOH A . M 7 HOH 257 2257 2257 HOH HOH A . M 7 HOH 258 2258 2258 HOH HOH A . M 7 HOH 259 2259 2259 HOH HOH A . M 7 HOH 260 2260 2260 HOH HOH A . M 7 HOH 261 2261 2261 HOH HOH A . M 7 HOH 262 2262 2262 HOH HOH A . M 7 HOH 263 2263 2263 HOH HOH A . M 7 HOH 264 2264 2264 HOH HOH A . M 7 HOH 265 2265 2265 HOH HOH A . M 7 HOH 266 2266 2266 HOH HOH A . M 7 HOH 267 2267 2267 HOH HOH A . M 7 HOH 268 2268 2268 HOH HOH A . M 7 HOH 269 2269 2269 HOH HOH A . M 7 HOH 270 2270 2270 HOH HOH A . M 7 HOH 271 2271 2271 HOH HOH A . M 7 HOH 272 2272 2272 HOH HOH A . M 7 HOH 273 2273 2273 HOH HOH A . M 7 HOH 274 2274 2274 HOH HOH A . M 7 HOH 275 2275 2275 HOH HOH A . M 7 HOH 276 2276 2276 HOH HOH A . M 7 HOH 277 2277 2277 HOH HOH A . M 7 HOH 278 2278 2278 HOH HOH A . M 7 HOH 279 2279 2279 HOH HOH A . M 7 HOH 280 2280 2280 HOH HOH A . M 7 HOH 281 2281 2281 HOH HOH A . M 7 HOH 282 2282 2282 HOH HOH A . M 7 HOH 283 2283 2283 HOH HOH A . M 7 HOH 284 2284 2284 HOH HOH A . M 7 HOH 285 2285 2285 HOH HOH A . M 7 HOH 286 2286 2286 HOH HOH A . M 7 HOH 287 2287 2287 HOH HOH A . M 7 HOH 288 2288 2288 HOH HOH A . M 7 HOH 289 2289 2289 HOH HOH A . M 7 HOH 290 2290 2290 HOH HOH A . M 7 HOH 291 2291 2291 HOH HOH A . M 7 HOH 292 2292 2292 HOH HOH A . M 7 HOH 293 2293 2293 HOH HOH A . M 7 HOH 294 2294 2294 HOH HOH A . M 7 HOH 295 2295 2295 HOH HOH A . M 7 HOH 296 2296 2296 HOH HOH A . M 7 HOH 297 2297 2297 HOH HOH A . M 7 HOH 298 2298 2298 HOH HOH A . M 7 HOH 299 2299 2299 HOH HOH A . M 7 HOH 300 2300 2300 HOH HOH A . M 7 HOH 301 2301 2301 HOH HOH A . M 7 HOH 302 2302 2302 HOH HOH A . M 7 HOH 303 2303 2303 HOH HOH A . M 7 HOH 304 2304 2304 HOH HOH A . M 7 HOH 305 2305 2305 HOH HOH A . M 7 HOH 306 2306 2306 HOH HOH A . M 7 HOH 307 2307 2307 HOH HOH A . M 7 HOH 308 2308 2308 HOH HOH A . M 7 HOH 309 2309 2309 HOH HOH A . M 7 HOH 310 2310 2310 HOH HOH A . M 7 HOH 311 2311 2311 HOH HOH A . M 7 HOH 312 2312 2312 HOH HOH A . M 7 HOH 313 2313 2313 HOH HOH A . M 7 HOH 314 2314 2314 HOH HOH A . M 7 HOH 315 2315 2315 HOH HOH A . M 7 HOH 316 2316 2316 HOH HOH A . M 7 HOH 317 2317 2317 HOH HOH A . M 7 HOH 318 2318 2318 HOH HOH A . M 7 HOH 319 2319 2319 HOH HOH A . M 7 HOH 320 2320 2320 HOH HOH A . M 7 HOH 321 2321 2321 HOH HOH A . M 7 HOH 322 2322 2322 HOH HOH A . M 7 HOH 323 2323 2323 HOH HOH A . M 7 HOH 324 2324 2324 HOH HOH A . M 7 HOH 325 2325 2325 HOH HOH A . M 7 HOH 326 2326 2326 HOH HOH A . M 7 HOH 327 2327 2327 HOH HOH A . M 7 HOH 328 2328 2328 HOH HOH A . M 7 HOH 329 2329 2329 HOH HOH A . M 7 HOH 330 2330 2330 HOH HOH A . M 7 HOH 331 2331 2331 HOH HOH A . M 7 HOH 332 2332 2332 HOH HOH A . M 7 HOH 333 2333 2333 HOH HOH A . M 7 HOH 334 2334 2334 HOH HOH A . M 7 HOH 335 2335 2335 HOH HOH A . M 7 HOH 336 2336 2336 HOH HOH A . M 7 HOH 337 2337 2337 HOH HOH A . M 7 HOH 338 2338 2338 HOH HOH A . M 7 HOH 339 2339 2339 HOH HOH A . M 7 HOH 340 2340 2340 HOH HOH A . M 7 HOH 341 2341 2341 HOH HOH A . M 7 HOH 342 2342 2342 HOH HOH A . M 7 HOH 343 2343 2343 HOH HOH A . M 7 HOH 344 2344 2344 HOH HOH A . M 7 HOH 345 2345 2345 HOH HOH A . M 7 HOH 346 2346 2346 HOH HOH A . M 7 HOH 347 2347 2347 HOH HOH A . M 7 HOH 348 2348 2348 HOH HOH A . M 7 HOH 349 2349 2349 HOH HOH A . M 7 HOH 350 2350 2350 HOH HOH A . M 7 HOH 351 2351 2351 HOH HOH A . M 7 HOH 352 2352 2352 HOH HOH A . M 7 HOH 353 2353 2353 HOH HOH A . M 7 HOH 354 2354 2354 HOH HOH A . M 7 HOH 355 2355 2355 HOH HOH A . M 7 HOH 356 2356 2356 HOH HOH A . M 7 HOH 357 2357 2357 HOH HOH A . M 7 HOH 358 2358 2358 HOH HOH A . M 7 HOH 359 2359 2359 HOH HOH A . M 7 HOH 360 2360 2360 HOH HOH A . M 7 HOH 361 2361 2361 HOH HOH A . M 7 HOH 362 2362 2362 HOH HOH A . M 7 HOH 363 2363 2363 HOH HOH A . M 7 HOH 364 2364 2364 HOH HOH A . M 7 HOH 365 2365 2365 HOH HOH A . M 7 HOH 366 2366 2366 HOH HOH A . M 7 HOH 367 2367 2367 HOH HOH A . M 7 HOH 368 2368 2368 HOH HOH A . M 7 HOH 369 2369 2369 HOH HOH A . M 7 HOH 370 2370 2370 HOH HOH A . M 7 HOH 371 2371 2371 HOH HOH A . M 7 HOH 372 2372 2372 HOH HOH A . M 7 HOH 373 2373 2373 HOH HOH A . M 7 HOH 374 2374 2374 HOH HOH A . M 7 HOH 375 2375 2375 HOH HOH A . M 7 HOH 376 2376 2376 HOH HOH A . M 7 HOH 377 2377 2377 HOH HOH A . M 7 HOH 378 2378 2378 HOH HOH A . M 7 HOH 379 2379 2379 HOH HOH A . M 7 HOH 380 2380 2380 HOH HOH A . M 7 HOH 381 2381 2381 HOH HOH A . M 7 HOH 382 2382 2382 HOH HOH A . M 7 HOH 383 2383 2383 HOH HOH A . M 7 HOH 384 2384 2384 HOH HOH A . M 7 HOH 385 2385 2385 HOH HOH A . M 7 HOH 386 2386 2386 HOH HOH A . M 7 HOH 387 2387 2387 HOH HOH A . M 7 HOH 388 2388 2388 HOH HOH A . M 7 HOH 389 2389 2389 HOH HOH A . M 7 HOH 390 2390 2390 HOH HOH A . M 7 HOH 391 2391 2391 HOH HOH A . M 7 HOH 392 2392 2392 HOH HOH A . M 7 HOH 393 2393 2393 HOH HOH A . M 7 HOH 394 2394 2394 HOH HOH A . M 7 HOH 395 2395 2395 HOH HOH A . M 7 HOH 396 2396 2396 HOH HOH A . M 7 HOH 397 2397 2397 HOH HOH A . M 7 HOH 398 2398 2398 HOH HOH A . M 7 HOH 399 2399 2399 HOH HOH A . M 7 HOH 400 2400 2400 HOH HOH A . M 7 HOH 401 2401 2401 HOH HOH A . M 7 HOH 402 2402 2402 HOH HOH A . M 7 HOH 403 2403 2403 HOH HOH A . M 7 HOH 404 2404 2404 HOH HOH A . M 7 HOH 405 2405 2405 HOH HOH A . M 7 HOH 406 2406 2406 HOH HOH A . M 7 HOH 407 2407 2407 HOH HOH A . M 7 HOH 408 2408 2408 HOH HOH A . M 7 HOH 409 2409 2409 HOH HOH A . M 7 HOH 410 2410 2410 HOH HOH A . M 7 HOH 411 2411 2411 HOH HOH A . M 7 HOH 412 2412 2412 HOH HOH A . M 7 HOH 413 2413 2413 HOH HOH A . M 7 HOH 414 2414 2414 HOH HOH A . M 7 HOH 415 2415 2415 HOH HOH A . M 7 HOH 416 2416 2416 HOH HOH A . M 7 HOH 417 2417 2417 HOH HOH A . M 7 HOH 418 2418 2418 HOH HOH A . M 7 HOH 419 2419 2419 HOH HOH A . M 7 HOH 420 2420 2420 HOH HOH A . M 7 HOH 421 2421 2421 HOH HOH A . M 7 HOH 422 2422 2422 HOH HOH A . M 7 HOH 423 2423 2423 HOH HOH A . M 7 HOH 424 2424 2424 HOH HOH A . M 7 HOH 425 2425 2425 HOH HOH A . M 7 HOH 426 2426 2426 HOH HOH A . M 7 HOH 427 2427 2427 HOH HOH A . M 7 HOH 428 2428 2428 HOH HOH A . M 7 HOH 429 2429 2429 HOH HOH A . M 7 HOH 430 2430 2430 HOH HOH A . M 7 HOH 431 2431 2431 HOH HOH A . M 7 HOH 432 2432 2432 HOH HOH A . M 7 HOH 433 2433 2433 HOH HOH A . M 7 HOH 434 2434 2434 HOH HOH A . M 7 HOH 435 2435 2435 HOH HOH A . M 7 HOH 436 2436 2436 HOH HOH A . M 7 HOH 437 2437 2437 HOH HOH A . M 7 HOH 438 2438 2438 HOH HOH A . M 7 HOH 439 2439 2439 HOH HOH A . M 7 HOH 440 2440 2440 HOH HOH A . M 7 HOH 441 2441 2441 HOH HOH A . M 7 HOH 442 2442 2442 HOH HOH A . M 7 HOH 443 2443 2443 HOH HOH A . M 7 HOH 444 2444 2444 HOH HOH A . M 7 HOH 445 2445 2445 HOH HOH A . M 7 HOH 446 2446 2446 HOH HOH A . M 7 HOH 447 2447 2447 HOH HOH A . M 7 HOH 448 2448 2448 HOH HOH A . M 7 HOH 449 2449 2449 HOH HOH A . M 7 HOH 450 2450 2450 HOH HOH A . M 7 HOH 451 2451 2451 HOH HOH A . M 7 HOH 452 2452 2452 HOH HOH A . M 7 HOH 453 2453 2453 HOH HOH A . M 7 HOH 454 2454 2454 HOH HOH A . M 7 HOH 455 2455 2455 HOH HOH A . M 7 HOH 456 2456 2456 HOH HOH A . M 7 HOH 457 2457 2457 HOH HOH A . M 7 HOH 458 2458 2458 HOH HOH A . M 7 HOH 459 2459 2459 HOH HOH A . M 7 HOH 460 2460 2460 HOH HOH A . M 7 HOH 461 2461 2461 HOH HOH A . M 7 HOH 462 2462 2462 HOH HOH A . M 7 HOH 463 2463 2463 HOH HOH A . M 7 HOH 464 2464 2464 HOH HOH A . M 7 HOH 465 2465 2465 HOH HOH A . M 7 HOH 466 2466 2466 HOH HOH A . M 7 HOH 467 2467 2467 HOH HOH A . M 7 HOH 468 2468 2468 HOH HOH A . M 7 HOH 469 2469 2469 HOH HOH A . M 7 HOH 470 2470 2470 HOH HOH A . M 7 HOH 471 2471 2471 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 # _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_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 AMoRE phasing . ? 4 # _pdbx_database_remark.id 700 _pdbx_database_remark.text ; SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. ; # _pdbx_entry_details.entry_id 1OC5 _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. ; # 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 NE A ARG 382 ? A CZ A ARG 382 ? A NH1 A ARG 382 ? A 123.31 120.30 3.01 0.50 N 2 1 NE A ARG 382 ? A CZ A ARG 382 ? A NH2 A ARG 382 ? A 116.31 120.30 -3.99 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 ? ? -112.35 -87.49 2 1 ASP A 175 ? ? -149.19 31.88 3 1 GLU A 224 ? ? 49.41 73.69 4 1 SER A 227 ? ? -115.88 -93.81 5 1 TRP A 274 ? ? -113.50 -76.32 6 1 PRO A 325 ? ? -104.29 40.44 # 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 2100 ? 5.87 . 2 1 O ? A HOH 2101 ? 5.93 . 3 1 O ? A HOH 2106 ? 6.78 . # _pdbx_unobs_or_zero_occ_atoms.id 1 _pdbx_unobs_or_zero_occ_atoms.PDB_model_num 1 _pdbx_unobs_or_zero_occ_atoms.polymer_flag N _pdbx_unobs_or_zero_occ_atoms.occupancy_flag 1 _pdbx_unobs_or_zero_occ_atoms.auth_asym_id A _pdbx_unobs_or_zero_occ_atoms.auth_comp_id GOL _pdbx_unobs_or_zero_occ_atoms.auth_seq_id 506 _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code ? _pdbx_unobs_or_zero_occ_atoms.auth_atom_id O3 _pdbx_unobs_or_zero_occ_atoms.label_alt_id ? _pdbx_unobs_or_zero_occ_atoms.label_asym_id H _pdbx_unobs_or_zero_occ_atoms.label_comp_id GOL _pdbx_unobs_or_zero_occ_atoms.label_seq_id 1 _pdbx_unobs_or_zero_occ_atoms.label_atom_id O3 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 GLYCEROL GOL 4 O1-METHYL-GLUCOSE MGL 5 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE SGC 6 BETA-D-GLUCOSE BGC 7 water HOH #