data_1GZ1 # _entry.id 1GZ1 # _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 1GZ1 PDBE EBI-9297 WWPDB D_1290009297 # 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 1HGW unspecified 'CEL6A D175A MUTANT' PDB 1HGY unspecified 'CEL6A D221A MUTANT' PDB 1OC5 unspecified ;D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-CELLOBIOSYL-4-DEOXY-4-THIO-BETA-D- CELLOBIOSIDE ; PDB 1OC6 unspecified 'STRUCTURE NATIVE OF THE D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS AT 1.5 ANGSTROM RESOLUTION' PDB 1OC7 unspecified ;D405N MUTANT OF THE CELLOBIOHYDROLASE CEL6A FROM HUMICOLA INSOLENS IN COMPLEX WITH METHYL-TETRATHIO-ALPHA-D-CELLOPENTOSIDE AT 1 .1 ANGSTROM RESOLUTION ; PDB 1OCB unspecified 'STRUCTURE OF THE WILD-TYPE CELLOBIOHYDROLASE CEL6A FROM HUMICOLAS INSOLENS IN COMPLEX WITH A FLUORESCENT SUBSTRATE' PDB 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 1GZ1 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2002-05-13 _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.' 2 'Driguez, H.' 3 'Davies, G.J.' 4 # _citation.id primary _citation.title ;Structure of the Humicola Insolens Cellobiohydrolase Cel6A D416A Mutant in Complex with a Non-Hydrolysable Substrate Analogue, Methyl Cellobiosyl-4-Thio-Beta-Cellobioside, at 1.9 A ; _citation.journal_abbrev 'Acta Crystallogr.,Sect.D' _citation.journal_volume 58 _citation.page_first 2201 _citation.page_last ? _citation.year 2002 _citation.journal_id_ASTM ABCRE6 _citation.country DK _citation.journal_id_ISSN 0907-4449 _citation.journal_id_CSD 0766 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 12454501 _citation.pdbx_database_id_DOI 10.1107/S0907444902017006 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Varrot, A.' 1 primary 'Frandsen, T.' 2 primary 'Driguez, H.' 3 primary 'Davies, G.J.' 4 # _cell.entry_id 1GZ1 _cell.length_a 48.257 _cell.length_b 68.380 _cell.length_c 55.180 _cell.angle_alpha 90.00 _cell.angle_beta 112.39 _cell.angle_gamma 90.00 _cell.Z_PDB 2 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1GZ1 _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'CELLOBIOHYDROLASE II' 39927.477 1 3.2.1.91 YES 'CATALYTIC CORE DOMAIN, RESIDUES 89-450' 'N-LINKED N-ACETYLGLUCOSAMINE ON RESIDUE ASN 141' 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 3 non-polymer man O1-METHYL-GLUCOSE 194.182 1 ? ? ? ? 4 non-polymer man 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE 196.221 1 ? ? ? ? 5 non-polymer man BETA-D-GLUCOSE 180.156 2 ? ? ? ? 6 non-polymer syn 'SODIUM ION' 22.990 2 ? ? ? ? 7 water nat water 18.015 270 ? ? ? ? # _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 ;YAGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQYA AQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAASTYR ELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPNPN YDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECDGTS DTTAARYAYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF ; _entity_poly.pdbx_seq_one_letter_code_can ;YAGNPFEGVQLWANNYYRSEVHTLAIPQITDPALRAAASAVAEVPSFQWLDRNVTVDTLLVQTLSEIREANQAGANPQYA AQIVVYDLPDRDCAAAASNGEWAIANNGVNNYKAYINRIREILISFSDVRTILVIEPDSLANMVTNMNVPKCSGAASTYR ELTIYALKQLDLPHVAMYMDAGHAGWLGWPANIQPAAELFAKIYEDAGKPRAVRGLATNVANYNAWSVSSPPPYTSPNPN YDEKHYIEAFRPLLEARGFPAQFIVDQGRSGKQPTGQKEWGHWCNAIGTGFGMRPTANTGHQYVDAFVWVKPGGECDGTS DTTAARYAYHCGLEDALKPAPEAGQWFNEYFIQLLRNANPPF ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 TYR n 1 2 ALA n 1 3 GLY n 1 4 ASN n 1 5 PRO n 1 6 PHE n 1 7 GLU n 1 8 GLY n 1 9 VAL n 1 10 GLN n 1 11 LEU n 1 12 TRP n 1 13 ALA n 1 14 ASN n 1 15 ASN n 1 16 TYR n 1 17 TYR n 1 18 ARG n 1 19 SER n 1 20 GLU n 1 21 VAL n 1 22 HIS n 1 23 THR n 1 24 LEU n 1 25 ALA n 1 26 ILE n 1 27 PRO n 1 28 GLN n 1 29 ILE n 1 30 THR n 1 31 ASP n 1 32 PRO n 1 33 ALA n 1 34 LEU n 1 35 ARG n 1 36 ALA n 1 37 ALA n 1 38 ALA n 1 39 SER n 1 40 ALA n 1 41 VAL n 1 42 ALA n 1 43 GLU n 1 44 VAL n 1 45 PRO n 1 46 SER n 1 47 PHE n 1 48 GLN n 1 49 TRP n 1 50 LEU n 1 51 ASP n 1 52 ARG n 1 53 ASN n 1 54 VAL n 1 55 THR n 1 56 VAL n 1 57 ASP n 1 58 THR n 1 59 LEU n 1 60 LEU n 1 61 VAL n 1 62 GLN n 1 63 THR n 1 64 LEU n 1 65 SER n 1 66 GLU n 1 67 ILE n 1 68 ARG n 1 69 GLU n 1 70 ALA n 1 71 ASN n 1 72 GLN n 1 73 ALA n 1 74 GLY n 1 75 ALA n 1 76 ASN n 1 77 PRO n 1 78 GLN n 1 79 TYR n 1 80 ALA n 1 81 ALA n 1 82 GLN n 1 83 ILE n 1 84 VAL n 1 85 VAL n 1 86 TYR n 1 87 ASP n 1 88 LEU n 1 89 PRO n 1 90 ASP n 1 91 ARG n 1 92 ASP n 1 93 CYS n 1 94 ALA n 1 95 ALA n 1 96 ALA n 1 97 ALA n 1 98 SER n 1 99 ASN n 1 100 GLY n 1 101 GLU n 1 102 TRP n 1 103 ALA n 1 104 ILE n 1 105 ALA n 1 106 ASN n 1 107 ASN n 1 108 GLY n 1 109 VAL n 1 110 ASN n 1 111 ASN n 1 112 TYR n 1 113 LYS n 1 114 ALA n 1 115 TYR n 1 116 ILE n 1 117 ASN n 1 118 ARG n 1 119 ILE n 1 120 ARG n 1 121 GLU n 1 122 ILE n 1 123 LEU n 1 124 ILE n 1 125 SER n 1 126 PHE n 1 127 SER n 1 128 ASP n 1 129 VAL n 1 130 ARG n 1 131 THR n 1 132 ILE n 1 133 LEU n 1 134 VAL n 1 135 ILE n 1 136 GLU n 1 137 PRO n 1 138 ASP n 1 139 SER n 1 140 LEU n 1 141 ALA n 1 142 ASN n 1 143 MET n 1 144 VAL n 1 145 THR n 1 146 ASN n 1 147 MET n 1 148 ASN n 1 149 VAL n 1 150 PRO n 1 151 LYS n 1 152 CYS n 1 153 SER n 1 154 GLY n 1 155 ALA n 1 156 ALA n 1 157 SER n 1 158 THR n 1 159 TYR n 1 160 ARG n 1 161 GLU n 1 162 LEU n 1 163 THR n 1 164 ILE n 1 165 TYR n 1 166 ALA n 1 167 LEU n 1 168 LYS n 1 169 GLN n 1 170 LEU n 1 171 ASP n 1 172 LEU n 1 173 PRO n 1 174 HIS n 1 175 VAL n 1 176 ALA n 1 177 MET n 1 178 TYR n 1 179 MET n 1 180 ASP n 1 181 ALA n 1 182 GLY n 1 183 HIS n 1 184 ALA n 1 185 GLY n 1 186 TRP n 1 187 LEU n 1 188 GLY n 1 189 TRP n 1 190 PRO n 1 191 ALA n 1 192 ASN n 1 193 ILE n 1 194 GLN n 1 195 PRO n 1 196 ALA n 1 197 ALA n 1 198 GLU n 1 199 LEU n 1 200 PHE n 1 201 ALA n 1 202 LYS n 1 203 ILE n 1 204 TYR n 1 205 GLU n 1 206 ASP n 1 207 ALA n 1 208 GLY n 1 209 LYS n 1 210 PRO n 1 211 ARG n 1 212 ALA n 1 213 VAL n 1 214 ARG n 1 215 GLY n 1 216 LEU n 1 217 ALA n 1 218 THR n 1 219 ASN n 1 220 VAL n 1 221 ALA n 1 222 ASN n 1 223 TYR n 1 224 ASN n 1 225 ALA n 1 226 TRP n 1 227 SER n 1 228 VAL n 1 229 SER n 1 230 SER n 1 231 PRO n 1 232 PRO n 1 233 PRO n 1 234 TYR n 1 235 THR n 1 236 SER n 1 237 PRO n 1 238 ASN n 1 239 PRO n 1 240 ASN n 1 241 TYR n 1 242 ASP n 1 243 GLU n 1 244 LYS n 1 245 HIS n 1 246 TYR n 1 247 ILE n 1 248 GLU n 1 249 ALA n 1 250 PHE n 1 251 ARG n 1 252 PRO n 1 253 LEU n 1 254 LEU n 1 255 GLU n 1 256 ALA n 1 257 ARG n 1 258 GLY n 1 259 PHE n 1 260 PRO n 1 261 ALA n 1 262 GLN n 1 263 PHE n 1 264 ILE n 1 265 VAL n 1 266 ASP n 1 267 GLN n 1 268 GLY n 1 269 ARG n 1 270 SER n 1 271 GLY n 1 272 LYS n 1 273 GLN n 1 274 PRO n 1 275 THR n 1 276 GLY n 1 277 GLN n 1 278 LYS n 1 279 GLU n 1 280 TRP n 1 281 GLY n 1 282 HIS n 1 283 TRP n 1 284 CYS n 1 285 ASN n 1 286 ALA n 1 287 ILE n 1 288 GLY n 1 289 THR n 1 290 GLY n 1 291 PHE n 1 292 GLY n 1 293 MET n 1 294 ARG n 1 295 PRO n 1 296 THR n 1 297 ALA n 1 298 ASN n 1 299 THR n 1 300 GLY n 1 301 HIS n 1 302 GLN n 1 303 TYR n 1 304 VAL n 1 305 ASP n 1 306 ALA n 1 307 PHE n 1 308 VAL n 1 309 TRP n 1 310 VAL n 1 311 LYS n 1 312 PRO n 1 313 GLY n 1 314 GLY n 1 315 GLU n 1 316 CYS n 1 317 ASP n 1 318 GLY n 1 319 THR n 1 320 SER n 1 321 ASP n 1 322 THR n 1 323 THR n 1 324 ALA n 1 325 ALA n 1 326 ARG n 1 327 TYR n 1 328 ALA n 1 329 TYR n 1 330 HIS n 1 331 CYS n 1 332 GLY n 1 333 LEU n 1 334 GLU n 1 335 ASP n 1 336 ALA n 1 337 LEU n 1 338 LYS n 1 339 PRO n 1 340 ALA n 1 341 PRO n 1 342 GLU n 1 343 ALA n 1 344 GLY n 1 345 GLN n 1 346 TRP n 1 347 PHE n 1 348 ASN n 1 349 GLU n 1 350 TYR n 1 351 PHE n 1 352 ILE n 1 353 GLN n 1 354 LEU n 1 355 LEU n 1 356 ARG n 1 357 ASN n 1 358 ALA n 1 359 ASN n 1 360 PRO n 1 361 PRO n 1 362 PHE n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'HUMICOLA INSOLENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 34413 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name 'ASPERGILLUS ORYZAE' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 5062 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description 'UNDER CONTROL OF THE FUNGAL AMYLASEURCE 6 PROMOTER AND AMYLOGLUCOSIDASE TERMINATOR' # _struct_ref.id 1 _struct_ref.db_name PDB _struct_ref.db_code 1GZ1 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession 1GZ1 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1GZ1 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 1 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 362 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession 1GZ1 _struct_ref_seq.db_align_beg 89 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 450 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 89 _struct_ref_seq.pdbx_auth_seq_align_end 450 # loop_ _chem_comp.id _chem_comp.type _chem_comp.mon_nstd_flag _chem_comp.name _chem_comp.pdbx_synonyms _chem_comp.formula _chem_comp.formula_weight ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 BGC saccharide . BETA-D-GLUCOSE ? 'C6 H12 O6' 180.156 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 MGL saccharide . O1-METHYL-GLUCOSE ? 'C7 H14 O6' 194.182 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 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 1GZ1 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.01 _exptl_crystal.density_percent_sol 42.0 _exptl_crystal.description 'SEARCH MODEL WAS THE D405N MUTANT OF HUMICOLA INSOLENS CELLOBIOHYDROLASE CEL6A IN COMPLEX WITH CELLOTRIOSE' # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 4.60 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details ;PROTEIN WAS CONCENTRATED TO 20 MG/ML IN WATER. CRYSTALLISATION IN 200MM MAGNESIUM ACETATE IN 100MM SODIUM ACETATE BUFFER AT PH 4.6. PRECIPITANT WAS 20%. POLYETHYLENE GLYCOL 5500. ; # _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 2001-10-15 _diffrn_detector.details 'TORROIDAL MIRROR' # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'DIAMOND (111), GE(220)' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 0.933 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID14-2' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID14-2 _diffrn_source.pdbx_wavelength 0.933 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 1GZ1 _reflns.observed_criterion_sigma_I 0.000 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 30.000 _reflns.d_resolution_high 1.900 _reflns.number_obs 26197 _reflns.number_all ? _reflns.percent_possible_obs 99.1 _reflns.pdbx_Rmerge_I_obs 0.06200 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 21.2000 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.800 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 1.90 _reflns_shell.d_res_low 1.93 _reflns_shell.percent_possible_all 98.0 _reflns_shell.Rmerge_I_obs 0.28000 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 4.600 _reflns_shell.pdbx_redundancy 3.70 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 1GZ1 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 24685 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 30.00 _refine.ls_d_res_high 1.90 _refine.ls_percent_reflns_obs 99.2 _refine.ls_R_factor_obs 0.168 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.166 _refine.ls_R_factor_R_free 0.211 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.100 _refine.ls_number_reflns_R_free 1324 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.958 _refine.correlation_coeff_Fo_to_Fc_free 0.935 _refine.B_iso_mean 17.18 _refine.aniso_B[1][1] -0.80000 _refine.aniso_B[2][2] -0.71000 _refine.aniso_B[3][3] 0.70000 _refine.aniso_B[1][2] 0.00000 _refine.aniso_B[1][3] -1.06000 _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 ? _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 0.165 _refine.pdbx_overall_ESU_R_Free 0.147 _refine.overall_SU_ML 0.152 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 5.047 _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 2821 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 62 _refine_hist.number_atoms_solvent 270 _refine_hist.number_atoms_total 3153 _refine_hist.d_res_high 1.90 _refine_hist.d_res_low 30.00 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.014 0.021 ? 2977 'X-RAY DIFFRACTION' ? r_bond_other_d 0.002 0.020 ? 2555 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.573 1.947 ? 4074 'X-RAY DIFFRACTION' ? r_angle_other_deg 2.009 3.000 ? 5942 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 5.001 3.000 ? 361 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 18.757 15.000 ? 471 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_chiral_restr 0.105 0.200 ? 441 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.006 0.020 ? 3340 'X-RAY DIFFRACTION' ? r_gen_planes_other 0.003 0.020 ? 603 'X-RAY DIFFRACTION' ? r_nbd_refined 0.244 0.300 ? 672 'X-RAY DIFFRACTION' ? r_nbd_other 0.216 0.300 ? 2585 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other 0.655 0.500 ? 2 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined 0.133 0.500 ? 259 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other 0.100 0.500 ? 3 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined 0.358 0.300 ? 5 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other 0.301 0.300 ? 29 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined 0.224 0.500 ? 9 '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 0.837 1.500 ? 1812 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it 1.466 2.000 ? 2909 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it 2.206 3.000 ? 1165 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it 3.508 4.500 ? 1165 '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 1.90 _refine_ls_shell.d_res_low 1.95 _refine_ls_shell.number_reflns_R_work 1803 _refine_ls_shell.R_factor_R_work 0.1940 _refine_ls_shell.percent_reflns_obs ? _refine_ls_shell.R_factor_R_free 0.2450 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 90 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 1GZ1 _struct.title ;Mutant D416A 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 1GZ1 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, CELLULOSE DEGRADATION, CELLOBIOHYDROLASE, CELLULASE, GLYCOSIDE HYDROLASE FAMILY 6, THIOOLIGOSACCHARIDE' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 5 ? F N N 5 ? G N N 6 ? H N N 6 ? I N N 7 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 14 ? ALA A 25 ? ASN A 102 ALA A 113 1 ? 12 HELX_P HELX_P2 2 ILE A 26 ? ILE A 29 ? ILE A 114 ILE A 117 5 ? 4 HELX_P HELX_P3 3 ASP A 31 ? ALA A 42 ? ASP A 119 ALA A 130 1 ? 12 HELX_P HELX_P4 4 ARG A 52 ? VAL A 56 ? ARG A 140 VAL A 144 5 ? 5 HELX_P HELX_P5 5 THR A 58 ? ALA A 73 ? THR A 146 ALA A 161 1 ? 16 HELX_P HELX_P6 6 ALA A 103 ? ASN A 106 ? ALA A 191 ASN A 194 5 ? 4 HELX_P HELX_P7 7 ASN A 107 ? PHE A 126 ? ASN A 195 PHE A 214 1 ? 20 HELX_P HELX_P8 8 LEU A 140 ? ASN A 146 ? LEU A 228 ASN A 234 1 ? 7 HELX_P HELX_P9 9 VAL A 149 ? LEU A 170 ? VAL A 237 LEU A 258 1 ? 22 HELX_P HELX_P10 10 TRP A 189 ? ALA A 207 ? TRP A 277 ALA A 295 1 ? 19 HELX_P HELX_P11 11 PRO A 232 ? SER A 236 ? PRO A 320 SER A 324 5 ? 5 HELX_P HELX_P12 12 ASP A 242 ? ARG A 257 ? ASP A 330 ARG A 345 1 ? 16 HELX_P HELX_P13 13 ALA A 328 ? LEU A 333 ? ALA A 416 LEU A 421 5 ? 6 HELX_P HELX_P14 14 PHE A 347 ? ASN A 357 ? PHE A 435 ASN A 445 1 ? 11 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 93 SG ? ? ? 1_555 A CYS 152 SG ? ? A CYS 181 A CYS 240 1_555 ? ? ? ? ? ? ? 2.108 ? disulf2 disulf ? ? A CYS 284 SG ? ? ? 1_555 A CYS 331 SG ? ? A CYS 372 A CYS 419 1_555 ? ? ? ? ? ? ? 2.021 ? covale1 covale ? ? A ASN 53 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 141 A NAG 500 1_555 ? ? ? ? ? ? ? 1.457 ? covale2 covale ? ? C MGL . O4 ? ? ? 1_555 D SGC . C1 ? ? A MGL 501 A SGC 502 1_555 ? ? ? ? ? ? ? 1.492 ? covale3 covale ? ? D SGC . S4 ? ? ? 1_555 E BGC . C1 ? ? A SGC 502 A BGC 503 1_555 ? ? ? ? ? ? ? 1.819 ? covale4 covale ? ? E BGC . O4 ? ? ? 1_555 F BGC . C1 ? ? A BGC 503 A BGC 504 1_555 ? ? ? ? ? ? ? 1.448 ? metalc1 metalc ? ? G NA . NA ? ? ? 1_555 A GLU 69 OE1 ? ? A NA 505 A GLU 157 1_555 ? ? ? ? ? ? ? 2.223 ? metalc2 metalc ? ? H NA . NA ? ? ? 1_555 A GLU 198 OE1 ? ? A NA 506 A GLU 286 1_555 ? ? ? ? ? ? ? 2.227 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ASN 76 A . ? ASN 164 A PRO 77 A ? PRO 165 A 1 1.73 2 SER 236 A . ? SER 324 A PRO 237 A ? PRO 325 A 1 0.67 3 GLN 273 A . ? GLN 361 A PRO 274 A ? PRO 362 A 1 -3.57 4 LYS 338 A . ? LYS 426 A PRO 339 A ? PRO 427 A 1 -4.04 5 ASN 359 A . ? ASN 447 A PRO 360 A ? PRO 448 A 1 -1.09 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 3 ? AB ? 7 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense AA 1 2 ? parallel AA 2 3 ? parallel AB 1 2 ? parallel AB 2 3 ? parallel AB 3 4 ? parallel AB 4 5 ? parallel AB 5 6 ? parallel AB 6 7 ? parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id AA 1 GLN A 10 ? LEU A 11 ? GLN A 98 LEU A 99 AA 2 TYR A 79 ? VAL A 85 ? TYR A 167 VAL A 173 AA 3 GLN A 48 ? LEU A 50 ? GLN A 136 LEU A 138 AB 1 GLN A 10 ? LEU A 11 ? GLN A 98 LEU A 99 AB 2 TYR A 79 ? VAL A 85 ? TYR A 167 VAL A 173 AB 3 THR A 131 ? ILE A 135 ? THR A 219 ILE A 223 AB 4 VAL A 175 ? ASP A 180 ? VAL A 263 ASP A 268 AB 5 VAL A 213 ? THR A 218 ? VAL A 301 THR A 306 AB 6 GLN A 262 ? ASP A 266 ? GLN A 350 ASP A 354 AB 7 VAL A 304 ? VAL A 308 ? VAL A 392 VAL A 396 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id AA 1 2 O GLN A 10 ? O GLN A 98 N ALA A 80 ? N ALA A 168 AA 2 3 N VAL A 84 ? N VAL A 172 O GLN A 48 ? O GLN A 136 AB 1 2 O GLN A 10 ? O GLN A 98 N ALA A 80 ? N ALA A 168 AB 2 3 N ILE A 83 ? N ILE A 171 O ILE A 132 ? O ILE A 220 AB 3 4 N LEU A 133 ? N LEU A 221 O ALA A 176 ? O ALA A 264 AB 4 5 O MET A 177 ? O MET A 265 N ARG A 214 ? N ARG A 302 AB 5 6 N LEU A 216 ? N LEU A 304 O GLN A 262 ? O GLN A 350 AB 6 7 O PHE A 263 ? O PHE A 351 N ASP A 305 ? N ASP A 393 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NA A 505' AC2 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NA A 506' AC3 Software ? ? ? ? 6 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 141 RESIDUES 500 TO 500' AC4 Software ? ? ? ? 28 'BINDING SITE FOR CHAIN A OF POLYSACCHARIDE RESIDUES 501 TO 504' # 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 3 GLU A 69 ? GLU A 157 . ? 1_555 ? 2 AC1 3 TYR A 241 ? TYR A 329 . ? 1_455 ? 3 AC1 3 HOH I . ? HOH A 2051 . ? 1_555 ? 4 AC2 2 GLU A 198 ? GLU A 286 . ? 1_555 ? 5 AC2 2 HOH I . ? HOH A 2154 . ? 1_555 ? 6 AC3 6 ASN A 53 ? ASN A 141 . ? 1_555 ? 7 AC3 6 ASP A 57 ? ASP A 145 . ? 1_555 ? 8 AC3 6 ASN A 111 ? ASN A 199 . ? 1_555 ? 9 AC3 6 HOH I . ? HOH A 2040 . ? 1_555 ? 10 AC3 6 HOH I . ? HOH A 2100 . ? 1_555 ? 11 AC3 6 HOH I . ? HOH A 2261 . ? 1_555 ? 12 AC4 28 TRP A 49 ? TRP A 137 . ? 1_555 ? 13 AC4 28 ASP A 51 ? ASP A 139 . ? 1_555 ? 14 AC4 28 TYR A 86 ? TYR A 174 . ? 1_555 ? 15 AC4 28 ARG A 91 ? ARG A 179 . ? 1_555 ? 16 AC4 28 ASN A 146 ? ASN A 234 . ? 1_555 ? 17 AC4 28 HIS A 183 ? HIS A 271 . ? 1_555 ? 18 AC4 28 GLY A 185 ? GLY A 273 . ? 1_555 ? 19 AC4 28 TRP A 186 ? TRP A 274 . ? 1_555 ? 20 AC4 28 ALA A 221 ? ALA A 309 . ? 1_555 ? 21 AC4 28 ASN A 222 ? ASN A 310 . ? 1_555 ? 22 AC4 28 GLY A 281 ? GLY A 369 . ? 1_555 ? 23 AC4 28 TRP A 283 ? TRP A 371 . ? 1_555 ? 24 AC4 28 LYS A 311 ? LYS A 399 . ? 1_555 ? 25 AC4 28 PRO A 312 ? PRO A 400 . ? 1_555 ? 26 AC4 28 GLU A 315 ? GLU A 403 . ? 1_555 ? 27 AC4 28 ASP A 317 ? ASP A 405 . ? 1_555 ? 28 AC4 28 GLY A 344 ? GLY A 432 . ? 1_555 ? 29 AC4 28 HOH I . ? HOH A 2120 . ? 1_555 ? 30 AC4 28 HOH I . ? HOH A 2166 . ? 1_555 ? 31 AC4 28 HOH I . ? HOH A 2205 . ? 1_555 ? 32 AC4 28 HOH I . ? HOH A 2222 . ? 1_555 ? 33 AC4 28 HOH I . ? HOH A 2264 . ? 1_555 ? 34 AC4 28 HOH I . ? HOH A 2265 . ? 1_555 ? 35 AC4 28 HOH I . ? HOH A 2266 . ? 1_555 ? 36 AC4 28 HOH I . ? HOH A 2267 . ? 1_555 ? 37 AC4 28 HOH I . ? HOH A 2268 . ? 1_555 ? 38 AC4 28 HOH I . ? HOH A 2269 . ? 1_555 ? 39 AC4 28 HOH I . ? HOH A 2270 . ? 1_555 ? # _database_PDB_matrix.entry_id 1GZ1 _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 1GZ1 _atom_sites.fract_transf_matrix[1][1] 0.020722 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.008537 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.014624 _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] 0.019600 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N NA O S # 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 . TYR A 1 1 ? 10.029 20.344 1.258 1.00 35.48 ? 89 TYR A N 1 ATOM 2 C CA . TYR A 1 1 ? 9.012 20.634 2.308 1.00 35.33 ? 89 TYR A CA 1 ATOM 3 C C . TYR A 1 1 ? 9.672 20.894 3.665 1.00 35.68 ? 89 TYR A C 1 ATOM 4 O O . TYR A 1 1 ? 10.400 20.031 4.166 1.00 35.97 ? 89 TYR A O 1 ATOM 5 C CB . TYR A 1 1 ? 8.028 19.471 2.437 1.00 35.23 ? 89 TYR A CB 1 ATOM 6 C CG . TYR A 1 1 ? 6.882 19.835 3.342 1.00 33.16 ? 89 TYR A CG 1 ATOM 7 C CD1 . TYR A 1 1 ? 5.878 20.665 2.887 1.00 31.58 ? 89 TYR A CD1 1 ATOM 8 C CD2 . TYR A 1 1 ? 6.843 19.414 4.670 1.00 31.51 ? 89 TYR A CD2 1 ATOM 9 C CE1 . TYR A 1 1 ? 4.851 21.050 3.698 1.00 31.81 ? 89 TYR A CE1 1 ATOM 10 C CE2 . TYR A 1 1 ? 5.807 19.792 5.503 1.00 32.81 ? 89 TYR A CE2 1 ATOM 11 C CZ . TYR A 1 1 ? 4.813 20.617 5.003 1.00 32.03 ? 89 TYR A CZ 1 ATOM 12 O OH . TYR A 1 1 ? 3.775 21.017 5.789 1.00 31.12 ? 89 TYR A OH 1 ATOM 13 N N . ALA A 1 2 ? 9.539 22.120 4.182 1.00 35.81 ? 90 ALA A N 1 ATOM 14 C CA . ALA A 1 2 ? 9.994 22.476 5.523 1.00 35.22 ? 90 ALA A CA 1 ATOM 15 C C . ALA A 1 2 ? 8.912 22.404 6.608 1.00 34.48 ? 90 ALA A C 1 ATOM 16 O O . ALA A 1 2 ? 7.986 23.239 6.649 1.00 35.81 ? 90 ALA A O 1 ATOM 17 C CB . ALA A 1 2 ? 10.600 23.876 5.491 1.00 35.83 ? 90 ALA A CB 1 ATOM 18 N N . GLY A 1 3 ? 9.070 21.437 7.512 1.00 32.49 ? 91 GLY A N 1 ATOM 19 C CA . GLY A 1 3 ? 8.121 21.206 8.588 1.00 30.27 ? 91 GLY A CA 1 ATOM 20 C C . GLY A 1 3 ? 8.204 19.775 9.111 1.00 27.56 ? 91 GLY A C 1 ATOM 21 O O . GLY A 1 3 ? 7.985 18.802 8.410 1.00 28.14 ? 91 GLY A O 1 ATOM 22 N N . ASN A 1 4 ? 8.556 19.648 10.374 1.00 25.18 ? 92 ASN A N 1 ATOM 23 C CA . ASN A 1 4 ? 8.619 18.344 11.001 1.00 22.55 ? 92 ASN A CA 1 ATOM 24 C C . ASN A 1 4 ? 7.202 17.879 11.299 1.00 20.51 ? 92 ASN A C 1 ATOM 25 O O . ASN A 1 4 ? 6.527 18.516 12.041 1.00 19.58 ? 92 ASN A O 1 ATOM 26 C CB . ASN A 1 4 ? 9.418 18.455 12.285 1.00 22.00 ? 92 ASN A CB 1 ATOM 27 C CG . ASN A 1 4 ? 9.444 17.161 13.061 1.00 20.38 ? 92 ASN A CG 1 ATOM 28 O OD1 . ASN A 1 4 ? 8.792 16.203 12.686 1.00 19.13 ? 92 ASN A OD1 1 ATOM 29 N ND2 . ASN A 1 4 ? 10.203 17.138 14.146 1.00 17.55 ? 92 ASN A ND2 1 ATOM 30 N N . PRO A 1 5 ? 6.748 16.787 10.700 1.00 19.33 ? 93 PRO A N 1 ATOM 31 C CA . PRO A 1 5 ? 5.385 16.315 10.897 1.00 17.91 ? 93 PRO A CA 1 ATOM 32 C C . PRO A 1 5 ? 5.063 15.928 12.323 1.00 17.10 ? 93 PRO A C 1 ATOM 33 O O . PRO A 1 5 ? 3.887 15.849 12.651 1.00 16.64 ? 93 PRO A O 1 ATOM 34 C CB . PRO A 1 5 ? 5.293 15.079 9.995 1.00 18.96 ? 93 PRO A CB 1 ATOM 35 C CG . PRO A 1 5 ? 6.668 14.737 9.603 1.00 19.44 ? 93 PRO A CG 1 ATOM 36 C CD . PRO A 1 5 ? 7.500 15.916 9.799 1.00 19.86 ? 93 PRO A CD 1 ATOM 37 N N . PHE A 1 6 ? 6.068 15.677 13.157 1.00 16.60 ? 94 PHE A N 1 ATOM 38 C CA . PHE A 1 6 ? 5.825 15.319 14.549 1.00 16.21 ? 94 PHE A CA 1 ATOM 39 C C . PHE A 1 6 ? 5.691 16.537 15.447 1.00 16.82 ? 94 PHE A C 1 ATOM 40 O O . PHE A 1 6 ? 5.340 16.426 16.608 1.00 17.34 ? 94 PHE A O 1 ATOM 41 C CB . PHE A 1 6 ? 6.972 14.449 15.059 1.00 16.00 ? 94 PHE A CB 1 ATOM 42 C CG . PHE A 1 6 ? 6.926 13.050 14.512 1.00 14.75 ? 94 PHE A CG 1 ATOM 43 C CD1 . PHE A 1 6 ? 7.467 12.759 13.296 1.00 15.53 ? 94 PHE A CD1 1 ATOM 44 C CD2 . PHE A 1 6 ? 6.266 12.056 15.198 1.00 16.45 ? 94 PHE A CD2 1 ATOM 45 C CE1 . PHE A 1 6 ? 7.391 11.477 12.776 1.00 16.47 ? 94 PHE A CE1 1 ATOM 46 C CE2 . PHE A 1 6 ? 6.211 10.779 14.695 1.00 16.49 ? 94 PHE A CE2 1 ATOM 47 C CZ . PHE A 1 6 ? 6.766 10.499 13.487 1.00 15.39 ? 94 PHE A CZ 1 ATOM 48 N N . GLU A 1 7 ? 6.043 17.691 14.920 1.00 18.39 ? 95 GLU A N 1 ATOM 49 C CA . GLU A 1 7 ? 6.048 18.887 15.719 1.00 20.27 ? 95 GLU A CA 1 ATOM 50 C C . GLU A 1 7 ? 4.660 19.487 15.794 1.00 19.55 ? 95 GLU A C 1 ATOM 51 O O . GLU A 1 7 ? 3.954 19.602 14.790 1.00 18.84 ? 95 GLU A O 1 ATOM 52 C CB . GLU A 1 7 ? 7.075 19.861 15.129 1.00 21.09 ? 95 GLU A CB 1 ATOM 53 C CG . GLU A 1 7 ? 6.947 21.294 15.587 1.00 26.46 ? 95 GLU A CG 1 ATOM 54 C CD . GLU A 1 7 ? 8.049 22.192 15.000 1.00 33.11 ? 95 GLU A CD 1 ATOM 55 O OE1 . GLU A 1 7 ? 8.633 21.861 13.922 1.00 35.81 ? 95 GLU A OE1 1 ATOM 56 O OE2 . GLU A 1 7 ? 8.329 23.247 15.617 1.00 37.41 ? 95 GLU A OE2 1 ATOM 57 N N . GLY A 1 8 ? 4.251 19.833 17.004 1.00 19.68 ? 96 GLY A N 1 ATOM 58 C CA . GLY A 1 8 ? 2.991 20.504 17.237 1.00 19.69 ? 96 GLY A CA 1 ATOM 59 C C . GLY A 1 8 ? 1.762 19.614 17.252 1.00 19.04 ? 96 GLY A C 1 ATOM 60 O O . GLY A 1 8 ? 0.672 20.129 17.121 1.00 18.57 ? 96 GLY A O 1 ATOM 61 N N . VAL A 1 9 ? 1.952 18.293 17.364 1.00 18.18 ? 97 VAL A N 1 ATOM 62 C CA . VAL A 1 9 ? 0.863 17.350 17.430 1.00 17.51 ? 97 VAL A CA 1 ATOM 63 C C . VAL A 1 9 ? 1.154 16.402 18.556 1.00 17.47 ? 97 VAL A C 1 ATOM 64 O O . VAL A 1 9 ? 2.283 16.305 18.993 1.00 17.24 ? 97 VAL A O 1 ATOM 65 C CB . VAL A 1 9 ? 0.686 16.484 16.160 1.00 17.10 ? 97 VAL A CB 1 ATOM 66 C CG1 . VAL A 1 9 ? 0.080 17.296 15.039 1.00 18.60 ? 97 VAL A CG1 1 ATOM 67 C CG2 . VAL A 1 9 ? 1.993 15.831 15.693 1.00 16.79 ? 97 VAL A CG2 1 ATOM 68 N N . GLN A 1 10 ? 0.101 15.749 19.025 1.00 17.08 ? 98 GLN A N 1 ATOM 69 C CA . GLN A 1 10 ? 0.166 14.674 19.956 1.00 18.13 ? 98 GLN A CA 1 ATOM 70 C C . GLN A 1 10 ? 0.096 13.443 19.072 1.00 17.53 ? 98 GLN A C 1 ATOM 71 O O . GLN A 1 10 ? -0.441 13.504 17.960 1.00 17.72 ? 98 GLN A O 1 ATOM 72 C CB . GLN A 1 10 ? -1.058 14.658 20.857 1.00 19.16 ? 98 GLN A CB 1 ATOM 73 C CG . GLN A 1 10 ? -1.136 15.753 21.875 1.00 21.08 ? 98 GLN A CG 1 ATOM 74 C CD . GLN A 1 10 ? -2.197 15.441 22.879 1.00 22.70 ? 98 GLN A CD 1 ATOM 75 O OE1 . GLN A 1 10 ? -2.029 14.545 23.715 1.00 25.40 ? 98 GLN A OE1 1 ATOM 76 N NE2 . GLN A 1 10 ? -3.322 16.111 22.766 1.00 21.33 ? 98 GLN A NE2 1 ATOM 77 N N . LEU A 1 11 ? 0.613 12.329 19.568 1.00 16.63 ? 99 LEU A N 1 ATOM 78 C CA . LEU A 1 11 ? 0.593 11.087 18.809 1.00 15.79 ? 99 LEU A CA 1 ATOM 79 C C . LEU A 1 11 ? -0.445 10.182 19.412 1.00 15.57 ? 99 LEU A C 1 ATOM 80 O O . LEU A 1 11 ? -0.409 9.947 20.602 1.00 15.73 ? 99 LEU A O 1 ATOM 81 C CB . LEU A 1 11 ? 1.965 10.429 18.878 1.00 15.89 ? 99 LEU A CB 1 ATOM 82 C CG . LEU A 1 11 ? 2.996 11.362 18.261 1.00 16.11 ? 99 LEU A CG 1 ATOM 83 C CD1 . LEU A 1 11 ? 4.364 10.870 18.506 1.00 19.79 ? 99 LEU A CD1 1 ATOM 84 C CD2 . LEU A 1 11 ? 2.747 11.448 16.780 1.00 16.56 ? 99 LEU A CD2 1 ATOM 85 N N . TRP A 1 12 ? -1.337 9.637 18.590 1.00 14.98 ? 100 TRP A N 1 ATOM 86 C CA . TRP A 1 12 ? -2.417 8.782 19.058 1.00 15.58 ? 100 TRP A CA 1 ATOM 87 C C . TRP A 1 12 ? -1.912 7.413 19.434 1.00 15.05 ? 100 TRP A C 1 ATOM 88 O O . TRP A 1 12 ? -1.190 6.808 18.659 1.00 14.61 ? 100 TRP A O 1 ATOM 89 C CB . TRP A 1 12 ? -3.428 8.603 17.921 1.00 16.07 ? 100 TRP A CB 1 ATOM 90 C CG . TRP A 1 12 ? -4.586 7.786 18.195 1.00 16.27 ? 100 TRP A CG 1 ATOM 91 C CD1 . TRP A 1 12 ? -4.831 6.547 17.690 1.00 18.05 ? 100 TRP A CD1 1 ATOM 92 C CD2 . TRP A 1 12 ? -5.728 8.129 18.993 1.00 18.62 ? 100 TRP A CD2 1 ATOM 93 N NE1 . TRP A 1 12 ? -6.047 6.088 18.127 1.00 18.02 ? 100 TRP A NE1 1 ATOM 94 C CE2 . TRP A 1 12 ? -6.619 7.030 18.938 1.00 17.85 ? 100 TRP A CE2 1 ATOM 95 C CE3 . TRP A 1 12 ? -6.091 9.249 19.760 1.00 19.35 ? 100 TRP A CE3 1 ATOM 96 C CZ2 . TRP A 1 12 ? -7.846 7.018 19.616 1.00 18.83 ? 100 TRP A CZ2 1 ATOM 97 C CZ3 . TRP A 1 12 ? -7.317 9.240 20.440 1.00 19.40 ? 100 TRP A CZ3 1 ATOM 98 C CH2 . TRP A 1 12 ? -8.179 8.123 20.364 1.00 20.31 ? 100 TRP A CH2 1 ATOM 99 N N . ALA A 1 13 ? -2.264 6.953 20.627 1.00 15.53 ? 101 ALA A N 1 ATOM 100 C CA . ALA A 1 13 ? -1.984 5.596 21.061 1.00 15.98 ? 101 ALA A CA 1 ATOM 101 C C . ALA A 1 13 ? -3.190 4.770 20.601 1.00 16.57 ? 101 ALA A C 1 ATOM 102 O O . ALA A 1 13 ? -4.354 5.038 21.009 1.00 17.76 ? 101 ALA A O 1 ATOM 103 C CB . ALA A 1 13 ? -1.789 5.564 22.583 1.00 16.93 ? 101 ALA A CB 1 ATOM 104 N N . ASN A 1 14 ? -2.966 3.822 19.698 1.00 15.86 ? 102 ASN A N 1 ATOM 105 C CA . ASN A 1 14 ? -4.095 3.137 19.077 1.00 16.59 ? 102 ASN A CA 1 ATOM 106 C C . ASN A 1 14 ? -4.736 2.070 19.939 1.00 17.08 ? 102 ASN A C 1 ATOM 107 O O . ASN A 1 14 ? -4.138 1.573 20.887 1.00 16.10 ? 102 ASN A O 1 ATOM 108 C CB . ASN A 1 14 ? -3.736 2.597 17.684 1.00 16.30 ? 102 ASN A CB 1 ATOM 109 C CG . ASN A 1 14 ? -2.823 1.408 17.750 1.00 15.01 ? 102 ASN A CG 1 ATOM 110 O OD1 . ASN A 1 14 ? -3.245 0.278 18.080 1.00 16.36 ? 102 ASN A OD1 1 ATOM 111 N ND2 . ASN A 1 14 ? -1.529 1.658 17.489 1.00 15.38 ? 102 ASN A ND2 1 ATOM 112 N N . ASN A 1 15 ? -5.988 1.741 19.618 1.00 17.95 ? 103 ASN A N 1 ATOM 113 C CA . ASN A 1 15 ? -6.747 0.814 20.448 1.00 18.19 ? 103 ASN A CA 1 ATOM 114 C C . ASN A 1 15 ? -6.472 -0.633 20.158 1.00 17.62 ? 103 ASN A C 1 ATOM 115 O O . ASN A 1 15 ? -6.894 -1.525 20.914 1.00 16.70 ? 103 ASN A O 1 ATOM 116 C CB . ASN A 1 15 ? -8.240 1.108 20.350 1.00 18.95 ? 103 ASN A CB 1 ATOM 117 C CG . ASN A 1 15 ? -8.642 2.209 21.279 1.00 21.63 ? 103 ASN A CG 1 ATOM 118 O OD1 . ASN A 1 15 ? -8.380 2.137 22.481 1.00 25.80 ? 103 ASN A OD1 1 ATOM 119 N ND2 . ASN A 1 15 ? -9.238 3.254 20.742 1.00 23.74 ? 103 ASN A ND2 1 ATOM 120 N N . TYR A 1 16 ? -5.784 -0.895 19.056 1.00 16.60 ? 104 TYR A N 1 ATOM 121 C CA . TYR A 1 16 ? -5.409 -2.260 18.759 1.00 15.18 ? 104 TYR A CA 1 ATOM 122 C C . TYR A 1 16 ? -4.347 -2.704 19.778 1.00 15.08 ? 104 TYR A C 1 ATOM 123 O O . TYR A 1 16 ? -4.472 -3.769 20.398 1.00 14.18 ? 104 TYR A O 1 ATOM 124 C CB . TYR A 1 16 ? -4.925 -2.390 17.328 1.00 15.59 ? 104 TYR A CB 1 ATOM 125 C CG . TYR A 1 16 ? -4.473 -3.793 16.968 1.00 16.79 ? 104 TYR A CG 1 ATOM 126 C CD1 . TYR A 1 16 ? -5.377 -4.706 16.488 1.00 19.10 ? 104 TYR A CD1 1 ATOM 127 C CD2 . TYR A 1 16 ? -3.142 -4.195 17.123 1.00 17.53 ? 104 TYR A CD2 1 ATOM 128 C CE1 . TYR A 1 16 ? -4.995 -6.002 16.148 1.00 20.98 ? 104 TYR A CE1 1 ATOM 129 C CE2 . TYR A 1 16 ? -2.729 -5.464 16.778 1.00 18.70 ? 104 TYR A CE2 1 ATOM 130 C CZ . TYR A 1 16 ? -3.678 -6.385 16.302 1.00 21.01 ? 104 TYR A CZ 1 ATOM 131 O OH . TYR A 1 16 ? -3.298 -7.650 15.937 1.00 21.35 ? 104 TYR A OH 1 ATOM 132 N N . TYR A 1 17 ? -3.316 -1.885 19.987 1.00 13.65 ? 105 TYR A N 1 ATOM 133 C CA . TYR A 1 17 ? -2.308 -2.206 20.970 1.00 13.81 ? 105 TYR A CA 1 ATOM 134 C C . TYR A 1 17 ? -2.861 -2.120 22.395 1.00 13.99 ? 105 TYR A C 1 ATOM 135 O O . TYR A 1 17 ? -2.559 -2.950 23.239 1.00 13.35 ? 105 TYR A O 1 ATOM 136 C CB . TYR A 1 17 ? -1.127 -1.249 20.841 1.00 13.90 ? 105 TYR A CB 1 ATOM 137 C CG . TYR A 1 17 ? 0.030 -1.616 21.711 1.00 13.26 ? 105 TYR A CG 1 ATOM 138 C CD1 . TYR A 1 17 ? 0.906 -2.613 21.345 1.00 12.24 ? 105 TYR A CD1 1 ATOM 139 C CD2 . TYR A 1 17 ? 0.259 -0.950 22.902 1.00 14.73 ? 105 TYR A CD2 1 ATOM 140 C CE1 . TYR A 1 17 ? 1.967 -2.944 22.141 1.00 13.06 ? 105 TYR A CE1 1 ATOM 141 C CE2 . TYR A 1 17 ? 1.313 -1.273 23.718 1.00 13.25 ? 105 TYR A CE2 1 ATOM 142 C CZ . TYR A 1 17 ? 2.173 -2.270 23.326 1.00 12.03 ? 105 TYR A CZ 1 ATOM 143 O OH . TYR A 1 17 ? 3.242 -2.667 24.100 1.00 14.18 ? 105 TYR A OH 1 ATOM 144 N N . ARG A 1 18 ? -3.613 -1.072 22.677 1.00 14.70 ? 106 ARG A N 1 ATOM 145 C CA . ARG A 1 18 ? -4.228 -0.967 23.986 1.00 17.02 ? 106 ARG A CA 1 ATOM 146 C C . ARG A 1 18 ? -5.017 -2.236 24.324 1.00 17.53 ? 106 ARG A C 1 ATOM 147 O O . ARG A 1 18 ? -4.846 -2.790 25.402 1.00 18.85 ? 106 ARG A O 1 ATOM 148 C CB . ARG A 1 18 ? -5.123 0.267 24.048 1.00 17.74 ? 106 ARG A CB 1 ATOM 149 C CG . ARG A 1 18 ? -5.731 0.501 25.410 1.00 18.74 ? 106 ARG A CG 1 ATOM 150 C CD . ARG A 1 18 ? -6.599 1.755 25.466 1.00 21.11 ? 106 ARG A CD 1 ATOM 151 N NE . ARG A 1 18 ? -5.813 2.960 25.619 1.00 22.55 ? 106 ARG A NE 1 ATOM 152 C CZ . ARG A 1 18 ? -5.583 3.829 24.642 1.00 24.65 ? 106 ARG A CZ 1 ATOM 153 N NH1 . ARG A 1 18 ? -6.086 3.629 23.431 1.00 27.46 ? 106 ARG A NH1 1 ATOM 154 N NH2 . ARG A 1 18 ? -4.841 4.894 24.870 1.00 26.95 ? 106 ARG A NH2 1 ATOM 155 N N . SER A 1 19 ? -5.882 -2.686 23.419 1.00 18.89 ? 107 SER A N 1 ATOM 156 C CA . SER A 1 19 ? -6.645 -3.905 23.676 1.00 20.67 ? 107 SER A CA 1 ATOM 157 C C . SER A 1 19 ? -5.710 -5.081 23.906 1.00 20.35 ? 107 SER A C 1 ATOM 158 O O . SER A 1 19 ? -5.954 -5.935 24.764 1.00 20.41 ? 107 SER A O 1 ATOM 159 C CB . SER A 1 19 ? -7.589 -4.246 22.530 1.00 20.96 ? 107 SER A CB 1 ATOM 160 O OG . SER A 1 19 ? -8.601 -3.273 22.454 1.00 25.62 ? 107 SER A OG 1 ATOM 161 N N . GLU A 1 20 ? -4.661 -5.193 23.103 1.00 19.64 ? 108 GLU A N 1 ATOM 162 C CA . GLU A 1 20 ? -3.701 -6.262 23.333 1.00 19.49 ? 108 GLU A CA 1 ATOM 163 C C . GLU A 1 20 ? -3.225 -6.223 24.787 1.00 19.37 ? 108 GLU A C 1 ATOM 164 O O . GLU A 1 20 ? -3.233 -7.236 25.465 1.00 19.57 ? 108 GLU A O 1 ATOM 165 C CB . GLU A 1 20 ? -2.513 -6.160 22.372 1.00 19.09 ? 108 GLU A CB 1 ATOM 166 C CG . GLU A 1 20 ? -2.831 -6.711 20.994 1.00 18.67 ? 108 GLU A CG 1 ATOM 167 C CD . GLU A 1 20 ? -1.639 -6.594 20.057 1.00 18.36 ? 108 GLU A CD 1 ATOM 168 O OE1 . GLU A 1 20 ? -0.945 -5.553 20.104 1.00 13.81 ? 108 GLU A OE1 1 ATOM 169 O OE2 . GLU A 1 20 ? -1.375 -7.569 19.340 1.00 18.16 ? 108 GLU A OE2 1 ATOM 170 N N . VAL A 1 21 ? -2.836 -5.060 25.283 1.00 19.73 ? 109 VAL A N 1 ATOM 171 C CA . VAL A 1 21 ? -2.267 -4.996 26.612 1.00 20.16 ? 109 VAL A CA 1 ATOM 172 C C . VAL A 1 21 ? -3.316 -5.340 27.667 1.00 21.05 ? 109 VAL A C 1 ATOM 173 O O . VAL A 1 21 ? -3.080 -6.159 28.561 1.00 20.48 ? 109 VAL A O 1 ATOM 174 C CB . VAL A 1 21 ? -1.651 -3.618 26.829 1.00 20.54 ? 109 VAL A CB 1 ATOM 175 C CG1 . VAL A 1 21 ? -1.228 -3.421 28.279 1.00 20.24 ? 109 VAL A CG1 1 ATOM 176 C CG2 . VAL A 1 21 ? -0.432 -3.467 25.898 1.00 20.95 ? 109 VAL A CG2 1 ATOM 177 N N . HIS A 1 22 ? -4.489 -4.750 27.513 1.00 21.80 ? 110 HIS A N 1 ATOM 178 C CA . HIS A 1 22 ? -5.569 -4.895 28.502 1.00 22.60 ? 110 HIS A CA 1 ATOM 179 C C . HIS A 1 22 ? -6.269 -6.222 28.476 1.00 22.63 ? 110 HIS A C 1 ATOM 180 O O . HIS A 1 22 ? -6.681 -6.718 29.512 1.00 22.19 ? 110 HIS A O 1 ATOM 181 C CB . HIS A 1 22 ? -6.572 -3.762 28.316 1.00 22.67 ? 110 HIS A CB 1 ATOM 182 C CG . HIS A 1 22 ? -6.092 -2.480 28.908 1.00 23.79 ? 110 HIS A CG 1 ATOM 183 N ND1 . HIS A 1 22 ? -6.218 -2.197 30.249 1.00 26.40 ? 110 HIS A ND1 1 ATOM 184 C CD2 . HIS A 1 22 ? -5.411 -1.445 28.367 1.00 25.76 ? 110 HIS A CD2 1 ATOM 185 C CE1 . HIS A 1 22 ? -5.665 -1.022 30.499 1.00 29.11 ? 110 HIS A CE1 1 ATOM 186 N NE2 . HIS A 1 22 ? -5.164 -0.546 29.374 1.00 26.65 ? 110 HIS A NE2 1 ATOM 187 N N . THR A 1 23 ? -6.419 -6.816 27.306 1.00 23.45 ? 111 THR A N 1 ATOM 188 C CA . THR A 1 23 ? -7.107 -8.096 27.244 1.00 24.41 ? 111 THR A CA 1 ATOM 189 C C . THR A 1 23 ? -6.189 -9.295 27.306 1.00 24.69 ? 111 THR A C 1 ATOM 190 O O . THR A 1 23 ? -6.597 -10.352 27.777 1.00 23.42 ? 111 THR A O 1 ATOM 191 C CB . THR A 1 23 ? -7.960 -8.208 25.993 1.00 24.62 ? 111 THR A CB 1 ATOM 192 O OG1 . THR A 1 23 ? -7.132 -8.415 24.835 1.00 29.67 ? 111 THR A OG1 1 ATOM 193 C CG2 . THR A 1 23 ? -8.696 -6.946 25.738 1.00 25.28 ? 111 THR A CG2 1 ATOM 194 N N . LEU A 1 24 ? -4.957 -9.157 26.818 1.00 24.48 ? 112 LEU A N 1 ATOM 195 C CA . LEU A 1 24 ? -4.068 -10.310 26.735 1.00 25.48 ? 112 LEU A CA 1 ATOM 196 C C . LEU A 1 24 ? -2.966 -10.307 27.782 1.00 25.73 ? 112 LEU A C 1 ATOM 197 O O . LEU A 1 24 ? -2.559 -11.359 28.241 1.00 26.64 ? 112 LEU A O 1 ATOM 198 C CB . LEU A 1 24 ? -3.447 -10.410 25.325 1.00 26.03 ? 112 LEU A CB 1 ATOM 199 C CG . LEU A 1 24 ? -4.457 -10.461 24.164 1.00 27.30 ? 112 LEU A CG 1 ATOM 200 C CD1 . LEU A 1 24 ? -3.776 -10.464 22.804 1.00 29.58 ? 112 LEU A CD1 1 ATOM 201 C CD2 . LEU A 1 24 ? -5.347 -11.695 24.283 1.00 28.57 ? 112 LEU A CD2 1 ATOM 202 N N . ALA A 1 25 ? -2.507 -9.136 28.189 1.00 25.51 ? 113 ALA A N 1 ATOM 203 C CA . ALA A 1 25 ? -1.381 -9.052 29.099 1.00 26.27 ? 113 ALA A CA 1 ATOM 204 C C . ALA A 1 25 ? -1.752 -8.776 30.558 1.00 26.91 ? 113 ALA A C 1 ATOM 205 O O . ALA A 1 25 ? -1.277 -9.463 31.438 1.00 27.10 ? 113 ALA A O 1 ATOM 206 C CB . ALA A 1 25 ? -0.398 -7.964 28.604 1.00 26.04 ? 113 ALA A CB 1 ATOM 207 N N . ILE A 1 26 ? -2.570 -7.757 30.806 1.00 28.41 ? 114 ILE A N 1 ATOM 208 C CA . ILE A 1 26 ? -2.806 -7.336 32.184 1.00 30.07 ? 114 ILE A CA 1 ATOM 209 C C . ILE A 1 26 ? -3.479 -8.401 33.019 1.00 31.26 ? 114 ILE A C 1 ATOM 210 O O . ILE A 1 26 ? -3.124 -8.572 34.181 1.00 30.95 ? 114 ILE A O 1 ATOM 211 C CB . ILE A 1 26 ? -3.582 -6.030 32.276 1.00 30.51 ? 114 ILE A CB 1 ATOM 212 C CG1 . ILE A 1 26 ? -2.619 -4.846 32.156 1.00 29.83 ? 114 ILE A CG1 1 ATOM 213 C CG2 . ILE A 1 26 ? -4.278 -5.944 33.631 1.00 30.27 ? 114 ILE A CG2 1 ATOM 214 C CD1 . ILE A 1 26 ? -3.260 -3.547 31.775 1.00 29.34 ? 114 ILE A CD1 1 ATOM 215 N N . PRO A 1 27 ? -4.456 -9.101 32.458 1.00 32.90 ? 115 PRO A N 1 ATOM 216 C CA . PRO A 1 27 ? -5.116 -10.174 33.198 1.00 34.11 ? 115 PRO A CA 1 ATOM 217 C C . PRO A 1 27 ? -4.138 -11.284 33.535 1.00 35.55 ? 115 PRO A C 1 ATOM 218 O O . PRO A 1 27 ? -4.414 -12.098 34.415 1.00 35.96 ? 115 PRO A O 1 ATOM 219 C CB . PRO A 1 27 ? -6.174 -10.691 32.212 1.00 34.48 ? 115 PRO A CB 1 ATOM 220 C CG . PRO A 1 27 ? -6.383 -9.587 31.223 1.00 34.01 ? 115 PRO A CG 1 ATOM 221 C CD . PRO A 1 27 ? -5.073 -8.874 31.144 1.00 33.19 ? 115 PRO A CD 1 ATOM 222 N N . GLN A 1 28 ? -2.997 -11.302 32.856 1.00 36.66 ? 116 GLN A N 1 ATOM 223 C CA . GLN A 1 28 ? -2.018 -12.386 32.991 1.00 37.74 ? 116 GLN A CA 1 ATOM 224 C C . GLN A 1 28 ? -0.889 -12.028 33.933 1.00 38.57 ? 116 GLN A C 1 ATOM 225 O O . GLN A 1 28 ? -0.018 -12.840 34.237 1.00 39.53 ? 116 GLN A O 1 ATOM 226 C CB . GLN A 1 28 ? -1.401 -12.673 31.623 1.00 38.16 ? 116 GLN A CB 1 ATOM 227 C CG . GLN A 1 28 ? -1.959 -13.881 30.929 1.00 38.45 ? 116 GLN A CG 1 ATOM 228 C CD . GLN A 1 28 ? -3.270 -14.318 31.552 1.00 39.74 ? 116 GLN A CD 1 ATOM 229 O OE1 . GLN A 1 28 ? -4.354 -14.037 31.028 1.00 39.12 ? 116 GLN A OE1 1 ATOM 230 N NE2 . GLN A 1 28 ? -3.173 -14.994 32.691 1.00 38.23 ? 116 GLN A NE2 1 ATOM 231 N N . ILE A 1 29 ? -0.890 -10.794 34.383 1.00 39.50 ? 117 ILE A N 1 ATOM 232 C CA . ILE A 1 29 ? 0.228 -10.305 35.158 1.00 40.29 ? 117 ILE A CA 1 ATOM 233 C C . ILE A 1 29 ? -0.163 -10.110 36.589 1.00 41.01 ? 117 ILE A C 1 ATOM 234 O O . ILE A 1 29 ? -0.940 -9.211 36.912 1.00 40.95 ? 117 ILE A O 1 ATOM 235 C CB . ILE A 1 29 ? 0.652 -8.976 34.596 1.00 40.39 ? 117 ILE A CB 1 ATOM 236 C CG1 . ILE A 1 29 ? 1.150 -9.154 33.168 1.00 40.29 ? 117 ILE A CG1 1 ATOM 237 C CG2 . ILE A 1 29 ? 1.728 -8.370 35.469 1.00 40.18 ? 117 ILE A CG2 1 ATOM 238 C CD1 . ILE A 1 29 ? 1.380 -7.828 32.497 1.00 39.56 ? 117 ILE A CD1 1 ATOM 239 N N . THR A 1 30 ? 0.369 -10.933 37.473 1.00 41.92 ? 118 THR A N 1 ATOM 240 C CA . THR A 1 30 ? -0.099 -10.825 38.843 1.00 42.51 ? 118 THR A CA 1 ATOM 241 C C . THR A 1 30 ? 0.571 -9.697 39.653 1.00 42.71 ? 118 THR A C 1 ATOM 242 O O . THR A 1 30 ? -0.074 -9.054 40.481 1.00 42.86 ? 118 THR A O 1 ATOM 243 C CB . THR A 1 30 ? 0.038 -12.179 39.558 1.00 42.60 ? 118 THR A CB 1 ATOM 244 O OG1 . THR A 1 30 ? 1.409 -12.603 39.570 1.00 43.84 ? 118 THR A OG1 1 ATOM 245 C CG2 . THR A 1 30 ? -0.717 -13.274 38.782 1.00 42.71 ? 118 THR A CG2 1 ATOM 246 N N . ASP A 1 31 ? 1.851 -9.444 39.394 1.00 42.59 ? 119 ASP A N 1 ATOM 247 C CA . ASP A 1 31 ? 2.649 -8.509 40.197 1.00 42.65 ? 119 ASP A CA 1 ATOM 248 C C . ASP A 1 31 ? 2.247 -7.035 40.076 1.00 41.94 ? 119 ASP A C 1 ATOM 249 O O . ASP A 1 31 ? 2.429 -6.445 39.009 1.00 42.53 ? 119 ASP A O 1 ATOM 250 C CB . ASP A 1 31 ? 4.097 -8.668 39.774 1.00 42.90 ? 119 ASP A CB 1 ATOM 251 C CG . ASP A 1 31 ? 5.004 -7.682 40.451 1.00 45.15 ? 119 ASP A CG 1 ATOM 252 O OD1 . ASP A 1 31 ? 4.494 -6.803 41.178 1.00 46.92 ? 119 ASP A OD1 1 ATOM 253 O OD2 . ASP A 1 31 ? 6.248 -7.714 40.303 1.00 49.33 ? 119 ASP A OD2 1 ATOM 254 N N . PRO A 1 32 ? 1.734 -6.420 41.153 1.00 40.86 ? 120 PRO A N 1 ATOM 255 C CA . PRO A 1 32 ? 1.185 -5.062 41.059 1.00 40.06 ? 120 PRO A CA 1 ATOM 256 C C . PRO A 1 32 ? 2.053 -4.094 40.261 1.00 39.33 ? 120 PRO A C 1 ATOM 257 O O . PRO A 1 32 ? 1.547 -3.402 39.370 1.00 39.25 ? 120 PRO A O 1 ATOM 258 C CB . PRO A 1 32 ? 1.078 -4.578 42.527 1.00 40.30 ? 120 PRO A CB 1 ATOM 259 C CG . PRO A 1 32 ? 1.325 -5.738 43.431 1.00 40.18 ? 120 PRO A CG 1 ATOM 260 C CD . PRO A 1 32 ? 1.621 -6.946 42.522 1.00 41.26 ? 120 PRO A CD 1 ATOM 261 N N . ALA A 1 33 ? 3.333 -4.013 40.601 1.00 38.29 ? 121 ALA A N 1 ATOM 262 C CA . ALA A 1 33 ? 4.224 -3.041 39.962 1.00 37.53 ? 121 ALA A CA 1 ATOM 263 C C . ALA A 1 33 ? 4.140 -3.115 38.441 1.00 36.74 ? 121 ALA A C 1 ATOM 264 O O . ALA A 1 33 ? 4.008 -2.108 37.739 1.00 36.11 ? 121 ALA A O 1 ATOM 265 C CB . ALA A 1 33 ? 5.660 -3.286 40.406 1.00 37.57 ? 121 ALA A CB 1 ATOM 266 N N . LEU A 1 34 ? 4.260 -4.332 37.947 1.00 36.09 ? 122 LEU A N 1 ATOM 267 C CA . LEU A 1 34 ? 4.221 -4.574 36.532 1.00 35.72 ? 122 LEU A CA 1 ATOM 268 C C . LEU A 1 34 ? 2.876 -4.226 35.959 1.00 35.08 ? 122 LEU A C 1 ATOM 269 O O . LEU A 1 34 ? 2.755 -3.769 34.827 1.00 33.85 ? 122 LEU A O 1 ATOM 270 C CB . LEU A 1 34 ? 4.502 -6.045 36.281 1.00 36.20 ? 122 LEU A CB 1 ATOM 271 C CG . LEU A 1 34 ? 5.959 -6.386 36.569 1.00 37.87 ? 122 LEU A CG 1 ATOM 272 C CD1 . LEU A 1 34 ? 6.339 -7.748 36.050 1.00 37.92 ? 122 LEU A CD1 1 ATOM 273 C CD2 . LEU A 1 34 ? 6.896 -5.343 35.945 1.00 39.71 ? 122 LEU A CD2 1 ATOM 274 N N . ARG A 1 35 ? 1.832 -4.466 36.722 1.00 34.15 ? 123 ARG A N 1 ATOM 275 C CA . ARG A 1 35 ? 0.541 -4.229 36.120 1.00 33.67 ? 123 ARG A CA 1 ATOM 276 C C . ARG A 1 35 ? 0.227 -2.746 36.039 1.00 32.06 ? 123 ARG A C 1 ATOM 277 O O . ARG A 1 35 ? -0.495 -2.312 35.153 1.00 31.87 ? 123 ARG A O 1 ATOM 278 C CB . ARG A 1 35 ? -0.537 -5.051 36.800 1.00 34.57 ? 123 ARG A CB 1 ATOM 279 C CG . ARG A 1 35 ? -1.919 -4.482 36.628 1.00 37.31 ? 123 ARG A CG 1 ATOM 280 C CD . ARG A 1 35 ? -2.900 -5.126 37.576 1.00 41.28 ? 123 ARG A CD 1 ATOM 281 N NE . ARG A 1 35 ? -4.274 -4.793 37.249 1.00 43.31 ? 123 ARG A NE 1 ATOM 282 C CZ . ARG A 1 35 ? -5.182 -5.727 37.022 1.00 44.82 ? 123 ARG A CZ 1 ATOM 283 N NH1 . ARG A 1 35 ? -4.818 -7.005 37.103 1.00 45.37 ? 123 ARG A NH1 1 ATOM 284 N NH2 . ARG A 1 35 ? -6.430 -5.409 36.717 1.00 45.23 ? 123 ARG A NH2 1 ATOM 285 N N . ALA A 1 36 ? 0.787 -1.951 36.934 1.00 30.36 ? 124 ALA A N 1 ATOM 286 C CA . ALA A 1 36 ? 0.664 -0.504 36.772 1.00 29.14 ? 124 ALA A CA 1 ATOM 287 C C . ALA A 1 36 ? 1.427 -0.074 35.501 1.00 27.90 ? 124 ALA A C 1 ATOM 288 O O . ALA A 1 36 ? 0.979 0.762 34.708 1.00 26.66 ? 124 ALA A O 1 ATOM 289 C CB . ALA A 1 36 ? 1.230 0.207 37.976 1.00 29.54 ? 124 ALA A CB 1 ATOM 290 N N . ALA A 1 37 ? 2.612 -0.636 35.357 1.00 26.98 ? 125 ALA A N 1 ATOM 291 C CA . ALA A 1 37 ? 3.493 -0.306 34.256 1.00 25.76 ? 125 ALA A CA 1 ATOM 292 C C . ALA A 1 37 ? 2.829 -0.693 32.955 1.00 24.41 ? 125 ALA A C 1 ATOM 293 O O . ALA A 1 37 ? 2.885 0.040 31.986 1.00 24.37 ? 125 ALA A O 1 ATOM 294 C CB . ALA A 1 37 ? 4.811 -1.046 34.416 1.00 25.67 ? 125 ALA A CB 1 ATOM 295 N N . ALA A 1 38 ? 2.176 -1.846 32.947 1.00 23.37 ? 126 ALA A N 1 ATOM 296 C CA . ALA A 1 38 ? 1.550 -2.343 31.725 1.00 23.04 ? 126 ALA A CA 1 ATOM 297 C C . ALA A 1 38 ? 0.505 -1.379 31.227 1.00 22.52 ? 126 ALA A C 1 ATOM 298 O O . ALA A 1 38 ? 0.448 -1.039 30.034 1.00 21.87 ? 126 ALA A O 1 ATOM 299 C CB . ALA A 1 38 ? 0.956 -3.739 31.942 1.00 22.76 ? 126 ALA A CB 1 ATOM 300 N N . SER A 1 39 ? -0.304 -0.886 32.157 1.00 21.72 ? 127 SER A N 1 ATOM 301 C CA . SER A 1 39 ? -1.347 0.012 31.775 1.00 20.91 ? 127 SER A CA 1 ATOM 302 C C . SER A 1 39 ? -0.732 1.266 31.232 1.00 20.60 ? 127 SER A C 1 ATOM 303 O O . SER A 1 39 ? -1.247 1.834 30.289 1.00 20.61 ? 127 SER A O 1 ATOM 304 C CB A SER A 1 39 ? -2.264 0.335 32.959 0.55 21.17 ? 127 SER A CB 1 ATOM 305 C CB B SER A 1 39 ? -2.257 0.307 32.962 0.45 21.09 ? 127 SER A CB 1 ATOM 306 O OG A SER A 1 39 ? -2.920 1.577 32.740 0.55 20.92 ? 127 SER A OG 1 ATOM 307 O OG B SER A 1 39 ? -3.092 -0.804 33.192 0.45 20.28 ? 127 SER A OG 1 ATOM 308 N N . ALA A 1 40 ? 0.391 1.684 31.801 1.00 20.27 ? 128 ALA A N 1 ATOM 309 C CA . ALA A 1 40 ? 1.046 2.889 31.297 1.00 20.90 ? 128 ALA A CA 1 ATOM 310 C C . ALA A 1 40 ? 1.641 2.686 29.871 1.00 20.11 ? 128 ALA A C 1 ATOM 311 O O . ALA A 1 40 ? 1.515 3.579 29.023 1.00 19.59 ? 128 ALA A O 1 ATOM 312 C CB . ALA A 1 40 ? 2.077 3.362 32.248 1.00 20.92 ? 128 ALA A CB 1 ATOM 313 N N . VAL A 1 41 ? 2.265 1.532 29.614 1.00 19.92 ? 129 VAL A N 1 ATOM 314 C CA . VAL A 1 41 ? 2.822 1.242 28.278 1.00 20.56 ? 129 VAL A CA 1 ATOM 315 C C . VAL A 1 41 ? 1.722 1.243 27.179 1.00 20.41 ? 129 VAL A C 1 ATOM 316 O O . VAL A 1 41 ? 1.982 1.592 26.031 1.00 18.46 ? 129 VAL A O 1 ATOM 317 C CB . VAL A 1 41 ? 3.534 -0.138 28.214 1.00 21.06 ? 129 VAL A CB 1 ATOM 318 C CG1 . VAL A 1 41 ? 4.196 -0.313 26.839 1.00 24.07 ? 129 VAL A CG1 1 ATOM 319 C CG2 . VAL A 1 41 ? 4.583 -0.251 29.239 1.00 22.83 ? 129 VAL A CG2 1 ATOM 320 N N . ALA A 1 42 ? 0.496 0.847 27.549 1.00 20.54 ? 130 ALA A N 1 ATOM 321 C CA . ALA A 1 42 ? -0.640 0.812 26.625 1.00 19.54 ? 130 ALA A CA 1 ATOM 322 C C . ALA A 1 42 ? -1.004 2.167 26.065 1.00 19.63 ? 130 ALA A C 1 ATOM 323 O O . ALA A 1 42 ? -1.618 2.222 25.002 1.00 19.63 ? 130 ALA A O 1 ATOM 324 C CB . ALA A 1 42 ? -1.858 0.207 27.300 1.00 19.94 ? 130 ALA A CB 1 ATOM 325 N N . GLU A 1 43 ? -0.641 3.238 26.795 1.00 18.92 ? 131 GLU A N 1 ATOM 326 C CA . GLU A 1 43 ? -0.881 4.617 26.425 1.00 19.69 ? 131 GLU A CA 1 ATOM 327 C C . GLU A 1 43 ? 0.290 5.252 25.673 1.00 18.98 ? 131 GLU A C 1 ATOM 328 O O . GLU A 1 43 ? 0.215 6.406 25.289 1.00 18.26 ? 131 GLU A O 1 ATOM 329 C CB . GLU A 1 43 ? -1.135 5.465 27.680 1.00 20.51 ? 131 GLU A CB 1 ATOM 330 C CG . GLU A 1 43 ? -2.300 4.998 28.528 1.00 21.33 ? 131 GLU A CG 1 ATOM 331 C CD . GLU A 1 43 ? -3.543 4.790 27.705 1.00 24.17 ? 131 GLU A CD 1 ATOM 332 O OE1 . GLU A 1 43 ? -3.881 5.697 26.905 1.00 24.63 ? 131 GLU A OE1 1 ATOM 333 O OE2 . GLU A 1 43 ? -4.160 3.708 27.835 1.00 26.46 ? 131 GLU A OE2 1 ATOM 334 N N . VAL A 1 44 ? 1.379 4.511 25.503 1.00 18.04 ? 132 VAL A N 1 ATOM 335 C CA . VAL A 1 44 ? 2.512 4.998 24.715 1.00 17.01 ? 132 VAL A CA 1 ATOM 336 C C . VAL A 1 44 ? 2.145 4.803 23.229 1.00 17.41 ? 132 VAL A C 1 ATOM 337 O O . VAL A 1 44 ? 1.804 3.696 22.806 1.00 17.43 ? 132 VAL A O 1 ATOM 338 C CB . VAL A 1 44 ? 3.818 4.248 25.086 1.00 17.00 ? 132 VAL A CB 1 ATOM 339 C CG1 . VAL A 1 44 ? 4.960 4.687 24.188 1.00 19.58 ? 132 VAL A CG1 1 ATOM 340 C CG2 . VAL A 1 44 ? 4.176 4.501 26.563 1.00 17.87 ? 132 VAL A CG2 1 ATOM 341 N N . PRO A 1 45 ? 2.203 5.868 22.442 1.00 15.94 ? 133 PRO A N 1 ATOM 342 C CA . PRO A 1 45 ? 1.769 5.831 21.050 1.00 16.09 ? 133 PRO A CA 1 ATOM 343 C C . PRO A 1 45 ? 2.753 5.197 20.085 1.00 14.63 ? 133 PRO A C 1 ATOM 344 O O . PRO A 1 45 ? 3.706 5.836 19.658 1.00 16.03 ? 133 PRO A O 1 ATOM 345 C CB . PRO A 1 45 ? 1.621 7.303 20.700 1.00 15.82 ? 133 PRO A CB 1 ATOM 346 C CG . PRO A 1 45 ? 2.587 7.989 21.563 1.00 17.99 ? 133 PRO A CG 1 ATOM 347 C CD . PRO A 1 45 ? 2.698 7.190 22.815 1.00 16.45 ? 133 PRO A CD 1 ATOM 348 N N . SER A 1 46 ? 2.465 3.961 19.730 1.00 14.42 ? 134 SER A N 1 ATOM 349 C CA . SER A 1 46 ? 3.232 3.192 18.761 1.00 12.93 ? 134 SER A CA 1 ATOM 350 C C . SER A 1 46 ? 2.535 3.106 17.401 1.00 12.09 ? 134 SER A C 1 ATOM 351 O O . SER A 1 46 ? 1.330 3.297 17.279 1.00 10.40 ? 134 SER A O 1 ATOM 352 C CB . SER A 1 46 ? 3.466 1.792 19.326 1.00 13.77 ? 134 SER A CB 1 ATOM 353 O OG . SER A 1 46 ? 2.247 1.120 19.553 1.00 13.76 ? 134 SER A OG 1 ATOM 354 N N . PHE A 1 47 ? 3.317 2.858 16.353 1.00 10.36 ? 135 PHE A N 1 ATOM 355 C CA . PHE A 1 47 ? 2.771 2.703 15.026 1.00 9.94 ? 135 PHE A CA 1 ATOM 356 C C . PHE A 1 47 ? 1.795 1.539 14.926 1.00 9.66 ? 135 PHE A C 1 ATOM 357 O O . PHE A 1 47 ? 1.978 0.501 15.552 1.00 9.73 ? 135 PHE A O 1 ATOM 358 C CB . PHE A 1 47 ? 3.892 2.507 13.999 1.00 9.52 ? 135 PHE A CB 1 ATOM 359 C CG . PHE A 1 47 ? 4.446 3.798 13.496 1.00 8.70 ? 135 PHE A CG 1 ATOM 360 C CD1 . PHE A 1 47 ? 5.248 4.587 14.317 1.00 11.68 ? 135 PHE A CD1 1 ATOM 361 C CD2 . PHE A 1 47 ? 4.101 4.277 12.229 1.00 10.30 ? 135 PHE A CD2 1 ATOM 362 C CE1 . PHE A 1 47 ? 5.749 5.818 13.852 1.00 10.12 ? 135 PHE A CE1 1 ATOM 363 C CE2 . PHE A 1 47 ? 4.600 5.465 11.768 1.00 10.75 ? 135 PHE A CE2 1 ATOM 364 C CZ . PHE A 1 47 ? 5.416 6.253 12.605 1.00 11.70 ? 135 PHE A CZ 1 ATOM 365 N N . GLN A 1 48 ? 0.737 1.743 14.156 1.00 9.05 ? 136 GLN A N 1 ATOM 366 C CA . GLN A 1 48 ? -0.174 0.659 13.840 1.00 10.85 ? 136 GLN A CA 1 ATOM 367 C C . GLN A 1 48 ? 0.148 0.123 12.459 1.00 9.28 ? 136 GLN A C 1 ATOM 368 O O . GLN A 1 48 ? 0.386 0.886 11.550 1.00 9.34 ? 136 GLN A O 1 ATOM 369 C CB . GLN A 1 48 ? -1.603 1.129 13.897 1.00 11.60 ? 136 GLN A CB 1 ATOM 370 C CG . GLN A 1 48 ? -2.583 0.066 13.456 1.00 16.20 ? 136 GLN A CG 1 ATOM 371 C CD . GLN A 1 48 ? -3.988 0.327 13.925 1.00 21.36 ? 136 GLN A CD 1 ATOM 372 O OE1 . GLN A 1 48 ? -4.414 1.469 14.050 1.00 22.31 ? 136 GLN A OE1 1 ATOM 373 N NE2 . GLN A 1 48 ? -4.712 -0.752 14.217 1.00 22.88 ? 136 GLN A NE2 1 ATOM 374 N N . TRP A 1 49 ? 0.252 -1.189 12.323 1.00 8.81 ? 137 TRP A N 1 ATOM 375 C CA . TRP A 1 49 ? 0.684 -1.798 11.071 1.00 8.88 ? 137 TRP A CA 1 ATOM 376 C C . TRP A 1 49 ? -0.440 -2.310 10.193 1.00 9.46 ? 137 TRP A C 1 ATOM 377 O O . TRP A 1 49 ? -1.334 -2.978 10.714 1.00 9.38 ? 137 TRP A O 1 ATOM 378 C CB . TRP A 1 49 ? 1.597 -2.981 11.413 1.00 8.38 ? 137 TRP A CB 1 ATOM 379 C CG . TRP A 1 49 ? 2.895 -2.576 12.014 1.00 9.08 ? 137 TRP A CG 1 ATOM 380 C CD1 . TRP A 1 49 ? 3.098 -1.829 13.125 1.00 8.51 ? 137 TRP A CD1 1 ATOM 381 C CD2 . TRP A 1 49 ? 4.191 -2.904 11.507 1.00 7.91 ? 137 TRP A CD2 1 ATOM 382 N NE1 . TRP A 1 49 ? 4.447 -1.707 13.373 1.00 10.06 ? 137 TRP A NE1 1 ATOM 383 C CE2 . TRP A 1 49 ? 5.141 -2.347 12.378 1.00 8.10 ? 137 TRP A CE2 1 ATOM 384 C CE3 . TRP A 1 49 ? 4.637 -3.648 10.418 1.00 6.97 ? 137 TRP A CE3 1 ATOM 385 C CZ2 . TRP A 1 49 ? 6.519 -2.505 12.185 1.00 8.11 ? 137 TRP A CZ2 1 ATOM 386 C CZ3 . TRP A 1 49 ? 5.977 -3.799 10.201 1.00 5.31 ? 137 TRP A CZ3 1 ATOM 387 C CH2 . TRP A 1 49 ? 6.922 -3.268 11.111 1.00 6.56 ? 137 TRP A CH2 1 ATOM 388 N N . LEU A 1 50 ? -0.416 -1.967 8.892 1.00 8.94 ? 138 LEU A N 1 ATOM 389 C CA . LEU A 1 50 ? -1.330 -2.548 7.894 1.00 10.04 ? 138 LEU A CA 1 ATOM 390 C C . LEU A 1 50 ? -0.604 -3.733 7.247 1.00 10.19 ? 138 LEU A C 1 ATOM 391 O O . LEU A 1 50 ? -0.204 -3.683 6.093 1.00 10.72 ? 138 LEU A O 1 ATOM 392 C CB . LEU A 1 50 ? -1.696 -1.545 6.834 1.00 10.51 ? 138 LEU A CB 1 ATOM 393 C CG . LEU A 1 50 ? -2.139 -0.197 7.404 1.00 11.65 ? 138 LEU A CG 1 ATOM 394 C CD1 . LEU A 1 50 ? -2.479 0.716 6.246 1.00 14.21 ? 138 LEU A CD1 1 ATOM 395 C CD2 . LEU A 1 50 ? -3.308 -0.435 8.276 1.00 12.22 ? 138 LEU A CD2 1 ATOM 396 N N . ASP A 1 51 ? -0.448 -4.812 8.008 1.00 10.39 ? 139 ASP A N 1 ATOM 397 C CA . ASP A 1 51 ? 0.372 -5.951 7.617 1.00 11.00 ? 139 ASP A CA 1 ATOM 398 C C . ASP A 1 51 ? -0.410 -6.980 6.792 1.00 12.41 ? 139 ASP A C 1 ATOM 399 O O . ASP A 1 51 ? 0.145 -7.981 6.329 1.00 12.36 ? 139 ASP A O 1 ATOM 400 C CB . ASP A 1 51 ? 0.937 -6.631 8.863 1.00 11.91 ? 139 ASP A CB 1 ATOM 401 C CG . ASP A 1 51 ? -0.136 -7.247 9.737 1.00 13.43 ? 139 ASP A CG 1 ATOM 402 O OD1 . ASP A 1 51 ? -1.207 -6.645 9.913 1.00 14.30 ? 139 ASP A OD1 1 ATOM 403 O OD2 . ASP A 1 51 ? 0.018 -8.342 10.290 1.00 15.99 ? 139 ASP A OD2 1 ATOM 404 N N . ARG A 1 52 ? -1.703 -6.717 6.630 1.00 12.28 ? 140 ARG A N 1 ATOM 405 C CA . ARG A 1 52 ? -2.624 -7.582 5.897 1.00 13.53 ? 140 ARG A CA 1 ATOM 406 C C . ARG A 1 52 ? -3.671 -6.713 5.212 1.00 13.67 ? 140 ARG A C 1 ATOM 407 O O . ARG A 1 52 ? -4.119 -5.720 5.801 1.00 13.62 ? 140 ARG A O 1 ATOM 408 C CB . ARG A 1 52 ? -3.347 -8.505 6.878 1.00 13.95 ? 140 ARG A CB 1 ATOM 409 C CG . ARG A 1 52 ? -2.492 -9.591 7.513 1.00 18.25 ? 140 ARG A CG 1 ATOM 410 C CD . ARG A 1 52 ? -3.156 -10.180 8.791 1.00 22.06 ? 140 ARG A CD 1 ATOM 411 N NE . ARG A 1 52 ? -3.214 -9.132 9.810 1.00 25.34 ? 140 ARG A NE 1 ATOM 412 C CZ . ARG A 1 52 ? -4.275 -8.834 10.554 1.00 28.17 ? 140 ARG A CZ 1 ATOM 413 N NH1 . ARG A 1 52 ? -5.416 -9.522 10.438 1.00 29.32 ? 140 ARG A NH1 1 ATOM 414 N NH2 . ARG A 1 52 ? -4.184 -7.852 11.439 1.00 29.00 ? 140 ARG A NH2 1 ATOM 415 N N . ASN A 1 53 ? -4.075 -7.101 4.007 1.00 14.56 ? 141 ASN A N 1 ATOM 416 C CA . ASN A 1 53 ? -5.071 -6.358 3.233 1.00 15.20 ? 141 ASN A CA 1 ATOM 417 C C . ASN A 1 53 ? -6.326 -6.065 4.058 1.00 15.25 ? 141 ASN A C 1 ATOM 418 O O . ASN A 1 53 ? -6.880 -4.981 3.985 1.00 15.94 ? 141 ASN A O 1 ATOM 419 C CB . ASN A 1 53 ? -5.441 -7.117 1.969 1.00 15.66 ? 141 ASN A CB 1 ATOM 420 C CG . ASN A 1 53 ? -6.294 -6.309 1.036 1.00 17.55 ? 141 ASN A CG 1 ATOM 421 O OD1 . ASN A 1 53 ? -6.118 -5.068 0.920 1.00 14.24 ? 141 ASN A OD1 1 ATOM 422 N ND2 . ASN A 1 53 ? -7.232 -6.978 0.360 1.00 17.42 ? 141 ASN A ND2 1 ATOM 423 N N . VAL A 1 54 ? -6.775 -7.025 4.840 1.00 15.43 ? 142 VAL A N 1 ATOM 424 C CA . VAL A 1 54 ? -7.999 -6.856 5.594 1.00 16.08 ? 142 VAL A CA 1 ATOM 425 C C . VAL A 1 54 ? -7.977 -5.680 6.584 1.00 16.05 ? 142 VAL A C 1 ATOM 426 O O . VAL A 1 54 ? -9.050 -5.214 7.034 1.00 16.30 ? 142 VAL A O 1 ATOM 427 C CB . VAL A 1 54 ? -8.373 -8.182 6.292 1.00 15.96 ? 142 VAL A CB 1 ATOM 428 C CG1 . VAL A 1 54 ? -7.494 -8.460 7.509 1.00 17.44 ? 142 VAL A CG1 1 ATOM 429 C CG2 . VAL A 1 54 ? -9.817 -8.202 6.640 1.00 18.56 ? 142 VAL A CG2 1 ATOM 430 N N . THR A 1 55 ? -6.786 -5.192 6.933 1.00 15.31 ? 143 THR A N 1 ATOM 431 C CA . THR A 1 55 ? -6.695 -4.090 7.878 1.00 14.73 ? 143 THR A CA 1 ATOM 432 C C . THR A 1 55 ? -7.084 -2.799 7.248 1.00 15.38 ? 143 THR A C 1 ATOM 433 O O . THR A 1 55 ? -7.417 -1.878 7.945 1.00 16.87 ? 143 THR A O 1 ATOM 434 C CB . THR A 1 55 ? -5.274 -3.899 8.497 1.00 13.87 ? 143 THR A CB 1 ATOM 435 O OG1 . THR A 1 55 ? -4.322 -3.601 7.477 1.00 13.34 ? 143 THR A OG1 1 ATOM 436 C CG2 . THR A 1 55 ? -4.766 -5.156 9.148 1.00 13.92 ? 143 THR A CG2 1 ATOM 437 N N . VAL A 1 56 ? -7.051 -2.704 5.936 1.00 16.44 ? 144 VAL A N 1 ATOM 438 C CA . VAL A 1 56 ? -7.248 -1.404 5.321 1.00 18.00 ? 144 VAL A CA 1 ATOM 439 C C . VAL A 1 56 ? -8.649 -0.839 5.596 1.00 19.19 ? 144 VAL A C 1 ATOM 440 O O . VAL A 1 56 ? -8.782 0.295 6.041 1.00 16.83 ? 144 VAL A O 1 ATOM 441 C CB . VAL A 1 56 ? -6.954 -1.454 3.831 1.00 18.10 ? 144 VAL A CB 1 ATOM 442 C CG1 . VAL A 1 56 ? -7.349 -0.138 3.128 1.00 19.17 ? 144 VAL A CG1 1 ATOM 443 C CG2 . VAL A 1 56 ? -5.479 -1.732 3.638 1.00 19.48 ? 144 VAL A CG2 1 ATOM 444 N N . ASP A 1 57 ? -9.667 -1.673 5.384 1.00 20.19 ? 145 ASP A N 1 ATOM 445 C CA . ASP A 1 57 ? -11.074 -1.258 5.489 1.00 21.96 ? 145 ASP A CA 1 ATOM 446 C C . ASP A 1 57 ? -11.635 -1.423 6.886 1.00 21.88 ? 145 ASP A C 1 ATOM 447 O O . ASP A 1 57 ? -12.794 -1.074 7.143 1.00 23.21 ? 145 ASP A O 1 ATOM 448 C CB . ASP A 1 57 ? -11.926 -2.084 4.514 1.00 22.88 ? 145 ASP A CB 1 ATOM 449 C CG . ASP A 1 57 ? -12.128 -1.415 3.180 1.00 25.41 ? 145 ASP A CG 1 ATOM 450 O OD1 . ASP A 1 57 ? -11.696 -0.266 2.992 1.00 34.12 ? 145 ASP A OD1 1 ATOM 451 O OD2 . ASP A 1 57 ? -12.761 -1.967 2.254 1.00 34.80 ? 145 ASP A OD2 1 ATOM 452 N N . THR A 1 58 ? -10.834 -1.950 7.797 1.00 20.99 ? 146 THR A N 1 ATOM 453 C CA . THR A 1 58 ? -11.274 -2.124 9.153 1.00 20.53 ? 146 THR A CA 1 ATOM 454 C C . THR A 1 58 ? -10.464 -1.273 10.108 1.00 19.44 ? 146 THR A C 1 ATOM 455 O O . THR A 1 58 ? -10.911 -0.191 10.494 1.00 17.86 ? 146 THR A O 1 ATOM 456 C CB . THR A 1 58 ? -11.215 -3.611 9.562 1.00 20.73 ? 146 THR A CB 1 ATOM 457 O OG1 . THR A 1 58 ? -9.881 -4.124 9.400 1.00 21.73 ? 146 THR A OG1 1 ATOM 458 C CG2 . THR A 1 58 ? -12.062 -4.456 8.619 1.00 22.30 ? 146 THR A CG2 1 ATOM 459 N N . LEU A 1 59 ? -9.256 -1.740 10.445 1.00 18.66 ? 147 LEU A N 1 ATOM 460 C CA . LEU A 1 59 ? -8.414 -1.065 11.423 1.00 18.46 ? 147 LEU A CA 1 ATOM 461 C C . LEU A 1 59 ? -7.976 0.312 11.027 1.00 16.58 ? 147 LEU A C 1 ATOM 462 O O . LEU A 1 59 ? -7.973 1.189 11.856 1.00 16.13 ? 147 LEU A O 1 ATOM 463 C CB . LEU A 1 59 ? -7.164 -1.878 11.783 1.00 18.29 ? 147 LEU A CB 1 ATOM 464 C CG . LEU A 1 59 ? -7.474 -3.316 12.231 1.00 22.78 ? 147 LEU A CG 1 ATOM 465 C CD1 . LEU A 1 59 ? -6.194 -4.016 12.703 1.00 23.36 ? 147 LEU A CD1 1 ATOM 466 C CD2 . LEU A 1 59 ? -8.537 -3.341 13.328 1.00 26.05 ? 147 LEU A CD2 1 ATOM 467 N N . LEU A 1 60 ? -7.565 0.507 9.784 1.00 16.37 ? 148 LEU A N 1 ATOM 468 C CA . LEU A 1 60 ? -7.110 1.828 9.375 1.00 15.19 ? 148 LEU A CA 1 ATOM 469 C C . LEU A 1 60 ? -8.252 2.852 9.577 1.00 15.28 ? 148 LEU A C 1 ATOM 470 O O . LEU A 1 60 ? -8.090 3.884 10.229 1.00 13.71 ? 148 LEU A O 1 ATOM 471 C CB . LEU A 1 60 ? -6.665 1.822 7.923 1.00 15.42 ? 148 LEU A CB 1 ATOM 472 C CG . LEU A 1 60 ? -6.286 3.203 7.389 1.00 15.74 ? 148 LEU A CG 1 ATOM 473 C CD1 . LEU A 1 60 ? -5.111 3.801 8.154 1.00 16.01 ? 148 LEU A CD1 1 ATOM 474 C CD2 . LEU A 1 60 ? -5.957 3.176 5.950 1.00 16.64 ? 148 LEU A CD2 1 ATOM 475 N N . VAL A 1 61 ? -9.399 2.555 8.985 1.00 16.00 ? 149 VAL A N 1 ATOM 476 C CA . VAL A 1 61 ? -10.589 3.414 9.102 1.00 16.23 ? 149 VAL A CA 1 ATOM 477 C C . VAL A 1 61 ? -11.027 3.610 10.556 1.00 16.87 ? 149 VAL A C 1 ATOM 478 O O . VAL A 1 61 ? -11.446 4.709 10.954 1.00 18.08 ? 149 VAL A O 1 ATOM 479 C CB . VAL A 1 61 ? -11.742 2.843 8.246 1.00 16.50 ? 149 VAL A CB 1 ATOM 480 C CG1 . VAL A 1 61 ? -13.038 3.639 8.427 1.00 17.20 ? 149 VAL A CG1 1 ATOM 481 C CG2 . VAL A 1 61 ? -11.332 2.836 6.832 1.00 17.30 ? 149 VAL A CG2 1 ATOM 482 N N . GLN A 1 62 ? -10.908 2.573 11.377 1.00 17.36 ? 150 GLN A N 1 ATOM 483 C CA . GLN A 1 62 ? -11.326 2.656 12.755 1.00 17.33 ? 150 GLN A CA 1 ATOM 484 C C . GLN A 1 62 ? -10.461 3.656 13.496 1.00 17.64 ? 150 GLN A C 1 ATOM 485 O O . GLN A 1 62 ? -10.949 4.528 14.203 1.00 15.62 ? 150 GLN A O 1 ATOM 486 C CB . GLN A 1 62 ? -11.197 1.288 13.412 1.00 18.21 ? 150 GLN A CB 1 ATOM 487 C CG . GLN A 1 62 ? -11.482 1.235 14.864 1.00 22.03 ? 150 GLN A CG 1 ATOM 488 C CD . GLN A 1 62 ? -11.455 -0.195 15.407 1.00 27.48 ? 150 GLN A CD 1 ATOM 489 O OE1 . GLN A 1 62 ? -10.457 -0.912 15.253 1.00 29.87 ? 150 GLN A OE1 1 ATOM 490 N NE2 . GLN A 1 62 ? -12.553 -0.614 16.020 1.00 28.43 ? 150 GLN A NE2 1 ATOM 491 N N . THR A 1 63 ? -9.148 3.531 13.295 1.00 16.34 ? 151 THR A N 1 ATOM 492 C CA . THR A 1 63 ? -8.198 4.409 13.969 1.00 15.49 ? 151 THR A CA 1 ATOM 493 C C . THR A 1 63 ? -8.304 5.863 13.515 1.00 14.55 ? 151 THR A C 1 ATOM 494 O O . THR A 1 63 ? -8.268 6.772 14.342 1.00 14.94 ? 151 THR A O 1 ATOM 495 C CB . THR A 1 63 ? -6.795 3.888 13.754 1.00 15.17 ? 151 THR A CB 1 ATOM 496 O OG1 . THR A 1 63 ? -6.548 2.772 14.647 1.00 14.46 ? 151 THR A OG1 1 ATOM 497 C CG2 . THR A 1 63 ? -5.764 4.976 14.113 1.00 15.07 ? 151 THR A CG2 1 ATOM 498 N N . LEU A 1 64 ? -8.396 6.089 12.220 1.00 14.95 ? 152 LEU A N 1 ATOM 499 C CA . LEU A 1 64 ? -8.535 7.450 11.709 1.00 15.04 ? 152 LEU A CA 1 ATOM 500 C C . LEU A 1 64 ? -9.851 8.045 12.226 1.00 16.15 ? 152 LEU A C 1 ATOM 501 O O . LEU A 1 64 ? -9.925 9.220 12.613 1.00 15.21 ? 152 LEU A O 1 ATOM 502 C CB . LEU A 1 64 ? -8.463 7.478 10.179 1.00 15.30 ? 152 LEU A CB 1 ATOM 503 C CG . LEU A 1 64 ? -7.060 7.181 9.626 1.00 15.99 ? 152 LEU A CG 1 ATOM 504 C CD1 . LEU A 1 64 ? -7.112 6.982 8.175 1.00 14.25 ? 152 LEU A CD1 1 ATOM 505 C CD2 . LEU A 1 64 ? -6.075 8.285 9.967 1.00 18.69 ? 152 LEU A CD2 1 ATOM 506 N N . SER A 1 65 ? -10.888 7.213 12.282 1.00 16.71 ? 153 SER A N 1 ATOM 507 C CA . SER A 1 65 ? -12.182 7.667 12.787 1.00 17.59 ? 153 SER A CA 1 ATOM 508 C C . SER A 1 65 ? -12.099 8.107 14.232 1.00 18.29 ? 153 SER A C 1 ATOM 509 O O . SER A 1 65 ? -12.691 9.126 14.614 1.00 18.66 ? 153 SER A O 1 ATOM 510 C CB . SER A 1 65 ? -13.234 6.562 12.616 1.00 17.79 ? 153 SER A CB 1 ATOM 511 O OG . SER A 1 65 ? -13.349 6.324 11.221 1.00 18.19 ? 153 SER A OG 1 ATOM 512 N N . GLU A 1 66 ? -11.362 7.344 15.034 1.00 17.12 ? 154 GLU A N 1 ATOM 513 C CA . GLU A 1 66 ? -11.223 7.622 16.441 1.00 17.73 ? 154 GLU A CA 1 ATOM 514 C C . GLU A 1 66 ? -10.399 8.890 16.660 1.00 17.06 ? 154 GLU A C 1 ATOM 515 O O . GLU A 1 66 ? -10.667 9.640 17.589 1.00 16.86 ? 154 GLU A O 1 ATOM 516 C CB . GLU A 1 66 ? -10.584 6.438 17.164 1.00 17.80 ? 154 GLU A CB 1 ATOM 517 C CG . GLU A 1 66 ? -11.580 5.323 17.459 1.00 20.33 ? 154 GLU A CG 1 ATOM 518 C CD . GLU A 1 66 ? -10.918 4.006 17.838 1.00 23.06 ? 154 GLU A CD 1 ATOM 519 O OE1 . GLU A 1 66 ? -9.675 3.961 17.965 1.00 21.78 ? 154 GLU A OE1 1 ATOM 520 O OE2 . GLU A 1 66 ? -11.648 3.005 17.998 1.00 24.42 ? 154 GLU A OE2 1 ATOM 521 N N . ILE A 1 67 ? -9.406 9.106 15.806 1.00 16.47 ? 155 ILE A N 1 ATOM 522 C CA . ILE A 1 67 ? -8.552 10.279 15.900 1.00 17.12 ? 155 ILE A CA 1 ATOM 523 C C . ILE A 1 67 ? -9.379 11.521 15.546 1.00 17.57 ? 155 ILE A C 1 ATOM 524 O O . ILE A 1 67 ? -9.428 12.473 16.312 1.00 17.09 ? 155 ILE A O 1 ATOM 525 C CB . ILE A 1 67 ? -7.333 10.182 14.982 1.00 16.76 ? 155 ILE A CB 1 ATOM 526 C CG1 . ILE A 1 67 ? -6.350 9.135 15.536 1.00 17.25 ? 155 ILE A CG1 1 ATOM 527 C CG2 . ILE A 1 67 ? -6.692 11.536 14.910 1.00 18.83 ? 155 ILE A CG2 1 ATOM 528 C CD1 . ILE A 1 67 ? -5.191 8.739 14.595 1.00 19.13 ? 155 ILE A CD1 1 ATOM 529 N N . ARG A 1 68 ? -10.026 11.495 14.399 1.00 17.72 ? 156 ARG A N 1 ATOM 530 C CA . ARG A 1 68 ? -10.936 12.592 14.013 1.00 19.51 ? 156 ARG A CA 1 ATOM 531 C C . ARG A 1 68 ? -11.880 12.943 15.160 1.00 20.15 ? 156 ARG A C 1 ATOM 532 O O . ARG A 1 68 ? -12.091 14.131 15.465 1.00 21.30 ? 156 ARG A O 1 ATOM 533 C CB . ARG A 1 68 ? -11.742 12.202 12.764 1.00 19.83 ? 156 ARG A CB 1 ATOM 534 C CG . ARG A 1 68 ? -12.934 13.123 12.468 1.00 19.92 ? 156 ARG A CG 1 ATOM 535 C CD . ARG A 1 68 ? -13.705 12.732 11.207 1.00 19.27 ? 156 ARG A CD 1 ATOM 536 N NE . ARG A 1 68 ? -12.981 13.043 9.972 1.00 19.89 ? 156 ARG A NE 1 ATOM 537 C CZ . ARG A 1 68 ? -13.240 12.488 8.805 1.00 18.69 ? 156 ARG A CZ 1 ATOM 538 N NH1 . ARG A 1 68 ? -14.202 11.572 8.698 1.00 21.23 ? 156 ARG A NH1 1 ATOM 539 N NH2 . ARG A 1 68 ? -12.552 12.835 7.750 1.00 20.56 ? 156 ARG A NH2 1 ATOM 540 N N . GLU A 1 69 ? -12.453 11.915 15.781 1.00 20.38 ? 157 GLU A N 1 ATOM 541 C CA . GLU A 1 69 ? -13.390 12.077 16.892 1.00 21.29 ? 157 GLU A CA 1 ATOM 542 C C . GLU A 1 69 ? -12.738 12.773 18.079 1.00 20.63 ? 157 GLU A C 1 ATOM 543 O O . GLU A 1 69 ? -13.325 13.670 18.706 1.00 19.46 ? 157 GLU A O 1 ATOM 544 C CB . GLU A 1 69 ? -13.877 10.710 17.361 1.00 21.40 ? 157 GLU A CB 1 ATOM 545 C CG . GLU A 1 69 ? -14.978 10.740 18.393 1.00 25.59 ? 157 GLU A CG 1 ATOM 546 C CD . GLU A 1 69 ? -15.539 9.363 18.678 1.00 31.42 ? 157 GLU A CD 1 ATOM 547 O OE1 . GLU A 1 69 ? -14.770 8.541 19.214 1.00 36.79 ? 157 GLU A OE1 1 ATOM 548 O OE2 . GLU A 1 69 ? -16.731 9.090 18.385 1.00 32.11 ? 157 GLU A OE2 1 ATOM 549 N N . ALA A 1 70 ? -11.539 12.324 18.426 1.00 19.86 ? 158 ALA A N 1 ATOM 550 C CA . ALA A 1 70 ? -10.853 12.911 19.574 1.00 20.65 ? 158 ALA A CA 1 ATOM 551 C C . ALA A 1 70 ? -10.521 14.369 19.274 1.00 20.19 ? 158 ALA A C 1 ATOM 552 O O . ALA A 1 70 ? -10.645 15.242 20.147 1.00 21.25 ? 158 ALA A O 1 ATOM 553 C CB . ALA A 1 70 ? -9.585 12.112 19.940 1.00 20.21 ? 158 ALA A CB 1 ATOM 554 N N . ASN A 1 71 ? -10.087 14.636 18.053 1.00 19.87 ? 159 ASN A N 1 ATOM 555 C CA . ASN A 1 71 ? -9.721 15.995 17.673 1.00 20.19 ? 159 ASN A CA 1 ATOM 556 C C . ASN A 1 71 ? -10.913 16.914 17.617 1.00 22.16 ? 159 ASN A C 1 ATOM 557 O O . ASN A 1 71 ? -10.808 18.097 17.980 1.00 22.80 ? 159 ASN A O 1 ATOM 558 C CB . ASN A 1 71 ? -9.033 16.022 16.314 1.00 19.41 ? 159 ASN A CB 1 ATOM 559 C CG . ASN A 1 71 ? -7.656 15.434 16.366 1.00 18.42 ? 159 ASN A CG 1 ATOM 560 O OD1 . ASN A 1 71 ? -7.098 15.277 17.451 1.00 17.38 ? 159 ASN A OD1 1 ATOM 561 N ND2 . ASN A 1 71 ? -7.098 15.105 15.214 1.00 12.37 ? 159 ASN A ND2 1 ATOM 562 N N . GLN A 1 72 ? -12.037 16.369 17.153 1.00 23.64 ? 160 GLN A N 1 ATOM 563 C CA . GLN A 1 72 ? -13.256 17.160 16.982 1.00 25.85 ? 160 GLN A CA 1 ATOM 564 C C . GLN A 1 72 ? -13.786 17.507 18.369 1.00 26.52 ? 160 GLN A C 1 ATOM 565 O O . GLN A 1 72 ? -14.357 18.569 18.567 1.00 28.38 ? 160 GLN A O 1 ATOM 566 C CB . GLN A 1 72 ? -14.288 16.426 16.123 1.00 25.71 ? 160 GLN A CB 1 ATOM 567 C CG . GLN A 1 72 ? -14.096 16.695 14.639 1.00 28.76 ? 160 GLN A CG 1 ATOM 568 C CD . GLN A 1 72 ? -15.049 15.943 13.728 1.00 31.77 ? 160 GLN A CD 1 ATOM 569 O OE1 . GLN A 1 72 ? -15.898 15.150 14.181 1.00 32.92 ? 160 GLN A OE1 1 ATOM 570 N NE2 . GLN A 1 72 ? -14.902 16.181 12.431 1.00 31.04 ? 160 GLN A NE2 1 ATOM 571 N N . ALA A 1 73 ? -13.566 16.617 19.334 1.00 27.42 ? 161 ALA A N 1 ATOM 572 C CA . ALA A 1 73 ? -13.934 16.867 20.728 1.00 27.81 ? 161 ALA A CA 1 ATOM 573 C C . ALA A 1 73 ? -12.996 17.806 21.482 1.00 28.54 ? 161 ALA A C 1 ATOM 574 O O . ALA A 1 73 ? -13.204 18.059 22.664 1.00 29.01 ? 161 ALA A O 1 ATOM 575 C CB . ALA A 1 73 ? -14.046 15.585 21.476 1.00 28.18 ? 161 ALA A CB 1 ATOM 576 N N . GLY A 1 74 ? -11.952 18.302 20.839 1.00 28.87 ? 162 GLY A N 1 ATOM 577 C CA . GLY A 1 74 ? -11.141 19.335 21.476 1.00 28.82 ? 162 GLY A CA 1 ATOM 578 C C . GLY A 1 74 ? -9.755 18.939 21.921 1.00 28.53 ? 162 GLY A C 1 ATOM 579 O O . GLY A 1 74 ? -9.146 19.629 22.747 1.00 28.14 ? 162 GLY A O 1 ATOM 580 N N . ALA A 1 75 ? -9.250 17.832 21.387 1.00 27.55 ? 163 ALA A N 1 ATOM 581 C CA . ALA A 1 75 ? -7.879 17.429 21.674 1.00 27.80 ? 163 ALA A CA 1 ATOM 582 C C . ALA A 1 75 ? -6.914 18.573 21.363 1.00 27.06 ? 163 ALA A C 1 ATOM 583 O O . ALA A 1 75 ? -6.885 19.108 20.251 1.00 26.05 ? 163 ALA A O 1 ATOM 584 C CB . ALA A 1 75 ? -7.500 16.198 20.840 1.00 27.98 ? 163 ALA A CB 1 ATOM 585 N N . ASN A 1 76 ? -6.086 18.943 22.323 1.00 27.35 ? 164 ASN A N 1 ATOM 586 C CA . ASN A 1 76 ? -5.175 20.041 22.045 1.00 28.12 ? 164 ASN A CA 1 ATOM 587 C C . ASN A 1 76 ? -3.800 19.796 22.613 1.00 26.58 ? 164 ASN A C 1 ATOM 588 O O . ASN A 1 76 ? -3.648 19.650 23.824 1.00 27.32 ? 164 ASN A O 1 ATOM 589 C CB . ASN A 1 76 ? -5.732 21.359 22.584 1.00 29.15 ? 164 ASN A CB 1 ATOM 590 C CG . ASN A 1 76 ? -4.674 22.437 22.637 1.00 32.15 ? 164 ASN A CG 1 ATOM 591 O OD1 . ASN A 1 76 ? -4.415 23.129 21.653 1.00 37.89 ? 164 ASN A OD1 1 ATOM 592 N ND2 . ASN A 1 76 ? -4.018 22.548 23.784 1.00 38.16 ? 164 ASN A ND2 1 ATOM 593 N N . PRO A 1 77 ? -2.795 19.716 21.757 1.00 25.40 ? 165 PRO A N 1 ATOM 594 C CA . PRO A 1 77 ? -2.927 19.885 20.309 1.00 23.81 ? 165 PRO A CA 1 ATOM 595 C C . PRO A 1 77 ? -3.573 18.635 19.695 1.00 21.66 ? 165 PRO A C 1 ATOM 596 O O . PRO A 1 77 ? -3.778 17.646 20.395 1.00 19.95 ? 165 PRO A O 1 ATOM 597 C CB . PRO A 1 77 ? -1.495 20.027 19.834 1.00 24.51 ? 165 PRO A CB 1 ATOM 598 C CG . PRO A 1 77 ? -0.613 19.624 20.977 1.00 25.54 ? 165 PRO A CG 1 ATOM 599 C CD . PRO A 1 77 ? -1.439 19.350 22.159 1.00 25.93 ? 165 PRO A CD 1 ATOM 600 N N . GLN A 1 78 ? -3.897 18.709 18.419 1.00 20.15 ? 166 GLN A N 1 ATOM 601 C CA . GLN A 1 78 ? -4.586 17.627 17.757 1.00 19.19 ? 166 GLN A CA 1 ATOM 602 C C . GLN A 1 78 ? -3.684 16.403 17.705 1.00 17.80 ? 166 GLN A C 1 ATOM 603 O O . GLN A 1 78 ? -2.443 16.517 17.736 1.00 16.88 ? 166 GLN A O 1 ATOM 604 C CB . GLN A 1 78 ? -4.921 18.026 16.338 1.00 19.78 ? 166 GLN A CB 1 ATOM 605 C CG . GLN A 1 78 ? -3.648 18.144 15.523 1.00 21.89 ? 166 GLN A CG 1 ATOM 606 C CD . GLN A 1 78 ? -3.842 18.569 14.078 1.00 25.78 ? 166 GLN A CD 1 ATOM 607 O OE1 . GLN A 1 78 ? -4.771 18.123 13.400 1.00 27.11 ? 166 GLN A OE1 1 ATOM 608 N NE2 . GLN A 1 78 ? -2.926 19.399 13.594 1.00 28.02 ? 166 GLN A NE2 1 ATOM 609 N N . TYR A 1 79 ? -4.337 15.252 17.621 1.00 16.67 ? 167 TYR A N 1 ATOM 610 C CA . TYR A 1 79 ? -3.717 13.933 17.464 1.00 17.09 ? 167 TYR A CA 1 ATOM 611 C C . TYR A 1 79 ? -3.357 13.628 16.009 1.00 16.07 ? 167 TYR A C 1 ATOM 612 O O . TYR A 1 79 ? -4.104 13.980 15.063 1.00 15.77 ? 167 TYR A O 1 ATOM 613 C CB . TYR A 1 79 ? -4.690 12.864 17.943 1.00 17.90 ? 167 TYR A CB 1 ATOM 614 C CG . TYR A 1 79 ? -4.712 12.716 19.435 1.00 19.46 ? 167 TYR A CG 1 ATOM 615 C CD1 . TYR A 1 79 ? -3.621 12.187 20.089 1.00 21.05 ? 167 TYR A CD1 1 ATOM 616 C CD2 . TYR A 1 79 ? -5.821 13.092 20.195 1.00 20.95 ? 167 TYR A CD2 1 ATOM 617 C CE1 . TYR A 1 79 ? -3.598 12.055 21.442 1.00 21.39 ? 167 TYR A CE1 1 ATOM 618 C CE2 . TYR A 1 79 ? -5.814 12.967 21.568 1.00 21.58 ? 167 TYR A CE2 1 ATOM 619 C CZ . TYR A 1 79 ? -4.704 12.434 22.190 1.00 22.98 ? 167 TYR A CZ 1 ATOM 620 O OH . TYR A 1 79 ? -4.662 12.287 23.554 1.00 25.12 ? 167 TYR A OH 1 ATOM 621 N N . ALA A 1 80 ? -2.220 12.971 15.825 1.00 13.80 ? 168 ALA A N 1 ATOM 622 C CA . ALA A 1 80 ? -1.842 12.512 14.524 1.00 13.91 ? 168 ALA A CA 1 ATOM 623 C C . ALA A 1 80 ? -1.738 11.004 14.548 1.00 13.17 ? 168 ALA A C 1 ATOM 624 O O . ALA A 1 80 ? -1.428 10.407 15.591 1.00 13.10 ? 168 ALA A O 1 ATOM 625 C CB . ALA A 1 80 ? -0.525 13.088 14.117 1.00 13.95 ? 168 ALA A CB 1 ATOM 626 N N . ALA A 1 81 ? -1.927 10.408 13.368 1.00 12.91 ? 169 ALA A N 1 ATOM 627 C CA . ALA A 1 81 ? -1.819 8.957 13.187 1.00 11.77 ? 169 ALA A CA 1 ATOM 628 C C . ALA A 1 81 ? -0.422 8.510 12.767 1.00 12.23 ? 169 ALA A C 1 ATOM 629 O O . ALA A 1 81 ? 0.268 9.223 12.010 1.00 12.66 ? 169 ALA A O 1 ATOM 630 C CB . ALA A 1 81 ? -2.777 8.526 12.146 1.00 12.62 ? 169 ALA A CB 1 ATOM 631 N N . GLN A 1 82 ? -0.023 7.312 13.220 1.00 11.24 ? 170 GLN A N 1 ATOM 632 C CA . GLN A 1 82 ? 1.242 6.682 12.791 1.00 11.76 ? 170 GLN A CA 1 ATOM 633 C C . GLN A 1 82 ? 0.888 5.305 12.239 1.00 10.75 ? 170 GLN A C 1 ATOM 634 O O . GLN A 1 82 ? 0.465 4.423 12.999 1.00 10.75 ? 170 GLN A O 1 ATOM 635 C CB . GLN A 1 82 ? 2.232 6.548 13.947 1.00 11.85 ? 170 GLN A CB 1 ATOM 636 C CG . GLN A 1 82 ? 2.555 7.854 14.709 1.00 10.66 ? 170 GLN A CG 1 ATOM 637 C CD . GLN A 1 82 ? 3.378 7.611 15.944 1.00 11.73 ? 170 GLN A CD 1 ATOM 638 O OE1 . GLN A 1 82 ? 4.620 7.658 15.895 1.00 12.19 ? 170 GLN A OE1 1 ATOM 639 N NE2 . GLN A 1 82 ? 2.713 7.290 17.035 1.00 12.05 ? 170 GLN A NE2 1 ATOM 640 N N . ILE A 1 83 ? 1.092 5.116 10.942 1.00 11.33 ? 171 ILE A N 1 ATOM 641 C CA . ILE A 1 83 ? 0.705 3.893 10.241 1.00 11.18 ? 171 ILE A CA 1 ATOM 642 C C . ILE A 1 83 ? 1.871 3.323 9.462 1.00 11.27 ? 171 ILE A C 1 ATOM 643 O O . ILE A 1 83 ? 2.663 4.067 8.856 1.00 10.45 ? 171 ILE A O 1 ATOM 644 C CB . ILE A 1 83 ? -0.433 4.197 9.276 1.00 11.58 ? 171 ILE A CB 1 ATOM 645 C CG1 . ILE A 1 83 ? -1.633 4.809 10.010 1.00 11.24 ? 171 ILE A CG1 1 ATOM 646 C CG2 . ILE A 1 83 ? -0.762 2.973 8.359 1.00 11.52 ? 171 ILE A CG2 1 ATOM 647 C CD1 . ILE A 1 83 ? -2.390 3.921 11.064 1.00 15.55 ? 171 ILE A CD1 1 ATOM 648 N N . VAL A 1 84 ? 2.003 2.005 9.504 1.00 9.92 ? 172 VAL A N 1 ATOM 649 C CA . VAL A 1 84 ? 2.990 1.310 8.659 1.00 10.23 ? 172 VAL A CA 1 ATOM 650 C C . VAL A 1 84 ? 2.332 0.612 7.474 1.00 10.31 ? 172 VAL A C 1 ATOM 651 O O . VAL A 1 84 ? 1.390 -0.173 7.632 1.00 10.99 ? 172 VAL A O 1 ATOM 652 C CB . VAL A 1 84 ? 3.774 0.225 9.437 1.00 10.45 ? 172 VAL A CB 1 ATOM 653 C CG1 . VAL A 1 84 ? 4.890 -0.343 8.551 1.00 10.53 ? 172 VAL A CG1 1 ATOM 654 C CG2 . VAL A 1 84 ? 4.333 0.794 10.736 1.00 11.30 ? 172 VAL A CG2 1 ATOM 655 N N . VAL A 1 85 ? 2.844 0.869 6.284 1.00 10.21 ? 173 VAL A N 1 ATOM 656 C CA . VAL A 1 85 ? 2.389 0.157 5.094 1.00 10.65 ? 173 VAL A CA 1 ATOM 657 C C . VAL A 1 85 ? 3.305 -1.049 4.933 1.00 11.09 ? 173 VAL A C 1 ATOM 658 O O . VAL A 1 85 ? 4.519 -0.889 4.806 1.00 10.10 ? 173 VAL A O 1 ATOM 659 C CB . VAL A 1 85 ? 2.477 1.079 3.884 1.00 10.98 ? 173 VAL A CB 1 ATOM 660 C CG1 . VAL A 1 85 ? 2.065 0.352 2.624 1.00 11.65 ? 173 VAL A CG1 1 ATOM 661 C CG2 . VAL A 1 85 ? 1.592 2.298 4.111 1.00 10.83 ? 173 VAL A CG2 1 ATOM 662 N N . TYR A 1 86 ? 2.740 -2.253 4.967 1.00 10.99 ? 174 TYR A N 1 ATOM 663 C CA . TYR A 1 86 ? 3.565 -3.466 5.070 1.00 11.63 ? 174 TYR A CA 1 ATOM 664 C C . TYR A 1 86 ? 2.918 -4.673 4.408 1.00 11.45 ? 174 TYR A C 1 ATOM 665 O O . TYR A 1 86 ? 2.453 -5.602 5.087 1.00 11.39 ? 174 TYR A O 1 ATOM 666 C CB . TYR A 1 86 ? 3.813 -3.774 6.533 1.00 12.28 ? 174 TYR A CB 1 ATOM 667 C CG . TYR A 1 86 ? 4.789 -4.894 6.776 1.00 12.11 ? 174 TYR A CG 1 ATOM 668 C CD1 . TYR A 1 86 ? 6.049 -4.888 6.179 1.00 14.09 ? 174 TYR A CD1 1 ATOM 669 C CD2 . TYR A 1 86 ? 4.463 -5.953 7.608 1.00 10.95 ? 174 TYR A CD2 1 ATOM 670 C CE1 . TYR A 1 86 ? 6.964 -5.927 6.413 1.00 10.49 ? 174 TYR A CE1 1 ATOM 671 C CE2 . TYR A 1 86 ? 5.355 -6.982 7.854 1.00 10.49 ? 174 TYR A CE2 1 ATOM 672 C CZ . TYR A 1 86 ? 6.602 -6.987 7.247 1.00 12.64 ? 174 TYR A CZ 1 ATOM 673 O OH . TYR A 1 86 ? 7.470 -8.065 7.518 1.00 11.03 ? 174 TYR A OH 1 ATOM 674 N N . ASP A 1 87 ? 2.927 -4.681 3.082 1.00 12.18 ? 175 ASP A N 1 ATOM 675 C CA . ASP A 1 87 ? 2.296 -5.779 2.344 1.00 11.81 ? 175 ASP A CA 1 ATOM 676 C C . ASP A 1 87 ? 2.790 -5.970 0.904 1.00 12.03 ? 175 ASP A C 1 ATOM 677 O O . ASP A 1 87 ? 2.048 -6.472 0.037 1.00 11.44 ? 175 ASP A O 1 ATOM 678 C CB . ASP A 1 87 ? 0.792 -5.617 2.396 1.00 12.18 ? 175 ASP A CB 1 ATOM 679 C CG . ASP A 1 87 ? 0.044 -6.937 2.358 1.00 13.37 ? 175 ASP A CG 1 ATOM 680 O OD1 . ASP A 1 87 ? 0.675 -8.011 2.426 1.00 11.33 ? 175 ASP A OD1 1 ATOM 681 O OD2 . ASP A 1 87 ? -1.196 -6.966 2.271 1.00 14.86 ? 175 ASP A OD2 1 ATOM 682 N N . LEU A 1 88 ? 4.062 -5.658 0.665 1.00 11.86 ? 176 LEU A N 1 ATOM 683 C CA . LEU A 1 88 ? 4.662 -5.956 -0.632 1.00 12.50 ? 176 LEU A CA 1 ATOM 684 C C . LEU A 1 88 ? 4.493 -7.443 -0.955 1.00 12.88 ? 176 LEU A C 1 ATOM 685 O O . LEU A 1 88 ? 4.508 -8.286 -0.060 1.00 12.24 ? 176 LEU A O 1 ATOM 686 C CB . LEU A 1 88 ? 6.141 -5.636 -0.637 1.00 12.52 ? 176 LEU A CB 1 ATOM 687 C CG . LEU A 1 88 ? 6.408 -4.144 -0.759 1.00 13.43 ? 176 LEU A CG 1 ATOM 688 C CD1 . LEU A 1 88 ? 7.837 -3.871 -0.474 1.00 11.85 ? 176 LEU A CD1 1 ATOM 689 C CD2 . LEU A 1 88 ? 6.059 -3.652 -2.163 1.00 13.13 ? 176 LEU A CD2 1 ATOM 690 N N . PRO A 1 89 ? 4.320 -7.755 -2.233 1.00 12.89 ? 177 PRO A N 1 ATOM 691 C CA . PRO A 1 89 ? 4.293 -9.151 -2.666 1.00 12.74 ? 177 PRO A CA 1 ATOM 692 C C . PRO A 1 89 ? 5.695 -9.688 -2.520 1.00 13.05 ? 177 PRO A C 1 ATOM 693 O O . PRO A 1 89 ? 6.661 -8.927 -2.612 1.00 13.13 ? 177 PRO A O 1 ATOM 694 C CB . PRO A 1 89 ? 3.925 -9.078 -4.164 1.00 13.31 ? 177 PRO A CB 1 ATOM 695 C CG . PRO A 1 89 ? 4.171 -7.684 -4.613 1.00 12.96 ? 177 PRO A CG 1 ATOM 696 C CD . PRO A 1 89 ? 4.196 -6.813 -3.358 1.00 12.27 ? 177 PRO A CD 1 ATOM 697 N N . ASP A 1 90 ? 5.813 -10.996 -2.295 1.00 13.11 ? 178 ASP A N 1 ATOM 698 C CA . ASP A 1 90 ? 7.097 -11.614 -2.012 1.00 13.69 ? 178 ASP A CA 1 ATOM 699 C C . ASP A 1 90 ? 7.774 -10.879 -0.851 1.00 12.76 ? 178 ASP A C 1 ATOM 700 O O . ASP A 1 90 ? 8.977 -10.594 -0.894 1.00 13.03 ? 178 ASP A O 1 ATOM 701 C CB . ASP A 1 90 ? 7.989 -11.624 -3.246 1.00 13.77 ? 178 ASP A CB 1 ATOM 702 C CG . ASP A 1 90 ? 7.695 -12.817 -4.194 1.00 16.78 ? 178 ASP A CG 1 ATOM 703 O OD1 . ASP A 1 90 ? 6.540 -13.301 -4.245 1.00 15.42 ? 178 ASP A OD1 1 ATOM 704 O OD2 . ASP A 1 90 ? 8.616 -13.333 -4.892 1.00 16.07 ? 178 ASP A OD2 1 ATOM 705 N N . ARG A 1 91 ? 6.979 -10.559 0.166 1.00 12.41 ? 179 ARG A N 1 ATOM 706 C CA . ARG A 1 91 ? 7.438 -9.866 1.362 1.00 12.30 ? 179 ARG A CA 1 ATOM 707 C C . ARG A 1 91 ? 8.535 -10.598 2.102 1.00 12.29 ? 179 ARG A C 1 ATOM 708 O O . ARG A 1 91 ? 8.531 -11.819 2.181 1.00 11.80 ? 179 ARG A O 1 ATOM 709 C CB . ARG A 1 91 ? 6.272 -9.643 2.332 1.00 12.68 ? 179 ARG A CB 1 ATOM 710 C CG . ARG A 1 91 ? 6.378 -8.349 3.099 1.00 13.49 ? 179 ARG A CG 1 ATOM 711 C CD . ARG A 1 91 ? 5.225 -8.045 4.046 1.00 14.27 ? 179 ARG A CD 1 ATOM 712 N NE . ARG A 1 91 ? 5.145 -8.998 5.144 1.00 14.96 ? 179 ARG A NE 1 ATOM 713 C CZ . ARG A 1 91 ? 4.068 -9.182 5.882 1.00 14.63 ? 179 ARG A CZ 1 ATOM 714 N NH1 . ARG A 1 91 ? 2.975 -8.471 5.645 1.00 12.44 ? 179 ARG A NH1 1 ATOM 715 N NH2 . ARG A 1 91 ? 4.103 -10.056 6.874 1.00 17.67 ? 179 ARG A NH2 1 ATOM 716 N N . ASP A 1 92 ? 9.478 -9.838 2.640 1.00 13.25 ? 180 ASP A N 1 ATOM 717 C CA . ASP A 1 92 ? 10.534 -10.399 3.474 1.00 14.42 ? 180 ASP A CA 1 ATOM 718 C C . ASP A 1 92 ? 11.277 -11.460 2.683 1.00 14.59 ? 180 ASP A C 1 ATOM 719 O O . ASP A 1 92 ? 11.350 -12.640 3.060 1.00 14.38 ? 180 ASP A O 1 ATOM 720 C CB . ASP A 1 92 ? 9.918 -10.964 4.746 1.00 14.49 ? 180 ASP A CB 1 ATOM 721 C CG . ASP A 1 92 ? 8.923 -10.003 5.399 1.00 16.57 ? 180 ASP A CG 1 ATOM 722 O OD1 . ASP A 1 92 ? 9.302 -8.873 5.893 1.00 12.22 ? 180 ASP A OD1 1 ATOM 723 O OD2 . ASP A 1 92 ? 7.727 -10.315 5.455 1.00 16.00 ? 180 ASP A OD2 1 ATOM 724 N N . CYS A 1 93 ? 11.873 -11.010 1.582 1.00 15.89 ? 181 CYS A N 1 ATOM 725 C CA . CYS A 1 93 ? 12.445 -11.906 0.580 1.00 17.40 ? 181 CYS A CA 1 ATOM 726 C C . CYS A 1 93 ? 13.581 -12.780 1.074 1.00 17.54 ? 181 CYS A C 1 ATOM 727 O O . CYS A 1 93 ? 13.847 -13.843 0.478 1.00 18.30 ? 181 CYS A O 1 ATOM 728 C CB . CYS A 1 93 ? 12.911 -11.123 -0.642 1.00 17.70 ? 181 CYS A CB 1 ATOM 729 S SG . CYS A 1 93 ? 14.235 -9.939 -0.257 1.00 20.40 ? 181 CYS A SG 1 ATOM 730 N N . ALA A 1 94 ? 14.215 -12.404 2.177 1.00 18.61 ? 182 ALA A N 1 ATOM 731 C CA . ALA A 1 94 ? 15.354 -13.161 2.679 1.00 19.81 ? 182 ALA A CA 1 ATOM 732 C C . ALA A 1 94 ? 14.942 -14.349 3.549 1.00 21.27 ? 182 ALA A C 1 ATOM 733 O O . ALA A 1 94 ? 15.771 -15.178 3.917 1.00 20.46 ? 182 ALA A O 1 ATOM 734 C CB . ALA A 1 94 ? 16.260 -12.258 3.459 1.00 19.25 ? 182 ALA A CB 1 ATOM 735 N N . ALA A 1 95 ? 13.665 -14.424 3.890 1.00 22.72 ? 183 ALA A N 1 ATOM 736 C CA . ALA A 1 95 ? 13.199 -15.480 4.761 1.00 23.98 ? 183 ALA A CA 1 ATOM 737 C C . ALA A 1 95 ? 12.826 -16.677 3.905 1.00 26.03 ? 183 ALA A C 1 ATOM 738 O O . ALA A 1 95 ? 12.493 -16.536 2.732 1.00 26.14 ? 183 ALA A O 1 ATOM 739 C CB . ALA A 1 95 ? 12.003 -15.013 5.572 1.00 24.48 ? 183 ALA A CB 1 ATOM 740 N N . ALA A 1 96 ? 12.856 -17.850 4.511 1.00 27.64 ? 184 ALA A N 1 ATOM 741 C CA . ALA A 1 96 ? 12.496 -19.057 3.809 1.00 29.28 ? 184 ALA A CA 1 ATOM 742 C C . ALA A 1 96 ? 11.031 -18.945 3.423 1.00 29.94 ? 184 ALA A C 1 ATOM 743 O O . ALA A 1 96 ? 10.671 -19.078 2.257 1.00 30.97 ? 184 ALA A O 1 ATOM 744 C CB . ALA A 1 96 ? 12.754 -20.278 4.714 1.00 29.79 ? 184 ALA A CB 1 ATOM 745 N N . ALA A 1 97 ? 10.203 -18.581 4.392 1.00 30.30 ? 185 ALA A N 1 ATOM 746 C CA . ALA A 1 97 ? 8.766 -18.462 4.176 1.00 30.46 ? 185 ALA A CA 1 ATOM 747 C C . ALA A 1 97 ? 8.275 -17.233 4.926 1.00 30.28 ? 185 ALA A C 1 ATOM 748 O O . ALA A 1 97 ? 8.462 -17.114 6.141 1.00 30.52 ? 185 ALA A O 1 ATOM 749 C CB . ALA A 1 97 ? 8.089 -19.691 4.701 1.00 30.96 ? 185 ALA A CB 1 ATOM 750 N N . SER A 1 98 ? 7.648 -16.317 4.212 1.00 30.11 ? 186 SER A N 1 ATOM 751 C CA . SER A 1 98 ? 7.172 -15.082 4.833 1.00 29.03 ? 186 SER A CA 1 ATOM 752 C C . SER A 1 98 ? 5.739 -15.182 5.287 1.00 27.63 ? 186 SER A C 1 ATOM 753 O O . SER A 1 98 ? 4.975 -15.983 4.774 1.00 26.59 ? 186 SER A O 1 ATOM 754 C CB . SER A 1 98 ? 7.298 -13.923 3.838 1.00 29.18 ? 186 SER A CB 1 ATOM 755 O OG . SER A 1 98 ? 6.783 -12.711 4.369 1.00 28.45 ? 186 SER A OG 1 ATOM 756 N N . ASN A 1 99 ? 5.384 -14.373 6.276 1.00 26.22 ? 187 ASN A N 1 ATOM 757 C CA . ASN A 1 99 ? 3.995 -14.238 6.613 1.00 26.39 ? 187 ASN A CA 1 ATOM 758 C C . ASN A 1 99 ? 3.259 -13.368 5.596 1.00 24.26 ? 187 ASN A C 1 ATOM 759 O O . ASN A 1 99 ? 2.050 -13.277 5.665 1.00 24.86 ? 187 ASN A O 1 ATOM 760 C CB . ASN A 1 99 ? 3.804 -13.664 8.012 1.00 27.38 ? 187 ASN A CB 1 ATOM 761 C CG . ASN A 1 99 ? 4.646 -14.378 9.047 1.00 30.71 ? 187 ASN A CG 1 ATOM 762 O OD1 . ASN A 1 99 ? 4.126 -15.143 9.857 1.00 32.60 ? 187 ASN A OD1 1 ATOM 763 N ND2 . ASN A 1 99 ? 5.975 -14.118 9.024 1.00 33.43 ? 187 ASN A ND2 1 ATOM 764 N N . GLY A 1 100 ? 3.952 -12.762 4.633 1.00 22.05 ? 188 GLY A N 1 ATOM 765 C CA . GLY A 1 100 ? 3.255 -11.940 3.647 1.00 20.71 ? 188 GLY A CA 1 ATOM 766 C C . GLY A 1 100 ? 2.225 -12.725 2.853 1.00 18.82 ? 188 GLY A C 1 ATOM 767 O O . GLY A 1 100 ? 2.426 -13.891 2.548 1.00 17.25 ? 188 GLY A O 1 ATOM 768 N N . GLU A 1 101 ? 1.110 -12.100 2.510 1.00 17.52 ? 189 GLU A N 1 ATOM 769 C CA . GLU A 1 101 ? 0.023 -12.837 1.862 1.00 16.78 ? 189 GLU A CA 1 ATOM 770 C C . GLU A 1 101 ? 0.058 -12.884 0.327 1.00 16.49 ? 189 GLU A C 1 ATOM 771 O O . GLU A 1 101 ? -0.574 -13.758 -0.289 1.00 16.91 ? 189 GLU A O 1 ATOM 772 C CB . GLU A 1 101 ? -1.335 -12.341 2.347 1.00 17.01 ? 189 GLU A CB 1 ATOM 773 C CG . GLU A 1 101 ? -1.696 -10.972 1.781 1.00 16.32 ? 189 GLU A CG 1 ATOM 774 C CD . GLU A 1 101 ? -2.726 -10.233 2.607 1.00 19.24 ? 189 GLU A CD 1 ATOM 775 O OE1 . GLU A 1 101 ? -3.602 -10.905 3.218 1.00 19.14 ? 189 GLU A OE1 1 ATOM 776 O OE2 . GLU A 1 101 ? -2.659 -8.975 2.633 1.00 13.22 ? 189 GLU A OE2 1 ATOM 777 N N . TRP A 1 102 ? 0.805 -11.993 -0.304 1.00 14.80 ? 190 TRP A N 1 ATOM 778 C CA . TRP A 1 102 ? 0.814 -11.948 -1.760 1.00 14.10 ? 190 TRP A CA 1 ATOM 779 C C . TRP A 1 102 ? 2.123 -12.381 -2.388 1.00 13.72 ? 190 TRP A C 1 ATOM 780 O O . TRP A 1 102 ? 3.197 -12.350 -1.774 1.00 13.13 ? 190 TRP A O 1 ATOM 781 C CB . TRP A 1 102 ? 0.461 -10.540 -2.227 1.00 13.47 ? 190 TRP A CB 1 ATOM 782 C CG . TRP A 1 102 ? -0.919 -10.194 -1.887 1.00 15.29 ? 190 TRP A CG 1 ATOM 783 C CD1 . TRP A 1 102 ? -1.977 -11.040 -1.832 1.00 16.33 ? 190 TRP A CD1 1 ATOM 784 C CD2 . TRP A 1 102 ? -1.428 -8.887 -1.573 1.00 14.17 ? 190 TRP A CD2 1 ATOM 785 N NE1 . TRP A 1 102 ? -3.104 -10.360 -1.453 1.00 15.90 ? 190 TRP A NE1 1 ATOM 786 C CE2 . TRP A 1 102 ? -2.793 -9.030 -1.302 1.00 15.18 ? 190 TRP A CE2 1 ATOM 787 C CE3 . TRP A 1 102 ? -0.841 -7.622 -1.427 1.00 11.94 ? 190 TRP A CE3 1 ATOM 788 C CZ2 . TRP A 1 102 ? -3.611 -7.941 -0.949 1.00 16.43 ? 190 TRP A CZ2 1 ATOM 789 C CZ3 . TRP A 1 102 ? -1.646 -6.536 -1.098 1.00 14.02 ? 190 TRP A CZ3 1 ATOM 790 C CH2 . TRP A 1 102 ? -3.008 -6.704 -0.832 1.00 14.70 ? 190 TRP A CH2 1 ATOM 791 N N . ALA A 1 103 ? 2.034 -12.796 -3.640 1.00 14.45 ? 191 ALA A N 1 ATOM 792 C CA . ALA A 1 103 ? 3.186 -13.239 -4.376 1.00 13.51 ? 191 ALA A CA 1 ATOM 793 C C . ALA A 1 103 ? 3.276 -12.567 -5.720 1.00 13.75 ? 191 ALA A C 1 ATOM 794 O O . ALA A 1 103 ? 2.297 -12.421 -6.441 1.00 12.95 ? 191 ALA A O 1 ATOM 795 C CB . ALA A 1 103 ? 3.169 -14.749 -4.562 1.00 14.67 ? 191 ALA A CB 1 ATOM 796 N N . ILE A 1 104 ? 4.490 -12.205 -6.085 1.00 14.12 ? 192 ILE A N 1 ATOM 797 C CA . ILE A 1 104 ? 4.711 -11.594 -7.371 1.00 15.85 ? 192 ILE A CA 1 ATOM 798 C C . ILE A 1 104 ? 4.169 -12.477 -8.505 1.00 16.79 ? 192 ILE A C 1 ATOM 799 O O . ILE A 1 104 ? 3.528 -11.973 -9.444 1.00 16.55 ? 192 ILE A O 1 ATOM 800 C CB . ILE A 1 104 ? 6.190 -11.349 -7.566 1.00 15.51 ? 192 ILE A CB 1 ATOM 801 C CG1 . ILE A 1 104 ? 6.676 -10.298 -6.569 1.00 16.98 ? 192 ILE A CG1 1 ATOM 802 C CG2 . ILE A 1 104 ? 6.434 -10.908 -8.962 1.00 18.09 ? 192 ILE A CG2 1 ATOM 803 C CD1 . ILE A 1 104 ? 8.143 -9.943 -6.732 1.00 17.78 ? 192 ILE A CD1 1 ATOM 804 N N . ALA A 1 105 ? 4.409 -13.791 -8.414 1.00 15.90 ? 193 ALA A N 1 ATOM 805 C CA . ALA A 1 105 ? 3.978 -14.712 -9.467 1.00 16.07 ? 193 ALA A CA 1 ATOM 806 C C . ALA A 1 105 ? 2.464 -14.944 -9.528 1.00 15.56 ? 193 ALA A C 1 ATOM 807 O O . ALA A 1 105 ? 1.970 -15.538 -10.515 1.00 15.88 ? 193 ALA A O 1 ATOM 808 C CB . ALA A 1 105 ? 4.720 -16.054 -9.346 1.00 16.32 ? 193 ALA A CB 1 ATOM 809 N N . ASN A 1 106 ? 1.736 -14.508 -8.493 1.00 14.96 ? 194 ASN A N 1 ATOM 810 C CA . ASN A 1 106 ? 0.290 -14.693 -8.400 1.00 15.12 ? 194 ASN A CA 1 ATOM 811 C C . ASN A 1 106 ? -0.453 -13.377 -8.232 1.00 14.79 ? 194 ASN A C 1 ATOM 812 O O . ASN A 1 106 ? -1.205 -13.208 -7.273 1.00 14.76 ? 194 ASN A O 1 ATOM 813 C CB . ASN A 1 106 ? -0.067 -15.579 -7.204 1.00 15.15 ? 194 ASN A CB 1 ATOM 814 C CG . ASN A 1 106 ? -1.446 -16.173 -7.308 1.00 15.66 ? 194 ASN A CG 1 ATOM 815 O OD1 . ASN A 1 106 ? -2.072 -16.138 -8.370 1.00 14.21 ? 194 ASN A OD1 1 ATOM 816 N ND2 . ASN A 1 106 ? -1.934 -16.747 -6.190 1.00 15.05 ? 194 ASN A ND2 1 ATOM 817 N N . ASN A 1 107 ? -0.223 -12.474 -9.173 1.00 15.62 ? 195 ASN A N 1 ATOM 818 C CA . ASN A 1 107 ? -0.918 -11.178 -9.271 1.00 16.02 ? 195 ASN A CA 1 ATOM 819 C C . ASN A 1 107 ? -0.606 -10.208 -8.116 1.00 16.06 ? 195 ASN A C 1 ATOM 820 O O . ASN A 1 107 ? -1.382 -9.294 -7.848 1.00 17.03 ? 195 ASN A O 1 ATOM 821 C CB . ASN A 1 107 ? -2.423 -11.386 -9.435 1.00 16.11 ? 195 ASN A CB 1 ATOM 822 C CG . ASN A 1 107 ? -3.065 -10.311 -10.319 1.00 17.01 ? 195 ASN A CG 1 ATOM 823 O OD1 . ASN A 1 107 ? -2.473 -9.859 -11.275 1.00 23.19 ? 195 ASN A OD1 1 ATOM 824 N ND2 . ASN A 1 107 ? -4.255 -9.884 -9.964 1.00 20.90 ? 195 ASN A ND2 1 ATOM 825 N N . GLY A 1 108 ? 0.533 -10.422 -7.466 1.00 15.85 ? 196 GLY A N 1 ATOM 826 C CA . GLY A 1 108 ? 1.018 -9.614 -6.365 1.00 16.60 ? 196 GLY A CA 1 ATOM 827 C C . GLY A 1 108 ? 1.136 -8.125 -6.664 1.00 15.70 ? 196 GLY A C 1 ATOM 828 O O . GLY A 1 108 ? 0.725 -7.330 -5.849 1.00 14.21 ? 196 GLY A O 1 ATOM 829 N N . VAL A 1 109 ? 1.673 -7.768 -7.813 1.00 16.47 ? 197 VAL A N 1 ATOM 830 C CA . VAL A 1 109 ? 1.768 -6.356 -8.188 1.00 17.42 ? 197 VAL A CA 1 ATOM 831 C C . VAL A 1 109 ? 0.373 -5.699 -8.227 1.00 17.24 ? 197 VAL A C 1 ATOM 832 O O . VAL A 1 109 ? 0.140 -4.650 -7.599 1.00 16.60 ? 197 VAL A O 1 ATOM 833 C CB . VAL A 1 109 ? 2.469 -6.215 -9.516 1.00 17.68 ? 197 VAL A CB 1 ATOM 834 C CG1 . VAL A 1 109 ? 2.179 -4.869 -10.149 1.00 20.72 ? 197 VAL A CG1 1 ATOM 835 C CG2 . VAL A 1 109 ? 3.940 -6.391 -9.341 1.00 18.12 ? 197 VAL A CG2 1 ATOM 836 N N . ASN A 1 110 ? -0.566 -6.311 -8.948 1.00 17.71 ? 198 ASN A N 1 ATOM 837 C CA . ASN A 1 110 ? -1.923 -5.759 -9.016 1.00 17.90 ? 198 ASN A CA 1 ATOM 838 C C . ASN A 1 110 ? -2.609 -5.712 -7.658 1.00 16.93 ? 198 ASN A C 1 ATOM 839 O O . ASN A 1 110 ? -3.422 -4.819 -7.384 1.00 17.17 ? 198 ASN A O 1 ATOM 840 C CB . ASN A 1 110 ? -2.826 -6.553 -9.969 1.00 18.97 ? 198 ASN A CB 1 ATOM 841 C CG . ASN A 1 110 ? -2.530 -6.308 -11.426 1.00 21.39 ? 198 ASN A CG 1 ATOM 842 O OD1 . ASN A 1 110 ? -1.951 -5.280 -11.822 1.00 24.45 ? 198 ASN A OD1 1 ATOM 843 N ND2 . ASN A 1 110 ? -2.932 -7.271 -12.253 1.00 25.29 ? 198 ASN A ND2 1 ATOM 844 N N . ASN A 1 111 ? -2.370 -6.715 -6.821 1.00 15.62 ? 199 ASN A N 1 ATOM 845 C CA . ASN A 1 111 ? -2.992 -6.722 -5.508 1.00 15.48 ? 199 ASN A CA 1 ATOM 846 C C . ASN A 1 111 ? -2.438 -5.543 -4.688 1.00 15.16 ? 199 ASN A C 1 ATOM 847 O O . ASN A 1 111 ? -3.171 -4.849 -3.966 1.00 15.37 ? 199 ASN A O 1 ATOM 848 C CB . ASN A 1 111 ? -2.696 -8.016 -4.757 1.00 15.94 ? 199 ASN A CB 1 ATOM 849 C CG . ASN A 1 111 ? -3.376 -9.227 -5.385 1.00 16.72 ? 199 ASN A CG 1 ATOM 850 O OD1 . ASN A 1 111 ? -4.227 -9.085 -6.258 1.00 16.86 ? 199 ASN A OD1 1 ATOM 851 N ND2 . ASN A 1 111 ? -2.969 -10.415 -4.967 1.00 15.84 ? 199 ASN A ND2 1 ATOM 852 N N . TYR A 1 112 ? -1.142 -5.321 -4.828 1.00 15.08 ? 200 TYR A N 1 ATOM 853 C CA . TYR A 1 112 ? -0.499 -4.293 -4.017 1.00 15.21 ? 200 TYR A CA 1 ATOM 854 C C . TYR A 1 112 ? -0.928 -2.907 -4.482 1.00 14.46 ? 200 TYR A C 1 ATOM 855 O O . TYR A 1 112 ? -1.221 -2.017 -3.656 1.00 12.41 ? 200 TYR A O 1 ATOM 856 C CB . TYR A 1 112 ? 1.000 -4.419 -4.099 1.00 14.93 ? 200 TYR A CB 1 ATOM 857 C CG . TYR A 1 112 ? 1.691 -3.515 -3.113 1.00 14.95 ? 200 TYR A CG 1 ATOM 858 C CD1 . TYR A 1 112 ? 1.802 -3.869 -1.783 1.00 13.39 ? 200 TYR A CD1 1 ATOM 859 C CD2 . TYR A 1 112 ? 2.195 -2.308 -3.494 1.00 15.37 ? 200 TYR A CD2 1 ATOM 860 C CE1 . TYR A 1 112 ? 2.441 -3.063 -0.875 1.00 13.94 ? 200 TYR A CE1 1 ATOM 861 C CE2 . TYR A 1 112 ? 2.829 -1.456 -2.557 1.00 14.94 ? 200 TYR A CE2 1 ATOM 862 C CZ . TYR A 1 112 ? 2.940 -1.848 -1.272 1.00 13.69 ? 200 TYR A CZ 1 ATOM 863 O OH . TYR A 1 112 ? 3.580 -1.057 -0.342 1.00 12.12 ? 200 TYR A OH 1 ATOM 864 N N . LYS A 1 113 ? -0.991 -2.726 -5.789 1.00 14.28 ? 201 LYS A N 1 ATOM 865 C CA . LYS A 1 113 ? -1.510 -1.437 -6.324 1.00 15.82 ? 201 LYS A CA 1 ATOM 866 C C . LYS A 1 113 ? -2.904 -1.113 -5.860 1.00 16.03 ? 201 LYS A C 1 ATOM 867 O O . LYS A 1 113 ? -3.173 0.035 -5.530 1.00 17.62 ? 201 LYS A O 1 ATOM 868 C CB . LYS A 1 113 ? -1.451 -1.371 -7.833 1.00 16.46 ? 201 LYS A CB 1 ATOM 869 C CG . LYS A 1 113 ? -0.068 -1.398 -8.288 1.00 17.44 ? 201 LYS A CG 1 ATOM 870 C CD . LYS A 1 113 ? -0.017 -1.322 -9.743 1.00 21.50 ? 201 LYS A CD 1 ATOM 871 C CE . LYS A 1 113 ? 1.377 -1.053 -10.216 1.00 22.75 ? 201 LYS A CE 1 ATOM 872 N NZ . LYS A 1 113 ? 1.434 -0.820 -11.680 1.00 27.18 ? 201 LYS A NZ 1 ATOM 873 N N . ALA A 1 114 ? -3.811 -2.090 -5.854 1.00 16.60 ? 202 ALA A N 1 ATOM 874 C CA . ALA A 1 114 ? -5.153 -1.874 -5.315 1.00 16.32 ? 202 ALA A CA 1 ATOM 875 C C . ALA A 1 114 ? -5.125 -1.506 -3.827 1.00 16.28 ? 202 ALA A C 1 ATOM 876 O O . ALA A 1 114 ? -5.861 -0.618 -3.428 1.00 15.14 ? 202 ALA A O 1 ATOM 877 C CB . ALA A 1 114 ? -6.035 -3.087 -5.549 1.00 17.31 ? 202 ALA A CB 1 ATOM 878 N N . TYR A 1 115 ? -4.391 -2.295 -3.019 1.00 15.27 ? 203 TYR A N 1 ATOM 879 C CA . TYR A 1 115 ? -4.010 -1.982 -1.635 1.00 14.70 ? 203 TYR A CA 1 ATOM 880 C C . TYR A 1 115 ? -3.603 -0.491 -1.482 1.00 14.00 ? 203 TYR A C 1 ATOM 881 O O . TYR A 1 115 ? -4.165 0.224 -0.707 1.00 13.03 ? 203 TYR A O 1 ATOM 882 C CB . TYR A 1 115 ? -2.809 -2.847 -1.296 1.00 14.62 ? 203 TYR A CB 1 ATOM 883 C CG . TYR A 1 115 ? -2.178 -2.669 0.060 1.00 12.75 ? 203 TYR A CG 1 ATOM 884 C CD1 . TYR A 1 115 ? -2.862 -3.014 1.189 1.00 13.61 ? 203 TYR A CD1 1 ATOM 885 C CD2 . TYR A 1 115 ? -0.885 -2.215 0.202 1.00 13.24 ? 203 TYR A CD2 1 ATOM 886 C CE1 . TYR A 1 115 ? -2.267 -2.963 2.466 1.00 13.09 ? 203 TYR A CE1 1 ATOM 887 C CE2 . TYR A 1 115 ? -0.292 -2.113 1.442 1.00 12.20 ? 203 TYR A CE2 1 ATOM 888 C CZ . TYR A 1 115 ? -0.964 -2.491 2.569 1.00 11.39 ? 203 TYR A CZ 1 ATOM 889 O OH . TYR A 1 115 ? -0.208 -2.364 3.760 1.00 13.79 ? 203 TYR A OH 1 ATOM 890 N N . ILE A 1 116 ? -2.612 -0.059 -2.231 1.00 14.01 ? 204 ILE A N 1 ATOM 891 C CA . ILE A 1 116 ? -2.173 1.330 -2.139 1.00 15.66 ? 204 ILE A CA 1 ATOM 892 C C . ILE A 1 116 ? -3.313 2.302 -2.525 1.00 15.98 ? 204 ILE A C 1 ATOM 893 O O . ILE A 1 116 ? -3.577 3.297 -1.841 1.00 14.70 ? 204 ILE A O 1 ATOM 894 C CB . ILE A 1 116 ? -0.972 1.524 -3.008 1.00 15.82 ? 204 ILE A CB 1 ATOM 895 C CG1 . ILE A 1 116 ? 0.268 0.834 -2.392 1.00 16.67 ? 204 ILE A CG1 1 ATOM 896 C CG2 . ILE A 1 116 ? -0.674 3.013 -3.190 1.00 17.34 ? 204 ILE A CG2 1 ATOM 897 C CD1 . ILE A 1 116 ? 0.573 1.271 -0.998 1.00 14.80 ? 204 ILE A CD1 1 ATOM 898 N N . ASN A 1 117 ? -3.998 1.988 -3.622 1.00 16.66 ? 205 ASN A N 1 ATOM 899 C CA . ASN A 1 117 ? -5.109 2.797 -4.083 1.00 17.36 ? 205 ASN A CA 1 ATOM 900 C C . ASN A 1 117 ? -6.201 2.933 -3.072 1.00 16.97 ? 205 ASN A C 1 ATOM 901 O O . ASN A 1 117 ? -6.768 3.997 -2.894 1.00 16.98 ? 205 ASN A O 1 ATOM 902 C CB . ASN A 1 117 ? -5.715 2.182 -5.338 1.00 18.76 ? 205 ASN A CB 1 ATOM 903 C CG . ASN A 1 117 ? -4.848 2.322 -6.516 1.00 19.52 ? 205 ASN A CG 1 ATOM 904 O OD1 . ASN A 1 117 ? -3.831 3.021 -6.494 1.00 20.44 ? 205 ASN A OD1 1 ATOM 905 N ND2 . ASN A 1 117 ? -5.205 1.594 -7.576 1.00 22.80 ? 205 ASN A ND2 1 ATOM 906 N N . ARG A 1 118 ? -6.516 1.856 -2.372 1.00 16.68 ? 206 ARG A N 1 ATOM 907 C CA . ARG A 1 118 ? -7.553 1.931 -1.384 1.00 16.90 ? 206 ARG A CA 1 ATOM 908 C C . ARG A 1 118 ? -7.073 2.757 -0.165 1.00 15.40 ? 206 ARG A C 1 ATOM 909 O O . ARG A 1 118 ? -7.829 3.557 0.430 1.00 14.22 ? 206 ARG A O 1 ATOM 910 C CB . ARG A 1 118 ? -7.994 0.523 -0.994 1.00 17.96 ? 206 ARG A CB 1 ATOM 911 C CG . ARG A 1 118 ? -9.125 0.472 -0.020 1.00 19.73 ? 206 ARG A CG 1 ATOM 912 C CD . ARG A 1 118 ? -10.360 1.285 -0.442 1.00 23.96 ? 206 ARG A CD 1 ATOM 913 N NE . ARG A 1 118 ? -11.300 1.268 0.661 1.00 26.54 ? 206 ARG A NE 1 ATOM 914 C CZ . ARG A 1 118 ? -12.169 2.206 0.919 1.00 28.65 ? 206 ARG A CZ 1 ATOM 915 N NH1 . ARG A 1 118 ? -12.230 3.258 0.132 1.00 30.28 ? 206 ARG A NH1 1 ATOM 916 N NH2 . ARG A 1 118 ? -12.972 2.116 1.969 1.00 28.85 ? 206 ARG A NH2 1 ATOM 917 N N . ILE A 1 119 ? -5.819 2.559 0.214 1.00 15.25 ? 207 ILE A N 1 ATOM 918 C CA . ILE A 1 119 ? -5.271 3.351 1.312 1.00 15.17 ? 207 ILE A CA 1 ATOM 919 C C . ILE A 1 119 ? -5.378 4.868 0.946 1.00 14.74 ? 207 ILE A C 1 ATOM 920 O O . ILE A 1 119 ? -5.797 5.705 1.750 1.00 14.51 ? 207 ILE A O 1 ATOM 921 C CB . ILE A 1 119 ? -3.818 2.976 1.593 1.00 14.53 ? 207 ILE A CB 1 ATOM 922 C CG1 . ILE A 1 119 ? -3.775 1.591 2.220 1.00 13.72 ? 207 ILE A CG1 1 ATOM 923 C CG2 . ILE A 1 119 ? -3.141 3.968 2.556 1.00 15.44 ? 207 ILE A CG2 1 ATOM 924 C CD1 . ILE A 1 119 ? -2.353 1.057 2.335 1.00 13.55 ? 207 ILE A CD1 1 ATOM 925 N N . ARG A 1 120 ? -5.010 5.166 -0.293 1.00 15.86 ? 208 ARG A N 1 ATOM 926 C CA . ARG A 1 120 ? -5.071 6.536 -0.775 1.00 17.69 ? 208 ARG A CA 1 ATOM 927 C C . ARG A 1 120 ? -6.474 7.098 -0.669 1.00 17.70 ? 208 ARG A C 1 ATOM 928 O O . ARG A 1 120 ? -6.654 8.231 -0.222 1.00 16.66 ? 208 ARG A O 1 ATOM 929 C CB . ARG A 1 120 ? -4.603 6.599 -2.206 1.00 18.00 ? 208 ARG A CB 1 ATOM 930 C CG . ARG A 1 120 ? -4.617 8.015 -2.770 1.00 20.96 ? 208 ARG A CG 1 ATOM 931 C CD . ARG A 1 120 ? -4.680 8.062 -4.263 1.00 26.42 ? 208 ARG A CD 1 ATOM 932 N NE . ARG A 1 120 ? -5.095 9.392 -4.703 1.00 31.15 ? 208 ARG A NE 1 ATOM 933 C CZ . ARG A 1 120 ? -4.258 10.420 -4.842 1.00 34.94 ? 208 ARG A CZ 1 ATOM 934 N NH1 . ARG A 1 120 ? -2.953 10.260 -4.632 1.00 34.68 ? 208 ARG A NH1 1 ATOM 935 N NH2 . ARG A 1 120 ? -4.719 11.603 -5.232 1.00 37.12 ? 208 ARG A NH2 1 ATOM 936 N N . GLU A 1 121 ? -7.459 6.302 -1.091 1.00 19.32 ? 209 GLU A N 1 ATOM 937 C CA . GLU A 1 121 ? -8.867 6.672 -1.024 1.00 19.99 ? 209 GLU A CA 1 ATOM 938 C C . GLU A 1 121 ? -9.208 7.037 0.380 1.00 19.32 ? 209 GLU A C 1 ATOM 939 O O . GLU A 1 121 ? -9.748 8.096 0.628 1.00 19.45 ? 209 GLU A O 1 ATOM 940 C CB . GLU A 1 121 ? -9.789 5.501 -1.400 1.00 22.05 ? 209 GLU A CB 1 ATOM 941 C CG . GLU A 1 121 ? -9.891 5.159 -2.857 1.00 25.18 ? 209 GLU A CG 1 ATOM 942 C CD . GLU A 1 121 ? -10.842 3.963 -3.098 1.00 32.53 ? 209 GLU A CD 1 ATOM 943 O OE1 . GLU A 1 121 ? -11.754 3.722 -2.269 1.00 33.42 ? 209 GLU A OE1 1 ATOM 944 O OE2 . GLU A 1 121 ? -10.682 3.251 -4.124 1.00 40.42 ? 209 GLU A OE2 1 ATOM 945 N N . ILE A 1 122 ? -8.904 6.150 1.311 1.00 17.23 ? 210 ILE A N 1 ATOM 946 C CA . ILE A 1 122 ? -9.154 6.388 2.719 1.00 15.97 ? 210 ILE A CA 1 ATOM 947 C C . ILE A 1 122 ? -8.411 7.621 3.251 1.00 15.83 ? 210 ILE A C 1 ATOM 948 O O . ILE A 1 122 ? -9.020 8.453 3.921 1.00 16.53 ? 210 ILE A O 1 ATOM 949 C CB . ILE A 1 122 ? -8.780 5.148 3.541 1.00 16.05 ? 210 ILE A CB 1 ATOM 950 C CG1 . ILE A 1 122 ? -9.789 4.023 3.264 1.00 17.66 ? 210 ILE A CG1 1 ATOM 951 C CG2 . ILE A 1 122 ? -8.776 5.463 4.989 1.00 15.21 ? 210 ILE A CG2 1 ATOM 952 C CD1 . ILE A 1 122 ? -9.335 2.656 3.809 1.00 20.47 ? 210 ILE A CD1 1 ATOM 953 N N . LEU A 1 123 ? -7.136 7.769 2.931 1.00 15.36 ? 211 LEU A N 1 ATOM 954 C CA . LEU A 1 123 ? -6.383 8.919 3.459 1.00 15.39 ? 211 LEU A CA 1 ATOM 955 C C . LEU A 1 123 ? -7.049 10.240 2.957 1.00 16.75 ? 211 LEU A C 1 ATOM 956 O O . LEU A 1 123 ? -7.202 11.214 3.712 1.00 16.83 ? 211 LEU A O 1 ATOM 957 C CB . LEU A 1 123 ? -4.925 8.830 3.034 1.00 15.03 ? 211 LEU A CB 1 ATOM 958 C CG . LEU A 1 123 ? -4.168 7.633 3.653 1.00 13.18 ? 211 LEU A CG 1 ATOM 959 C CD1 . LEU A 1 123 ? -2.719 7.724 3.392 1.00 15.33 ? 211 LEU A CD1 1 ATOM 960 C CD2 . LEU A 1 123 ? -4.382 7.568 5.100 1.00 14.52 ? 211 LEU A CD2 1 ATOM 961 N N . ILE A 1 124 ? -7.439 10.253 1.682 1.00 17.51 ? 212 ILE A N 1 ATOM 962 C CA . ILE A 1 124 ? -8.070 11.437 1.098 1.00 18.59 ? 212 ILE A CA 1 ATOM 963 C C . ILE A 1 124 ? -9.372 11.734 1.829 1.00 19.11 ? 212 ILE A C 1 ATOM 964 O O . ILE A 1 124 ? -9.748 12.896 1.947 1.00 20.51 ? 212 ILE A O 1 ATOM 965 C CB . ILE A 1 124 ? -8.326 11.262 -0.409 1.00 18.62 ? 212 ILE A CB 1 ATOM 966 C CG1 . ILE A 1 124 ? -7.029 11.351 -1.178 1.00 19.99 ? 212 ILE A CG1 1 ATOM 967 C CG2 . ILE A 1 124 ? -9.211 12.388 -0.946 1.00 19.27 ? 212 ILE A CG2 1 ATOM 968 C CD1 . ILE A 1 124 ? -7.192 11.008 -2.600 1.00 21.79 ? 212 ILE A CD1 1 ATOM 969 N N . SER A 1 125 ? -10.061 10.718 2.336 1.00 18.66 ? 213 SER A N 1 ATOM 970 C CA . SER A 1 125 ? -11.293 10.966 3.053 1.00 18.76 ? 213 SER A CA 1 ATOM 971 C C . SER A 1 125 ? -11.005 11.447 4.475 1.00 17.87 ? 213 SER A C 1 ATOM 972 O O . SER A 1 125 ? -11.884 11.966 5.128 1.00 17.38 ? 213 SER A O 1 ATOM 973 C CB . SER A 1 125 ? -12.167 9.704 3.105 1.00 18.84 ? 213 SER A CB 1 ATOM 974 O OG . SER A 1 125 ? -11.619 8.751 3.989 1.00 19.15 ? 213 SER A OG 1 ATOM 975 N N . PHE A 1 126 ? -9.774 11.261 4.949 1.00 17.11 ? 214 PHE A N 1 ATOM 976 C CA . PHE A 1 126 ? -9.413 11.668 6.290 1.00 15.94 ? 214 PHE A CA 1 ATOM 977 C C . PHE A 1 126 ? -8.324 12.749 6.197 1.00 16.40 ? 214 PHE A C 1 ATOM 978 O O . PHE A 1 126 ? -7.356 12.767 6.990 1.00 15.73 ? 214 PHE A O 1 ATOM 979 C CB . PHE A 1 126 ? -8.962 10.479 7.131 1.00 16.48 ? 214 PHE A CB 1 ATOM 980 C CG . PHE A 1 126 ? -10.097 9.699 7.729 1.00 15.65 ? 214 PHE A CG 1 ATOM 981 C CD1 . PHE A 1 126 ? -10.754 10.163 8.826 1.00 15.34 ? 214 PHE A CD1 1 ATOM 982 C CD2 . PHE A 1 126 ? -10.521 8.523 7.158 1.00 16.28 ? 214 PHE A CD2 1 ATOM 983 C CE1 . PHE A 1 126 ? -11.764 9.479 9.362 1.00 16.41 ? 214 PHE A CE1 1 ATOM 984 C CE2 . PHE A 1 126 ? -11.550 7.855 7.681 1.00 14.73 ? 214 PHE A CE2 1 ATOM 985 C CZ . PHE A 1 126 ? -12.174 8.328 8.798 1.00 16.08 ? 214 PHE A CZ 1 ATOM 986 N N . SER A 1 127 ? -8.498 13.659 5.233 1.00 14.65 ? 215 SER A N 1 ATOM 987 C CA . SER A 1 127 ? -7.539 14.736 5.024 1.00 15.86 ? 215 SER A CA 1 ATOM 988 C C . SER A 1 127 ? -7.454 15.704 6.217 1.00 15.31 ? 215 SER A C 1 ATOM 989 O O . SER A 1 127 ? -6.589 16.558 6.242 1.00 15.85 ? 215 SER A O 1 ATOM 990 C CB . SER A 1 127 ? -7.848 15.500 3.739 1.00 16.52 ? 215 SER A CB 1 ATOM 991 O OG . SER A 1 127 ? -9.101 16.174 3.833 1.00 18.09 ? 215 SER A OG 1 ATOM 992 N N . ASP A 1 128 ? -8.313 15.536 7.216 1.00 16.12 ? 216 ASP A N 1 ATOM 993 C CA . ASP A 1 128 ? -8.253 16.335 8.431 1.00 16.43 ? 216 ASP A CA 1 ATOM 994 C C . ASP A 1 128 ? -7.468 15.645 9.556 1.00 16.38 ? 216 ASP A C 1 ATOM 995 O O . ASP A 1 128 ? -7.467 16.133 10.685 1.00 17.17 ? 216 ASP A O 1 ATOM 996 C CB . ASP A 1 128 ? -9.675 16.657 8.930 1.00 17.38 ? 216 ASP A CB 1 ATOM 997 C CG . ASP A 1 128 ? -10.534 15.411 9.139 1.00 17.72 ? 216 ASP A CG 1 ATOM 998 O OD1 . ASP A 1 128 ? -10.362 14.430 8.383 1.00 19.04 ? 216 ASP A OD1 1 ATOM 999 O OD2 . ASP A 1 128 ? -11.419 15.318 10.029 1.00 20.53 ? 216 ASP A OD2 1 ATOM 1000 N N . VAL A 1 129 ? -6.802 14.528 9.255 1.00 14.82 ? 217 VAL A N 1 ATOM 1001 C CA . VAL A 1 129 ? -6.028 13.785 10.251 1.00 14.60 ? 217 VAL A CA 1 ATOM 1002 C C . VAL A 1 129 ? -4.593 13.703 9.715 1.00 14.46 ? 217 VAL A C 1 ATOM 1003 O O . VAL A 1 129 ? -4.306 13.069 8.711 1.00 14.16 ? 217 VAL A O 1 ATOM 1004 C CB . VAL A 1 129 ? -6.614 12.383 10.496 1.00 14.99 ? 217 VAL A CB 1 ATOM 1005 C CG1 . VAL A 1 129 ? -5.781 11.580 11.464 1.00 14.49 ? 217 VAL A CG1 1 ATOM 1006 C CG2 . VAL A 1 129 ? -8.063 12.484 11.001 1.00 13.52 ? 217 VAL A CG2 1 ATOM 1007 N N . ARG A 1 130 ? -3.693 14.408 10.370 1.00 13.64 ? 218 ARG A N 1 ATOM 1008 C CA . ARG A 1 130 ? -2.333 14.401 9.942 1.00 13.06 ? 218 ARG A CA 1 ATOM 1009 C C . ARG A 1 130 ? -1.887 12.965 10.093 1.00 12.96 ? 218 ARG A C 1 ATOM 1010 O O . ARG A 1 130 ? -2.126 12.361 11.122 1.00 14.06 ? 218 ARG A O 1 ATOM 1011 C CB . ARG A 1 130 ? -1.498 15.312 10.815 1.00 12.84 ? 218 ARG A CB 1 ATOM 1012 C CG . ARG A 1 130 ? -0.128 15.468 10.256 1.00 12.50 ? 218 ARG A CG 1 ATOM 1013 C CD . ARG A 1 130 ? 0.875 16.156 11.187 1.00 11.67 ? 218 ARG A CD 1 ATOM 1014 N NE . ARG A 1 130 ? 0.469 17.527 11.462 1.00 15.34 ? 218 ARG A NE 1 ATOM 1015 C CZ . ARG A 1 130 ? 1.248 18.485 11.986 1.00 14.36 ? 218 ARG A CZ 1 ATOM 1016 N NH1 . ARG A 1 130 ? 2.498 18.223 12.354 1.00 12.55 ? 218 ARG A NH1 1 ATOM 1017 N NH2 . ARG A 1 130 ? 0.760 19.710 12.131 1.00 16.18 ? 218 ARG A NH2 1 ATOM 1018 N N . THR A 1 131 ? -1.234 12.435 9.073 1.00 12.62 ? 219 THR A N 1 ATOM 1019 C CA . THR A 1 131 ? -0.930 11.013 9.004 1.00 12.54 ? 219 THR A CA 1 ATOM 1020 C C . THR A 1 131 ? 0.520 10.773 8.634 1.00 12.36 ? 219 THR A C 1 ATOM 1021 O O . THR A 1 131 ? 1.026 11.233 7.605 1.00 12.23 ? 219 THR A O 1 ATOM 1022 C CB . THR A 1 131 ? -1.821 10.364 7.955 1.00 13.41 ? 219 THR A CB 1 ATOM 1023 O OG1 . THR A 1 131 ? -3.193 10.512 8.337 1.00 14.48 ? 219 THR A OG1 1 ATOM 1024 C CG2 . THR A 1 131 ? -1.615 8.843 7.910 1.00 13.60 ? 219 THR A CG2 1 ATOM 1025 N N . ILE A 1 132 ? 1.193 10.049 9.496 1.00 12.10 ? 220 ILE A N 1 ATOM 1026 C CA . ILE A 1 132 ? 2.592 9.752 9.275 1.00 12.08 ? 220 ILE A CA 1 ATOM 1027 C C . ILE A 1 132 ? 2.721 8.290 8.959 1.00 11.02 ? 220 ILE A C 1 ATOM 1028 O O . ILE A 1 132 ? 2.253 7.462 9.730 1.00 10.34 ? 220 ILE A O 1 ATOM 1029 C CB . ILE A 1 132 ? 3.410 10.073 10.520 1.00 12.08 ? 220 ILE A CB 1 ATOM 1030 C CG1 . ILE A 1 132 ? 3.367 11.559 10.815 1.00 15.39 ? 220 ILE A CG1 1 ATOM 1031 C CG2 . ILE A 1 132 ? 4.870 9.646 10.328 1.00 11.89 ? 220 ILE A CG2 1 ATOM 1032 C CD1 . ILE A 1 132 ? 3.596 11.869 12.252 1.00 17.09 ? 220 ILE A CD1 1 ATOM 1033 N N . LEU A 1 133 ? 3.410 8.001 7.864 1.00 11.00 ? 221 LEU A N 1 ATOM 1034 C CA . LEU A 1 133 ? 3.617 6.645 7.373 1.00 11.73 ? 221 LEU A CA 1 ATOM 1035 C C . LEU A 1 133 ? 5.041 6.170 7.331 1.00 12.34 ? 221 LEU A C 1 ATOM 1036 O O . LEU A 1 133 ? 5.951 6.887 6.882 1.00 12.65 ? 221 LEU A O 1 ATOM 1037 C CB . LEU A 1 133 ? 3.117 6.498 5.921 1.00 11.94 ? 221 LEU A CB 1 ATOM 1038 C CG . LEU A 1 133 ? 1.688 6.936 5.589 1.00 12.22 ? 221 LEU A CG 1 ATOM 1039 C CD1 . LEU A 1 133 ? 1.378 6.848 4.113 1.00 16.82 ? 221 LEU A CD1 1 ATOM 1040 C CD2 . LEU A 1 133 ? 0.713 6.112 6.381 1.00 14.00 ? 221 LEU A CD2 1 ATOM 1041 N N . VAL A 1 134 ? 5.228 4.914 7.722 1.00 11.47 ? 222 VAL A N 1 ATOM 1042 C CA . VAL A 1 134 ? 6.492 4.256 7.515 1.00 11.28 ? 222 VAL A CA 1 ATOM 1043 C C . VAL A 1 134 ? 6.208 3.301 6.362 1.00 11.08 ? 222 VAL A C 1 ATOM 1044 O O . VAL A 1 134 ? 5.280 2.501 6.451 1.00 11.41 ? 222 VAL A O 1 ATOM 1045 C CB . VAL A 1 134 ? 6.980 3.529 8.768 1.00 11.95 ? 222 VAL A CB 1 ATOM 1046 C CG1 . VAL A 1 134 ? 8.053 2.516 8.402 1.00 10.68 ? 222 VAL A CG1 1 ATOM 1047 C CG2 . VAL A 1 134 ? 7.472 4.542 9.823 1.00 13.65 ? 222 VAL A CG2 1 ATOM 1048 N N . ILE A 1 135 ? 6.947 3.418 5.259 1.00 11.54 ? 223 ILE A N 1 ATOM 1049 C CA . ILE A 1 135 ? 6.752 2.563 4.072 1.00 11.96 ? 223 ILE A CA 1 ATOM 1050 C C . ILE A 1 135 ? 7.664 1.332 4.043 1.00 12.37 ? 223 ILE A C 1 ATOM 1051 O O . ILE A 1 135 ? 8.909 1.440 4.031 1.00 12.82 ? 223 ILE A O 1 ATOM 1052 C CB . ILE A 1 135 ? 6.946 3.395 2.762 1.00 12.63 ? 223 ILE A CB 1 ATOM 1053 C CG1 . ILE A 1 135 ? 6.097 4.666 2.839 1.00 12.56 ? 223 ILE A CG1 1 ATOM 1054 C CG2 . ILE A 1 135 ? 6.668 2.554 1.504 1.00 12.92 ? 223 ILE A CG2 1 ATOM 1055 C CD1 . ILE A 1 135 ? 4.650 4.443 2.844 1.00 14.08 ? 223 ILE A CD1 1 ATOM 1056 N N . GLU A 1 136 ? 7.008 0.168 4.109 1.00 11.46 ? 224 GLU A N 1 ATOM 1057 C CA . GLU A 1 136 ? 7.593 -1.144 3.910 1.00 11.55 ? 224 GLU A CA 1 ATOM 1058 C C . GLU A 1 136 ? 8.894 -1.505 4.625 1.00 11.36 ? 224 GLU A C 1 ATOM 1059 O O . GLU A 1 136 ? 9.937 -1.620 4.024 1.00 11.30 ? 224 GLU A O 1 ATOM 1060 C CB . GLU A 1 136 ? 7.712 -1.411 2.414 1.00 10.69 ? 224 GLU A CB 1 ATOM 1061 C CG . GLU A 1 136 ? 6.351 -1.357 1.714 1.00 13.55 ? 224 GLU A CG 1 ATOM 1062 C CD . GLU A 1 136 ? 5.441 -2.563 2.051 1.00 14.00 ? 224 GLU A CD 1 ATOM 1063 O OE1 . GLU A 1 136 ? 5.900 -3.584 2.609 1.00 14.07 ? 224 GLU A OE1 1 ATOM 1064 O OE2 . GLU A 1 136 ? 4.230 -2.490 1.764 1.00 11.25 ? 224 GLU A OE2 1 ATOM 1065 N N . PRO A 1 137 ? 8.814 -1.744 5.924 1.00 11.40 ? 225 PRO A N 1 ATOM 1066 C CA . PRO A 1 137 ? 9.951 -2.300 6.623 1.00 11.32 ? 225 PRO A CA 1 ATOM 1067 C C . PRO A 1 137 ? 10.420 -3.603 5.993 1.00 11.57 ? 225 PRO A C 1 ATOM 1068 O O . PRO A 1 137 ? 9.619 -4.356 5.378 1.00 11.72 ? 225 PRO A O 1 ATOM 1069 C CB . PRO A 1 137 ? 9.387 -2.565 8.027 1.00 11.83 ? 225 PRO A CB 1 ATOM 1070 C CG . PRO A 1 137 ? 8.387 -1.492 8.199 1.00 12.19 ? 225 PRO A CG 1 ATOM 1071 C CD . PRO A 1 137 ? 7.705 -1.429 6.833 1.00 10.48 ? 225 PRO A CD 1 ATOM 1072 N N . ASP A 1 138 ? 11.719 -3.849 6.109 1.00 11.74 ? 226 ASP A N 1 ATOM 1073 C CA . ASP A 1 138 ? 12.314 -5.121 5.682 1.00 11.48 ? 226 ASP A CA 1 ATOM 1074 C C . ASP A 1 138 ? 12.157 -5.337 4.190 1.00 11.53 ? 226 ASP A C 1 ATOM 1075 O O . ASP A 1 138 ? 11.898 -6.438 3.761 1.00 11.41 ? 226 ASP A O 1 ATOM 1076 C CB . ASP A 1 138 ? 11.689 -6.309 6.460 1.00 13.52 ? 226 ASP A CB 1 ATOM 1077 C CG . ASP A 1 138 ? 12.470 -7.605 6.265 1.00 13.58 ? 226 ASP A CG 1 ATOM 1078 O OD1 . ASP A 1 138 ? 13.697 -7.484 6.078 1.00 12.04 ? 226 ASP A OD1 1 ATOM 1079 O OD2 . ASP A 1 138 ? 11.956 -8.752 6.254 1.00 15.40 ? 226 ASP A OD2 1 ATOM 1080 N N . SER A 1 139 ? 12.278 -4.271 3.393 1.00 11.30 ? 227 SER A N 1 ATOM 1081 C CA . SER A 1 139 ? 12.173 -4.417 1.928 1.00 11.40 ? 227 SER A CA 1 ATOM 1082 C C . SER A 1 139 ? 13.428 -3.977 1.141 1.00 12.37 ? 227 SER A C 1 ATOM 1083 O O . SER A 1 139 ? 14.254 -4.815 0.820 1.00 14.33 ? 227 SER A O 1 ATOM 1084 C CB . SER A 1 139 ? 10.910 -3.742 1.380 1.00 11.75 ? 227 SER A CB 1 ATOM 1085 O OG . SER A 1 139 ? 11.005 -2.299 1.391 1.00 10.90 ? 227 SER A OG 1 ATOM 1086 N N . LEU A 1 140 ? 13.566 -2.713 0.807 1.00 12.94 ? 228 LEU A N 1 ATOM 1087 C CA . LEU A 1 140 ? 14.717 -2.221 0.018 1.00 14.19 ? 228 LEU A CA 1 ATOM 1088 C C . LEU A 1 140 ? 16.070 -2.493 0.698 1.00 14.75 ? 228 LEU A C 1 ATOM 1089 O O . LEU A 1 140 ? 17.114 -2.561 0.042 1.00 17.11 ? 228 LEU A O 1 ATOM 1090 C CB . LEU A 1 140 ? 14.564 -0.710 -0.316 1.00 14.24 ? 228 LEU A CB 1 ATOM 1091 C CG . LEU A 1 140 ? 13.353 -0.361 -1.201 1.00 17.00 ? 228 LEU A CG 1 ATOM 1092 C CD1 . LEU A 1 140 ? 13.284 1.085 -1.520 1.00 19.07 ? 228 LEU A CD1 1 ATOM 1093 C CD2 . LEU A 1 140 ? 13.347 -1.127 -2.497 1.00 20.87 ? 228 LEU A CD2 1 ATOM 1094 N N . ALA A 1 141 ? 16.085 -2.602 2.016 1.00 14.85 ? 229 ALA A N 1 ATOM 1095 C CA . ALA A 1 141 ? 17.356 -2.838 2.680 1.00 14.68 ? 229 ALA A CA 1 ATOM 1096 C C . ALA A 1 141 ? 17.976 -4.159 2.182 1.00 15.07 ? 229 ALA A C 1 ATOM 1097 O O . ALA A 1 141 ? 19.196 -4.287 2.057 1.00 16.58 ? 229 ALA A O 1 ATOM 1098 C CB . ALA A 1 141 ? 17.195 -2.841 4.230 1.00 14.29 ? 229 ALA A CB 1 ATOM 1099 N N . ASN A 1 142 ? 17.125 -5.135 1.886 1.00 15.22 ? 230 ASN A N 1 ATOM 1100 C CA . ASN A 1 142 ? 17.591 -6.424 1.387 1.00 15.02 ? 230 ASN A CA 1 ATOM 1101 C C . ASN A 1 142 ? 18.325 -6.288 0.058 1.00 16.33 ? 230 ASN A C 1 ATOM 1102 O O . ASN A 1 142 ? 19.138 -7.144 -0.302 1.00 15.66 ? 230 ASN A O 1 ATOM 1103 C CB . ASN A 1 142 ? 16.414 -7.394 1.258 1.00 14.62 ? 230 ASN A CB 1 ATOM 1104 C CG . ASN A 1 142 ? 15.899 -7.818 2.598 1.00 13.46 ? 230 ASN A CG 1 ATOM 1105 O OD1 . ASN A 1 142 ? 16.594 -8.524 3.318 1.00 11.06 ? 230 ASN A OD1 1 ATOM 1106 N ND2 . ASN A 1 142 ? 14.718 -7.326 2.978 1.00 13.24 ? 230 ASN A ND2 1 ATOM 1107 N N . MET A 1 143 ? 17.986 -5.261 -0.691 1.00 16.35 ? 231 MET A N 1 ATOM 1108 C CA . MET A 1 143 ? 18.634 -5.039 -1.969 1.00 18.12 ? 231 MET A CA 1 ATOM 1109 C C . MET A 1 143 ? 20.062 -4.601 -1.801 1.00 18.76 ? 231 MET A C 1 ATOM 1110 O O . MET A 1 143 ? 20.863 -4.682 -2.739 1.00 19.38 ? 231 MET A O 1 ATOM 1111 C CB . MET A 1 143 ? 17.862 -4.016 -2.779 1.00 17.85 ? 231 MET A CB 1 ATOM 1112 C CG . MET A 1 143 ? 16.845 -4.630 -3.641 1.00 19.80 ? 231 MET A CG 1 ATOM 1113 S SD . MET A 1 143 ? 15.304 -5.027 -2.857 1.00 19.02 ? 231 MET A SD 1 ATOM 1114 C CE . MET A 1 143 ? 15.521 -6.679 -2.342 1.00 19.64 ? 231 MET A CE 1 ATOM 1115 N N . VAL A 1 144 ? 20.417 -4.158 -0.607 1.00 18.17 ? 232 VAL A N 1 ATOM 1116 C CA . VAL A 1 144 ? 21.761 -3.697 -0.425 1.00 18.39 ? 232 VAL A CA 1 ATOM 1117 C C . VAL A 1 144 ? 22.640 -4.895 -0.079 1.00 18.81 ? 232 VAL A C 1 ATOM 1118 O O . VAL A 1 144 ? 23.768 -5.009 -0.558 1.00 18.77 ? 232 VAL A O 1 ATOM 1119 C CB . VAL A 1 144 ? 21.834 -2.577 0.620 1.00 18.55 ? 232 VAL A CB 1 ATOM 1120 C CG1 . VAL A 1 144 ? 23.280 -2.220 0.882 1.00 19.72 ? 232 VAL A CG1 1 ATOM 1121 C CG2 . VAL A 1 144 ? 21.015 -1.405 0.164 1.00 17.98 ? 232 VAL A CG2 1 ATOM 1122 N N . THR A 1 145 ? 22.117 -5.812 0.722 1.00 18.89 ? 233 THR A N 1 ATOM 1123 C CA . THR A 1 145 ? 22.955 -6.889 1.210 1.00 19.06 ? 233 THR A CA 1 ATOM 1124 C C . THR A 1 145 ? 22.553 -8.274 0.813 1.00 19.57 ? 233 THR A C 1 ATOM 1125 O O . THR A 1 145 ? 23.370 -9.146 0.953 1.00 20.52 ? 233 THR A O 1 ATOM 1126 C CB . THR A 1 145 ? 23.029 -6.883 2.752 1.00 19.00 ? 233 THR A CB 1 ATOM 1127 O OG1 . THR A 1 145 ? 21.722 -7.076 3.304 1.00 18.28 ? 233 THR A OG1 1 ATOM 1128 C CG2 . THR A 1 145 ? 23.476 -5.562 3.267 1.00 19.46 ? 233 THR A CG2 1 ATOM 1129 N N . ASN A 1 146 ? 21.335 -8.499 0.331 1.00 20.06 ? 234 ASN A N 1 ATOM 1130 C CA . ASN A 1 146 ? 20.864 -9.855 0.081 1.00 20.00 ? 234 ASN A CA 1 ATOM 1131 C C . ASN A 1 146 ? 20.610 -10.226 -1.378 1.00 20.47 ? 234 ASN A C 1 ATOM 1132 O O . ASN A 1 146 ? 19.847 -11.136 -1.663 1.00 18.59 ? 234 ASN A O 1 ATOM 1133 C CB . ASN A 1 146 ? 19.625 -10.113 0.940 1.00 19.46 ? 234 ASN A CB 1 ATOM 1134 C CG . ASN A 1 146 ? 19.980 -10.325 2.396 1.00 20.30 ? 234 ASN A CG 1 ATOM 1135 O OD1 . ASN A 1 146 ? 21.004 -10.954 2.700 1.00 16.72 ? 234 ASN A OD1 1 ATOM 1136 N ND2 . ASN A 1 146 ? 19.145 -9.815 3.305 1.00 16.52 ? 234 ASN A ND2 1 ATOM 1137 N N . MET A 1 147 ? 21.290 -9.565 -2.305 1.00 21.49 ? 235 MET A N 1 ATOM 1138 C CA . MET A 1 147 ? 21.062 -9.863 -3.714 1.00 23.02 ? 235 MET A CA 1 ATOM 1139 C C . MET A 1 147 ? 21.574 -11.258 -4.102 1.00 24.21 ? 235 MET A C 1 ATOM 1140 O O . MET A 1 147 ? 21.208 -11.783 -5.150 1.00 26.28 ? 235 MET A O 1 ATOM 1141 C CB . MET A 1 147 ? 21.574 -8.728 -4.604 1.00 22.63 ? 235 MET A CB 1 ATOM 1142 C CG . MET A 1 147 ? 20.741 -7.441 -4.444 1.00 22.37 ? 235 MET A CG 1 ATOM 1143 S SD . MET A 1 147 ? 19.043 -7.617 -4.971 1.00 22.20 ? 235 MET A SD 1 ATOM 1144 C CE . MET A 1 147 ? 19.255 -7.526 -6.697 1.00 25.70 ? 235 MET A CE 1 ATOM 1145 N N . ASN A 1 148 ? 22.348 -11.892 -3.231 1.00 24.95 ? 236 ASN A N 1 ATOM 1146 C CA . ASN A 1 148 ? 22.821 -13.245 -3.482 1.00 25.50 ? 236 ASN A CA 1 ATOM 1147 C C . ASN A 1 148 ? 21.719 -14.250 -3.122 1.00 24.80 ? 236 ASN A C 1 ATOM 1148 O O . ASN A 1 148 ? 21.867 -15.439 -3.323 1.00 24.95 ? 236 ASN A O 1 ATOM 1149 C CB . ASN A 1 148 ? 24.028 -13.530 -2.616 1.00 25.83 ? 236 ASN A CB 1 ATOM 1150 C CG . ASN A 1 148 ? 23.689 -13.385 -1.135 1.00 29.76 ? 236 ASN A CG 1 ATOM 1151 O OD1 . ASN A 1 148 ? 23.477 -12.262 -0.651 1.00 31.42 ? 236 ASN A OD1 1 ATOM 1152 N ND2 . ASN A 1 148 ? 23.536 -14.522 -0.434 1.00 33.15 ? 236 ASN A ND2 1 ATOM 1153 N N . VAL A 1 149 ? 20.622 -13.765 -2.562 1.00 23.35 ? 237 VAL A N 1 ATOM 1154 C CA . VAL A 1 149 ? 19.520 -14.632 -2.214 1.00 22.85 ? 237 VAL A CA 1 ATOM 1155 C C . VAL A 1 149 ? 18.520 -14.572 -3.359 1.00 22.20 ? 237 VAL A C 1 ATOM 1156 O O . VAL A 1 149 ? 17.975 -13.510 -3.668 1.00 22.25 ? 237 VAL A O 1 ATOM 1157 C CB . VAL A 1 149 ? 18.844 -14.210 -0.892 1.00 23.04 ? 237 VAL A CB 1 ATOM 1158 C CG1 . VAL A 1 149 ? 17.630 -15.073 -0.642 1.00 22.83 ? 237 VAL A CG1 1 ATOM 1159 C CG2 . VAL A 1 149 ? 19.805 -14.329 0.266 1.00 23.57 ? 237 VAL A CG2 1 ATOM 1160 N N . PRO A 1 150 ? 18.267 -15.703 -3.997 1.00 21.45 ? 238 PRO A N 1 ATOM 1161 C CA . PRO A 1 150 ? 17.427 -15.710 -5.191 1.00 21.11 ? 238 PRO A CA 1 ATOM 1162 C C . PRO A 1 150 ? 16.060 -15.013 -5.055 1.00 20.45 ? 238 PRO A C 1 ATOM 1163 O O . PRO A 1 150 ? 15.682 -14.296 -5.987 1.00 19.94 ? 238 PRO A O 1 ATOM 1164 C CB . PRO A 1 150 ? 17.282 -17.193 -5.509 1.00 21.69 ? 238 PRO A CB 1 ATOM 1165 C CG . PRO A 1 150 ? 18.487 -17.804 -4.917 1.00 22.13 ? 238 PRO A CG 1 ATOM 1166 C CD . PRO A 1 150 ? 18.771 -17.041 -3.667 1.00 21.91 ? 238 PRO A CD 1 ATOM 1167 N N . LYS A 1 151 ? 15.339 -15.168 -3.945 1.00 19.48 ? 239 LYS A N 1 ATOM 1168 C CA . LYS A 1 151 ? 14.024 -14.514 -3.883 1.00 18.83 ? 239 LYS A CA 1 ATOM 1169 C C . LYS A 1 151 ? 14.211 -13.001 -3.851 1.00 18.20 ? 239 LYS A C 1 ATOM 1170 O O . LYS A 1 151 ? 13.389 -12.245 -4.364 1.00 18.17 ? 239 LYS A O 1 ATOM 1171 C CB . LYS A 1 151 ? 13.226 -14.967 -2.648 1.00 18.80 ? 239 LYS A CB 1 ATOM 1172 C CG . LYS A 1 151 ? 11.740 -14.625 -2.696 1.00 20.67 ? 239 LYS A CG 1 ATOM 1173 C CD . LYS A 1 151 ? 10.966 -15.224 -1.500 1.00 22.15 ? 239 LYS A CD 1 ATOM 1174 C CE . LYS A 1 151 ? 9.447 -15.064 -1.641 1.00 23.98 ? 239 LYS A CE 1 ATOM 1175 N NZ . LYS A 1 151 ? 8.690 -15.886 -0.628 1.00 22.79 ? 239 LYS A NZ 1 ATOM 1176 N N . CYS A 1 152 ? 15.295 -12.549 -3.236 1.00 17.80 ? 240 CYS A N 1 ATOM 1177 C CA . CYS A 1 152 ? 15.529 -11.110 -3.151 1.00 18.61 ? 240 CYS A CA 1 ATOM 1178 C C . CYS A 1 152 ? 15.934 -10.571 -4.517 1.00 18.61 ? 240 CYS A C 1 ATOM 1179 O O . CYS A 1 152 ? 15.436 -9.545 -4.940 1.00 17.22 ? 240 CYS A O 1 ATOM 1180 C CB . CYS A 1 152 ? 16.585 -10.753 -2.118 1.00 18.69 ? 240 CYS A CB 1 ATOM 1181 S SG . CYS A 1 152 ? 16.034 -11.028 -0.399 1.00 20.45 ? 240 CYS A SG 1 ATOM 1182 N N . SER A 1 153 ? 16.822 -11.289 -5.208 1.00 18.80 ? 241 SER A N 1 ATOM 1183 C CA . SER A 1 153 ? 17.282 -10.853 -6.509 1.00 20.01 ? 241 SER A CA 1 ATOM 1184 C C . SER A 1 153 ? 16.081 -10.726 -7.394 1.00 19.29 ? 241 SER A C 1 ATOM 1185 O O . SER A 1 153 ? 15.919 -9.750 -8.137 1.00 20.24 ? 241 SER A O 1 ATOM 1186 C CB . SER A 1 153 ? 18.247 -11.887 -7.116 1.00 21.31 ? 241 SER A CB 1 ATOM 1187 O OG . SER A 1 153 ? 18.461 -11.608 -8.502 1.00 25.70 ? 241 SER A OG 1 ATOM 1188 N N . GLY A 1 154 ? 15.242 -11.749 -7.340 1.00 18.30 ? 242 GLY A N 1 ATOM 1189 C CA . GLY A 1 154 ? 14.055 -11.796 -8.147 1.00 17.68 ? 242 GLY A CA 1 ATOM 1190 C C . GLY A 1 154 ? 12.998 -10.778 -7.758 1.00 17.46 ? 242 GLY A C 1 ATOM 1191 O O . GLY A 1 154 ? 12.167 -10.478 -8.570 1.00 17.47 ? 242 GLY A O 1 ATOM 1192 N N . ALA A 1 155 ? 13.017 -10.256 -6.534 1.00 17.04 ? 243 ALA A N 1 ATOM 1193 C CA . ALA A 1 155 ? 11.972 -9.299 -6.106 1.00 16.44 ? 243 ALA A CA 1 ATOM 1194 C C . ALA A 1 155 ? 12.359 -7.834 -6.258 1.00 16.46 ? 243 ALA A C 1 ATOM 1195 O O . ALA A 1 155 ? 11.503 -6.972 -6.205 1.00 15.38 ? 243 ALA A O 1 ATOM 1196 C CB . ALA A 1 155 ? 11.602 -9.540 -4.665 1.00 16.54 ? 243 ALA A CB 1 ATOM 1197 N N . ALA A 1 156 ? 13.645 -7.578 -6.459 1.00 16.56 ? 244 ALA A N 1 ATOM 1198 C CA . ALA A 1 156 ? 14.213 -6.223 -6.420 1.00 17.19 ? 244 ALA A CA 1 ATOM 1199 C C . ALA A 1 156 ? 13.505 -5.192 -7.288 1.00 17.96 ? 244 ALA A C 1 ATOM 1200 O O . ALA A 1 156 ? 13.181 -4.113 -6.807 1.00 16.79 ? 244 ALA A O 1 ATOM 1201 C CB . ALA A 1 156 ? 15.663 -6.287 -6.769 1.00 16.99 ? 244 ALA A CB 1 ATOM 1202 N N . SER A 1 157 ? 13.266 -5.527 -8.560 1.00 18.07 ? 245 SER A N 1 ATOM 1203 C CA . SER A 1 157 ? 12.651 -4.581 -9.474 1.00 18.65 ? 245 SER A CA 1 ATOM 1204 C C . SER A 1 157 ? 11.226 -4.279 -9.051 1.00 18.74 ? 245 SER A C 1 ATOM 1205 O O . SER A 1 157 ? 10.753 -3.164 -9.221 1.00 19.22 ? 245 SER A O 1 ATOM 1206 C CB . SER A 1 157 ? 12.646 -5.116 -10.911 1.00 20.04 ? 245 SER A CB 1 ATOM 1207 O OG . SER A 1 157 ? 11.847 -6.292 -11.003 1.00 21.76 ? 245 SER A OG 1 ATOM 1208 N N . THR A 1 158 ? 10.535 -5.287 -8.517 1.00 17.66 ? 246 THR A N 1 ATOM 1209 C CA . THR A 1 158 ? 9.177 -5.108 -8.079 1.00 18.19 ? 246 THR A CA 1 ATOM 1210 C C . THR A 1 158 ? 9.145 -4.268 -6.810 1.00 17.42 ? 246 THR A C 1 ATOM 1211 O O . THR A 1 158 ? 8.310 -3.402 -6.689 1.00 17.75 ? 246 THR A O 1 ATOM 1212 C CB . THR A 1 158 ? 8.523 -6.464 -7.833 1.00 18.80 ? 246 THR A CB 1 ATOM 1213 O OG1 . THR A 1 158 ? 8.543 -7.251 -9.051 1.00 18.10 ? 246 THR A OG1 1 ATOM 1214 C CG2 . THR A 1 158 ? 7.045 -6.279 -7.495 1.00 19.44 ? 246 THR A CG2 1 ATOM 1215 N N . TYR A 1 159 ? 9.999 -4.580 -5.839 1.00 17.14 ? 247 TYR A N 1 ATOM 1216 C CA . TYR A 1 159 ? 10.152 -3.725 -4.664 1.00 17.32 ? 247 TYR A CA 1 ATOM 1217 C C . TYR A 1 159 ? 10.306 -2.235 -5.086 1.00 18.28 ? 247 TYR A C 1 ATOM 1218 O O . TYR A 1 159 ? 9.594 -1.349 -4.612 1.00 18.53 ? 247 TYR A O 1 ATOM 1219 C CB . TYR A 1 159 ? 11.366 -4.153 -3.874 1.00 16.73 ? 247 TYR A CB 1 ATOM 1220 C CG . TYR A 1 159 ? 11.118 -5.298 -2.932 1.00 15.32 ? 247 TYR A CG 1 ATOM 1221 C CD1 . TYR A 1 159 ? 10.027 -6.138 -3.087 1.00 14.66 ? 247 TYR A CD1 1 ATOM 1222 C CD2 . TYR A 1 159 ? 11.973 -5.538 -1.887 1.00 14.90 ? 247 TYR A CD2 1 ATOM 1223 C CE1 . TYR A 1 159 ? 9.812 -7.227 -2.216 1.00 15.06 ? 247 TYR A CE1 1 ATOM 1224 C CE2 . TYR A 1 159 ? 11.779 -6.601 -1.030 1.00 15.93 ? 247 TYR A CE2 1 ATOM 1225 C CZ . TYR A 1 159 ? 10.703 -7.450 -1.193 1.00 17.00 ? 247 TYR A CZ 1 ATOM 1226 O OH . TYR A 1 159 ? 10.563 -8.510 -0.289 1.00 17.90 ? 247 TYR A OH 1 ATOM 1227 N N . ARG A 1 160 ? 11.216 -1.983 -6.006 1.00 19.36 ? 248 ARG A N 1 ATOM 1228 C CA . ARG A 1 160 ? 11.476 -0.615 -6.432 1.00 20.25 ? 248 ARG A CA 1 ATOM 1229 C C . ARG A 1 160 ? 10.255 0.059 -7.038 1.00 19.91 ? 248 ARG A C 1 ATOM 1230 O O . ARG A 1 160 ? 9.904 1.173 -6.633 1.00 18.75 ? 248 ARG A O 1 ATOM 1231 C CB . ARG A 1 160 ? 12.641 -0.598 -7.407 1.00 21.43 ? 248 ARG A CB 1 ATOM 1232 C CG . ARG A 1 160 ? 13.049 0.790 -7.867 1.00 25.75 ? 248 ARG A CG 1 ATOM 1233 C CD . ARG A 1 160 ? 13.881 0.763 -9.156 1.00 31.21 ? 248 ARG A CD 1 ATOM 1234 N NE . ARG A 1 160 ? 13.877 2.024 -9.901 1.00 35.02 ? 248 ARG A NE 1 ATOM 1235 C CZ . ARG A 1 160 ? 12.971 2.330 -10.827 1.00 39.36 ? 248 ARG A CZ 1 ATOM 1236 N NH1 . ARG A 1 160 ? 11.985 1.471 -11.097 1.00 39.82 ? 248 ARG A NH1 1 ATOM 1237 N NH2 . ARG A 1 160 ? 13.035 3.487 -11.482 1.00 39.79 ? 248 ARG A NH2 1 ATOM 1238 N N . GLU A 1 161 ? 9.606 -0.631 -7.979 1.00 19.89 ? 249 GLU A N 1 ATOM 1239 C CA . GLU A 1 161 ? 8.440 -0.135 -8.694 1.00 20.56 ? 249 GLU A CA 1 ATOM 1240 C C . GLU A 1 161 ? 7.282 0.170 -7.793 1.00 19.71 ? 249 GLU A C 1 ATOM 1241 O O . GLU A 1 161 ? 6.643 1.206 -7.923 1.00 19.68 ? 249 GLU A O 1 ATOM 1242 C CB . GLU A 1 161 ? 7.977 -1.159 -9.745 1.00 21.50 ? 249 GLU A CB 1 ATOM 1243 C CG . GLU A 1 161 ? 6.516 -1.035 -10.180 1.00 26.74 ? 249 GLU A CG 1 ATOM 1244 C CD . GLU A 1 161 ? 6.071 -2.157 -11.123 1.00 32.72 ? 249 GLU A CD 1 ATOM 1245 O OE1 . GLU A 1 161 ? 6.752 -3.221 -11.163 1.00 36.37 ? 249 GLU A OE1 1 ATOM 1246 O OE2 . GLU A 1 161 ? 5.033 -1.992 -11.816 1.00 33.53 ? 249 GLU A OE2 1 ATOM 1247 N N . LEU A 1 162 ? 6.979 -0.767 -6.902 1.00 17.60 ? 250 LEU A N 1 ATOM 1248 C CA . LEU A 1 162 ? 5.861 -0.618 -6.005 1.00 17.02 ? 250 LEU A CA 1 ATOM 1249 C C . LEU A 1 162 ? 6.165 0.438 -4.925 1.00 16.43 ? 250 LEU A C 1 ATOM 1250 O O . LEU A 1 162 ? 5.280 1.113 -4.464 1.00 16.41 ? 250 LEU A O 1 ATOM 1251 C CB . LEU A 1 162 ? 5.553 -1.971 -5.376 1.00 16.26 ? 250 LEU A CB 1 ATOM 1252 C CG . LEU A 1 162 ? 5.072 -3.000 -6.399 1.00 16.03 ? 250 LEU A CG 1 ATOM 1253 C CD1 . LEU A 1 162 ? 4.605 -4.299 -5.687 1.00 17.15 ? 250 LEU A CD1 1 ATOM 1254 C CD2 . LEU A 1 162 ? 3.962 -2.462 -7.252 1.00 17.89 ? 250 LEU A CD2 1 ATOM 1255 N N . THR A 1 163 ? 7.420 0.550 -4.545 1.00 17.30 ? 251 THR A N 1 ATOM 1256 C CA . THR A 1 163 ? 7.802 1.569 -3.574 1.00 17.74 ? 251 THR A CA 1 ATOM 1257 C C . THR A 1 163 ? 7.577 2.952 -4.214 1.00 17.57 ? 251 THR A C 1 ATOM 1258 O O . THR A 1 163 ? 6.972 3.842 -3.625 1.00 16.63 ? 251 THR A O 1 ATOM 1259 C CB . THR A 1 163 ? 9.235 1.409 -3.170 1.00 17.87 ? 251 THR A CB 1 ATOM 1260 O OG1 . THR A 1 163 ? 9.415 0.191 -2.420 1.00 17.25 ? 251 THR A OG1 1 ATOM 1261 C CG2 . THR A 1 163 ? 9.637 2.512 -2.231 1.00 17.66 ? 251 THR A CG2 1 ATOM 1262 N N . ILE A 1 164 ? 8.072 3.120 -5.425 1.00 17.84 ? 252 ILE A N 1 ATOM 1263 C CA . ILE A 1 164 ? 7.833 4.368 -6.140 1.00 18.51 ? 252 ILE A CA 1 ATOM 1264 C C . ILE A 1 164 ? 6.333 4.622 -6.268 1.00 18.13 ? 252 ILE A C 1 ATOM 1265 O O . ILE A 1 164 ? 5.861 5.730 -6.013 1.00 18.89 ? 252 ILE A O 1 ATOM 1266 C CB . ILE A 1 164 ? 8.565 4.352 -7.492 1.00 19.05 ? 252 ILE A CB 1 ATOM 1267 C CG1 . ILE A 1 164 ? 10.068 4.443 -7.265 1.00 19.41 ? 252 ILE A CG1 1 ATOM 1268 C CG2 . ILE A 1 164 ? 8.090 5.491 -8.376 1.00 20.95 ? 252 ILE A CG2 1 ATOM 1269 C CD1 . ILE A 1 164 ? 10.891 3.974 -8.434 1.00 21.97 ? 252 ILE A CD1 1 ATOM 1270 N N . TYR A 1 165 ? 5.559 3.597 -6.626 1.00 17.72 ? 253 TYR A N 1 ATOM 1271 C CA . TYR A 1 165 ? 4.121 3.731 -6.748 1.00 17.37 ? 253 TYR A CA 1 ATOM 1272 C C . TYR A 1 165 ? 3.505 4.236 -5.474 1.00 17.44 ? 253 TYR A C 1 ATOM 1273 O O . TYR A 1 165 ? 2.636 5.108 -5.477 1.00 16.91 ? 253 TYR A O 1 ATOM 1274 C CB . TYR A 1 165 ? 3.489 2.371 -7.083 1.00 17.34 ? 253 TYR A CB 1 ATOM 1275 C CG . TYR A 1 165 ? 2.051 2.448 -7.435 1.00 16.21 ? 253 TYR A CG 1 ATOM 1276 C CD1 . TYR A 1 165 ? 1.650 2.824 -8.713 1.00 21.91 ? 253 TYR A CD1 1 ATOM 1277 C CD2 . TYR A 1 165 ? 1.069 2.126 -6.516 1.00 16.17 ? 253 TYR A CD2 1 ATOM 1278 C CE1 . TYR A 1 165 ? 0.331 2.887 -9.068 1.00 20.22 ? 253 TYR A CE1 1 ATOM 1279 C CE2 . TYR A 1 165 ? -0.268 2.170 -6.871 1.00 17.56 ? 253 TYR A CE2 1 ATOM 1280 C CZ . TYR A 1 165 ? -0.627 2.570 -8.158 1.00 20.26 ? 253 TYR A CZ 1 ATOM 1281 O OH . TYR A 1 165 ? -1.955 2.644 -8.528 1.00 21.85 ? 253 TYR A OH 1 ATOM 1282 N N . ALA A 1 166 ? 3.968 3.700 -4.352 1.00 17.28 ? 254 ALA A N 1 ATOM 1283 C CA . ALA A 1 166 ? 3.418 4.107 -3.079 1.00 16.72 ? 254 ALA A CA 1 ATOM 1284 C C . ALA A 1 166 ? 3.810 5.552 -2.789 1.00 16.43 ? 254 ALA A C 1 ATOM 1285 O O . ALA A 1 166 ? 3.003 6.348 -2.317 1.00 15.08 ? 254 ALA A O 1 ATOM 1286 C CB . ALA A 1 166 ? 3.932 3.201 -1.969 1.00 17.39 ? 254 ALA A CB 1 ATOM 1287 N N . LEU A 1 167 ? 5.056 5.887 -3.053 1.00 16.00 ? 255 LEU A N 1 ATOM 1288 C CA . LEU A 1 167 ? 5.491 7.237 -2.707 1.00 16.33 ? 255 LEU A CA 1 ATOM 1289 C C . LEU A 1 167 ? 4.689 8.273 -3.477 1.00 17.13 ? 255 LEU A C 1 ATOM 1290 O O . LEU A 1 167 ? 4.377 9.339 -2.963 1.00 16.43 ? 255 LEU A O 1 ATOM 1291 C CB . LEU A 1 167 ? 6.971 7.423 -2.968 1.00 16.13 ? 255 LEU A CB 1 ATOM 1292 C CG . LEU A 1 167 ? 7.872 6.506 -2.173 1.00 14.77 ? 255 LEU A CG 1 ATOM 1293 C CD1 . LEU A 1 167 ? 9.265 6.754 -2.598 1.00 16.74 ? 255 LEU A CD1 1 ATOM 1294 C CD2 . LEU A 1 167 ? 7.677 6.764 -0.671 1.00 16.74 ? 255 LEU A CD2 1 ATOM 1295 N N . LYS A 1 168 ? 4.317 7.938 -4.701 1.00 18.15 ? 256 LYS A N 1 ATOM 1296 C CA . LYS A 1 168 ? 3.617 8.891 -5.536 1.00 19.37 ? 256 LYS A CA 1 ATOM 1297 C C . LYS A 1 168 ? 2.143 8.938 -5.206 1.00 18.88 ? 256 LYS A C 1 ATOM 1298 O O . LYS A 1 168 ? 1.579 10.017 -5.079 1.00 18.37 ? 256 LYS A O 1 ATOM 1299 C CB . LYS A 1 168 ? 3.847 8.548 -7.005 1.00 20.76 ? 256 LYS A CB 1 ATOM 1300 C CG . LYS A 1 168 ? 5.244 8.854 -7.447 1.00 22.97 ? 256 LYS A CG 1 ATOM 1301 C CD . LYS A 1 168 ? 5.508 8.389 -8.877 1.00 28.55 ? 256 LYS A CD 1 ATOM 1302 C CE . LYS A 1 168 ? 5.180 9.480 -9.890 1.00 32.04 ? 256 LYS A CE 1 ATOM 1303 N NZ . LYS A 1 168 ? 5.987 9.293 -11.145 1.00 35.29 ? 256 LYS A NZ 1 ATOM 1304 N N . GLN A 1 169 ? 1.527 7.775 -4.999 1.00 17.27 ? 257 GLN A N 1 ATOM 1305 C CA . GLN A 1 169 ? 0.090 7.724 -4.753 1.00 17.42 ? 257 GLN A CA 1 ATOM 1306 C C . GLN A 1 169 ? -0.294 8.225 -3.382 1.00 17.16 ? 257 GLN A C 1 ATOM 1307 O O . GLN A 1 169 ? -1.423 8.666 -3.146 1.00 16.24 ? 257 GLN A O 1 ATOM 1308 C CB . GLN A 1 169 ? -0.415 6.285 -4.892 1.00 17.58 ? 257 GLN A CB 1 ATOM 1309 C CG . GLN A 1 169 ? -0.265 5.715 -6.262 1.00 19.32 ? 257 GLN A CG 1 ATOM 1310 C CD . GLN A 1 169 ? -0.937 6.559 -7.345 1.00 23.40 ? 257 GLN A CD 1 ATOM 1311 O OE1 . GLN A 1 169 ? -0.308 6.832 -8.401 1.00 26.79 ? 257 GLN A OE1 1 ATOM 1312 N NE2 . GLN A 1 169 ? -2.185 6.959 -7.113 1.00 17.98 ? 257 GLN A NE2 1 ATOM 1313 N N . LEU A 1 170 ? 0.619 8.095 -2.432 1.00 16.95 ? 258 LEU A N 1 ATOM 1314 C CA . LEU A 1 170 ? 0.310 8.551 -1.091 1.00 16.54 ? 258 LEU A CA 1 ATOM 1315 C C . LEU A 1 170 ? 0.944 9.911 -0.782 1.00 16.77 ? 258 LEU A C 1 ATOM 1316 O O . LEU A 1 170 ? 1.022 10.307 0.374 1.00 16.47 ? 258 LEU A O 1 ATOM 1317 C CB . LEU A 1 170 ? 0.749 7.508 -0.060 1.00 16.82 ? 258 LEU A CB 1 ATOM 1318 C CG . LEU A 1 170 ? 0.183 6.084 -0.324 1.00 17.61 ? 258 LEU A CG 1 ATOM 1319 C CD1 . LEU A 1 170 ? 0.715 5.042 0.686 1.00 19.76 ? 258 LEU A CD1 1 ATOM 1320 C CD2 . LEU A 1 170 ? -1.346 6.046 -0.313 1.00 18.08 ? 258 LEU A CD2 1 ATOM 1321 N N . ASP A 1 171 ? 1.378 10.612 -1.819 1.00 16.36 ? 259 ASP A N 1 ATOM 1322 C CA . ASP A 1 171 ? 1.919 11.948 -1.676 1.00 16.19 ? 259 ASP A CA 1 ATOM 1323 C C . ASP A 1 171 ? 0.726 12.890 -1.590 1.00 15.90 ? 259 ASP A C 1 ATOM 1324 O O . ASP A 1 171 ? 0.323 13.493 -2.577 1.00 15.33 ? 259 ASP A O 1 ATOM 1325 C CB . ASP A 1 171 ? 2.782 12.261 -2.896 1.00 17.28 ? 259 ASP A CB 1 ATOM 1326 C CG . ASP A 1 171 ? 3.273 13.704 -2.951 1.00 18.66 ? 259 ASP A CG 1 ATOM 1327 O OD1 . ASP A 1 171 ? 3.477 14.361 -1.893 1.00 17.11 ? 259 ASP A OD1 1 ATOM 1328 O OD2 . ASP A 1 171 ? 3.537 14.236 -4.058 1.00 21.44 ? 259 ASP A OD2 1 ATOM 1329 N N . LEU A 1 172 ? 0.115 12.962 -0.420 1.00 14.96 ? 260 LEU A N 1 ATOM 1330 C CA . LEU A 1 172 ? -1.035 13.808 -0.216 1.00 14.69 ? 260 LEU A CA 1 ATOM 1331 C C . LEU A 1 172 ? -0.558 14.898 0.727 1.00 15.19 ? 260 LEU A C 1 ATOM 1332 O O . LEU A 1 172 ? 0.410 14.690 1.457 1.00 12.79 ? 260 LEU A O 1 ATOM 1333 C CB . LEU A 1 172 ? -2.193 13.057 0.429 1.00 15.28 ? 260 LEU A CB 1 ATOM 1334 C CG . LEU A 1 172 ? -2.679 11.815 -0.354 1.00 16.41 ? 260 LEU A CG 1 ATOM 1335 C CD1 . LEU A 1 172 ? -3.621 11.017 0.489 1.00 18.70 ? 260 LEU A CD1 1 ATOM 1336 C CD2 . LEU A 1 172 ? -3.385 12.324 -1.606 1.00 17.75 ? 260 LEU A CD2 1 ATOM 1337 N N . PRO A 1 173 ? -1.213 16.050 0.737 1.00 14.99 ? 261 PRO A N 1 ATOM 1338 C CA . PRO A 1 173 ? -0.749 17.139 1.587 1.00 14.60 ? 261 PRO A CA 1 ATOM 1339 C C . PRO A 1 173 ? -0.734 16.946 3.097 1.00 13.16 ? 261 PRO A C 1 ATOM 1340 O O . PRO A 1 173 ? 0.088 17.577 3.772 1.00 12.93 ? 261 PRO A O 1 ATOM 1341 C CB . PRO A 1 173 ? -1.722 18.281 1.248 1.00 14.52 ? 261 PRO A CB 1 ATOM 1342 C CG . PRO A 1 173 ? -2.243 17.965 -0.080 1.00 16.36 ? 261 PRO A CG 1 ATOM 1343 C CD . PRO A 1 173 ? -2.386 16.439 -0.067 1.00 15.71 ? 261 PRO A CD 1 ATOM 1344 N N . HIS A 1 174 ? -1.606 16.112 3.627 1.00 12.33 ? 262 HIS A N 1 ATOM 1345 C CA . HIS A 1 174 ? -1.644 15.901 5.066 1.00 12.49 ? 262 HIS A CA 1 ATOM 1346 C C . HIS A 1 174 ? -0.797 14.697 5.483 1.00 13.12 ? 262 HIS A C 1 ATOM 1347 O O . HIS A 1 174 ? -0.803 14.319 6.634 1.00 13.12 ? 262 HIS A O 1 ATOM 1348 C CB . HIS A 1 174 ? -3.060 15.731 5.521 1.00 12.50 ? 262 HIS A CB 1 ATOM 1349 C CG . HIS A 1 174 ? -3.711 14.511 4.969 1.00 11.88 ? 262 HIS A CG 1 ATOM 1350 N ND1 . HIS A 1 174 ? -4.029 14.389 3.639 1.00 15.81 ? 262 HIS A ND1 1 ATOM 1351 C CD2 . HIS A 1 174 ? -4.060 13.341 5.555 1.00 13.89 ? 262 HIS A CD2 1 ATOM 1352 C CE1 . HIS A 1 174 ? -4.574 13.201 3.428 1.00 16.32 ? 262 HIS A CE1 1 ATOM 1353 N NE2 . HIS A 1 174 ? -4.601 12.543 4.571 1.00 14.98 ? 262 HIS A NE2 1 ATOM 1354 N N . VAL A 1 175 ? 0.012 14.191 4.568 1.00 12.65 ? 263 VAL A N 1 ATOM 1355 C CA . VAL A 1 175 ? 0.818 12.998 4.824 1.00 13.77 ? 263 VAL A CA 1 ATOM 1356 C C . VAL A 1 175 ? 2.320 13.263 4.861 1.00 13.78 ? 263 VAL A C 1 ATOM 1357 O O . VAL A 1 175 ? 2.805 14.164 4.168 1.00 13.83 ? 263 VAL A O 1 ATOM 1358 C CB . VAL A 1 175 ? 0.577 11.979 3.697 1.00 13.15 ? 263 VAL A CB 1 ATOM 1359 C CG1 . VAL A 1 175 ? 1.599 10.866 3.739 1.00 15.31 ? 263 VAL A CG1 1 ATOM 1360 C CG2 . VAL A 1 175 ? -0.826 11.458 3.797 1.00 15.03 ? 263 VAL A CG2 1 ATOM 1361 N N . ALA A 1 176 ? 3.040 12.517 5.716 1.00 13.43 ? 264 ALA A N 1 ATOM 1362 C CA . ALA A 1 176 ? 4.497 12.495 5.691 1.00 13.71 ? 264 ALA A CA 1 ATOM 1363 C C . ALA A 1 176 ? 4.943 11.033 5.583 1.00 13.35 ? 264 ALA A C 1 ATOM 1364 O O . ALA A 1 176 ? 4.395 10.175 6.252 1.00 14.70 ? 264 ALA A O 1 ATOM 1365 C CB . ALA A 1 176 ? 5.084 13.163 6.904 1.00 13.36 ? 264 ALA A CB 1 ATOM 1366 N N . MET A 1 177 ? 5.887 10.745 4.700 1.00 13.52 ? 265 MET A N 1 ATOM 1367 C CA . MET A 1 177 ? 6.359 9.394 4.482 1.00 12.61 ? 265 MET A CA 1 ATOM 1368 C C . MET A 1 177 ? 7.834 9.238 4.821 1.00 12.49 ? 265 MET A C 1 ATOM 1369 O O . MET A 1 177 ? 8.673 10.094 4.514 1.00 10.80 ? 265 MET A O 1 ATOM 1370 C CB . MET A 1 177 ? 6.125 8.934 3.043 1.00 11.76 ? 265 MET A CB 1 ATOM 1371 C CG . MET A 1 177 ? 4.732 8.459 2.723 1.00 14.79 ? 265 MET A CG 1 ATOM 1372 S SD . MET A 1 177 ? 4.512 8.037 0.987 1.00 17.44 ? 265 MET A SD 1 ATOM 1373 C CE . MET A 1 177 ? 4.489 9.739 0.311 1.00 15.93 ? 265 MET A CE 1 ATOM 1374 N N . TYR A 1 178 ? 8.125 8.126 5.484 1.00 11.42 ? 266 TYR A N 1 ATOM 1375 C CA . TYR A 1 178 ? 9.483 7.732 5.750 1.00 11.31 ? 266 TYR A CA 1 ATOM 1376 C C . TYR A 1 178 ? 9.695 6.324 5.216 1.00 11.83 ? 266 TYR A C 1 ATOM 1377 O O . TYR A 1 178 ? 8.980 5.361 5.617 1.00 11.15 ? 266 TYR A O 1 ATOM 1378 C CB . TYR A 1 178 ? 9.763 7.768 7.249 1.00 11.09 ? 266 TYR A CB 1 ATOM 1379 C CG . TYR A 1 178 ? 9.629 9.116 7.879 1.00 9.82 ? 266 TYR A CG 1 ATOM 1380 C CD1 . TYR A 1 178 ? 8.407 9.576 8.335 1.00 9.31 ? 266 TYR A CD1 1 ATOM 1381 C CD2 . TYR A 1 178 ? 10.732 9.935 8.013 1.00 10.47 ? 266 TYR A CD2 1 ATOM 1382 C CE1 . TYR A 1 178 ? 8.288 10.806 8.955 1.00 13.24 ? 266 TYR A CE1 1 ATOM 1383 C CE2 . TYR A 1 178 ? 10.644 11.158 8.648 1.00 11.25 ? 266 TYR A CE2 1 ATOM 1384 C CZ . TYR A 1 178 ? 9.423 11.604 9.103 1.00 10.96 ? 266 TYR A CZ 1 ATOM 1385 O OH . TYR A 1 178 ? 9.309 12.815 9.712 1.00 11.38 ? 266 TYR A OH 1 ATOM 1386 N N . MET A 1 179 ? 10.641 6.165 4.296 1.00 12.38 ? 267 MET A N 1 ATOM 1387 C CA . MET A 1 179 ? 10.954 4.808 3.800 1.00 12.34 ? 267 MET A CA 1 ATOM 1388 C C . MET A 1 179 ? 11.823 4.068 4.815 1.00 12.35 ? 267 MET A C 1 ATOM 1389 O O . MET A 1 179 ? 12.707 4.657 5.431 1.00 12.21 ? 267 MET A O 1 ATOM 1390 C CB . MET A 1 179 ? 11.723 4.858 2.472 1.00 12.95 ? 267 MET A CB 1 ATOM 1391 C CG . MET A 1 179 ? 10.859 5.080 1.256 1.00 14.56 ? 267 MET A CG 1 ATOM 1392 S SD . MET A 1 179 ? 11.858 5.090 -0.232 1.00 16.77 ? 267 MET A SD 1 ATOM 1393 C CE . MET A 1 179 ? 12.351 6.885 -0.186 1.00 21.40 ? 267 MET A CE 1 ATOM 1394 N N . ASP A 1 180 ? 11.601 2.780 5.010 1.00 11.95 ? 268 ASP A N 1 ATOM 1395 C CA . ASP A 1 180 ? 12.494 2.028 5.896 1.00 12.45 ? 268 ASP A CA 1 ATOM 1396 C C . ASP A 1 180 ? 13.910 1.979 5.336 1.00 12.88 ? 268 ASP A C 1 ATOM 1397 O O . ASP A 1 180 ? 14.097 1.800 4.136 1.00 13.16 ? 268 ASP A O 1 ATOM 1398 C CB . ASP A 1 180 ? 12.003 0.595 6.070 1.00 12.98 ? 268 ASP A CB 1 ATOM 1399 C CG . ASP A 1 180 ? 12.867 -0.161 6.997 1.00 14.94 ? 268 ASP A CG 1 ATOM 1400 O OD1 . ASP A 1 180 ? 12.676 0.034 8.219 1.00 17.72 ? 268 ASP A OD1 1 ATOM 1401 O OD2 . ASP A 1 180 ? 13.758 -0.933 6.610 1.00 15.12 ? 268 ASP A OD2 1 ATOM 1402 N N . ALA A 1 181 ? 14.913 2.096 6.202 1.00 12.14 ? 269 ALA A N 1 ATOM 1403 C CA . ALA A 1 181 ? 16.293 2.087 5.755 1.00 12.46 ? 269 ALA A CA 1 ATOM 1404 C C . ALA A 1 181 ? 17.140 1.316 6.731 1.00 12.15 ? 269 ALA A C 1 ATOM 1405 O O . ALA A 1 181 ? 18.172 1.783 7.147 1.00 12.18 ? 269 ALA A O 1 ATOM 1406 C CB . ALA A 1 181 ? 16.822 3.512 5.630 1.00 12.88 ? 269 ALA A CB 1 ATOM 1407 N N . GLY A 1 182 ? 16.660 0.152 7.135 1.00 11.48 ? 270 GLY A N 1 ATOM 1408 C CA . GLY A 1 182 ? 17.432 -0.773 7.934 1.00 11.92 ? 270 GLY A CA 1 ATOM 1409 C C . GLY A 1 182 ? 17.900 -0.181 9.230 1.00 11.78 ? 270 GLY A C 1 ATOM 1410 O O . GLY A 1 182 ? 17.172 0.571 9.837 1.00 11.90 ? 270 GLY A O 1 ATOM 1411 N N . HIS A 1 183 ? 19.108 -0.523 9.647 1.00 11.81 ? 271 HIS A N 1 ATOM 1412 C CA . HIS A 1 183 ? 19.653 0.019 10.874 1.00 12.87 ? 271 HIS A CA 1 ATOM 1413 C C . HIS A 1 183 ? 21.168 0.004 10.869 1.00 13.57 ? 271 HIS A C 1 ATOM 1414 O O . HIS A 1 183 ? 21.801 -0.526 9.946 1.00 15.01 ? 271 HIS A O 1 ATOM 1415 C CB . HIS A 1 183 ? 19.132 -0.755 12.090 1.00 11.87 ? 271 HIS A CB 1 ATOM 1416 C CG . HIS A 1 183 ? 19.547 -2.191 12.101 1.00 12.14 ? 271 HIS A CG 1 ATOM 1417 N ND1 . HIS A 1 183 ? 20.747 -2.612 12.623 1.00 11.11 ? 271 HIS A ND1 1 ATOM 1418 C CD2 . HIS A 1 183 ? 18.900 -3.312 11.691 1.00 13.18 ? 271 HIS A CD2 1 ATOM 1419 C CE1 . HIS A 1 183 ? 20.853 -3.918 12.482 1.00 12.16 ? 271 HIS A CE1 1 ATOM 1420 N NE2 . HIS A 1 183 ? 19.747 -4.373 11.910 1.00 12.67 ? 271 HIS A NE2 1 ATOM 1421 N N . ALA A 1 184 ? 21.738 0.567 11.909 1.00 14.19 ? 272 ALA A N 1 ATOM 1422 C CA . ALA A 1 184 ? 23.196 0.718 12.007 1.00 16.08 ? 272 ALA A CA 1 ATOM 1423 C C . ALA A 1 184 ? 23.938 -0.570 11.710 1.00 16.19 ? 272 ALA A C 1 ATOM 1424 O O . ALA A 1 184 ? 24.978 -0.552 11.068 1.00 17.65 ? 272 ALA A O 1 ATOM 1425 C CB . ALA A 1 184 ? 23.579 1.261 13.379 1.00 15.57 ? 272 ALA A CB 1 ATOM 1426 N N . GLY A 1 185 ? 23.379 -1.694 12.145 1.00 16.74 ? 273 GLY A N 1 ATOM 1427 C CA . GLY A 1 185 ? 24.034 -2.974 11.995 1.00 16.65 ? 273 GLY A CA 1 ATOM 1428 C C . GLY A 1 185 ? 23.762 -3.686 10.696 1.00 15.91 ? 273 GLY A C 1 ATOM 1429 O O . GLY A 1 185 ? 24.245 -4.779 10.483 1.00 17.11 ? 273 GLY A O 1 ATOM 1430 N N . TRP A 1 186 ? 22.968 -3.074 9.846 1.00 15.04 ? 274 TRP A N 1 ATOM 1431 C CA . TRP A 1 186 ? 22.586 -3.663 8.591 1.00 14.31 ? 274 TRP A CA 1 ATOM 1432 C C . TRP A 1 186 ? 23.242 -2.837 7.482 1.00 15.08 ? 274 TRP A C 1 ATOM 1433 O O . TRP A 1 186 ? 24.118 -3.330 6.794 1.00 14.72 ? 274 TRP A O 1 ATOM 1434 C CB . TRP A 1 186 ? 21.081 -3.624 8.441 1.00 13.79 ? 274 TRP A CB 1 ATOM 1435 C CG . TRP A 1 186 ? 20.570 -4.443 7.307 1.00 13.62 ? 274 TRP A CG 1 ATOM 1436 C CD1 . TRP A 1 186 ? 21.282 -4.967 6.282 1.00 13.26 ? 274 TRP A CD1 1 ATOM 1437 C CD2 . TRP A 1 186 ? 19.216 -4.818 7.085 1.00 14.12 ? 274 TRP A CD2 1 ATOM 1438 N NE1 . TRP A 1 186 ? 20.457 -5.668 5.439 1.00 14.59 ? 274 TRP A NE1 1 ATOM 1439 C CE2 . TRP A 1 186 ? 19.176 -5.586 5.919 1.00 13.23 ? 274 TRP A CE2 1 ATOM 1440 C CE3 . TRP A 1 186 ? 18.020 -4.594 7.780 1.00 13.21 ? 274 TRP A CE3 1 ATOM 1441 C CZ2 . TRP A 1 186 ? 18.000 -6.128 5.429 1.00 14.57 ? 274 TRP A CZ2 1 ATOM 1442 C CZ3 . TRP A 1 186 ? 16.857 -5.126 7.286 1.00 11.09 ? 274 TRP A CZ3 1 ATOM 1443 C CH2 . TRP A 1 186 ? 16.848 -5.866 6.110 1.00 12.55 ? 274 TRP A CH2 1 ATOM 1444 N N . LEU A 1 187 ? 22.805 -1.597 7.321 1.00 15.83 ? 275 LEU A N 1 ATOM 1445 C CA . LEU A 1 187 ? 23.290 -0.731 6.243 1.00 17.21 ? 275 LEU A CA 1 ATOM 1446 C C . LEU A 1 187 ? 24.378 0.243 6.678 1.00 18.55 ? 275 LEU A C 1 ATOM 1447 O O . LEU A 1 187 ? 24.970 0.959 5.840 1.00 19.23 ? 275 LEU A O 1 ATOM 1448 C CB . LEU A 1 187 ? 22.134 0.060 5.668 1.00 17.54 ? 275 LEU A CB 1 ATOM 1449 C CG . LEU A 1 187 ? 20.960 -0.783 5.159 1.00 16.85 ? 275 LEU A CG 1 ATOM 1450 C CD1 . LEU A 1 187 ? 19.973 0.059 4.433 1.00 19.42 ? 275 LEU A CD1 1 ATOM 1451 C CD2 . LEU A 1 187 ? 21.425 -1.921 4.300 1.00 18.76 ? 275 LEU A CD2 1 ATOM 1452 N N . GLY A 1 188 ? 24.647 0.272 7.978 1.00 18.91 ? 276 GLY A N 1 ATOM 1453 C CA . GLY A 1 188 ? 25.553 1.246 8.541 1.00 19.84 ? 276 GLY A CA 1 ATOM 1454 C C . GLY A 1 188 ? 27.003 0.870 8.370 1.00 20.48 ? 276 GLY A C 1 ATOM 1455 O O . GLY A 1 188 ? 27.869 1.694 8.514 1.00 20.80 ? 276 GLY A O 1 ATOM 1456 N N . TRP A 1 189 ? 27.275 -0.393 8.108 1.00 21.87 ? 277 TRP A N 1 ATOM 1457 C CA . TRP A 1 189 ? 28.643 -0.815 7.848 1.00 23.01 ? 277 TRP A CA 1 ATOM 1458 C C . TRP A 1 189 ? 29.227 -0.020 6.662 1.00 23.74 ? 277 TRP A C 1 ATOM 1459 O O . TRP A 1 189 ? 28.550 0.211 5.657 1.00 23.60 ? 277 TRP A O 1 ATOM 1460 C CB . TRP A 1 189 ? 28.659 -2.291 7.515 1.00 22.77 ? 277 TRP A CB 1 ATOM 1461 C CG . TRP A 1 189 ? 28.349 -3.204 8.665 1.00 23.17 ? 277 TRP A CG 1 ATOM 1462 C CD1 . TRP A 1 189 ? 27.137 -3.746 8.988 1.00 24.47 ? 277 TRP A CD1 1 ATOM 1463 C CD2 . TRP A 1 189 ? 29.274 -3.696 9.637 1.00 21.80 ? 277 TRP A CD2 1 ATOM 1464 N NE1 . TRP A 1 189 ? 27.258 -4.560 10.093 1.00 23.00 ? 277 TRP A NE1 1 ATOM 1465 C CE2 . TRP A 1 189 ? 28.559 -4.550 10.507 1.00 21.64 ? 277 TRP A CE2 1 ATOM 1466 C CE3 . TRP A 1 189 ? 30.645 -3.521 9.850 1.00 22.79 ? 277 TRP A CE3 1 ATOM 1467 C CZ2 . TRP A 1 189 ? 29.160 -5.190 11.592 1.00 22.69 ? 277 TRP A CZ2 1 ATOM 1468 C CZ3 . TRP A 1 189 ? 31.251 -4.186 10.918 1.00 23.58 ? 277 TRP A CZ3 1 ATOM 1469 C CH2 . TRP A 1 189 ? 30.501 -5.001 11.778 1.00 22.16 ? 277 TRP A CH2 1 ATOM 1470 N N . PRO A 1 190 ? 30.465 0.432 6.789 1.00 25.40 ? 278 PRO A N 1 ATOM 1471 C CA . PRO A 1 190 ? 31.146 1.126 5.692 1.00 26.42 ? 278 PRO A CA 1 ATOM 1472 C C . PRO A 1 190 ? 31.043 0.472 4.312 1.00 26.74 ? 278 PRO A C 1 ATOM 1473 O O . PRO A 1 190 ? 30.912 1.200 3.352 1.00 27.49 ? 278 PRO A O 1 ATOM 1474 C CB . PRO A 1 190 ? 32.582 1.209 6.187 1.00 26.62 ? 278 PRO A CB 1 ATOM 1475 C CG . PRO A 1 190 ? 32.415 1.334 7.706 1.00 26.31 ? 278 PRO A CG 1 ATOM 1476 C CD . PRO A 1 190 ? 31.291 0.395 8.008 1.00 25.96 ? 278 PRO A CD 1 ATOM 1477 N N . ALA A 1 191 ? 31.043 -0.849 4.194 1.00 27.86 ? 279 ALA A N 1 ATOM 1478 C CA . ALA A 1 191 ? 30.875 -1.479 2.882 1.00 27.94 ? 279 ALA A CA 1 ATOM 1479 C C . ALA A 1 191 ? 29.449 -1.378 2.333 1.00 27.90 ? 279 ALA A C 1 ATOM 1480 O O . ALA A 1 191 ? 29.223 -1.633 1.153 1.00 28.66 ? 279 ALA A O 1 ATOM 1481 C CB . ALA A 1 191 ? 31.253 -2.930 2.944 1.00 28.82 ? 279 ALA A CB 1 ATOM 1482 N N . ASN A 1 192 ? 28.492 -1.003 3.178 1.00 26.84 ? 280 ASN A N 1 ATOM 1483 C CA . ASN A 1 192 ? 27.079 -0.956 2.771 1.00 26.27 ? 280 ASN A CA 1 ATOM 1484 C C . ASN A 1 192 ? 26.457 0.430 2.697 1.00 25.30 ? 280 ASN A C 1 ATOM 1485 O O . ASN A 1 192 ? 25.526 0.665 1.924 1.00 25.07 ? 280 ASN A O 1 ATOM 1486 C CB . ASN A 1 192 ? 26.211 -1.793 3.749 1.00 25.90 ? 280 ASN A CB 1 ATOM 1487 C CG . ASN A 1 192 ? 26.574 -3.268 3.752 1.00 26.21 ? 280 ASN A CG 1 ATOM 1488 O OD1 . ASN A 1 192 ? 27.082 -3.777 2.772 1.00 23.80 ? 280 ASN A OD1 1 ATOM 1489 N ND2 . ASN A 1 192 ? 26.253 -3.978 4.857 1.00 26.76 ? 280 ASN A ND2 1 ATOM 1490 N N . ILE A 1 193 ? 26.969 1.352 3.506 1.00 25.20 ? 281 ILE A N 1 ATOM 1491 C CA . ILE A 1 193 ? 26.315 2.643 3.664 1.00 24.88 ? 281 ILE A CA 1 ATOM 1492 C C . ILE A 1 193 ? 26.227 3.470 2.375 1.00 25.12 ? 281 ILE A C 1 ATOM 1493 O O . ILE A 1 193 ? 25.239 4.148 2.124 1.00 22.76 ? 281 ILE A O 1 ATOM 1494 C CB . ILE A 1 193 ? 26.929 3.408 4.836 1.00 25.10 ? 281 ILE A CB 1 ATOM 1495 C CG1 . ILE A 1 193 ? 25.981 4.508 5.254 1.00 25.24 ? 281 ILE A CG1 1 ATOM 1496 C CG2 . ILE A 1 193 ? 28.335 3.953 4.503 1.00 25.00 ? 281 ILE A CG2 1 ATOM 1497 C CD1 . ILE A 1 193 ? 26.341 5.129 6.555 1.00 25.32 ? 281 ILE A CD1 1 ATOM 1498 N N . GLN A 1 194 ? 27.211 3.331 1.499 1.00 25.39 ? 282 GLN A N 1 ATOM 1499 C CA . GLN A 1 194 ? 27.208 4.174 0.296 1.00 26.13 ? 282 GLN A CA 1 ATOM 1500 C C . GLN A 1 194 ? 26.223 3.665 -0.748 1.00 24.45 ? 282 GLN A C 1 ATOM 1501 O O . GLN A 1 194 ? 25.423 4.401 -1.327 1.00 22.95 ? 282 GLN A O 1 ATOM 1502 C CB . GLN A 1 194 ? 28.613 4.320 -0.277 1.00 27.72 ? 282 GLN A CB 1 ATOM 1503 C CG . GLN A 1 194 ? 28.711 5.303 -1.407 1.00 32.57 ? 282 GLN A CG 1 ATOM 1504 C CD . GLN A 1 194 ? 29.947 6.173 -1.256 1.00 38.67 ? 282 GLN A CD 1 ATOM 1505 O OE1 . GLN A 1 194 ? 29.837 7.359 -0.961 1.00 45.04 ? 282 GLN A OE1 1 ATOM 1506 N NE2 . GLN A 1 194 ? 31.128 5.575 -1.424 1.00 42.22 ? 282 GLN A NE2 1 ATOM 1507 N N . PRO A 1 195 ? 26.276 2.373 -0.969 1.00 22.94 ? 283 PRO A N 1 ATOM 1508 C CA . PRO A 1 195 ? 25.354 1.713 -1.864 1.00 22.38 ? 283 PRO A CA 1 ATOM 1509 C C . PRO A 1 195 ? 23.910 1.928 -1.369 1.00 20.52 ? 283 PRO A C 1 ATOM 1510 O O . PRO A 1 195 ? 22.947 2.007 -2.134 1.00 20.40 ? 283 PRO A O 1 ATOM 1511 C CB . PRO A 1 195 ? 25.793 0.255 -1.766 1.00 22.82 ? 283 PRO A CB 1 ATOM 1512 C CG . PRO A 1 195 ? 27.153 0.312 -1.252 1.00 23.77 ? 283 PRO A CG 1 ATOM 1513 C CD . PRO A 1 195 ? 27.221 1.442 -0.362 1.00 23.42 ? 283 PRO A CD 1 ATOM 1514 N N . ALA A 1 196 ? 23.752 2.070 -0.069 1.00 19.03 ? 284 ALA A N 1 ATOM 1515 C CA . ALA A 1 196 ? 22.421 2.287 0.482 1.00 18.40 ? 284 ALA A CA 1 ATOM 1516 C C . ALA A 1 196 ? 21.971 3.694 0.162 1.00 17.47 ? 284 ALA A C 1 ATOM 1517 O O . ALA A 1 196 ? 20.810 3.971 -0.153 1.00 17.83 ? 284 ALA A O 1 ATOM 1518 C CB . ALA A 1 196 ? 22.434 2.077 1.971 1.00 17.75 ? 284 ALA A CB 1 ATOM 1519 N N . ALA A 1 197 ? 22.897 4.622 0.251 1.00 17.31 ? 285 ALA A N 1 ATOM 1520 C CA . ALA A 1 197 ? 22.508 5.980 0.004 1.00 18.23 ? 285 ALA A CA 1 ATOM 1521 C C . ALA A 1 197 ? 22.105 6.144 -1.449 1.00 18.66 ? 285 ALA A C 1 ATOM 1522 O O . ALA A 1 197 ? 21.149 6.838 -1.785 1.00 18.37 ? 285 ALA A O 1 ATOM 1523 C CB . ALA A 1 197 ? 23.644 6.907 0.338 1.00 18.04 ? 285 ALA A CB 1 ATOM 1524 N N . GLU A 1 198 ? 22.876 5.495 -2.300 1.00 20.31 ? 286 GLU A N 1 ATOM 1525 C CA . GLU A 1 198 ? 22.603 5.448 -3.732 1.00 21.79 ? 286 GLU A CA 1 ATOM 1526 C C . GLU A 1 198 ? 21.179 4.962 -3.995 1.00 21.04 ? 286 GLU A C 1 ATOM 1527 O O . GLU A 1 198 ? 20.390 5.626 -4.653 1.00 20.31 ? 286 GLU A O 1 ATOM 1528 C CB . GLU A 1 198 ? 23.538 4.417 -4.304 1.00 22.60 ? 286 GLU A CB 1 ATOM 1529 C CG . GLU A 1 198 ? 24.226 4.795 -5.576 1.00 29.09 ? 286 GLU A CG 1 ATOM 1530 C CD . GLU A 1 198 ? 25.568 4.115 -5.639 1.00 33.08 ? 286 GLU A CD 1 ATOM 1531 O OE1 . GLU A 1 198 ? 25.584 2.923 -5.961 1.00 40.34 ? 286 GLU A OE1 1 ATOM 1532 O OE2 . GLU A 1 198 ? 26.588 4.756 -5.325 1.00 37.55 ? 286 GLU A OE2 1 ATOM 1533 N N . LEU A 1 199 ? 20.901 3.760 -3.500 1.00 20.35 ? 287 LEU A N 1 ATOM 1534 C CA . LEU A 1 199 ? 19.602 3.154 -3.635 1.00 20.37 ? 287 LEU A CA 1 ATOM 1535 C C . LEU A 1 199 ? 18.497 4.119 -3.245 1.00 18.78 ? 287 LEU A C 1 ATOM 1536 O O . LEU A 1 199 ? 17.612 4.447 -4.031 1.00 19.56 ? 287 LEU A O 1 ATOM 1537 C CB . LEU A 1 199 ? 19.564 1.899 -2.756 1.00 20.21 ? 287 LEU A CB 1 ATOM 1538 C CG . LEU A 1 199 ? 18.258 1.112 -2.896 1.00 23.79 ? 287 LEU A CG 1 ATOM 1539 C CD1 . LEU A 1 199 ? 17.913 0.853 -4.353 1.00 26.69 ? 287 LEU A CD1 1 ATOM 1540 C CD2 . LEU A 1 199 ? 18.332 -0.219 -2.184 1.00 26.69 ? 287 LEU A CD2 1 ATOM 1541 N N . PHE A 1 200 ? 18.520 4.584 -2.015 1.00 17.96 ? 288 PHE A N 1 ATOM 1542 C CA . PHE A 1 200 ? 17.416 5.382 -1.520 1.00 16.79 ? 288 PHE A CA 1 ATOM 1543 C C . PHE A 1 200 ? 17.312 6.741 -2.202 1.00 16.84 ? 288 PHE A C 1 ATOM 1544 O O . PHE A 1 200 ? 16.226 7.199 -2.528 1.00 14.67 ? 288 PHE A O 1 ATOM 1545 C CB . PHE A 1 200 ? 17.526 5.506 -0.014 1.00 16.66 ? 288 PHE A CB 1 ATOM 1546 C CG . PHE A 1 200 ? 17.261 4.210 0.695 1.00 16.30 ? 288 PHE A CG 1 ATOM 1547 C CD1 . PHE A 1 200 ? 15.968 3.739 0.821 1.00 18.85 ? 288 PHE A CD1 1 ATOM 1548 C CD2 . PHE A 1 200 ? 18.298 3.477 1.214 1.00 20.76 ? 288 PHE A CD2 1 ATOM 1549 C CE1 . PHE A 1 200 ? 15.723 2.513 1.446 1.00 17.18 ? 288 PHE A CE1 1 ATOM 1550 C CE2 . PHE A 1 200 ? 18.056 2.286 1.841 1.00 19.92 ? 288 PHE A CE2 1 ATOM 1551 C CZ . PHE A 1 200 ? 16.766 1.826 1.973 1.00 19.55 ? 288 PHE A CZ 1 ATOM 1552 N N . ALA A 1 201 ? 18.449 7.378 -2.410 1.00 18.21 ? 289 ALA A N 1 ATOM 1553 C CA . ALA A 1 201 ? 18.461 8.676 -3.090 1.00 19.03 ? 289 ALA A CA 1 ATOM 1554 C C . ALA A 1 201 ? 17.865 8.557 -4.495 1.00 20.03 ? 289 ALA A C 1 ATOM 1555 O O . ALA A 1 201 ? 17.105 9.424 -4.950 1.00 20.55 ? 289 ALA A O 1 ATOM 1556 C CB . ALA A 1 201 ? 19.876 9.229 -3.140 1.00 18.92 ? 289 ALA A CB 1 ATOM 1557 N N . LYS A 1 202 ? 18.206 7.478 -5.186 1.00 21.53 ? 290 LYS A N 1 ATOM 1558 C CA . LYS A 1 202 ? 17.718 7.261 -6.559 1.00 22.25 ? 290 LYS A CA 1 ATOM 1559 C C . LYS A 1 202 ? 16.222 6.997 -6.601 1.00 21.92 ? 290 LYS A C 1 ATOM 1560 O O . LYS A 1 202 ? 15.502 7.490 -7.470 1.00 22.21 ? 290 LYS A O 1 ATOM 1561 C CB . LYS A 1 202 ? 18.506 6.134 -7.210 1.00 23.49 ? 290 LYS A CB 1 ATOM 1562 C CG . LYS A 1 202 ? 17.821 5.538 -8.422 1.00 27.67 ? 290 LYS A CG 1 ATOM 1563 C CD . LYS A 1 202 ? 18.773 5.333 -9.594 1.00 32.49 ? 290 LYS A CD 1 ATOM 1564 C CE . LYS A 1 202 ? 18.065 5.633 -10.942 1.00 35.75 ? 290 LYS A CE 1 ATOM 1565 N NZ . LYS A 1 202 ? 17.379 4.442 -11.567 1.00 35.00 ? 290 LYS A NZ 1 ATOM 1566 N N . ILE A 1 203 ? 15.740 6.230 -5.642 1.00 20.56 ? 291 ILE A N 1 ATOM 1567 C CA . ILE A 1 203 ? 14.316 6.040 -5.520 1.00 20.83 ? 291 ILE A CA 1 ATOM 1568 C C . ILE A 1 203 ? 13.600 7.382 -5.338 1.00 19.03 ? 291 ILE A C 1 ATOM 1569 O O . ILE A 1 203 ? 12.589 7.639 -5.976 1.00 18.77 ? 291 ILE A O 1 ATOM 1570 C CB . ILE A 1 203 ? 14.051 5.111 -4.364 1.00 20.87 ? 291 ILE A CB 1 ATOM 1571 C CG1 . ILE A 1 203 ? 14.530 3.749 -4.822 1.00 23.30 ? 291 ILE A CG1 1 ATOM 1572 C CG2 . ILE A 1 203 ? 12.588 5.103 -4.044 1.00 22.34 ? 291 ILE A CG2 1 ATOM 1573 C CD1 . ILE A 1 203 ? 14.366 2.685 -3.856 1.00 26.25 ? 291 ILE A CD1 1 ATOM 1574 N N . TYR A 1 204 ? 14.116 8.230 -4.451 1.00 18.10 ? 292 TYR A N 1 ATOM 1575 C CA . TYR A 1 204 ? 13.542 9.559 -4.215 1.00 18.33 ? 292 TYR A CA 1 ATOM 1576 C C . TYR A 1 204 ? 13.461 10.328 -5.526 1.00 19.25 ? 292 TYR A C 1 ATOM 1577 O O . TYR A 1 204 ? 12.443 10.940 -5.880 1.00 19.23 ? 292 TYR A O 1 ATOM 1578 C CB . TYR A 1 204 ? 14.442 10.311 -3.258 1.00 17.94 ? 292 TYR A CB 1 ATOM 1579 C CG . TYR A 1 204 ? 13.958 11.650 -2.815 1.00 18.93 ? 292 TYR A CG 1 ATOM 1580 C CD1 . TYR A 1 204 ? 12.752 11.781 -2.154 1.00 18.68 ? 292 TYR A CD1 1 ATOM 1581 C CD2 . TYR A 1 204 ? 14.737 12.785 -2.990 1.00 17.10 ? 292 TYR A CD2 1 ATOM 1582 C CE1 . TYR A 1 204 ? 12.323 12.980 -1.702 1.00 16.13 ? 292 TYR A CE1 1 ATOM 1583 C CE2 . TYR A 1 204 ? 14.318 14.001 -2.547 1.00 18.06 ? 292 TYR A CE2 1 ATOM 1584 C CZ . TYR A 1 204 ? 13.119 14.112 -1.908 1.00 19.82 ? 292 TYR A CZ 1 ATOM 1585 O OH . TYR A 1 204 ? 12.727 15.349 -1.472 1.00 19.63 ? 292 TYR A OH 1 ATOM 1586 N N . GLU A 1 205 ? 14.544 10.244 -6.270 1.00 21.12 ? 293 GLU A N 1 ATOM 1587 C CA . GLU A 1 205 ? 14.641 10.978 -7.532 1.00 22.98 ? 293 GLU A CA 1 ATOM 1588 C C . GLU A 1 205 ? 13.627 10.462 -8.577 1.00 23.40 ? 293 GLU A C 1 ATOM 1589 O O . GLU A 1 205 ? 12.843 11.237 -9.118 1.00 23.55 ? 293 GLU A O 1 ATOM 1590 C CB . GLU A 1 205 ? 16.077 10.929 -8.039 1.00 23.12 ? 293 GLU A CB 1 ATOM 1591 C CG . GLU A 1 205 ? 16.291 11.708 -9.335 1.00 27.35 ? 293 GLU A CG 1 ATOM 1592 C CD . GLU A 1 205 ? 17.748 11.740 -9.774 1.00 32.70 ? 293 GLU A CD 1 ATOM 1593 O OE1 . GLU A 1 205 ? 18.593 12.310 -9.036 1.00 36.83 ? 293 GLU A OE1 1 ATOM 1594 O OE2 . GLU A 1 205 ? 18.048 11.196 -10.866 1.00 35.03 ? 293 GLU A OE2 1 ATOM 1595 N N . ASP A 1 206 ? 13.605 9.147 -8.796 1.00 24.24 ? 294 ASP A N 1 ATOM 1596 C CA . ASP A 1 206 ? 12.721 8.524 -9.789 1.00 24.38 ? 294 ASP A CA 1 ATOM 1597 C C . ASP A 1 206 ? 11.269 8.715 -9.430 1.00 23.61 ? 294 ASP A C 1 ATOM 1598 O O . ASP A 1 206 ? 10.389 8.670 -10.281 1.00 22.87 ? 294 ASP A O 1 ATOM 1599 C CB . ASP A 1 206 ? 13.008 7.021 -9.869 1.00 24.92 ? 294 ASP A CB 1 ATOM 1600 C CG . ASP A 1 206 ? 14.357 6.721 -10.490 1.00 27.08 ? 294 ASP A CG 1 ATOM 1601 O OD1 . ASP A 1 206 ? 14.997 7.691 -10.975 1.00 28.55 ? 294 ASP A OD1 1 ATOM 1602 O OD2 . ASP A 1 206 ? 14.872 5.563 -10.517 1.00 30.20 ? 294 ASP A OD2 1 ATOM 1603 N N . ALA A 1 207 ? 11.011 8.893 -8.140 1.00 22.58 ? 295 ALA A N 1 ATOM 1604 C CA . ALA A 1 207 ? 9.666 9.115 -7.678 1.00 21.63 ? 295 ALA A CA 1 ATOM 1605 C C . ALA A 1 207 ? 9.285 10.569 -7.848 1.00 21.59 ? 295 ALA A C 1 ATOM 1606 O O . ALA A 1 207 ? 8.161 10.943 -7.565 1.00 20.26 ? 295 ALA A O 1 ATOM 1607 C CB . ALA A 1 207 ? 9.532 8.735 -6.227 1.00 21.74 ? 295 ALA A CB 1 ATOM 1608 N N . GLY A 1 208 ? 10.228 11.403 -8.253 1.00 21.33 ? 296 GLY A N 1 ATOM 1609 C CA . GLY A 1 208 ? 9.880 12.792 -8.509 1.00 21.28 ? 296 GLY A CA 1 ATOM 1610 C C . GLY A 1 208 ? 10.016 13.682 -7.301 1.00 20.43 ? 296 GLY A C 1 ATOM 1611 O O . GLY A 1 208 ? 9.440 14.760 -7.284 1.00 19.41 ? 296 GLY A O 1 ATOM 1612 N N . LYS A 1 209 ? 10.766 13.218 -6.301 1.00 20.10 ? 297 LYS A N 1 ATOM 1613 C CA . LYS A 1 209 ? 10.964 13.963 -5.041 1.00 20.21 ? 297 LYS A CA 1 ATOM 1614 C C . LYS A 1 209 ? 9.626 14.497 -4.520 1.00 19.27 ? 297 LYS A C 1 ATOM 1615 O O . LYS A 1 209 ? 9.443 15.702 -4.382 1.00 19.96 ? 297 LYS A O 1 ATOM 1616 C CB . LYS A 1 209 ? 11.996 15.094 -5.220 1.00 20.96 ? 297 LYS A CB 1 ATOM 1617 C CG . LYS A 1 209 ? 13.341 14.624 -5.772 1.00 21.96 ? 297 LYS A CG 1 ATOM 1618 C CD . LYS A 1 209 ? 14.491 15.688 -5.672 1.00 24.27 ? 297 LYS A CD 1 ATOM 1619 C CE . LYS A 1 209 ? 15.814 15.152 -6.290 1.00 24.03 ? 297 LYS A CE 1 ATOM 1620 N NZ . LYS A 1 209 ? 17.052 15.833 -5.796 1.00 26.36 ? 297 LYS A NZ 1 ATOM 1621 N N . PRO A 1 210 ? 8.678 13.610 -4.231 1.00 17.92 ? 298 PRO A N 1 ATOM 1622 C CA . PRO A 1 210 ? 7.360 14.033 -3.760 1.00 17.42 ? 298 PRO A CA 1 ATOM 1623 C C . PRO A 1 210 ? 7.484 14.785 -2.448 1.00 17.10 ? 298 PRO A C 1 ATOM 1624 O O . PRO A 1 210 ? 8.309 14.450 -1.612 1.00 16.27 ? 298 PRO A O 1 ATOM 1625 C CB . PRO A 1 210 ? 6.606 12.721 -3.566 1.00 18.20 ? 298 PRO A CB 1 ATOM 1626 C CG . PRO A 1 210 ? 7.413 11.683 -4.272 1.00 17.14 ? 298 PRO A CG 1 ATOM 1627 C CD . PRO A 1 210 ? 8.811 12.148 -4.250 1.00 18.68 ? 298 PRO A CD 1 ATOM 1628 N N . ARG A 1 211 ? 6.659 15.807 -2.294 1.00 16.59 ? 299 ARG A N 1 ATOM 1629 C CA . ARG A 1 211 ? 6.719 16.685 -1.166 1.00 16.17 ? 299 ARG A CA 1 ATOM 1630 C C . ARG A 1 211 ? 6.649 15.906 0.135 1.00 15.88 ? 299 ARG A C 1 ATOM 1631 O O . ARG A 1 211 ? 7.381 16.174 1.090 1.00 14.52 ? 299 ARG A O 1 ATOM 1632 C CB . ARG A 1 211 ? 5.517 17.594 -1.209 1.00 16.70 ? 299 ARG A CB 1 ATOM 1633 C CG . ARG A 1 211 ? 5.504 18.604 -0.116 1.00 17.46 ? 299 ARG A CG 1 ATOM 1634 C CD . ARG A 1 211 ? 4.115 18.946 0.323 1.00 18.49 ? 299 ARG A CD 1 ATOM 1635 N NE . ARG A 1 211 ? 3.370 17.783 0.742 1.00 16.55 ? 299 ARG A NE 1 ATOM 1636 C CZ . ARG A 1 211 ? 3.425 17.229 1.954 1.00 16.79 ? 299 ARG A CZ 1 ATOM 1637 N NH1 . ARG A 1 211 ? 4.180 17.755 2.909 1.00 13.99 ? 299 ARG A NH1 1 ATOM 1638 N NH2 . ARG A 1 211 ? 2.721 16.141 2.207 1.00 15.76 ? 299 ARG A NH2 1 ATOM 1639 N N . ALA A 1 212 ? 5.744 14.936 0.132 1.00 15.12 ? 300 ALA A N 1 ATOM 1640 C CA . ALA A 1 212 ? 5.414 14.135 1.300 1.00 14.85 ? 300 ALA A CA 1 ATOM 1641 C C . ALA A 1 212 ? 6.525 13.238 1.820 1.00 15.00 ? 300 ALA A C 1 ATOM 1642 O O . ALA A 1 212 ? 6.470 12.825 2.976 1.00 16.01 ? 300 ALA A O 1 ATOM 1643 C CB . ALA A 1 212 ? 4.193 13.296 0.993 1.00 14.73 ? 300 ALA A CB 1 ATOM 1644 N N . VAL A 1 213 ? 7.478 12.863 0.971 1.00 15.87 ? 301 VAL A N 1 ATOM 1645 C CA . VAL A 1 213 ? 8.575 12.006 1.406 1.00 16.08 ? 301 VAL A CA 1 ATOM 1646 C C . VAL A 1 213 ? 9.534 12.844 2.225 1.00 15.92 ? 301 VAL A C 1 ATOM 1647 O O . VAL A 1 213 ? 10.322 13.620 1.690 1.00 16.85 ? 301 VAL A O 1 ATOM 1648 C CB . VAL A 1 213 ? 9.313 11.394 0.230 1.00 15.59 ? 301 VAL A CB 1 ATOM 1649 C CG1 . VAL A 1 213 ? 10.488 10.556 0.710 1.00 16.51 ? 301 VAL A CG1 1 ATOM 1650 C CG2 . VAL A 1 213 ? 8.331 10.595 -0.623 1.00 18.03 ? 301 VAL A CG2 1 ATOM 1651 N N . ARG A 1 214 ? 9.488 12.631 3.519 1.00 15.52 ? 302 ARG A N 1 ATOM 1652 C CA . ARG A 1 214 ? 10.244 13.404 4.472 1.00 14.62 ? 302 ARG A CA 1 ATOM 1653 C C . ARG A 1 214 ? 11.626 12.794 4.642 1.00 15.03 ? 302 ARG A C 1 ATOM 1654 O O . ARG A 1 214 ? 12.635 13.510 4.880 1.00 13.65 ? 302 ARG A O 1 ATOM 1655 C CB . ARG A 1 214 ? 9.460 13.447 5.780 1.00 15.37 ? 302 ARG A CB 1 ATOM 1656 C CG . ARG A 1 214 ? 10.116 14.149 6.912 1.00 15.37 ? 302 ARG A CG 1 ATOM 1657 C CD . ARG A 1 214 ? 10.412 15.623 6.625 1.00 15.17 ? 302 ARG A CD 1 ATOM 1658 N NE . ARG A 1 214 ? 10.918 16.298 7.816 1.00 14.57 ? 302 ARG A NE 1 ATOM 1659 C CZ . ARG A 1 214 ? 11.191 17.585 7.890 1.00 17.56 ? 302 ARG A CZ 1 ATOM 1660 N NH1 . ARG A 1 214 ? 11.043 18.365 6.817 1.00 16.38 ? 302 ARG A NH1 1 ATOM 1661 N NH2 . ARG A 1 214 ? 11.637 18.093 9.025 1.00 16.37 ? 302 ARG A NH2 1 ATOM 1662 N N . GLY A 1 215 ? 11.703 11.472 4.552 1.00 13.07 ? 303 GLY A N 1 ATOM 1663 C CA . GLY A 1 215 ? 12.984 10.830 4.701 1.00 13.33 ? 303 GLY A CA 1 ATOM 1664 C C . GLY A 1 215 ? 12.920 9.338 4.967 1.00 13.26 ? 303 GLY A C 1 ATOM 1665 O O . GLY A 1 215 ? 12.151 8.648 4.311 1.00 11.35 ? 303 GLY A O 1 ATOM 1666 N N . LEU A 1 216 ? 13.664 8.898 5.982 1.00 11.95 ? 304 LEU A N 1 ATOM 1667 C CA . LEU A 1 216 ? 13.870 7.474 6.236 1.00 11.95 ? 304 LEU A CA 1 ATOM 1668 C C . LEU A 1 216 ? 13.654 7.140 7.698 1.00 11.66 ? 304 LEU A C 1 ATOM 1669 O O . LEU A 1 216 ? 13.860 7.970 8.590 1.00 10.10 ? 304 LEU A O 1 ATOM 1670 C CB . LEU A 1 216 ? 15.277 7.060 5.864 1.00 12.03 ? 304 LEU A CB 1 ATOM 1671 C CG . LEU A 1 216 ? 15.711 7.414 4.418 1.00 12.27 ? 304 LEU A CG 1 ATOM 1672 C CD1 . LEU A 1 216 ? 17.155 7.061 4.260 1.00 14.05 ? 304 LEU A CD1 1 ATOM 1673 C CD2 . LEU A 1 216 ? 14.907 6.610 3.454 1.00 13.26 ? 304 LEU A CD2 1 ATOM 1674 N N . ALA A 1 217 ? 13.215 5.906 7.926 1.00 12.16 ? 305 ALA A N 1 ATOM 1675 C CA . ALA A 1 217 ? 12.998 5.390 9.280 1.00 12.47 ? 305 ALA A CA 1 ATOM 1676 C C . ALA A 1 217 ? 14.068 4.344 9.535 1.00 12.49 ? 305 ALA A C 1 ATOM 1677 O O . ALA A 1 217 ? 14.278 3.503 8.690 1.00 12.49 ? 305 ALA A O 1 ATOM 1678 C CB . ALA A 1 217 ? 11.620 4.745 9.384 1.00 13.19 ? 305 ALA A CB 1 ATOM 1679 N N . THR A 1 218 ? 14.750 4.386 10.679 1.00 12.35 ? 306 THR A N 1 ATOM 1680 C CA . THR A 1 218 ? 15.762 3.379 10.981 1.00 12.02 ? 306 THR A CA 1 ATOM 1681 C C . THR A 1 218 ? 15.446 2.648 12.277 1.00 11.81 ? 306 THR A C 1 ATOM 1682 O O . THR A 1 218 ? 14.688 3.144 13.107 1.00 11.09 ? 306 THR A O 1 ATOM 1683 C CB . THR A 1 218 ? 17.164 3.958 11.080 1.00 13.48 ? 306 THR A CB 1 ATOM 1684 O OG1 . THR A 1 218 ? 17.252 4.853 12.203 1.00 14.82 ? 306 THR A OG1 1 ATOM 1685 C CG2 . THR A 1 218 ? 17.464 4.806 9.886 1.00 14.63 ? 306 THR A CG2 1 ATOM 1686 N N . ASN A 1 219 ? 16.047 1.463 12.395 1.00 10.40 ? 307 ASN A N 1 ATOM 1687 C CA . ASN A 1 219 ? 15.958 0.591 13.560 1.00 10.86 ? 307 ASN A CA 1 ATOM 1688 C C . ASN A 1 219 ? 14.590 -0.005 13.773 1.00 9.55 ? 307 ASN A C 1 ATOM 1689 O O . ASN A 1 219 ? 14.279 -0.430 14.886 1.00 8.31 ? 307 ASN A O 1 ATOM 1690 C CB . ASN A 1 219 ? 16.363 1.338 14.840 1.00 10.49 ? 307 ASN A CB 1 ATOM 1691 C CG . ASN A 1 219 ? 16.900 0.404 15.944 1.00 11.10 ? 307 ASN A CG 1 ATOM 1692 O OD1 . ASN A 1 219 ? 17.656 -0.524 15.671 1.00 11.91 ? 307 ASN A OD1 1 ATOM 1693 N ND2 . ASN A 1 219 ? 16.505 0.665 17.223 1.00 10.79 ? 307 ASN A ND2 1 ATOM 1694 N N . VAL A 1 220 ? 13.765 0.018 12.731 1.00 9.98 ? 308 VAL A N 1 ATOM 1695 C CA . VAL A 1 220 ? 12.423 -0.530 12.809 1.00 10.96 ? 308 VAL A CA 1 ATOM 1696 C C . VAL A 1 220 ? 12.498 -2.003 13.157 1.00 10.28 ? 308 VAL A C 1 ATOM 1697 O O . VAL A 1 220 ? 13.113 -2.782 12.464 1.00 10.42 ? 308 VAL A O 1 ATOM 1698 C CB . VAL A 1 220 ? 11.698 -0.365 11.480 1.00 10.81 ? 308 VAL A CB 1 ATOM 1699 C CG1 . VAL A 1 220 ? 10.353 -0.972 11.559 1.00 12.28 ? 308 VAL A CG1 1 ATOM 1700 C CG2 . VAL A 1 220 ? 11.583 1.106 11.125 1.00 10.15 ? 308 VAL A CG2 1 ATOM 1701 N N . ALA A 1 221 ? 11.834 -2.363 14.246 1.00 10.28 ? 309 ALA A N 1 ATOM 1702 C CA . ALA A 1 221 ? 11.806 -3.713 14.768 1.00 9.40 ? 309 ALA A CA 1 ATOM 1703 C C . ALA A 1 221 ? 13.136 -4.205 15.247 1.00 9.50 ? 309 ALA A C 1 ATOM 1704 O O . ALA A 1 221 ? 13.265 -5.371 15.518 1.00 8.89 ? 309 ALA A O 1 ATOM 1705 C CB . ALA A 1 221 ? 11.204 -4.693 13.807 1.00 10.00 ? 309 ALA A CB 1 ATOM 1706 N N . ASN A 1 222 ? 14.116 -3.320 15.369 1.00 10.37 ? 310 ASN A N 1 ATOM 1707 C CA . ASN A 1 222 ? 15.387 -3.727 15.902 1.00 10.57 ? 310 ASN A CA 1 ATOM 1708 C C . ASN A 1 222 ? 15.618 -3.122 17.301 1.00 10.72 ? 310 ASN A C 1 ATOM 1709 O O . ASN A 1 222 ? 14.682 -2.519 17.901 1.00 11.91 ? 310 ASN A O 1 ATOM 1710 C CB . ASN A 1 222 ? 16.514 -3.468 14.891 1.00 9.98 ? 310 ASN A CB 1 ATOM 1711 C CG . ASN A 1 222 ? 17.637 -4.500 14.986 1.00 11.20 ? 310 ASN A CG 1 ATOM 1712 O OD1 . ASN A 1 222 ? 18.488 -4.406 15.856 1.00 11.57 ? 310 ASN A OD1 1 ATOM 1713 N ND2 . ASN A 1 222 ? 17.604 -5.524 14.126 1.00 10.95 ? 310 ASN A ND2 1 ATOM 1714 N N . TYR A 1 223 ? 16.856 -3.226 17.790 1.00 10.14 ? 311 TYR A N 1 ATOM 1715 C CA . TYR A 1 223 ? 17.183 -2.986 19.187 1.00 10.49 ? 311 TYR A CA 1 ATOM 1716 C C . TYR A 1 223 ? 18.293 -1.961 19.425 1.00 10.65 ? 311 TYR A C 1 ATOM 1717 O O . TYR A 1 223 ? 18.660 -1.710 20.555 1.00 11.67 ? 311 TYR A O 1 ATOM 1718 C CB . TYR A 1 223 ? 17.600 -4.318 19.801 1.00 10.42 ? 311 TYR A CB 1 ATOM 1719 C CG . TYR A 1 223 ? 16.693 -5.488 19.461 1.00 11.04 ? 311 TYR A CG 1 ATOM 1720 C CD1 . TYR A 1 223 ? 15.487 -5.664 20.136 1.00 11.33 ? 311 TYR A CD1 1 ATOM 1721 C CD2 . TYR A 1 223 ? 17.048 -6.435 18.489 1.00 13.41 ? 311 TYR A CD2 1 ATOM 1722 C CE1 . TYR A 1 223 ? 14.651 -6.728 19.854 1.00 11.94 ? 311 TYR A CE1 1 ATOM 1723 C CE2 . TYR A 1 223 ? 16.213 -7.515 18.218 1.00 13.42 ? 311 TYR A CE2 1 ATOM 1724 C CZ . TYR A 1 223 ? 15.003 -7.640 18.903 1.00 11.95 ? 311 TYR A CZ 1 ATOM 1725 O OH . TYR A 1 223 ? 14.194 -8.726 18.629 1.00 13.36 ? 311 TYR A OH 1 ATOM 1726 N N . ASN A 1 224 ? 18.839 -1.375 18.375 1.00 10.71 ? 312 ASN A N 1 ATOM 1727 C CA . ASN A 1 224 ? 19.986 -0.502 18.553 1.00 11.64 ? 312 ASN A CA 1 ATOM 1728 C C . ASN A 1 224 ? 19.754 0.701 19.447 1.00 11.98 ? 312 ASN A C 1 ATOM 1729 O O . ASN A 1 224 ? 18.694 1.261 19.491 1.00 11.82 ? 312 ASN A O 1 ATOM 1730 C CB . ASN A 1 224 ? 20.483 -0.011 17.212 1.00 10.83 ? 312 ASN A CB 1 ATOM 1731 C CG . ASN A 1 224 ? 20.901 -1.155 16.296 1.00 13.00 ? 312 ASN A CG 1 ATOM 1732 O OD1 . ASN A 1 224 ? 21.119 -2.267 16.747 1.00 17.79 ? 312 ASN A OD1 1 ATOM 1733 N ND2 . ASN A 1 224 ? 21.010 -0.872 15.016 1.00 16.08 ? 312 ASN A ND2 1 ATOM 1734 N N . ALA A 1 225 ? 20.794 1.120 20.146 1.00 12.78 ? 313 ALA A N 1 ATOM 1735 C CA . ALA A 1 225 ? 20.745 2.380 20.864 1.00 13.40 ? 313 ALA A CA 1 ATOM 1736 C C . ALA A 1 225 ? 20.673 3.552 19.890 1.00 13.76 ? 313 ALA A C 1 ATOM 1737 O O . ALA A 1 225 ? 21.123 3.453 18.724 1.00 14.31 ? 313 ALA A O 1 ATOM 1738 C CB . ALA A 1 225 ? 21.996 2.546 21.698 1.00 14.28 ? 313 ALA A CB 1 ATOM 1739 N N . TRP A 1 226 ? 20.052 4.633 20.353 1.00 15.35 ? 314 TRP A N 1 ATOM 1740 C CA . TRP A 1 226 ? 20.173 5.920 19.681 1.00 15.46 ? 314 TRP A CA 1 ATOM 1741 C C . TRP A 1 226 ? 21.640 6.411 19.885 1.00 16.84 ? 314 TRP A C 1 ATOM 1742 O O . TRP A 1 226 ? 22.366 6.643 18.910 1.00 15.56 ? 314 TRP A O 1 ATOM 1743 C CB . TRP A 1 226 ? 19.143 6.930 20.193 1.00 15.89 ? 314 TRP A CB 1 ATOM 1744 C CG . TRP A 1 226 ? 19.544 8.365 19.949 1.00 14.68 ? 314 TRP A CG 1 ATOM 1745 C CD1 . TRP A 1 226 ? 19.786 9.304 20.894 1.00 15.95 ? 314 TRP A CD1 1 ATOM 1746 C CD2 . TRP A 1 226 ? 19.749 9.009 18.682 1.00 15.89 ? 314 TRP A CD2 1 ATOM 1747 N NE1 . TRP A 1 226 ? 20.164 10.484 20.298 1.00 16.87 ? 314 TRP A NE1 1 ATOM 1748 C CE2 . TRP A 1 226 ? 20.154 10.326 18.942 1.00 17.02 ? 314 TRP A CE2 1 ATOM 1749 C CE3 . TRP A 1 226 ? 19.673 8.586 17.343 1.00 17.64 ? 314 TRP A CE3 1 ATOM 1750 C CZ2 . TRP A 1 226 ? 20.453 11.244 17.919 1.00 17.07 ? 314 TRP A CZ2 1 ATOM 1751 C CZ3 . TRP A 1 226 ? 19.962 9.477 16.337 1.00 17.03 ? 314 TRP A CZ3 1 ATOM 1752 C CH2 . TRP A 1 226 ? 20.367 10.800 16.633 1.00 18.91 ? 314 TRP A CH2 1 ATOM 1753 N N . SER A 1 227 ? 22.079 6.537 21.137 1.00 18.28 ? 315 SER A N 1 ATOM 1754 C CA . SER A 1 227 ? 23.452 7.008 21.424 1.00 20.48 ? 315 SER A CA 1 ATOM 1755 C C . SER A 1 227 ? 24.016 6.479 22.752 1.00 22.21 ? 315 SER A C 1 ATOM 1756 O O . SER A 1 227 ? 23.549 6.866 23.820 1.00 24.62 ? 315 SER A O 1 ATOM 1757 C CB . SER A 1 227 ? 23.486 8.535 21.447 1.00 20.16 ? 315 SER A CB 1 ATOM 1758 O OG . SER A 1 227 ? 24.773 9.050 21.795 1.00 21.00 ? 315 SER A OG 1 ATOM 1759 N N . VAL A 1 228 ? 25.006 5.592 22.696 1.00 24.10 ? 316 VAL A N 1 ATOM 1760 C CA . VAL A 1 228 ? 25.663 5.074 23.913 1.00 25.20 ? 316 VAL A CA 1 ATOM 1761 C C . VAL A 1 228 ? 27.133 5.435 23.866 1.00 26.46 ? 316 VAL A C 1 ATOM 1762 O O . VAL A 1 228 ? 27.713 5.487 22.788 1.00 25.88 ? 316 VAL A O 1 ATOM 1763 C CB . VAL A 1 228 ? 25.577 3.547 24.080 1.00 25.00 ? 316 VAL A CB 1 ATOM 1764 C CG1 . VAL A 1 228 ? 24.268 3.154 24.722 1.00 27.14 ? 316 VAL A CG1 1 ATOM 1765 C CG2 . VAL A 1 228 ? 25.798 2.844 22.758 1.00 24.81 ? 316 VAL A CG2 1 ATOM 1766 N N . SER A 1 229 ? 27.727 5.652 25.038 1.00 28.06 ? 317 SER A N 1 ATOM 1767 C CA . SER A 1 229 ? 29.117 6.101 25.165 1.00 29.71 ? 317 SER A CA 1 ATOM 1768 C C . SER A 1 229 ? 30.163 5.065 24.734 1.00 30.08 ? 317 SER A C 1 ATOM 1769 O O . SER A 1 229 ? 31.265 5.418 24.325 1.00 31.76 ? 317 SER A O 1 ATOM 1770 C CB . SER A 1 229 ? 29.367 6.529 26.608 1.00 29.93 ? 317 SER A CB 1 ATOM 1771 O OG . SER A 1 229 ? 28.818 5.569 27.511 1.00 31.73 ? 317 SER A OG 1 ATOM 1772 N N . SER A 1 230 ? 29.846 3.798 24.837 1.00 29.90 ? 318 SER A N 1 ATOM 1773 C CA . SER A 1 230 ? 30.776 2.816 24.316 1.00 29.58 ? 318 SER A CA 1 ATOM 1774 C C . SER A 1 230 ? 30.066 1.716 23.556 1.00 28.13 ? 318 SER A C 1 ATOM 1775 O O . SER A 1 230 ? 29.015 1.217 23.970 1.00 27.49 ? 318 SER A O 1 ATOM 1776 C CB . SER A 1 230 ? 31.540 2.125 25.422 1.00 30.35 ? 318 SER A CB 1 ATOM 1777 O OG . SER A 1 230 ? 30.615 1.559 26.323 1.00 31.57 ? 318 SER A OG 1 ATOM 1778 N N . PRO A 1 231 ? 30.715 1.243 22.505 1.00 26.71 ? 319 PRO A N 1 ATOM 1779 C CA . PRO A 1 231 ? 30.112 0.262 21.610 1.00 25.52 ? 319 PRO A CA 1 ATOM 1780 C C . PRO A 1 231 ? 29.762 -1.076 22.223 1.00 24.23 ? 319 PRO A C 1 ATOM 1781 O O . PRO A 1 231 ? 30.622 -1.726 22.794 1.00 23.33 ? 319 PRO A O 1 ATOM 1782 C CB . PRO A 1 231 ? 31.196 0.044 20.550 1.00 25.83 ? 319 PRO A CB 1 ATOM 1783 C CG . PRO A 1 231 ? 32.136 1.152 20.696 1.00 27.05 ? 319 PRO A CG 1 ATOM 1784 C CD . PRO A 1 231 ? 32.070 1.616 22.087 1.00 27.49 ? 319 PRO A CD 1 ATOM 1785 N N . PRO A 1 232 ? 28.526 -1.529 22.064 1.00 22.20 ? 320 PRO A N 1 ATOM 1786 C CA . PRO A 1 232 ? 28.219 -2.885 22.485 1.00 22.37 ? 320 PRO A CA 1 ATOM 1787 C C . PRO A 1 232 ? 29.168 -3.859 21.770 1.00 21.91 ? 320 PRO A C 1 ATOM 1788 O O . PRO A 1 232 ? 29.475 -3.694 20.581 1.00 22.50 ? 320 PRO A O 1 ATOM 1789 C CB . PRO A 1 232 ? 26.745 -3.069 22.090 1.00 21.64 ? 320 PRO A CB 1 ATOM 1790 C CG . PRO A 1 232 ? 26.204 -1.698 21.963 1.00 21.79 ? 320 PRO A CG 1 ATOM 1791 C CD . PRO A 1 232 ? 27.340 -0.820 21.552 1.00 22.57 ? 320 PRO A CD 1 ATOM 1792 N N . PRO A 1 233 ? 29.663 -4.853 22.503 1.00 22.30 ? 321 PRO A N 1 ATOM 1793 C CA . PRO A 1 233 ? 30.605 -5.857 21.969 1.00 21.72 ? 321 PRO A CA 1 ATOM 1794 C C . PRO A 1 233 ? 30.231 -6.480 20.641 1.00 20.94 ? 321 PRO A C 1 ATOM 1795 O O . PRO A 1 233 ? 31.081 -6.590 19.731 1.00 20.73 ? 321 PRO A O 1 ATOM 1796 C CB . PRO A 1 233 ? 30.639 -6.912 23.079 1.00 22.07 ? 321 PRO A CB 1 ATOM 1797 C CG . PRO A 1 233 ? 30.400 -6.103 24.326 1.00 23.39 ? 321 PRO A CG 1 ATOM 1798 C CD . PRO A 1 233 ? 29.384 -5.082 23.931 1.00 23.04 ? 321 PRO A CD 1 ATOM 1799 N N . TYR A 1 234 ? 28.968 -6.825 20.466 1.00 19.36 ? 322 TYR A N 1 ATOM 1800 C CA . TYR A 1 234 ? 28.577 -7.414 19.207 1.00 18.60 ? 322 TYR A CA 1 ATOM 1801 C C . TYR A 1 234 ? 28.624 -6.408 18.030 1.00 18.13 ? 322 TYR A C 1 ATOM 1802 O O . TYR A 1 234 ? 28.450 -6.824 16.906 1.00 17.21 ? 322 TYR A O 1 ATOM 1803 C CB . TYR A 1 234 ? 27.196 -8.053 19.335 1.00 18.56 ? 322 TYR A CB 1 ATOM 1804 C CG . TYR A 1 234 ? 26.224 -7.129 20.020 1.00 17.20 ? 322 TYR A CG 1 ATOM 1805 C CD1 . TYR A 1 234 ? 25.654 -6.070 19.329 1.00 14.90 ? 322 TYR A CD1 1 ATOM 1806 C CD2 . TYR A 1 234 ? 25.900 -7.295 21.350 1.00 15.39 ? 322 TYR A CD2 1 ATOM 1807 C CE1 . TYR A 1 234 ? 24.776 -5.183 19.939 1.00 11.57 ? 322 TYR A CE1 1 ATOM 1808 C CE2 . TYR A 1 234 ? 25.020 -6.433 21.982 1.00 15.70 ? 322 TYR A CE2 1 ATOM 1809 C CZ . TYR A 1 234 ? 24.464 -5.370 21.285 1.00 15.97 ? 322 TYR A CZ 1 ATOM 1810 O OH . TYR A 1 234 ? 23.620 -4.496 21.950 1.00 14.28 ? 322 TYR A OH 1 ATOM 1811 N N . THR A 1 235 ? 28.871 -5.113 18.273 1.00 18.67 ? 323 THR A N 1 ATOM 1812 C CA . THR A 1 235 ? 28.947 -4.148 17.152 1.00 18.70 ? 323 THR A CA 1 ATOM 1813 C C . THR A 1 235 ? 30.310 -4.026 16.464 1.00 20.39 ? 323 THR A C 1 ATOM 1814 O O . THR A 1 235 ? 30.421 -3.472 15.352 1.00 18.13 ? 323 THR A O 1 ATOM 1815 C CB . THR A 1 235 ? 28.500 -2.751 17.538 1.00 19.20 ? 323 THR A CB 1 ATOM 1816 O OG1 . THR A 1 235 ? 29.355 -2.175 18.550 1.00 17.64 ? 323 THR A OG1 1 ATOM 1817 C CG2 . THR A 1 235 ? 27.045 -2.762 18.100 1.00 17.93 ? 323 THR A CG2 1 ATOM 1818 N N . SER A 1 236 ? 31.345 -4.509 17.118 1.00 22.48 ? 324 SER A N 1 ATOM 1819 C CA . SER A 1 236 ? 32.711 -4.322 16.616 1.00 24.42 ? 324 SER A CA 1 ATOM 1820 C C . SER A 1 236 ? 32.890 -5.159 15.371 1.00 25.09 ? 324 SER A C 1 ATOM 1821 O O . SER A 1 236 ? 32.386 -6.266 15.310 1.00 25.18 ? 324 SER A O 1 ATOM 1822 C CB . SER A 1 236 ? 33.700 -4.753 17.707 1.00 25.52 ? 324 SER A CB 1 ATOM 1823 O OG . SER A 1 236 ? 35.047 -4.490 17.317 1.00 28.49 ? 324 SER A OG 1 ATOM 1824 N N . PRO A 1 237 ? 33.625 -4.695 14.365 1.00 26.33 ? 325 PRO A N 1 ATOM 1825 C CA . PRO A 1 237 ? 34.334 -3.415 14.305 1.00 27.13 ? 325 PRO A CA 1 ATOM 1826 C C . PRO A 1 237 ? 33.604 -2.203 13.643 1.00 27.16 ? 325 PRO A C 1 ATOM 1827 O O . PRO A 1 237 ? 34.257 -1.269 13.143 1.00 28.08 ? 325 PRO A O 1 ATOM 1828 C CB . PRO A 1 237 ? 35.568 -3.779 13.450 1.00 27.40 ? 325 PRO A CB 1 ATOM 1829 C CG . PRO A 1 237 ? 35.284 -5.132 12.851 1.00 27.18 ? 325 PRO A CG 1 ATOM 1830 C CD . PRO A 1 237 ? 33.911 -5.540 13.201 1.00 26.71 ? 325 PRO A CD 1 ATOM 1831 N N . ASN A 1 238 ? 32.283 -2.161 13.666 1.00 25.54 ? 326 ASN A N 1 ATOM 1832 C CA . ASN A 1 238 ? 31.572 -1.078 12.972 1.00 24.46 ? 326 ASN A CA 1 ATOM 1833 C C . ASN A 1 238 ? 31.634 0.261 13.689 1.00 23.86 ? 326 ASN A C 1 ATOM 1834 O O . ASN A 1 238 ? 31.246 0.349 14.839 1.00 23.93 ? 326 ASN A O 1 ATOM 1835 C CB . ASN A 1 238 ? 30.106 -1.508 12.773 1.00 24.62 ? 326 ASN A CB 1 ATOM 1836 C CG . ASN A 1 238 ? 29.331 -0.581 11.857 1.00 24.75 ? 326 ASN A CG 1 ATOM 1837 O OD1 . ASN A 1 238 ? 29.790 0.511 11.498 1.00 21.83 ? 326 ASN A OD1 1 ATOM 1838 N ND2 . ASN A 1 238 ? 28.119 -1.006 11.499 1.00 23.57 ? 326 ASN A ND2 1 ATOM 1839 N N . PRO A 1 239 ? 32.130 1.326 13.062 1.00 23.13 ? 327 PRO A N 1 ATOM 1840 C CA . PRO A 1 239 ? 32.159 2.621 13.756 1.00 22.97 ? 327 PRO A CA 1 ATOM 1841 C C . PRO A 1 239 ? 30.766 3.156 13.967 1.00 21.32 ? 327 PRO A C 1 ATOM 1842 O O . PRO A 1 239 ? 30.535 3.912 14.894 1.00 21.27 ? 327 PRO A O 1 ATOM 1843 C CB . PRO A 1 239 ? 32.928 3.541 12.800 1.00 23.13 ? 327 PRO A CB 1 ATOM 1844 C CG . PRO A 1 239 ? 32.841 2.880 11.490 1.00 23.98 ? 327 PRO A CG 1 ATOM 1845 C CD . PRO A 1 239 ? 32.690 1.407 11.709 1.00 24.03 ? 327 PRO A CD 1 ATOM 1846 N N . ASN A 1 240 ? 29.831 2.708 13.148 1.00 21.02 ? 328 ASN A N 1 ATOM 1847 C CA . ASN A 1 240 ? 28.460 3.155 13.275 1.00 19.67 ? 328 ASN A CA 1 ATOM 1848 C C . ASN A 1 240 ? 27.742 2.161 14.128 1.00 19.02 ? 328 ASN A C 1 ATOM 1849 O O . ASN A 1 240 ? 26.976 1.340 13.633 1.00 19.81 ? 328 ASN A O 1 ATOM 1850 C CB . ASN A 1 240 ? 27.856 3.286 11.899 1.00 20.06 ? 328 ASN A CB 1 ATOM 1851 C CG . ASN A 1 240 ? 28.560 4.336 11.104 1.00 20.58 ? 328 ASN A CG 1 ATOM 1852 O OD1 . ASN A 1 240 ? 28.881 5.401 11.650 1.00 19.76 ? 328 ASN A OD1 1 ATOM 1853 N ND2 . ASN A 1 240 ? 28.902 4.026 9.849 1.00 20.70 ? 328 ASN A ND2 1 ATOM 1854 N N . TYR A 1 241 ? 27.968 2.255 15.425 1.00 18.29 ? 329 TYR A N 1 ATOM 1855 C CA . TYR A 1 241 ? 27.506 1.209 16.312 1.00 18.09 ? 329 TYR A CA 1 ATOM 1856 C C . TYR A 1 241 ? 26.231 1.554 17.058 1.00 18.25 ? 329 TYR A C 1 ATOM 1857 O O . TYR A 1 241 ? 25.800 0.759 17.903 1.00 19.24 ? 329 TYR A O 1 ATOM 1858 C CB . TYR A 1 241 ? 28.595 0.850 17.297 1.00 17.72 ? 329 TYR A CB 1 ATOM 1859 C CG . TYR A 1 241 ? 29.068 2.044 18.061 1.00 18.84 ? 329 TYR A CG 1 ATOM 1860 C CD1 . TYR A 1 241 ? 28.334 2.538 19.121 1.00 18.98 ? 329 TYR A CD1 1 ATOM 1861 C CD2 . TYR A 1 241 ? 30.205 2.734 17.668 1.00 22.38 ? 329 TYR A CD2 1 ATOM 1862 C CE1 . TYR A 1 241 ? 28.747 3.637 19.823 1.00 23.03 ? 329 TYR A CE1 1 ATOM 1863 C CE2 . TYR A 1 241 ? 30.624 3.863 18.352 1.00 23.17 ? 329 TYR A CE2 1 ATOM 1864 C CZ . TYR A 1 241 ? 29.904 4.307 19.433 1.00 23.50 ? 329 TYR A CZ 1 ATOM 1865 O OH . TYR A 1 241 ? 30.328 5.431 20.126 1.00 25.28 ? 329 TYR A OH 1 ATOM 1866 N N . ASP A 1 242 ? 25.710 2.751 16.799 1.00 17.31 ? 330 ASP A N 1 ATOM 1867 C CA . ASP A 1 242 ? 24.402 3.190 17.235 1.00 16.99 ? 330 ASP A CA 1 ATOM 1868 C C . ASP A 1 242 ? 23.742 4.034 16.122 1.00 16.48 ? 330 ASP A C 1 ATOM 1869 O O . ASP A 1 242 ? 24.399 4.408 15.097 1.00 17.69 ? 330 ASP A O 1 ATOM 1870 C CB . ASP A 1 242 ? 24.466 3.925 18.559 1.00 17.59 ? 330 ASP A CB 1 ATOM 1871 C CG . ASP A 1 242 ? 25.357 5.159 18.538 1.00 19.01 ? 330 ASP A CG 1 ATOM 1872 O OD1 . ASP A 1 242 ? 25.633 5.761 17.458 1.00 20.30 ? 330 ASP A OD1 1 ATOM 1873 O OD2 . ASP A 1 242 ? 25.788 5.623 19.614 1.00 18.45 ? 330 ASP A OD2 1 ATOM 1874 N N . GLU A 1 243 ? 22.451 4.291 16.257 1.00 15.52 ? 331 GLU A N 1 ATOM 1875 C CA . GLU A 1 243 ? 21.725 4.990 15.183 1.00 14.84 ? 331 GLU A CA 1 ATOM 1876 C C . GLU A 1 243 ? 22.228 6.409 14.935 1.00 15.05 ? 331 GLU A C 1 ATOM 1877 O O . GLU A 1 243 ? 22.205 6.886 13.801 1.00 15.56 ? 331 GLU A O 1 ATOM 1878 C CB . GLU A 1 243 ? 20.229 4.961 15.456 1.00 14.72 ? 331 GLU A CB 1 ATOM 1879 C CG . GLU A 1 243 ? 19.706 3.509 15.536 1.00 14.15 ? 331 GLU A CG 1 ATOM 1880 C CD . GLU A 1 243 ? 19.862 2.777 14.195 1.00 16.38 ? 331 GLU A CD 1 ATOM 1881 O OE1 . GLU A 1 243 ? 19.410 3.358 13.177 1.00 15.68 ? 331 GLU A OE1 1 ATOM 1882 O OE2 . GLU A 1 243 ? 20.442 1.664 14.148 1.00 18.14 ? 331 GLU A OE2 1 ATOM 1883 N N . LYS A 1 244 ? 22.684 7.071 15.987 1.00 15.43 ? 332 LYS A N 1 ATOM 1884 C CA . LYS A 1 244 ? 23.188 8.418 15.885 1.00 17.14 ? 332 LYS A CA 1 ATOM 1885 C C . LYS A 1 244 ? 24.396 8.420 14.949 1.00 17.50 ? 332 LYS A C 1 ATOM 1886 O O . LYS A 1 244 ? 24.444 9.240 14.036 1.00 16.73 ? 332 LYS A O 1 ATOM 1887 C CB . LYS A 1 244 ? 23.520 9.023 17.265 1.00 18.02 ? 332 LYS A CB 1 ATOM 1888 C CG . LYS A 1 244 ? 24.164 10.391 17.183 1.00 19.42 ? 332 LYS A CG 1 ATOM 1889 C CD . LYS A 1 244 ? 24.410 10.985 18.539 1.00 21.95 ? 332 LYS A CD 1 ATOM 1890 C CE . LYS A 1 244 ? 25.121 12.316 18.412 1.00 23.32 ? 332 LYS A CE 1 ATOM 1891 N NZ . LYS A 1 244 ? 24.693 13.239 19.488 1.00 23.05 ? 332 LYS A NZ 1 ATOM 1892 N N . HIS A 1 245 ? 25.353 7.512 15.169 1.00 18.02 ? 333 HIS A N 1 ATOM 1893 C CA . HIS A 1 245 ? 26.533 7.402 14.317 1.00 19.53 ? 333 HIS A CA 1 ATOM 1894 C C . HIS A 1 245 ? 26.137 7.075 12.894 1.00 19.27 ? 333 HIS A C 1 ATOM 1895 O O . HIS A 1 245 ? 26.670 7.645 11.941 1.00 19.26 ? 333 HIS A O 1 ATOM 1896 C CB . HIS A 1 245 ? 27.506 6.342 14.845 1.00 20.36 ? 333 HIS A CB 1 ATOM 1897 C CG . HIS A 1 245 ? 28.406 6.842 15.942 1.00 22.41 ? 333 HIS A CG 1 ATOM 1898 N ND1 . HIS A 1 245 ? 27.995 6.956 17.249 1.00 26.98 ? 333 HIS A ND1 1 ATOM 1899 C CD2 . HIS A 1 245 ? 29.700 7.252 15.917 1.00 27.26 ? 333 HIS A CD2 1 ATOM 1900 C CE1 . HIS A 1 245 ? 28.995 7.416 17.990 1.00 28.65 ? 333 HIS A CE1 1 ATOM 1901 N NE2 . HIS A 1 245 ? 30.040 7.612 17.201 1.00 29.95 ? 333 HIS A NE2 1 ATOM 1902 N N . TYR A 1 246 ? 25.213 6.130 12.752 1.00 17.97 ? 334 TYR A N 1 ATOM 1903 C CA . TYR A 1 246 ? 24.661 5.729 11.461 1.00 17.38 ? 334 TYR A CA 1 ATOM 1904 C C . TYR A 1 246 ? 24.094 6.895 10.671 1.00 16.72 ? 334 TYR A C 1 ATOM 1905 O O . TYR A 1 246 ? 24.501 7.168 9.530 1.00 17.87 ? 334 TYR A O 1 ATOM 1906 C CB . TYR A 1 246 ? 23.509 4.727 11.708 1.00 17.36 ? 334 TYR A CB 1 ATOM 1907 C CG . TYR A 1 246 ? 22.785 4.271 10.467 1.00 17.62 ? 334 TYR A CG 1 ATOM 1908 C CD1 . TYR A 1 246 ? 23.459 4.130 9.280 1.00 15.87 ? 334 TYR A CD1 1 ATOM 1909 C CD2 . TYR A 1 246 ? 21.425 3.902 10.503 1.00 17.68 ? 334 TYR A CD2 1 ATOM 1910 C CE1 . TYR A 1 246 ? 22.843 3.683 8.150 1.00 18.21 ? 334 TYR A CE1 1 ATOM 1911 C CE2 . TYR A 1 246 ? 20.792 3.441 9.380 1.00 14.50 ? 334 TYR A CE2 1 ATOM 1912 C CZ . TYR A 1 246 ? 21.487 3.352 8.191 1.00 17.63 ? 334 TYR A CZ 1 ATOM 1913 O OH . TYR A 1 246 ? 20.788 2.893 7.097 1.00 16.98 ? 334 TYR A OH 1 ATOM 1914 N N . ILE A 1 247 ? 23.186 7.615 11.301 1.00 15.84 ? 335 ILE A N 1 ATOM 1915 C CA . ILE A 1 247 ? 22.495 8.712 10.666 1.00 16.14 ? 335 ILE A CA 1 ATOM 1916 C C . ILE A 1 247 ? 23.447 9.872 10.319 1.00 16.85 ? 335 ILE A C 1 ATOM 1917 O O . ILE A 1 247 ? 23.355 10.434 9.244 1.00 17.15 ? 335 ILE A O 1 ATOM 1918 C CB . ILE A 1 247 ? 21.337 9.120 11.537 1.00 15.58 ? 335 ILE A CB 1 ATOM 1919 C CG1 . ILE A 1 247 ? 20.281 7.996 11.453 1.00 14.99 ? 335 ILE A CG1 1 ATOM 1920 C CG2 . ILE A 1 247 ? 20.802 10.455 11.116 1.00 16.69 ? 335 ILE A CG2 1 ATOM 1921 C CD1 . ILE A 1 247 ? 19.244 8.017 12.510 1.00 16.25 ? 335 ILE A CD1 1 ATOM 1922 N N . GLU A 1 248 ? 24.384 10.157 11.207 1.00 17.36 ? 336 GLU A N 1 ATOM 1923 C CA . GLU A 1 248 ? 25.354 11.223 10.966 1.00 18.27 ? 336 GLU A CA 1 ATOM 1924 C C . GLU A 1 248 ? 26.257 10.892 9.772 1.00 17.97 ? 336 GLU A C 1 ATOM 1925 O O . GLU A 1 248 ? 26.655 11.795 9.028 1.00 18.86 ? 336 GLU A O 1 ATOM 1926 C CB . GLU A 1 248 ? 26.112 11.566 12.258 1.00 17.89 ? 336 GLU A CB 1 ATOM 1927 C CG . GLU A 1 248 ? 25.243 12.469 13.142 1.00 20.31 ? 336 GLU A CG 1 ATOM 1928 C CD . GLU A 1 248 ? 25.890 12.966 14.420 1.00 21.74 ? 336 GLU A CD 1 ATOM 1929 O OE1 . GLU A 1 248 ? 27.045 12.649 14.642 1.00 21.74 ? 336 GLU A OE1 1 ATOM 1930 O OE2 . GLU A 1 248 ? 25.224 13.680 15.212 1.00 24.26 ? 336 GLU A OE2 1 ATOM 1931 N N . ALA A 1 249 ? 26.586 9.619 9.591 1.00 17.41 ? 337 ALA A N 1 ATOM 1932 C CA . ALA A 1 249 ? 27.305 9.150 8.402 1.00 16.86 ? 337 ALA A CA 1 ATOM 1933 C C . ALA A 1 249 ? 26.440 9.051 7.148 1.00 17.37 ? 337 ALA A C 1 ATOM 1934 O O . ALA A 1 249 ? 26.899 9.320 6.013 1.00 16.63 ? 337 ALA A O 1 ATOM 1935 C CB . ALA A 1 249 ? 27.928 7.828 8.667 1.00 17.54 ? 337 ALA A CB 1 ATOM 1936 N N . PHE A 1 250 ? 25.200 8.614 7.335 1.00 15.67 ? 338 PHE A N 1 ATOM 1937 C CA . PHE A 1 250 ? 24.271 8.388 6.259 1.00 15.91 ? 338 PHE A CA 1 ATOM 1938 C C . PHE A 1 250 ? 23.782 9.674 5.571 1.00 15.29 ? 338 PHE A C 1 ATOM 1939 O O . PHE A 1 250 ? 23.770 9.727 4.352 1.00 16.01 ? 338 PHE A O 1 ATOM 1940 C CB . PHE A 1 250 ? 23.056 7.641 6.833 1.00 16.15 ? 338 PHE A CB 1 ATOM 1941 C CG . PHE A 1 250 ? 22.274 6.850 5.830 1.00 15.23 ? 338 PHE A CG 1 ATOM 1942 C CD1 . PHE A 1 250 ? 22.782 6.594 4.602 1.00 13.96 ? 338 PHE A CD1 1 ATOM 1943 C CD2 . PHE A 1 250 ? 21.015 6.363 6.144 1.00 12.56 ? 338 PHE A CD2 1 ATOM 1944 C CE1 . PHE A 1 250 ? 22.105 5.853 3.696 1.00 14.61 ? 338 PHE A CE1 1 ATOM 1945 C CE2 . PHE A 1 250 ? 20.295 5.615 5.209 1.00 15.53 ? 338 PHE A CE2 1 ATOM 1946 C CZ . PHE A 1 250 ? 20.843 5.373 3.978 1.00 16.95 ? 338 PHE A CZ 1 ATOM 1947 N N . ARG A 1 251 ? 23.363 10.680 6.338 1.00 16.29 ? 339 ARG A N 1 ATOM 1948 C CA . ARG A 1 251 ? 22.716 11.869 5.789 1.00 16.68 ? 339 ARG A CA 1 ATOM 1949 C C . ARG A 1 251 ? 23.539 12.587 4.696 1.00 17.77 ? 339 ARG A C 1 ATOM 1950 O O . ARG A 1 251 ? 23.034 12.809 3.603 1.00 17.10 ? 339 ARG A O 1 ATOM 1951 C CB . ARG A 1 251 ? 22.316 12.817 6.904 1.00 17.14 ? 339 ARG A CB 1 ATOM 1952 C CG . ARG A 1 251 ? 21.758 14.147 6.504 1.00 17.53 ? 339 ARG A CG 1 ATOM 1953 C CD . ARG A 1 251 ? 20.659 14.198 5.454 1.00 18.76 ? 339 ARG A CD 1 ATOM 1954 N NE . ARG A 1 251 ? 20.412 15.626 5.254 1.00 19.02 ? 339 ARG A NE 1 ATOM 1955 C CZ . ARG A 1 251 ? 19.528 16.358 5.922 1.00 20.91 ? 339 ARG A CZ 1 ATOM 1956 N NH1 . ARG A 1 251 ? 18.694 15.800 6.776 1.00 21.92 ? 339 ARG A NH1 1 ATOM 1957 N NH2 . ARG A 1 251 ? 19.461 17.671 5.724 1.00 21.30 ? 339 ARG A NH2 1 ATOM 1958 N N . PRO A 1 252 ? 24.797 12.913 4.971 1.00 18.95 ? 340 PRO A N 1 ATOM 1959 C CA . PRO A 1 252 ? 25.650 13.563 3.958 1.00 20.21 ? 340 PRO A CA 1 ATOM 1960 C C . PRO A 1 252 ? 25.724 12.777 2.652 1.00 20.09 ? 340 PRO A C 1 ATOM 1961 O O . PRO A 1 252 ? 25.807 13.350 1.581 1.00 21.69 ? 340 PRO A O 1 ATOM 1962 C CB . PRO A 1 252 ? 27.051 13.569 4.602 1.00 20.17 ? 340 PRO A CB 1 ATOM 1963 C CG . PRO A 1 252 ? 26.896 13.174 6.004 1.00 21.24 ? 340 PRO A CG 1 ATOM 1964 C CD . PRO A 1 252 ? 25.490 12.718 6.239 1.00 19.21 ? 340 PRO A CD 1 ATOM 1965 N N . LEU A 1 253 ? 25.746 11.461 2.711 1.00 20.38 ? 341 LEU A N 1 ATOM 1966 C CA . LEU A 1 253 ? 25.840 10.698 1.478 1.00 19.96 ? 341 LEU A CA 1 ATOM 1967 C C . LEU A 1 253 ? 24.526 10.780 0.696 1.00 19.44 ? 341 LEU A C 1 ATOM 1968 O O . LEU A 1 253 ? 24.524 10.827 -0.536 1.00 20.21 ? 341 LEU A O 1 ATOM 1969 C CB . LEU A 1 253 ? 26.200 9.266 1.787 1.00 20.40 ? 341 LEU A CB 1 ATOM 1970 C CG . LEU A 1 253 ? 27.526 9.063 2.529 1.00 22.21 ? 341 LEU A CG 1 ATOM 1971 C CD1 . LEU A 1 253 ? 27.527 7.722 3.154 1.00 23.59 ? 341 LEU A CD1 1 ATOM 1972 C CD2 . LEU A 1 253 ? 28.731 9.160 1.623 1.00 24.70 ? 341 LEU A CD2 1 ATOM 1973 N N . LEU A 1 254 ? 23.414 10.785 1.424 1.00 19.11 ? 342 LEU A N 1 ATOM 1974 C CA . LEU A 1 254 ? 22.090 10.896 0.826 1.00 18.57 ? 342 LEU A CA 1 ATOM 1975 C C . LEU A 1 254 ? 21.924 12.308 0.220 1.00 19.21 ? 342 LEU A C 1 ATOM 1976 O O . LEU A 1 254 ? 21.439 12.482 -0.909 1.00 18.48 ? 342 LEU A O 1 ATOM 1977 C CB . LEU A 1 254 ? 21.022 10.671 1.904 1.00 17.59 ? 342 LEU A CB 1 ATOM 1978 C CG . LEU A 1 254 ? 20.905 9.235 2.442 1.00 18.25 ? 342 LEU A CG 1 ATOM 1979 C CD1 . LEU A 1 254 ? 20.204 9.180 3.802 1.00 18.95 ? 342 LEU A CD1 1 ATOM 1980 C CD2 . LEU A 1 254 ? 20.163 8.435 1.414 1.00 18.76 ? 342 LEU A CD2 1 ATOM 1981 N N . GLU A 1 255 ? 22.370 13.295 0.976 1.00 19.75 ? 343 GLU A N 1 ATOM 1982 C CA . GLU A 1 255 ? 22.209 14.659 0.568 1.00 21.66 ? 343 GLU A CA 1 ATOM 1983 C C . GLU A 1 255 ? 22.997 14.984 -0.703 1.00 21.61 ? 343 GLU A C 1 ATOM 1984 O O . GLU A 1 255 ? 22.481 15.617 -1.610 1.00 21.40 ? 343 GLU A O 1 ATOM 1985 C CB . GLU A 1 255 ? 22.627 15.586 1.702 1.00 22.67 ? 343 GLU A CB 1 ATOM 1986 C CG . GLU A 1 255 ? 22.460 17.061 1.374 1.00 24.68 ? 343 GLU A CG 1 ATOM 1987 C CD . GLU A 1 255 ? 21.868 17.845 2.528 1.00 26.69 ? 343 GLU A CD 1 ATOM 1988 O OE1 . GLU A 1 255 ? 22.014 17.404 3.692 1.00 27.43 ? 343 GLU A OE1 1 ATOM 1989 O OE2 . GLU A 1 255 ? 21.258 18.903 2.292 1.00 28.94 ? 343 GLU A OE2 1 ATOM 1990 N N . ALA A 1 256 ? 24.228 14.522 -0.753 1.00 21.99 ? 344 ALA A N 1 ATOM 1991 C CA . ALA A 1 256 ? 25.097 14.763 -1.896 1.00 22.89 ? 344 ALA A CA 1 ATOM 1992 C C . ALA A 1 256 ? 24.488 14.142 -3.168 1.00 23.24 ? 344 ALA A C 1 ATOM 1993 O O . ALA A 1 256 ? 24.829 14.498 -4.298 1.00 23.46 ? 344 ALA A O 1 ATOM 1994 C CB . ALA A 1 256 ? 26.460 14.191 -1.598 1.00 23.17 ? 344 ALA A CB 1 ATOM 1995 N N . ARG A 1 257 ? 23.564 13.201 -2.987 1.00 23.35 ? 345 ARG A N 1 ATOM 1996 C CA . ARG A 1 257 ? 22.895 12.597 -4.129 1.00 23.59 ? 345 ARG A CA 1 ATOM 1997 C C . ARG A 1 257 ? 21.443 13.064 -4.262 1.00 22.06 ? 345 ARG A C 1 ATOM 1998 O O . ARG A 1 257 ? 20.635 12.421 -4.938 1.00 23.04 ? 345 ARG A O 1 ATOM 1999 C CB . ARG A 1 257 ? 23.031 11.080 -4.097 1.00 24.00 ? 345 ARG A CB 1 ATOM 2000 C CG . ARG A 1 257 ? 24.476 10.623 -4.021 1.00 28.16 ? 345 ARG A CG 1 ATOM 2001 C CD . ARG A 1 257 ? 24.650 9.275 -3.380 1.00 30.89 ? 345 ARG A CD 1 ATOM 2002 N NE . ARG A 1 257 ? 26.027 8.812 -3.396 1.00 33.40 ? 345 ARG A NE 1 ATOM 2003 C CZ . ARG A 1 257 ? 26.986 9.311 -2.621 1.00 33.57 ? 345 ARG A CZ 1 ATOM 2004 N NH1 . ARG A 1 257 ? 26.709 10.294 -1.777 1.00 32.60 ? 345 ARG A NH1 1 ATOM 2005 N NH2 . ARG A 1 257 ? 28.225 8.834 -2.697 1.00 37.42 ? 345 ARG A NH2 1 ATOM 2006 N N . GLY A 1 258 ? 21.118 14.179 -3.615 1.00 20.92 ? 346 GLY A N 1 ATOM 2007 C CA . GLY A 1 258 ? 19.850 14.864 -3.830 1.00 20.51 ? 346 GLY A CA 1 ATOM 2008 C C . GLY A 1 258 ? 18.685 14.544 -2.911 1.00 20.21 ? 346 GLY A C 1 ATOM 2009 O O . GLY A 1 258 ? 17.561 14.960 -3.170 1.00 19.51 ? 346 GLY A O 1 ATOM 2010 N N . PHE A 1 259 ? 18.949 13.806 -1.838 1.00 19.14 ? 347 PHE A N 1 ATOM 2011 C CA . PHE A 1 259 ? 17.886 13.412 -0.938 1.00 18.46 ? 347 PHE A CA 1 ATOM 2012 C C . PHE A 1 259 ? 18.313 13.787 0.474 1.00 17.96 ? 347 PHE A C 1 ATOM 2013 O O . PHE A 1 259 ? 19.053 13.057 1.131 1.00 17.93 ? 347 PHE A O 1 ATOM 2014 C CB . PHE A 1 259 ? 17.679 11.918 -1.091 1.00 18.63 ? 347 PHE A CB 1 ATOM 2015 C CG . PHE A 1 259 ? 16.585 11.352 -0.261 1.00 18.19 ? 347 PHE A CG 1 ATOM 2016 C CD1 . PHE A 1 259 ? 15.543 12.102 0.253 1.00 19.44 ? 347 PHE A CD1 1 ATOM 2017 C CD2 . PHE A 1 259 ? 16.616 10.001 -0.015 1.00 19.73 ? 347 PHE A CD2 1 ATOM 2018 C CE1 . PHE A 1 259 ? 14.556 11.476 1.022 1.00 19.86 ? 347 PHE A CE1 1 ATOM 2019 C CE2 . PHE A 1 259 ? 15.662 9.372 0.732 1.00 19.47 ? 347 PHE A CE2 1 ATOM 2020 C CZ . PHE A 1 259 ? 14.626 10.083 1.253 1.00 18.67 ? 347 PHE A CZ 1 ATOM 2021 N N . PRO A 1 260 ? 17.893 14.962 0.906 1.00 17.55 ? 348 PRO A N 1 ATOM 2022 C CA . PRO A 1 260 ? 18.204 15.482 2.241 1.00 17.23 ? 348 PRO A CA 1 ATOM 2023 C C . PRO A 1 260 ? 17.282 14.887 3.310 1.00 16.64 ? 348 PRO A C 1 ATOM 2024 O O . PRO A 1 260 ? 16.526 15.587 4.002 1.00 15.35 ? 348 PRO A O 1 ATOM 2025 C CB . PRO A 1 260 ? 17.914 16.985 2.116 1.00 17.99 ? 348 PRO A CB 1 ATOM 2026 C CG . PRO A 1 260 ? 17.175 17.176 0.851 1.00 19.14 ? 348 PRO A CG 1 ATOM 2027 C CD . PRO A 1 260 ? 17.157 15.952 0.096 1.00 18.06 ? 348 PRO A CD 1 ATOM 2028 N N . ALA A 1 261 ? 17.380 13.584 3.440 1.00 15.61 ? 349 ALA A N 1 ATOM 2029 C CA . ALA A 1 261 ? 16.470 12.856 4.309 1.00 15.59 ? 349 ALA A CA 1 ATOM 2030 C C . ALA A 1 261 ? 16.550 13.210 5.796 1.00 15.15 ? 349 ALA A C 1 ATOM 2031 O O . ALA A 1 261 ? 17.631 13.279 6.369 1.00 16.07 ? 349 ALA A O 1 ATOM 2032 C CB . ALA A 1 261 ? 16.721 11.395 4.115 1.00 15.13 ? 349 ALA A CB 1 ATOM 2033 N N . GLN A 1 262 ? 15.390 13.479 6.388 1.00 14.68 ? 350 GLN A N 1 ATOM 2034 C CA . GLN A 1 262 ? 15.230 13.546 7.826 1.00 14.46 ? 350 GLN A CA 1 ATOM 2035 C C . GLN A 1 262 ? 14.865 12.138 8.302 1.00 13.87 ? 350 GLN A C 1 ATOM 2036 O O . GLN A 1 262 ? 14.306 11.336 7.531 1.00 12.89 ? 350 GLN A O 1 ATOM 2037 C CB . GLN A 1 262 ? 14.123 14.523 8.186 1.00 15.36 ? 350 GLN A CB 1 ATOM 2038 C CG . GLN A 1 262 ? 14.468 15.976 7.913 1.00 17.62 ? 350 GLN A CG 1 ATOM 2039 C CD . GLN A 1 262 ? 15.490 16.498 8.906 1.00 20.22 ? 350 GLN A CD 1 ATOM 2040 O OE1 . GLN A 1 262 ? 16.613 16.764 8.531 1.00 20.79 ? 350 GLN A OE1 1 ATOM 2041 N NE2 . GLN A 1 262 ? 15.092 16.618 10.190 1.00 18.23 ? 350 GLN A NE2 1 ATOM 2042 N N . PHE A 1 263 ? 15.143 11.835 9.563 1.00 12.20 ? 351 PHE A N 1 ATOM 2043 C CA . PHE A 1 263 ? 15.000 10.480 10.042 1.00 12.67 ? 351 PHE A CA 1 ATOM 2044 C C . PHE A 1 263 ? 14.047 10.374 11.219 1.00 11.63 ? 351 PHE A C 1 ATOM 2045 O O . PHE A 1 263 ? 13.834 11.362 11.965 1.00 12.12 ? 351 PHE A O 1 ATOM 2046 C CB . PHE A 1 263 ? 16.368 9.997 10.498 1.00 12.94 ? 351 PHE A CB 1 ATOM 2047 C CG . PHE A 1 263 ? 17.306 9.748 9.395 1.00 12.48 ? 351 PHE A CG 1 ATOM 2048 C CD1 . PHE A 1 263 ? 17.992 10.784 8.805 1.00 15.82 ? 351 PHE A CD1 1 ATOM 2049 C CD2 . PHE A 1 263 ? 17.481 8.488 8.911 1.00 14.79 ? 351 PHE A CD2 1 ATOM 2050 C CE1 . PHE A 1 263 ? 18.829 10.546 7.769 1.00 14.65 ? 351 PHE A CE1 1 ATOM 2051 C CE2 . PHE A 1 263 ? 18.335 8.240 7.886 1.00 14.14 ? 351 PHE A CE2 1 ATOM 2052 C CZ . PHE A 1 263 ? 19.011 9.262 7.309 1.00 16.19 ? 351 PHE A CZ 1 ATOM 2053 N N . ILE A 1 264 ? 13.417 9.212 11.341 1.00 11.45 ? 352 ILE A N 1 ATOM 2054 C CA . ILE A 1 264 ? 12.793 8.829 12.602 1.00 10.63 ? 352 ILE A CA 1 ATOM 2055 C C . ILE A 1 264 ? 13.496 7.545 13.023 1.00 10.56 ? 352 ILE A C 1 ATOM 2056 O O . ILE A 1 264 ? 13.915 6.766 12.186 1.00 9.92 ? 352 ILE A O 1 ATOM 2057 C CB . ILE A 1 264 ? 11.277 8.659 12.520 1.00 10.99 ? 352 ILE A CB 1 ATOM 2058 C CG1 . ILE A 1 264 ? 10.865 7.595 11.496 1.00 9.62 ? 352 ILE A CG1 1 ATOM 2059 C CG2 . ILE A 1 264 ? 10.646 10.030 12.222 1.00 10.66 ? 352 ILE A CG2 1 ATOM 2060 C CD1 . ILE A 1 264 ? 9.338 7.345 11.575 1.00 10.55 ? 352 ILE A CD1 1 ATOM 2061 N N . VAL A 1 265 ? 13.625 7.333 14.324 1.00 10.17 ? 353 VAL A N 1 ATOM 2062 C CA . VAL A 1 265 ? 14.361 6.208 14.828 1.00 10.21 ? 353 VAL A CA 1 ATOM 2063 C C . VAL A 1 265 ? 13.518 5.394 15.823 1.00 9.88 ? 353 VAL A C 1 ATOM 2064 O O . VAL A 1 265 ? 13.048 5.939 16.802 1.00 11.20 ? 353 VAL A O 1 ATOM 2065 C CB . VAL A 1 265 ? 15.604 6.699 15.520 1.00 10.63 ? 353 VAL A CB 1 ATOM 2066 C CG1 . VAL A 1 265 ? 16.462 5.526 15.989 1.00 11.58 ? 353 VAL A CG1 1 ATOM 2067 C CG2 . VAL A 1 265 ? 16.429 7.569 14.555 1.00 11.49 ? 353 VAL A CG2 1 ATOM 2068 N N . ASP A 1 266 ? 13.296 4.119 15.533 1.00 9.45 ? 354 ASP A N 1 ATOM 2069 C CA . ASP A 1 266 ? 12.589 3.234 16.455 1.00 10.14 ? 354 ASP A CA 1 ATOM 2070 C C . ASP A 1 266 ? 13.448 3.059 17.705 1.00 10.29 ? 354 ASP A C 1 ATOM 2071 O O . ASP A 1 266 ? 14.635 2.726 17.595 1.00 10.86 ? 354 ASP A O 1 ATOM 2072 C CB . ASP A 1 266 ? 12.349 1.881 15.792 1.00 9.91 ? 354 ASP A CB 1 ATOM 2073 C CG . ASP A 1 266 ? 11.193 1.078 16.407 1.00 10.84 ? 354 ASP A CG 1 ATOM 2074 O OD1 . ASP A 1 266 ? 10.726 1.423 17.512 1.00 9.52 ? 354 ASP A OD1 1 ATOM 2075 O OD2 . ASP A 1 266 ? 10.723 0.055 15.832 1.00 9.82 ? 354 ASP A OD2 1 ATOM 2076 N N . GLN A 1 267 ? 12.836 3.255 18.873 1.00 10.43 ? 355 GLN A N 1 ATOM 2077 C CA . GLN A 1 267 ? 13.482 2.986 20.162 1.00 10.43 ? 355 GLN A CA 1 ATOM 2078 C C . GLN A 1 267 ? 12.590 2.131 21.072 1.00 10.86 ? 355 GLN A C 1 ATOM 2079 O O . GLN A 1 267 ? 12.860 1.984 22.268 1.00 10.36 ? 355 GLN A O 1 ATOM 2080 C CB . GLN A 1 267 ? 13.824 4.288 20.869 1.00 10.96 ? 355 GLN A CB 1 ATOM 2081 C CG . GLN A 1 267 ? 14.979 5.051 20.193 1.00 10.99 ? 355 GLN A CG 1 ATOM 2082 C CD . GLN A 1 267 ? 16.309 4.407 20.449 1.00 11.87 ? 355 GLN A CD 1 ATOM 2083 O OE1 . GLN A 1 267 ? 16.859 4.524 21.562 1.00 12.41 ? 355 GLN A OE1 1 ATOM 2084 N NE2 . GLN A 1 267 ? 16.845 3.726 19.436 1.00 12.47 ? 355 GLN A NE2 1 ATOM 2085 N N . GLY A 1 268 ? 11.557 1.544 20.492 1.00 10.92 ? 356 GLY A N 1 ATOM 2086 C CA . GLY A 1 268 ? 10.569 0.808 21.254 1.00 11.51 ? 356 GLY A CA 1 ATOM 2087 C C . GLY A 1 268 ? 11.165 -0.359 22.026 1.00 12.09 ? 356 GLY A C 1 ATOM 2088 O O . GLY A 1 268 ? 10.588 -0.736 23.027 1.00 13.06 ? 356 GLY A O 1 ATOM 2089 N N . ARG A 1 269 ? 12.256 -0.957 21.550 1.00 10.97 ? 357 ARG A N 1 ATOM 2090 C CA . ARG A 1 269 ? 12.899 -2.050 22.279 1.00 11.71 ? 357 ARG A CA 1 ATOM 2091 C C . ARG A 1 269 ? 14.400 -1.785 22.483 1.00 11.86 ? 357 ARG A C 1 ATOM 2092 O O . ARG A 1 269 ? 15.191 -2.714 22.478 1.00 11.33 ? 357 ARG A O 1 ATOM 2093 C CB . ARG A 1 269 ? 12.677 -3.383 21.560 1.00 11.91 ? 357 ARG A CB 1 ATOM 2094 C CG . ARG A 1 269 ? 11.214 -3.681 21.257 1.00 12.41 ? 357 ARG A CG 1 ATOM 2095 C CD . ARG A 1 269 ? 10.903 -5.126 20.833 1.00 12.86 ? 357 ARG A CD 1 ATOM 2096 N NE . ARG A 1 269 ? 11.340 -5.339 19.457 1.00 10.30 ? 357 ARG A NE 1 ATOM 2097 C CZ . ARG A 1 269 ? 11.304 -6.492 18.822 1.00 12.64 ? 357 ARG A CZ 1 ATOM 2098 N NH1 . ARG A 1 269 ? 10.801 -7.588 19.404 1.00 15.45 ? 357 ARG A NH1 1 ATOM 2099 N NH2 . ARG A 1 269 ? 11.742 -6.547 17.580 1.00 13.26 ? 357 ARG A NH2 1 ATOM 2100 N N . SER A 1 270 ? 14.771 -0.513 22.647 1.00 11.64 ? 358 SER A N 1 ATOM 2101 C CA . SER A 1 270 ? 16.185 -0.109 22.758 1.00 12.04 ? 358 SER A CA 1 ATOM 2102 C C . SER A 1 270 ? 16.605 0.340 24.144 1.00 12.75 ? 358 SER A C 1 ATOM 2103 O O . SER A 1 270 ? 17.700 0.879 24.322 1.00 13.03 ? 358 SER A O 1 ATOM 2104 C CB . SER A 1 270 ? 16.454 1.022 21.779 1.00 10.94 ? 358 SER A CB 1 ATOM 2105 O OG . SER A 1 270 ? 16.273 0.564 20.442 1.00 9.75 ? 358 SER A OG 1 ATOM 2106 N N . GLY A 1 271 ? 15.742 0.147 25.126 1.00 13.50 ? 359 GLY A N 1 ATOM 2107 C CA . GLY A 1 271 ? 15.998 0.700 26.439 1.00 14.22 ? 359 GLY A CA 1 ATOM 2108 C C . GLY A 1 271 ? 17.174 0.126 27.171 1.00 14.56 ? 359 GLY A C 1 ATOM 2109 O O . GLY A 1 271 ? 17.821 0.837 27.952 1.00 14.68 ? 359 GLY A O 1 ATOM 2110 N N . LYS A 1 272 ? 17.432 -1.153 26.949 1.00 14.83 ? 360 LYS A N 1 ATOM 2111 C CA . LYS A 1 272 ? 18.519 -1.833 27.645 1.00 16.15 ? 360 LYS A CA 1 ATOM 2112 C C . LYS A 1 272 ? 19.695 -2.069 26.722 1.00 16.43 ? 360 LYS A C 1 ATOM 2113 O O . LYS A 1 272 ? 19.570 -2.732 25.678 1.00 16.74 ? 360 LYS A O 1 ATOM 2114 C CB . LYS A 1 272 ? 18.062 -3.148 28.225 1.00 15.78 ? 360 LYS A CB 1 ATOM 2115 C CG . LYS A 1 272 ? 19.114 -3.788 29.148 1.00 18.57 ? 360 LYS A CG 1 ATOM 2116 C CD . LYS A 1 272 ? 18.522 -4.930 29.983 1.00 21.71 ? 360 LYS A CD 1 ATOM 2117 C CE . LYS A 1 272 ? 19.603 -5.869 30.599 1.00 26.45 ? 360 LYS A CE 1 ATOM 2118 N NZ . LYS A 1 272 ? 20.837 -5.226 31.059 1.00 26.14 ? 360 LYS A NZ 1 ATOM 2119 N N . GLN A 1 273 ? 20.830 -1.502 27.093 1.00 15.90 ? 361 GLN A N 1 ATOM 2120 C CA . GLN A 1 273 ? 22.031 -1.616 26.297 1.00 16.07 ? 361 GLN A CA 1 ATOM 2121 C C . GLN A 1 273 ? 23.253 -1.926 27.158 1.00 16.72 ? 361 GLN A C 1 ATOM 2122 O O . GLN A 1 273 ? 23.426 -1.310 28.176 1.00 16.12 ? 361 GLN A O 1 ATOM 2123 C CB . GLN A 1 273 ? 22.315 -0.275 25.609 1.00 16.46 ? 361 GLN A CB 1 ATOM 2124 C CG . GLN A 1 273 ? 21.182 0.238 24.747 1.00 15.23 ? 361 GLN A CG 1 ATOM 2125 C CD . GLN A 1 273 ? 21.004 -0.590 23.503 1.00 14.66 ? 361 GLN A CD 1 ATOM 2126 O OE1 . GLN A 1 273 ? 21.926 -1.276 23.091 1.00 15.83 ? 361 GLN A OE1 1 ATOM 2127 N NE2 . GLN A 1 273 ? 19.821 -0.560 22.920 1.00 10.82 ? 361 GLN A NE2 1 ATOM 2128 N N . PRO A 1 274 ? 24.103 -2.841 26.729 1.00 17.18 ? 362 PRO A N 1 ATOM 2129 C CA . PRO A 1 274 ? 23.895 -3.627 25.508 1.00 16.66 ? 362 PRO A CA 1 ATOM 2130 C C . PRO A 1 274 ? 22.745 -4.565 25.673 1.00 16.20 ? 362 PRO A C 1 ATOM 2131 O O . PRO A 1 274 ? 22.329 -4.770 26.803 1.00 15.44 ? 362 PRO A O 1 ATOM 2132 C CB . PRO A 1 274 ? 25.149 -4.504 25.421 1.00 17.49 ? 362 PRO A CB 1 ATOM 2133 C CG . PRO A 1 274 ? 26.137 -3.918 26.379 1.00 18.19 ? 362 PRO A CG 1 ATOM 2134 C CD . PRO A 1 274 ? 25.367 -3.177 27.409 1.00 18.85 ? 362 PRO A CD 1 ATOM 2135 N N . THR A 1 275 ? 22.226 -5.112 24.572 1.00 15.97 ? 363 THR A N 1 ATOM 2136 C CA . THR A 1 275 ? 21.182 -6.149 24.640 1.00 16.21 ? 363 THR A CA 1 ATOM 2137 C C . THR A 1 275 ? 21.799 -7.496 24.973 1.00 17.57 ? 363 THR A C 1 ATOM 2138 O O . THR A 1 275 ? 22.993 -7.592 25.249 1.00 18.12 ? 363 THR A O 1 ATOM 2139 C CB . THR A 1 275 ? 20.474 -6.337 23.296 1.00 15.49 ? 363 THR A CB 1 ATOM 2140 O OG1 . THR A 1 275 ? 21.389 -6.919 22.367 1.00 14.49 ? 363 THR A OG1 1 ATOM 2141 C CG2 . THR A 1 275 ? 20.120 -4.991 22.649 1.00 13.94 ? 363 THR A CG2 1 ATOM 2142 N N . GLY A 1 276 ? 20.988 -8.548 24.894 1.00 17.80 ? 364 GLY A N 1 ATOM 2143 C CA . GLY A 1 276 ? 21.458 -9.878 25.170 1.00 18.32 ? 364 GLY A CA 1 ATOM 2144 C C . GLY A 1 276 ? 21.750 -10.613 23.882 1.00 18.14 ? 364 GLY A C 1 ATOM 2145 O O . GLY A 1 276 ? 21.867 -11.857 23.873 1.00 18.81 ? 364 GLY A O 1 ATOM 2146 N N . GLN A 1 277 ? 21.843 -9.880 22.782 1.00 18.30 ? 365 GLN A N 1 ATOM 2147 C CA . GLN A 1 277 ? 22.169 -10.485 21.520 1.00 18.71 ? 365 GLN A CA 1 ATOM 2148 C C . GLN A 1 277 ? 23.622 -10.986 21.567 1.00 19.17 ? 365 GLN A C 1 ATOM 2149 O O . GLN A 1 277 ? 24.526 -10.273 22.007 1.00 19.02 ? 365 GLN A O 1 ATOM 2150 C CB . GLN A 1 277 ? 22.039 -9.478 20.359 1.00 18.82 ? 365 GLN A CB 1 ATOM 2151 C CG . GLN A 1 277 ? 20.653 -8.925 20.098 1.00 17.81 ? 365 GLN A CG 1 ATOM 2152 C CD . GLN A 1 277 ? 20.674 -7.676 19.228 1.00 15.44 ? 365 GLN A CD 1 ATOM 2153 O OE1 . GLN A 1 277 ? 21.004 -6.592 19.705 1.00 15.53 ? 365 GLN A OE1 1 ATOM 2154 N NE2 . GLN A 1 277 ? 20.287 -7.815 17.980 1.00 17.07 ? 365 GLN A NE2 1 ATOM 2155 N N . LYS A 1 278 ? 23.829 -12.206 21.109 1.00 19.45 ? 366 LYS A N 1 ATOM 2156 C CA . LYS A 1 278 ? 25.166 -12.769 21.019 1.00 20.28 ? 366 LYS A CA 1 ATOM 2157 C C . LYS A 1 278 ? 25.898 -12.268 19.797 1.00 19.78 ? 366 LYS A C 1 ATOM 2158 O O . LYS A 1 278 ? 27.128 -12.157 19.805 1.00 17.98 ? 366 LYS A O 1 ATOM 2159 C CB . LYS A 1 278 ? 25.050 -14.282 20.965 1.00 21.76 ? 366 LYS A CB 1 ATOM 2160 C CG . LYS A 1 278 ? 24.312 -14.824 22.173 1.00 26.63 ? 366 LYS A CG 1 ATOM 2161 C CD . LYS A 1 278 ? 25.247 -15.464 23.160 1.00 33.92 ? 366 LYS A CD 1 ATOM 2162 C CE . LYS A 1 278 ? 26.145 -14.480 23.868 1.00 36.18 ? 366 LYS A CE 1 ATOM 2163 N NZ . LYS A 1 278 ? 25.674 -14.224 25.251 1.00 39.41 ? 366 LYS A NZ 1 ATOM 2164 N N . GLU A 1 279 ? 25.144 -12.003 18.733 1.00 19.09 ? 367 GLU A N 1 ATOM 2165 C CA . GLU A 1 279 ? 25.685 -11.426 17.511 1.00 20.04 ? 367 GLU A CA 1 ATOM 2166 C C . GLU A 1 279 ? 24.702 -10.366 17.057 1.00 18.65 ? 367 GLU A C 1 ATOM 2167 O O . GLU A 1 279 ? 23.512 -10.509 17.285 1.00 17.33 ? 367 GLU A O 1 ATOM 2168 C CB . GLU A 1 279 ? 25.845 -12.489 16.424 1.00 21.16 ? 367 GLU A CB 1 ATOM 2169 C CG . GLU A 1 279 ? 26.659 -13.714 16.833 1.00 25.86 ? 367 GLU A CG 1 ATOM 2170 C CD . GLU A 1 279 ? 28.169 -13.508 16.779 1.00 33.09 ? 367 GLU A CD 1 ATOM 2171 O OE1 . GLU A 1 279 ? 28.626 -12.482 16.239 1.00 36.92 ? 367 GLU A OE1 1 ATOM 2172 O OE2 . GLU A 1 279 ? 28.905 -14.396 17.273 1.00 38.64 ? 367 GLU A OE2 1 ATOM 2173 N N . TRP A 1 280 ? 25.182 -9.319 16.399 1.00 16.90 ? 368 TRP A N 1 ATOM 2174 C CA . TRP A 1 280 ? 24.308 -8.195 16.024 1.00 16.86 ? 368 TRP A CA 1 ATOM 2175 C C . TRP A 1 280 ? 23.169 -8.561 15.077 1.00 16.44 ? 368 TRP A C 1 ATOM 2176 O O . TRP A 1 280 ? 22.117 -7.934 15.125 1.00 15.93 ? 368 TRP A O 1 ATOM 2177 C CB . TRP A 1 280 ? 25.142 -7.099 15.391 1.00 16.31 ? 368 TRP A CB 1 ATOM 2178 C CG . TRP A 1 280 ? 24.668 -5.713 15.568 1.00 17.05 ? 368 TRP A CG 1 ATOM 2179 C CD1 . TRP A 1 280 ? 23.529 -5.283 16.178 1.00 17.69 ? 368 TRP A CD1 1 ATOM 2180 C CD2 . TRP A 1 280 ? 25.346 -4.541 15.112 1.00 18.31 ? 368 TRP A CD2 1 ATOM 2181 N NE1 . TRP A 1 280 ? 23.450 -3.916 16.120 1.00 16.40 ? 368 TRP A NE1 1 ATOM 2182 C CE2 . TRP A 1 280 ? 24.558 -3.435 15.470 1.00 17.70 ? 368 TRP A CE2 1 ATOM 2183 C CE3 . TRP A 1 280 ? 26.558 -4.318 14.442 1.00 19.46 ? 368 TRP A CE3 1 ATOM 2184 C CZ2 . TRP A 1 280 ? 24.939 -2.126 15.194 1.00 18.10 ? 368 TRP A CZ2 1 ATOM 2185 C CZ3 . TRP A 1 280 ? 26.930 -3.022 14.159 1.00 20.15 ? 368 TRP A CZ3 1 ATOM 2186 C CH2 . TRP A 1 280 ? 26.116 -1.939 14.529 1.00 19.22 ? 368 TRP A CH2 1 ATOM 2187 N N . GLY A 1 281 ? 23.381 -9.559 14.221 1.00 15.84 ? 369 GLY A N 1 ATOM 2188 C CA . GLY A 1 281 ? 22.390 -9.952 13.236 1.00 15.87 ? 369 GLY A CA 1 ATOM 2189 C C . GLY A 1 281 ? 21.286 -10.825 13.785 1.00 15.23 ? 369 GLY A C 1 ATOM 2190 O O . GLY A 1 281 ? 20.418 -11.288 13.048 1.00 15.38 ? 369 GLY A O 1 ATOM 2191 N N . HIS A 1 282 ? 21.322 -11.052 15.094 1.00 14.83 ? 370 HIS A N 1 ATOM 2192 C CA . HIS A 1 282 ? 20.300 -11.822 15.787 1.00 14.01 ? 370 HIS A CA 1 ATOM 2193 C C . HIS A 1 282 ? 19.096 -10.958 16.069 1.00 13.15 ? 370 HIS A C 1 ATOM 2194 O O . HIS A 1 282 ? 18.979 -10.328 17.122 1.00 15.05 ? 370 HIS A O 1 ATOM 2195 C CB . HIS A 1 282 ? 20.889 -12.444 17.032 1.00 15.00 ? 370 HIS A CB 1 ATOM 2196 C CG . HIS A 1 282 ? 21.870 -13.526 16.708 1.00 14.34 ? 370 HIS A CG 1 ATOM 2197 N ND1 . HIS A 1 282 ? 22.461 -14.331 17.659 1.00 18.53 ? 370 HIS A ND1 1 ATOM 2198 C CD2 . HIS A 1 282 ? 22.375 -13.918 15.514 1.00 17.34 ? 370 HIS A CD2 1 ATOM 2199 C CE1 . HIS A 1 282 ? 23.278 -15.185 17.061 1.00 19.25 ? 370 HIS A CE1 1 ATOM 2200 N NE2 . HIS A 1 282 ? 23.254 -14.947 15.759 1.00 18.08 ? 370 HIS A NE2 1 ATOM 2201 N N . TRP A 1 283 ? 18.190 -10.936 15.095 1.00 13.03 ? 371 TRP A N 1 ATOM 2202 C CA . TRP A 1 283 ? 17.036 -10.042 15.107 1.00 11.92 ? 371 TRP A CA 1 ATOM 2203 C C . TRP A 1 283 ? 15.719 -10.503 15.744 1.00 12.21 ? 371 TRP A C 1 ATOM 2204 O O . TRP A 1 283 ? 14.844 -9.670 15.941 1.00 13.44 ? 371 TRP A O 1 ATOM 2205 C CB . TRP A 1 283 ? 16.718 -9.662 13.655 1.00 11.88 ? 371 TRP A CB 1 ATOM 2206 C CG . TRP A 1 283 ? 16.404 -10.824 12.773 1.00 11.90 ? 371 TRP A CG 1 ATOM 2207 C CD1 . TRP A 1 283 ? 17.267 -11.511 11.955 1.00 13.42 ? 371 TRP A CD1 1 ATOM 2208 C CD2 . TRP A 1 283 ? 15.129 -11.441 12.599 1.00 13.03 ? 371 TRP A CD2 1 ATOM 2209 N NE1 . TRP A 1 283 ? 16.598 -12.525 11.303 1.00 13.42 ? 371 TRP A NE1 1 ATOM 2210 C CE2 . TRP A 1 283 ? 15.288 -12.509 11.690 1.00 13.49 ? 371 TRP A CE2 1 ATOM 2211 C CE3 . TRP A 1 283 ? 13.870 -11.217 13.139 1.00 12.80 ? 371 TRP A CE3 1 ATOM 2212 C CZ2 . TRP A 1 283 ? 14.220 -13.313 11.284 1.00 14.87 ? 371 TRP A CZ2 1 ATOM 2213 C CZ3 . TRP A 1 283 ? 12.829 -12.019 12.758 1.00 10.55 ? 371 TRP A CZ3 1 ATOM 2214 C CH2 . TRP A 1 283 ? 13.005 -13.057 11.836 1.00 14.73 ? 371 TRP A CH2 1 ATOM 2215 N N . CYS A 1 284 ? 15.564 -11.792 16.045 1.00 12.42 ? 372 CYS A N 1 ATOM 2216 C CA . CYS A 1 284 ? 14.289 -12.320 16.456 1.00 13.56 ? 372 CYS A CA 1 ATOM 2217 C C . CYS A 1 284 ? 14.065 -12.488 17.976 1.00 13.31 ? 372 CYS A C 1 ATOM 2218 O O . CYS A 1 284 ? 14.814 -13.201 18.648 1.00 14.35 ? 372 CYS A O 1 ATOM 2219 C CB . CYS A 1 284 ? 14.092 -13.655 15.754 1.00 13.93 ? 372 CYS A CB 1 ATOM 2220 S SG . CYS A 1 284 ? 12.440 -14.302 15.959 1.00 15.51 ? 372 CYS A SG 1 ATOM 2221 N N . ASN A 1 285 ? 13.040 -11.818 18.501 1.00 13.39 ? 373 ASN A N 1 ATOM 2222 C CA . ASN A 1 285 ? 12.670 -11.964 19.897 1.00 13.31 ? 373 ASN A CA 1 ATOM 2223 C C . ASN A 1 285 ? 13.877 -11.947 20.820 1.00 13.25 ? 373 ASN A C 1 ATOM 2224 O O . ASN A 1 285 ? 14.051 -12.803 21.678 1.00 13.08 ? 373 ASN A O 1 ATOM 2225 C CB . ASN A 1 285 ? 11.876 -13.260 20.050 1.00 12.42 ? 373 ASN A CB 1 ATOM 2226 C CG . ASN A 1 285 ? 10.669 -13.300 19.152 1.00 12.49 ? 373 ASN A CG 1 ATOM 2227 O OD1 . ASN A 1 285 ? 10.020 -12.269 18.902 1.00 10.87 ? 373 ASN A OD1 1 ATOM 2228 N ND2 . ASN A 1 285 ? 10.346 -14.480 18.650 1.00 13.11 ? 373 ASN A ND2 1 ATOM 2229 N N . ALA A 1 286 ? 14.720 -10.942 20.663 1.00 14.06 ? 374 ALA A N 1 ATOM 2230 C CA . ALA A 1 286 ? 15.984 -10.948 21.375 1.00 13.64 ? 374 ALA A CA 1 ATOM 2231 C C . ALA A 1 286 ? 15.810 -10.808 22.892 1.00 12.83 ? 374 ALA A C 1 ATOM 2232 O O . ALA A 1 286 ? 14.943 -10.094 23.369 1.00 12.83 ? 374 ALA A O 1 ATOM 2233 C CB . ALA A 1 286 ? 16.921 -9.848 20.808 1.00 13.98 ? 374 ALA A CB 1 ATOM 2234 N N . ILE A 1 287 ? 16.597 -11.571 23.642 1.00 13.43 ? 375 ILE A N 1 ATOM 2235 C CA . ILE A 1 287 ? 16.559 -11.495 25.096 1.00 14.42 ? 375 ILE A CA 1 ATOM 2236 C C . ILE A 1 287 ? 17.345 -10.291 25.544 1.00 14.17 ? 375 ILE A C 1 ATOM 2237 O O . ILE A 1 287 ? 18.158 -9.761 24.788 1.00 14.13 ? 375 ILE A O 1 ATOM 2238 C CB . ILE A 1 287 ? 17.145 -12.776 25.742 1.00 15.03 ? 375 ILE A CB 1 ATOM 2239 C CG1 . ILE A 1 287 ? 18.605 -13.001 25.344 1.00 17.81 ? 375 ILE A CG1 1 ATOM 2240 C CG2 . ILE A 1 287 ? 16.279 -13.990 25.384 1.00 16.05 ? 375 ILE A CG2 1 ATOM 2241 C CD1 . ILE A 1 287 ? 19.292 -14.162 26.099 1.00 19.61 ? 375 ILE A CD1 1 ATOM 2242 N N . GLY A 1 288 ? 17.074 -9.837 26.759 1.00 13.60 ? 376 GLY A N 1 ATOM 2243 C CA . GLY A 1 288 ? 17.823 -8.775 27.379 1.00 13.89 ? 376 GLY A CA 1 ATOM 2244 C C . GLY A 1 288 ? 17.541 -7.399 26.807 1.00 13.27 ? 376 GLY A C 1 ATOM 2245 O O . GLY A 1 288 ? 18.438 -6.581 26.749 1.00 13.59 ? 376 GLY A O 1 ATOM 2246 N N . THR A 1 289 ? 16.314 -7.174 26.358 1.00 12.68 ? 377 THR A N 1 ATOM 2247 C CA . THR A 1 289 ? 15.919 -5.923 25.784 1.00 12.09 ? 377 THR A CA 1 ATOM 2248 C C . THR A 1 289 ? 14.807 -5.353 26.654 1.00 12.65 ? 377 THR A C 1 ATOM 2249 O O . THR A 1 289 ? 14.183 -6.085 27.433 1.00 12.16 ? 377 THR A O 1 ATOM 2250 C CB . THR A 1 289 ? 15.412 -6.114 24.360 1.00 13.22 ? 377 THR A CB 1 ATOM 2251 O OG1 . THR A 1 289 ? 14.241 -6.932 24.365 1.00 9.91 ? 377 THR A OG1 1 ATOM 2252 C CG2 . THR A 1 289 ? 16.434 -6.815 23.486 1.00 12.45 ? 377 THR A CG2 1 ATOM 2253 N N . GLY A 1 290 ? 14.576 -4.050 26.510 1.00 11.43 ? 378 GLY A N 1 ATOM 2254 C CA . GLY A 1 290 ? 13.605 -3.314 27.299 1.00 11.47 ? 378 GLY A CA 1 ATOM 2255 C C . GLY A 1 290 ? 12.957 -2.205 26.492 1.00 11.72 ? 378 GLY A C 1 ATOM 2256 O O . GLY A 1 290 ? 13.495 -1.774 25.495 1.00 10.77 ? 378 GLY A O 1 ATOM 2257 N N . PHE A 1 291 ? 11.774 -1.769 26.909 1.00 13.09 ? 379 PHE A N 1 ATOM 2258 C CA . PHE A 1 291 ? 11.157 -0.614 26.311 1.00 13.59 ? 379 PHE A CA 1 ATOM 2259 C C . PHE A 1 291 ? 12.138 0.548 26.408 1.00 13.36 ? 379 PHE A C 1 ATOM 2260 O O . PHE A 1 291 ? 12.787 0.711 27.437 1.00 13.97 ? 379 PHE A O 1 ATOM 2261 C CB . PHE A 1 291 ? 9.881 -0.281 27.060 1.00 14.03 ? 379 PHE A CB 1 ATOM 2262 C CG . PHE A 1 291 ? 8.756 -1.194 26.746 1.00 15.24 ? 379 PHE A CG 1 ATOM 2263 C CD1 . PHE A 1 291 ? 8.258 -1.258 25.458 1.00 16.02 ? 379 PHE A CD1 1 ATOM 2264 C CD2 . PHE A 1 291 ? 8.195 -2.000 27.711 1.00 17.41 ? 379 PHE A CD2 1 ATOM 2265 C CE1 . PHE A 1 291 ? 7.217 -2.121 25.143 1.00 14.99 ? 379 PHE A CE1 1 ATOM 2266 C CE2 . PHE A 1 291 ? 7.114 -2.839 27.407 1.00 15.92 ? 379 PHE A CE2 1 ATOM 2267 C CZ . PHE A 1 291 ? 6.638 -2.902 26.125 1.00 15.01 ? 379 PHE A CZ 1 ATOM 2268 N N . GLY A 1 292 ? 12.199 1.398 25.382 1.00 13.97 ? 380 GLY A N 1 ATOM 2269 C CA . GLY A 1 292 ? 13.175 2.463 25.356 1.00 14.53 ? 380 GLY A CA 1 ATOM 2270 C C . GLY A 1 292 ? 12.563 3.835 25.466 1.00 15.36 ? 380 GLY A C 1 ATOM 2271 O O . GLY A 1 292 ? 11.429 4.012 25.906 1.00 15.74 ? 380 GLY A O 1 ATOM 2272 N N . MET A 1 293 ? 13.324 4.829 25.054 1.00 16.34 ? 381 MET A N 1 ATOM 2273 C CA . MET A 1 293 ? 12.837 6.182 25.193 1.00 16.85 ? 381 MET A CA 1 ATOM 2274 C C . MET A 1 293 ? 11.482 6.389 24.546 1.00 16.80 ? 381 MET A C 1 ATOM 2275 O O . MET A 1 293 ? 11.200 5.825 23.476 1.00 15.64 ? 381 MET A O 1 ATOM 2276 C CB . MET A 1 293 ? 13.822 7.179 24.652 1.00 18.21 ? 381 MET A CB 1 ATOM 2277 C CG . MET A 1 293 ? 14.392 6.912 23.312 1.00 21.69 ? 381 MET A CG 1 ATOM 2278 S SD . MET A 1 293 ? 15.547 8.256 22.674 1.00 30.36 ? 381 MET A SD 1 ATOM 2279 C CE . MET A 1 293 ? 16.727 8.322 23.971 1.00 29.67 ? 381 MET A CE 1 ATOM 2280 N N . ARG A 1 294 ? 10.656 7.192 25.211 1.00 16.46 ? 382 ARG A N 1 ATOM 2281 C CA . ARG A 1 294 ? 9.295 7.410 24.770 1.00 16.48 ? 382 ARG A CA 1 ATOM 2282 C C . ARG A 1 294 ? 9.278 8.316 23.536 1.00 15.55 ? 382 ARG A C 1 ATOM 2283 O O . ARG A 1 294 ? 10.090 9.223 23.406 1.00 16.01 ? 382 ARG A O 1 ATOM 2284 C CB . ARG A 1 294 ? 8.495 8.085 25.894 1.00 16.49 ? 382 ARG A CB 1 ATOM 2285 C CG . ARG A 1 294 ? 8.727 7.467 27.267 1.00 19.43 ? 382 ARG A CG 1 ATOM 2286 C CD . ARG A 1 294 ? 8.158 6.067 27.419 1.00 22.04 ? 382 ARG A CD 1 ATOM 2287 N NE . ARG A 1 294 ? 8.073 5.738 28.841 1.00 27.21 ? 382 ARG A NE 1 ATOM 2288 C CZ . ARG A 1 294 ? 9.001 5.073 29.499 1.00 25.03 ? 382 ARG A CZ 1 ATOM 2289 N NH1 . ARG A 1 294 ? 10.068 4.638 28.848 1.00 25.21 ? 382 ARG A NH1 1 ATOM 2290 N NH2 . ARG A 1 294 ? 8.863 4.835 30.801 1.00 24.96 ? 382 ARG A NH2 1 ATOM 2291 N N . PRO A 1 295 ? 8.325 8.089 22.645 1.00 15.58 ? 383 PRO A N 1 ATOM 2292 C CA . PRO A 1 295 ? 8.194 8.881 21.431 1.00 15.06 ? 383 PRO A CA 1 ATOM 2293 C C . PRO A 1 295 ? 8.155 10.372 21.698 1.00 16.25 ? 383 PRO A C 1 ATOM 2294 O O . PRO A 1 295 ? 7.470 10.830 22.630 1.00 15.57 ? 383 PRO A O 1 ATOM 2295 C CB . PRO A 1 295 ? 6.886 8.372 20.843 1.00 14.78 ? 383 PRO A CB 1 ATOM 2296 C CG . PRO A 1 295 ? 6.816 6.989 21.295 1.00 15.23 ? 383 PRO A CG 1 ATOM 2297 C CD . PRO A 1 295 ? 7.331 7.006 22.685 1.00 15.03 ? 383 PRO A CD 1 ATOM 2298 N N . THR A 1 296 ? 8.908 11.121 20.901 1.00 15.63 ? 384 THR A N 1 ATOM 2299 C CA . THR A 1 296 ? 8.946 12.554 21.058 1.00 16.74 ? 384 THR A CA 1 ATOM 2300 C C . THR A 1 296 ? 9.546 13.236 19.837 1.00 16.48 ? 384 THR A C 1 ATOM 2301 O O . THR A 1 296 ? 10.390 12.681 19.145 1.00 15.03 ? 384 THR A O 1 ATOM 2302 C CB . THR A 1 296 ? 9.769 12.895 22.309 1.00 16.92 ? 384 THR A CB 1 ATOM 2303 O OG1 . THR A 1 296 ? 9.851 14.306 22.474 1.00 17.53 ? 384 THR A OG1 1 ATOM 2304 C CG2 . THR A 1 296 ? 11.243 12.474 22.142 1.00 18.20 ? 384 THR A CG2 1 ATOM 2305 N N . ALA A 1 297 ? 9.101 14.452 19.550 1.00 16.82 ? 385 ALA A N 1 ATOM 2306 C CA . ALA A 1 297 ? 9.741 15.182 18.472 1.00 17.63 ? 385 ALA A CA 1 ATOM 2307 C C . ALA A 1 297 ? 10.959 15.918 19.001 1.00 18.54 ? 385 ALA A C 1 ATOM 2308 O O . ALA A 1 297 ? 11.717 16.467 18.223 1.00 19.22 ? 385 ALA A O 1 ATOM 2309 C CB . ALA A 1 297 ? 8.752 16.181 17.809 1.00 17.50 ? 385 ALA A CB 1 ATOM 2310 N N . ASN A 1 298 ? 11.158 15.944 20.319 1.00 19.35 ? 386 ASN A N 1 ATOM 2311 C CA . ASN A 1 298 ? 12.247 16.783 20.866 1.00 20.37 ? 386 ASN A CA 1 ATOM 2312 C C . ASN A 1 298 ? 13.511 15.963 20.949 1.00 19.80 ? 386 ASN A C 1 ATOM 2313 O O . ASN A 1 298 ? 13.931 15.552 22.034 1.00 21.45 ? 386 ASN A O 1 ATOM 2314 C CB . ASN A 1 298 ? 11.891 17.343 22.248 1.00 20.52 ? 386 ASN A CB 1 ATOM 2315 C CG . ASN A 1 298 ? 10.508 17.930 22.292 1.00 23.10 ? 386 ASN A CG 1 ATOM 2316 O OD1 . ASN A 1 298 ? 10.205 18.864 21.552 1.00 26.34 ? 386 ASN A OD1 1 ATOM 2317 N ND2 . ASN A 1 298 ? 9.648 17.383 23.157 1.00 27.43 ? 386 ASN A ND2 1 ATOM 2318 N N . THR A 1 299 ? 14.111 15.709 19.808 1.00 19.61 ? 387 THR A N 1 ATOM 2319 C CA . THR A 1 299 ? 15.222 14.774 19.734 1.00 19.28 ? 387 THR A CA 1 ATOM 2320 C C . THR A 1 299 ? 16.551 15.418 20.059 1.00 20.32 ? 387 THR A C 1 ATOM 2321 O O . THR A 1 299 ? 17.512 14.740 20.356 1.00 19.62 ? 387 THR A O 1 ATOM 2322 C CB . THR A 1 299 ? 15.365 14.228 18.333 1.00 19.66 ? 387 THR A CB 1 ATOM 2323 O OG1 . THR A 1 299 ? 15.571 15.325 17.441 1.00 18.51 ? 387 THR A OG1 1 ATOM 2324 C CG2 . THR A 1 299 ? 14.103 13.501 17.861 1.00 18.66 ? 387 THR A CG2 1 ATOM 2325 N N . GLY A 1 300 ? 16.623 16.729 19.922 1.00 20.55 ? 388 GLY A N 1 ATOM 2326 C CA . GLY A 1 300 ? 17.870 17.397 20.155 1.00 21.65 ? 388 GLY A CA 1 ATOM 2327 C C . GLY A 1 300 ? 18.778 17.252 18.950 1.00 21.73 ? 388 GLY A C 1 ATOM 2328 O O . GLY A 1 300 ? 19.901 17.681 18.999 1.00 22.89 ? 388 GLY A O 1 ATOM 2329 N N . HIS A 1 301 ? 18.307 16.642 17.864 1.00 21.28 ? 389 HIS A N 1 ATOM 2330 C CA . HIS A 1 301 ? 19.163 16.442 16.700 1.00 19.60 ? 389 HIS A CA 1 ATOM 2331 C C . HIS A 1 301 ? 18.576 16.992 15.404 1.00 20.64 ? 389 HIS A C 1 ATOM 2332 O O . HIS A 1 301 ? 17.453 16.646 15.017 1.00 19.58 ? 389 HIS A O 1 ATOM 2333 C CB . HIS A 1 301 ? 19.476 14.960 16.518 1.00 20.57 ? 389 HIS A CB 1 ATOM 2334 C CG . HIS A 1 301 ? 20.679 14.717 15.671 1.00 18.31 ? 389 HIS A CG 1 ATOM 2335 N ND1 . HIS A 1 301 ? 20.702 15.005 14.327 1.00 19.58 ? 389 HIS A ND1 1 ATOM 2336 C CD2 . HIS A 1 301 ? 21.927 14.290 15.988 1.00 19.14 ? 389 HIS A CD2 1 ATOM 2337 C CE1 . HIS A 1 301 ? 21.897 14.737 13.838 1.00 20.26 ? 389 HIS A CE1 1 ATOM 2338 N NE2 . HIS A 1 301 ? 22.660 14.293 14.823 1.00 20.76 ? 389 HIS A NE2 1 ATOM 2339 N N . GLN A 1 302 ? 19.378 17.789 14.700 1.00 20.17 ? 390 GLN A N 1 ATOM 2340 C CA . GLN A 1 302 ? 18.943 18.429 13.467 1.00 21.25 ? 390 GLN A CA 1 ATOM 2341 C C . GLN A 1 302 ? 18.415 17.474 12.379 1.00 19.64 ? 390 GLN A C 1 ATOM 2342 O O . GLN A 1 302 ? 17.547 17.849 11.605 1.00 19.79 ? 390 GLN A O 1 ATOM 2343 C CB . GLN A 1 302 ? 20.101 19.274 12.942 1.00 21.86 ? 390 GLN A CB 1 ATOM 2344 C CG A GLN A 1 302 ? 21.227 18.573 12.229 0.50 23.07 ? 390 GLN A CG 1 ATOM 2345 C CG B GLN A 1 302 ? 20.070 19.524 11.455 0.50 23.96 ? 390 GLN A CG 1 ATOM 2346 C CD A GLN A 1 302 ? 22.331 19.452 11.683 0.50 26.95 ? 390 GLN A CD 1 ATOM 2347 C CD B GLN A 1 302 ? 20.979 20.655 11.013 0.50 27.01 ? 390 GLN A CD 1 ATOM 2348 O OE1 A GLN A 1 302 ? 23.520 19.133 11.852 0.50 28.21 ? 390 GLN A OE1 1 ATOM 2349 O OE1 B GLN A 1 302 ? 22.202 20.491 10.968 0.50 30.03 ? 390 GLN A OE1 1 ATOM 2350 N NE2 A GLN A 1 302 ? 21.958 20.510 10.976 0.50 29.81 ? 390 GLN A NE2 1 ATOM 2351 N NE2 B GLN A 1 302 ? 20.389 21.794 10.671 0.50 27.39 ? 390 GLN A NE2 1 ATOM 2352 N N . TYR A 1 303 ? 18.920 16.249 12.325 1.00 18.27 ? 391 TYR A N 1 ATOM 2353 C CA . TYR A 1 303 ? 18.553 15.329 11.250 1.00 17.76 ? 391 TYR A CA 1 ATOM 2354 C C . TYR A 1 303 ? 17.440 14.338 11.666 1.00 17.41 ? 391 TYR A C 1 ATOM 2355 O O . TYR A 1 303 ? 16.985 13.528 10.840 1.00 17.57 ? 391 TYR A O 1 ATOM 2356 C CB . TYR A 1 303 ? 19.781 14.559 10.774 1.00 17.71 ? 391 TYR A CB 1 ATOM 2357 C CG . TYR A 1 303 ? 20.923 15.390 10.185 1.00 20.43 ? 391 TYR A CG 1 ATOM 2358 C CD1 . TYR A 1 303 ? 20.686 16.576 9.489 1.00 23.22 ? 391 TYR A CD1 1 ATOM 2359 C CD2 . TYR A 1 303 ? 22.239 14.956 10.285 1.00 23.53 ? 391 TYR A CD2 1 ATOM 2360 C CE1 . TYR A 1 303 ? 21.731 17.304 8.935 1.00 23.96 ? 391 TYR A CE1 1 ATOM 2361 C CE2 . TYR A 1 303 ? 23.289 15.694 9.734 1.00 25.46 ? 391 TYR A CE2 1 ATOM 2362 C CZ . TYR A 1 303 ? 23.026 16.855 9.071 1.00 26.99 ? 391 TYR A CZ 1 ATOM 2363 O OH . TYR A 1 303 ? 24.080 17.567 8.529 1.00 31.68 ? 391 TYR A OH 1 ATOM 2364 N N . VAL A 1 304 ? 16.992 14.419 12.919 1.00 15.95 ? 392 VAL A N 1 ATOM 2365 C CA . VAL A 1 304 ? 16.026 13.465 13.472 1.00 15.24 ? 392 VAL A CA 1 ATOM 2366 C C . VAL A 1 304 ? 14.735 14.150 13.884 1.00 15.21 ? 392 VAL A C 1 ATOM 2367 O O . VAL A 1 304 ? 14.688 14.931 14.880 1.00 14.67 ? 392 VAL A O 1 ATOM 2368 C CB . VAL A 1 304 ? 16.621 12.738 14.676 1.00 15.07 ? 392 VAL A CB 1 ATOM 2369 C CG1 . VAL A 1 304 ? 15.711 11.579 15.104 1.00 14.97 ? 392 VAL A CG1 1 ATOM 2370 C CG2 . VAL A 1 304 ? 18.020 12.184 14.320 1.00 14.26 ? 392 VAL A CG2 1 ATOM 2371 N N . ASP A 1 305 ? 13.675 13.887 13.106 1.00 13.97 ? 393 ASP A N 1 ATOM 2372 C CA . ASP A 1 305 ? 12.384 14.452 13.393 1.00 13.58 ? 393 ASP A CA 1 ATOM 2373 C C . ASP A 1 305 ? 11.788 13.932 14.681 1.00 13.73 ? 393 ASP A C 1 ATOM 2374 O O . ASP A 1 305 ? 11.053 14.651 15.338 1.00 13.38 ? 393 ASP A O 1 ATOM 2375 C CB . ASP A 1 305 ? 11.393 14.171 12.269 1.00 14.32 ? 393 ASP A CB 1 ATOM 2376 C CG . ASP A 1 305 ? 11.663 14.999 10.999 1.00 15.62 ? 393 ASP A CG 1 ATOM 2377 O OD1 . ASP A 1 305 ? 12.386 16.032 11.053 1.00 16.38 ? 393 ASP A OD1 1 ATOM 2378 O OD2 . ASP A 1 305 ? 11.172 14.687 9.901 1.00 13.91 ? 393 ASP A OD2 1 ATOM 2379 N N . ALA A 1 306 ? 12.034 12.666 15.006 1.00 13.09 ? 394 ALA A N 1 ATOM 2380 C CA . ALA A 1 306 ? 11.428 12.075 16.182 1.00 13.13 ? 394 ALA A CA 1 ATOM 2381 C C . ALA A 1 306 ? 11.994 10.725 16.533 1.00 12.83 ? 394 ALA A C 1 ATOM 2382 O O . ALA A 1 306 ? 12.424 9.959 15.665 1.00 13.70 ? 394 ALA A O 1 ATOM 2383 C CB . ALA A 1 306 ? 9.948 11.897 15.966 1.00 12.83 ? 394 ALA A CB 1 ATOM 2384 N N . PHE A 1 307 ? 12.002 10.473 17.831 1.00 12.56 ? 395 PHE A N 1 ATOM 2385 C CA . PHE A 1 307 ? 12.188 9.138 18.365 1.00 12.39 ? 395 PHE A CA 1 ATOM 2386 C C . PHE A 1 307 ? 10.776 8.561 18.439 1.00 12.37 ? 395 PHE A C 1 ATOM 2387 O O . PHE A 1 307 ? 9.865 9.230 18.936 1.00 12.26 ? 395 PHE A O 1 ATOM 2388 C CB . PHE A 1 307 ? 12.798 9.197 19.731 1.00 12.88 ? 395 PHE A CB 1 ATOM 2389 C CG . PHE A 1 307 ? 14.188 9.775 19.726 1.00 14.97 ? 395 PHE A CG 1 ATOM 2390 C CD1 . PHE A 1 307 ? 15.073 9.401 18.743 1.00 17.23 ? 395 PHE A CD1 1 ATOM 2391 C CD2 . PHE A 1 307 ? 14.578 10.741 20.639 1.00 19.15 ? 395 PHE A CD2 1 ATOM 2392 C CE1 . PHE A 1 307 ? 16.341 9.918 18.705 1.00 17.86 ? 395 PHE A CE1 1 ATOM 2393 C CE2 . PHE A 1 307 ? 15.853 11.262 20.596 1.00 19.18 ? 395 PHE A CE2 1 ATOM 2394 C CZ . PHE A 1 307 ? 16.728 10.847 19.603 1.00 19.14 ? 395 PHE A CZ 1 ATOM 2395 N N . VAL A 1 308 ? 10.611 7.344 17.925 1.00 11.19 ? 396 VAL A N 1 ATOM 2396 C CA . VAL A 1 308 ? 9.311 6.705 17.821 1.00 11.09 ? 396 VAL A CA 1 ATOM 2397 C C . VAL A 1 308 ? 9.320 5.256 18.296 1.00 10.93 ? 396 VAL A C 1 ATOM 2398 O O . VAL A 1 308 ? 10.362 4.669 18.582 1.00 11.17 ? 396 VAL A O 1 ATOM 2399 C CB . VAL A 1 308 ? 8.835 6.726 16.352 1.00 10.07 ? 396 VAL A CB 1 ATOM 2400 C CG1 . VAL A 1 308 ? 8.463 8.129 15.915 1.00 10.39 ? 396 VAL A CG1 1 ATOM 2401 C CG2 . VAL A 1 308 ? 9.899 6.153 15.447 1.00 9.66 ? 396 VAL A CG2 1 ATOM 2402 N N . TRP A 1 309 ? 8.127 4.696 18.404 1.00 10.25 ? 397 TRP A N 1 ATOM 2403 C CA . TRP A 1 309 ? 7.983 3.283 18.626 1.00 10.19 ? 397 TRP A CA 1 ATOM 2404 C C . TRP A 1 309 ? 7.289 2.719 17.373 1.00 10.42 ? 397 TRP A C 1 ATOM 2405 O O . TRP A 1 309 ? 6.085 2.900 17.199 1.00 10.68 ? 397 TRP A O 1 ATOM 2406 C CB . TRP A 1 309 ? 7.161 3.005 19.858 1.00 10.89 ? 397 TRP A CB 1 ATOM 2407 C CG . TRP A 1 309 ? 7.864 3.196 21.097 1.00 9.69 ? 397 TRP A CG 1 ATOM 2408 C CD1 . TRP A 1 309 ? 9.007 3.903 21.318 1.00 9.06 ? 397 TRP A CD1 1 ATOM 2409 C CD2 . TRP A 1 309 ? 7.495 2.622 22.337 1.00 12.35 ? 397 TRP A CD2 1 ATOM 2410 N NE1 . TRP A 1 309 ? 9.350 3.829 22.651 1.00 13.86 ? 397 TRP A NE1 1 ATOM 2411 C CE2 . TRP A 1 309 ? 8.423 3.064 23.299 1.00 13.45 ? 397 TRP A CE2 1 ATOM 2412 C CE3 . TRP A 1 309 ? 6.421 1.825 22.751 1.00 12.57 ? 397 TRP A CE3 1 ATOM 2413 C CZ2 . TRP A 1 309 ? 8.346 2.702 24.637 1.00 14.30 ? 397 TRP A CZ2 1 ATOM 2414 C CZ3 . TRP A 1 309 ? 6.347 1.451 24.088 1.00 12.89 ? 397 TRP A CZ3 1 ATOM 2415 C CH2 . TRP A 1 309 ? 7.297 1.918 25.019 1.00 13.39 ? 397 TRP A CH2 1 ATOM 2416 N N . VAL A 1 310 ? 8.050 2.093 16.474 1.00 10.18 ? 398 VAL A N 1 ATOM 2417 C CA . VAL A 1 310 ? 7.470 1.546 15.263 1.00 9.58 ? 398 VAL A CA 1 ATOM 2418 C C . VAL A 1 310 ? 6.992 0.109 15.504 1.00 10.52 ? 398 VAL A C 1 ATOM 2419 O O . VAL A 1 310 ? 5.824 -0.165 15.392 1.00 11.43 ? 398 VAL A O 1 ATOM 2420 C CB . VAL A 1 310 ? 8.390 1.664 14.039 1.00 8.77 ? 398 VAL A CB 1 ATOM 2421 C CG1 . VAL A 1 310 ? 7.619 1.328 12.810 1.00 8.42 ? 398 VAL A CG1 1 ATOM 2422 C CG2 . VAL A 1 310 ? 8.910 3.071 13.923 1.00 10.04 ? 398 VAL A CG2 1 ATOM 2423 N N . LYS A 1 311 ? 7.891 -0.783 15.888 1.00 10.97 ? 399 LYS A N 1 ATOM 2424 C CA . LYS A 1 311 ? 7.540 -2.148 16.181 1.00 11.22 ? 399 LYS A CA 1 ATOM 2425 C C . LYS A 1 311 ? 6.884 -2.112 17.563 1.00 11.45 ? 399 LYS A C 1 ATOM 2426 O O . LYS A 1 311 ? 7.487 -1.572 18.478 1.00 11.89 ? 399 LYS A O 1 ATOM 2427 C CB . LYS A 1 311 ? 8.805 -2.994 16.167 1.00 10.74 ? 399 LYS A CB 1 ATOM 2428 C CG . LYS A 1 311 ? 8.641 -4.390 16.764 1.00 11.19 ? 399 LYS A CG 1 ATOM 2429 C CD . LYS A 1 311 ? 7.705 -5.254 15.956 1.00 10.34 ? 399 LYS A CD 1 ATOM 2430 C CE . LYS A 1 311 ? 7.486 -6.614 16.623 1.00 9.92 ? 399 LYS A CE 1 ATOM 2431 N NZ . LYS A 1 311 ? 6.772 -7.603 15.756 1.00 10.61 ? 399 LYS A NZ 1 ATOM 2432 N N . PRO A 1 312 ? 5.648 -2.589 17.734 1.00 11.46 ? 400 PRO A N 1 ATOM 2433 C CA . PRO A 1 312 ? 5.041 -2.546 19.061 1.00 12.90 ? 400 PRO A CA 1 ATOM 2434 C C . PRO A 1 312 ? 5.523 -3.662 19.964 1.00 12.93 ? 400 PRO A C 1 ATOM 2435 O O . PRO A 1 312 ? 5.231 -4.809 19.736 1.00 14.37 ? 400 PRO A O 1 ATOM 2436 C CB . PRO A 1 312 ? 3.533 -2.667 18.758 1.00 12.60 ? 400 PRO A CB 1 ATOM 2437 C CG . PRO A 1 312 ? 3.430 -2.346 17.246 1.00 11.25 ? 400 PRO A CG 1 ATOM 2438 C CD . PRO A 1 312 ? 4.672 -3.063 16.735 1.00 11.66 ? 400 PRO A CD 1 ATOM 2439 N N . GLY A 1 313 ? 6.228 -3.315 21.021 1.00 14.52 ? 401 GLY A N 1 ATOM 2440 C CA . GLY A 1 313 ? 6.846 -4.327 21.861 1.00 13.67 ? 401 GLY A CA 1 ATOM 2441 C C . GLY A 1 313 ? 5.815 -5.235 22.479 1.00 13.98 ? 401 GLY A C 1 ATOM 2442 O O . GLY A 1 313 ? 4.840 -4.741 23.015 1.00 14.89 ? 401 GLY A O 1 ATOM 2443 N N . GLY A 1 314 ? 6.054 -6.538 22.393 1.00 13.11 ? 402 GLY A N 1 ATOM 2444 C CA . GLY A 1 314 ? 5.137 -7.553 22.868 1.00 13.83 ? 402 GLY A CA 1 ATOM 2445 C C . GLY A 1 314 ? 4.502 -8.294 21.707 1.00 13.66 ? 402 GLY A C 1 ATOM 2446 O O . GLY A 1 314 ? 3.962 -9.404 21.869 1.00 15.23 ? 402 GLY A O 1 ATOM 2447 N N . GLU A 1 315 ? 4.571 -7.699 20.516 1.00 12.44 ? 403 GLU A N 1 ATOM 2448 C CA . GLU A 1 315 ? 4.130 -8.383 19.308 1.00 11.98 ? 403 GLU A CA 1 ATOM 2449 C C . GLU A 1 315 ? 5.340 -9.163 18.760 1.00 12.13 ? 403 GLU A C 1 ATOM 2450 O O . GLU A 1 315 ? 6.397 -8.598 18.527 1.00 12.77 ? 403 GLU A O 1 ATOM 2451 C CB . GLU A 1 315 ? 3.549 -7.414 18.276 1.00 11.76 ? 403 GLU A CB 1 ATOM 2452 C CG . GLU A 1 315 ? 2.203 -6.832 18.696 1.00 12.49 ? 403 GLU A CG 1 ATOM 2453 C CD . GLU A 1 315 ? 1.660 -5.785 17.736 1.00 14.79 ? 403 GLU A CD 1 ATOM 2454 O OE1 . GLU A 1 315 ? 2.185 -5.624 16.573 1.00 13.63 ? 403 GLU A OE1 1 ATOM 2455 O OE2 . GLU A 1 315 ? 0.671 -5.136 18.143 1.00 14.94 ? 403 GLU A OE2 1 ATOM 2456 N N . CYS A 1 316 ? 5.156 -10.455 18.535 1.00 11.74 ? 404 CYS A N 1 ATOM 2457 C CA . CYS A 1 316 ? 6.237 -11.371 18.226 1.00 11.86 ? 404 CYS A CA 1 ATOM 2458 C C . CYS A 1 316 ? 6.968 -11.061 16.922 1.00 11.44 ? 404 CYS A C 1 ATOM 2459 O O . CYS A 1 316 ? 6.385 -10.517 15.995 1.00 10.17 ? 404 CYS A O 1 ATOM 2460 C CB . CYS A 1 316 ? 5.680 -12.787 18.096 1.00 12.09 ? 404 CYS A CB 1 ATOM 2461 S SG . CYS A 1 316 ? 6.921 -14.091 18.262 1.00 14.08 ? 404 CYS A SG 1 ATOM 2462 N N . ASP A 1 317 ? 8.214 -11.486 16.825 1.00 10.65 ? 405 ASP A N 1 ATOM 2463 C CA . ASP A 1 317 ? 8.957 -11.282 15.562 1.00 11.07 ? 405 ASP A CA 1 ATOM 2464 C C . ASP A 1 317 ? 8.878 -12.491 14.650 1.00 11.55 ? 405 ASP A C 1 ATOM 2465 O O . ASP A 1 317 ? 9.172 -12.396 13.445 1.00 10.98 ? 405 ASP A O 1 ATOM 2466 C CB . ASP A 1 317 ? 10.426 -11.027 15.847 1.00 11.14 ? 405 ASP A CB 1 ATOM 2467 C CG . ASP A 1 317 ? 10.655 -9.810 16.654 1.00 12.51 ? 405 ASP A CG 1 ATOM 2468 O OD1 . ASP A 1 317 ? 10.015 -8.755 16.368 1.00 14.66 ? 405 ASP A OD1 1 ATOM 2469 O OD2 . ASP A 1 317 ? 11.464 -9.808 17.619 1.00 12.82 ? 405 ASP A OD2 1 ATOM 2470 N N . GLY A 1 318 ? 8.559 -13.656 15.224 1.00 12.24 ? 406 GLY A N 1 ATOM 2471 C CA . GLY A 1 318 ? 8.486 -14.881 14.451 1.00 12.77 ? 406 GLY A CA 1 ATOM 2472 C C . GLY A 1 318 ? 8.441 -16.082 15.386 1.00 14.18 ? 406 GLY A C 1 ATOM 2473 O O . GLY A 1 318 ? 8.805 -15.983 16.571 1.00 13.35 ? 406 GLY A O 1 ATOM 2474 N N . THR A 1 319 ? 7.976 -17.219 14.882 1.00 15.20 ? 407 THR A N 1 ATOM 2475 C CA . THR A 1 319 ? 7.814 -18.370 15.745 1.00 16.63 ? 407 THR A CA 1 ATOM 2476 C C . THR A 1 319 ? 9.103 -19.216 15.944 1.00 18.28 ? 407 THR A C 1 ATOM 2477 O O . THR A 1 319 ? 9.954 -19.312 15.070 1.00 18.02 ? 407 THR A O 1 ATOM 2478 C CB . THR A 1 319 ? 6.647 -19.218 15.259 1.00 16.68 ? 407 THR A CB 1 ATOM 2479 O OG1 . THR A 1 319 ? 6.472 -20.316 16.147 1.00 17.09 ? 407 THR A OG1 1 ATOM 2480 C CG2 . THR A 1 319 ? 6.941 -19.839 13.985 1.00 17.09 ? 407 THR A CG2 1 ATOM 2481 N N . SER A 1 320 ? 9.222 -19.830 17.113 1.00 19.49 ? 408 SER A N 1 ATOM 2482 C CA . SER A 1 320 ? 10.404 -20.620 17.433 1.00 21.87 ? 408 SER A CA 1 ATOM 2483 C C . SER A 1 320 ? 10.112 -22.112 17.306 1.00 24.37 ? 408 SER A C 1 ATOM 2484 O O . SER A 1 320 ? 10.949 -22.951 17.603 1.00 25.00 ? 408 SER A O 1 ATOM 2485 C CB . SER A 1 320 ? 10.809 -20.319 18.861 1.00 21.49 ? 408 SER A CB 1 ATOM 2486 O OG . SER A 1 320 ? 9.752 -20.630 19.743 1.00 20.43 ? 408 SER A OG 1 ATOM 2487 N N . ASP A 1 321 ? 8.900 -22.428 16.880 1.00 26.77 ? 409 ASP A N 1 ATOM 2488 C CA . ASP A 1 321 ? 8.461 -23.816 16.756 1.00 28.77 ? 409 ASP A CA 1 ATOM 2489 C C . ASP A 1 321 ? 9.041 -24.400 15.508 1.00 29.44 ? 409 ASP A C 1 ATOM 2490 O O . ASP A 1 321 ? 8.598 -24.098 14.412 1.00 29.59 ? 409 ASP A O 1 ATOM 2491 C CB . ASP A 1 321 ? 6.935 -23.851 16.704 1.00 29.20 ? 409 ASP A CB 1 ATOM 2492 C CG . ASP A 1 321 ? 6.368 -25.257 16.483 1.00 32.18 ? 409 ASP A CG 1 ATOM 2493 O OD1 . ASP A 1 321 ? 6.952 -26.059 15.689 1.00 32.21 ? 409 ASP A OD1 1 ATOM 2494 O OD2 . ASP A 1 321 ? 5.298 -25.599 17.039 1.00 31.58 ? 409 ASP A OD2 1 ATOM 2495 N N . THR A 1 322 ? 10.043 -25.257 15.672 1.00 31.27 ? 410 THR A N 1 ATOM 2496 C CA . THR A 1 322 ? 10.707 -25.863 14.541 1.00 32.84 ? 410 THR A CA 1 ATOM 2497 C C . THR A 1 322 ? 9.737 -26.722 13.746 1.00 33.61 ? 410 THR A C 1 ATOM 2498 O O . THR A 1 322 ? 10.004 -27.026 12.597 1.00 33.85 ? 410 THR A O 1 ATOM 2499 C CB . THR A 1 322 ? 11.917 -26.710 14.997 1.00 33.49 ? 410 THR A CB 1 ATOM 2500 O OG1 . THR A 1 322 ? 11.511 -27.652 16.009 1.00 34.18 ? 410 THR A OG1 1 ATOM 2501 C CG2 . THR A 1 322 ? 12.971 -25.827 15.701 1.00 34.25 ? 410 THR A CG2 1 ATOM 2502 N N . THR A 1 323 ? 8.612 -27.108 14.346 1.00 34.65 ? 411 THR A N 1 ATOM 2503 C CA . THR A 1 323 ? 7.625 -27.935 13.634 1.00 35.39 ? 411 THR A CA 1 ATOM 2504 C C . THR A 1 323 ? 6.716 -27.069 12.768 1.00 35.36 ? 411 THR A C 1 ATOM 2505 O O . THR A 1 323 ? 5.812 -27.567 12.086 1.00 35.98 ? 411 THR A O 1 ATOM 2506 C CB . THR A 1 323 ? 6.770 -28.765 14.618 1.00 35.44 ? 411 THR A CB 1 ATOM 2507 O OG1 . THR A 1 323 ? 5.643 -28.010 15.077 1.00 35.76 ? 411 THR A OG1 1 ATOM 2508 C CG2 . THR A 1 323 ? 7.545 -29.100 15.904 1.00 37.30 ? 411 THR A CG2 1 ATOM 2509 N N . ALA A 1 324 ? 6.983 -25.771 12.748 1.00 34.82 ? 412 ALA A N 1 ATOM 2510 C CA . ALA A 1 324 ? 6.057 -24.849 12.111 1.00 34.49 ? 412 ALA A CA 1 ATOM 2511 C C . ALA A 1 324 ? 6.539 -24.356 10.775 1.00 33.68 ? 412 ALA A C 1 ATOM 2512 O O . ALA A 1 324 ? 7.707 -24.160 10.543 1.00 33.68 ? 412 ALA A O 1 ATOM 2513 C CB . ALA A 1 324 ? 5.736 -23.707 13.046 1.00 34.47 ? 412 ALA A CB 1 ATOM 2514 N N . ALA A 1 325 ? 5.582 -24.134 9.894 1.00 33.97 ? 413 ALA A N 1 ATOM 2515 C CA . ALA A 1 325 ? 5.855 -23.809 8.501 1.00 33.34 ? 413 ALA A CA 1 ATOM 2516 C C . ALA A 1 325 ? 6.632 -22.531 8.241 1.00 32.94 ? 413 ALA A C 1 ATOM 2517 O O . ALA A 1 325 ? 7.406 -22.433 7.279 1.00 32.98 ? 413 ALA A O 1 ATOM 2518 C CB . ALA A 1 325 ? 4.552 -23.761 7.789 1.00 33.98 ? 413 ALA A CB 1 ATOM 2519 N N . ARG A 1 326 ? 6.409 -21.522 9.061 1.00 31.94 ? 414 ARG A N 1 ATOM 2520 C CA . ARG A 1 326 ? 7.149 -20.284 8.875 1.00 31.30 ? 414 ARG A CA 1 ATOM 2521 C C . ARG A 1 326 ? 8.253 -20.141 9.917 1.00 29.94 ? 414 ARG A C 1 ATOM 2522 O O . ARG A 1 326 ? 8.749 -19.048 10.185 1.00 28.99 ? 414 ARG A O 1 ATOM 2523 C CB . ARG A 1 326 ? 6.192 -19.109 8.934 1.00 31.82 ? 414 ARG A CB 1 ATOM 2524 C CG . ARG A 1 326 ? 5.228 -19.072 7.762 1.00 34.00 ? 414 ARG A CG 1 ATOM 2525 C CD . ARG A 1 326 ? 4.026 -18.171 8.013 1.00 37.17 ? 414 ARG A CD 1 ATOM 2526 N NE . ARG A 1 326 ? 2.880 -18.962 8.424 1.00 40.96 ? 414 ARG A NE 1 ATOM 2527 C CZ . ARG A 1 326 ? 2.211 -19.723 7.562 1.00 43.02 ? 414 ARG A CZ 1 ATOM 2528 N NH1 . ARG A 1 326 ? 2.596 -19.741 6.289 1.00 43.40 ? 414 ARG A NH1 1 ATOM 2529 N NH2 . ARG A 1 326 ? 1.170 -20.446 7.945 1.00 45.27 ? 414 ARG A NH2 1 ATOM 2530 N N . TYR A 1 327 ? 8.633 -21.261 10.507 1.00 28.47 ? 415 TYR A N 1 ATOM 2531 C CA . TYR A 1 327 ? 9.784 -21.273 11.397 1.00 27.90 ? 415 TYR A CA 1 ATOM 2532 C C . TYR A 1 327 ? 10.944 -20.567 10.733 1.00 26.45 ? 415 TYR A C 1 ATOM 2533 O O . TYR A 1 327 ? 11.166 -20.700 9.544 1.00 25.67 ? 415 TYR A O 1 ATOM 2534 C CB . TYR A 1 327 ? 10.195 -22.695 11.743 1.00 27.92 ? 415 TYR A CB 1 ATOM 2535 C CG . TYR A 1 327 ? 11.486 -22.749 12.534 1.00 28.97 ? 415 TYR A CG 1 ATOM 2536 C CD1 . TYR A 1 327 ? 11.563 -22.199 13.808 1.00 31.17 ? 415 TYR A CD1 1 ATOM 2537 C CD2 . TYR A 1 327 ? 12.626 -23.343 12.003 1.00 32.40 ? 415 TYR A CD2 1 ATOM 2538 C CE1 . TYR A 1 327 ? 12.747 -22.233 14.538 1.00 31.98 ? 415 TYR A CE1 1 ATOM 2539 C CE2 . TYR A 1 327 ? 13.820 -23.386 12.717 1.00 30.52 ? 415 TYR A CE2 1 ATOM 2540 C CZ . TYR A 1 327 ? 13.875 -22.835 13.983 1.00 31.79 ? 415 TYR A CZ 1 ATOM 2541 O OH . TYR A 1 327 ? 15.052 -22.883 14.695 1.00 30.79 ? 415 TYR A OH 1 ATOM 2542 N N . ALA A 1 328 ? 11.666 -19.764 11.506 1.00 26.20 ? 416 ALA A N 1 ATOM 2543 C CA . ALA A 1 328 ? 12.867 -19.124 11.013 1.00 24.97 ? 416 ALA A CA 1 ATOM 2544 C C . ALA A 1 328 ? 14.011 -19.370 11.995 1.00 24.07 ? 416 ALA A C 1 ATOM 2545 O O . ALA A 1 328 ? 13.861 -19.144 13.187 1.00 23.89 ? 416 ALA A O 1 ATOM 2546 C CB . ALA A 1 328 ? 12.654 -17.664 10.816 1.00 25.60 ? 416 ALA A CB 1 ATOM 2547 N N . TYR A 1 329 ? 15.125 -19.854 11.445 1.00 22.86 ? 417 TYR A N 1 ATOM 2548 C CA . TYR A 1 329 ? 16.372 -20.129 12.134 1.00 22.30 ? 417 TYR A CA 1 ATOM 2549 C C . TYR A 1 329 ? 16.706 -19.151 13.232 1.00 20.27 ? 417 TYR A C 1 ATOM 2550 O O . TYR A 1 329 ? 17.064 -19.562 14.331 1.00 19.30 ? 417 TYR A O 1 ATOM 2551 C CB . TYR A 1 329 ? 17.521 -20.131 11.091 1.00 23.79 ? 417 TYR A CB 1 ATOM 2552 C CG . TYR A 1 329 ? 18.935 -20.065 11.663 1.00 26.00 ? 417 TYR A CG 1 ATOM 2553 C CD1 . TYR A 1 329 ? 19.508 -21.175 12.270 1.00 30.53 ? 417 TYR A CD1 1 ATOM 2554 C CD2 . TYR A 1 329 ? 19.696 -18.912 11.572 1.00 28.85 ? 417 TYR A CD2 1 ATOM 2555 C CE1 . TYR A 1 329 ? 20.778 -21.134 12.780 1.00 30.54 ? 417 TYR A CE1 1 ATOM 2556 C CE2 . TYR A 1 329 ? 20.980 -18.867 12.066 1.00 29.21 ? 417 TYR A CE2 1 ATOM 2557 C CZ . TYR A 1 329 ? 21.518 -19.980 12.669 1.00 31.87 ? 417 TYR A CZ 1 ATOM 2558 O OH . TYR A 1 329 ? 22.800 -19.957 13.185 1.00 33.73 ? 417 TYR A OH 1 ATOM 2559 N N . HIS A 1 330 ? 16.582 -17.856 12.955 1.00 17.96 ? 418 HIS A N 1 ATOM 2560 C CA . HIS A 1 330 ? 16.999 -16.853 13.957 1.00 17.57 ? 418 HIS A CA 1 ATOM 2561 C C . HIS A 1 330 ? 16.141 -16.856 15.200 1.00 17.04 ? 418 HIS A C 1 ATOM 2562 O O . HIS A 1 330 ? 16.584 -16.424 16.269 1.00 16.13 ? 418 HIS A O 1 ATOM 2563 C CB . HIS A 1 330 ? 17.017 -15.450 13.352 1.00 18.12 ? 418 HIS A CB 1 ATOM 2564 C CG . HIS A 1 330 ? 18.183 -15.223 12.464 1.00 19.21 ? 418 HIS A CG 1 ATOM 2565 N ND1 . HIS A 1 330 ? 18.127 -15.447 11.110 1.00 20.01 ? 418 HIS A ND1 1 ATOM 2566 C CD2 . HIS A 1 330 ? 19.457 -14.867 12.739 1.00 22.00 ? 418 HIS A CD2 1 ATOM 2567 C CE1 . HIS A 1 330 ? 19.319 -15.225 10.586 1.00 21.88 ? 418 HIS A CE1 1 ATOM 2568 N NE2 . HIS A 1 330 ? 20.143 -14.863 11.550 1.00 20.91 ? 418 HIS A NE2 1 ATOM 2569 N N . CYS A 1 331 ? 14.900 -17.314 15.047 1.00 16.88 ? 419 CYS A N 1 ATOM 2570 C CA . CYS A 1 331 ? 13.961 -17.359 16.151 1.00 16.68 ? 419 CYS A CA 1 ATOM 2571 C C . CYS A 1 331 ? 14.198 -18.589 17.027 1.00 17.13 ? 419 CYS A C 1 ATOM 2572 O O . CYS A 1 331 ? 13.568 -18.724 18.068 1.00 16.72 ? 419 CYS A O 1 ATOM 2573 C CB . CYS A 1 331 ? 12.532 -17.376 15.632 1.00 17.70 ? 419 CYS A CB 1 ATOM 2574 S SG . CYS A 1 331 ? 12.175 -15.864 14.705 1.00 19.23 ? 419 CYS A SG 1 ATOM 2575 N N . GLY A 1 332 ? 15.122 -19.460 16.638 1.00 17.55 ? 420 GLY A N 1 ATOM 2576 C CA . GLY A 1 332 ? 15.366 -20.660 17.440 1.00 18.32 ? 420 GLY A CA 1 ATOM 2577 C C . GLY A 1 332 ? 16.678 -20.625 18.177 1.00 19.23 ? 420 GLY A C 1 ATOM 2578 O O . GLY A 1 332 ? 17.078 -21.622 18.779 1.00 19.74 ? 420 GLY A O 1 ATOM 2579 N N . LEU A 1 333 ? 17.361 -19.492 18.120 1.00 19.56 ? 421 LEU A N 1 ATOM 2580 C CA . LEU A 1 333 ? 18.672 -19.401 18.727 1.00 20.34 ? 421 LEU A CA 1 ATOM 2581 C C . LEU A 1 333 ? 18.590 -19.250 20.216 1.00 19.98 ? 421 LEU A C 1 ATOM 2582 O O . LEU A 1 333 ? 17.544 -18.946 20.795 1.00 18.32 ? 421 LEU A O 1 ATOM 2583 C CB . LEU A 1 333 ? 19.490 -18.259 18.131 1.00 20.41 ? 421 LEU A CB 1 ATOM 2584 C CG . LEU A 1 333 ? 19.664 -18.313 16.615 1.00 21.53 ? 421 LEU A CG 1 ATOM 2585 C CD1 . LEU A 1 333 ? 20.088 -16.943 16.144 1.00 22.28 ? 421 LEU A CD1 1 ATOM 2586 C CD2 . LEU A 1 333 ? 20.672 -19.412 16.160 1.00 25.12 ? 421 LEU A CD2 1 ATOM 2587 N N . GLU A 1 334 ? 19.749 -19.453 20.821 1.00 21.20 ? 422 GLU A N 1 ATOM 2588 C CA . GLU A 1 334 ? 19.935 -19.390 22.271 1.00 22.56 ? 422 GLU A CA 1 ATOM 2589 C C . GLU A 1 334 ? 19.575 -17.995 22.843 1.00 21.13 ? 422 GLU A C 1 ATOM 2590 O O . GLU A 1 334 ? 19.124 -17.882 23.981 1.00 19.69 ? 422 GLU A O 1 ATOM 2591 C CB . GLU A 1 334 ? 21.364 -19.912 22.569 1.00 24.22 ? 422 GLU A CB 1 ATOM 2592 C CG . GLU A 1 334 ? 22.225 -19.307 23.645 1.00 30.84 ? 422 GLU A CG 1 ATOM 2593 C CD . GLU A 1 334 ? 23.710 -19.491 23.321 1.00 37.83 ? 422 GLU A CD 1 ATOM 2594 O OE1 . GLU A 1 334 ? 24.078 -20.389 22.510 1.00 41.25 ? 422 GLU A OE1 1 ATOM 2595 O OE2 . GLU A 1 334 ? 24.514 -18.689 23.855 1.00 42.52 ? 422 GLU A OE2 1 ATOM 2596 N N . ASP A 1 335 ? 19.716 -16.943 22.047 1.00 19.24 ? 423 ASP A N 1 ATOM 2597 C CA . ASP A 1 335 ? 19.411 -15.593 22.522 1.00 19.11 ? 423 ASP A CA 1 ATOM 2598 C C . ASP A 1 335 ? 18.053 -15.083 22.017 1.00 18.37 ? 423 ASP A C 1 ATOM 2599 O O . ASP A 1 335 ? 17.815 -13.877 22.024 1.00 17.48 ? 423 ASP A O 1 ATOM 2600 C CB . ASP A 1 335 ? 20.534 -14.588 22.166 1.00 19.38 ? 423 ASP A CB 1 ATOM 2601 C CG . ASP A 1 335 ? 20.867 -14.576 20.695 1.00 22.91 ? 423 ASP A CG 1 ATOM 2602 O OD1 . ASP A 1 335 ? 20.095 -15.219 19.939 1.00 27.82 ? 423 ASP A OD1 1 ATOM 2603 O OD2 . ASP A 1 335 ? 21.846 -13.951 20.196 1.00 20.78 ? 423 ASP A OD2 1 ATOM 2604 N N . ALA A 1 336 ? 17.211 -15.986 21.518 1.00 17.31 ? 424 ALA A N 1 ATOM 2605 C CA . ALA A 1 336 ? 15.829 -15.653 21.161 1.00 18.09 ? 424 ALA A CA 1 ATOM 2606 C C . ALA A 1 336 ? 14.920 -16.217 22.246 1.00 18.29 ? 424 ALA A C 1 ATOM 2607 O O . ALA A 1 336 ? 15.114 -17.376 22.668 1.00 18.87 ? 424 ALA A O 1 ATOM 2608 C CB . ALA A 1 336 ? 15.490 -16.261 19.830 1.00 18.27 ? 424 ALA A CB 1 ATOM 2609 N N . LEU A 1 337 ? 13.950 -15.445 22.714 1.00 17.21 ? 425 LEU A N 1 ATOM 2610 C CA . LEU A 1 337 ? 13.072 -15.938 23.784 1.00 17.47 ? 425 LEU A CA 1 ATOM 2611 C C . LEU A 1 337 ? 12.091 -16.906 23.202 1.00 18.65 ? 425 LEU A C 1 ATOM 2612 O O . LEU A 1 337 ? 11.515 -16.691 22.141 1.00 18.21 ? 425 LEU A O 1 ATOM 2613 C CB . LEU A 1 337 ? 12.303 -14.833 24.498 1.00 17.15 ? 425 LEU A CB 1 ATOM 2614 C CG . LEU A 1 337 ? 11.554 -15.123 25.813 1.00 17.33 ? 425 LEU A CG 1 ATOM 2615 C CD1 . LEU A 1 337 ? 12.493 -15.389 26.971 1.00 16.94 ? 425 LEU A CD1 1 ATOM 2616 C CD2 . LEU A 1 337 ? 10.728 -13.942 26.173 1.00 17.41 ? 425 LEU A CD2 1 ATOM 2617 N N . LYS A 1 338 ? 11.887 -17.980 23.948 1.00 19.56 ? 426 LYS A N 1 ATOM 2618 C CA . LYS A 1 338 ? 11.099 -19.123 23.502 1.00 21.25 ? 426 LYS A CA 1 ATOM 2619 C C . LYS A 1 338 ? 10.163 -19.630 24.612 1.00 22.02 ? 426 LYS A C 1 ATOM 2620 O O . LYS A 1 338 ? 10.423 -19.373 25.800 1.00 22.28 ? 426 LYS A O 1 ATOM 2621 C CB . LYS A 1 338 ? 12.076 -20.223 23.116 1.00 21.70 ? 426 LYS A CB 1 ATOM 2622 C CG . LYS A 1 338 ? 13.013 -19.903 21.963 1.00 24.09 ? 426 LYS A CG 1 ATOM 2623 C CD . LYS A 1 338 ? 13.894 -21.135 21.604 1.00 25.08 ? 426 LYS A CD 1 ATOM 2624 C CE . LYS A 1 338 ? 15.401 -20.941 21.726 1.00 25.99 ? 426 LYS A CE 1 ATOM 2625 N NZ . LYS A 1 338 ? 15.901 -19.990 22.718 1.00 25.46 ? 426 LYS A NZ 1 ATOM 2626 N N . PRO A 1 339 ? 9.050 -20.286 24.273 1.00 22.90 ? 427 PRO A N 1 ATOM 2627 C CA . PRO A 1 339 ? 8.541 -20.529 22.912 1.00 22.70 ? 427 PRO A CA 1 ATOM 2628 C C . PRO A 1 339 ? 7.779 -19.332 22.425 1.00 21.64 ? 427 PRO A C 1 ATOM 2629 O O . PRO A 1 339 ? 7.125 -18.658 23.217 1.00 22.36 ? 427 PRO A O 1 ATOM 2630 C CB . PRO A 1 339 ? 7.587 -21.703 23.106 1.00 23.13 ? 427 PRO A CB 1 ATOM 2631 C CG . PRO A 1 339 ? 7.104 -21.568 24.496 1.00 23.95 ? 427 PRO A CG 1 ATOM 2632 C CD . PRO A 1 339 ? 8.246 -21.005 25.274 1.00 23.70 ? 427 PRO A CD 1 ATOM 2633 N N . ALA A 1 340 ? 7.877 -19.065 21.133 1.00 20.33 ? 428 ALA A N 1 ATOM 2634 C CA . ALA A 1 340 ? 7.328 -17.838 20.574 1.00 19.00 ? 428 ALA A CA 1 ATOM 2635 C C . ALA A 1 340 ? 6.280 -18.184 19.526 1.00 18.15 ? 428 ALA A C 1 ATOM 2636 O O . ALA A 1 340 ? 6.481 -19.098 18.729 1.00 16.19 ? 428 ALA A O 1 ATOM 2637 C CB . ALA A 1 340 ? 8.467 -17.021 19.922 1.00 18.81 ? 428 ALA A CB 1 ATOM 2638 N N . PRO A 1 341 ? 5.201 -17.415 19.500 1.00 18.40 ? 429 PRO A N 1 ATOM 2639 C CA . PRO A 1 341 ? 4.118 -17.648 18.560 1.00 18.85 ? 429 PRO A CA 1 ATOM 2640 C C . PRO A 1 341 ? 4.445 -17.033 17.208 1.00 19.43 ? 429 PRO A C 1 ATOM 2641 O O . PRO A 1 341 ? 5.585 -16.640 16.955 1.00 19.11 ? 429 PRO A O 1 ATOM 2642 C CB . PRO A 1 341 ? 2.966 -16.920 19.232 1.00 19.09 ? 429 PRO A CB 1 ATOM 2643 C CG . PRO A 1 341 ? 3.622 -15.723 19.746 1.00 19.45 ? 429 PRO A CG 1 ATOM 2644 C CD . PRO A 1 341 ? 4.924 -16.222 20.314 1.00 18.20 ? 429 PRO A CD 1 ATOM 2645 N N . GLU A 1 342 ? 3.448 -16.971 16.334 1.00 19.44 ? 430 GLU A N 1 ATOM 2646 C CA . GLU A 1 342 ? 3.666 -16.473 14.984 1.00 19.42 ? 430 GLU A CA 1 ATOM 2647 C C . GLU A 1 342 ? 3.978 -14.981 14.985 1.00 17.48 ? 430 GLU A C 1 ATOM 2648 O O . GLU A 1 342 ? 3.609 -14.253 15.889 1.00 17.00 ? 430 GLU A O 1 ATOM 2649 C CB . GLU A 1 342 ? 2.435 -16.772 14.118 1.00 19.89 ? 430 GLU A CB 1 ATOM 2650 C CG . GLU A 1 342 ? 2.269 -18.266 13.806 1.00 23.57 ? 430 GLU A CG 1 ATOM 2651 C CD . GLU A 1 342 ? 3.215 -18.788 12.737 1.00 27.33 ? 430 GLU A CD 1 ATOM 2652 O OE1 . GLU A 1 342 ? 3.613 -18.009 11.847 1.00 28.55 ? 430 GLU A OE1 1 ATOM 2653 O OE2 . GLU A 1 342 ? 3.555 -20.004 12.780 1.00 32.56 ? 430 GLU A OE2 1 ATOM 2654 N N . ALA A 1 343 ? 4.679 -14.537 13.954 1.00 16.68 ? 431 ALA A N 1 ATOM 2655 C CA . ALA A 1 343 ? 5.011 -13.134 13.848 1.00 15.63 ? 431 ALA A CA 1 ATOM 2656 C C . ALA A 1 343 ? 3.743 -12.282 13.924 1.00 14.43 ? 431 ALA A C 1 ATOM 2657 O O . ALA A 1 343 ? 2.749 -12.557 13.250 1.00 13.67 ? 431 ALA A O 1 ATOM 2658 C CB . ALA A 1 343 ? 5.744 -12.874 12.546 1.00 15.78 ? 431 ALA A CB 1 ATOM 2659 N N . GLY A 1 344 ? 3.810 -11.249 14.743 1.00 14.63 ? 432 GLY A N 1 ATOM 2660 C CA . GLY A 1 344 ? 2.742 -10.286 14.886 1.00 15.12 ? 432 GLY A CA 1 ATOM 2661 C C . GLY A 1 344 ? 1.797 -10.662 16.004 1.00 16.25 ? 432 GLY A C 1 ATOM 2662 O O . GLY A 1 344 ? 0.989 -9.861 16.429 1.00 16.71 ? 432 GLY A O 1 ATOM 2663 N N . GLN A 1 345 ? 1.884 -11.892 16.493 1.00 16.45 ? 433 GLN A N 1 ATOM 2664 C CA . GLN A 1 345 ? 0.952 -12.324 17.526 1.00 16.70 ? 433 GLN A CA 1 ATOM 2665 C C . GLN A 1 345 ? 1.503 -11.959 18.898 1.00 16.34 ? 433 GLN A C 1 ATOM 2666 O O . GLN A 1 345 ? 2.725 -11.807 19.077 1.00 14.96 ? 433 GLN A O 1 ATOM 2667 C CB . GLN A 1 345 ? 0.726 -13.827 17.418 1.00 17.36 ? 433 GLN A CB 1 ATOM 2668 C CG . GLN A 1 345 ? 0.017 -14.247 16.141 1.00 19.56 ? 433 GLN A CG 1 ATOM 2669 C CD . GLN A 1 345 ? -1.355 -13.620 16.089 1.00 24.45 ? 433 GLN A CD 1 ATOM 2670 O OE1 . GLN A 1 345 ? -2.102 -13.721 17.070 1.00 28.33 ? 433 GLN A OE1 1 ATOM 2671 N NE2 . GLN A 1 345 ? -1.670 -12.905 14.996 1.00 22.86 ? 433 GLN A NE2 1 ATOM 2672 N N . TRP A 1 346 ? 0.612 -11.868 19.884 1.00 15.46 ? 434 TRP A N 1 ATOM 2673 C CA . TRP A 1 346 ? 1.029 -11.405 21.182 1.00 15.99 ? 434 TRP A CA 1 ATOM 2674 C C . TRP A 1 346 ? 1.923 -12.426 21.894 1.00 16.59 ? 434 TRP A C 1 ATOM 2675 O O . TRP A 1 346 ? 1.600 -13.610 21.996 1.00 15.60 ? 434 TRP A O 1 ATOM 2676 C CB . TRP A 1 346 ? -0.175 -11.013 22.021 1.00 16.30 ? 434 TRP A CB 1 ATOM 2677 C CG . TRP A 1 346 ? 0.241 -10.276 23.257 1.00 15.46 ? 434 TRP A CG 1 ATOM 2678 C CD1 . TRP A 1 346 ? 0.379 -10.808 24.507 1.00 15.13 ? 434 TRP A CD1 1 ATOM 2679 C CD2 . TRP A 1 346 ? 0.640 -8.922 23.349 1.00 14.43 ? 434 TRP A CD2 1 ATOM 2680 N NE1 . TRP A 1 346 ? 0.800 -9.843 25.385 1.00 16.72 ? 434 TRP A NE1 1 ATOM 2681 C CE2 . TRP A 1 346 ? 0.961 -8.665 24.700 1.00 15.37 ? 434 TRP A CE2 1 ATOM 2682 C CE3 . TRP A 1 346 ? 0.716 -7.866 22.433 1.00 17.33 ? 434 TRP A CE3 1 ATOM 2683 C CZ2 . TRP A 1 346 ? 1.385 -7.425 25.146 1.00 14.83 ? 434 TRP A CZ2 1 ATOM 2684 C CZ3 . TRP A 1 346 ? 1.124 -6.620 22.886 1.00 17.73 ? 434 TRP A CZ3 1 ATOM 2685 C CH2 . TRP A 1 346 ? 1.451 -6.409 24.230 1.00 16.56 ? 434 TRP A CH2 1 ATOM 2686 N N . PHE A 1 347 ? 3.060 -11.946 22.387 1.00 16.33 ? 435 PHE A N 1 ATOM 2687 C CA . PHE A 1 347 ? 4.063 -12.786 23.012 1.00 16.37 ? 435 PHE A CA 1 ATOM 2688 C C . PHE A 1 347 ? 4.254 -12.262 24.435 1.00 16.10 ? 435 PHE A C 1 ATOM 2689 O O . PHE A 1 347 ? 5.195 -11.507 24.728 1.00 14.64 ? 435 PHE A O 1 ATOM 2690 C CB . PHE A 1 347 ? 5.375 -12.662 22.225 1.00 16.86 ? 435 PHE A CB 1 ATOM 2691 C CG . PHE A 1 347 ? 6.410 -13.650 22.613 1.00 17.43 ? 435 PHE A CG 1 ATOM 2692 C CD1 . PHE A 1 347 ? 6.169 -14.557 23.626 1.00 20.17 ? 435 PHE A CD1 1 ATOM 2693 C CD2 . PHE A 1 347 ? 7.635 -13.662 21.984 1.00 19.66 ? 435 PHE A CD2 1 ATOM 2694 C CE1 . PHE A 1 347 ? 7.116 -15.469 23.985 1.00 21.39 ? 435 PHE A CE1 1 ATOM 2695 C CE2 . PHE A 1 347 ? 8.598 -14.590 22.324 1.00 19.78 ? 435 PHE A CE2 1 ATOM 2696 C CZ . PHE A 1 347 ? 8.332 -15.506 23.331 1.00 21.93 ? 435 PHE A CZ 1 ATOM 2697 N N . ASN A 1 348 ? 3.383 -12.689 25.337 1.00 16.70 ? 436 ASN A N 1 ATOM 2698 C CA . ASN A 1 348 ? 3.332 -12.057 26.632 1.00 16.63 ? 436 ASN A CA 1 ATOM 2699 C C . ASN A 1 348 ? 4.596 -12.107 27.475 1.00 16.73 ? 436 ASN A C 1 ATOM 2700 O O . ASN A 1 348 ? 4.875 -11.147 28.205 1.00 17.11 ? 436 ASN A O 1 ATOM 2701 C CB . ASN A 1 348 ? 2.159 -12.571 27.457 1.00 17.68 ? 436 ASN A CB 1 ATOM 2702 C CG . ASN A 1 348 ? 1.753 -11.582 28.472 1.00 20.18 ? 436 ASN A CG 1 ATOM 2703 O OD1 . ASN A 1 348 ? 1.284 -10.478 28.141 1.00 18.57 ? 436 ASN A OD1 1 ATOM 2704 N ND2 . ASN A 1 348 ? 1.993 -11.911 29.730 1.00 24.53 ? 436 ASN A ND2 1 ATOM 2705 N N . GLU A 1 349 ? 5.351 -13.202 27.389 1.00 16.05 ? 437 GLU A N 1 ATOM 2706 C CA . GLU A 1 349 ? 6.571 -13.289 28.159 1.00 16.80 ? 437 GLU A CA 1 ATOM 2707 C C . GLU A 1 349 ? 7.567 -12.238 27.674 1.00 16.50 ? 437 GLU A C 1 ATOM 2708 O O . GLU A 1 349 ? 8.353 -11.710 28.466 1.00 14.69 ? 437 GLU A O 1 ATOM 2709 C CB . GLU A 1 349 ? 7.168 -14.682 28.086 1.00 17.60 ? 437 GLU A CB 1 ATOM 2710 C CG . GLU A 1 349 ? 6.271 -15.716 28.772 1.00 21.21 ? 437 GLU A CG 1 ATOM 2711 C CD . GLU A 1 349 ? 5.298 -16.454 27.848 1.00 26.98 ? 437 GLU A CD 1 ATOM 2712 O OE1 . GLU A 1 349 ? 4.671 -15.855 26.925 1.00 25.99 ? 437 GLU A OE1 1 ATOM 2713 O OE2 . GLU A 1 349 ? 5.165 -17.679 28.049 1.00 30.49 ? 437 GLU A OE2 1 ATOM 2714 N N . TYR A 1 350 ? 7.513 -11.943 26.375 1.00 15.11 ? 438 TYR A N 1 ATOM 2715 C CA . TYR A 1 350 ? 8.413 -10.946 25.799 1.00 14.61 ? 438 TYR A CA 1 ATOM 2716 C C . TYR A 1 350 ? 7.969 -9.557 26.237 1.00 13.61 ? 438 TYR A C 1 ATOM 2717 O O . TYR A 1 350 ? 8.771 -8.712 26.591 1.00 13.37 ? 438 TYR A O 1 ATOM 2718 C CB . TYR A 1 350 ? 8.472 -11.077 24.273 1.00 14.95 ? 438 TYR A CB 1 ATOM 2719 C CG . TYR A 1 350 ? 9.702 -10.384 23.733 1.00 13.10 ? 438 TYR A CG 1 ATOM 2720 C CD1 . TYR A 1 350 ? 9.691 -9.064 23.398 1.00 12.74 ? 438 TYR A CD1 1 ATOM 2721 C CD2 . TYR A 1 350 ? 10.888 -11.061 23.618 1.00 11.87 ? 438 TYR A CD2 1 ATOM 2722 C CE1 . TYR A 1 350 ? 10.849 -8.421 22.950 1.00 11.86 ? 438 TYR A CE1 1 ATOM 2723 C CE2 . TYR A 1 350 ? 12.005 -10.455 23.150 1.00 13.83 ? 438 TYR A CE2 1 ATOM 2724 C CZ . TYR A 1 350 ? 11.991 -9.125 22.804 1.00 12.69 ? 438 TYR A CZ 1 ATOM 2725 O OH . TYR A 1 350 ? 13.169 -8.504 22.362 1.00 15.42 ? 438 TYR A OH 1 ATOM 2726 N N . PHE A 1 351 ? 6.668 -9.335 26.265 1.00 14.41 ? 439 PHE A N 1 ATOM 2727 C CA . PHE A 1 351 ? 6.137 -8.102 26.835 1.00 14.70 ? 439 PHE A CA 1 ATOM 2728 C C . PHE A 1 351 ? 6.644 -7.875 28.254 1.00 13.88 ? 439 PHE A C 1 ATOM 2729 O O . PHE A 1 351 ? 7.088 -6.779 28.613 1.00 12.83 ? 439 PHE A O 1 ATOM 2730 C CB . PHE A 1 351 ? 4.623 -8.160 26.852 1.00 15.03 ? 439 PHE A CB 1 ATOM 2731 C CG . PHE A 1 351 ? 3.998 -6.924 27.367 1.00 15.48 ? 439 PHE A CG 1 ATOM 2732 C CD1 . PHE A 1 351 ? 3.987 -5.790 26.599 1.00 12.57 ? 439 PHE A CD1 1 ATOM 2733 C CD2 . PHE A 1 351 ? 3.417 -6.889 28.629 1.00 18.42 ? 439 PHE A CD2 1 ATOM 2734 C CE1 . PHE A 1 351 ? 3.420 -4.629 27.049 1.00 15.11 ? 439 PHE A CE1 1 ATOM 2735 C CE2 . PHE A 1 351 ? 2.846 -5.728 29.095 1.00 17.51 ? 439 PHE A CE2 1 ATOM 2736 C CZ . PHE A 1 351 ? 2.816 -4.590 28.291 1.00 17.20 ? 439 PHE A CZ 1 ATOM 2737 N N . ILE A 1 352 ? 6.589 -8.916 29.080 1.00 14.60 ? 440 ILE A N 1 ATOM 2738 C CA . ILE A 1 352 ? 7.052 -8.777 30.473 1.00 14.65 ? 440 ILE A CA 1 ATOM 2739 C C . ILE A 1 352 ? 8.551 -8.480 30.556 1.00 13.52 ? 440 ILE A C 1 ATOM 2740 O O . ILE A 1 352 ? 8.989 -7.672 31.349 1.00 13.04 ? 440 ILE A O 1 ATOM 2741 C CB . ILE A 1 352 ? 6.692 -9.992 31.299 1.00 15.59 ? 440 ILE A CB 1 ATOM 2742 C CG1 . ILE A 1 352 ? 5.166 -10.120 31.405 1.00 17.13 ? 440 ILE A CG1 1 ATOM 2743 C CG2 . ILE A 1 352 ? 7.226 -9.829 32.699 1.00 16.49 ? 440 ILE A CG2 1 ATOM 2744 C CD1 . ILE A 1 352 ? 4.728 -11.517 31.834 1.00 19.39 ? 440 ILE A CD1 1 ATOM 2745 N N . GLN A 1 353 ? 9.331 -9.128 29.712 1.00 13.58 ? 441 GLN A N 1 ATOM 2746 C CA . GLN A 1 353 ? 10.749 -8.829 29.642 1.00 13.69 ? 441 GLN A CA 1 ATOM 2747 C C . GLN A 1 353 ? 10.939 -7.350 29.328 1.00 13.09 ? 441 GLN A C 1 ATOM 2748 O O . GLN A 1 353 ? 11.720 -6.644 29.980 1.00 12.35 ? 441 GLN A O 1 ATOM 2749 C CB . GLN A 1 353 ? 11.419 -9.705 28.577 1.00 13.25 ? 441 GLN A CB 1 ATOM 2750 C CG . GLN A 1 353 ? 12.861 -9.419 28.404 1.00 13.73 ? 441 GLN A CG 1 ATOM 2751 C CD . GLN A 1 353 ? 13.413 -10.049 27.123 1.00 15.78 ? 441 GLN A CD 1 ATOM 2752 O OE1 . GLN A 1 353 ? 13.474 -11.272 27.002 1.00 14.17 ? 441 GLN A OE1 1 ATOM 2753 N NE2 . GLN A 1 353 ? 13.784 -9.217 26.162 1.00 16.62 ? 441 GLN A NE2 1 ATOM 2754 N N . LEU A 1 354 ? 10.255 -6.860 28.307 1.00 13.82 ? 442 LEU A N 1 ATOM 2755 C CA . LEU A 1 354 ? 10.417 -5.459 27.938 1.00 13.99 ? 442 LEU A CA 1 ATOM 2756 C C . LEU A 1 354 ? 10.050 -4.505 29.096 1.00 15.35 ? 442 LEU A C 1 ATOM 2757 O O . LEU A 1 354 ? 10.677 -3.442 29.287 1.00 13.97 ? 442 LEU A O 1 ATOM 2758 C CB . LEU A 1 354 ? 9.549 -5.126 26.720 1.00 13.74 ? 442 LEU A CB 1 ATOM 2759 C CG . LEU A 1 354 ? 10.076 -5.644 25.364 1.00 15.14 ? 442 LEU A CG 1 ATOM 2760 C CD1 . LEU A 1 354 ? 9.040 -5.444 24.273 1.00 14.39 ? 442 LEU A CD1 1 ATOM 2761 C CD2 . LEU A 1 354 ? 11.408 -4.977 24.979 1.00 14.54 ? 442 LEU A CD2 1 ATOM 2762 N N . LEU A 1 355 ? 9.006 -4.883 29.832 1.00 15.50 ? 443 LEU A N 1 ATOM 2763 C CA . LEU A 1 355 ? 8.515 -4.083 30.958 1.00 18.32 ? 443 LEU A CA 1 ATOM 2764 C C . LEU A 1 355 ? 9.553 -4.063 32.075 1.00 17.86 ? 443 LEU A C 1 ATOM 2765 O O . LEU A 1 355 ? 9.928 -3.031 32.605 1.00 18.88 ? 443 LEU A O 1 ATOM 2766 C CB . LEU A 1 355 ? 7.212 -4.696 31.463 1.00 18.53 ? 443 LEU A CB 1 ATOM 2767 C CG . LEU A 1 355 ? 6.081 -3.798 31.913 1.00 23.61 ? 443 LEU A CG 1 ATOM 2768 C CD1 . LEU A 1 355 ? 5.828 -2.635 30.977 1.00 23.47 ? 443 LEU A CD1 1 ATOM 2769 C CD2 . LEU A 1 355 ? 4.820 -4.642 32.018 1.00 24.45 ? 443 LEU A CD2 1 ATOM 2770 N N . ARG A 1 356 ? 10.053 -5.224 32.418 1.00 19.40 ? 444 ARG A N 1 ATOM 2771 C CA . ARG A 1 356 ? 11.070 -5.290 33.453 1.00 20.05 ? 444 ARG A CA 1 ATOM 2772 C C . ARG A 1 356 ? 12.288 -4.439 33.108 1.00 20.10 ? 444 ARG A C 1 ATOM 2773 O O . ARG A 1 356 ? 12.856 -3.761 33.968 1.00 20.23 ? 444 ARG A O 1 ATOM 2774 C CB . ARG A 1 356 ? 11.506 -6.730 33.634 1.00 20.71 ? 444 ARG A CB 1 ATOM 2775 C CG . ARG A 1 356 ? 10.414 -7.601 34.255 1.00 22.74 ? 444 ARG A CG 1 ATOM 2776 C CD . ARG A 1 356 ? 10.987 -8.837 34.948 1.00 25.38 ? 444 ARG A CD 1 ATOM 2777 N NE . ARG A 1 356 ? 9.962 -9.835 35.194 1.00 26.54 ? 444 ARG A NE 1 ATOM 2778 C CZ . ARG A 1 356 ? 9.242 -9.839 36.316 1.00 32.73 ? 444 ARG A CZ 1 ATOM 2779 N NH1 . ARG A 1 356 ? 9.504 -8.925 37.243 1.00 32.90 ? 444 ARG A NH1 1 ATOM 2780 N NH2 . ARG A 1 356 ? 8.304 -10.758 36.537 1.00 34.71 ? 444 ARG A NH2 1 ATOM 2781 N N . ASN A 1 357 ? 12.706 -4.506 31.843 1.00 19.60 ? 445 ASN A N 1 ATOM 2782 C CA . ASN A 1 357 ? 13.917 -3.838 31.396 1.00 19.05 ? 445 ASN A CA 1 ATOM 2783 C C . ASN A 1 357 ? 13.728 -2.420 30.898 1.00 19.01 ? 445 ASN A C 1 ATOM 2784 O O . ASN A 1 357 ? 14.692 -1.817 30.437 1.00 18.98 ? 445 ASN A O 1 ATOM 2785 C CB . ASN A 1 357 ? 14.588 -4.652 30.300 1.00 19.30 ? 445 ASN A CB 1 ATOM 2786 C CG . ASN A 1 357 ? 15.161 -5.967 30.805 1.00 20.58 ? 445 ASN A CG 1 ATOM 2787 O OD1 . ASN A 1 357 ? 15.575 -6.080 31.961 1.00 19.22 ? 445 ASN A OD1 1 ATOM 2788 N ND2 . ASN A 1 357 ? 15.201 -6.961 29.931 1.00 18.84 ? 445 ASN A ND2 1 ATOM 2789 N N . ALA A 1 358 ? 12.523 -1.873 31.028 1.00 18.92 ? 446 ALA A N 1 ATOM 2790 C CA . ALA A 1 358 ? 12.223 -0.508 30.581 1.00 18.95 ? 446 ALA A CA 1 ATOM 2791 C C . ALA A 1 358 ? 13.179 0.569 31.115 1.00 19.77 ? 446 ALA A C 1 ATOM 2792 O O . ALA A 1 358 ? 13.443 0.659 32.314 1.00 18.99 ? 446 ALA A O 1 ATOM 2793 C CB . ALA A 1 358 ? 10.798 -0.135 30.933 1.00 18.13 ? 446 ALA A CB 1 ATOM 2794 N N . ASN A 1 359 ? 13.628 1.426 30.203 1.00 20.49 ? 447 ASN A N 1 ATOM 2795 C CA . ASN A 1 359 ? 14.538 2.515 30.521 1.00 20.84 ? 447 ASN A CA 1 ATOM 2796 C C . ASN A 1 359 ? 14.187 3.648 29.573 1.00 21.65 ? 447 ASN A C 1 ATOM 2797 O O . ASN A 1 359 ? 14.384 3.548 28.350 1.00 20.88 ? 447 ASN A O 1 ATOM 2798 C CB . ASN A 1 359 ? 15.977 2.037 30.331 1.00 21.01 ? 447 ASN A CB 1 ATOM 2799 C CG . ASN A 1 359 ? 16.986 3.076 30.652 1.00 22.18 ? 447 ASN A CG 1 ATOM 2800 O OD1 . ASN A 1 359 ? 16.649 4.169 31.062 1.00 24.04 ? 447 ASN A OD1 1 ATOM 2801 N ND2 . ASN A 1 359 ? 18.270 2.723 30.513 1.00 29.83 ? 447 ASN A ND2 1 ATOM 2802 N N . PRO A 1 360 ? 13.619 4.720 30.099 1.00 22.85 ? 448 PRO A N 1 ATOM 2803 C CA . PRO A 1 360 ? 13.283 4.890 31.514 1.00 23.68 ? 448 PRO A CA 1 ATOM 2804 C C . PRO A 1 360 ? 12.157 3.975 31.974 1.00 24.34 ? 448 PRO A C 1 ATOM 2805 O O . PRO A 1 360 ? 11.309 3.575 31.179 1.00 22.36 ? 448 PRO A O 1 ATOM 2806 C CB . PRO A 1 360 ? 12.829 6.346 31.593 1.00 23.91 ? 448 PRO A CB 1 ATOM 2807 C CG . PRO A 1 360 ? 12.675 6.814 30.271 1.00 24.68 ? 448 PRO A CG 1 ATOM 2808 C CD . PRO A 1 360 ? 13.255 5.879 29.300 1.00 23.78 ? 448 PRO A CD 1 ATOM 2809 N N . PRO A 1 361 ? 12.127 3.647 33.258 1.00 26.20 ? 449 PRO A N 1 ATOM 2810 C CA . PRO A 1 361 ? 11.132 2.711 33.744 1.00 27.42 ? 449 PRO A CA 1 ATOM 2811 C C . PRO A 1 361 ? 9.753 3.301 33.732 1.00 28.31 ? 449 PRO A C 1 ATOM 2812 O O . PRO A 1 361 ? 9.578 4.513 33.582 1.00 28.76 ? 449 PRO A O 1 ATOM 2813 C CB . PRO A 1 361 ? 11.557 2.444 35.197 1.00 27.96 ? 449 PRO A CB 1 ATOM 2814 C CG . PRO A 1 361 ? 12.432 3.501 35.567 1.00 27.94 ? 449 PRO A CG 1 ATOM 2815 C CD . PRO A 1 361 ? 12.997 4.130 34.341 1.00 27.11 ? 449 PRO A CD 1 ATOM 2816 N N . PHE A 1 362 ? 8.792 2.406 33.866 1.00 29.57 ? 450 PHE A N 1 ATOM 2817 C CA . PHE A 1 362 ? 7.399 2.739 33.985 1.00 31.22 ? 450 PHE A CA 1 ATOM 2818 C C . PHE A 1 362 ? 7.004 2.695 35.460 1.00 32.84 ? 450 PHE A C 1 ATOM 2819 O O . PHE A 1 362 ? 5.868 2.412 35.853 1.00 35.51 ? 450 PHE A O 1 ATOM 2820 C CB . PHE A 1 362 ? 6.591 1.749 33.170 1.00 30.75 ? 450 PHE A CB 1 ATOM 2821 C CG . PHE A 1 362 ? 6.560 2.089 31.717 1.00 29.32 ? 450 PHE A CG 1 ATOM 2822 C CD1 . PHE A 1 362 ? 5.753 3.117 31.262 1.00 27.96 ? 450 PHE A CD1 1 ATOM 2823 C CD2 . PHE A 1 362 ? 7.367 1.421 30.814 1.00 28.52 ? 450 PHE A CD2 1 ATOM 2824 C CE1 . PHE A 1 362 ? 5.737 3.467 29.933 1.00 28.69 ? 450 PHE A CE1 1 ATOM 2825 C CE2 . PHE A 1 362 ? 7.337 1.751 29.470 1.00 27.20 ? 450 PHE A CE2 1 ATOM 2826 C CZ . PHE A 1 362 ? 6.535 2.779 29.033 1.00 26.71 ? 450 PHE A CZ 1 ATOM 2827 O OXT . PHE A 1 362 ? 7.857 2.944 36.315 1.00 34.74 ? 450 PHE A OXT 1 HETATM 2828 C C1 . NAG B 2 . ? -8.038 -6.121 -0.500 1.00 16.19 ? 500 NAG A C1 1 HETATM 2829 C C2 . NAG B 2 . ? -8.649 -7.255 -1.343 1.00 18.14 ? 500 NAG A C2 1 HETATM 2830 C C3 . NAG B 2 . ? -9.806 -6.689 -2.176 1.00 22.92 ? 500 NAG A C3 1 HETATM 2831 C C4 . NAG B 2 . ? -10.843 -6.036 -1.280 1.00 24.72 ? 500 NAG A C4 1 HETATM 2832 C C5 . NAG B 2 . ? -10.098 -4.997 -0.441 1.00 23.53 ? 500 NAG A C5 1 HETATM 2833 C C6 . NAG B 2 . ? -11.022 -4.277 0.518 1.00 24.24 ? 500 NAG A C6 1 HETATM 2834 C C7 . NAG B 2 . ? -7.552 -9.130 -2.555 1.00 17.23 ? 500 NAG A C7 1 HETATM 2835 C C8 . NAG B 2 . ? -6.552 -9.499 -3.586 1.00 14.95 ? 500 NAG A C8 1 HETATM 2836 N N2 . NAG B 2 . ? -7.634 -7.826 -2.197 1.00 14.80 ? 500 NAG A N2 1 HETATM 2837 O O3 . NAG B 2 . ? -10.421 -7.681 -2.970 1.00 22.62 ? 500 NAG A O3 1 HETATM 2838 O O4 . NAG B 2 . ? -11.806 -5.353 -2.078 1.00 22.77 ? 500 NAG A O4 1 HETATM 2839 O O5 . NAG B 2 . ? -9.063 -5.612 0.295 1.00 19.00 ? 500 NAG A O5 1 HETATM 2840 O O6 . NAG B 2 . ? -10.304 -3.187 1.053 1.00 25.49 ? 500 NAG A O6 1 HETATM 2841 O O7 . NAG B 2 . ? -8.236 -10.033 -2.120 1.00 20.50 ? 500 NAG A O7 1 HETATM 2842 C C1 . MGL C 3 . ? 21.674 -7.951 9.146 1.00 20.61 ? 501 MGL A C1 1 HETATM 2843 C C2 . MGL C 3 . ? 20.814 -7.143 10.102 1.00 17.04 ? 501 MGL A C2 1 HETATM 2844 C C3 . MGL C 3 . ? 19.527 -7.885 10.398 1.00 14.81 ? 501 MGL A C3 1 HETATM 2845 C C4 . MGL C 3 . ? 18.868 -8.330 9.098 1.00 15.77 ? 501 MGL A C4 1 HETATM 2846 C C5 . MGL C 3 . ? 19.860 -9.091 8.228 1.00 17.00 ? 501 MGL A C5 1 HETATM 2847 C C6 . MGL C 3 . ? 19.217 -9.520 6.937 1.00 17.37 ? 501 MGL A C6 1 HETATM 2848 C C7 . MGL C 3 . ? 23.511 -7.652 7.671 1.00 28.80 ? 501 MGL A C7 1 HETATM 2849 O O1 . MGL C 3 . ? 22.832 -7.184 8.833 1.00 23.99 ? 501 MGL A O1 1 HETATM 2850 O O2 . MGL C 3 . ? 21.529 -6.964 11.312 1.00 14.20 ? 501 MGL A O2 1 HETATM 2851 O O3 . MGL C 3 . ? 18.676 -7.059 11.185 1.00 13.08 ? 501 MGL A O3 1 HETATM 2852 O O4 . MGL C 3 . ? 17.764 -9.192 9.378 1.00 15.63 ? 501 MGL A O4 1 HETATM 2853 O O5 . MGL C 3 . ? 20.949 -8.224 7.966 1.00 18.35 ? 501 MGL A O5 1 HETATM 2854 O O6 . MGL C 3 . ? 20.100 -10.304 6.134 1.00 17.67 ? 501 MGL A O6 1 HETATM 2855 C C1 . SGC D 4 . ? 16.377 -8.706 9.123 1.00 14.79 ? 502 SGC A C1 1 HETATM 2856 C C2 . SGC D 4 . ? 15.453 -9.903 9.248 1.00 13.96 ? 502 SGC A C2 1 HETATM 2857 O O2 . SGC D 4 . ? 15.623 -10.766 8.135 1.00 15.04 ? 502 SGC A O2 1 HETATM 2858 C C3 . SGC D 4 . ? 14.004 -9.468 9.320 1.00 16.63 ? 502 SGC A C3 1 HETATM 2859 O O3 . SGC D 4 . ? 13.074 -10.495 9.584 1.00 14.24 ? 502 SGC A O3 1 HETATM 2860 C C4 . SGC D 4 . ? 13.789 -8.322 10.452 1.00 13.60 ? 502 SGC A C4 1 HETATM 2861 C C5 . SGC D 4 . ? 14.935 -7.259 10.425 1.00 15.49 ? 502 SGC A C5 1 HETATM 2862 O O5 . SGC D 4 . ? 16.261 -7.810 10.245 1.00 14.33 ? 502 SGC A O5 1 HETATM 2863 C C6 . SGC D 4 . ? 14.976 -6.509 11.747 1.00 16.64 ? 502 SGC A C6 1 HETATM 2864 O O6 . SGC D 4 . ? 15.893 -5.489 11.680 1.00 21.32 ? 502 SGC A O6 1 HETATM 2865 S S4 . SGC D 4 . ? 12.257 -7.362 10.320 1.00 14.35 ? 502 SGC A S4 1 HETATM 2866 C C2 . BGC E 5 . ? 10.725 -8.079 12.461 1.00 13.59 ? 503 BGC A C2 1 HETATM 2867 C C3 . BGC E 5 . ? 9.281 -8.467 12.792 1.00 13.24 ? 503 BGC A C3 1 HETATM 2868 C C4 . BGC E 5 . ? 8.280 -7.778 11.869 1.00 11.84 ? 503 BGC A C4 1 HETATM 2869 C C5 . BGC E 5 . ? 8.785 -7.745 10.418 1.00 10.26 ? 503 BGC A C5 1 HETATM 2870 C C6 . BGC E 5 . ? 9.162 -6.364 9.902 1.00 12.74 ? 503 BGC A C6 1 HETATM 2871 C C1 . BGC E 5 . ? 11.019 -8.490 11.029 1.00 12.49 ? 503 BGC A C1 1 HETATM 2872 O O2 . BGC E 5 . ? 11.593 -8.684 13.419 1.00 14.40 ? 503 BGC A O2 1 HETATM 2873 O O3 . BGC E 5 . ? 9.015 -8.057 14.101 1.00 12.85 ? 503 BGC A O3 1 HETATM 2874 O O4 . BGC E 5 . ? 7.149 -8.634 11.955 1.00 11.16 ? 503 BGC A O4 1 HETATM 2875 O O5 . BGC E 5 . ? 9.817 -8.692 10.287 1.00 11.34 ? 503 BGC A O5 1 HETATM 2876 O O6 . BGC E 5 . ? 9.815 -5.649 10.907 1.00 12.77 ? 503 BGC A O6 1 HETATM 2877 C C2 . BGC F 5 . ? 4.727 -8.965 11.623 1.00 10.57 ? 504 BGC A C2 1 HETATM 2878 C C3 . BGC F 5 . ? 3.412 -8.222 11.438 1.00 11.71 ? 504 BGC A C3 1 HETATM 2879 C C4 . BGC F 5 . ? 3.185 -7.205 12.540 1.00 11.94 ? 504 BGC A C4 1 HETATM 2880 C C5 . BGC F 5 . ? 4.410 -6.317 12.722 1.00 10.34 ? 504 BGC A C5 1 HETATM 2881 C C6 . BGC F 5 . ? 4.330 -5.404 13.916 1.00 10.50 ? 504 BGC A C6 1 HETATM 2882 C C1 . BGC F 5 . ? 5.854 -7.991 12.041 1.00 9.96 ? 504 BGC A C1 1 HETATM 2883 O O2 . BGC F 5 . ? 4.961 -9.681 10.438 1.00 12.38 ? 504 BGC A O2 1 HETATM 2884 O O3 . BGC F 5 . ? 2.358 -9.150 11.426 1.00 14.81 ? 504 BGC A O3 1 HETATM 2885 O O4 . BGC F 5 . ? 2.124 -6.332 12.158 1.00 9.32 ? 504 BGC A O4 1 HETATM 2886 O O5 . BGC F 5 . ? 5.614 -6.994 12.952 1.00 10.43 ? 504 BGC A O5 1 HETATM 2887 O O6 . BGC F 5 . ? 4.388 -6.148 15.107 1.00 9.72 ? 504 BGC A O6 1 HETATM 2888 NA NA . NA G 6 . ? -15.227 6.371 19.375 1.00 40.68 ? 505 NA A NA 1 HETATM 2889 NA NA . NA H 6 . ? 25.792 0.738 -5.584 1.00 41.66 ? 506 NA A NA 1 HETATM 2890 O O . HOH I 7 . ? 10.363 17.712 4.032 1.00 28.85 ? 2001 HOH A O 1 HETATM 2891 O O . HOH I 7 . ? 5.760 23.205 7.576 1.00 22.25 ? 2002 HOH A O 1 HETATM 2892 O O . HOH I 7 . ? 9.887 25.800 8.452 1.00 37.27 ? 2003 HOH A O 1 HETATM 2893 O O . HOH I 7 . ? 11.492 19.746 14.793 1.00 33.15 ? 2004 HOH A O 1 HETATM 2894 O O . HOH I 7 . ? 4.815 20.787 11.331 1.00 23.91 ? 2005 HOH A O 1 HETATM 2895 O O . HOH I 7 . ? 4.551 14.819 18.531 1.00 19.02 ? 2006 HOH A O 1 HETATM 2896 O O . HOH I 7 . ? -1.190 20.871 15.287 1.00 23.78 ? 2007 HOH A O 1 HETATM 2897 O O . HOH I 7 . ? -5.602 15.668 24.639 1.00 33.31 ? 2008 HOH A O 1 HETATM 2898 O O . HOH I 7 . ? -0.082 10.239 23.261 1.00 39.97 ? 2009 HOH A O 1 HETATM 2899 O O . HOH I 7 . ? 2.592 12.724 21.854 0.55 11.35 ? 2010 HOH A O 1 HETATM 2900 O O . HOH I 7 . ? -0.056 7.837 16.320 1.00 19.60 ? 2011 HOH A O 1 HETATM 2901 O O . HOH I 7 . ? -5.874 7.024 22.547 1.00 32.57 ? 2012 HOH A O 1 HETATM 2902 O O . HOH I 7 . ? -3.462 8.580 22.760 1.00 26.36 ? 2013 HOH A O 1 HETATM 2903 O O . HOH I 7 . ? -10.525 3.216 23.967 1.00 41.47 ? 2014 HOH A O 1 HETATM 2904 O O . HOH I 7 . ? -6.238 -5.852 19.776 1.00 23.21 ? 2015 HOH A O 1 HETATM 2905 O O . HOH I 7 . ? -2.861 -9.786 18.919 1.00 33.41 ? 2016 HOH A O 1 HETATM 2906 O O . HOH I 7 . ? -9.035 -10.627 28.781 1.00 31.76 ? 2017 HOH A O 1 HETATM 2907 O O . HOH I 7 . ? -4.272 -14.720 27.267 1.00 34.62 ? 2018 HOH A O 1 HETATM 2908 O O . HOH I 7 . ? -3.376 -10.284 39.183 1.00 34.33 ? 2019 HOH A O 1 HETATM 2909 O O . HOH I 7 . ? 3.296 -11.292 36.974 1.00 38.45 ? 2020 HOH A O 1 HETATM 2910 O O . HOH I 7 . ? 7.681 -5.758 40.514 1.00 39.12 ? 2021 HOH A O 1 HETATM 2911 O O . HOH I 7 . ? -1.118 -2.438 39.971 1.00 35.24 ? 2022 HOH A O 1 HETATM 2912 O O . HOH I 7 . ? -1.042 22.990 13.851 1.00 32.40 ? 2023 HOH A O 1 HETATM 2913 O O . HOH I 7 . ? -4.110 -6.060 40.608 1.00 35.50 ? 2024 HOH A O 1 HETATM 2914 O O . HOH I 7 . ? 3.204 11.223 23.617 0.45 10.31 ? 2025 HOH A O 1 HETATM 2915 O O . HOH I 7 . ? -1.764 1.788 22.413 1.00 16.68 ? 2026 HOH A O 1 HETATM 2916 O O . HOH I 7 . ? -1.545 8.259 25.009 1.00 22.65 ? 2027 HOH A O 1 HETATM 2917 O O . HOH I 7 . ? -3.937 1.951 29.675 1.00 21.94 ? 2028 HOH A O 1 HETATM 2918 O O . HOH I 7 . ? 2.020 8.089 26.481 1.00 26.17 ? 2029 HOH A O 1 HETATM 2919 O O . HOH I 7 . ? 2.851 1.212 22.327 1.00 15.88 ? 2030 HOH A O 1 HETATM 2920 O O . HOH I 7 . ? 0.811 -0.148 17.918 1.00 11.20 ? 2031 HOH A O 1 HETATM 2921 O O . HOH I 7 . ? -0.134 3.015 20.255 1.00 16.83 ? 2032 HOH A O 1 HETATM 2922 O O . HOH I 7 . ? -0.898 4.594 17.219 1.00 14.83 ? 2033 HOH A O 1 HETATM 2923 O O . HOH I 7 . ? 4.827 8.272 25.937 1.00 25.71 ? 2034 HOH A O 1 HETATM 2924 O O . HOH I 7 . ? -0.595 -2.933 14.413 1.00 14.59 ? 2035 HOH A O 1 HETATM 2925 O O . HOH I 7 . ? -0.073 -10.210 4.616 1.00 15.72 ? 2036 HOH A O 1 HETATM 2926 O O . HOH I 7 . ? -0.819 -9.386 12.682 1.00 31.26 ? 2037 HOH A O 1 HETATM 2927 O O . HOH I 7 . ? -2.562 -5.898 12.413 1.00 28.57 ? 2038 HOH A O 1 HETATM 2928 O O . HOH I 7 . ? -3.455 -10.761 12.998 1.00 34.78 ? 2039 HOH A O 1 HETATM 2929 O O . HOH I 7 . ? -9.426 -4.079 3.601 1.00 14.64 ? 2040 HOH A O 1 HETATM 2930 O O . HOH I 7 . ? -11.490 -5.815 4.424 1.00 25.62 ? 2041 HOH A O 1 HETATM 2931 O O . HOH I 7 . ? -11.411 6.186 21.225 1.00 34.54 ? 2042 HOH A O 1 HETATM 2932 O O . HOH I 7 . ? -17.662 13.984 7.440 1.00 27.32 ? 2043 HOH A O 1 HETATM 2933 O O . HOH I 7 . ? -13.790 -4.694 3.220 1.00 27.81 ? 2044 HOH A O 1 HETATM 2934 O O . HOH I 7 . ? -9.047 -2.475 16.701 1.00 27.13 ? 2045 HOH A O 1 HETATM 2935 O O . HOH I 7 . ? -7.762 0.202 14.935 1.00 24.15 ? 2046 HOH A O 1 HETATM 2936 O O . HOH I 7 . ? 8.095 -14.225 -8.570 1.00 22.89 ? 2047 HOH A O 1 HETATM 2937 O O . HOH I 7 . ? -14.858 10.115 13.764 1.00 18.72 ? 2048 HOH A O 1 HETATM 2938 O O . HOH I 7 . ? -15.592 7.310 10.060 1.00 30.32 ? 2049 HOH A O 1 HETATM 2939 O O . HOH I 7 . ? -7.160 3.409 17.461 1.00 14.67 ? 2050 HOH A O 1 HETATM 2940 O O . HOH I 7 . ? -13.695 4.388 20.485 1.00 25.06 ? 2051 HOH A O 1 HETATM 2941 O O . HOH I 7 . ? -11.982 8.790 19.778 1.00 18.51 ? 2052 HOH A O 1 HETATM 2942 O O . HOH I 7 . ? -2.771 -15.435 3.800 1.00 29.03 ? 2053 HOH A O 1 HETATM 2943 O O . HOH I 7 . ? -6.812 -11.880 5.740 1.00 22.02 ? 2054 HOH A O 1 HETATM 2944 O O . HOH I 7 . ? -15.530 9.938 10.814 1.00 26.01 ? 2055 HOH A O 1 HETATM 2945 O O . HOH I 7 . ? -14.707 10.737 6.355 1.00 33.00 ? 2056 HOH A O 1 HETATM 2946 O O . HOH I 7 . ? -17.582 10.810 7.591 1.00 36.98 ? 2057 HOH A O 1 HETATM 2947 O O . HOH I 7 . ? 4.398 -9.030 -11.907 1.00 23.15 ? 2058 HOH A O 1 HETATM 2948 O O . HOH I 7 . ? -15.988 14.278 18.753 1.00 23.97 ? 2059 HOH A O 1 HETATM 2949 O O . HOH I 7 . ? -8.660 19.184 18.259 1.00 30.46 ? 2060 HOH A O 1 HETATM 2950 O O . HOH I 7 . ? -16.249 12.468 14.496 1.00 36.35 ? 2061 HOH A O 1 HETATM 2951 O O . HOH I 7 . ? -10.677 9.538 -4.005 1.00 37.70 ? 2062 HOH A O 1 HETATM 2952 O O . HOH I 7 . ? -13.624 7.901 -0.526 1.00 37.98 ? 2063 HOH A O 1 HETATM 2953 O O . HOH I 7 . ? -10.587 21.578 24.269 1.00 32.78 ? 2064 HOH A O 1 HETATM 2954 O O . HOH I 7 . ? -3.561 23.048 19.312 1.00 43.39 ? 2065 HOH A O 1 HETATM 2955 O O . HOH I 7 . ? -4.472 15.599 12.808 1.00 22.34 ? 2066 HOH A O 1 HETATM 2956 O O . HOH I 7 . ? -3.427 21.370 17.019 1.00 25.60 ? 2067 HOH A O 1 HETATM 2957 O O . HOH I 7 . ? -1.922 5.639 14.635 1.00 15.03 ? 2068 HOH A O 1 HETATM 2958 O O . HOH I 7 . ? 5.955 6.361 17.928 1.00 11.37 ? 2069 HOH A O 1 HETATM 2959 O O . HOH I 7 . ? 4.788 5.174 -10.368 1.00 30.67 ? 2070 HOH A O 1 HETATM 2960 O O . HOH I 7 . ? 2.286 -9.820 0.756 1.00 12.03 ? 2071 HOH A O 1 HETATM 2961 O O . HOH I 7 . ? 11.119 -12.935 -5.850 1.00 25.45 ? 2072 HOH A O 1 HETATM 2962 O O . HOH I 7 . ? 9.297 -15.890 -5.617 1.00 28.56 ? 2073 HOH A O 1 HETATM 2963 O O . HOH I 7 . ? 6.179 -15.397 -2.427 1.00 19.66 ? 2074 HOH A O 1 HETATM 2964 O O . HOH I 7 . ? 1.611 -10.013 8.432 1.00 20.11 ? 2075 HOH A O 1 HETATM 2965 O O . HOH I 7 . ? -6.101 15.262 -0.399 1.00 26.23 ? 2076 HOH A O 1 HETATM 2966 O O . HOH I 7 . ? 14.282 -16.418 0.560 1.00 23.23 ? 2077 HOH A O 1 HETATM 2967 O O . HOH I 7 . ? 13.593 -10.675 4.408 1.00 25.28 ? 2078 HOH A O 1 HETATM 2968 O O . HOH I 7 . ? 10.481 -14.999 1.870 1.00 32.59 ? 2079 HOH A O 1 HETATM 2969 O O . HOH I 7 . ? 13.516 -18.110 7.385 1.00 25.56 ? 2080 HOH A O 1 HETATM 2970 O O . HOH I 7 . ? 11.973 -18.488 0.197 1.00 27.65 ? 2081 HOH A O 1 HETATM 2971 O O . HOH I 7 . ? -0.167 -12.053 6.988 1.00 37.88 ? 2082 HOH A O 1 HETATM 2972 O O . HOH I 7 . ? -5.819 -9.809 4.082 1.00 13.57 ? 2083 HOH A O 1 HETATM 2973 O O . HOH I 7 . ? -1.537 -14.355 -2.703 1.00 13.31 ? 2084 HOH A O 1 HETATM 2974 O O . HOH I 7 . ? -4.758 -13.215 2.629 1.00 24.32 ? 2085 HOH A O 1 HETATM 2975 O O . HOH I 7 . ? 4.614 -12.486 0.594 1.00 28.10 ? 2086 HOH A O 1 HETATM 2976 O O . HOH I 7 . ? -5.674 -11.378 -0.330 1.00 20.07 ? 2087 HOH A O 1 HETATM 2977 O O . HOH I 7 . ? 2.712 -9.552 -9.983 1.00 22.17 ? 2088 HOH A O 1 HETATM 2978 O O . HOH I 7 . ? 5.962 13.793 -10.327 1.00 37.87 ? 2089 HOH A O 1 HETATM 2979 O O . HOH I 7 . ? -0.701 -12.609 -4.515 1.00 15.36 ? 2090 HOH A O 1 HETATM 2980 O O . HOH I 7 . ? -4.353 -14.571 -8.560 1.00 30.19 ? 2091 HOH A O 1 HETATM 2981 O O . HOH I 7 . ? 0.705 17.412 -3.178 1.00 29.09 ? 2092 HOH A O 1 HETATM 2982 O O . HOH I 7 . ? 6.808 16.262 5.891 1.00 23.40 ? 2093 HOH A O 1 HETATM 2983 O O . HOH I 7 . ? -6.002 -8.197 -11.629 1.00 34.16 ? 2094 HOH A O 1 HETATM 2984 O O . HOH I 7 . ? 1.454 -12.643 -11.401 1.00 18.51 ? 2095 HOH A O 1 HETATM 2985 O O . HOH I 7 . ? -4.706 -3.393 -9.290 1.00 25.86 ? 2096 HOH A O 1 HETATM 2986 O O . HOH I 7 . ? 0.112 -8.444 -10.881 1.00 15.08 ? 2097 HOH A O 1 HETATM 2987 O O . HOH I 7 . ? 20.061 9.693 24.446 1.00 39.49 ? 2098 HOH A O 1 HETATM 2988 O O . HOH I 7 . ? -6.364 -7.152 -7.091 0.55 11.57 ? 2099 HOH A O 1 HETATM 2989 O O . HOH I 7 . ? -5.748 -5.737 -3.326 1.00 16.08 ? 2100 HOH A O 1 HETATM 2990 O O . HOH I 7 . ? 1.243 -2.857 -13.105 1.00 34.66 ? 2101 HOH A O 1 HETATM 2991 O O . HOH I 7 . ? -0.864 1.447 -12.622 1.00 36.09 ? 2102 HOH A O 1 HETATM 2992 O O . HOH I 7 . ? -8.230 -0.268 -4.825 1.00 22.12 ? 2103 HOH A O 1 HETATM 2993 O O . HOH I 7 . ? -7.328 -3.357 -2.410 1.00 21.32 ? 2104 HOH A O 1 HETATM 2994 O O . HOH I 7 . ? -7.888 -0.019 -7.490 1.00 27.30 ? 2105 HOH A O 1 HETATM 2995 O O . HOH I 7 . ? 30.213 10.978 10.393 1.00 22.24 ? 2106 HOH A O 1 HETATM 2996 O O . HOH I 7 . ? -6.026 6.581 -7.100 1.00 31.67 ? 2107 HOH A O 1 HETATM 2997 O O . HOH I 7 . ? -11.441 9.292 -1.023 1.00 21.14 ? 2108 HOH A O 1 HETATM 2998 O O . HOH I 7 . ? -12.298 15.203 4.707 1.00 40.55 ? 2109 HOH A O 1 HETATM 2999 O O . HOH I 7 . ? 21.865 -9.130 28.799 1.00 31.40 ? 2110 HOH A O 1 HETATM 3000 O O . HOH I 7 . ? -6.354 19.256 6.532 1.00 9.88 ? 2111 HOH A O 1 HETATM 3001 O O . HOH I 7 . ? -8.731 15.563 13.007 1.00 23.29 ? 2112 HOH A O 1 HETATM 3002 O O . HOH I 7 . ? 2.816 21.633 12.836 1.00 20.64 ? 2113 HOH A O 1 HETATM 3003 O O . HOH I 7 . ? -5.360 10.475 6.682 1.00 11.00 ? 2114 HOH A O 1 HETATM 3004 O O . HOH I 7 . ? 10.591 9.541 29.537 1.00 20.63 ? 2115 HOH A O 1 HETATM 3005 O O . HOH I 7 . ? 14.843 8.779 27.879 1.00 26.79 ? 2116 HOH A O 1 HETATM 3006 O O . HOH I 7 . ? 10.452 1.630 1.804 1.00 22.24 ? 2117 HOH A O 1 HETATM 3007 O O . HOH I 7 . ? 8.148 -5.049 3.264 1.00 15.84 ? 2118 HOH A O 1 HETATM 3008 O O . HOH I 7 . ? 9.638 -7.018 2.286 1.00 16.18 ? 2119 HOH A O 1 HETATM 3009 O O . HOH I 7 . ? 15.618 -9.331 5.837 1.00 19.64 ? 2120 HOH A O 1 HETATM 3010 O O . HOH I 7 . ? 13.755 -1.866 3.817 1.00 9.80 ? 2121 HOH A O 1 HETATM 3011 O O . HOH I 7 . ? 7.610 -24.055 20.425 0.50 26.27 ? 2122 HOH A O 1 HETATM 3012 O O . HOH I 7 . ? 10.624 -23.739 23.937 1.00 34.04 ? 2123 HOH A O 1 HETATM 3013 O O . HOH I 7 . ? 24.804 -3.231 -2.916 1.00 35.99 ? 2124 HOH A O 1 HETATM 3014 O O . HOH I 7 . ? 23.698 -7.603 -2.064 1.00 22.06 ? 2125 HOH A O 1 HETATM 3015 O O . HOH I 7 . ? 20.604 -14.595 -6.486 1.00 36.43 ? 2126 HOH A O 1 HETATM 3016 O O . HOH I 7 . ? 22.867 -12.636 1.800 1.00 23.03 ? 2127 HOH A O 1 HETATM 3017 O O . HOH I 7 . ? 23.225 -17.256 -4.562 1.00 31.47 ? 2128 HOH A O 1 HETATM 3018 O O . HOH I 7 . ? 15.424 -17.422 -2.085 1.00 19.88 ? 2129 HOH A O 1 HETATM 3019 O O . HOH I 7 . ? 9.111 -18.250 -0.542 1.00 27.49 ? 2130 HOH A O 1 HETATM 3020 O O . HOH I 7 . ? 7.010 -13.877 0.640 1.00 17.44 ? 2131 HOH A O 1 HETATM 3021 O O . HOH I 7 . ? -0.966 -16.924 19.062 1.00 29.87 ? 2132 HOH A O 1 HETATM 3022 O O . HOH I 7 . ? 14.606 -8.046 -9.723 1.00 21.25 ? 2133 HOH A O 1 HETATM 3023 O O . HOH I 7 . ? -1.318 -13.939 24.834 1.00 34.98 ? 2134 HOH A O 1 HETATM 3024 O O . HOH I 7 . ? 10.971 -13.719 -8.542 1.00 31.09 ? 2135 HOH A O 1 HETATM 3025 O O . HOH I 7 . ? 10.200 -5.558 -12.807 1.00 45.47 ? 2136 HOH A O 1 HETATM 3026 O O . HOH I 7 . ? 10.929 -8.136 -9.492 1.00 16.10 ? 2137 HOH A O 1 HETATM 3027 O O . HOH I 7 . ? 11.457 -1.367 -11.077 1.00 29.35 ? 2138 HOH A O 1 HETATM 3028 O O . HOH I 7 . ? 6.854 -7.662 -11.192 1.00 29.45 ? 2139 HOH A O 1 HETATM 3029 O O . HOH I 7 . ? 15.191 3.860 -8.386 1.00 29.42 ? 2140 HOH A O 1 HETATM 3030 O O . HOH I 7 . ? 6.128 2.699 -10.105 1.00 17.66 ? 2141 HOH A O 1 HETATM 3031 O O . HOH I 7 . ? 9.808 -0.084 0.194 1.00 21.76 ? 2142 HOH A O 1 HETATM 3032 O O . HOH I 7 . ? 4.759 16.483 -4.307 1.00 17.28 ? 2143 HOH A O 1 HETATM 3033 O O . HOH I 7 . ? 3.560 12.572 -6.399 1.00 31.32 ? 2144 HOH A O 1 HETATM 3034 O O . HOH I 7 . ? -4.840 16.481 1.872 1.00 15.92 ? 2145 HOH A O 1 HETATM 3035 O O . HOH I 7 . ? -9.184 -4.491 -6.399 1.00 26.89 ? 2146 HOH A O 1 HETATM 3036 O O . HOH I 7 . ? 13.958 -3.053 8.081 1.00 21.75 ? 2147 HOH A O 1 HETATM 3037 O O . HOH I 7 . ? 12.952 0.191 2.423 1.00 19.84 ? 2148 HOH A O 1 HETATM 3038 O O . HOH I 7 . ? 14.514 0.251 9.824 1.00 12.99 ? 2149 HOH A O 1 HETATM 3039 O O . HOH I 7 . ? 30.016 2.388 1.234 1.00 35.92 ? 2150 HOH A O 1 HETATM 3040 O O . HOH I 7 . ? 32.134 -2.120 6.370 1.00 38.41 ? 2151 HOH A O 1 HETATM 3041 O O . HOH I 7 . ? 27.605 -3.611 -0.062 1.00 39.61 ? 2152 HOH A O 1 HETATM 3042 O O . HOH I 7 . ? 26.902 -6.719 5.406 1.00 29.97 ? 2153 HOH A O 1 HETATM 3043 O O . HOH I 7 . ? 22.938 0.710 -4.625 1.00 35.48 ? 2154 HOH A O 1 HETATM 3044 O O . HOH I 7 . ? 17.104 3.086 -6.319 1.00 28.49 ? 2155 HOH A O 1 HETATM 3045 O O . HOH I 7 . ? 17.873 12.009 -4.721 1.00 22.99 ? 2156 HOH A O 1 HETATM 3046 O O . HOH I 7 . ? 10.442 15.569 -0.463 0.60 18.47 ? 2157 HOH A O 1 HETATM 3047 O O . HOH I 7 . ? 18.497 14.247 -7.332 1.00 33.84 ? 2158 HOH A O 1 HETATM 3048 O O . HOH I 7 . ? 11.651 11.579 -12.751 1.00 44.39 ? 2159 HOH A O 1 HETATM 3049 O O . HOH I 7 . ? 5.694 12.823 -7.489 1.00 32.81 ? 2160 HOH A O 1 HETATM 3050 O O . HOH I 7 . ? 4.420 16.255 5.119 1.00 13.90 ? 2161 HOH A O 1 HETATM 3051 O O . HOH I 7 . ? 9.636 17.671 0.368 0.40 21.71 ? 2162 HOH A O 1 HETATM 3052 O O . HOH I 7 . ? 8.209 15.981 3.964 1.00 22.01 ? 2163 HOH A O 1 HETATM 3053 O O . HOH I 7 . ? 1.529 16.290 -0.766 1.00 21.91 ? 2164 HOH A O 1 HETATM 3054 O O . HOH I 7 . ? 12.887 16.103 3.723 1.00 29.26 ? 2165 HOH A O 1 HETATM 3055 O O . HOH I 7 . ? 15.268 -2.653 10.848 1.00 12.79 ? 2166 HOH A O 1 HETATM 3056 O O . HOH I 7 . ? 12.008 -3.039 17.970 1.00 10.34 ? 2167 HOH A O 1 HETATM 3057 O O . HOH I 7 . ? 13.855 -0.253 19.215 1.00 11.18 ? 2168 HOH A O 1 HETATM 3058 O O . HOH I 7 . ? 20.567 -5.657 16.428 1.00 17.07 ? 2169 HOH A O 1 HETATM 3059 O O . HOH I 7 . ? 19.962 12.215 22.742 1.00 43.35 ? 2170 HOH A O 1 HETATM 3060 O O . HOH I 7 . ? 20.250 6.487 23.367 0.60 13.63 ? 2171 HOH A O 1 HETATM 3061 O O . HOH I 7 . ? 26.398 8.235 20.277 1.00 25.03 ? 2172 HOH A O 1 HETATM 3062 O O . HOH I 7 . ? 25.487 5.648 27.378 1.00 38.56 ? 2173 HOH A O 1 HETATM 3063 O O . HOH I 7 . ? 27.484 -0.353 25.183 1.00 27.47 ? 2174 HOH A O 1 HETATM 3064 O O . HOH I 7 . ? 22.658 -2.426 20.672 1.00 15.99 ? 2175 HOH A O 1 HETATM 3065 O O . HOH I 7 . ? 31.679 -1.046 17.314 1.00 21.51 ? 2176 HOH A O 1 HETATM 3066 O O . HOH I 7 . ? 36.270 -7.009 16.725 1.00 31.76 ? 2177 HOH A O 1 HETATM 3067 O O . HOH I 7 . ? 32.742 5.461 16.183 1.00 31.56 ? 2178 HOH A O 1 HETATM 3068 O O . HOH I 7 . ? 30.743 5.528 8.136 1.00 26.67 ? 2179 HOH A O 1 HETATM 3069 O O . HOH I 7 . ? 23.373 -0.016 19.276 1.00 16.91 ? 2180 HOH A O 1 HETATM 3070 O O . HOH I 7 . ? 27.827 14.840 18.888 1.00 33.62 ? 2181 HOH A O 1 HETATM 3071 O O . HOH I 7 . ? 22.276 14.360 19.523 1.00 28.31 ? 2182 HOH A O 1 HETATM 3072 O O . HOH I 7 . ? 28.974 8.929 12.147 1.00 21.84 ? 2183 HOH A O 1 HETATM 3073 O O . HOH I 7 . ? 26.718 14.428 9.429 1.00 25.87 ? 2184 HOH A O 1 HETATM 3074 O O . HOH I 7 . ? 28.588 14.437 16.409 1.00 35.51 ? 2185 HOH A O 1 HETATM 3075 O O . HOH I 7 . ? 29.584 9.509 5.537 1.00 25.62 ? 2186 HOH A O 1 HETATM 3076 O O . HOH I 7 . ? 26.460 15.900 1.876 1.00 31.07 ? 2187 HOH A O 1 HETATM 3077 O O . HOH I 7 . ? 29.385 12.905 1.250 1.00 31.21 ? 2188 HOH A O 1 HETATM 3078 O O . HOH I 7 . ? 26.756 16.036 -5.029 1.00 28.39 ? 2189 HOH A O 1 HETATM 3079 O O . HOH I 7 . ? 29.101 11.531 -1.227 1.00 25.09 ? 2190 HOH A O 1 HETATM 3080 O O . HOH I 7 . ? 20.407 10.014 -6.835 1.00 29.78 ? 2191 HOH A O 1 HETATM 3081 O O . HOH I 7 . ? 10.193 -0.948 18.771 1.00 10.19 ? 2192 HOH A O 1 HETATM 3082 O O . HOH I 7 . ? 15.680 4.036 23.908 1.00 12.89 ? 2193 HOH A O 1 HETATM 3083 O O . HOH I 7 . ? 19.278 4.563 23.144 0.40 12.55 ? 2194 HOH A O 1 HETATM 3084 O O . HOH I 7 . ? 16.787 -2.922 24.454 1.00 12.00 ? 2195 HOH A O 1 HETATM 3085 O O . HOH I 7 . ? 22.846 -4.516 29.473 1.00 22.55 ? 2196 HOH A O 1 HETATM 3086 O O . HOH I 7 . ? 21.192 -0.215 29.599 1.00 28.41 ? 2197 HOH A O 1 HETATM 3087 O O . HOH I 7 . ? 22.312 -2.307 31.079 1.00 29.84 ? 2198 HOH A O 1 HETATM 3088 O O . HOH I 7 . ? 20.892 -6.763 27.998 1.00 14.46 ? 2199 HOH A O 1 HETATM 3089 O O . HOH I 7 . ? 22.672 -13.176 26.200 1.00 33.85 ? 2200 HOH A O 1 HETATM 3090 O O . HOH I 7 . ? 20.878 -3.928 19.109 1.00 17.30 ? 2201 HOH A O 1 HETATM 3091 O O . HOH I 7 . ? 24.907 -9.244 24.360 1.00 24.97 ? 2202 HOH A O 1 HETATM 3092 O O . HOH I 7 . ? 25.303 -11.438 26.138 1.00 32.17 ? 2203 HOH A O 1 HETATM 3093 O O . HOH I 7 . ? 27.913 -9.595 15.859 1.00 24.18 ? 2204 HOH A O 1 HETATM 3094 O O . HOH I 7 . ? 19.526 -7.696 14.043 1.00 16.35 ? 2205 HOH A O 1 HETATM 3095 O O . HOH I 7 . ? 25.761 -10.906 13.124 1.00 20.92 ? 2206 HOH A O 1 HETATM 3096 O O . HOH I 7 . ? 21.161 -11.768 10.355 1.00 28.59 ? 2207 HOH A O 1 HETATM 3097 O O . HOH I 7 . ? 24.588 -13.546 13.192 1.00 45.43 ? 2208 HOH A O 1 HETATM 3098 O O . HOH I 7 . ? 17.685 -13.145 18.954 1.00 23.62 ? 2209 HOH A O 1 HETATM 3099 O O . HOH I 7 . ? 9.207 -10.133 20.543 1.00 18.97 ? 2210 HOH A O 1 HETATM 3100 O O . HOH I 7 . ? 16.336 -11.394 28.847 1.00 27.97 ? 2211 HOH A O 1 HETATM 3101 O O . HOH I 7 . ? 11.522 10.504 25.203 1.00 18.62 ? 2212 HOH A O 1 HETATM 3102 O O . HOH I 7 . ? 11.925 8.984 27.392 1.00 14.18 ? 2213 HOH A O 1 HETATM 3103 O O . HOH I 7 . ? 5.215 9.591 23.824 1.00 20.67 ? 2214 HOH A O 1 HETATM 3104 O O . HOH I 7 . ? 12.919 17.099 16.085 1.00 25.14 ? 2215 HOH A O 1 HETATM 3105 O O . HOH I 7 . ? 6.874 15.316 20.777 1.00 30.69 ? 2216 HOH A O 1 HETATM 3106 O O . HOH I 7 . ? 14.775 18.748 19.028 1.00 33.55 ? 2217 HOH A O 1 HETATM 3107 O O . HOH I 7 . ? 22.190 18.332 15.444 1.00 24.08 ? 2218 HOH A O 1 HETATM 3108 O O . HOH I 7 . ? 13.222 18.352 12.612 1.00 20.09 ? 2219 HOH A O 1 HETATM 3109 O O . HOH I 7 . ? 7.820 -1.114 21.997 1.00 12.18 ? 2220 HOH A O 1 HETATM 3110 O O . HOH I 7 . ? -0.281 -2.756 17.226 1.00 13.68 ? 2221 HOH A O 1 HETATM 3111 O O . HOH I 7 . ? 0.832 -5.489 14.334 1.00 13.54 ? 2222 HOH A O 1 HETATM 3112 O O . HOH I 7 . ? 8.054 -7.770 20.637 1.00 12.27 ? 2223 HOH A O 1 HETATM 3113 O O . HOH I 7 . ? 8.162 -16.725 11.961 1.00 27.38 ? 2224 HOH A O 1 HETATM 3114 O O . HOH I 7 . ? 11.978 -24.544 20.439 0.40 16.93 ? 2225 HOH A O 1 HETATM 3115 O O . HOH I 7 . ? 13.267 -23.815 18.728 0.60 15.82 ? 2226 HOH A O 1 HETATM 3116 O O . HOH I 7 . ? 9.472 -23.012 20.873 0.50 16.75 ? 2227 HOH A O 1 HETATM 3117 O O . HOH I 7 . ? 10.795 -26.465 18.458 1.00 32.78 ? 2228 HOH A O 1 HETATM 3118 O O . HOH I 7 . ? 9.972 -26.082 9.723 1.00 44.98 ? 2229 HOH A O 1 HETATM 3119 O O . HOH I 7 . ? 0.876 -21.723 5.086 1.00 28.28 ? 2230 HOH A O 1 HETATM 3120 O O . HOH I 7 . ? 17.050 -24.072 13.849 1.00 32.00 ? 2231 HOH A O 1 HETATM 3121 O O . HOH I 7 . ? 18.157 -22.197 15.244 1.00 24.97 ? 2232 HOH A O 1 HETATM 3122 O O . HOH I 7 . ? 15.016 -20.211 8.438 1.00 23.56 ? 2233 HOH A O 1 HETATM 3123 O O . HOH I 7 . ? 17.618 -13.831 16.333 1.00 14.06 ? 2234 HOH A O 1 HETATM 3124 O O . HOH I 7 . ? 16.149 -16.618 10.230 1.00 23.31 ? 2235 HOH A O 1 HETATM 3125 O O . HOH I 7 . ? 11.904 -16.780 19.309 1.00 12.00 ? 2236 HOH A O 1 HETATM 3126 O O . HOH I 7 . ? 15.928 -24.046 18.911 1.00 18.14 ? 2237 HOH A O 1 HETATM 3127 O O . HOH I 7 . ? 19.597 -22.800 19.798 1.00 29.03 ? 2238 HOH A O 1 HETATM 3128 O O . HOH I 7 . ? 21.993 -20.359 19.190 1.00 27.50 ? 2239 HOH A O 1 HETATM 3129 O O . HOH I 7 . ? 13.660 -18.692 26.056 1.00 22.55 ? 2240 HOH A O 1 HETATM 3130 O O . HOH I 7 . ? 17.382 -21.653 24.546 1.00 33.25 ? 2241 HOH A O 1 HETATM 3131 O O . HOH I 7 . ? 9.628 -20.717 27.978 1.00 37.53 ? 2242 HOH A O 1 HETATM 3132 O O . HOH I 7 . ? 5.556 -21.667 19.719 1.00 27.58 ? 2243 HOH A O 1 HETATM 3133 O O . HOH I 7 . ? 0.650 -17.821 17.033 1.00 26.17 ? 2244 HOH A O 1 HETATM 3134 O O . HOH I 7 . ? 5.351 -16.235 11.808 1.00 25.27 ? 2245 HOH A O 1 HETATM 3135 O O . HOH I 7 . ? 0.118 -11.993 13.142 1.00 22.13 ? 2246 HOH A O 1 HETATM 3136 O O . HOH I 7 . ? -0.401 -8.031 14.936 1.00 35.39 ? 2247 HOH A O 1 HETATM 3137 O O . HOH I 7 . ? -2.199 -12.201 19.258 1.00 20.23 ? 2248 HOH A O 1 HETATM 3138 O O . HOH I 7 . ? -0.348 -15.425 21.164 1.00 18.80 ? 2249 HOH A O 1 HETATM 3139 O O . HOH I 7 . ? 1.328 -14.618 24.717 1.00 21.72 ? 2250 HOH A O 1 HETATM 3140 O O . HOH I 7 . ? 9.173 -12.891 30.678 1.00 21.56 ? 2251 HOH A O 1 HETATM 3141 O O . HOH I 7 . ? 13.383 -12.647 29.283 1.00 22.41 ? 2252 HOH A O 1 HETATM 3142 O O . HOH I 7 . ? 11.249 -6.370 37.544 1.00 37.55 ? 2253 HOH A O 1 HETATM 3143 O O . HOH I 7 . ? 17.101 -1.404 31.391 1.00 23.24 ? 2254 HOH A O 1 HETATM 3144 O O . HOH I 7 . ? 16.308 -9.670 30.526 1.00 25.70 ? 2255 HOH A O 1 HETATM 3145 O O . HOH I 7 . ? 13.273 -1.086 34.198 1.00 20.73 ? 2256 HOH A O 1 HETATM 3146 O O . HOH I 7 . ? 16.398 4.498 26.761 1.00 19.48 ? 2257 HOH A O 1 HETATM 3147 O O . HOH I 7 . ? 19.223 -0.091 31.236 1.00 31.36 ? 2258 HOH A O 1 HETATM 3148 O O . HOH I 7 . ? 9.519 -0.502 34.336 1.00 29.23 ? 2259 HOH A O 1 HETATM 3149 O O . HOH I 7 . ? 4.561 5.291 34.178 1.00 34.39 ? 2260 HOH A O 1 HETATM 3150 O O . HOH I 7 . ? -7.690 -2.868 0.270 1.00 23.98 ? 2261 HOH A O 1 HETATM 3151 O O . HOH I 7 . ? -7.299 -6.409 -5.523 0.45 11.76 ? 2262 HOH A O 1 HETATM 3152 O O . HOH I 7 . ? -10.563 -7.750 2.733 1.00 26.65 ? 2263 HOH A O 1 HETATM 3153 O O . HOH I 7 . ? 22.200 -9.539 4.791 1.00 25.30 ? 2264 HOH A O 1 HETATM 3154 O O . HOH I 7 . ? 20.005 -12.496 7.465 1.00 35.30 ? 2265 HOH A O 1 HETATM 3155 O O . HOH I 7 . ? 17.703 -12.702 8.484 1.00 24.60 ? 2266 HOH A O 1 HETATM 3156 O O . HOH I 7 . ? 11.809 -3.861 10.106 1.00 13.44 ? 2267 HOH A O 1 HETATM 3157 O O . HOH I 7 . ? 13.689 -7.708 14.436 1.00 14.83 ? 2268 HOH A O 1 HETATM 3158 O O . HOH I 7 . ? 3.029 -11.888 10.404 1.00 18.47 ? 2269 HOH A O 1 HETATM 3159 O O . HOH I 7 . ? 7.023 -10.870 9.388 1.00 33.71 ? 2270 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 TYR 1 89 89 TYR TYR A . n A 1 2 ALA 2 90 90 ALA ALA A . n A 1 3 GLY 3 91 91 GLY GLY A . n A 1 4 ASN 4 92 92 ASN ASN A . n A 1 5 PRO 5 93 93 PRO PRO A . n A 1 6 PHE 6 94 94 PHE PHE A . n A 1 7 GLU 7 95 95 GLU GLU A . n A 1 8 GLY 8 96 96 GLY GLY A . n A 1 9 VAL 9 97 97 VAL VAL A . n A 1 10 GLN 10 98 98 GLN GLN A . n A 1 11 LEU 11 99 99 LEU LEU A . n A 1 12 TRP 12 100 100 TRP TRP A . n A 1 13 ALA 13 101 101 ALA ALA A . n A 1 14 ASN 14 102 102 ASN ASN A . n A 1 15 ASN 15 103 103 ASN ASN A . n A 1 16 TYR 16 104 104 TYR TYR A . n A 1 17 TYR 17 105 105 TYR TYR A . n A 1 18 ARG 18 106 106 ARG ARG A . n A 1 19 SER 19 107 107 SER SER A . n A 1 20 GLU 20 108 108 GLU GLU A . n A 1 21 VAL 21 109 109 VAL VAL A . n A 1 22 HIS 22 110 110 HIS HIS A . n A 1 23 THR 23 111 111 THR THR A . n A 1 24 LEU 24 112 112 LEU LEU A . n A 1 25 ALA 25 113 113 ALA ALA A . n A 1 26 ILE 26 114 114 ILE ILE A . n A 1 27 PRO 27 115 115 PRO PRO A . n A 1 28 GLN 28 116 116 GLN GLN A . n A 1 29 ILE 29 117 117 ILE ILE A . n A 1 30 THR 30 118 118 THR THR A . n A 1 31 ASP 31 119 119 ASP ASP A . n A 1 32 PRO 32 120 120 PRO PRO A . n A 1 33 ALA 33 121 121 ALA ALA A . n A 1 34 LEU 34 122 122 LEU LEU A . n A 1 35 ARG 35 123 123 ARG ARG A . n A 1 36 ALA 36 124 124 ALA ALA A . n A 1 37 ALA 37 125 125 ALA ALA A . n A 1 38 ALA 38 126 126 ALA ALA A . n A 1 39 SER 39 127 127 SER SER A . n A 1 40 ALA 40 128 128 ALA ALA A . n A 1 41 VAL 41 129 129 VAL VAL A . n A 1 42 ALA 42 130 130 ALA ALA A . n A 1 43 GLU 43 131 131 GLU GLU A . n A 1 44 VAL 44 132 132 VAL VAL A . n A 1 45 PRO 45 133 133 PRO PRO A . n A 1 46 SER 46 134 134 SER SER A . n A 1 47 PHE 47 135 135 PHE PHE A . n A 1 48 GLN 48 136 136 GLN GLN A . n A 1 49 TRP 49 137 137 TRP TRP A . n A 1 50 LEU 50 138 138 LEU LEU A . n A 1 51 ASP 51 139 139 ASP ASP A . n A 1 52 ARG 52 140 140 ARG ARG A . n A 1 53 ASN 53 141 141 ASN ASN A . n A 1 54 VAL 54 142 142 VAL VAL A . n A 1 55 THR 55 143 143 THR THR A . n A 1 56 VAL 56 144 144 VAL VAL A . n A 1 57 ASP 57 145 145 ASP ASP A . n A 1 58 THR 58 146 146 THR THR A . n A 1 59 LEU 59 147 147 LEU LEU A . n A 1 60 LEU 60 148 148 LEU LEU A . n A 1 61 VAL 61 149 149 VAL VAL A . n A 1 62 GLN 62 150 150 GLN GLN A . n A 1 63 THR 63 151 151 THR THR A . n A 1 64 LEU 64 152 152 LEU LEU A . n A 1 65 SER 65 153 153 SER SER A . n A 1 66 GLU 66 154 154 GLU GLU A . n A 1 67 ILE 67 155 155 ILE ILE A . n A 1 68 ARG 68 156 156 ARG ARG A . n A 1 69 GLU 69 157 157 GLU GLU A . n A 1 70 ALA 70 158 158 ALA ALA A . n A 1 71 ASN 71 159 159 ASN ASN A . n A 1 72 GLN 72 160 160 GLN GLN A . n A 1 73 ALA 73 161 161 ALA ALA A . n A 1 74 GLY 74 162 162 GLY GLY A . n A 1 75 ALA 75 163 163 ALA ALA A . n A 1 76 ASN 76 164 164 ASN ASN A . n A 1 77 PRO 77 165 165 PRO PRO A . n A 1 78 GLN 78 166 166 GLN GLN A . n A 1 79 TYR 79 167 167 TYR TYR A . n A 1 80 ALA 80 168 168 ALA ALA A . n A 1 81 ALA 81 169 169 ALA ALA A . n A 1 82 GLN 82 170 170 GLN GLN A . n A 1 83 ILE 83 171 171 ILE ILE A . n A 1 84 VAL 84 172 172 VAL VAL A . n A 1 85 VAL 85 173 173 VAL VAL A . n A 1 86 TYR 86 174 174 TYR TYR A . n A 1 87 ASP 87 175 175 ASP ASP A . n A 1 88 LEU 88 176 176 LEU LEU A . n A 1 89 PRO 89 177 177 PRO PRO A . n A 1 90 ASP 90 178 178 ASP ASP A . n A 1 91 ARG 91 179 179 ARG ARG A . n A 1 92 ASP 92 180 180 ASP ASP A . n A 1 93 CYS 93 181 181 CYS CYS A . n A 1 94 ALA 94 182 182 ALA ALA A . n A 1 95 ALA 95 183 183 ALA ALA A . n A 1 96 ALA 96 184 184 ALA ALA A . n A 1 97 ALA 97 185 185 ALA ALA A . n A 1 98 SER 98 186 186 SER SER A . n A 1 99 ASN 99 187 187 ASN ASN A . n A 1 100 GLY 100 188 188 GLY GLY A . n A 1 101 GLU 101 189 189 GLU GLU A . n A 1 102 TRP 102 190 190 TRP TRP A . n A 1 103 ALA 103 191 191 ALA ALA A . n A 1 104 ILE 104 192 192 ILE ILE A . n A 1 105 ALA 105 193 193 ALA ALA A . n A 1 106 ASN 106 194 194 ASN ASN A . n A 1 107 ASN 107 195 195 ASN ASN A . n A 1 108 GLY 108 196 196 GLY GLY A . n A 1 109 VAL 109 197 197 VAL VAL A . n A 1 110 ASN 110 198 198 ASN ASN A . n A 1 111 ASN 111 199 199 ASN ASN A . n A 1 112 TYR 112 200 200 TYR TYR A . n A 1 113 LYS 113 201 201 LYS LYS A . n A 1 114 ALA 114 202 202 ALA ALA A . n A 1 115 TYR 115 203 203 TYR TYR A . n A 1 116 ILE 116 204 204 ILE ILE A . n A 1 117 ASN 117 205 205 ASN ASN A . n A 1 118 ARG 118 206 206 ARG ARG A . n A 1 119 ILE 119 207 207 ILE ILE A . n A 1 120 ARG 120 208 208 ARG ARG A . n A 1 121 GLU 121 209 209 GLU GLU A . n A 1 122 ILE 122 210 210 ILE ILE A . n A 1 123 LEU 123 211 211 LEU LEU A . n A 1 124 ILE 124 212 212 ILE ILE A . n A 1 125 SER 125 213 213 SER SER A . n A 1 126 PHE 126 214 214 PHE PHE A . n A 1 127 SER 127 215 215 SER SER A . n A 1 128 ASP 128 216 216 ASP ASP A . n A 1 129 VAL 129 217 217 VAL VAL A . n A 1 130 ARG 130 218 218 ARG ARG A . n A 1 131 THR 131 219 219 THR THR A . n A 1 132 ILE 132 220 220 ILE ILE A . n A 1 133 LEU 133 221 221 LEU LEU A . n A 1 134 VAL 134 222 222 VAL VAL A . n A 1 135 ILE 135 223 223 ILE ILE A . n A 1 136 GLU 136 224 224 GLU GLU A . n A 1 137 PRO 137 225 225 PRO PRO A . n A 1 138 ASP 138 226 226 ASP ASP A . n A 1 139 SER 139 227 227 SER SER A . n A 1 140 LEU 140 228 228 LEU LEU A . n A 1 141 ALA 141 229 229 ALA ALA A . n A 1 142 ASN 142 230 230 ASN ASN A . n A 1 143 MET 143 231 231 MET MET A . n A 1 144 VAL 144 232 232 VAL VAL A . n A 1 145 THR 145 233 233 THR THR A . n A 1 146 ASN 146 234 234 ASN ASN A . n A 1 147 MET 147 235 235 MET MET A . n A 1 148 ASN 148 236 236 ASN ASN A . n A 1 149 VAL 149 237 237 VAL VAL A . n A 1 150 PRO 150 238 238 PRO PRO A . n A 1 151 LYS 151 239 239 LYS LYS A . n A 1 152 CYS 152 240 240 CYS CYS A . n A 1 153 SER 153 241 241 SER SER A . n A 1 154 GLY 154 242 242 GLY GLY A . n A 1 155 ALA 155 243 243 ALA ALA A . n A 1 156 ALA 156 244 244 ALA ALA A . n A 1 157 SER 157 245 245 SER SER A . n A 1 158 THR 158 246 246 THR THR A . n A 1 159 TYR 159 247 247 TYR TYR A . n A 1 160 ARG 160 248 248 ARG ARG A . n A 1 161 GLU 161 249 249 GLU GLU A . n A 1 162 LEU 162 250 250 LEU LEU A . n A 1 163 THR 163 251 251 THR THR A . n A 1 164 ILE 164 252 252 ILE ILE A . n A 1 165 TYR 165 253 253 TYR TYR A . n A 1 166 ALA 166 254 254 ALA ALA A . n A 1 167 LEU 167 255 255 LEU LEU A . n A 1 168 LYS 168 256 256 LYS LYS A . n A 1 169 GLN 169 257 257 GLN GLN A . n A 1 170 LEU 170 258 258 LEU LEU A . n A 1 171 ASP 171 259 259 ASP ASP A . n A 1 172 LEU 172 260 260 LEU LEU A . n A 1 173 PRO 173 261 261 PRO PRO A . n A 1 174 HIS 174 262 262 HIS HIS A . n A 1 175 VAL 175 263 263 VAL VAL A . n A 1 176 ALA 176 264 264 ALA ALA A . n A 1 177 MET 177 265 265 MET MET A . n A 1 178 TYR 178 266 266 TYR TYR A . n A 1 179 MET 179 267 267 MET MET A . n A 1 180 ASP 180 268 268 ASP ASP A . n A 1 181 ALA 181 269 269 ALA ALA A . n A 1 182 GLY 182 270 270 GLY GLY A . n A 1 183 HIS 183 271 271 HIS HIS A . n A 1 184 ALA 184 272 272 ALA ALA A . n A 1 185 GLY 185 273 273 GLY GLY A . n A 1 186 TRP 186 274 274 TRP TRP A . n A 1 187 LEU 187 275 275 LEU LEU A . n A 1 188 GLY 188 276 276 GLY GLY A . n A 1 189 TRP 189 277 277 TRP TRP A . n A 1 190 PRO 190 278 278 PRO PRO A . n A 1 191 ALA 191 279 279 ALA ALA A . n A 1 192 ASN 192 280 280 ASN ASN A . n A 1 193 ILE 193 281 281 ILE ILE A . n A 1 194 GLN 194 282 282 GLN GLN A . n A 1 195 PRO 195 283 283 PRO PRO A . n A 1 196 ALA 196 284 284 ALA ALA A . n A 1 197 ALA 197 285 285 ALA ALA A . n A 1 198 GLU 198 286 286 GLU GLU A . n A 1 199 LEU 199 287 287 LEU LEU A . n A 1 200 PHE 200 288 288 PHE PHE A . n A 1 201 ALA 201 289 289 ALA ALA A . n A 1 202 LYS 202 290 290 LYS LYS A . n A 1 203 ILE 203 291 291 ILE ILE A . n A 1 204 TYR 204 292 292 TYR TYR A . n A 1 205 GLU 205 293 293 GLU GLU A . n A 1 206 ASP 206 294 294 ASP ASP A . n A 1 207 ALA 207 295 295 ALA ALA A . n A 1 208 GLY 208 296 296 GLY GLY A . n A 1 209 LYS 209 297 297 LYS LYS A . n A 1 210 PRO 210 298 298 PRO PRO A . n A 1 211 ARG 211 299 299 ARG ARG A . n A 1 212 ALA 212 300 300 ALA ALA A . n A 1 213 VAL 213 301 301 VAL VAL A . n A 1 214 ARG 214 302 302 ARG ARG A . n A 1 215 GLY 215 303 303 GLY GLY A . n A 1 216 LEU 216 304 304 LEU LEU A . n A 1 217 ALA 217 305 305 ALA ALA A . n A 1 218 THR 218 306 306 THR THR A . n A 1 219 ASN 219 307 307 ASN ASN A . n A 1 220 VAL 220 308 308 VAL VAL A . n A 1 221 ALA 221 309 309 ALA ALA A . n A 1 222 ASN 222 310 310 ASN ASN A . n A 1 223 TYR 223 311 311 TYR TYR A . n A 1 224 ASN 224 312 312 ASN ASN A . n A 1 225 ALA 225 313 313 ALA ALA A . n A 1 226 TRP 226 314 314 TRP TRP A . n A 1 227 SER 227 315 315 SER SER A . n A 1 228 VAL 228 316 316 VAL VAL A . n A 1 229 SER 229 317 317 SER SER A . n A 1 230 SER 230 318 318 SER SER A . n A 1 231 PRO 231 319 319 PRO PRO A . n A 1 232 PRO 232 320 320 PRO PRO A . n A 1 233 PRO 233 321 321 PRO PRO A . n A 1 234 TYR 234 322 322 TYR TYR A . n A 1 235 THR 235 323 323 THR THR A . n A 1 236 SER 236 324 324 SER SER A . n A 1 237 PRO 237 325 325 PRO PRO A . n A 1 238 ASN 238 326 326 ASN ASN A . n A 1 239 PRO 239 327 327 PRO PRO A . n A 1 240 ASN 240 328 328 ASN ASN A . n A 1 241 TYR 241 329 329 TYR TYR A . n A 1 242 ASP 242 330 330 ASP ASP A . n A 1 243 GLU 243 331 331 GLU GLU A . n A 1 244 LYS 244 332 332 LYS LYS A . n A 1 245 HIS 245 333 333 HIS HIS A . n A 1 246 TYR 246 334 334 TYR TYR A . n A 1 247 ILE 247 335 335 ILE ILE A . n A 1 248 GLU 248 336 336 GLU GLU A . n A 1 249 ALA 249 337 337 ALA ALA A . n A 1 250 PHE 250 338 338 PHE PHE A . n A 1 251 ARG 251 339 339 ARG ARG A . n A 1 252 PRO 252 340 340 PRO PRO A . n A 1 253 LEU 253 341 341 LEU LEU A . n A 1 254 LEU 254 342 342 LEU LEU A . n A 1 255 GLU 255 343 343 GLU GLU A . n A 1 256 ALA 256 344 344 ALA ALA A . n A 1 257 ARG 257 345 345 ARG ARG A . n A 1 258 GLY 258 346 346 GLY GLY A . n A 1 259 PHE 259 347 347 PHE PHE A . n A 1 260 PRO 260 348 348 PRO PRO A . n A 1 261 ALA 261 349 349 ALA ALA A . n A 1 262 GLN 262 350 350 GLN GLN A . n A 1 263 PHE 263 351 351 PHE PHE A . n A 1 264 ILE 264 352 352 ILE ILE A . n A 1 265 VAL 265 353 353 VAL VAL A . n A 1 266 ASP 266 354 354 ASP ASP A . n A 1 267 GLN 267 355 355 GLN GLN A . n A 1 268 GLY 268 356 356 GLY GLY A . n A 1 269 ARG 269 357 357 ARG ARG A . n A 1 270 SER 270 358 358 SER SER A . n A 1 271 GLY 271 359 359 GLY GLY A . n A 1 272 LYS 272 360 360 LYS LYS A . n A 1 273 GLN 273 361 361 GLN GLN A . n A 1 274 PRO 274 362 362 PRO PRO A . n A 1 275 THR 275 363 363 THR THR A . n A 1 276 GLY 276 364 364 GLY GLY A . n A 1 277 GLN 277 365 365 GLN GLN A . n A 1 278 LYS 278 366 366 LYS LYS A . n A 1 279 GLU 279 367 367 GLU GLU A . n A 1 280 TRP 280 368 368 TRP TRP A . n A 1 281 GLY 281 369 369 GLY GLY A . n A 1 282 HIS 282 370 370 HIS HIS A . n A 1 283 TRP 283 371 371 TRP TRP A . n A 1 284 CYS 284 372 372 CYS CYS A . n A 1 285 ASN 285 373 373 ASN ASN A . n A 1 286 ALA 286 374 374 ALA ALA A . n A 1 287 ILE 287 375 375 ILE ILE A . n A 1 288 GLY 288 376 376 GLY GLY A . n A 1 289 THR 289 377 377 THR THR A . n A 1 290 GLY 290 378 378 GLY GLY A . n A 1 291 PHE 291 379 379 PHE PHE A . n A 1 292 GLY 292 380 380 GLY GLY A . n A 1 293 MET 293 381 381 MET MET A . n A 1 294 ARG 294 382 382 ARG ARG A . n A 1 295 PRO 295 383 383 PRO PRO A . n A 1 296 THR 296 384 384 THR THR A . n A 1 297 ALA 297 385 385 ALA ALA A . n A 1 298 ASN 298 386 386 ASN ASN A . n A 1 299 THR 299 387 387 THR THR A . n A 1 300 GLY 300 388 388 GLY GLY A . n A 1 301 HIS 301 389 389 HIS HIS A . n A 1 302 GLN 302 390 390 GLN GLN A . n A 1 303 TYR 303 391 391 TYR TYR A . n A 1 304 VAL 304 392 392 VAL VAL A . n A 1 305 ASP 305 393 393 ASP ASP A . n A 1 306 ALA 306 394 394 ALA ALA A . n A 1 307 PHE 307 395 395 PHE PHE A . n A 1 308 VAL 308 396 396 VAL VAL A . n A 1 309 TRP 309 397 397 TRP TRP A . n A 1 310 VAL 310 398 398 VAL VAL A . n A 1 311 LYS 311 399 399 LYS LYS A . n A 1 312 PRO 312 400 400 PRO PRO A . n A 1 313 GLY 313 401 401 GLY GLY A . n A 1 314 GLY 314 402 402 GLY GLY A . n A 1 315 GLU 315 403 403 GLU GLU A . n A 1 316 CYS 316 404 404 CYS CYS A . n A 1 317 ASP 317 405 405 ASP ASP A . n A 1 318 GLY 318 406 406 GLY GLY A . n A 1 319 THR 319 407 407 THR THR A . n A 1 320 SER 320 408 408 SER SER A . n A 1 321 ASP 321 409 409 ASP ASP A . n A 1 322 THR 322 410 410 THR THR A . n A 1 323 THR 323 411 411 THR THR A . n A 1 324 ALA 324 412 412 ALA ALA A . n A 1 325 ALA 325 413 413 ALA ALA A . n A 1 326 ARG 326 414 414 ARG ARG A . n A 1 327 TYR 327 415 415 TYR TYR A . n A 1 328 ALA 328 416 416 ALA ALA A . n A 1 329 TYR 329 417 417 TYR TYR A . n A 1 330 HIS 330 418 418 HIS HIS A . n A 1 331 CYS 331 419 419 CYS CYS A . n A 1 332 GLY 332 420 420 GLY GLY A . n A 1 333 LEU 333 421 421 LEU LEU A . n A 1 334 GLU 334 422 422 GLU GLU A . n A 1 335 ASP 335 423 423 ASP ASP A . n A 1 336 ALA 336 424 424 ALA ALA A . n A 1 337 LEU 337 425 425 LEU LEU A . n A 1 338 LYS 338 426 426 LYS LYS A . n A 1 339 PRO 339 427 427 PRO PRO A . n A 1 340 ALA 340 428 428 ALA ALA A . n A 1 341 PRO 341 429 429 PRO PRO A . n A 1 342 GLU 342 430 430 GLU GLU A . n A 1 343 ALA 343 431 431 ALA ALA A . n A 1 344 GLY 344 432 432 GLY GLY A . n A 1 345 GLN 345 433 433 GLN GLN A . n A 1 346 TRP 346 434 434 TRP TRP A . n A 1 347 PHE 347 435 435 PHE PHE A . n A 1 348 ASN 348 436 436 ASN ASN A . n A 1 349 GLU 349 437 437 GLU GLU A . n A 1 350 TYR 350 438 438 TYR TYR A . n A 1 351 PHE 351 439 439 PHE PHE A . n A 1 352 ILE 352 440 440 ILE ILE A . n A 1 353 GLN 353 441 441 GLN GLN A . n A 1 354 LEU 354 442 442 LEU LEU A . n A 1 355 LEU 355 443 443 LEU LEU A . n A 1 356 ARG 356 444 444 ARG ARG A . n A 1 357 ASN 357 445 445 ASN ASN A . n A 1 358 ALA 358 446 446 ALA ALA A . n A 1 359 ASN 359 447 447 ASN ASN A . n A 1 360 PRO 360 448 448 PRO PRO A . n A 1 361 PRO 361 449 449 PRO PRO A . n A 1 362 PHE 362 450 450 PHE PHE A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 500 500 NAG NAG A . C 3 MGL 1 501 501 MGL MGL A . D 4 SGC 2 502 502 SGC SGC A . E 5 BGC 3 503 503 BGC BGC A . F 5 BGC 4 504 504 BGC BGC A . G 6 NA 1 505 505 NA NA A . H 6 NA 1 506 506 NA NA A . I 7 HOH 1 2001 2001 HOH HOH A . I 7 HOH 2 2002 2002 HOH HOH A . I 7 HOH 3 2003 2003 HOH HOH A . I 7 HOH 4 2004 2004 HOH HOH A . I 7 HOH 5 2005 2005 HOH HOH A . I 7 HOH 6 2006 2006 HOH HOH A . I 7 HOH 7 2007 2007 HOH HOH A . I 7 HOH 8 2008 2008 HOH HOH A . I 7 HOH 9 2009 2009 HOH HOH A . I 7 HOH 10 2010 2010 HOH HOH A . I 7 HOH 11 2011 2011 HOH HOH A . I 7 HOH 12 2012 2012 HOH HOH A . I 7 HOH 13 2013 2013 HOH HOH A . I 7 HOH 14 2014 2014 HOH HOH A . I 7 HOH 15 2015 2015 HOH HOH A . I 7 HOH 16 2016 2016 HOH HOH A . I 7 HOH 17 2017 2017 HOH HOH A . I 7 HOH 18 2018 2018 HOH HOH A . I 7 HOH 19 2019 2019 HOH HOH A . I 7 HOH 20 2020 2020 HOH HOH A . I 7 HOH 21 2021 2021 HOH HOH A . I 7 HOH 22 2022 2022 HOH HOH A . I 7 HOH 23 2023 2023 HOH HOH A . I 7 HOH 24 2024 2024 HOH HOH A . I 7 HOH 25 2025 2025 HOH HOH A . I 7 HOH 26 2026 2026 HOH HOH A . I 7 HOH 27 2027 2027 HOH HOH A . I 7 HOH 28 2028 2028 HOH HOH A . I 7 HOH 29 2029 2029 HOH HOH A . I 7 HOH 30 2030 2030 HOH HOH A . I 7 HOH 31 2031 2031 HOH HOH A . I 7 HOH 32 2032 2032 HOH HOH A . I 7 HOH 33 2033 2033 HOH HOH A . I 7 HOH 34 2034 2034 HOH HOH A . I 7 HOH 35 2035 2035 HOH HOH A . I 7 HOH 36 2036 2036 HOH HOH A . I 7 HOH 37 2037 2037 HOH HOH A . I 7 HOH 38 2038 2038 HOH HOH A . I 7 HOH 39 2039 2039 HOH HOH A . I 7 HOH 40 2040 2040 HOH HOH A . I 7 HOH 41 2041 2041 HOH HOH A . I 7 HOH 42 2042 2042 HOH HOH A . I 7 HOH 43 2043 2043 HOH HOH A . I 7 HOH 44 2044 2044 HOH HOH A . I 7 HOH 45 2045 2045 HOH HOH A . I 7 HOH 46 2046 2046 HOH HOH A . I 7 HOH 47 2047 2047 HOH HOH A . I 7 HOH 48 2048 2048 HOH HOH A . I 7 HOH 49 2049 2049 HOH HOH A . I 7 HOH 50 2050 2050 HOH HOH A . I 7 HOH 51 2051 2051 HOH HOH A . I 7 HOH 52 2052 2052 HOH HOH A . I 7 HOH 53 2053 2053 HOH HOH A . I 7 HOH 54 2054 2054 HOH HOH A . I 7 HOH 55 2055 2055 HOH HOH A . I 7 HOH 56 2056 2056 HOH HOH A . I 7 HOH 57 2057 2057 HOH HOH A . I 7 HOH 58 2058 2058 HOH HOH A . I 7 HOH 59 2059 2059 HOH HOH A . I 7 HOH 60 2060 2060 HOH HOH A . I 7 HOH 61 2061 2061 HOH HOH A . I 7 HOH 62 2062 2062 HOH HOH A . I 7 HOH 63 2063 2063 HOH HOH A . I 7 HOH 64 2064 2064 HOH HOH A . I 7 HOH 65 2065 2065 HOH HOH A . I 7 HOH 66 2066 2066 HOH HOH A . I 7 HOH 67 2067 2067 HOH HOH A . I 7 HOH 68 2068 2068 HOH HOH A . I 7 HOH 69 2069 2069 HOH HOH A . I 7 HOH 70 2070 2070 HOH HOH A . I 7 HOH 71 2071 2071 HOH HOH A . I 7 HOH 72 2072 2072 HOH HOH A . I 7 HOH 73 2073 2073 HOH HOH A . I 7 HOH 74 2074 2074 HOH HOH A . I 7 HOH 75 2075 2075 HOH HOH A . I 7 HOH 76 2076 2076 HOH HOH A . I 7 HOH 77 2077 2077 HOH HOH A . I 7 HOH 78 2078 2078 HOH HOH A . I 7 HOH 79 2079 2079 HOH HOH A . I 7 HOH 80 2080 2080 HOH HOH A . I 7 HOH 81 2081 2081 HOH HOH A . I 7 HOH 82 2082 2082 HOH HOH A . I 7 HOH 83 2083 2083 HOH HOH A . I 7 HOH 84 2084 2084 HOH HOH A . I 7 HOH 85 2085 2085 HOH HOH A . I 7 HOH 86 2086 2086 HOH HOH A . I 7 HOH 87 2087 2087 HOH HOH A . I 7 HOH 88 2088 2088 HOH HOH A . I 7 HOH 89 2089 2089 HOH HOH A . I 7 HOH 90 2090 2090 HOH HOH A . I 7 HOH 91 2091 2091 HOH HOH A . I 7 HOH 92 2092 2092 HOH HOH A . I 7 HOH 93 2093 2093 HOH HOH A . I 7 HOH 94 2094 2094 HOH HOH A . I 7 HOH 95 2095 2095 HOH HOH A . I 7 HOH 96 2096 2096 HOH HOH A . I 7 HOH 97 2097 2097 HOH HOH A . I 7 HOH 98 2098 2098 HOH HOH A . I 7 HOH 99 2099 2099 HOH HOH A . I 7 HOH 100 2100 2100 HOH HOH A . I 7 HOH 101 2101 2101 HOH HOH A . I 7 HOH 102 2102 2102 HOH HOH A . I 7 HOH 103 2103 2103 HOH HOH A . I 7 HOH 104 2104 2104 HOH HOH A . I 7 HOH 105 2105 2105 HOH HOH A . I 7 HOH 106 2106 2106 HOH HOH A . I 7 HOH 107 2107 2107 HOH HOH A . I 7 HOH 108 2108 2108 HOH HOH A . I 7 HOH 109 2109 2109 HOH HOH A . I 7 HOH 110 2110 2110 HOH HOH A . I 7 HOH 111 2111 2111 HOH HOH A . I 7 HOH 112 2112 2112 HOH HOH A . I 7 HOH 113 2113 2113 HOH HOH A . I 7 HOH 114 2114 2114 HOH HOH A . I 7 HOH 115 2115 2115 HOH HOH A . I 7 HOH 116 2116 2116 HOH HOH A . I 7 HOH 117 2117 2117 HOH HOH A . I 7 HOH 118 2118 2118 HOH HOH A . I 7 HOH 119 2119 2119 HOH HOH A . I 7 HOH 120 2120 2120 HOH HOH A . I 7 HOH 121 2121 2121 HOH HOH A . I 7 HOH 122 2122 2122 HOH HOH A . I 7 HOH 123 2123 2123 HOH HOH A . I 7 HOH 124 2124 2124 HOH HOH A . I 7 HOH 125 2125 2125 HOH HOH A . I 7 HOH 126 2126 2126 HOH HOH A . I 7 HOH 127 2127 2127 HOH HOH A . I 7 HOH 128 2128 2128 HOH HOH A . I 7 HOH 129 2129 2129 HOH HOH A . I 7 HOH 130 2130 2130 HOH HOH A . I 7 HOH 131 2131 2131 HOH HOH A . I 7 HOH 132 2132 2132 HOH HOH A . I 7 HOH 133 2133 2133 HOH HOH A . I 7 HOH 134 2134 2134 HOH HOH A . I 7 HOH 135 2135 2135 HOH HOH A . I 7 HOH 136 2136 2136 HOH HOH A . I 7 HOH 137 2137 2137 HOH HOH A . I 7 HOH 138 2138 2138 HOH HOH A . I 7 HOH 139 2139 2139 HOH HOH A . I 7 HOH 140 2140 2140 HOH HOH A . I 7 HOH 141 2141 2141 HOH HOH A . I 7 HOH 142 2142 2142 HOH HOH A . I 7 HOH 143 2143 2143 HOH HOH A . I 7 HOH 144 2144 2144 HOH HOH A . I 7 HOH 145 2145 2145 HOH HOH A . I 7 HOH 146 2146 2146 HOH HOH A . I 7 HOH 147 2147 2147 HOH HOH A . I 7 HOH 148 2148 2148 HOH HOH A . I 7 HOH 149 2149 2149 HOH HOH A . I 7 HOH 150 2150 2150 HOH HOH A . I 7 HOH 151 2151 2151 HOH HOH A . I 7 HOH 152 2152 2152 HOH HOH A . I 7 HOH 153 2153 2153 HOH HOH A . I 7 HOH 154 2154 2154 HOH HOH A . I 7 HOH 155 2155 2155 HOH HOH A . I 7 HOH 156 2156 2156 HOH HOH A . I 7 HOH 157 2157 2157 HOH HOH A . I 7 HOH 158 2158 2158 HOH HOH A . I 7 HOH 159 2159 2159 HOH HOH A . I 7 HOH 160 2160 2160 HOH HOH A . I 7 HOH 161 2161 2161 HOH HOH A . I 7 HOH 162 2162 2162 HOH HOH A . I 7 HOH 163 2163 2163 HOH HOH A . I 7 HOH 164 2164 2164 HOH HOH A . I 7 HOH 165 2165 2165 HOH HOH A . I 7 HOH 166 2166 2166 HOH HOH A . I 7 HOH 167 2167 2167 HOH HOH A . I 7 HOH 168 2168 2168 HOH HOH A . I 7 HOH 169 2169 2169 HOH HOH A . I 7 HOH 170 2170 2170 HOH HOH A . I 7 HOH 171 2171 2171 HOH HOH A . I 7 HOH 172 2172 2172 HOH HOH A . I 7 HOH 173 2173 2173 HOH HOH A . I 7 HOH 174 2174 2174 HOH HOH A . I 7 HOH 175 2175 2175 HOH HOH A . I 7 HOH 176 2176 2176 HOH HOH A . I 7 HOH 177 2177 2177 HOH HOH A . I 7 HOH 178 2178 2178 HOH HOH A . I 7 HOH 179 2179 2179 HOH HOH A . I 7 HOH 180 2180 2180 HOH HOH A . I 7 HOH 181 2181 2181 HOH HOH A . I 7 HOH 182 2182 2182 HOH HOH A . I 7 HOH 183 2183 2183 HOH HOH A . I 7 HOH 184 2184 2184 HOH HOH A . I 7 HOH 185 2185 2185 HOH HOH A . I 7 HOH 186 2186 2186 HOH HOH A . I 7 HOH 187 2187 2187 HOH HOH A . I 7 HOH 188 2188 2188 HOH HOH A . I 7 HOH 189 2189 2189 HOH HOH A . I 7 HOH 190 2190 2190 HOH HOH A . I 7 HOH 191 2191 2191 HOH HOH A . I 7 HOH 192 2192 2192 HOH HOH A . I 7 HOH 193 2193 2193 HOH HOH A . I 7 HOH 194 2194 2194 HOH HOH A . I 7 HOH 195 2195 2195 HOH HOH A . I 7 HOH 196 2196 2196 HOH HOH A . I 7 HOH 197 2197 2197 HOH HOH A . I 7 HOH 198 2198 2198 HOH HOH A . I 7 HOH 199 2199 2199 HOH HOH A . I 7 HOH 200 2200 2200 HOH HOH A . I 7 HOH 201 2201 2201 HOH HOH A . I 7 HOH 202 2202 2202 HOH HOH A . I 7 HOH 203 2203 2203 HOH HOH A . I 7 HOH 204 2204 2204 HOH HOH A . I 7 HOH 205 2205 2205 HOH HOH A . I 7 HOH 206 2206 2206 HOH HOH A . I 7 HOH 207 2207 2207 HOH HOH A . I 7 HOH 208 2208 2208 HOH HOH A . I 7 HOH 209 2209 2209 HOH HOH A . I 7 HOH 210 2210 2210 HOH HOH A . I 7 HOH 211 2211 2211 HOH HOH A . I 7 HOH 212 2212 2212 HOH HOH A . I 7 HOH 213 2213 2213 HOH HOH A . I 7 HOH 214 2214 2214 HOH HOH A . I 7 HOH 215 2215 2215 HOH HOH A . I 7 HOH 216 2216 2216 HOH HOH A . I 7 HOH 217 2217 2217 HOH HOH A . I 7 HOH 218 2218 2218 HOH HOH A . I 7 HOH 219 2219 2219 HOH HOH A . I 7 HOH 220 2220 2220 HOH HOH A . I 7 HOH 221 2221 2221 HOH HOH A . I 7 HOH 222 2222 2222 HOH HOH A . I 7 HOH 223 2223 2223 HOH HOH A . I 7 HOH 224 2224 2224 HOH HOH A . I 7 HOH 225 2225 2225 HOH HOH A . I 7 HOH 226 2226 2226 HOH HOH A . I 7 HOH 227 2227 2227 HOH HOH A . I 7 HOH 228 2228 2228 HOH HOH A . I 7 HOH 229 2229 2229 HOH HOH A . I 7 HOH 230 2230 2230 HOH HOH A . I 7 HOH 231 2231 2231 HOH HOH A . I 7 HOH 232 2232 2232 HOH HOH A . I 7 HOH 233 2233 2233 HOH HOH A . I 7 HOH 234 2234 2234 HOH HOH A . I 7 HOH 235 2235 2235 HOH HOH A . I 7 HOH 236 2236 2236 HOH HOH A . I 7 HOH 237 2237 2237 HOH HOH A . I 7 HOH 238 2238 2238 HOH HOH A . I 7 HOH 239 2239 2239 HOH HOH A . I 7 HOH 240 2240 2240 HOH HOH A . I 7 HOH 241 2241 2241 HOH HOH A . I 7 HOH 242 2242 2242 HOH HOH A . I 7 HOH 243 2243 2243 HOH HOH A . I 7 HOH 244 2244 2244 HOH HOH A . I 7 HOH 245 2245 2245 HOH HOH A . I 7 HOH 246 2246 2246 HOH HOH A . I 7 HOH 247 2247 2247 HOH HOH A . I 7 HOH 248 2248 2248 HOH HOH A . I 7 HOH 249 2249 2249 HOH HOH A . I 7 HOH 250 2250 2250 HOH HOH A . I 7 HOH 251 2251 2251 HOH HOH A . I 7 HOH 252 2252 2252 HOH HOH A . I 7 HOH 253 2253 2253 HOH HOH A . I 7 HOH 254 2254 2254 HOH HOH A . I 7 HOH 255 2255 2255 HOH HOH A . I 7 HOH 256 2256 2256 HOH HOH A . I 7 HOH 257 2257 2257 HOH HOH A . I 7 HOH 258 2258 2258 HOH HOH A . I 7 HOH 259 2259 2259 HOH HOH A . I 7 HOH 260 2260 2260 HOH HOH A . I 7 HOH 261 2261 2261 HOH HOH A . I 7 HOH 262 2262 2262 HOH HOH A . I 7 HOH 263 2263 2263 HOH HOH A . I 7 HOH 264 2264 2264 HOH HOH A . I 7 HOH 265 2265 2265 HOH HOH A . I 7 HOH 266 2266 2266 HOH HOH A . I 7 HOH 267 2267 2267 HOH HOH A . I 7 HOH 268 2268 2268 HOH HOH A . I 7 HOH 269 2269 2269 HOH HOH A . I 7 HOH 270 2270 2270 HOH HOH A . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 53 _pdbx_struct_mod_residue.auth_asym_id A _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 141 _pdbx_struct_mod_residue.PDB_ins_code ? _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I # _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 2003-02-12 2 'Structure model' 1 1 2011-10-19 # _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' 'Derived calculations' 2 2 'Structure model' 'Non-polymer description' 3 2 'Structure model' Other 4 2 'Structure model' 'Structure summary' 5 2 'Structure model' 'Version format compliance' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal REFMAC refinement 5.0 ? 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 1GZ1 _pdbx_entry_details.compound_details 'ENGINEERED MUTATION ASP 416 ALA' _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THIS MUTANT HAS BEEN PRODUCED BY SITE-DIRECTED MUTAGENESIS. THE CLONING WAS PERFORMED SUCH HAS ONLY THE PRO-SEQUENCE AND THE CATALYTIC DOMAIN WERE EXPRESSED. THE CELLULOSE BINDING DOMAIN HAS BEEN REMOVED. THE CONSTRUCT IS POST-TRANSLATIONALLY CLEAVED TO YIELD TO A MATURE PROTEIN OF 450 RESIDUES WHICH COMMENCES AT RESIDUE TYR 89. ; # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 226 ? ? CG A ASP 226 ? ? OD2 A ASP 226 ? ? 124.54 118.30 6.24 0.90 N 2 1 CB A ASP 423 ? ? CG A ASP 423 ? ? OD2 A ASP 423 ? ? 124.05 118.30 5.75 0.90 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 ? ? -115.80 -79.04 2 1 TYR A 174 ? ? -150.54 73.93 3 1 ASP A 175 ? ? -158.42 31.80 4 1 GLU A 224 ? ? 47.67 73.71 5 1 SER A 227 ? ? -120.04 -86.00 6 1 ALA A 269 ? ? -141.05 46.06 7 1 ASN A 310 ? ? -110.06 -168.13 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 O1-METHYL-GLUCOSE MGL 4 4-DEOXY-4-THIO-BETA-D-GLUCOPYRANOSE SGC 5 BETA-D-GLUCOSE BGC 6 'SODIUM ION' NA 7 water HOH #